CNRS Nantes University UFIP UFIP
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***  GPCR  ***

elNémo ID: 211110123738138497

Job options:

ID        	=	 211110123738138497
JOBID     	=	 GPCR
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER GPCR

HEADER    obj01
CRYST1   34.295  106.240  183.403  90.00  90.00  90.00 P 21 21 21    4
ATOM      1  N   ALA A  19      14.637  -3.224 -74.879  1.00106.82      A    N  
ANISOU    1  N   ALA A  19    11168  23417   6001   -116   1329    514  A    N  
ATOM      2  CA  ALA A  19      14.276  -2.637 -73.589  1.00104.07      A    C  
ANISOU    2  CA  ALA A  19    10781  22812   5947   -157   1221    611  A    C  
ATOM      3  C   ALA A  19      13.158  -1.575 -73.751  1.00106.52      A    C  
ANISOU    3  C   ALA A  19    11118  23109   6245   -240   1043    779  A    C  
ATOM      4  O   ALA A  19      13.348  -0.639 -74.537  1.00108.00      A    O  
ANISOU    4  O   ALA A  19    11307  23457   6271   -285   1038    975  A    O  
ATOM      5  CB  ALA A  19      15.508  -2.021 -72.938  1.00104.14      A    C  
ANISOU    5  CB  ALA A  19    10672  22801   6096   -162   1314    782  A    C  
ATOM      6  N   PRO A  20      11.990  -1.694 -73.051  1.00 99.52      A    N  
ANISOU    6  N   PRO A  20    10253  22053   5507   -245    903    721  A    N  
ATOM      7  CA  PRO A  20      10.914  -0.694 -73.233  1.00 98.68      A    C  
ANISOU    7  CA  PRO A  20    10156  21977   5360   -260    744    891  A    C  
ATOM      8  C   PRO A  20      11.188   0.663 -72.561  1.00100.56      A    C  
ANISOU    8  C   PRO A  20    10409  22065   5733   -257    722   1160  A    C  
ATOM      9  O   PRO A  20      11.627   0.674 -71.401  1.00 98.05      A    O  
ANISOU    9  O   PRO A  20    10072  21536   5648   -260    755   1160  A    O  
ATOM     10  CB  PRO A  20       9.666  -1.388 -72.654  1.00 99.09      A    C  
ANISOU   10  CB  PRO A  20    10195  21943   5513   -262    625    731  A    C  
ATOM     11  CG  PRO A  20      10.087  -2.798 -72.337  1.00103.30      A    C  
ANISOU   11  CG  PRO A  20    10762  22386   6101   -279    722    463  A    C  
ATOM     12  CD  PRO A  20      11.565  -2.749 -72.115  1.00 99.01      A    C  
ANISOU   12  CD  PRO A  20    10204  21792   5622   -226    888    509  A    C  
ATOM     13  N   PRO A  21      10.936   1.814 -73.260  1.00 97.13      A    N  
ANISOU   13  N   PRO A  21    10039  21723   5142   -256    665   1390  A    N  
ATOM     14  CA  PRO A  21      11.203   3.133 -72.647  1.00 96.30      A    C  
ANISOU   14  CA  PRO A  21    10027  21422   5140   -270    648   1643  A    C  
ATOM     15  C   PRO A  21      10.405   3.446 -71.378  1.00 98.22      A    C  
ANISOU   15  C   PRO A  21    10302  21408   5609   -187    549   1658  A    C  
ATOM     16  O   PRO A  21       9.250   3.029 -71.238  1.00 96.93      A    O  
ANISOU   16  O   PRO A  21    10084  21284   5460    -95    450   1558  A    O  
ATOM     17  CB  PRO A  21      10.891   4.127 -73.772  1.00 99.98      A    C  
ANISOU   17  CB  PRO A  21    10598  22037   5354   -254    600   1864  A    C  
ATOM     18  CG  PRO A  21       9.999   3.403 -74.684  1.00105.22      A    C  
ANISOU   18  CG  PRO A  21    11190  22958   5831   -193    531   1730  A    C  
ATOM     19  CD  PRO A  21      10.432   1.971 -74.638  1.00100.19      A    C  
ANISOU   19  CD  PRO A  21    10448  22383   5235   -245    616   1436  A    C  
ATOM     20  N   MET A  22      11.040   4.213 -70.470  1.00 94.22      A    N  
ANISOU   20  N   MET A  22     9882  20661   5256   -239    579   1788  A    N  
ATOM     21  CA  MET A  22      10.527   4.642 -69.162  1.00 92.86      A    C  
ANISOU   21  CA  MET A  22     9775  20213   5295   -169    512   1815  A    C  
ATOM     22  C   MET A  22       9.216   5.444 -69.224  1.00 98.24      A    C  
ANISOU   22  C   MET A  22    10563  20854   5909     13    386   1945  A    C  
ATOM     23  O   MET A  22       8.508   5.517 -68.215  1.00 96.58      A    O  
ANISOU   23  O   MET A  22    10359  20488   5849    125    327   1916  A    O  
ATOM     24  CB  MET A  22      11.606   5.416 -68.383  1.00 95.08      A    C  
ANISOU   24  CB  MET A  22    10164  20272   5690   -308    573   1940  A    C  
ATOM     25  CG  MET A  22      12.896   4.627 -68.191  1.00 98.23      A    C  
ANISOU   25  CG  MET A  22    10406  20756   6162   -447    693   1823  A    C  
ATOM     26  SD  MET A  22      13.858   5.072 -66.726  1.00101.57      A    S  
ANISOU   26  SD  MET A  22    10869  20940   6782   -601    727   1889  A    S  
ATOM     27  CE  MET A  22      15.343   4.144 -67.050  1.00 98.43      A    C  
ANISOU   27  CE  MET A  22    10237  20823   6338   -721    879   1812  A    C  
ATOM     28  N   LYS A  23       8.882   6.016 -70.407  1.00 97.29      A    N  
ANISOU   28  N   LYS A  23    10515  20901   5549     66    351   2094  A    N  
ATOM     29  CA  LYS A  23       7.662   6.792 -70.645  1.00 98.50      A    C  
ANISOU   29  CA  LYS A  23    10759  21078   5588    288    237   2248  A    C  
ATOM     30  C   LYS A  23       6.407   5.916 -70.657  1.00104.08      A    C  
ANISOU   30  C   LYS A  23    11249  22021   6274    411    141   2091  A    C  
ATOM     31  O   LYS A  23       5.306   6.427 -70.449  1.00105.03      A    O  
ANISOU   31  O   LYS A  23    11379  22165   6361    627     46   2188  A    O  
ATOM     32  CB  LYS A  23       7.768   7.619 -71.944  1.00103.22      A    C  
ANISOU   32  CB  LYS A  23    11499  21804   5914    306    232   2471  A    C  
ATOM     33  CG  LYS A  23       7.920   6.807 -73.241  1.00105.99      A    C  
ANISOU   33  CG  LYS A  23    11694  22519   6058    209    254   2375  A    C  
ATOM     34  CD  LYS A  23       7.643   7.660 -74.468  1.00107.54      A    C  
ANISOU   34  CD  LYS A  23    12017  22880   5964    291    213   2612  A    C  
ATOM     35  CE  LYS A  23       7.856   6.914 -75.763  1.00113.29      A    C  
ANISOU   35  CE  LYS A  23    12610  23974   6461    188    240   2518  A    C  
ATOM     36  NZ  LYS A  23       6.690   6.077 -76.150  1.00117.19      A    N1+
ANISOU   36  NZ  LYS A  23    12900  24764   6865    267    136   2339  A    N1+
ATOM     37  N   ASP A  24       6.572   4.605 -70.912  1.00101.02      A    N  
ANISOU   37  N   ASP A  24    10678  21818   5886    273    168   1854  A    N  
ATOM     38  CA  ASP A  24       5.476   3.635 -70.987  1.00101.43      A    C  
ANISOU   38  CA  ASP A  24    10538  22108   5894    295     80   1681  A    C  
ATOM     39  C   ASP A  24       4.936   3.238 -69.621  1.00106.08      A    C  
ANISOU   39  C   ASP A  24    11049  22542   6716    337     51   1577  A    C  
ATOM     40  O   ASP A  24       3.793   2.786 -69.530  1.00107.35      A    O  
ANISOU   40  O   ASP A  24    11059  22898   6829    389    -47   1517  A    O  
ATOM     41  CB  ASP A  24       5.904   2.394 -71.787  1.00103.15      A    C  
ANISOU   41  CB  ASP A  24    10669  22511   6010    112    132   1455  A    C  
ATOM     42  CG  ASP A  24       6.467   2.691 -73.170  1.00110.63      A    C  
ANISOU   42  CG  ASP A  24    11680  23646   6707     64    176   1537  A    C  
ATOM     43  OD1 ASP A  24       6.137   3.765 -73.736  1.00110.89      A    O  
ANISOU   43  OD1 ASP A  24    11796  23746   6593    173    127   1777  A    O  
ATOM     44  OD2 ASP A  24       7.227   1.852 -73.689  1.00116.10      A    O1-
ANISOU   44  OD2 ASP A  24    12357  24418   7338    -65    265   1366  A    O1-
ATOM     45  N   TYR A  25       5.755   3.412 -68.565  1.00101.17      A    N  
ANISOU   45  N   TYR A  25    10512  21602   6325    296    133   1565  A    N  
ATOM     46  CA  TYR A  25       5.417   3.106 -67.171  1.00 99.26      A    C  
ANISOU   46  CA  TYR A  25    10222  21181   6313    329    122   1479  A    C  
ATOM     47  C   TYR A  25       4.877   4.370 -66.478  1.00103.29      A    C  
ANISOU   47  C   TYR A  25    10850  21532   6862    542     73   1676  A    C  
ATOM     48  O   TYR A  25       4.227   4.271 -65.438  1.00100.60      A    O  
ANISOU   48  O   TYR A  25    10449  21125   6650    632     39   1632  A    O  
ATOM     49  CB  TYR A  25       6.656   2.574 -66.414  1.00 98.84      A    C  
ANISOU   49  CB  TYR A  25    10200  20894   6460    183    236   1368  A    C  
ATOM     50  CG  TYR A  25       7.436   1.474 -67.111  1.00100.98      A    C  
ANISOU   50  CG  TYR A  25    10410  21282   6677     32    317   1195  A    C  
ATOM     51  CD1 TYR A  25       8.340   1.769 -68.133  1.00104.00      A    C  
ANISOU   51  CD1 TYR A  25    10849  21753   6915    -31    390   1263  A    C  
ATOM     52  CD2 TYR A  25       7.352   0.152 -66.680  1.00100.84      A    C  
ANISOU   52  CD2 TYR A  25    10304  21264   6746    -39    335    969  A    C  
ATOM     53  CE1 TYR A  25       9.092   0.770 -68.749  1.00104.18      A    C  
ANISOU   53  CE1 TYR A  25    10826  21889   6869   -122    483   1101  A    C  
ATOM     54  CE2 TYR A  25       8.099  -0.857 -67.290  1.00102.26      A    C  
ANISOU   54  CE2 TYR A  25    10484  21511   6861   -132    424    805  A    C  
ATOM     55  CZ  TYR A  25       8.972  -0.541 -68.322  1.00109.80      A    C  
ANISOU   55  CZ  TYR A  25    11481  22574   7663   -155    502    868  A    C  
ATOM     56  OH  TYR A  25       9.720  -1.518 -68.926  1.00110.96      A    O  
ANISOU   56  OH  TYR A  25    11636  22799   7724   -202    607    705  A    O  
ATOM     57  N   MET A  26       5.159   5.557 -67.061  1.00103.43      A    N  
ANISOU   57  N   MET A  26    11065  21480   6755    627     76   1894  A    N  
ATOM     58  CA  MET A  26       4.726   6.863 -66.563  1.00105.33      A    C  
ANISOU   58  CA  MET A  26    11511  21523   6988    857     43   2097  A    C  
ATOM     59  C   MET A  26       3.247   7.067 -66.867  1.00115.77      A    C  
ANISOU   59  C   MET A  26    12717  23118   8151   1131    -65   2177  A    C  
ATOM     60  O   MET A  26       2.885   7.762 -67.825  1.00117.33      A    O  
ANISOU   60  O   MET A  26    12987  23465   8129   1270   -108   2350  A    O  
ATOM     61  CB  MET A  26       5.582   8.000 -67.156  1.00108.83      A    C  
ANISOU   61  CB  MET A  26    12250  21771   7329    816     90   2307  A    C  
ATOM     62  CG  MET A  26       6.950   8.124 -66.522  1.00110.54      A    C  
ANISOU   62  CG  MET A  26    12589  21708   7702    567    187   2276  A    C  
ATOM     63  SD  MET A  26       7.870   9.551 -67.133  1.00116.25      A    S  
ANISOU   63  SD  MET A  26    13680  22210   8281    454    235   2541  A    S  
ATOM     64  CE  MET A  26       9.429   9.263 -66.363  1.00111.13      A    C  
ANISOU   64  CE  MET A  26    13024  21384   7817    111    334   2447  A    C  
ATOM     65  N   ILE A  27       2.394   6.430 -66.050  1.00115.49      A    N  
ANISOU   65  N   ILE A  27    12484  23186   8213   1204   -108   2058  A    N  
ATOM     66  CA  ILE A  27       0.936   6.495 -66.172  1.00118.69      A    C  
ANISOU   66  CA  ILE A  27    12701  23927   8468   1452   -210   2123  A    C  
ATOM     67  C   ILE A  27       0.375   7.484 -65.143  1.00127.04      A    C  
ANISOU   67  C   ILE A  27    13894  24796   9578   1780   -211   2258  A    C  
ATOM     68  O   ILE A  27       0.648   7.369 -63.942  1.00124.84      A    O  
ANISOU   68  O   ILE A  27    13661  24265   9507   1745   -162   2166  A    O  
ATOM     69  CB  ILE A  27       0.260   5.092 -66.119  1.00121.08      A    C  
ANISOU   69  CB  ILE A  27    12659  24573   8772   1275   -264   1909  A    C  
ATOM     70  CG1 ILE A  27       0.863   4.142 -67.182  1.00121.26      A    C  
ANISOU   70  CG1 ILE A  27    12627  24726   8719    970   -247   1762  A    C  
ATOM     71  CG2 ILE A  27      -1.255   5.212 -66.299  1.00124.17      A    C  
ANISOU   71  CG2 ILE A  27    12809  25405   8964   1499   -379   2001  A    C  
ATOM     72  CD1 ILE A  27       0.847   2.673 -66.815  1.00126.95      A    C  
ANISOU   72  CD1 ILE A  27    13174  25522   9538    699   -241   1496  A    C  
ATOM     73  N   LEU A  28      -0.385   8.475 -65.649  1.00129.32      A    N  
ANISOU   73  N   LEU A  28    14269  25208   9658   2121   -262   2482  A    N  
ATOM     74  CA  LEU A  28      -1.021   9.574 -64.915  1.00131.91      A    C  
ANISOU   74  CA  LEU A  28    14780  25381   9959   2531   -259   2649  A    C  
ATOM     75  C   LEU A  28      -2.093  10.198 -65.805  1.00141.08      A    C  
ANISOU   75  C   LEU A  28    15866  26913  10827   2902   -341   2866  A    C  
ATOM     76  O   LEU A  28      -1.926  10.250 -67.031  1.00142.54      A    O  
ANISOU   76  O   LEU A  28    16025  27298  10834   2829   -382   2941  A    O  
ATOM     77  CB  LEU A  28       0.016  10.645 -64.475  1.00132.22      A    C  
ANISOU   77  CB  LEU A  28    15309  24844  10085   2539   -171   2750  A    C  
ATOM     78  CG  LEU A  28       0.859  11.339 -65.571  1.00139.13      A    C  
ANISOU   78  CG  LEU A  28    16481  25565  10818   2461   -152   2919  A    C  
ATOM     79  CD1 LEU A  28       1.160  12.777 -65.203  1.00141.33      A    C  
ANISOU   79  CD1 LEU A  28    17279  25343  11079   2638    -97   3100  A    C  
ATOM     80  CD2 LEU A  28       2.139  10.563 -65.878  1.00139.88      A    C  
ANISOU   80  CD2 LEU A  28    16509  25628  11012   1992   -106   2775  A    C  
ATOM     81  N   SER A  29      -3.191  10.664 -65.202  1.00139.55      A    N  
ANISOU   81  N   SER A  29    15626  26837  10562   3320   -363   2973  A    N  
ATOM     82  CA  SER A  29      -4.276  11.262 -65.970  1.00143.38      A    C  
ANISOU   82  CA  SER A  29    16005  27724  10749   3738   -441   3199  A    C  
ATOM     83  C   SER A  29      -4.704  12.633 -65.426  1.00150.58      A    C  
ANISOU   83  C   SER A  29    17270  28366  11577   4288   -394   3421  A    C  
ATOM     84  O   SER A  29      -5.686  12.739 -64.684  1.00151.77      A    O  
ANISOU   84  O   SER A  29    17255  28720  11689   4635   -399   3451  A    O  
ATOM     85  CB  SER A  29      -5.448  10.290 -66.096  1.00147.81      A    C  
ANISOU   85  CB  SER A  29    16006  28952  11203   3724   -540   3119  A    C  
ATOM     86  OG  SER A  29      -5.051   9.085 -66.731  1.00154.41      A    O  
ANISOU   86  OG  SER A  29    16602  29992  12076   3224   -581   2916  A    O  
ATOM     87  N   GLY A  30      -3.931  13.657 -65.804  1.00148.37      A    N  
ANISOU   87  N   GLY A  30    17495  27625  11256   4350   -342   3576  A    N  
ATOM     88  CA  GLY A  30      -4.140  15.064 -65.465  1.00151.20      A    C  
ANISOU   88  CA  GLY A  30    18339  27606  11506   4839   -287   3800  A    C  
ATOM     89  C   GLY A  30      -4.323  15.403 -63.994  1.00153.73      A    C  
ANISOU   89  C   GLY A  30    18838  27597  11977   5039   -210   3722  A    C  
ATOM     90  O   GLY A  30      -3.349  15.374 -63.234  1.00151.02      A    O  
ANISOU   90  O   GLY A  30    18739  26784  11859   4709   -142   3574  A    O  
ATOM     91  N   PRO A  31      -5.570  15.741 -63.561  1.00151.68      A    N  
ANISOU   91  N   PRO A  31    18447  27611  11574   5592   -217   3825  A    N  
ATOM     92  CA  PRO A  31      -5.792  16.107 -62.151  1.00150.80      A    C  
ANISOU   92  CA  PRO A  31    18523  27199  11576   5827   -132   3752  A    C  
ATOM     93  C   PRO A  31      -5.604  14.975 -61.142  1.00149.63      A    C  
ANISOU   93  C   PRO A  31    18024  27135  11693   5430   -122   3467  A    C  
ATOM     94  O   PRO A  31      -5.474  15.263 -59.949  1.00149.11      A    O  
ANISOU   94  O   PRO A  31    18183  26720  11753   5508    -44   3381  A    O  
ATOM     95  CB  PRO A  31      -7.228  16.650 -62.141  1.00156.83      A    C  
ANISOU   95  CB  PRO A  31    19149  28367  12073   6542   -144   3953  A    C  
ATOM     96  CG  PRO A  31      -7.572  16.900 -63.578  1.00164.21      A    C  
ANISOU   96  CG  PRO A  31    19996  29652  12744   6716   -227   4179  A    C  
ATOM     97  CD  PRO A  31      -6.823  15.858 -64.332  1.00156.65      A    C  
ANISOU   97  CD  PRO A  31    18756  28857  11905   6053   -297   4026  A    C  
ATOM     98  N   GLN A  32      -5.575  13.700 -61.597  1.00142.85      A    N  
ANISOU   98  N   GLN A  32    16658  26711  10906   5005   -196   3320  A    N  
ATOM     99  CA  GLN A  32      -5.355  12.579 -60.678  1.00138.41      A    C  
ANISOU   99  CA  GLN A  32    15803  26199  10589   4619   -183   3060  A    C  
ATOM    100  C   GLN A  32      -3.883  12.516 -60.224  1.00137.27      A    C  
ANISOU  100  C   GLN A  32    15996  25465  10697   4174   -117   2910  A    C  
ATOM    101  O   GLN A  32      -3.608  12.046 -59.121  1.00133.87      A    O  
ANISOU  101  O   GLN A  32    15510  24886  10467   3988    -76   2735  A    O  
ATOM    102  CB  GLN A  32      -5.884  11.240 -61.234  1.00138.64      A    C  
ANISOU  102  CB  GLN A  32    15235  26853  10589   4326   -278   2948  A    C  
ATOM    103  CG  GLN A  32      -5.024  10.566 -62.294  1.00150.20      A    C  
ANISOU  103  CG  GLN A  32    16655  28323  12092   3846   -319   2861  A    C  
ATOM    104  CD  GLN A  32      -5.477   9.153 -62.562  1.00165.61      A    C  
ANISOU  104  CD  GLN A  32    18094  30791  14040   3512   -397   2698  A    C  
ATOM    106  NE2 GLN A  32      -4.724   8.187 -62.057  1.00151.73      A    N  
ANISOU  106  NE2 GLN A  32    16291  28848  12511   3061   -364   2468  A    N  
ATOM    105  OE1 GLN A  32      -6.497   8.910 -63.219  1.00163.44      A    O  
ANISOU  105  OE1 GLN A  32    17473  31087  13541   3648   -488   2780  A    O  
ATOM    107  N   LYS A  33      -2.962  13.043 -61.065  1.00133.56      A    N  
ANISOU  107  N   LYS A  33    15868  24685  10192   4020   -108   2998  A    N  
ATOM    108  CA  LYS A  33      -1.525  13.148 -60.811  1.00130.76      A    C  
ANISOU  108  CA  LYS A  33    15839  23823  10021   3609    -49   2907  A    C  
ATOM    109  C   LYS A  33      -1.245  14.228 -59.760  1.00135.32      A    C  
ANISOU  109  C   LYS A  33    16918  23855  10643   3793     28   2943  A    C  
ATOM    110  O   LYS A  33      -0.324  14.063 -58.954  1.00132.91      A    O  
ANISOU  110  O   LYS A  33    16737  23231  10532   3471     73   2798  A    O  
ATOM    111  CB  LYS A  33      -0.773  13.470 -62.107  1.00133.90      A    C  
ANISOU  111  CB  LYS A  33    16426  24137  10312   3419    -61   3027  A    C  
ATOM    112  N   THR A  34      -2.041  15.326 -59.764  1.00134.95      A    N  
ANISOU  112  N   THR A  34    17171  23708  10397   4322     44   3138  A    N  
ATOM    113  CA  THR A  34      -1.923  16.430 -58.796  1.00136.25      A    C  
ANISOU  113  CA  THR A  34    17882  23336  10553   4566    122   3176  A    C  
ATOM    114  C   THR A  34      -2.405  15.990 -57.405  1.00137.64      A    C  
ANISOU  114  C   THR A  34    17856  23584  10856   4673    155   3008  A    C  
ATOM    115  O   THR A  34      -1.966  16.551 -56.398  1.00136.68      A    O  
ANISOU  115  O   THR A  34    18120  23001  10811   4646    219   2938  A    O  
ATOM    116  CB  THR A  34      -2.627  17.711 -59.281  1.00149.17      A    C  
ANISOU  116  CB  THR A  34    19934  24831  11913   5146    140   3439  A    C  
ATOM    118  CG2 THR A  34      -2.095  18.216 -60.625  1.00149.88      A    C  
ANISOU  118  CG2 THR A  34    20304  24775  11868   5015    116   3623  A    C  
ATOM    117  OG1 THR A  34      -4.035  17.493 -59.340  1.00150.33      A    O  
ANISOU  117  OG1 THR A  34    19673  25538  11909   5642    105   3517  A    O  
ATOM    119  N   ALA A  35      -3.302  14.979 -57.362  1.00132.72      A    N  
ANISOU  119  N   ALA A  35    16637  23553  10238   4763    109   2944  A    N  
ATOM    120  CA  ALA A  35      -3.826  14.395 -56.131  1.00130.96      A    C  
ANISOU  120  CA  ALA A  35    16133  23503  10124   4825    136   2793  A    C  
ATOM    121  C   ALA A  35      -2.724  13.583 -55.437  1.00130.23      A    C  
ANISOU  121  C   ALA A  35    15986  23189  10306   4257    150   2567  A    C  
ATOM    122  O   ALA A  35      -2.597  13.669 -54.216  1.00129.47      A    O  
ANISOU  122  O   ALA A  35    15992  22890  10312   4270    203   2458  A    O  
ATOM    123  CB  ALA A  35      -5.032  13.517 -56.429  1.00132.11      A    C  
ANISOU  123  CB  ALA A  35    15648  24370  10180   4965     72   2802  A    C  
ATOM    124  N   VAL A  36      -1.903  12.832 -56.213  1.00123.48      A    N  
ANISOU  124  N   VAL A  36    14988  22377   9550   3786    109   2505  A    N  
ATOM    125  CA  VAL A  36      -0.774  12.056 -55.671  1.00119.18      A    C  
ANISOU  125  CA  VAL A  36    14390  21648   9245   3273    125   2315  A    C  
ATOM    126  C   VAL A  36       0.341  13.024 -55.261  1.00122.27      A    C  
ANISOU  126  C   VAL A  36    15332  21449   9676   3133    177   2337  A    C  
ATOM    127  O   VAL A  36       1.045  12.764 -54.290  1.00119.12      A    O  
ANISOU  127  O   VAL A  36    14994  20830   9437   2886    208   2201  A    O  
ATOM    128  CB  VAL A  36      -0.217  10.951 -56.614  1.00120.87      A    C  
ANISOU  128  CB  VAL A  36    14278  22121   9525   2862     79   2239  A    C  
ATOM    129  CG1 VAL A  36       0.344   9.788 -55.808  1.00117.20      A    C  
ANISOU  129  CG1 VAL A  36    13628  21608   9293   2460    100   2032  A    C  
ATOM    130  CG2 VAL A  36      -1.262  10.450 -57.600  1.00121.66      A    C  
ANISOU  130  CG2 VAL A  36    13955  22780   9492   3003     10   2274  A    C  
ATOM    131  N   ALA A  37       0.484  14.145 -56.004  1.00121.74      A    N  
ANISOU  131  N   ALA A  37    15674  21137   9444   3275    183   2518  A    N  
ATOM    132  CA  ALA A  37       1.483  15.193 -55.772  1.00122.57      A    C  
ANISOU  132  CA  ALA A  37    16360  20675   9535   3112    225   2569  A    C  
ATOM    133  C   ALA A  37       1.346  15.856 -54.398  1.00126.28      A    C  
ANISOU  133  C   ALA A  37    17188  20776  10018   3296    278   2512  A    C  
ATOM    134  O   ALA A  37       2.360  16.226 -53.809  1.00125.43      A    O  
ANISOU  134  O   ALA A  37    17419  20264   9975   2977    303   2454  A    O  
ATOM    135  CB  ALA A  37       1.413  16.241 -56.872  1.00126.69      A    C  
ANISOU  135  CB  ALA A  37    17258  21039   9841   3294    220   2798  A    C  
ATOM    136  N   VAL A  38       0.108  15.997 -53.889  1.00123.52      A    N  
ANISOU  136  N   VAL A  38    16752  20595   9586   3800    297   2527  A    N  
ATOM    137  CA  VAL A  38      -0.135  16.590 -52.573  1.00124.25      A    C  
ANISOU  137  CA  VAL A  38    17163  20382   9663   4038    360   2462  A    C  
ATOM    138  C   VAL A  38      -0.113  15.492 -51.473  1.00124.45      A    C  
ANISOU  138  C   VAL A  38    16772  20624   9890   3829    362   2252  A    C  
ATOM    139  O   VAL A  38       0.443  15.729 -50.397  1.00123.44      A    O  
ANISOU  139  O   VAL A  38    16907  20163   9833   3680    398   2141  A    O  
ATOM    140  CB  VAL A  38      -1.394  17.511 -52.544  1.00132.00      A    C  
ANISOU  140  CB  VAL A  38    18367  21379  10409   4749    403   2612  A    C  
ATOM    141  CG1 VAL A  38      -2.701  16.727 -52.654  1.00131.62      A    C  
ANISOU  141  CG1 VAL A  38    17690  22000  10319   5087    377   2629  A    C  
ATOM    142  CG2 VAL A  38      -1.398  18.423 -51.322  1.00133.83      A    C  
ANISOU  142  CG2 VAL A  38    19128  21142  10580   4988    484   2557  A    C  
ATOM    143  N   LEU A  39      -0.655  14.285 -51.780  1.00118.57      A    N  
ANISOU  143  N   LEU A  39    15405  20421   9225   3772    319   2199  A    N  
ATOM    144  CA  LEU A  39      -0.717  13.136 -50.871  1.00115.29      A    C  
ANISOU  144  CA  LEU A  39    14572  20247   8985   3570    318   2023  A    C  
ATOM    145  C   LEU A  39       0.670  12.579 -50.536  1.00115.50      A    C  
ANISOU  145  C   LEU A  39    14619  20054   9213   3010    309   1889  A    C  
ATOM    146  O   LEU A  39       1.012  12.501 -49.359  1.00114.03      A    O  
ANISOU  146  O   LEU A  39    14515  19692   9120   2902    339   1774  A    O  
ATOM    147  CB  LEU A  39      -1.629  12.033 -51.441  1.00114.50      A    C  
ANISOU  147  CB  LEU A  39    13867  20753   8883   3604    268   2019  A    C  
ATOM    148  CG  LEU A  39      -1.896  10.830 -50.534  1.00117.04      A    C  
ANISOU  148  CG  LEU A  39    13765  21359   9345   3449    270   1865  A    C  
ATOM    149  CD1 LEU A  39      -3.152  11.031 -49.713  1.00119.24      A    C  
ANISOU  149  CD1 LEU A  39    13906  21898   9500   3903    306   1900  A    C  
ATOM    150  CD2 LEU A  39      -2.014   9.566 -51.345  1.00118.02      A    C  
ANISOU  150  CD2 LEU A  39    13421  21887   9535   3147    207   1812  A    C  
ATOM    151  N   CYS A  40       1.456  12.199 -51.564  1.00110.55      A    N  
ANISOU  151  N   CYS A  40    13906  19468   8630   2676    272   1911  A    N  
ATOM    152  CA  CYS A  40       2.809  11.651 -51.422  1.00107.78      A    C  
ANISOU  152  CA  CYS A  40    13528  18985   8439   2174    268   1812  A    C  
ATOM    153  C   CYS A  40       3.749  12.608 -50.699  1.00111.98      A    C  
ANISOU  153  C   CYS A  40    14547  19034   8964   2009    295   1811  A    C  
ATOM    154  O   CYS A  40       4.583  12.152 -49.913  1.00110.09      A    O  
ANISOU  154  O   CYS A  40    14253  18719   8858   1689    298   1698  A    O  
ATOM    155  CB  CYS A  40       3.370  11.225 -52.777  1.00107.60      A    C  
ANISOU  155  CB  CYS A  40    13344  19130   8411   1933    237   1861  A    C  
ATOM    156  SG  CYS A  40       4.912  10.279 -52.685  1.00108.59      A    S  
ANISOU  156  SG  CYS A  40    13278  19260   8720   1389    243   1735  A    S  
ATOM    157  N   THR A  41       3.594  13.929 -50.940  1.00110.90      A    N  
ANISOU  157  N   THR A  41    14906  18575   8656   2227    313   1940  A    N  
ATOM    158  CA  THR A  41       4.387  14.986 -50.304  1.00111.93      A    C  
ANISOU  158  CA  THR A  41    15592  18204   8734   2062    335   1945  A    C  
ATOM    159  C   THR A  41       4.056  15.091 -48.810  1.00115.32      A    C  
ANISOU  159  C   THR A  41    16137  18488   9191   2207    368   1820  A    C  
ATOM    160  O   THR A  41       4.978  15.062 -47.992  1.00113.95      A    O  
ANISOU  160  O   THR A  41    16085  18120   9089   1858    364   1723  A    O  
ATOM    161  CB  THR A  41       4.249  16.308 -51.077  1.00120.66      A    C  
ANISOU  161  CB  THR A  41    17231  18984   9628   2250    348   2127  A    C  
ATOM    163  CG2 THR A  41       5.037  17.453 -50.445  1.00120.02      A    C  
ANISOU  163  CG2 THR A  41    17794  18344   9463   2020    368   2133  A    C  
ATOM    162  OG1 THR A  41       4.702  16.098 -52.418  1.00118.45      A    O  
ANISOU  162  OG1 THR A  41    16793  18884   9330   2059    318   2234  A    O  
ATOM    164  N   LEU A  42       2.751  15.184 -48.457  1.00112.78      A    N  
ANISOU  164  N   LEU A  42    15746  18309   8797   2717    399   1828  A    N  
ATOM    165  CA  LEU A  42       2.290  15.287 -47.065  1.00112.50      A    C  
ANISOU  165  CA  LEU A  42    15798  18188   8760   2922    444   1716  A    C  
ATOM    166  C   LEU A  42       2.586  14.043 -46.229  1.00111.81      A    C  
ANISOU  166  C   LEU A  42    15250  18360   8871   2635    428   1559  A    C  
ATOM    167  O   LEU A  42       3.052  14.193 -45.103  1.00111.08      A    O  
ANISOU  167  O   LEU A  42    15347  18046   8812   2477    442   1453  A    O  
ATOM    168  CB  LEU A  42       0.808  15.668 -46.981  1.00114.93      A    C  
ANISOU  168  CB  LEU A  42    16092  18661   8914   3565    492   1786  A    C  
ATOM    169  CG  LEU A  42       0.518  17.166 -47.020  1.00124.06      A    C  
ANISOU  169  CG  LEU A  42    17904  19394   9837   3963    542   1906  A    C  
ATOM    170  CD1 LEU A  42      -0.822  17.447 -47.667  1.00126.59      A    C  
ANISOU  170  CD1 LEU A  42    18068  20034   9995   4590    569   2046  A    C  
ATOM    171  CD2 LEU A  42       0.574  17.779 -45.628  1.00128.34      A    C  
ANISOU  171  CD2 LEU A  42    18944  19509  10311   4043    603   1799  A    C  
ATOM    172  N   LEU A  43       2.353  12.830 -46.778  1.00105.69      A    N  
ANISOU  172  N   LEU A  43    13910  18033   8213   2552    396   1544  A    N  
ATOM    173  CA  LEU A  43       2.638  11.566 -46.085  1.00102.61      A    C  
ANISOU  173  CA  LEU A  43    13100  17880   8005   2285    383   1410  A    C  
ATOM    174  C   LEU A  43       4.141  11.363 -45.891  1.00105.70      A    C  
ANISOU  174  C   LEU A  43    13567  18083   8512   1787    358   1350  A    C  
ATOM    175  O   LEU A  43       4.567  10.978 -44.802  1.00104.09      A    O  
ANISOU  175  O   LEU A  43    13295  17854   8400   1615    362   1245  A    O  
ATOM    176  CB  LEU A  43       2.033  10.346 -46.808  1.00101.00      A    C  
ANISOU  176  CB  LEU A  43    12353  18153   7869   2289    355   1411  A    C  
ATOM    177  CG  LEU A  43       0.505  10.240 -46.911  1.00107.24      A    C  
ANISOU  177  CG  LEU A  43    12905  19290   8553   2714    368   1460  A    C  
ATOM    178  CD1 LEU A  43       0.112   9.032 -47.728  1.00106.11      A    C  
ANISOU  178  CD1 LEU A  43    12272  19586   8459   2590    324   1454  A    C  
ATOM    179  CD2 LEU A  43      -0.159  10.152 -45.545  1.00109.63      A    C  
ANISOU  179  CD2 LEU A  43    13146  19652   8858   2896    416   1383  A    C  
ATOM    180  N   GLY A  44       4.918  11.653 -46.938  1.00103.31      A    N  
ANISOU  180  N   GLY A  44    13391  17681   8182   1570    334   1432  A    N  
ATOM    181  CA  GLY A  44       6.374  11.539 -46.942  1.00102.45      A    C  
ANISOU  181  CA  GLY A  44    13326  17457   8142   1101    312   1409  A    C  
ATOM    182  C   GLY A  44       7.072  12.474 -45.973  1.00108.27      A    C  
ANISOU  182  C   GLY A  44    14501  17818   8819    927    314   1378  A    C  
ATOM    183  O   GLY A  44       8.123  12.122 -45.428  1.00106.84      A    O  
ANISOU  183  O   GLY A  44    14235  17643   8717    569    294   1314  A    O  
ATOM    184  N   LEU A  45       6.492  13.674 -45.753  1.00107.65      A    N  
ANISOU  184  N   LEU A  45    14909  17413   8580   1187    338   1426  A    N  
ATOM    185  CA  LEU A  45       7.026  14.680 -44.836  1.00109.30      A    C  
ANISOU  185  CA  LEU A  45    15633  17208   8688   1037    341   1386  A    C  
ATOM    186  C   LEU A  45       6.706  14.284 -43.403  1.00110.46      A    C  
ANISOU  186  C   LEU A  45    15688  17395   8887   1136    358   1244  A    C  
ATOM    187  O   LEU A  45       7.553  14.444 -42.527  1.00110.04      A    O  
ANISOU  187  O   LEU A  45    15794  17184   8831    818    336   1166  A    O  
ATOM    188  CB  LEU A  45       6.464  16.080 -45.157  1.00113.50      A    C  
ANISOU  188  CB  LEU A  45    16775  17341   9009   1328    374   1483  A    C  
ATOM    189  CG  LEU A  45       7.150  17.267 -44.463  1.00121.65      A    C  
ANISOU  189  CG  LEU A  45    18466  17861   9894   1078    371   1459  A    C  
ATOM    190  CD1 LEU A  45       8.434  17.670 -45.187  1.00122.84      A    C  
ANISOU  190  CD1 LEU A  45    18791  17878  10003    555    327   1553  A    C  
ATOM    191  CD2 LEU A  45       6.216  18.457 -44.374  1.00128.06      A    C  
ANISOU  191  CD2 LEU A  45    19876  18281  10501   1550    431   1502  A    C  
ATOM    192  N   LEU A  46       5.490  13.757 -43.173  1.00105.44      A    N  
ANISOU  192  N   LEU A  46    14774  17007   8282   1555    395   1218  A    N  
ATOM    193  CA  LEU A  46       5.023  13.306 -41.864  1.00104.10      A    C  
ANISOU  193  CA  LEU A  46    14467  16936   8151   1691    422   1100  A    C  
ATOM    194  C   LEU A  46       5.761  12.048 -41.409  1.00104.03      A    C  
ANISOU  194  C   LEU A  46    14012  17188   8328   1332    386   1020  A    C  
ATOM    195  O   LEU A  46       6.153  11.974 -40.245  1.00102.89      A    O  
ANISOU  195  O   LEU A  46    13921  16976   8195   1205    384    925  A    O  
ATOM    196  CB  LEU A  46       3.502  13.054 -41.890  1.00104.56      A    C  
ANISOU  196  CB  LEU A  46    14293  17264   8171   2213    473   1124  A    C  
ATOM    197  CG  LEU A  46       2.559  14.121 -41.291  1.00112.77      A    C  
ANISOU  197  CG  LEU A  46    15742  18091   9014   2700    544   1128  A    C  
ATOM    198  CD1 LEU A  46       2.728  14.261 -39.780  1.00113.28      A    C  
ANISOU  198  CD1 LEU A  46    15989  18001   9052   2666    575    992  A    C  
ATOM    199  CD2 LEU A  46       2.643  15.463 -42.024  1.00118.60      A    C  
ANISOU  199  CD2 LEU A  46    17061  18424   9576   2842    556   1232  A    C  
ATOM    200  N   SER A  47       5.970  11.074 -42.330  1.00 98.34      A    N  
ANISOU  200  N   SER A  47    12878  16754   7732   1181    359   1059  A    N  
ATOM    201  CA  SER A  47       6.670   9.814 -42.050  1.00 95.16      A    C  
ANISOU  201  CA  SER A  47    12070  16593   7495    887    335    999  A    C  
ATOM    202  C   SER A  47       8.122  10.044 -41.642  1.00 98.46      A    C  
ANISOU  202  C   SER A  47    12638  16855   7916    466    297    981  A    C  
ATOM    203  O   SER A  47       8.574   9.460 -40.654  1.00 96.51      A    O  
ANISOU  203  O   SER A  47    12245  16688   7736    313    285    909  A    O  
ATOM    204  CB  SER A  47       6.601   8.873 -43.248  1.00 96.72      A    C  
ANISOU  204  CB  SER A  47    11883  17081   7784    852    326   1042  A    C  
ATOM    205  OG  SER A  47       7.180   7.618 -42.933  1.00102.96      A    O  
ANISOU  205  OG  SER A  47    12322  18080   8720    640    317    981  A    O  
ATOM    206  N   ALA A  48       8.835  10.915 -42.388  1.00 96.35      A    N  
ANISOU  206  N   ALA A  48    12662  16389   7556    271    276   1058  A    N  
ATOM    207  CA  ALA A  48      10.230  11.275 -42.131  1.00 96.72      A    C  
ANISOU  207  CA  ALA A  48    12861  16325   7564   -176    233   1066  A    C  
ATOM    208  C   ALA A  48      10.390  12.002 -40.790  1.00101.42      A    C  
ANISOU  208  C   ALA A  48    13817  16660   8059   -257    219    986  A    C  
ATOM    209  O   ALA A  48      11.327  11.698 -40.049  1.00100.39      A    O  
ANISOU  209  O   ALA A  48    13589  16609   7947   -579    178    944  A    O  
ATOM    210  CB  ALA A  48      10.772  12.129 -43.268  1.00 99.33      A    C  
ANISOU  210  CB  ALA A  48    13456  16499   7787   -353    222   1182  A    C  
ATOM    211  N   LEU A  49       9.456  12.923 -40.463  1.00 99.59      A    N  
ANISOU  211  N   LEU A  49    13992  16143   7706     59    255    964  A    N  
ATOM    212  CA  LEU A  49       9.483  13.685 -39.211  1.00101.18      A    C  
ANISOU  212  CA  LEU A  49    14607  16058   7780     33    254    871  A    C  
ATOM    213  C   LEU A  49       9.133  12.842 -37.975  1.00102.67      A    C  
ANISOU  213  C   LEU A  49    14506  16454   8050    141    265    761  A    C  
ATOM    214  O   LEU A  49       9.625  13.131 -36.881  1.00103.11      A    O  
ANISOU  214  O   LEU A  49    14768  16382   8027    -50    239    677  A    O  
ATOM    215  CB  LEU A  49       8.612  14.950 -39.297  1.00104.38      A    C  
ANISOU  215  CB  LEU A  49    15579  16076   8004    390    306    885  A    C  
ATOM    216  CG  LEU A  49       9.231  16.128 -40.068  1.00112.21      A    C  
ANISOU  216  CG  LEU A  49    17098  16696   8842    167    286    976  A    C  
ATOM    217  CD1 LEU A  49       8.163  17.067 -40.581  1.00115.21      A    C  
ANISOU  217  CD1 LEU A  49    17892  16800   9084    657    352   1041  A    C  
ATOM    218  CD2 LEU A  49      10.236  16.898 -39.215  1.00116.73      A    C  
ANISOU  218  CD2 LEU A  49    18134  16950   9267   -277    239    907  A    C  
ATOM    219  N   GLU A  50       8.312  11.792 -38.153  1.00 96.49      A    N  
ANISOU  219  N   GLU A  50    13257  15996   7409    412    299    764  A    N  
ATOM    220  CA  GLU A  50       7.930  10.884 -37.069  1.00 94.48      A    C  
ANISOU  220  CA  GLU A  50    12701  15962   7235    507    315    683  A    C  
ATOM    221  C   GLU A  50       9.079   9.924 -36.730  1.00 96.90      A    C  
ANISOU  221  C   GLU A  50    12671  16486   7660    127    261    672  A    C  
ATOM    222  O   GLU A  50       9.324   9.667 -35.548  1.00 96.72      A    O  
ANISOU  222  O   GLU A  50    12617  16504   7629     41    247    603  A    O  
ATOM    223  CB  GLU A  50       6.664  10.095 -37.431  1.00 94.24      A    C  
ANISOU  223  CB  GLU A  50    12317  16204   7286    889    369    703  A    C  
ATOM    224  CG  GLU A  50       5.366  10.841 -37.184  1.00103.32      A    C  
ANISOU  224  CG  GLU A  50    13715  17246   8296   1346    436    694  A    C  
ATOM    225  CD  GLU A  50       4.138  10.123 -37.707  1.00115.64      A    C  
ANISOU  225  CD  GLU A  50    14904  19133   9903   1686    477    745  A    C  
ATOM    226  OE1 GLU A  50       3.827   9.025 -37.194  1.00 98.19      A    O  
ANISOU  226  OE1 GLU A  50    12296  17219   7792   1683    488    714  A    O  
ATOM    227  OE2 GLU A  50       3.483  10.657 -38.631  1.00113.23      A    O1-
ANISOU  227  OE2 GLU A  50    14709  18797   9517   1941    495    824  A    O1-
ATOM    228  N   ASN A  51       9.777   9.396 -37.762  1.00 91.84      A    N  
ANISOU  228  N   ASN A  51    11779  16003   7113    -73    235    746  A    N  
ATOM    229  CA  ASN A  51      10.896   8.464 -37.598  1.00 89.88      A    C  
ANISOU  229  CA  ASN A  51    11197  15992   6962   -376    195    757  A    C  
ATOM    230  C   ASN A  51      12.167   9.133 -37.048  1.00 96.56      A    C  
ANISOU  230  C   ASN A  51    12255  16739   7695   -780    130    759  A    C  
ATOM    231  O   ASN A  51      12.817   8.560 -36.166  1.00 95.72      A    O  
ANISOU  231  O   ASN A  51    11949  16807   7613   -958     96    738  A    O  
ATOM    232  CB  ASN A  51      11.173   7.697 -38.890  1.00 85.38      A    C  
ANISOU  232  CB  ASN A  51    10302  15636   6502   -401    206    828  A    C  
ATOM    233  CG  ASN A  51      10.188   6.581 -39.139  1.00 93.51      A    C  
ANISOU  233  CG  ASN A  51    11016  16858   7654   -118    251    809  A    C  
ATOM    235  ND2 ASN A  51       9.239   6.814 -40.031  1.00 88.58      A    N  
ANISOU  235  ND2 ASN A  51    10432  16211   7012    112    279    837  A    N  
ATOM    234  OD1 ASN A  51      10.262   5.504 -38.540  1.00 77.64      A    O  
ANISOU  234  OD1 ASN A  51     8734  15025   5739   -115    259    777  A    O  
ATOM    236  N   VAL A  52      12.493  10.361 -37.535  1.00 95.49      A    N  
ANISOU  236  N   VAL A  52    12539  16328   7415   -933    111    790  A    N  
ATOM    237  CA  VAL A  52      13.659  11.145 -37.094  1.00 97.17      A    C  
ANISOU  237  CA  VAL A  52    13015  16426   7479  -1379     42    795  A    C  
ATOM    238  C   VAL A  52      13.545  11.535 -35.600  1.00101.10      A    C  
ANISOU  238  C   VAL A  52    13764  16779   7870  -1411     18    682  A    C  
ATOM    239  O   VAL A  52      14.561  11.805 -34.961  1.00101.91      A    O  
ANISOU  239  O   VAL A  52    13934  16920   7869  -1806    -54    669  A    O  
ATOM    240  CB  VAL A  52      13.954  12.355 -38.026  1.00103.59      A    C  
ANISOU  240  CB  VAL A  52    14251  16955   8152  -1563     32    868  A    C  
ATOM    241  CG1 VAL A  52      13.027  13.537 -37.747  1.00105.70      A    C  
ANISOU  241  CG1 VAL A  52    15112  16772   8276  -1325     65    813  A    C  
ATOM    242  CG2 VAL A  52      15.422  12.774 -37.951  1.00105.34      A    C  
ANISOU  242  CG2 VAL A  52    14537  17237   8251  -2136    -46    918  A    C  
ATOM    243  N   ALA A  53      12.315  11.534 -35.053  1.00 97.09      A    N  
ANISOU  243  N   ALA A  53    13367  16150   7371   -998     78    605  A    N  
ATOM    244  CA  ALA A  53      12.063  11.800 -33.641  1.00 98.05      A    C  
ANISOU  244  CA  ALA A  53    13705  16160   7388   -953     75    491  A    C  
ATOM    245  C   ALA A  53      12.494  10.567 -32.834  1.00100.11      A    C  
ANISOU  245  C   ALA A  53    13490  16787   7759  -1037     47    478  A    C  
ATOM    246  O   ALA A  53      13.208  10.716 -31.841  1.00100.41      A    O  
ANISOU  246  O   ALA A  53    13611  16847   7692  -1305    -14    428  A    O  
ATOM    247  CB  ALA A  53      10.589  12.092 -33.415  1.00 99.09      A    C  
ANISOU  247  CB  ALA A  53    14035  16125   7491   -443    165    435  A    C  
ATOM    248  N   VAL A  54      12.108   9.349 -33.307  1.00 94.23      A    N  
ANISOU  248  N   VAL A  54    12267  16326   7209   -829     86    529  A    N  
ATOM    249  CA  VAL A  54      12.439   8.046 -32.701  1.00 92.05      A    C  
ANISOU  249  CA  VAL A  54    11544  16378   7051   -853     74    540  A    C  
ATOM    250  C   VAL A  54      13.964   7.828 -32.681  1.00 96.49      A    C  
ANISOU  250  C   VAL A  54    11933  17138   7591  -1265     -8    600  A    C  
ATOM    251  O   VAL A  54      14.492   7.297 -31.704  1.00 95.95      A    O  
ANISOU  251  O   VAL A  54    11700  17253   7504  -1378    -47    591  A    O  
ATOM    252  CB  VAL A  54      11.656   6.872 -33.368  1.00 93.25      A    C  
ANISOU  252  CB  VAL A  54    11315  16726   7392   -562    139    581  A    C  
ATOM    253  CG1 VAL A  54      12.090   5.507 -32.826  1.00 91.09      A    C  
ANISOU  253  CG1 VAL A  54    10635  16744   7232   -601    131    608  A    C  
ATOM    254  CG2 VAL A  54      10.151   7.051 -33.192  1.00 93.21      A    C  
ANISOU  254  CG2 VAL A  54    11420  16621   7376   -176    212    532  A    C  
ATOM    255  N   LEU A  55      14.664   8.271 -33.736  1.00 94.15      A    N  
ANISOU  255  N   LEU A  55    11669  16832   7271  -1485    -32    673  A    N  
ATOM    256  CA  LEU A  55      16.119   8.167 -33.818  1.00 95.16      A    C  
ANISOU  256  CA  LEU A  55    11613  17200   7345  -1883   -104    748  A    C  
ATOM    257  C   LEU A  55      16.765   9.080 -32.777  1.00101.47      A    C  
ANISOU  257  C   LEU A  55    12718  17903   7935  -2236   -189    699  A    C  
ATOM    258  O   LEU A  55      17.661   8.636 -32.061  1.00101.04      A    O  
ANISOU  258  O   LEU A  55    12426  18132   7831  -2462   -254    727  A    O  
ATOM    259  CB  LEU A  55      16.624   8.515 -35.229  1.00 95.92      A    C  
ANISOU  259  CB  LEU A  55    11700  17307   7438  -2038    -98    841  A    C  
ATOM    260  CG  LEU A  55      16.478   7.418 -36.273  1.00 98.57      A    C  
ANISOU  260  CG  LEU A  55    11659  17843   7951  -1796    -32    901  A    C  
ATOM    261  CD1 LEU A  55      15.838   7.956 -37.539  1.00 99.32      A    C  
ANISOU  261  CD1 LEU A  55    11942  17760   8036  -1751      3    942  A    C  
ATOM    262  CD2 LEU A  55      17.820   6.782 -36.588  1.00100.95      A    C  
ANISOU  262  CD2 LEU A  55    11531  18547   8280  -1967    -52    989  A    C  
ATOM    263  N   TYR A  56      16.271  10.335 -32.659  1.00100.52      A    N  
ANISOU  263  N   TYR A  56    13140  17380   7673  -2265   -188    624  A    N  
ATOM    264  CA  TYR A  56      16.784  11.324 -31.707  1.00103.71      A    C  
ANISOU  264  CA  TYR A  56    13951  17608   7845  -2614   -265    551  A    C  
ATOM    265  C   TYR A  56      16.636  10.827 -30.269  1.00106.76      A    C  
ANISOU  265  C   TYR A  56    14254  18110   8202  -2533   -286    464  A    C  
ATOM    266  O   TYR A  56      17.631  10.745 -29.561  1.00108.31      A    O  
ANISOU  266  O   TYR A  56    14388  18498   8268  -2897   -379    465  A    O  
ATOM    267  CB  TYR A  56      16.109  12.699 -31.909  1.00107.74      A    C  
ANISOU  267  CB  TYR A  56    15123  17600   8214  -2562   -233    482  A    C  
ATOM    268  CG  TYR A  56      16.692  13.800 -31.047  1.00113.93      A    C  
ANISOU  268  CG  TYR A  56    16421  18139   8730  -2974   -313    397  A    C  
ATOM    269  CD1 TYR A  56      17.834  14.491 -31.441  1.00118.72      A    C  
ANISOU  269  CD1 TYR A  56    17191  18740   9179  -3536   -398    461  A    C  
ATOM    270  CD2 TYR A  56      16.101  14.153 -29.837  1.00116.13      A    C  
ANISOU  270  CD2 TYR A  56    17033  18202   8887  -2826   -300    251  A    C  
ATOM    271  CE1 TYR A  56      18.383  15.497 -30.645  1.00123.44      A    C  
ANISOU  271  CE1 TYR A  56    18287  19109   9504  -3979   -481    376  A    C  
ATOM    272  CE2 TYR A  56      16.643  15.153 -29.031  1.00120.91      A    C  
ANISOU  272  CE2 TYR A  56    18151  18568   9223  -3228   -376    154  A    C  
ATOM    273  CZ  TYR A  56      17.782  15.827 -29.442  1.00131.42      A    C  
ANISOU  273  CZ  TYR A  56    19658  19878  10397  -3821   -471    214  A    C  
ATOM    274  OH  TYR A  56      18.314  16.817 -28.651  1.00137.97      A    O  
ANISOU  274  OH  TYR A  56    21025  20462  10936  -4272   -553    112  A    O  
ATOM    275  N   LEU A  57      15.410  10.445 -29.877  1.00100.68      A    N  
ANISOU  275  N   LEU A  57    13449  17266   7537  -2068   -200    403  A    N  
ATOM    276  CA  LEU A  57      15.024   9.925 -28.567  1.00 99.56      A    C  
ANISOU  276  CA  LEU A  57    13225  17227   7378  -1916   -195    329  A    C  
ATOM    277  C   LEU A  57      15.881   8.741 -28.090  1.00102.65      A    C  
ANISOU  277  C   LEU A  57    13106  18060   7837  -2061   -252    408  A    C  
ATOM    278  O   LEU A  57      16.223   8.701 -26.907  1.00104.14      A    O  
ANISOU  278  O   LEU A  57    13317  18351   7901  -2201   -309    363  A    O  
ATOM    279  CB  LEU A  57      13.531   9.539 -28.589  1.00 97.61      A    C  
ANISOU  279  CB  LEU A  57    12940  16895   7253  -1387    -78    291  A    C  
ATOM    280  CG  LEU A  57      12.510  10.527 -27.992  1.00103.81      A    C  
ANISOU  280  CG  LEU A  57    14220  17339   7884  -1143    -18    164  A    C  
ATOM    281  CD1 LEU A  57      12.534  11.886 -28.687  1.00106.26      A    C  
ANISOU  281  CD1 LEU A  57    15057  17252   8067  -1200    -12    141  A    C  
ATOM    282  CD2 LEU A  57      11.112   9.966 -28.090  1.00104.09      A    C  
ANISOU  282  CD2 LEU A  57    14072  17439   8038   -642     93    159  A    C  
ATOM    283  N   ILE A  58      16.234   7.793 -28.992  1.00 96.79      A    N  
ANISOU  283  N   ILE A  58    11928  17577   7270  -2012   -235    527  A    N  
ATOM    284  CA  ILE A  58      17.066   6.625 -28.646  1.00 95.83      A    C  
ANISOU  284  CA  ILE A  58    11332  17871   7208  -2082   -274    622  A    C  
ATOM    285  C   ILE A  58      18.538   7.034 -28.465  1.00103.51      A    C  
ANISOU  285  C   ILE A  58    12251  19070   8007  -2561   -391    681  A    C  
ATOM    286  O   ILE A  58      19.163   6.656 -27.467  1.00103.93      A    O  
ANISOU  286  O   ILE A  58    12135  19387   7968  -2697   -461    703  A    O  
ATOM    287  CB  ILE A  58      16.875   5.430 -29.633  1.00 96.13      A    C  
ANISOU  287  CB  ILE A  58    10971  18082   7474  -1817   -200    715  A    C  
ATOM    288  CG1 ILE A  58      15.429   4.867 -29.554  1.00 94.58      A    C  
ANISOU  288  CG1 ILE A  58    10777  17740   7419  -1397   -101    661  A    C  
ATOM    289  CG2 ILE A  58      17.914   4.311 -29.389  1.00 95.96      A    C  
ANISOU  289  CG2 ILE A  58    10505  18472   7484  -1876   -235    828  A    C  
ATOM    290  CD1 ILE A  58      14.981   3.957 -30.758  1.00100.84      A    C  
ANISOU  290  CD1 ILE A  58    11325  18583   8407  -1163    -23    717  A    C  
ATOM    291  N   LEU A  59      19.081   7.812 -29.423  1.00102.52      A    N  
ANISOU  291  N   LEU A  59    12263  18869   7819  -2827   -415    718  A    N  
ATOM    292  CA  LEU A  59      20.469   8.286 -29.398  1.00105.32      A    C  
ANISOU  292  CA  LEU A  59    12560  19469   7987  -3337   -525    790  A    C  
ATOM    293  C   LEU A  59      20.746   9.283 -28.265  1.00113.09      A    C  
ANISOU  293  C   LEU A  59    13927  20327   8713  -3703   -625    692  A    C  
ATOM    294  O   LEU A  59      21.885   9.359 -27.809  1.00115.30      A    O  
ANISOU  294  O   LEU A  59    14031  20951   8828  -4099   -734    753  A    O  
ATOM    295  CB  LEU A  59      20.901   8.880 -30.763  1.00106.16      A    C  
ANISOU  295  CB  LEU A  59    12736  19516   8085  -3539   -512    863  A    C  
ATOM    296  CG  LEU A  59      20.925   7.953 -31.997  1.00108.39      A    C  
ANISOU  296  CG  LEU A  59    12598  20018   8568  -3282   -431    974  A    C  
ATOM    297  CD1 LEU A  59      21.163   8.751 -33.266  1.00109.16      A    C  
ANISOU  297  CD1 LEU A  59    12885  19947   8645  -3428   -404   1018  A    C  
ATOM    298  CD2 LEU A  59      21.983   6.865 -31.879  1.00111.66      A    C  
ANISOU  298  CD2 LEU A  59    12467  20987   8970  -3376   -467   1104  A    C  
ATOM    299  N   SER A  60      19.719  10.039 -27.812  1.00110.89      A    N  
ANISOU  299  N   SER A  60    14168  19586   8379  -3568   -589    544  A    N  
ATOM    300  CA  SER A  60      19.835  11.038 -26.739  1.00114.62      A    C  
ANISOU  300  CA  SER A  60    15102  19861   8587  -3881   -669    419  A    C  
ATOM    301  C   SER A  60      19.706  10.458 -25.329  1.00120.15      A    C  
ANISOU  301  C   SER A  60    15660  20754   9239  -3772   -699    363  A    C  
ATOM    302  O   SER A  60      20.243  11.036 -24.381  1.00122.48      A    O  
ANISOU  302  O   SER A  60    16136  21109   9290  -4149   -806    304  A    O  
ATOM    303  CB  SER A  60      18.807  12.151 -26.919  1.00119.20      A    C  
ANISOU  303  CB  SER A  60    16342  19848   9100  -3734   -601    285  A    C  
ATOM    304  OG  SER A  60      19.014  12.856 -28.131  1.00129.52      A    O  
ANISOU  304  OG  SER A  60    17849  20954  10409  -3884   -585    345  A    O  
ATOM    305  N   SER A  61      18.972   9.348 -25.181  1.00115.31      A    N  
ANISOU  305  N   SER A  61    14747  20230   8836  -3283   -608    381  A    N  
ATOM    306  CA  SER A  61      18.749   8.747 -23.875  1.00115.66      A    C  
ANISOU  306  CA  SER A  61    14658  20445   8843  -3139   -620    343  A    C  
ATOM    307  C   SER A  61      19.691   7.599 -23.559  1.00120.57      A    C  
ANISOU  307  C   SER A  61    14710  21600   9500  -3220   -687    492  A    C  
ATOM    308  O   SER A  61      19.618   6.520 -24.151  1.00117.62      A    O  
ANISOU  308  O   SER A  61    13928  21422   9340  -2963   -627    610  A    O  
ATOM    309  CB  SER A  61      17.293   8.337 -23.704  1.00117.87      A    C  
ANISOU  309  CB  SER A  61    14980  20523   9283  -2602   -486    282  A    C  
ATOM    310  OG  SER A  61      16.470   9.488 -23.788  1.00130.58      A    O  
ANISOU  310  OG  SER A  61    17134  21673  10806  -2500   -428    146  A    O  
ATOM    311  N   HIS A  62      20.585   7.879 -22.600  1.00121.24      A    N  
ANISOU  311  N   HIS A  62    14802  21915   9347  -3582   -812    484  A    N  
ATOM    312  CA  HIS A  62      21.622   7.052 -21.974  1.00122.46      A    C  
ANISOU  312  CA  HIS A  62    14483  22614   9432  -3721   -907    619  A    C  
ATOM    313  C   HIS A  62      21.161   5.617 -21.671  1.00123.76      A    C  
ANISOU  313  C   HIS A  62    14258  22967   9800  -3245   -827    710  A    C  
ATOM    314  O   HIS A  62      21.916   4.673 -21.909  1.00123.04      A    O  
ANISOU  314  O   HIS A  62    13701  23273   9777  -3187   -844    876  A    O  
ATOM    315  CB  HIS A  62      22.062   7.741 -20.670  1.00127.00      A    C  
ANISOU  315  CB  HIS A  62    15292  23271   9692  -4102  -1037    529  A    C  
ATOM    316  CG  HIS A  62      20.900   8.280 -19.888  1.00130.87      A    C  
ANISOU  316  CG  HIS A  62    16272  23335  10118  -3916   -977    336  A    C  
ATOM    318  CD2 HIS A  62      20.250   7.749 -18.828  1.00132.24      A    C  
ANISOU  318  CD2 HIS A  62    16424  23545  10278  -3643   -943    292  A    C  
ATOM    317  ND1 HIS A  62      20.257   9.452 -20.262  1.00133.83      A    N  
ANISOU  317  ND1 HIS A  62    17224  23191  10434  -3960   -929    179  A    N  
ATOM    319  CE1 HIS A  62      19.260   9.604 -19.408  1.00133.38      A    C  
ANISOU  319  CE1 HIS A  62    17463  22894  10322  -3696   -864     40  A    C  
ATOM    320  NE2 HIS A  62      19.218   8.607 -18.523  1.00132.74      A    N  
ANISOU  320  NE2 HIS A  62    17031  23142  10264  -3518   -871    100  A    N  
ATOM    321  N   GLN A  63      19.929   5.465 -21.144  1.00118.69      A    N  
ANISOU  321  N   GLN A  63    13819  22043   9233  -2905   -734    608  A    N  
ATOM    322  CA  GLN A  63      19.319   4.181 -20.795  1.00115.95      A    C  
ANISOU  322  CA  GLN A  63    13188  21807   9059  -2485   -650    681  A    C  
ATOM    323  C   GLN A  63      18.973   3.338 -22.029  1.00115.69      A    C  
ANISOU  323  C   GLN A  63    12907  21744   9305  -2183   -543    772  A    C  
ATOM    324  O   GLN A  63      18.994   2.109 -21.945  1.00114.11      A    O  
ANISOU  324  O   GLN A  63    12375  21755   9228  -1948   -506    892  A    O  
ATOM    325  CB  GLN A  63      18.074   4.378 -19.891  1.00117.15      A    C  
ANISOU  325  CB  GLN A  63    13641  21692   9178  -2253   -577    545  A    C  
ATOM    326  CG  GLN A  63      16.891   5.125 -20.545  1.00136.69      A    C  
ANISOU  326  CG  GLN A  63    16486  23720  11730  -2067   -470    410  A    C  
ATOM    327  CD  GLN A  63      15.581   5.016 -19.790  1.00157.89      A    C  
ANISOU  327  CD  GLN A  63    19358  26234  14399  -1753   -372    311  A    C  
ATOM    329  NE2 GLN A  63      15.164   3.800 -19.452  1.00148.21      A    N  
ANISOU  329  NE2 GLN A  63    17830  25172  13312  -1473   -304    400  A    N  
ATOM    328  OE1 GLN A  63      14.915   6.021 -19.517  1.00155.33      A    O  
ANISOU  328  OE1 GLN A  63    19465  25628  13926  -1749   -347    159  A    O  
ATOM    330  N   LEU A  64      18.648   4.002 -23.161  1.00110.34      A    N  
ANISOU  330  N   LEU A  64    12422  20792   8711  -2192   -495    715  A    N  
ATOM    331  CA  LEU A  64      18.239   3.350 -24.407  1.00107.17      A    C  
ANISOU  331  CA  LEU A  64    11842  20330   8549  -1931   -396    775  A    C  
ATOM    332  C   LEU A  64      19.409   2.943 -25.305  1.00110.03      A    C  
ANISOU  332  C   LEU A  64    11876  20983   8948  -2064   -430    913  A    C  
ATOM    333  O   LEU A  64      19.483   1.779 -25.708  1.00108.05      A    O  
ANISOU  333  O   LEU A  64    11316  20888   8850  -1818   -371   1014  A    O  
ATOM    334  CB  LEU A  64      17.220   4.216 -25.192  1.00106.56      A    C  
ANISOU  334  CB  LEU A  64    12110  19847   8531  -1828   -322    662  A    C  
ATOM    335  CG  LEU A  64      15.937   4.680 -24.474  1.00111.00      A    C  
ANISOU  335  CG  LEU A  64    12997  20128   9050  -1620   -261    528  A    C  
ATOM    336  CD1 LEU A  64      15.156   5.651 -25.337  1.00110.79      A    C  
ANISOU  336  CD1 LEU A  64    13308  19748   9041  -1527   -202    443  A    C  
ATOM    337  CD2 LEU A  64      15.047   3.514 -24.108  1.00111.95      A    C  
ANISOU  337  CD2 LEU A  64    12895  20329   9313  -1272   -174    562  A    C  
ATOM    338  N   ARG A  65      20.311   3.901 -25.620  1.00107.94      A    N  
ANISOU  338  N   ARG A  65    11694  20792   8525  -2455   -518    918  A    N  
ATOM    339  CA  ARG A  65      21.484   3.723 -26.491  1.00108.30      A    C  
ANISOU  339  CA  ARG A  65    11432  21159   8556  -2634   -552   1052  A    C  
ATOM    340  C   ARG A  65      22.375   2.519 -26.122  1.00111.55      A    C  
ANISOU  340  C   ARG A  65    11365  22052   8969  -2519   -573   1212  A    C  
ATOM    341  O   ARG A  65      22.918   1.873 -27.021  1.00110.47      A    O  
ANISOU  341  O   ARG A  65    10926  22130   8916  -2405   -529   1325  A    O  
ATOM    342  CB  ARG A  65      22.325   5.018 -26.581  1.00111.39      A    C  
ANISOU  342  CB  ARG A  65    12017  21587   8720  -3157   -661   1035  A    C  
ATOM    343  CG  ARG A  65      22.831   5.559 -25.238  1.00122.83      A    C  
ANISOU  343  CG  ARG A  65    13582  23176   9913  -3494   -790    994  A    C  
ATOM    344  CD  ARG A  65      23.999   6.514 -25.387  1.00132.13      A    C  
ANISOU  344  CD  ARG A  65    14802  24556  10845  -4072   -913   1032  A    C  
ATOM    345  NE  ARG A  65      23.563   7.875 -25.699  1.00139.16      A    N  
ANISOU  345  NE  ARG A  65    16263  24970  11641  -4333   -920    893  A    N  
ATOM    346  CZ  ARG A  65      24.328   8.956 -25.573  1.00157.71      A    C  
ANISOU  346  CZ  ARG A  65    18833  27350  13740  -4900  -1029    881  A    C  
ATOM    347  NH1 ARG A  65      23.851  10.153 -25.882  1.00144.99      A    N1+
ANISOU  347  NH1 ARG A  65    17809  25234  12047  -5085  -1020    756  A    N1+
ATOM    348  NH2 ARG A  65      25.575   8.847 -25.127  1.00149.71      A    N  
ANISOU  348  NH2 ARG A  65    17464  26882  12537  -5290  -1150   1004  A    N  
ATOM    349  N   ARG A  66      22.513   2.225 -24.812  1.00108.52      A    N  
ANISOU  349  N   ARG A  66    10925  21832   8474  -2520   -635   1225  A    N  
ATOM    350  CA  ARG A  66      23.333   1.127 -24.295  1.00108.92      A    C  
ANISOU  350  CA  ARG A  66    10559  22335   8491  -2382   -662   1389  A    C  
ATOM    351  C   ARG A  66      22.656  -0.255 -24.377  1.00109.24      A    C  
ANISOU  351  C   ARG A  66    10468  22288   8752  -1884   -539   1441  A    C  
ATOM    352  O   ARG A  66      23.347  -1.275 -24.321  1.00109.81      A    O  
ANISOU  352  O   ARG A  66    10206  22687   8831  -1689   -528   1597  A    O  
ATOM    353  CB  ARG A  66      23.801   1.429 -22.861  1.00112.17      A    C  
ANISOU  353  CB  ARG A  66    10982  22974   8664  -2614   -789   1390  A    C  
ATOM    354  N   LYS A  67      21.319  -0.294 -24.495  1.00101.88      A    N  
ANISOU  354  N   LYS A  67     9805  20929   7975  -1681   -448   1319  A    N  
ATOM    355  CA  LYS A  67      20.592  -1.557 -24.573  1.00 98.75      A    C  
ANISOU  355  CA  LYS A  67     9333  20419   7769  -1279   -335   1357  A    C  
ATOM    356  C   LYS A  67      20.577  -2.088 -26.009  1.00100.30      A    C  
ANISOU  356  C   LYS A  67     9418  20553   8137  -1103   -242   1391  A    C  
ATOM    357  O   LYS A  67      20.119  -1.372 -26.908  1.00 99.13      A    O  
ANISOU  357  O   LYS A  67     9438  20180   8046  -1189   -215   1298  A    O  
ATOM    358  CB  LYS A  67      19.161  -1.408 -24.048  1.00 99.00      A    C  
ANISOU  358  CB  LYS A  67     9657  20094   7865  -1163   -279   1225  A    C  
ATOM    359  CG  LYS A  67      19.044  -1.330 -22.543  1.00109.32      A    C  
ANISOU  359  CG  LYS A  67    11026  21477   9033  -1191   -329   1219  A    C  
ATOM    360  CD  LYS A  67      17.602  -1.056 -22.161  1.00119.70      A    C  
ANISOU  360  CD  LYS A  67    12605  22470  10405  -1051   -252   1093  A    C  
ATOM    361  CE  LYS A  67      17.235  -1.665 -20.835  1.00135.20      A    C  
ANISOU  361  CE  LYS A  67    14573  24521  12277   -969   -258   1119  A    C  
ATOM    362  NZ  LYS A  67      15.760  -1.708 -20.645  1.00144.84      A    N1+
ANISOU  362  NZ  LYS A  67    15975  25489  13567   -784   -156   1028  A    N1+
ATOM    363  N   PRO A  68      21.048  -3.343 -26.244  1.00 95.27      A    N  
ANISOU  363  N   PRO A  68     8530  20098   7569   -839   -187   1521  A    N  
ATOM    364  CA  PRO A  68      21.012  -3.906 -27.611  1.00 93.19      A    C  
ANISOU  364  CA  PRO A  68     8196  19761   7451   -657    -89   1536  A    C  
ATOM    365  C   PRO A  68      19.604  -4.030 -28.206  1.00 93.67      A    C  
ANISOU  365  C   PRO A  68     8492  19412   7687   -527      2   1412  A    C  
ATOM    366  O   PRO A  68      19.469  -4.055 -29.430  1.00 92.76      A    O  
ANISOU  366  O   PRO A  68     8387  19202   7658   -490     58   1379  A    O  
ATOM    367  CB  PRO A  68      21.665  -5.285 -27.450  1.00 95.73      A    C  
ANISOU  367  CB  PRO A  68     8280  20311   7781   -356    -42   1691  A    C  
ATOM    368  CG  PRO A  68      22.426  -5.217 -26.157  1.00102.25      A    C  
ANISOU  368  CG  PRO A  68     8965  21457   8429   -446   -144   1792  A    C  
ATOM    369  CD  PRO A  68      21.632  -4.306 -25.285  1.00 97.53      A    C  
ANISOU  369  CD  PRO A  68     8619  20653   7787   -671   -205   1663  A    C  
ATOM    370  N   SER A  69      18.559  -4.088 -27.354  1.00 88.10      A    N  
ANISOU  370  N   SER A  69     7956  18504   7012   -466     17   1348  A    N  
ATOM    371  CA  SER A  69      17.169  -4.187 -27.807  1.00 85.71      A    C  
ANISOU  371  CA  SER A  69     7837  17884   6843   -357     96   1244  A    C  
ATOM    372  C   SER A  69      16.694  -2.910 -28.509  1.00 88.77      A    C  
ANISOU  372  C   SER A  69     8402  18101   7224   -512     80   1127  A    C  
ATOM    373  O   SER A  69      15.929  -2.998 -29.469  1.00 87.15      A    O  
ANISOU  373  O   SER A  69     8260  17727   7127   -421    143   1074  A    O  
ATOM    374  CB  SER A  69      16.241  -4.522 -26.643  1.00 87.86      A    C  
ANISOU  374  CB  SER A  69     8213  18058   7112   -277    114   1224  A    C  
ATOM    375  OG  SER A  69      15.912  -3.381 -25.869  1.00 95.23      A    O  
ANISOU  375  OG  SER A  69     9296  18966   7922   -439     51   1146  A    O  
ATOM    376  N   TYR A  70      17.138  -1.731 -28.019  1.00 85.85      A    N  
ANISOU  376  N   TYR A  70     8137  17772   6711   -749     -6   1092  A    N  
ATOM    377  CA  TYR A  70      16.763  -0.428 -28.570  1.00 85.19      A    C  
ANISOU  377  CA  TYR A  70     8289  17492   6587   -900    -24    993  A    C  
ATOM    378  C   TYR A  70      17.587  -0.009 -29.795  1.00 87.47      A    C  
ANISOU  378  C   TYR A  70     8510  17854   6872  -1042    -38   1031  A    C  
ATOM    379  O   TYR A  70      17.143   0.866 -30.549  1.00 87.14      A    O  
ANISOU  379  O   TYR A  70     8662  17612   6836  -1098    -26    967  A    O  
ATOM    380  CB  TYR A  70      16.772   0.654 -27.486  1.00 88.10      A    C  
ANISOU  380  CB  TYR A  70     8884  17807   6783  -1098   -101    923  A    C  
ATOM    381  CG  TYR A  70      15.557   0.564 -26.590  1.00 90.13      A    C  
ANISOU  381  CG  TYR A  70     9290  17910   7045   -923    -56    848  A    C  
ATOM    382  CD1 TYR A  70      14.334   1.101 -26.985  1.00 91.54      A    C  
ANISOU  382  CD1 TYR A  70     9686  17832   7263   -787      7    751  A    C  
ATOM    383  CD2 TYR A  70      15.615  -0.097 -25.367  1.00 91.86      A    C  
ANISOU  383  CD2 TYR A  70     9409  18276   7219   -869    -69    890  A    C  
ATOM    384  CE1 TYR A  70      13.203   0.996 -26.177  1.00 92.97      A    C  
ANISOU  384  CE1 TYR A  70     9960  17933   7431   -608     60    694  A    C  
ATOM    385  CE2 TYR A  70      14.493  -0.200 -24.544  1.00 92.85      A    C  
ANISOU  385  CE2 TYR A  70     9651  18294   7334   -714    -18    832  A    C  
ATOM    386  CZ  TYR A  70      13.287   0.348 -24.954  1.00100.92      A    C  
ANISOU  386  CZ  TYR A  70    10867  19088   8390   -585     50    733  A    C  
ATOM    387  OH  TYR A  70      12.173   0.236 -24.157  1.00101.94      A    O  
ANISOU  387  OH  TYR A  70    11071  19171   8489   -420    110    687  A    O  
ATOM    388  N   LEU A  71      18.746  -0.651 -30.024  1.00 82.78      A    N  
ANISOU  388  N   LEU A  71     7636  17561   6257  -1072    -55   1146  A    N  
ATOM    389  CA  LEU A  71      19.569  -0.356 -31.198  1.00 82.87      A    C  
ANISOU  389  CA  LEU A  71     7533  17706   6248  -1194    -54   1200  A    C  
ATOM    390  C   LEU A  71      18.958  -0.992 -32.466  1.00 85.11      A    C  
ANISOU  390  C   LEU A  71     7793  17854   6692   -959     49   1181  A    C  
ATOM    391  O   LEU A  71      19.097  -0.432 -33.558  1.00 84.80      A    O  
ANISOU  391  O   LEU A  71     7794  17778   6649  -1053     62   1174  A    O  
ATOM    392  CB  LEU A  71      21.053  -0.740 -30.992  1.00 84.52      A    C  
ANISOU  392  CB  LEU A  71     7420  18348   6345  -1286   -100   1340  A    C  
ATOM    393  CG  LEU A  71      21.846   0.123 -29.986  1.00 91.05      A    C  
ANISOU  393  CG  LEU A  71     8253  19377   6965  -1628   -227   1365  A    C  
ATOM    394  CD1 LEU A  71      22.989  -0.658 -29.369  1.00 92.54      A    C  
ANISOU  394  CD1 LEU A  71     8087  20014   7058  -1579   -265   1511  A    C  
ATOM    395  CD2 LEU A  71      22.358   1.412 -30.620  1.00 94.44      A    C  
ANISOU  395  CD2 LEU A  71     8788  19829   7266  -2014   -286   1357  A    C  
ATOM    396  N   PHE A  72      18.241  -2.129 -32.308  1.00 80.24      A    N  
ANISOU  396  N   PHE A  72     7139  17151   6198   -681    119   1170  A    N  
ATOM    397  CA  PHE A  72      17.537  -2.801 -33.408  1.00 78.59      A    C  
ANISOU  397  CA  PHE A  72     6940  16797   6122   -484    210   1133  A    C  
ATOM    398  C   PHE A  72      16.313  -1.977 -33.818  1.00 80.26      A    C  
ANISOU  398  C   PHE A  72     7387  16740   6370   -508    217   1027  A    C  
ATOM    399  O   PHE A  72      16.072  -1.817 -35.017  1.00 79.07      A    O  
ANISOU  399  O   PHE A  72     7263  16522   6258   -488    251   1003  A    O  
ATOM    400  CB  PHE A  72      17.157  -4.257 -33.054  1.00 79.91      A    C  
ANISOU  400  CB  PHE A  72     7042  16940   6381   -235    276   1156  A    C  
ATOM    401  CG  PHE A  72      18.312  -5.152 -32.645  1.00 83.11      A    C  
ANISOU  401  CG  PHE A  72     7240  17597   6740   -131    282   1277  A    C  
ATOM    402  CD1 PHE A  72      19.537  -5.086 -33.303  1.00 87.19      A    C  
ANISOU  402  CD1 PHE A  72     7567  18372   7189   -152    283   1356  A    C  
ATOM    403  CD2 PHE A  72      18.159  -6.091 -31.633  1.00 86.09      A    C  
ANISOU  403  CD2 PHE A  72     7605  17976   7128     12    294   1327  A    C  
ATOM    404  CE1 PHE A  72      20.597  -5.918 -32.931  1.00 89.60      A    C  
ANISOU  404  CE1 PHE A  72     7657  18955   7430     -1    296   1484  A    C  
ATOM    405  CE2 PHE A  72      19.225  -6.920 -31.258  1.00 90.27      A    C  
ANISOU  405  CE2 PHE A  72     7953  18747   7598    157    302   1458  A    C  
ATOM    406  CZ  PHE A  72      20.434  -6.829 -31.912  1.00 89.21      A    C  
ANISOU  406  CZ  PHE A  72     7615  18888   7391    168    304   1536  A    C  
ATOM    407  N   ILE A  73      15.590  -1.397 -32.820  1.00 75.87      A    N  
ANISOU  407  N   ILE A  73     6996  16054   5775   -537    185    970  A    N  
ATOM    408  CA  ILE A  73      14.442  -0.499 -33.020  1.00 74.90      A    C  
ANISOU  408  CA  ILE A  73     7106  15705   5649   -514    193    881  A    C  
ATOM    409  C   ILE A  73      14.913   0.764 -33.795  1.00 79.68      A    C  
ANISOU  409  C   ILE A  73     7855  16246   6172   -698    154    876  A    C  
ATOM    410  O   ILE A  73      14.254   1.177 -34.750  1.00 78.03      A    O  
ANISOU  410  O   ILE A  73     7752  15903   5991   -632    183    845  A    O  
ATOM    411  CB  ILE A  73      13.721  -0.172 -31.670  1.00 77.79      A    C  
ANISOU  411  CB  ILE A  73     7613  15987   5955   -482    177    828  A    C  
ATOM    412  CG1 ILE A  73      13.086  -1.450 -31.062  1.00 77.20      A    C  
ANISOU  412  CG1 ILE A  73     7408  15962   5963   -309    229    845  A    C  
ATOM    413  CG2 ILE A  73      12.649   0.921 -31.851  1.00 77.89      A    C  
ANISOU  413  CG2 ILE A  73     7885  15788   5923   -425    190    745  A    C  
ATOM    414  CD1 ILE A  73      12.806  -1.418 -29.528  1.00 80.84      A    C  
ANISOU  414  CD1 ILE A  73     7933  16437   6346   -297    213    829  A    C  
ATOM    415  N   GLY A  74      16.065   1.316 -33.396  1.00 78.24      A    N  
ANISOU  415  N   GLY A  74     7667  16186   5876   -940     85    920  A    N  
ATOM    416  CA  GLY A  74      16.692   2.468 -34.039  1.00 79.52      A    C  
ANISOU  416  CA  GLY A  74     7969  16311   5933  -1188     42    936  A    C  
ATOM    417  C   GLY A  74      17.017   2.227 -35.504  1.00 82.79      A    C  
ANISOU  417  C   GLY A  74     8249  16805   6402  -1171     85    990  A    C  
ATOM    418  O   GLY A  74      16.851   3.128 -36.335  1.00 82.68      A    O  
ANISOU  418  O   GLY A  74     8422  16648   6345  -1262     84    984  A    O  
ATOM    419  N   SER A  75      17.452   0.989 -35.833  1.00 78.27      A    N  
ANISOU  419  N   SER A  75     7380  16447   5912  -1032    132   1043  A    N  
ATOM    420  CA  SER A  75      17.765   0.568 -37.201  1.00 77.57      A    C  
ANISOU  420  CA  SER A  75     7149  16458   5865   -974    189   1083  A    C  
ATOM    421  C   SER A  75      16.493   0.516 -38.070  1.00 77.61      A    C  
ANISOU  421  C   SER A  75     7287  16240   5962   -792    242   1012  A    C  
ATOM    422  O   SER A  75      16.563   0.821 -39.260  1.00 75.96      A    O  
ANISOU  422  O   SER A  75     7095  16028   5739   -821    265   1028  A    O  
ATOM    423  CB  SER A  75      18.492  -0.773 -37.207  1.00 81.49      A    C  
ANISOU  423  CB  SER A  75     7350  17209   6405   -820    236   1145  A    C  
ATOM    424  OG  SER A  75      19.178  -0.975 -38.433  1.00 89.82      A    O  
ANISOU  424  OG  SER A  75     8258  18432   7440   -816    284   1198  A    O  
ATOM    425  N   LEU A  76      15.335   0.165 -37.461  1.00 73.12      A    N  
ANISOU  425  N   LEU A  76     6797  15519   5465   -619    258    943  A    N  
ATOM    426  CA  LEU A  76      14.021   0.143 -38.122  1.00 71.60      A    C  
ANISOU  426  CA  LEU A  76     6703  15171   5332   -457    296    882  A    C  
ATOM    427  C   LEU A  76      13.599   1.596 -38.418  1.00 77.29      A    C  
ANISOU  427  C   LEU A  76     7684  15717   5967   -528    263    868  A    C  
ATOM    428  O   LEU A  76      13.201   1.881 -39.546  1.00 77.15      A    O  
ANISOU  428  O   LEU A  76     7717  15649   5948   -477    283    871  A    O  
ATOM    429  CB  LEU A  76      12.972  -0.611 -37.270  1.00 70.35      A    C  
ANISOU  429  CB  LEU A  76     6528  14961   5241   -292    320    832  A    C  
ATOM    430  CG  LEU A  76      11.492  -0.631 -37.742  1.00 74.23      A    C  
ANISOU  430  CG  LEU A  76     7080  15360   5766   -138    351    778  A    C  
ATOM    431  CD1 LEU A  76      11.292  -1.493 -39.013  1.00 73.69      A    C  
ANISOU  431  CD1 LEU A  76     6892  15351   5756    -79    395    770  A    C  
ATOM    432  CD2 LEU A  76      10.585  -1.144 -36.642  1.00 75.06      A    C  
ANISOU  432  CD2 LEU A  76     7173  15453   5893    -38    366    747  A    C  
ATOM    433  N   ALA A  77      13.779   2.519 -37.435  1.00 75.31      A    N  
ANISOU  433  N   ALA A  77     7620  15368   5625   -651    213    857  A    N  
ATOM    434  CA  ALA A  77      13.503   3.958 -37.571  1.00 76.24      A    C  
ANISOU  434  CA  ALA A  77     8067  15266   5633   -723    185    844  A    C  
ATOM    435  C   ALA A  77      14.356   4.591 -38.687  1.00 82.55      A    C  
ANISOU  435  C   ALA A  77     8922  16079   6365   -930    168    914  A    C  
ATOM    436  O   ALA A  77      13.845   5.432 -39.426  1.00 82.33      A    O  
ANISOU  436  O   ALA A  77     9125  15871   6285   -892    175    921  A    O  
ATOM    437  CB  ALA A  77      13.750   4.673 -36.250  1.00 77.80      A    C  
ANISOU  437  CB  ALA A  77     8469  15365   5726   -852    135    808  A    C  
ATOM    438  N   LEU A  78      15.643   4.168 -38.822  1.00 81.09      A    N  
ANISOU  438  N   LEU A  78     8514  16131   6167  -1132    152    979  A    N  
ATOM    439  CA  LEU A  78      16.564   4.663 -39.856  1.00 82.86      A    C  
ANISOU  439  CA  LEU A  78     8727  16445   6311  -1356    145   1062  A    C  
ATOM    440  C   LEU A  78      16.135   4.175 -41.240  1.00 86.60      A    C  
ANISOU  440  C   LEU A  78     9091  16959   6856  -1178    208   1077  A    C  
ATOM    441  O   LEU A  78      16.077   4.983 -42.168  1.00 87.39      A    O  
ANISOU  441  O   LEU A  78     9357  16961   6887  -1254    210   1118  A    O  
ATOM    442  CB  LEU A  78      18.031   4.264 -39.554  1.00 84.03      A    C  
ANISOU  442  CB  LEU A  78     8605  16920   6404  -1588    118   1138  A    C  
ATOM    443  CG  LEU A  78      19.132   4.584 -40.615  1.00 90.38      A    C  
ANISOU  443  CG  LEU A  78     9293  17937   7110  -1830    123   1245  A    C  
ATOM    444  CD1 LEU A  78      19.294   6.087 -40.847  1.00 92.72      A    C  
ANISOU  444  CD1 LEU A  78     9937  18039   7252  -2158     68   1279  A    C  
ATOM    445  CD2 LEU A  78      20.482   4.013 -40.194  1.00 92.83      A    C  
ANISOU  445  CD2 LEU A  78     9251  18655   7364  -1967    108   1326  A    C  
ATOM    446  N   ALA A  79      15.812   2.862 -41.361  1.00 81.32      A    N  
ANISOU  446  N   ALA A  79     8173  16419   6308   -951    259   1042  A    N  
ATOM    447  CA  ALA A  79      15.389   2.210 -42.603  1.00 79.77      A    C  
ANISOU  447  CA  ALA A  79     7867  16275   6168   -787    318   1033  A    C  
ATOM    448  C   ALA A  79      14.108   2.826 -43.128  1.00 83.87      A    C  
ANISOU  448  C   ALA A  79     8595  16589   6683   -651    317    999  A    C  
ATOM    449  O   ALA A  79      13.987   3.026 -44.339  1.00 84.81      A    O  
ANISOU  449  O   ALA A  79     8733  16723   6769   -633    337   1028  A    O  
ATOM    450  CB  ALA A  79      15.210   0.717 -42.385  1.00 79.04      A    C  
ANISOU  450  CB  ALA A  79     7552  16296   6184   -598    366    987  A    C  
ATOM    451  N   ASP A  80      13.177   3.172 -42.214  1.00 79.08      A    N  
ANISOU  451  N   ASP A  80     8140  15818   6089   -541    296    948  A    N  
ATOM    452  CA  ASP A  80      11.897   3.814 -42.529  1.00 78.51      A    C  
ANISOU  452  CA  ASP A  80     8253  15588   5988   -360    297    928  A    C  
ATOM    453  C   ASP A  80      12.078   5.282 -42.954  1.00 82.33      A    C  
ANISOU  453  C   ASP A  80     9052  15885   6345   -460    270    988  A    C  
ATOM    454  O   ASP A  80      11.418   5.716 -43.892  1.00 82.81      A    O  
ANISOU  454  O   ASP A  80     9208  15893   6364   -337    281   1019  A    O  
ATOM    455  CB  ASP A  80      10.923   3.698 -41.343  1.00 80.16      A    C  
ANISOU  455  CB  ASP A  80     8505  15727   6227   -190    297    864  A    C  
ATOM    456  CG  ASP A  80      10.335   2.311 -41.102  1.00 92.00      A    C  
ANISOU  456  CG  ASP A  80     9747  17376   7833    -61    330    815  A    C  
ATOM    457  OD1 ASP A  80      10.953   1.312 -41.539  1.00 92.16      A    O  
ANISOU  457  OD1 ASP A  80     9570  17529   7916   -124    351    818  A    O  
ATOM    458  OD2 ASP A  80       9.267   2.225 -40.459  1.00 99.41      A    O1-
ANISOU  458  OD2 ASP A  80    10696  18300   8775    102    340    778  A    O1-
ATOM    459  N   PHE A  81      12.982   6.030 -42.283  1.00 78.31      A    N  
ANISOU  459  N   PHE A  81     8716  15280   5756   -701    233   1010  A    N  
ATOM    460  CA  PHE A  81      13.288   7.428 -42.590  1.00 79.20      A    C  
ANISOU  460  CA  PHE A  81     9190  15175   5728   -866    205   1069  A    C  
ATOM    461  C   PHE A  81      13.974   7.568 -43.959  1.00 84.20      A    C  
ANISOU  461  C   PHE A  81     9761  15913   6317  -1019    217   1164  A    C  
ATOM    462  O   PHE A  81      13.616   8.464 -44.729  1.00 85.14      A    O  
ANISOU  462  O   PHE A  81    10137  15861   6349   -982    220   1221  A    O  
ATOM    463  CB  PHE A  81      14.154   8.050 -41.481  1.00 81.84      A    C  
ANISOU  463  CB  PHE A  81     9707  15418   5972  -1158    154   1059  A    C  
ATOM    464  CG  PHE A  81      14.855   9.336 -41.854  1.00 85.43      A    C  
ANISOU  464  CG  PHE A  81    10508  15689   6262  -1468    120   1133  A    C  
ATOM    465  CD1 PHE A  81      14.136  10.510 -42.048  1.00 90.00      A    C  
ANISOU  465  CD1 PHE A  81    11550  15911   6734  -1365    124   1141  A    C  
ATOM    466  CD2 PHE A  81      16.234   9.376 -41.999  1.00 87.89      A    C  
ANISOU  466  CD2 PHE A  81    10694  16194   6507  -1861     87   1205  A    C  
ATOM    467  CE1 PHE A  81      14.785  11.698 -42.398  1.00 93.30      A    C  
ANISOU  467  CE1 PHE A  81    12348  16116   6987  -1678     94   1217  A    C  
ATOM    468  CE2 PHE A  81      16.882  10.565 -42.347  1.00 93.22      A    C  
ANISOU  468  CE2 PHE A  81    11699  16707   7011  -2207     53   1284  A    C  
ATOM    469  CZ  PHE A  81      16.154  11.717 -42.542  1.00 92.94      A    C  
ANISOU  469  CZ  PHE A  81    12172  16264   6877  -2127     56   1286  A    C  
ATOM    470  N   LEU A  82      14.977   6.709 -44.247  1.00 80.05      A    N  
ANISOU  470  N   LEU A  82     8904  15676   5833  -1171    230   1190  A    N  
ATOM    471  CA  LEU A  82      15.699   6.739 -45.520  1.00 80.33      A    C  
ANISOU  471  CA  LEU A  82     8833  15874   5815  -1310    255   1280  A    C  
ATOM    472  C   LEU A  82      14.747   6.395 -46.679  1.00 83.48      A    C  
ANISOU  472  C   LEU A  82     9180  16284   6253  -1043    296   1272  A    C  
ATOM    473  O   LEU A  82      14.785   7.056 -47.718  1.00 82.71      A    O  
ANISOU  473  O   LEU A  82     9214  16150   6064  -1099    304   1352  A    O  
ATOM    474  CB  LEU A  82      16.917   5.797 -45.498  1.00 79.95      A    C  
ANISOU  474  CB  LEU A  82     8416  16171   5789  -1454    275   1305  A    C  
ATOM    475  CG  LEU A  82      18.090   6.167 -44.580  1.00 86.15      A    C  
ANISOU  475  CG  LEU A  82     9192  17059   6484  -1792    225   1354  A    C  
ATOM    476  CD1 LEU A  82      19.110   5.044 -44.523  1.00 85.84      A    C  
ANISOU  476  CD1 LEU A  82     8733  17408   6475  -1806    254   1379  A    C  
ATOM    477  CD2 LEU A  82      18.766   7.465 -45.009  1.00 91.02      A    C  
ANISOU  477  CD2 LEU A  82    10040  17615   6928  -2149    195   1461  A    C  
ATOM    478  N   ALA A  83      13.848   5.402 -46.454  1.00 79.77      A    N  
ANISOU  478  N   ALA A  83     8542  15867   5901   -774    317   1180  A    N  
ATOM    479  CA  ALA A  83      12.823   4.962 -47.404  1.00 79.02      A    C  
ANISOU  479  CA  ALA A  83     8376  15817   5830   -541    342   1157  A    C  
ATOM    480  C   ALA A  83      11.861   6.102 -47.694  1.00 82.86      A    C  
ANISOU  480  C   ALA A  83     9160  16093   6230   -406    318   1199  A    C  
ATOM    481  O   ALA A  83      11.746   6.475 -48.852  1.00 83.59      A    O  
ANISOU  481  O   ALA A  83     9308  16207   6246   -383    325   1266  A    O  
ATOM    482  CB  ALA A  83      12.064   3.764 -46.856  1.00 78.30      A    C  
ANISOU  482  CB  ALA A  83     8079  15811   5859   -353    359   1054  A    C  
ATOM    483  N   SER A  84      11.239   6.705 -46.645  1.00 78.99      A    N  
ANISOU  483  N   SER A  84     8880  15402   5732   -307    295   1171  A    N  
ATOM    484  CA  SER A  84      10.307   7.837 -46.750  1.00 80.46      A    C  
ANISOU  484  CA  SER A  84     9389  15367   5817   -111    284   1213  A    C  
ATOM    485  C   SER A  84      10.829   8.954 -47.655  1.00 88.12      A    C  
ANISOU  485  C   SER A  84    10653  16180   6650   -253    276   1332  A    C  
ATOM    486  O   SER A  84      10.083   9.439 -48.509  1.00 89.31      A    O  
ANISOU  486  O   SER A  84    10937  16277   6720    -54    279   1398  A    O  
ATOM    487  CB  SER A  84       9.980   8.407 -45.374  1.00 83.94      A    C  
ANISOU  487  CB  SER A  84    10053  15599   6240    -37    274   1161  A    C  
ATOM    488  OG  SER A  84       9.388   7.426 -44.542  1.00 91.68      A    O  
ANISOU  488  OG  SER A  84    10776  16728   7330    106    286   1068  A    O  
ATOM    489  N   VAL A  85      12.116   9.327 -47.498  1.00 85.70      A    N  
ANISOU  489  N   VAL A  85    10430  15830   6300   -608    263   1371  A    N  
ATOM    490  CA  VAL A  85      12.754  10.375 -48.298  1.00 87.76      A    C  
ANISOU  490  CA  VAL A  85    10978  15950   6416   -826    256   1495  A    C  
ATOM    491  C   VAL A  85      13.022   9.898 -49.739  1.00 91.98      A    C  
ANISOU  491  C   VAL A  85    11281  16730   6936   -854    283   1567  A    C  
ATOM    492  O   VAL A  85      12.607  10.581 -50.676  1.00 93.03      A    O  
ANISOU  492  O   VAL A  85    11620  16762   6966   -758    287   1661  A    O  
ATOM    493  CB  VAL A  85      14.012  10.964 -47.605  1.00 92.79      A    C  
ANISOU  493  CB  VAL A  85    11783  16492   6980  -1248    226   1520  A    C  
ATOM    494  CG1 VAL A  85      14.622  12.095 -48.428  1.00 95.20      A    C  
ANISOU  494  CG1 VAL A  85    12403  16653   7116  -1529    219   1662  A    C  
ATOM    495  CG2 VAL A  85      13.682  11.456 -46.198  1.00 93.11      A    C  
ANISOU  495  CG2 VAL A  85    12113  16261   7003  -1208    198   1438  A    C  
ATOM    496  N   VAL A  86      13.677   8.725 -49.916  1.00 87.49      A    N  
ANISOU  496  N   VAL A  86    10306  16480   6456   -951    308   1523  A    N  
ATOM    497  CA  VAL A  86      14.012   8.171 -51.241  1.00 87.29      A    C  
ANISOU  497  CA  VAL A  86    10053  16710   6403   -974    347   1569  A    C  
ATOM    498  C   VAL A  86      12.745   7.886 -52.073  1.00 90.40      A    C  
ANISOU  498  C   VAL A  86    10407  17140   6801   -650    352   1549  A    C  
ATOM    499  O   VAL A  86      12.616   8.431 -53.165  1.00 90.42      A    O  
ANISOU  499  O   VAL A  86    10528  17139   6688   -638    356   1648  A    O  
ATOM    500  CB  VAL A  86      14.978   6.950 -51.171  1.00 90.13      A    C  
ANISOU  500  CB  VAL A  86    10018  17388   6840  -1088    386   1516  A    C  
ATOM    501  CG1 VAL A  86      15.214   6.346 -52.552  1.00 90.03      A    C  
ANISOU  501  CG1 VAL A  86     9795  17629   6785  -1050    440   1538  A    C  
ATOM    502  CG2 VAL A  86      16.315   7.339 -50.541  1.00 91.27      A    C  
ANISOU  502  CG2 VAL A  86    10163  17587   6928  -1437    374   1577  A    C  
ATOM    503  N   PHE A  87      11.806   7.081 -51.529  1.00 86.03      A    N  
ANISOU  503  N   PHE A  87     9693  16636   6360   -410    346   1434  A    N  
ATOM    504  CA  PHE A  87      10.539   6.693 -52.164  1.00 85.41      A    C  
ANISOU  504  CA  PHE A  87     9523  16655   6274   -133    339   1405  A    C  
ATOM    505  C   PHE A  87       9.666   7.881 -52.595  1.00 92.49      A    C  
ANISOU  505  C   PHE A  87    10713  17387   7042     53    311   1512  A    C  
ATOM    506  O   PHE A  87       9.184   7.861 -53.719  1.00 93.15      A    O  
ANISOU  506  O   PHE A  87    10756  17598   7039    152    308   1567  A    O  
ATOM    507  CB  PHE A  87       9.736   5.708 -51.278  1.00 84.89      A    C  
ANISOU  507  CB  PHE A  87     9257  16663   6334     27    335   1276  A    C  
ATOM    508  CG  PHE A  87       8.456   5.166 -51.882  1.00 85.67      A    C  
ANISOU  508  CG  PHE A  87     9216  16924   6410    254    319   1243  A    C  
ATOM    509  CD1 PHE A  87       8.493   4.210 -52.894  1.00 87.82      A    C  
ANISOU  509  CD1 PHE A  87     9277  17422   6671    219    333   1198  A    C  
ATOM    510  CD2 PHE A  87       7.215   5.595 -51.423  1.00 87.71      A    C  
ANISOU  510  CD2 PHE A  87     9551  17138   6638    498    291   1255  A    C  
ATOM    511  CE1 PHE A  87       7.310   3.710 -53.452  1.00 88.45      A    C  
ANISOU  511  CE1 PHE A  87     9225  17680   6702    374    305   1165  A    C  
ATOM    512  CE2 PHE A  87       6.034   5.092 -51.981  1.00 90.44      A    C  
ANISOU  512  CE2 PHE A  87     9722  17706   6936    679    268   1239  A    C  
ATOM    513  CZ  PHE A  87       6.090   4.156 -52.994  1.00 87.87      A    C  
ANISOU  513  CZ  PHE A  87     9188  17604   6594    591    268   1193  A    C  
ATOM    514  N   ALA A  88       9.454   8.896 -51.729  1.00 90.69      A    N  
ANISOU  514  N   ALA A  88    10795  16881   6783    121    295   1542  A    N  
ATOM    515  CA  ALA A  88       8.622  10.056 -52.079  1.00 92.75      A    C  
ANISOU  515  CA  ALA A  88    11387  16949   6904    360    281   1651  A    C  
ATOM    516  C   ALA A  88       9.260  10.968 -53.133  1.00 99.18      A    C  
ANISOU  516  C   ALA A  88    12469  17643   7573    205    284   1803  A    C  
ATOM    517  O   ALA A  88       8.551  11.439 -54.021  1.00 99.89      A    O  
ANISOU  517  O   ALA A  88    12672  17739   7544    423    275   1906  A    O  
ATOM    518  CB  ALA A  88       8.249  10.852 -50.840  1.00 94.29      A    C  
ANISOU  518  CB  ALA A  88    11888  16853   7086    490    278   1628  A    C  
ATOM    519  N   CYS A  89      10.584  11.203 -53.050  1.00 96.77      A    N  
ANISOU  519  N   CYS A  89    12248  17262   7259   -178    294   1832  A    N  
ATOM    520  CA  CYS A  89      11.292  12.057 -54.008  1.00 99.26      A    C  
ANISOU  520  CA  CYS A  89    12811  17481   7423   -397    302   1988  A    C  
ATOM    521  C   CYS A  89      11.466  11.407 -55.364  1.00101.93      A    C  
ANISOU  521  C   CYS A  89    12861  18142   7728   -421    322   2030  A    C  
ATOM    522  O   CYS A  89      11.531  12.117 -56.362  1.00103.63      A    O  
ANISOU  522  O   CYS A  89    13277  18305   7793   -456    326   2176  A    O  
ATOM    523  CB  CYS A  89      12.620  12.540 -53.441  1.00101.11      A    C  
ANISOU  523  CB  CYS A  89    13203  17584   7631   -834    302   2013  A    C  
ATOM    524  SG  CYS A  89      12.450  13.521 -51.931  1.00106.90      A    S  
ANISOU  524  SG  CYS A  89    14412  17870   8336   -851    274   1974  A    S  
ATOM    525  N   SER A  90      11.534  10.066 -55.404  1.00 95.65      A    N  
ANISOU  525  N   SER A  90    11628  17660   7054   -400    338   1902  A    N  
ATOM    526  CA  SER A  90      11.671   9.288 -56.636  1.00 94.78      A    C  
ANISOU  526  CA  SER A  90    11240  17864   6907   -404    365   1903  A    C  
ATOM    527  C   SER A  90      10.307   8.996 -57.278  1.00 97.44      A    C  
ANISOU  527  C   SER A  90    11494  18320   7209    -68    335   1886  A    C  
ATOM    528  O   SER A  90      10.245   8.742 -58.481  1.00 98.30      A    O  
ANISOU  528  O   SER A  90    11502  18630   7218    -50    343   1929  A    O  
ATOM    529  CB  SER A  90      12.422   7.988 -56.370  1.00 97.30      A    C  
ANISOU  529  CB  SER A  90    11189  18432   7347   -537    405   1771  A    C  
ATOM    530  OG  SER A  90      11.741   7.194 -55.412  1.00107.43      A    O  
ANISOU  530  OG  SER A  90    12321  19716   8780   -373    388   1627  A    O  
ATOM    531  N   PHE A  91       9.220   9.038 -56.481  1.00 91.73      A    N  
ANISOU  531  N   PHE A  91    10801  17509   6544    191    301   1830  A    N  
ATOM    532  CA  PHE A  91       7.857   8.799 -56.954  1.00 90.59      A    C  
ANISOU  532  CA  PHE A  91    10542  17531   6345    505    264   1826  A    C  
ATOM    533  C   PHE A  91       7.326  10.053 -57.628  1.00 98.21      A    C  
ANISOU  533  C   PHE A  91    11819  18368   7128    701    242   2009  A    C  
ATOM    534  O   PHE A  91       6.961   9.990 -58.804  1.00 99.28      A    O  
ANISOU  534  O   PHE A  91    11869  18712   7141    793    223   2077  A    O  
ATOM    535  CB  PHE A  91       6.942   8.371 -55.800  1.00 90.17      A    C  
ANISOU  535  CB  PHE A  91    10376  17483   6402    700    246   1716  A    C  
ATOM    536  CG  PHE A  91       5.633   7.757 -56.224  1.00 90.55      A    C  
ANISOU  536  CG  PHE A  91    10162  17832   6411    927    209   1676  A    C  
ATOM    537  CD1 PHE A  91       4.519   8.552 -56.462  1.00 94.04      A    C  
ANISOU  537  CD1 PHE A  91    10701  18316   6715   1252    173   1787  A    C  
ATOM    538  CD2 PHE A  91       5.502   6.379 -56.349  1.00 90.33      A    C  
ANISOU  538  CD2 PHE A  91     9800  18055   6466    815    209   1531  A    C  
ATOM    539  CE1 PHE A  91       3.308   7.982 -56.838  1.00 94.82      A    C  
ANISOU  539  CE1 PHE A  91    10513  18763   6752   1430    129   1761  A    C  
ATOM    540  CE2 PHE A  91       4.285   5.809 -56.719  1.00 92.74      A    C  
ANISOU  540  CE2 PHE A  91     9871  18654   6712    959    165   1492  A    C  
ATOM    541  CZ  PHE A  91       3.195   6.615 -56.954  1.00 92.48      A    C  
ANISOU  541  CZ  PHE A  91     9885  18718   6536   1252    121   1609  A    C  
ATOM    542  N   VAL A  92       7.319  11.198 -56.894  1.00 96.44      A    N  
ANISOU  542  N   VAL A  92    11988  17787   6869    766    245   2090  A    N  
ATOM    543  CA  VAL A  92       6.853  12.508 -57.375  1.00 99.51      A    C  
ANISOU  543  CA  VAL A  92    12777  17958   7073    985    235   2276  A    C  
ATOM    544  C   VAL A  92       7.683  12.994 -58.600  1.00103.80      A    C  
ANISOU  544  C   VAL A  92    13475  18484   7480    757    248   2426  A    C  
ATOM    545  O   VAL A  92       7.161  13.713 -59.448  1.00105.68      A    O  
ANISOU  545  O   VAL A  92    13918  18690   7546    965    233   2588  A    O  
ATOM    546  CB  VAL A  92       6.749  13.562 -56.226  1.00105.47      A    C  
ANISOU  546  CB  VAL A  92    13973  18285   7814   1093    248   2299  A    C  
ATOM    547  CG1 VAL A  92       8.116  14.102 -55.793  1.00105.94      A    C  
ANISOU  547  CG1 VAL A  92    14327  18040   7887    666    270   2313  A    C  
ATOM    548  CG2 VAL A  92       5.801  14.702 -56.595  1.00108.64      A    C  
ANISOU  548  CG2 VAL A  92    14745  18506   8025   1508    242   2466  A    C  
ATOM    549  N   ASN A  93       8.946  12.553 -58.709  1.00 98.20      A    N  
ANISOU  549  N   ASN A  93    12640  17840   6833    350    279   2381  A    N  
ATOM    550  CA  ASN A  93       9.805  12.904 -59.831  1.00 99.08      A    C  
ANISOU  550  CA  ASN A  93    12839  17997   6811     98    303   2518  A    C  
ATOM    551  C   ASN A  93       9.483  12.030 -61.046  1.00100.17      A    C  
ANISOU  551  C   ASN A  93    12623  18541   6895    178    300   2500  A    C  
ATOM    552  O   ASN A  93       9.422  12.553 -62.159  1.00101.16      A    O  
ANISOU  552  O   ASN A  93    12878  18712   6845    200    298   2656  A    O  
ATOM    553  CB  ASN A  93      11.275  12.776 -59.438  1.00101.01      A    C  
ANISOU  553  CB  ASN A  93    13052  18213   7115   -355    342   2487  A    C  
ATOM    554  CG  ASN A  93      12.222  13.517 -60.344  1.00126.63      A    C  
ANISOU  554  CG  ASN A  93    16491  21433  10190   -661    372   2666  A    C  
ATOM    556  ND2 ASN A  93      12.443  14.793 -60.056  1.00121.26      A    N  
ANISOU  556  ND2 ASN A  93    16312  20367   9393   -772    364   2812  A    N  
ATOM    555  OD1 ASN A  93      12.774  12.956 -61.295  1.00119.31      A    O  
ANISOU  555  OD1 ASN A  93    15289  20824   9220   -810    408   2675  A    O  
ATOM    557  N   PHE A  94       9.265  10.709 -60.833  1.00 92.98      A    N  
ANISOU  557  N   PHE A  94    11299  17911   6119    212    298   2311  A    N  
ATOM    558  CA  PHE A  94       8.961   9.756 -61.905  1.00 91.49      A    C  
ANISOU  558  CA  PHE A  94    10791  18096   5875    258    294   2252  A    C  
ATOM    559  C   PHE A  94       7.541   9.935 -62.448  1.00 96.39      A    C  
ANISOU  559  C   PHE A  94    11396  18852   6376    605    228   2310  A    C  
ATOM    560  O   PHE A  94       7.381  10.206 -63.644  1.00 97.54      A    O  
ANISOU  560  O   PHE A  94    11558  19160   6345    648    214   2421  A    O  
ATOM    561  CB  PHE A  94       9.199   8.299 -61.447  1.00 89.96      A    C  
ANISOU  561  CB  PHE A  94    10233  18100   5848    163    319   2029  A    C  
ATOM    562  CG  PHE A  94       9.126   7.247 -62.534  1.00 90.37      A    C  
ANISOU  562  CG  PHE A  94    10010  18493   5832    135    333   1940  A    C  
ATOM    563  CD1 PHE A  94      10.231   6.969 -63.331  1.00 92.95      A    C  
ANISOU  563  CD1 PHE A  94    10273  18951   6094    -84    403   1950  A    C  
ATOM    564  CD2 PHE A  94       7.965   6.508 -62.734  1.00 91.46      A    C  
ANISOU  564  CD2 PHE A  94     9956  18841   5955    312    280   1838  A    C  
ATOM    565  CE1 PHE A  94      10.166   5.993 -64.334  1.00 93.54      A    C  
ANISOU  565  CE1 PHE A  94    10135  19321   6085    -91    426   1851  A    C  
ATOM    566  CE2 PHE A  94       7.902   5.530 -63.735  1.00 93.98      A    C  
ANISOU  566  CE2 PHE A  94    10070  19449   6188    255    291   1737  A    C  
ATOM    567  CZ  PHE A  94       9.004   5.278 -64.527  1.00 92.24      A    C  
ANISOU  567  CZ  PHE A  94     9827  19316   5902     69    368   1736  A    C  
ATOM    568  N   HIS A  95       6.520   9.785 -61.573  1.00 91.51      A    N  
ANISOU  568  N   HIS A  95    10729  18207   5836    853    188   2246  A    N  
ATOM    569  CA  HIS A  95       5.113   9.861 -61.957  1.00 92.32      A    C  
ANISOU  569  CA  HIS A  95    10739  18519   5818   1196    123   2298  A    C  
ATOM    570  C   HIS A  95       4.589  11.284 -62.203  1.00101.73      A    C  
ANISOU  570  C   HIS A  95    12294  19521   6837   1489    103   2526  A    C  
ATOM    571  O   HIS A  95       3.864  11.483 -63.185  1.00103.71      A    O  
ANISOU  571  O   HIS A  95    12491  20009   6906   1701     56   2640  A    O  
ATOM    572  CB  HIS A  95       4.210   9.116 -60.954  1.00 90.77      A    C  
ANISOU  572  CB  HIS A  95    10297  18443   5750   1337     96   2147  A    C  
ATOM    573  CG  HIS A  95       4.255   7.618 -61.077  1.00 91.55      A    C  
ANISOU  573  CG  HIS A  95    10023  18824   5939   1141     93   1949  A    C  
ATOM    575  CD2 HIS A  95       4.653   6.689 -60.178  1.00 90.51      A    C  
ANISOU  575  CD2 HIS A  95     9744  18649   5997    966    126   1773  A    C  
ATOM    574  ND1 HIS A  95       3.814   6.967 -62.220  1.00 93.71      A    N  
ANISOU  574  ND1 HIS A  95    10076  19450   6078   1125     52   1924  A    N  
ATOM    576  CE1 HIS A  95       3.983   5.676 -61.988  1.00 90.94      A    C  
ANISOU  576  CE1 HIS A  95     9490  19223   5841    930     67   1725  A    C  
ATOM    577  NE2 HIS A  95       4.483   5.459 -60.773  1.00 89.41      A    N  
ANISOU  577  NE2 HIS A  95     9329  18797   5845    844    113   1637  A    N  
ATOM    578  N   VAL A  96       4.934  12.265 -61.338  1.00100.08      A    N  
ANISOU  578  N   VAL A  96    12473  18889   6664   1512    136   2595  A    N  
ATOM    579  CA  VAL A  96       4.404  13.633 -61.484  1.00103.57      A    C  
ANISOU  579  CA  VAL A  96    13342  19077   6931   1828    130   2808  A    C  
ATOM    580  C   VAL A  96       5.240  14.503 -62.455  1.00111.41      A    C  
ANISOU  580  C   VAL A  96    14686  19874   7772   1642    153   2997  A    C  
ATOM    581  O   VAL A  96       4.705  14.925 -63.486  1.00112.82      A    O  
ANISOU  581  O   VAL A  96    14938  20177   7753   1857    125   3168  A    O  
ATOM    582  CB  VAL A  96       4.155  14.344 -60.118  1.00107.32      A    C  
ANISOU  582  CB  VAL A  96    14129  19175   7471   2012    155   2789  A    C  
ATOM    583  CG1 VAL A  96       3.678  15.783 -60.304  1.00110.73      A    C  
ANISOU  583  CG1 VAL A  96    15082  19290   7700   2365    163   3010  A    C  
ATOM    584  CG2 VAL A  96       3.163  13.561 -59.263  1.00105.39      A    C  
ANISOU  584  CG2 VAL A  96    13529  19180   7335   2241    134   2638  A    C  
ATOM    585  N   PHE A  97       6.518  14.786 -62.121  1.00109.44      A    N  
ANISOU  585  N   PHE A  97    14643  19346   7594   1239    201   2982  A    N  
ATOM    586  CA  PHE A  97       7.386  15.666 -62.917  1.00112.59      A    C  
ANISOU  586  CA  PHE A  97    15394  19543   7842    989    230   3168  A    C  
ATOM    587  C   PHE A  97       8.067  15.019 -64.148  1.00117.75      A    C  
ANISOU  587  C   PHE A  97    15754  20552   8434    718    244   3183  A    C  
ATOM    588  O   PHE A  97       8.686  15.745 -64.935  1.00119.21      A    O  
ANISOU  588  O   PHE A  97    16205  20630   8459    538    269   3365  A    O  
ATOM    589  CB  PHE A  97       8.439  16.338 -62.019  1.00114.80      A    C  
ANISOU  589  CB  PHE A  97    16025  19408   8187    637    270   3160  A    C  
ATOM    590  CG  PHE A  97       7.840  17.331 -61.054  1.00118.45      A    C  
ANISOU  590  CG  PHE A  97    16968  19416   8620    893    268   3202  A    C  
ATOM    591  CD1 PHE A  97       7.504  18.615 -61.470  1.00125.55      A    C  
ANISOU  591  CD1 PHE A  97    18437  19956   9309   1069    275   3425  A    C  
ATOM    592  CD2 PHE A  97       7.597  16.980 -59.731  1.00119.15      A    C  
ANISOU  592  CD2 PHE A  97    16973  19425   8875    974    267   3022  A    C  
ATOM    593  CE1 PHE A  97       6.929  19.527 -60.583  1.00128.86      A    C  
ANISOU  593  CE1 PHE A  97    19352  19929   9681   1348    287   3453  A    C  
ATOM    594  CE2 PHE A  97       7.030  17.895 -58.840  1.00124.13      A    C  
ANISOU  594  CE2 PHE A  97    18068  19639   9457   1235    276   3049  A    C  
ATOM    595  CZ  PHE A  97       6.699  19.162 -59.272  1.00126.30      A    C  
ANISOU  595  CZ  PHE A  97    18925  19546   9518   1431    289   3258  A    C  
ATOM    596  N   HIS A  98       7.927  13.682 -64.326  1.00113.33      A    N  
ANISOU  596  N   HIS A  98    14682  20400   7980    692    235   2997  A    N  
ATOM    597  CA  HIS A  98       8.514  12.887 -65.422  1.00113.26      A    C  
ANISOU  597  CA  HIS A  98    14370  20750   7913    473    259   2962  A    C  
ATOM    598  C   HIS A  98      10.053  12.965 -65.412  1.00118.01      A    C  
ANISOU  598  C   HIS A  98    15026  21273   8540     25    333   2976  A    C  
ATOM    599  O   HIS A  98      10.652  13.807 -66.084  1.00120.02      A    O  
ANISOU  599  O   HIS A  98    15550  21420   8634   -148    360   3169  A    O  
ATOM    600  CB  HIS A  98       7.905  13.228 -66.802  1.00116.50      A    C  
ANISOU  600  CB  HIS A  98    14818  21366   8081    661    224   3131  A    C  
ATOM    601  CG  HIS A  98       6.407  13.266 -66.810  1.00120.83      A    C  
ANISOU  601  CG  HIS A  98    15302  22039   8567   1107    145   3154  A    C  
ATOM    603  CD2 HIS A  98       5.512  12.264 -66.652  1.00120.93      A    C  
ANISOU  603  CD2 HIS A  98    14931  22374   8644   1271     94   2988  A    C  
ATOM    602  ND1 HIS A  98       5.719  14.456 -66.977  1.00125.73      A    N  
ANISOU  602  ND1 HIS A  98    16288  22461   9024   1426    116   3380  A    N  
ATOM    604  CE1 HIS A  98       4.436  14.140 -66.927  1.00125.12      A    C  
ANISOU  604  CE1 HIS A  98    15991  22638   8912   1796     49   3350  A    C  
ATOM    605  NE2 HIS A  98       4.263  12.834 -66.736  1.00122.67      A    N  
ANISOU  605  NE2 HIS A  98    15224  22652   8733   1687     30   3117  A    N  
ATOM    606  N   GLY A  99      10.659  12.099 -64.607  1.00112.73      A    N  
ANISOU  606  N   GLY A  99    14101  20670   8061   -155    364   2786  A    N  
ATOM    607  CA  GLY A  99      12.101  12.035 -64.418  1.00112.69      A    C  
ANISOU  607  CA  GLY A  99    14062  20667   8089   -556    431   2784  A    C  
ATOM    608  C   GLY A  99      12.824  11.257 -65.490  1.00116.72      A    C  
ANISOU  608  C   GLY A  99    14276  21561   8513   -720    493   2762  A    C  
ATOM    609  O   GLY A  99      12.900  10.026 -65.424  1.00114.53      A    O  
ANISOU  609  O   GLY A  99    13643  21538   8333   -680    517   2572  A    O  
ATOM    610  N   VAL A 100      13.384  11.981 -66.468  1.00115.55      A    N  
ANISOU  610  N   VAL A 100    14300  21440   8165   -906    527   2960  A    N  
ATOM    611  CA  VAL A 100      14.125  11.387 -67.576  1.00116.04      A    C  
ANISOU  611  CA  VAL A 100    14114  21878   8099  -1066    601   2969  A    C  
ATOM    612  C   VAL A 100      15.517  10.933 -67.092  1.00118.88      A    C  
ANISOU  612  C   VAL A 100    14244  22383   8541  -1374    683   2893  A    C  
ATOM    613  O   VAL A 100      16.529  11.587 -67.357  1.00120.94      A    O  
ANISOU  613  O   VAL A 100    14609  22646   8696  -1705    730   3049  A    O  
ATOM    614  CB  VAL A 100      14.145  12.276 -68.856  1.00123.44      A    C  
ANISOU  614  CB  VAL A 100    15293  22837   8770  -1144    613   3219  A    C  
ATOM    615  CG1 VAL A 100      12.837  12.142 -69.626  1.00123.62      A    C  
ANISOU  615  CG1 VAL A 100    15336  22948   8685   -787    547   3241  A    C  
ATOM    616  CG2 VAL A 100      14.433  13.745 -68.534  1.00125.88      A    C  
ANISOU  616  CG2 VAL A 100    16073  22746   9008  -1346    600   3442  A    C  
ATOM    617  N   ASP A 101      15.548   9.805 -66.357  1.00112.03      A    N  
ANISOU  617  N   ASP A 101    13066  21648   7853  -1263    696   2664  A    N  
ATOM    618  CA  ASP A 101      16.775   9.247 -65.788  1.00111.06      A    C  
ANISOU  618  CA  ASP A 101    12690  21689   7818  -1465    769   2580  A    C  
ATOM    619  C   ASP A 101      17.466   8.241 -66.694  1.00114.14      A    C  
ANISOU  619  C   ASP A 101    12757  22503   8106  -1482    875   2517  A    C  
ATOM    620  O   ASP A 101      16.801   7.386 -67.283  1.00112.99      A    O  
ANISOU  620  O   ASP A 101    12491  22504   7937  -1252    880   2388  A    O  
ATOM    621  CB  ASP A 101      16.503   8.608 -64.414  1.00110.59      A    C  
ANISOU  621  CB  ASP A 101    12517  21500   8002  -1320    732   2385  A    C  
ATOM    622  CG  ASP A 101      16.108   9.595 -63.335  1.00123.33      A    C  
ANISOU  622  CG  ASP A 101    14416  22733   9710  -1382    659   2442  A    C  
ATOM    623  OD1 ASP A 101      16.946  10.454 -62.983  1.00125.94      A    O  
ANISOU  623  OD1 ASP A 101    14818  23009  10027  -1684    676   2528  A    O  
ATOM    624  OD2 ASP A 101      14.962   9.503 -62.834  1.00127.73      A    O1-
ANISOU  624  OD2 ASP A 101    15125  23068  10339  -1130    587   2398  A    O1-
ATOM    625  N   SER A 102      18.811   8.322 -66.773  1.00111.00      A    N  
ANISOU  625  N   SER A 102    12219  22323   7631  -1759    960   2602  A    N  
ATOM    626  CA  SER A 102      19.635   7.385 -67.536  1.00110.86      A    C  
ANISOU  626  CA  SER A 102    11880  22741   7501  -1756   1085   2550  A    C  
ATOM    627  C   SER A 102      19.746   6.052 -66.772  1.00111.77      A    C  
ANISOU  627  C   SER A 102    11727  22946   7794  -1558   1122   2318  A    C  
ATOM    628  O   SER A 102      19.513   6.019 -65.554  1.00109.16      A    O  
ANISOU  628  O   SER A 102    11431  22385   7658  -1538   1058   2250  A    O  
ATOM    629  CB  SER A 102      21.014   7.976 -67.814  1.00116.94      A    C  
ANISOU  629  CB  SER A 102    12572  23756   8103  -2119   1164   2750  A    C  
ATOM    630  OG  SER A 102      21.767   8.193 -66.632  1.00125.07      A    O  
ANISOU  630  OG  SER A 102    13554  24724   9241  -2337   1145   2777  A    O  
ATOM    631  N   LYS A 103      20.085   4.961 -67.496  1.00108.23      A    N  
ANISOU  631  N   LYS A 103    11045  22815   7262  -1398   1228   2197  A    N  
ATOM    632  CA  LYS A 103      20.204   3.585 -66.990  1.00106.52      A    C  
ANISOU  632  CA  LYS A 103    10619  22682   7170  -1170   1285   1977  A    C  
ATOM    633  C   LYS A 103      20.965   3.458 -65.657  1.00108.96      A    C  
ANISOU  633  C   LYS A 103    10791  22978   7632  -1253   1290   1981  A    C  
ATOM    634  O   LYS A 103      20.485   2.776 -64.753  1.00106.49      A    O  
ANISOU  634  O   LYS A 103    10473  22478   7511  -1088   1250   1828  A    O  
ATOM    635  CB  LYS A 103      20.819   2.665 -68.059  1.00111.03      A    C  
ANISOU  635  CB  LYS A 103    10996  23632   7559  -1034   1432   1901  A    C  
ATOM    636  CG  LYS A 103      20.337   1.218 -67.977  1.00128.62      A    C  
ANISOU  636  CG  LYS A 103    13184  25819   9866   -723   1465   1633  A    C  
ATOM    637  CD  LYS A 103      20.973   0.321 -69.040  1.00140.42      A    C  
ANISOU  637  CD  LYS A 103    14537  27663  11152   -566   1626   1547  A    C  
ATOM    638  CE  LYS A 103      20.426  -1.087 -68.991  1.00148.41      A    C  
ANISOU  638  CE  LYS A 103    15596  28571  12222   -280   1659   1273  A    C  
ATOM    639  NZ  LYS A 103      21.134  -1.996 -69.930  1.00158.87      A    N1+
ANISOU  639  NZ  LYS A 103    16822  30209  13333    -90   1834   1176  A    N1+
ATOM    640  N   ALA A 104      22.127   4.128 -65.535  1.00106.55      A    N  
ANISOU  640  N   ALA A 104    10374  22886   7226  -1531   1333   2164  A    N  
ATOM    641  CA  ALA A 104      22.963   4.102 -64.334  1.00105.76      A    C  
ANISOU  641  CA  ALA A 104    10113  22848   7222  -1658   1331   2196  A    C  
ATOM    642  C   ALA A 104      22.316   4.819 -63.153  1.00107.14      A    C  
ANISOU  642  C   ALA A 104    10528  22604   7578  -1775   1189   2205  A    C  
ATOM    643  O   ALA A 104      22.348   4.291 -62.042  1.00105.19      A    O  
ANISOU  643  O   ALA A 104    10197  22273   7496  -1681   1162   2104  A    O  
ATOM    644  CB  ALA A 104      24.331   4.696 -64.631  1.00109.50      A    C  
ANISOU  644  CB  ALA A 104    10392  23719   7496  -1976   1406   2404  A    C  
ATOM    645  N   VAL A 105      21.724   6.008 -63.396  1.00103.85      A    N  
ANISOU  645  N   VAL A 105    10427  21916   7113  -1952   1104   2328  A    N  
ATOM    646  CA  VAL A 105      21.049   6.845 -62.387  1.00102.41      A    C  
ANISOU  646  CA  VAL A 105    10541  21307   7061  -2041    979   2346  A    C  
ATOM    647  C   VAL A 105      19.769   6.167 -61.864  1.00102.01      A    C  
ANISOU  647  C   VAL A 105    10566  20985   7208  -1697    917   2152  A    C  
ATOM    648  O   VAL A 105      19.511   6.197 -60.660  1.00 99.77      A    O  
ANISOU  648  O   VAL A 105    10345  20482   7080  -1684    853   2092  A    O  
ATOM    649  CB  VAL A 105      20.785   8.286 -62.920  1.00108.56      A    C  
ANISOU  649  CB  VAL A 105    11684  21863   7699  -2282    925   2543  A    C  
ATOM    650  CG1 VAL A 105      20.107   9.171 -61.872  1.00107.61      A    C  
ANISOU  650  CG1 VAL A 105    11914  21284   7688  -2343    812   2556  A    C  
ATOM    651  CG2 VAL A 105      22.080   8.937 -63.403  1.00111.67      A    C  
ANISOU  651  CG2 VAL A 105    11999  22549   7882  -2684    988   2745  A    C  
ATOM    652  N   PHE A 106      18.986   5.552 -62.768  1.00 97.63      A    N  
ANISOU  652  N   PHE A 106     9996  20473   6627  -1444    935   2058  A    N  
ATOM    653  CA  PHE A 106      17.742   4.858 -62.429  1.00 94.71      A    C  
ANISOU  653  CA  PHE A 106     9669  19911   6407  -1158    877   1884  A    C  
ATOM    654  C   PHE A 106      17.973   3.579 -61.616  1.00 96.47      A    C  
ANISOU  654  C   PHE A 106     9673  20199   6783  -1015    916   1707  A    C  
ATOM    655  O   PHE A 106      17.209   3.326 -60.680  1.00 94.11      A    O  
ANISOU  655  O   PHE A 106     9434  19677   6647   -905    850   1612  A    O  
ATOM    656  CB  PHE A 106      16.925   4.554 -63.693  1.00 96.51      A    C  
ANISOU  656  CB  PHE A 106     9929  20219   6521   -987    879   1840  A    C  
ATOM    657  CG  PHE A 106      15.547   3.996 -63.426  1.00 96.00      A    C  
ANISOU  657  CG  PHE A 106     9913  19996   6569   -750    803   1690  A    C  
ATOM    658  CD1 PHE A 106      14.475   4.841 -63.167  1.00 98.57      A    C  
ANISOU  658  CD1 PHE A 106    10452  20079   6921   -686    699   1756  A    C  
ATOM    659  CD2 PHE A 106      15.317   2.626 -63.454  1.00 96.99      A    C  
ANISOU  659  CD2 PHE A 106     9879  20226   6746   -592    839   1490  A    C  
ATOM    660  CE1 PHE A 106      13.201   4.325 -62.927  1.00 98.07      A    C  
ANISOU  660  CE1 PHE A 106    10382  19943   6935   -479    631   1633  A    C  
ATOM    661  CE2 PHE A 106      14.042   2.110 -63.205  1.00 98.36      A    C  
ANISOU  661  CE2 PHE A 106    10087  20286   7001   -434    764   1362  A    C  
ATOM    662  CZ  PHE A 106      12.994   2.963 -62.947  1.00 96.12      A    C  
ANISOU  662  CZ  PHE A 106     9955  19825   6740   -384    659   1439  A    C  
ATOM    663  N   LEU A 107      18.997   2.767 -61.987  1.00 93.55      A    N  
ANISOU  663  N   LEU A 107     9060  20138   6345   -991   1029   1671  A    N  
ATOM    664  CA  LEU A 107      19.316   1.507 -61.311  1.00 92.32      A    C  
ANISOU  664  CA  LEU A 107     8722  20051   6305   -816   1084   1521  A    C  
ATOM    665  C   LEU A 107      19.740   1.693 -59.848  1.00 97.42      A    C  
ANISOU  665  C   LEU A 107     9323  20600   7093   -911   1040   1551  A    C  
ATOM    666  O   LEU A 107      19.361   0.874 -59.001  1.00 95.12      A    O  
ANISOU  666  O   LEU A 107     9005  20184   6953   -749   1025   1422  A    O  
ATOM    667  CB  LEU A 107      20.339   0.676 -62.089  1.00 93.66      A    C  
ANISOU  667  CB  LEU A 107     8669  20584   6336   -722   1229   1496  A    C  
ATOM    668  CG  LEU A 107      19.793  -0.122 -63.269  1.00 98.54      A    C  
ANISOU  668  CG  LEU A 107     9327  21262   6851   -522   1287   1358  A    C  
ATOM    669  CD1 LEU A 107      20.907  -0.541 -64.199  1.00101.26      A    C  
ANISOU  669  CD1 LEU A 107     9486  21991   6995   -470   1439   1388  A    C  
ATOM    670  CD2 LEU A 107      19.021  -1.340 -62.813  1.00 98.68      A    C  
ANISOU  670  CD2 LEU A 107     9396  21095   7004   -291   1279   1142  A    C  
ATOM    671  N   LEU A 108      20.477   2.786 -59.540  1.00 96.83      A    N  
ANISOU  671  N   LEU A 108     9262  20574   6954  -1198   1014   1723  A    N  
ATOM    672  CA  LEU A 108      20.861   3.073 -58.158  1.00 96.93      A    C  
ANISOU  672  CA  LEU A 108     9256  20502   7071  -1333    957   1754  A    C  
ATOM    673  C   LEU A 108      19.669   3.615 -57.345  1.00 97.91      A    C  
ANISOU  673  C   LEU A 108     9658  20208   7335  -1308    840   1705  A    C  
ATOM    674  O   LEU A 108      19.625   3.386 -56.140  1.00 96.74      A    O  
ANISOU  674  O   LEU A 108     9489  19950   7316  -1281    800   1647  A    O  
ATOM    675  CB  LEU A 108      22.127   3.957 -58.034  1.00 99.94      A    C  
ANISOU  675  CB  LEU A 108     9550  21110   7311  -1693    966   1942  A    C  
ATOM    676  CG  LEU A 108      22.092   5.393 -58.564  1.00107.01      A    C  
ANISOU  676  CG  LEU A 108    10716  21863   8079  -2005    911   2103  A    C  
ATOM    677  CD1 LEU A 108      21.848   6.388 -57.432  1.00107.23      A    C  
ANISOU  677  CD1 LEU A 108    10996  21575   8173  -2225    800   2142  A    C  
ATOM    678  CD2 LEU A 108      23.411   5.747 -59.238  1.00112.89      A    C  
ANISOU  678  CD2 LEU A 108    11279  23008   8607  -2289    986   2275  A    C  
ATOM    679  N   LYS A 109      18.699   4.294 -58.009  1.00 93.29      A    N  
ANISOU  679  N   LYS A 109     9318  19419   6707  -1285    792   1734  A    N  
ATOM    680  CA  LYS A 109      17.479   4.834 -57.393  1.00 91.36      A    C  
ANISOU  680  CA  LYS A 109     9332  18820   6560  -1196    696   1700  A    C  
ATOM    681  C   LYS A 109      16.556   3.694 -56.980  1.00 93.62      A    C  
ANISOU  681  C   LYS A 109     9529  19050   6994   -915    688   1520  A    C  
ATOM    682  O   LYS A 109      16.111   3.658 -55.827  1.00 92.96      A    O  
ANISOU  682  O   LYS A 109     9500  18784   7038   -864    637   1463  A    O  
ATOM    683  CB  LYS A 109      16.736   5.781 -58.349  1.00 94.28      A    C  
ANISOU  683  CB  LYS A 109     9957  19054   6811  -1190    660   1799  A    C  
ATOM    684  CG  LYS A 109      17.270   7.201 -58.356  1.00106.93      A    C  
ANISOU  684  CG  LYS A 109    11808  20530   8291  -1483    634   1982  A    C  
ATOM    685  CD  LYS A 109      16.480   8.093 -59.309  1.00113.28      A    C  
ANISOU  685  CD  LYS A 109    12886  21194   8963  -1432    608   2097  A    C  
ATOM    686  CE  LYS A 109      17.138   9.435 -59.513  1.00117.33      A    C  
ANISOU  686  CE  LYS A 109    13698  21553   9330  -1750    593   2290  A    C  
ATOM    687  NZ  LYS A 109      16.199  10.417 -60.107  1.00123.21      A    N1+
ANISOU  687  NZ  LYS A 109    14798  22052   9965  -1634    553   2404  A    N1+
ATOM    688  N   ILE A 110      16.277   2.753 -57.918  1.00 89.11      A    N  
ANISOU  688  N   ILE A 110     8834  18636   6387   -755    740   1430  A    N  
ATOM    689  CA  ILE A 110      15.442   1.573 -57.657  1.00 86.66      A    C  
ANISOU  689  CA  ILE A 110     8457  18284   6185   -542    737   1258  A    C  
ATOM    690  C   ILE A 110      16.151   0.644 -56.631  1.00 90.12      A    C  
ANISOU  690  C   ILE A 110     8738  18763   6741   -508    782   1182  A    C  
ATOM    691  O   ILE A 110      15.475   0.023 -55.806  1.00 88.50      A    O  
ANISOU  691  O   ILE A 110     8541  18421   6663   -398    751   1078  A    O  
ATOM    692  CB  ILE A 110      14.958   0.857 -58.962  1.00 89.28      A    C  
ANISOU  692  CB  ILE A 110     8753  18754   6415   -425    772   1174  A    C  
ATOM    693  CG1 ILE A 110      13.761  -0.070 -58.690  1.00 87.87      A    C  
ANISOU  693  CG1 ILE A 110     8585  18480   6321   -275    729   1017  A    C  
ATOM    694  CG2 ILE A 110      16.083   0.131 -59.713  1.00 90.43      A    C  
ANISOU  694  CG2 ILE A 110     8742  19153   6464   -416    891   1145  A    C  
ATOM    695  CD1 ILE A 110      12.671   0.034 -59.674  1.00 94.09      A    C  
ANISOU  695  CD1 ILE A 110     9433  19323   6995   -219    682    996  A    C  
ATOM    696  N   GLY A 111      17.492   0.632 -56.661  1.00 87.48      A    N  
ANISOU  696  N   GLY A 111     8258  18636   6346   -606    850   1254  A    N  
ATOM    697  CA  GLY A 111      18.333  -0.118 -55.733  1.00 87.22      A    C  
ANISOU  697  CA  GLY A 111     8053  18700   6385   -561    895   1225  A    C  
ATOM    698  C   GLY A 111      18.281   0.452 -54.325  1.00 90.64      A    C  
ANISOU  698  C   GLY A 111     8542  18969   6927   -669    813   1262  A    C  
ATOM    699  O   GLY A 111      18.254  -0.308 -53.350  1.00 89.87      A    O  
ANISOU  699  O   GLY A 111     8380  18823   6942   -559    814   1190  A    O  
ATOM    700  N   SER A 112      18.243   1.805 -54.213  1.00 87.01      A    N  
ANISOU  700  N   SER A 112     8240  18400   6420   -884    744   1375  A    N  
ATOM    701  CA  SER A 112      18.152   2.532 -52.942  1.00 85.93      A    C  
ANISOU  701  CA  SER A 112     8225  18074   6350  -1011    663   1405  A    C  
ATOM    702  C   SER A 112      16.797   2.297 -52.286  1.00 87.43      A    C  
ANISOU  702  C   SER A 112     8550  17999   6672   -824    610   1294  A    C  
ATOM    703  O   SER A 112      16.742   2.179 -51.066  1.00 85.87      A    O  
ANISOU  703  O   SER A 112     8354  17708   6564   -820    575   1260  A    O  
ATOM    704  CB  SER A 112      18.377   4.027 -53.149  1.00 90.52      A    C  
ANISOU  704  CB  SER A 112     9023  18556   6816  -1280    613   1542  A    C  
ATOM    705  OG  SER A 112      19.736   4.314 -53.433  1.00100.53      A    O  
ANISOU  705  OG  SER A 112    10143  20102   7953  -1527    653   1662  A    O  
ATOM    706  N   VAL A 113      15.710   2.221 -53.099  1.00 83.25      A    N  
ANISOU  706  N   VAL A 113     8109  17390   6133   -676    603   1247  A    N  
ATOM    707  CA  VAL A 113      14.331   1.972 -52.649  1.00 81.63      A    C  
ANISOU  707  CA  VAL A 113     7986  17012   6018   -499    556   1154  A    C  
ATOM    708  C   VAL A 113      14.227   0.555 -52.066  1.00 83.70      A    C  
ANISOU  708  C   VAL A 113     8087  17324   6393   -376    591   1030  A    C  
ATOM    709  O   VAL A 113      13.753   0.398 -50.939  1.00 82.08      A    O  
ANISOU  709  O   VAL A 113     7904  16998   6286   -331    558    988  A    O  
ATOM    710  CB  VAL A 113      13.289   2.233 -53.781  1.00 85.95      A    C  
ANISOU  710  CB  VAL A 113     8620  17553   6486   -394    537   1156  A    C  
ATOM    711  CG1 VAL A 113      11.931   1.602 -53.475  1.00 84.43      A    C  
ANISOU  711  CG1 VAL A 113     8410  17306   6364   -217    501   1052  A    C  
ATOM    712  CG2 VAL A 113      13.133   3.724 -54.052  1.00 87.22      A    C  
ANISOU  712  CG2 VAL A 113     9013  17583   6545   -466    493   1290  A    C  
ATOM    713  N   THR A 114      14.709  -0.460 -52.824  1.00 80.19      A    N  
ANISOU  713  N   THR A 114     7509  17044   5918   -318    665    977  A    N  
ATOM    714  CA  THR A 114      14.703  -1.877 -52.439  1.00 79.10      A    C  
ANISOU  714  CA  THR A 114     7275  16922   5856   -190    714    863  A    C  
ATOM    715  C   THR A 114      15.507  -2.129 -51.144  1.00 82.31      A    C  
ANISOU  715  C   THR A 114     7599  17330   6344   -201    723    890  A    C  
ATOM    716  O   THR A 114      14.991  -2.794 -50.242  1.00 79.70      A    O  
ANISOU  716  O   THR A 114     7282  16888   6114   -123    710    823  A    O  
ATOM    717  CB  THR A 114      15.159  -2.762 -53.618  1.00 87.01      A    C  
ANISOU  717  CB  THR A 114     8211  18082   6768   -112    805    807  A    C  
ATOM    719  CG2 THR A 114      14.882  -4.241 -53.388  1.00 82.72      A    C  
ANISOU  719  CG2 THR A 114     7673  17479   6278     31    854    669  A    C  
ATOM    718  OG1 THR A 114      14.511  -2.339 -54.821  1.00 90.50      A    O  
ANISOU  718  OG1 THR A 114     8724  18557   7105   -137    785    808  A    O  
ATOM    720  N   MET A 115      16.751  -1.579 -51.055  1.00 80.79      A    N  
ANISOU  720  N   MET A 115     7313  17292   6090   -319    740    999  A    N  
ATOM    721  CA  MET A 115      17.659  -1.721 -49.908  1.00 81.21      A    C  
ANISOU  721  CA  MET A 115     7250  17425   6179   -356    738   1049  A    C  
ATOM    722  C   MET A 115      17.079  -1.194 -48.577  1.00 83.69      A    C  
ANISOU  722  C   MET A 115     7675  17543   6581   -422    651   1046  A    C  
ATOM    723  O   MET A 115      17.111  -1.921 -47.577  1.00 82.04      A    O  
ANISOU  723  O   MET A 115     7408  17312   6450   -337    652   1014  A    O  
ATOM    724  CB  MET A 115      19.028  -1.091 -50.208  1.00 85.48      A    C  
ANISOU  724  CB  MET A 115     7654  18230   6596   -529    760   1180  A    C  
ATOM    725  CG  MET A 115      20.074  -1.373 -49.139  1.00 89.96      A    C  
ANISOU  725  CG  MET A 115     8035  18982   7163   -556    762   1243  A    C  
ATOM    726  SD  MET A 115      21.291  -0.051 -48.987  1.00 96.42      A    S  
ANISOU  726  SD  MET A 115     8763  20039   7832   -923    714   1412  A    S  
ATOM    727  CE  MET A 115      20.333   1.190 -48.131  1.00 91.94      A    C  
ANISOU  727  CE  MET A 115     8518  19094   7320  -1122    588   1393  A    C  
ATOM    728  N   THR A 116      16.545   0.049 -48.572  1.00 80.43      A    N  
ANISOU  728  N   THR A 116     7440  16978   6140   -548    582   1081  A    N  
ATOM    729  CA  THR A 116      15.946   0.674 -47.383  1.00 79.73      A    C  
ANISOU  729  CA  THR A 116     7501  16690   6104   -588    509   1071  A    C  
ATOM    730  C   THR A 116      14.683  -0.057 -46.916  1.00 82.97      A    C  
ANISOU  730  C   THR A 116     7944  16964   6618   -397    504    967  A    C  
ATOM    731  O   THR A 116      14.323   0.051 -45.747  1.00 83.32      A    O  
ANISOU  731  O   THR A 116     8054  16894   6711   -388    465    949  A    O  
ATOM    732  CB  THR A 116      15.693   2.173 -47.594  1.00 87.11      A    C  
ANISOU  732  CB  THR A 116     8669  17476   6952   -733    455   1137  A    C  
ATOM    734  CG2 THR A 116      16.972   2.959 -47.902  1.00 83.69      A    C  
ANISOU  734  CG2 THR A 116     8227  17171   6399  -1004    450   1252  A    C  
ATOM    733  OG1 THR A 116      14.705   2.353 -48.613  1.00 87.36      A    O  
ANISOU  733  OG1 THR A 116     8792  17443   6957   -617    462   1123  A    O  
ATOM    735  N   PHE A 117      14.014  -0.789 -47.827  1.00 78.55      A    N  
ANISOU  735  N   PHE A 117     7341  16433   6072   -269    542    901  A    N  
ATOM    736  CA  PHE A 117      12.823  -1.584 -47.526  1.00 77.04      A    C  
ANISOU  736  CA  PHE A 117     7158  16160   5953   -142    538    809  A    C  
ATOM    737  C   PHE A 117      13.202  -2.982 -47.014  1.00 79.55      A    C  
ANISOU  737  C   PHE A 117     7374  16511   6339    -71    591    756  A    C  
ATOM    738  O   PHE A 117      12.546  -3.478 -46.099  1.00 77.95      A    O  
ANISOU  738  O   PHE A 117     7186  16225   6207    -27    578    714  A    O  
ATOM    739  CB  PHE A 117      11.899  -1.695 -48.753  1.00 79.14      A    C  
ANISOU  739  CB  PHE A 117     7453  16449   6166    -86    538    766  A    C  
ATOM    740  CG  PHE A 117      10.868  -0.601 -48.919  1.00 81.06      A    C  
ANISOU  740  CG  PHE A 117     7813  16627   6359    -60    478    806  A    C  
ATOM    741  CD1 PHE A 117      10.029  -0.247 -47.868  1.00 83.21      A    C  
ANISOU  741  CD1 PHE A 117     8142  16804   6669      3    439    800  A    C  
ATOM    742  CD2 PHE A 117      10.672   0.008 -50.154  1.00 85.03      A    C  
ANISOU  742  CD2 PHE A 117     8371  17179   6759    -64    468    853  A    C  
ATOM    743  CE1 PHE A 117       9.062   0.748 -48.028  1.00 85.19      A    C  
ANISOU  743  CE1 PHE A 117     8509  17007   6852     92    397    844  A    C  
ATOM    744  CE2 PHE A 117       9.688   0.991 -50.322  1.00 88.76      A    C  
ANISOU  744  CE2 PHE A 117     8966  17591   7167     13    418    906  A    C  
ATOM    745  CZ  PHE A 117       8.887   1.352 -49.257  1.00 86.50      A    C  
ANISOU  745  CZ  PHE A 117     8740  17209   6916    108    386    901  A    C  
ATOM    746  N   THR A 118      14.244  -3.616 -47.609  1.00 76.96      A    N  
ANISOU  746  N   THR A 118     6957  16311   5975    -44    658    765  A    N  
ATOM    747  CA  THR A 118      14.740  -4.944 -47.223  1.00 77.41      A    C  
ANISOU  747  CA  THR A 118     6953  16389   6070     75    724    729  A    C  
ATOM    748  C   THR A 118      15.338  -4.904 -45.805  1.00 83.28      A    C  
ANISOU  748  C   THR A 118     7633  17147   6861     65    701    794  A    C  
ATOM    749  O   THR A 118      15.098  -5.828 -45.022  1.00 83.11      A    O  
ANISOU  749  O   THR A 118     7626  17049   6901    159    720    764  A    O  
ATOM    750  CB  THR A 118      15.710  -5.503 -48.283  1.00 85.50      A    C  
ANISOU  750  CB  THR A 118     7905  17569   7011    156    812    730  A    C  
ATOM    752  CG2 THR A 118      16.144  -6.947 -47.997  1.00 82.63      A    C  
ANISOU  752  CG2 THR A 118     7542  17189   6666    343    898    685  A    C  
ATOM    751  OG1 THR A 118      15.080  -5.445 -49.565  1.00 86.50      A    O  
ANISOU  751  OG1 THR A 118     8104  17688   7075    139    820    669  A    O  
ATOM    753  N   ALA A 119      16.062  -3.810 -45.464  1.00 80.79      A    N  
ANISOU  753  N   ALA A 119     7270  16925   6503    -72    653    885  A    N  
ATOM    754  CA  ALA A 119      16.673  -3.602 -44.145  1.00 80.64      A    C  
ANISOU  754  CA  ALA A 119     7190  16955   6495   -129    614    949  A    C  
ATOM    755  C   ALA A 119      15.643  -3.492 -43.018  1.00 82.61      A    C  
ANISOU  755  C   ALA A 119     7553  17017   6818   -130    560    906  A    C  
ATOM    756  O   ALA A 119      15.997  -3.747 -41.872  1.00 81.75      A    O  
ANISOU  756  O   ALA A 119     7397  16936   6730   -120    543    936  A    O  
ATOM    757  CB  ALA A 119      17.572  -2.376 -44.161  1.00 82.49      A    C  
ANISOU  757  CB  ALA A 119     7385  17323   6633   -342    567   1044  A    C  
ATOM    758  N   SER A 120      14.375  -3.136 -43.341  1.00 78.70      A    N  
ANISOU  758  N   SER A 120     7188  16369   6346   -124    537    845  A    N  
ATOM    759  CA  SER A 120      13.269  -3.039 -42.372  1.00 77.94      A    C  
ANISOU  759  CA  SER A 120     7178  16136   6298    -97    500    805  A    C  
ATOM    760  C   SER A 120      12.822  -4.432 -41.931  1.00 80.56      A    C  
ANISOU  760  C   SER A 120     7474  16436   6701      9    542    759  A    C  
ATOM    761  O   SER A 120      12.546  -4.643 -40.747  1.00 79.62      A    O  
ANISOU  761  O   SER A 120     7365  16273   6614     22    526    764  A    O  
ATOM    762  CB  SER A 120      12.077  -2.300 -42.976  1.00 81.90      A    C  
ANISOU  762  CB  SER A 120     7789  16554   6775    -83    474    771  A    C  
ATOM    763  OG  SER A 120      12.412  -0.959 -43.288  1.00 93.91      A    O  
ANISOU  763  OG  SER A 120     9415  18045   8222   -174    436    823  A    O  
ATOM    764  N   VAL A 121      12.737  -5.373 -42.899  1.00 76.89      A    N  
ANISOU  764  N   VAL A 121     6995  15979   6240     73    598    713  A    N  
ATOM    765  CA  VAL A 121      12.345  -6.776 -42.699  1.00 76.49      A    C  
ANISOU  765  CA  VAL A 121     6975  15854   6232    147    647    664  A    C  
ATOM    766  C   VAL A 121      13.460  -7.477 -41.922  1.00 79.71      A    C  
ANISOU  766  C   VAL A 121     7334  16296   6655    235    683    724  A    C  
ATOM    767  O   VAL A 121      13.172  -8.250 -41.004  1.00 79.89      A    O  
ANISOU  767  O   VAL A 121     7399  16237   6718    275    695    729  A    O  
ATOM    768  CB  VAL A 121      11.993  -7.495 -44.044  1.00 80.89      A    C  
ANISOU  768  CB  VAL A 121     7587  16392   6757    169    694    584  A    C  
ATOM    769  CG1 VAL A 121      11.600  -8.959 -43.822  1.00 81.31      A    C  
ANISOU  769  CG1 VAL A 121     7743  16319   6834    205    744    526  A    C  
ATOM    770  CG2 VAL A 121      10.881  -6.758 -44.792  1.00 80.03      A    C  
ANISOU  770  CG2 VAL A 121     7494  16305   6609     90    646    545  A    C  
ATOM    771  N   GLY A 122      14.710  -7.156 -42.274  1.00 75.19      A    N  
ANISOU  771  N   GLY A 122     6660  15875   6033    262    699    786  A    N  
ATOM    772  CA  GLY A 122      15.906  -7.664 -41.621  1.00 74.80      A    C  
ANISOU  772  CA  GLY A 122     6508  15948   5964    366    729    870  A    C  
ATOM    773  C   GLY A 122      15.970  -7.200 -40.184  1.00 77.54      A    C  
ANISOU  773  C   GLY A 122     6818  16319   6326    295    660    931  A    C  
ATOM    774  O   GLY A 122      16.147  -8.024 -39.283  1.00 77.48      A    O  
ANISOU  774  O   GLY A 122     6804  16300   6335    401    679    971  A    O  
ATOM    775  N   SER A 123      15.773  -5.874 -39.962  1.00 73.70      A    N  
ANISOU  775  N   SER A 123     6340  15844   5817    121    584    935  A    N  
ATOM    776  CA  SER A 123      15.769  -5.229 -38.639  1.00 73.52      A    C  
ANISOU  776  CA  SER A 123     6326  15827   5781     24    513    970  A    C  
ATOM    777  C   SER A 123      14.758  -5.883 -37.713  1.00 77.34      A    C  
ANISOU  777  C   SER A 123     6893  16165   6327     93    519    934  A    C  
ATOM    778  O   SER A 123      15.084  -6.137 -36.548  1.00 77.50      A    O  
ANISOU  778  O   SER A 123     6881  16231   6336    108    498    985  A    O  
ATOM    779  CB  SER A 123      15.478  -3.733 -38.751  1.00 76.57      A    C  
ANISOU  779  CB  SER A 123     6807  16165   6122   -150    447    951  A    C  
ATOM    780  OG  SER A 123      16.614  -3.014 -39.203  1.00 84.62      A    O  
ANISOU  780  OG  SER A 123     7753  17342   7056   -286    426   1014  A    O  
ATOM    781  N   LEU A 124      13.548  -6.190 -38.247  1.00 72.97      A    N  
ANISOU  781  N   LEU A 124     6432  15471   5822    121    546    856  A    N  
ATOM    782  CA  LEU A 124      12.471  -6.856 -37.516  1.00 72.42      A    C  
ANISOU  782  CA  LEU A 124     6427  15293   5794    149    559    827  A    C  
ATOM    783  C   LEU A 124      12.867  -8.278 -37.120  1.00 77.26      A    C  
ANISOU  783  C   LEU A 124     7048  15874   6433    257    616    865  A    C  
ATOM    784  O   LEU A 124      12.632  -8.668 -35.970  1.00 78.23      A    O  
ANISOU  784  O   LEU A 124     7192  15968   6564    270    611    903  A    O  
ATOM    785  CB  LEU A 124      11.129  -6.851 -38.296  1.00 71.86      A    C  
ANISOU  785  CB  LEU A 124     6417  15150   5738    120    569    748  A    C  
ATOM    786  CG  LEU A 124      10.191  -5.633 -38.106  1.00 76.00      A    C  
ANISOU  786  CG  LEU A 124     6967  15679   6229     78    520    723  A    C  
ATOM    787  CD1 LEU A 124       8.908  -5.808 -38.877  1.00 76.09      A    C  
ANISOU  787  CD1 LEU A 124     6986  15693   6234     73    529    667  A    C  
ATOM    788  CD2 LEU A 124       9.810  -5.425 -36.651  1.00 77.76      A    C  
ANISOU  788  CD2 LEU A 124     7207  15898   6441     80    501    743  A    C  
ATOM    789  N   LEU A 125      13.485  -9.039 -38.052  1.00 72.59      A    N  
ANISOU  789  N   LEU A 125     6461  15282   5837    353    675    861  A    N  
ATOM    790  CA  LEU A 125      13.926 -10.411 -37.804  1.00 73.33      A    C  
ANISOU  790  CA  LEU A 125     6618  15309   5935    507    745    898  A    C  
ATOM    791  C   LEU A 125      14.900 -10.487 -36.619  1.00 78.65      A    C  
ANISOU  791  C   LEU A 125     7196  16107   6580    598    727   1017  A    C  
ATOM    792  O   LEU A 125      14.726 -11.350 -35.758  1.00 78.84      A    O  
ANISOU  792  O   LEU A 125     7302  16039   6614    672    751   1063  A    O  
ATOM    793  CB  LEU A 125      14.521 -11.023 -39.082  1.00 74.35      A    C  
ANISOU  793  CB  LEU A 125     6780  15435   6035    628    819    864  A    C  
ATOM    794  CG  LEU A 125      15.232 -12.375 -38.966  1.00 80.83      A    C  
ANISOU  794  CG  LEU A 125     7697  16186   6829    860    909    909  A    C  
ATOM    795  CD1 LEU A 125      14.246 -13.524 -38.815  1.00 81.30      A    C  
ANISOU  795  CD1 LEU A 125     8014  15963   6913    841    954    849  A    C  
ATOM    796  CD2 LEU A 125      16.132 -12.601 -40.155  1.00 85.14      A    C  
ANISOU  796  CD2 LEU A 125     8207  16831   7313   1016    980    895  A    C  
ATOM    797  N   LEU A 126      15.890  -9.560 -36.561  1.00 75.81      A    N  
ANISOU  797  N   LEU A 126     6667  15970   6169    563    679   1074  A    N  
ATOM    798  CA  LEU A 126      16.867  -9.463 -35.470  1.00 76.56      A    C  
ANISOU  798  CA  LEU A 126     6628  16258   6205    605    640   1191  A    C  
ATOM    799  C   LEU A 126      16.192  -9.052 -34.147  1.00 80.48      A    C  
ANISOU  799  C   LEU A 126     7169  16701   6707    488    574   1195  A    C  
ATOM    800  O   LEU A 126      16.615  -9.506 -33.088  1.00 81.29      A    O  
ANISOU  800  O   LEU A 126     7233  16879   6774    564    562   1285  A    O  
ATOM    801  CB  LEU A 126      17.994  -8.470 -35.815  1.00 77.06      A    C  
ANISOU  801  CB  LEU A 126     6498  16596   6184    514    594   1242  A    C  
ATOM    802  CG  LEU A 126      19.055  -8.914 -36.821  1.00 82.50      A    C  
ANISOU  802  CG  LEU A 126     7065  17459   6822    664    664   1285  A    C  
ATOM    803  CD1 LEU A 126      19.868  -7.733 -37.296  1.00 82.75      A    C  
ANISOU  803  CD1 LEU A 126     6934  17734   6772    472    612   1315  A    C  
ATOM    804  CD2 LEU A 126      19.982  -9.971 -36.234  1.00 86.28      A    C  
ANISOU  804  CD2 LEU A 126     7439  18103   7241    931    712   1409  A    C  
ATOM    805  N   ALA A 127      15.146  -8.208 -34.214  1.00 76.14      A    N  
ANISOU  805  N   ALA A 127     6703  16040   6188    331    538   1104  A    N  
ATOM    806  CA  ALA A 127      14.385  -7.764 -33.046  1.00 75.86      A    C  
ANISOU  806  CA  ALA A 127     6724  15957   6141    246    493   1091  A    C  
ATOM    807  C   ALA A 127      13.590  -8.938 -32.440  1.00 81.78      A    C  
ANISOU  807  C   ALA A 127     7565  16575   6933    325    545   1105  A    C  
ATOM    808  O   ALA A 127      13.463  -9.019 -31.209  1.00 82.20      A    O  
ANISOU  808  O   ALA A 127     7624  16657   6952    321    524   1156  A    O  
ATOM    809  CB  ALA A 127      13.450  -6.618 -33.423  1.00 75.29      A    C  
ANISOU  809  CB  ALA A 127     6726  15808   6072    125    462    996  A    C  
ATOM    810  N   ALA A 128      13.083  -9.856 -33.312  1.00 77.88      A    N  
ANISOU  810  N   ALA A 128     7158  15938   6493    373    612   1063  A    N  
ATOM    811  CA  ALA A 128      12.313 -11.046 -32.929  1.00 77.57      A    C  
ANISOU  811  CA  ALA A 128     7248  15745   6480    394    666   1075  A    C  
ATOM    812  C   ALA A 128      13.190 -12.178 -32.374  1.00 82.31      A    C  
ANISOU  812  C   ALA A 128     7895  16321   7058    564    708   1187  A    C  
ATOM    813  O   ALA A 128      12.706 -12.957 -31.553  1.00 83.19      A    O  
ANISOU  813  O   ALA A 128     8110  16336   7163    566    732   1240  A    O  
ATOM    814  CB  ALA A 128      11.485 -11.545 -34.098  1.00 78.16      A    C  
ANISOU  814  CB  ALA A 128     7426  15681   6589    343    713    984  A    C  
ATOM    815  N   ILE A 129      14.466 -12.276 -32.800  1.00 78.18      A    N  
ANISOU  815  N   ILE A 129     7292  15904   6508    720    723   1237  A    N  
ATOM    816  CA  ILE A 129      15.362 -13.307 -32.264  1.00 79.27      A    C  
ANISOU  816  CA  ILE A 129     7457  16060   6602    947    766   1364  A    C  
ATOM    817  C   ILE A 129      15.955 -12.816 -30.914  1.00 83.18      A    C  
ANISOU  817  C   ILE A 129     7798  16775   7032    945    691   1475  A    C  
ATOM    818  O   ILE A 129      16.148 -13.626 -30.000  1.00 83.80      A    O  
ANISOU  818  O   ILE A 129     7928  16842   7069   1084    711   1591  A    O  
ATOM    819  CB  ILE A 129      16.403 -13.812 -33.299  1.00 83.37      A    C  
ANISOU  819  CB  ILE A 129     7953  16632   7094   1166    832   1382  A    C  
ATOM    820  CG1 ILE A 129      15.684 -14.422 -34.531  1.00 83.67      A    C  
ANISOU  820  CG1 ILE A 129     8202  16414   7175   1153    908   1259  A    C  
ATOM    821  CG2 ILE A 129      17.361 -14.841 -32.678  1.00 86.38      A    C  
ANISOU  821  CG2 ILE A 129     8347  17070   7404   1467    881   1536  A    C  
ATOM    822  CD1 ILE A 129      16.534 -14.484 -35.859  1.00 90.68      A    C  
ANISOU  822  CD1 ILE A 129     9033  17391   8029   1294    962   1220  A    C  
ATOM    823  N   ASP A 130      16.148 -11.478 -30.774  1.00 78.37      A    N  
ANISOU  823  N   ASP A 130     7038  16340   6398    768    605   1435  A    N  
ATOM    824  CA  ASP A 130      16.623 -10.799 -29.556  1.00 78.07      A    C  
ANISOU  824  CA  ASP A 130     6880  16509   6276    695    519   1504  A    C  
ATOM    825  C   ASP A 130      15.682 -11.092 -28.382  1.00 81.97      A    C  
ANISOU  825  C   ASP A 130     7490  16887   6767    650    517   1519  A    C  
ATOM    826  O   ASP A 130      16.148 -11.337 -27.278  1.00 82.66      A    O  
ANISOU  826  O   ASP A 130     7531  17100   6776    710    487   1629  A    O  
ATOM    827  CB  ASP A 130      16.714  -9.274 -29.797  1.00 78.60      A    C  
ANISOU  827  CB  ASP A 130     6861  16694   6310    475    437   1424  A    C  
ATOM    828  CG  ASP A 130      17.022  -8.439 -28.567  1.00 85.46      A    C  
ANISOU  828  CG  ASP A 130     7652  17753   7066    348    341   1466  A    C  
ATOM    829  OD1 ASP A 130      18.154  -8.526 -28.061  1.00 88.21      A    O  
ANISOU  829  OD1 ASP A 130     7837  18359   7320    397    302   1580  A    O  
ATOM    830  OD2 ASP A 130      16.135  -7.685 -28.124  1.00 88.24      A    O1-
ANISOU  830  OD2 ASP A 130     8105  18016   7405    205    306   1385  A    O1-
ATOM    831  N   ARG A 131      14.363 -11.070 -28.635  1.00 78.21      A    N  
ANISOU  831  N   ARG A 131     7146  16213   6358    543    549   1419  A    N  
ATOM    832  CA  ARG A 131      13.324 -11.333 -27.642  1.00 78.14      A    C  
ANISOU  832  CA  ARG A 131     7229  16125   6335    481    561   1432  A    C  
ATOM    833  C   ARG A 131      13.274 -12.805 -27.274  1.00 82.74      A    C  
ANISOU  833  C   ARG A 131     7939  16576   6921    607    629   1541  A    C  
ATOM    834  O   ARG A 131      13.086 -13.115 -26.095  1.00 83.34      A    O  
ANISOU  834  O   ARG A 131     8045  16683   6938    614    623   1631  A    O  
ATOM    835  CB  ARG A 131      11.953 -10.868 -28.152  1.00 78.30      A    C  
ANISOU  835  CB  ARG A 131     7310  16037   6402    340    581   1310  A    C  
ATOM    836  CG  ARG A 131      11.796  -9.359 -28.196  1.00 91.27      A    C  
ANISOU  836  CG  ARG A 131     8888  17764   8026    246    523   1209  A    C  
ATOM    837  CD  ARG A 131      11.417  -8.812 -26.843  1.00106.95      A    C  
ANISOU  837  CD  ARG A 131    10856  19864   9915    193    469   1214  A    C  
ATOM    838  NE  ARG A 131      11.825  -7.419 -26.688  1.00118.61      A    N  
ANISOU  838  NE  ARG A 131    12325  21387  11353    118    410   1131  A    N  
ATOM    839  CZ  ARG A 131      13.000  -7.032 -26.212  1.00137.51      A    C  
ANISOU  839  CZ  ARG A 131    14700  23899  13651     52    337   1144  A    C  
ATOM    840  NH1 ARG A 131      13.907  -7.933 -25.850  1.00124.67      A    N1+
ANISOU  840  NH1 ARG A 131    13018  22397  11952     72    308   1241  A    N1+
ATOM    841  NH2 ARG A 131      13.280  -5.746 -26.097  1.00130.40      A    N  
ANISOU  841  NH2 ARG A 131    13849  22990  12705    -49    289   1066  A    N  
ATOM    842  N   TYR A 132      13.436 -13.712 -28.277  1.00 78.64      A    N  
ANISOU  842  N   TYR A 132     7530  15893   6455    709    698   1534  A    N  
ATOM    843  CA  TYR A 132      13.431 -15.162 -28.051  1.00 79.48      A    C  
ANISOU  843  CA  TYR A 132     7841  15806   6553    843    775   1632  A    C  
ATOM    844  C   TYR A 132      14.561 -15.580 -27.106  1.00 84.09      A    C  
ANISOU  844  C   TYR A 132     8370  16527   7052   1065    762   1803  A    C  
ATOM    845  O   TYR A 132      14.289 -16.300 -26.152  1.00 84.31      A    O  
ANISOU  845  O   TYR A 132     8523  16476   7037   1096    783   1911  A    O  
ATOM    846  CB  TYR A 132      13.443 -15.978 -29.368  1.00 80.91      A    C  
ANISOU  846  CB  TYR A 132     8192  15770   6780    920    855   1570  A    C  
ATOM    847  CG  TYR A 132      13.538 -17.476 -29.147  1.00 84.68      A    C  
ANISOU  847  CG  TYR A 132     8953  15995   7226   1080    942   1670  A    C  
ATOM    848  CD1 TYR A 132      12.442 -18.207 -28.699  1.00 87.35      A    C  
ANISOU  848  CD1 TYR A 132     9524  16105   7560    910    980   1681  A    C  
ATOM    849  CD2 TYR A 132      14.739 -18.154 -29.340  1.00 87.52      A    C  
ANISOU  849  CD2 TYR A 132     9357  16358   7539   1409    989   1767  A    C  
ATOM    850  CE1 TYR A 132      12.539 -19.574 -28.440  1.00 90.66      A    C  
ANISOU  850  CE1 TYR A 132    10265  16248   7934   1039   1062   1783  A    C  
ATOM    851  CE2 TYR A 132      14.848 -19.521 -29.084  1.00 91.11      A    C  
ANISOU  851  CE2 TYR A 132    10126  16546   7946   1601   1077   1871  A    C  
ATOM    852  CZ  TYR A 132      13.743 -20.229 -28.641  1.00 99.70      A    C  
ANISOU  852  CZ  TYR A 132    11495  17350   9035   1402   1112   1875  A    C  
ATOM    853  OH  TYR A 132      13.843 -21.577 -28.400  1.00104.67      A    O  
ANISOU  853  OH  TYR A 132    12497  17667   9605   1572   1202   1981  A    O  
ATOM    854  N   LEU A 133      15.805 -15.101 -27.344  1.00 80.98      A    N  
ANISOU  854  N   LEU A 133     7776  16375   6619   1204    722   1840  A    N  
ATOM    855  CA  LEU A 133      16.974 -15.410 -26.503  1.00 82.66      A    C  
ANISOU  855  CA  LEU A 133     7871  16812   6724   1424    695   2015  A    C  
ATOM    856  C   LEU A 133      16.837 -14.845 -25.075  1.00 86.62      A    C  
ANISOU  856  C   LEU A 133     8272  17494   7145   1295    608   2075  A    C  
ATOM    857  O   LEU A 133      17.256 -15.500 -24.123  1.00 87.92      A    O  
ANISOU  857  O   LEU A 133     8447  17738   7220   1455    605   2236  A    O  
ATOM    858  CB  LEU A 133      18.288 -14.949 -27.162  1.00 83.23      A    C  
ANISOU  858  CB  LEU A 133     7701  17173   6748   1554    669   2040  A    C  
ATOM    859  CG  LEU A 133      18.576 -15.515 -28.569  1.00 88.78      A    C  
ANISOU  859  CG  LEU A 133     8489  17746   7498   1735    766   1992  A    C  
ATOM    860  CD1 LEU A 133      19.448 -14.573 -29.380  1.00 88.39      A    C  
ANISOU  860  CD1 LEU A 133     8168  18000   7417   1713    727   1960  A    C  
ATOM    861  CD2 LEU A 133      19.180 -16.912 -28.513  1.00 94.35      A    C  
ANISOU  861  CD2 LEU A 133     9362  18340   8148   2114    864   2133  A    C  
ATOM    862  N   CYS A 134      16.208 -13.660 -24.935  1.00 81.35      A    N  
ANISOU  862  N   CYS A 134     7535  16878   6495   1026    545   1946  A    N  
ATOM    863  CA  CYS A 134      15.956 -12.983 -23.661  1.00 81.34      A    C  
ANISOU  863  CA  CYS A 134     7475  17027   6406    882    469   1960  A    C  
ATOM    864  C   CYS A 134      14.943 -13.755 -22.792  1.00 86.13      A    C  
ANISOU  864  C   CYS A 134     8258  17462   7004    865    521   2015  A    C  
ATOM    865  O   CYS A 134      15.217 -13.990 -21.610  1.00 86.51      A    O  
ANISOU  865  O   CYS A 134     8287  17639   6944    917    490   2140  A    O  
ATOM    866  CB  CYS A 134      15.509 -11.540 -23.900  1.00 79.88      A    C  
ANISOU  866  CB  CYS A 134     7230  16888   6232    644    410   1794  A    C  
ATOM    867  SG  CYS A 134      15.057 -10.629 -22.394  1.00 83.52      A    S  
ANISOU  867  SG  CYS A 134     7685  17486   6565    473    334   1767  A    S  
ATOM    868  N   LEU A 135      13.782 -14.139 -23.382  1.00 81.94      A    N  
ANISOU  868  N   LEU A 135     7888  16675   6568    770    595   1930  A    N  
ATOM    869  CA  LEU A 135      12.700 -14.860 -22.703  1.00 82.62      A    C  
ANISOU  869  CA  LEU A 135     8138  16612   6641    690    652   1977  A    C  
ATOM    870  C   LEU A 135      12.891 -16.388 -22.623  1.00 89.85      A    C  
ANISOU  870  C   LEU A 135     9270  17318   7551    848    729   2127  A    C  
ATOM    871  O   LEU A 135      12.233 -17.021 -21.797  1.00 90.75      A    O  
ANISOU  871  O   LEU A 135     9517  17352   7614    789    765   2219  A    O  
ATOM    872  CB  LEU A 135      11.324 -14.527 -23.324  1.00 81.32      A    C  
ANISOU  872  CB  LEU A 135     8019  16331   6548    481    688   1830  A    C  
ATOM    873  CG  LEU A 135      10.830 -13.069 -23.234  1.00 84.44      A    C  
ANISOU  873  CG  LEU A 135     8269  16891   6923    351    633   1696  A    C  
ATOM    874  CD1 LEU A 135       9.769 -12.791 -24.270  1.00 83.73      A    C  
ANISOU  874  CD1 LEU A 135     8191  16710   6911    232    666   1562  A    C  
ATOM    875  CD2 LEU A 135      10.302 -12.724 -21.848  1.00 85.79      A    C  
ANISOU  875  CD2 LEU A 135     8421  17193   6981    282    622   1733  A    C  
ATOM    876  N   ARG A 136      13.760 -16.984 -23.472  1.00 87.92      A    N  
ANISOU  876  N   ARG A 136     9085  16976   7343   1054    765   2154  A    N  
ATOM    877  CA  ARG A 136      14.003 -18.434 -23.458  1.00 90.48      A    C  
ANISOU  877  CA  ARG A 136     9678  17056   7644   1255    850   2292  A    C  
ATOM    878  C   ARG A 136      15.201 -18.779 -22.570  1.00 98.41      A    C  
ANISOU  878  C   ARG A 136    10608  18249   8534   1545    822   2492  A    C  
ATOM    879  O   ARG A 136      15.080 -19.665 -21.724  1.00 99.98      A    O  
ANISOU  879  O   ARG A 136    10993  18334   8661   1629    859   2649  A    O  
ATOM    880  CB  ARG A 136      14.106 -19.020 -24.892  1.00 90.13      A    C  
ANISOU  880  CB  ARG A 136     9802  16768   7676   1347    926   2206  A    C  
ATOM    881  CG  ARG A 136      14.505 -20.496 -25.018  1.00100.85      A    C  
ANISOU  881  CG  ARG A 136    11497  17832   8992   1610   1026   2333  A    C  
ATOM    882  CD  ARG A 136      13.436 -21.493 -24.606  1.00109.81      A    C  
ANISOU  882  CD  ARG A 136    12992  18617  10113   1428   1094   2370  A    C  
ATOM    883  NE  ARG A 136      13.942 -22.868 -24.645  1.00119.99      A    N  
ANISOU  883  NE  ARG A 136    14663  19588  11340   1708   1192   2502  A    N  
ATOM    884  CZ  ARG A 136      14.525 -23.489 -23.621  1.00136.56      A    C  
ANISOU  884  CZ  ARG A 136    16874  21675  13337   1947   1209   2719  A    C  
ATOM    885  NH1 ARG A 136      14.955 -24.736 -23.753  1.00126.87      A    N1+
ANISOU  885  NH1 ARG A 136    16043  20116  12044   2235   1309   2834  A    N1+
ATOM    886  NH2 ARG A 136      14.683 -22.867 -22.459  1.00122.84      A    N  
ANISOU  886  NH2 ARG A 136    14877  20250  11546   1913   1128   2822  A    N  
ATOM    887  N   TYR A 137      16.339 -18.065 -22.739  1.00 96.43      A    N  
ANISOU  887  N   TYR A 137    10075  18315   8247   1678    753   2499  A    N  
ATOM    888  CA  TYR A 137      17.559 -18.251 -21.927  1.00 98.79      A    C  
ANISOU  888  CA  TYR A 137    10221  18906   8409   1943    706   2693  A    C  
ATOM    889  C   TYR A 137      17.896 -16.915 -21.199  1.00101.50      A    C  
ANISOU  889  C   TYR A 137    10242  19649   8673   1753    571   2662  A    C  
ATOM    890  O   TYR A 137      18.795 -16.189 -21.653  1.00100.86      A    O  
ANISOU  890  O   TYR A 137     9910  19849   8563   1770    509   2632  A    O  
ATOM    891  CB  TYR A 137      18.752 -18.747 -22.782  1.00101.97      A    C  
ANISOU  891  CB  TYR A 137    10568  19385   8789   2295    751   2763  A    C  
ATOM    892  CG  TYR A 137      18.415 -19.823 -23.794  1.00105.68      A    C  
ANISOU  892  CG  TYR A 137    11382  19437   9335   2452    886   2728  A    C  
ATOM    893  CD1 TYR A 137      18.389 -21.168 -23.432  1.00110.28      A    C  
ANISOU  893  CD1 TYR A 137    12302  19737   9863   2701    977   2883  A    C  
ATOM    894  CD2 TYR A 137      18.166 -19.500 -25.128  1.00105.54      A    C  
ANISOU  894  CD2 TYR A 137    11380  19297   9423   2356    923   2543  A    C  
ATOM    895  CE1 TYR A 137      18.096 -22.164 -24.363  1.00112.68      A    C  
ANISOU  895  CE1 TYR A 137    12984  19617  10211   2827   1102   2838  A    C  
ATOM    896  CE2 TYR A 137      17.880 -20.488 -26.070  1.00107.90      A    C  
ANISOU  896  CE2 TYR A 137    12019  19214   9766   2484   1043   2495  A    C  
ATOM    897  CZ  TYR A 137      17.839 -21.818 -25.681  1.00120.00      A    C  
ANISOU  897  CZ  TYR A 137    13915  20441  11238   2710   1133   2635  A    C  
ATOM    898  OH  TYR A 137      17.551 -22.794 -26.606  1.00124.79      A    O  
ANISOU  898  OH  TYR A 137    14917  20630  11866   2813   1252   2573  A    O  
ATOM    899  N   PRO A 138      17.176 -16.563 -20.091  1.00 96.96      A    N  
ANISOU  899  N   PRO A 138     9689  19107   8045   1554    528   2663  A    N  
ATOM    900  CA  PRO A 138      17.416 -15.263 -19.434  1.00 96.26      A    C  
ANISOU  900  CA  PRO A 138     9364  19347   7864   1355    406   2602  A    C  
ATOM    901  C   PRO A 138      18.841 -14.997 -18.891  1.00104.02      A    C  
ANISOU  901  C   PRO A 138    10085  20754   8682   1486    305   2742  A    C  
ATOM    902  O   PRO A 138      19.355 -13.940 -19.269  1.00103.94      A    O  
ANISOU  902  O   PRO A 138     9875  20971   8647   1330    223   2643  A    O  
ATOM    903  CB  PRO A 138      16.353 -15.213 -18.331  1.00 97.47      A    C  
ANISOU  903  CB  PRO A 138     9639  19427   7970   1187    410   2598  A    C  
ATOM    904  CG  PRO A 138      15.300 -16.167 -18.773  1.00101.23      A    C  
ANISOU  904  CG  PRO A 138    10379  19523   8560   1181    531   2587  A    C  
ATOM    905  CD  PRO A 138      16.046 -17.270 -19.452  1.00 98.28      A    C  
ANISOU  905  CD  PRO A 138    10111  19010   8222   1468    595   2702  A    C  
ATOM    906  N   PRO A 139      19.530 -15.844 -18.067  1.00103.33      A    N  
ANISOU  906  N   PRO A 139     9978  20815   8466   1750    301   2971  A    N  
ATOM    907  CA  PRO A 139      20.879 -15.457 -17.601  1.00104.76      A    C  
ANISOU  907  CA  PRO A 139     9848  21490   8468   1840    188   3099  A    C  
ATOM    908  C   PRO A 139      21.963 -15.428 -18.678  1.00108.79      A    C  
ANISOU  908  C   PRO A 139    10152  22195   8986   2017    194   3124  A    C  
ATOM    909  O   PRO A 139      22.901 -14.637 -18.582  1.00109.18      A    O  
ANISOU  909  O   PRO A 139     9893  22686   8905   1934     85   3153  A    O  
ATOM    910  CB  PRO A 139      21.188 -16.492 -16.519  1.00109.38      A    C  
ANISOU  910  CB  PRO A 139    10494  22152   8913   2111    197   3350  A    C  
ATOM    911  CG  PRO A 139      20.391 -17.682 -16.900  1.00114.11      A    C  
ANISOU  911  CG  PRO A 139    11450  22263   9643   2284    347   3383  A    C  
ATOM    912  CD  PRO A 139      19.123 -17.140 -17.478  1.00106.70      A    C  
ANISOU  912  CD  PRO A 139    10666  20995   8881   1961    391   3137  A    C  
ATOM    913  N   SER A 140      21.828 -16.282 -19.702  1.00105.26      A    N  
ANISOU  913  N   SER A 140     9882  21439   8675   2241    323   3113  A    N  
ATOM    914  CA  SER A 140      22.778 -16.393 -20.813  1.00105.62      A    C  
ANISOU  914  CA  SER A 140     9766  21638   8725   2458    361   3135  A    C  
ATOM    915  C   SER A 140      22.720 -15.229 -21.820  1.00105.78      A    C  
ANISOU  915  C   SER A 140     9650  21708   8833   2156    325   2925  A    C  
ATOM    916  O   SER A 140      23.665 -15.063 -22.587  1.00105.88      A    O  
ANISOU  916  O   SER A 140     9447  21976   8808   2273    330   2954  A    O  
ATOM    917  CB  SER A 140      22.611 -17.735 -21.521  1.00110.12      A    C  
ANISOU  917  CB  SER A 140    10633  21828   9379   2821    521   3190  A    C  
ATOM    918  OG  SER A 140      22.765 -18.810 -20.607  1.00121.89      A    O  
ANISOU  918  OG  SER A 140    12281  23262  10770   3124    557   3407  A    O  
ATOM    919  N   TYR A 141      21.638 -14.417 -21.804  1.00 99.64      A    N  
ANISOU  919  N   TYR A 141     8993  20713   8153   1787    293   2730  A    N  
ATOM    920  CA  TYR A 141      21.447 -13.278 -22.716  1.00 97.31      A    C  
ANISOU  920  CA  TYR A 141     8630  20407   7937   1500    262   2535  A    C  
ATOM    921  C   TYR A 141      22.483 -12.158 -22.526  1.00102.19      A    C  
ANISOU  921  C   TYR A 141     8932  21492   8405   1304    131   2551  A    C  
ATOM    922  O   TYR A 141      22.999 -11.655 -23.526  1.00101.23      A    O  
ANISOU  922  O   TYR A 141     8674  21490   8300   1244    131   2500  A    O  
ATOM    923  CB  TYR A 141      20.007 -12.740 -22.632  1.00 95.64      A    C  
ANISOU  923  CB  TYR A 141     8641  19859   7837   1220    269   2349  A    C  
ATOM    924  CG  TYR A 141      19.751 -11.442 -23.378  1.00 94.95      A    C  
ANISOU  924  CG  TYR A 141     8517  19753   7806    935    227   2161  A    C  
ATOM    925  CD1 TYR A 141      19.428 -11.444 -24.734  1.00 95.43      A    C  
ANISOU  925  CD1 TYR A 141     8646  19611   8001    954    302   2057  A    C  
ATOM    926  CD2 TYR A 141      19.741 -10.221 -22.708  1.00 95.07      A    C  
ANISOU  926  CD2 TYR A 141     8476  19919   7727    647    118   2083  A    C  
ATOM    927  CE1 TYR A 141      19.159 -10.256 -25.414  1.00 93.82      A    C  
ANISOU  927  CE1 TYR A 141     8432  19378   7839    710    266   1903  A    C  
ATOM    928  CE2 TYR A 141      19.482  -9.027 -23.378  1.00 94.16      A    C  
ANISOU  928  CE2 TYR A 141     8386  19740   7649    403     87   1921  A    C  
ATOM    929  CZ  TYR A 141      19.189  -9.049 -24.731  1.00 98.21      A    C  
ANISOU  929  CZ  TYR A 141     8948  20066   8300    443    161   1841  A    C  
ATOM    930  OH  TYR A 141      18.928  -7.865 -25.377  1.00 95.19      A    O  
ANISOU  930  OH  TYR A 141     8609  19616   7943    219    130   1701  A    O  
ATOM    931  N   LYS A 142      22.771 -11.756 -21.265  1.00100.44      A    N  
ANISOU  931  N   LYS A 142     8605  21535   8021   1171     18   2620  A    N  
ATOM    932  CA  LYS A 142      23.760 -10.708 -20.969  1.00101.92      A    C  
ANISOU  932  CA  LYS A 142     8513  22184   8027    920   -123   2639  A    C  
ATOM    933  C   LYS A 142      25.182 -11.099 -21.408  1.00109.29      A    C  
ANISOU  933  C   LYS A 142     9110  23571   8842   1140   -131   2819  A    C  
ATOM    934  O   LYS A 142      25.941 -10.241 -21.870  1.00109.90      A    O  
ANISOU  934  O   LYS A 142     8966  23955   8838    915   -200   2794  A    O  
ATOM    935  CB  LYS A 142      23.716 -10.276 -19.498  1.00105.12      A    C  
ANISOU  935  CB  LYS A 142     8906  22774   8260    744   -240   2673  A    C  
ATOM    936  CG  LYS A 142      22.599  -9.268 -19.210  1.00113.69      A    C  
ANISOU  936  CG  LYS A 142    10235  23574   9387    400   -271   2454  A    C  
ATOM    937  CD  LYS A 142      23.008  -8.269 -18.132  1.00121.92      A    C  
ANISOU  937  CD  LYS A 142    11179  24946  10201     53   -431   2422  A    C  
ATOM    938  CE  LYS A 142      22.396  -6.898 -18.317  1.00124.79      A    C  
ANISOU  938  CE  LYS A 142    11759  25071  10586   -307   -463   2184  A    C  
ATOM    939  NZ  LYS A 142      21.043  -6.790 -17.708  1.00131.68      A    N1+
ANISOU  939  NZ  LYS A 142    12917  25621  11495   -323   -421   2068  A    N1+
ATOM    940  N   ALA A 143      25.513 -12.402 -21.314  1.00107.21      A    N  
ANISOU  940  N   ALA A 143     8827  23344   8562   1589    -49   3005  A    N  
ATOM    941  CA  ALA A 143      26.793 -12.958 -21.748  1.00109.56      A    C  
ANISOU  941  CA  ALA A 143     8819  24070   8738   1917    -25   3198  A    C  
ATOM    942  C   ALA A 143      26.855 -13.043 -23.276  1.00112.86      A    C  
ANISOU  942  C   ALA A 143     9251  24345   9287   2025     90   3113  A    C  
ATOM    943  O   ALA A 143      27.936 -12.897 -23.846  1.00114.68      A    O  
ANISOU  943  O   ALA A 143     9157  25018   9400   2096     80   3203  A    O  
ATOM    944  CB  ALA A 143      26.990 -14.338 -21.145  1.00112.45      A    C  
ANISOU  944  CB  ALA A 143     9248  24434   9045   2409     45   3416  A    C  
ATOM    945  N   LEU A 144      25.701 -13.281 -23.936  1.00107.26      A    N  
ANISOU  945  N   LEU A 144     8900  23058   8798   2029    198   2947  A    N  
ATOM    946  CA  LEU A 144      25.589 -13.391 -25.396  1.00106.32      A    C  
ANISOU  946  CA  LEU A 144     8849  22743   8804   2117    310   2843  A    C  
ATOM    947  C   LEU A 144      25.455 -12.025 -26.096  1.00108.12      A    C  
ANISOU  947  C   LEU A 144     9002  23001   9077   1680    246   2666  A    C  
ATOM    948  O   LEU A 144      26.423 -11.575 -26.706  1.00108.62      A    O  
ANISOU  948  O   LEU A 144     8785  23440   9045   1639    227   2711  A    O  
ATOM    949  CB  LEU A 144      24.448 -14.342 -25.804  1.00104.88      A    C  
ANISOU  949  CB  LEU A 144     9083  21962   8805   2302    446   2755  A    C  
ATOM    950  N   LEU A 145      24.277 -11.365 -26.000  1.00102.12      A    N  
ANISOU  950  N   LEU A 145     8492  21867   8443   1366    217   2482  A    N  
ATOM    951  CA  LEU A 145      24.040 -10.064 -26.635  1.00100.25      A    C  
ANISOU  951  CA  LEU A 145     8254  21592   8243    980    162   2319  A    C  
ATOM    952  C   LEU A 145      24.712  -8.914 -25.890  1.00105.25      A    C  
ANISOU  952  C   LEU A 145     8682  22611   8698    631      8   2347  A    C  
ATOM    953  O   LEU A 145      24.414  -8.663 -24.719  1.00105.74      A    O  
ANISOU  953  O   LEU A 145     8796  22694   8686    509    -74   2355  A    O  
ATOM    954  CB  LEU A 145      22.543  -9.791 -26.843  1.00 97.24      A    C  
ANISOU  954  CB  LEU A 145     8208  20705   8035    825    195   2128  A    C  
ATOM    955  N   THR A 146      25.634  -8.234 -26.584  1.00102.00      A    N  
ANISOU  955  N   THR A 146     8043  22516   8197    456    -30   2364  A    N  
ATOM    956  CA  THR A 146      26.404  -7.085 -26.100  1.00103.18      A    C  
ANISOU  956  CA  THR A 146     7995  23059   8148     55   -179   2390  A    C  
ATOM    957  C   THR A 146      26.180  -5.910 -27.067  1.00103.66      A    C  
ANISOU  957  C   THR A 146     8161  22975   8251   -304   -194   2243  A    C  
ATOM    958  O   THR A 146      25.795  -6.139 -28.216  1.00101.78      A    O  
ANISOU  958  O   THR A 146     8002  22517   8154   -168    -88   2183  A    O  
ATOM    959  CB  THR A 146      27.908  -7.442 -25.998  1.00119.46      A    C  
ANISOU  959  CB  THR A 146     9615  25770  10003    193   -212   2615  A    C  
ATOM    961  CG2 THR A 146      28.619  -6.660 -24.908  1.00121.09      A    C  
ANISOU  961  CG2 THR A 146     9609  26439   9960   -201   -389   2679  A    C  
ATOM    960  OG1 THR A 146      28.076  -8.841 -25.758  1.00122.78      A    O  
ANISOU  960  OG1 THR A 146     9989  26229  10434    689   -135   2761  A    O  
ATOM    962  N   ARG A 147      26.429  -4.664 -26.606  1.00 99.19      A    N  
ANISOU  962  N   ARG A 147     7622  22521   7544   -764   -327   2187  A    N  
ATOM    963  CA  ARG A 147      26.294  -3.424 -27.384  1.00 97.47      A    C  
ANISOU  963  CA  ARG A 147     7550  22162   7322  -1150   -359   2064  A    C  
ATOM    964  C   ARG A 147      27.136  -3.469 -28.667  1.00101.12      A    C  
ANISOU  964  C   ARG A 147     7758  22902   7759  -1135   -305   2149  A    C  
ATOM    965  O   ARG A 147      26.636  -3.104 -29.732  1.00 99.31      A    O  
ANISOU  965  O   ARG A 147     7698  22389   7646  -1183   -240   2050  A    O  
ATOM    966  CB  ARG A 147      26.677  -2.216 -26.516  1.00 98.23      A    C  
ANISOU  966  CB  ARG A 147     7699  22418   7204  -1643   -519   2031  A    C  
ATOM    967  CG  ARG A 147      26.383  -0.852 -27.122  1.00104.90      A    C  
ANISOU  967  CG  ARG A 147     8823  23002   8032  -2056   -555   1890  A    C  
ATOM    968  CD  ARG A 147      26.577   0.211 -26.063  1.00120.25      A    C  
ANISOU  968  CD  ARG A 147    10910  25027   9752  -2519   -708   1837  A    C  
ATOM    969  NE  ARG A 147      26.678   1.558 -26.624  1.00133.61      A    N  
ANISOU  969  NE  ARG A 147    12887  26503  11377  -2952   -751   1728  A    N  
ATOM    970  CZ  ARG A 147      26.894   2.655 -25.902  1.00153.71      A    C  
ANISOU  970  CZ  ARG A 147    15653  29040  13710  -3423   -878   1656  A    C  
ATOM    971  NH1 ARG A 147      26.975   3.838 -26.494  1.00145.66      A    N1+
ANISOU  971  NH1 ARG A 147    14945  27767  12630  -3791   -902   1566  A    N1+
ATOM    972  NH2 ARG A 147      27.032   2.576 -24.583  1.00140.02      A    N  
ANISOU  972  NH2 ARG A 147    13858  27539  11806  -3535   -982   1675  A    N  
ATOM    973  N   GLY A 148      28.373  -3.957 -28.549  1.00 99.04      A    N  
ANISOU  973  N   GLY A 148     7084  23213   7333  -1036   -325   2339  A    N  
ATOM    974  CA  GLY A 148      29.318  -4.106 -29.653  1.00 99.80      A    C  
ANISOU  974  CA  GLY A 148     6867  23689   7362   -975   -264   2451  A    C  
ATOM    975  C   GLY A 148      28.920  -5.199 -30.622  1.00100.77      A    C  
ANISOU  975  C   GLY A 148     7034  23584   7670   -472    -89   2441  A    C  
ATOM    976  O   GLY A 148      28.841  -4.953 -31.828  1.00100.99      A    O  
ANISOU  976  O   GLY A 148     7087  23529   7755   -499    -14   2393  A    O  
ATOM    977  N   ARG A 149      28.621  -6.401 -30.094  1.00 94.74      A    N  
ANISOU  977  N   ARG A 149     6320  22689   6990    -29    -23   2482  A    N  
ATOM    978  CA  ARG A 149      28.183  -7.574 -30.861  1.00 92.43      A    C  
ANISOU  978  CA  ARG A 149     6143  22118   6856    454    143   2464  A    C  
ATOM    979  C   ARG A 149      26.896  -7.299 -31.635  1.00 91.59      A    C  
ANISOU  979  C   ARG A 149     6417  21419   6964    370    203   2257  A    C  
ATOM    980  O   ARG A 149      26.742  -7.825 -32.737  1.00 91.37      A    O  
ANISOU  980  O   ARG A 149     6439  21257   7021    594    324   2220  A    O  
ATOM    981  CB  ARG A 149      28.013  -8.806 -29.955  1.00 92.66      A    C  
ANISOU  981  CB  ARG A 149     6229  22066   6911    866    182   2549  A    C  
ATOM    982  CG  ARG A 149      29.319  -9.292 -29.336  1.00105.16      A    C  
ANISOU  982  CG  ARG A 149     7415  24257   8283   1135    171   2787  A    C  
ATOM    983  CD  ARG A 149      29.123 -10.535 -28.508  1.00112.66      A    C  
ANISOU  983  CD  ARG A 149     8460  25110   9236   1488    186   2883  A    C  
ATOM    984  NE  ARG A 149      30.383 -10.995 -27.922  1.00126.78      A    N  
ANISOU  984  NE  ARG A 149     9869  27492  10810   1824    187   3131  A    N  
ATOM    985  CZ  ARG A 149      30.472 -11.889 -26.943  1.00143.96      A    C  
ANISOU  985  CZ  ARG A 149    12021  29772  12904   2089    161   3277  A    C  
ATOM    986  NH1 ARG A 149      31.659 -12.250 -26.474  1.00136.80      A    N1+
ANISOU  986  NH1 ARG A 149    10744  29452  11784   2428    164   3518  A    N1+
ATOM    987  NH2 ARG A 149      29.373 -12.424 -26.420  1.00126.66      A    N  
ANISOU  987  NH2 ARG A 149    10163  27131  10829   2027    133   3197  A    N  
ATOM    988  N   ALA A 150      25.984  -6.466 -31.073  1.00 84.15      A    N  
ANISOU  988  N   ALA A 150     5737  20150   6087     60    120   2124  A    N  
ATOM    989  CA  ALA A 150      24.726  -6.083 -31.721  1.00 79.80      A    C  
ANISOU  989  CA  ALA A 150     5522  19088   5711    -30    161   1941  A    C  
ATOM    990  C   ALA A 150      25.022  -5.202 -32.929  1.00 82.81      A    C  
ANISOU  990  C   ALA A 150     5868  19532   6065   -264    165   1901  A    C  
ATOM    991  O   ALA A 150      24.468  -5.451 -33.998  1.00 81.37      A    O  
ANISOU  991  O   ALA A 150     5816  19101   6001   -142    257   1820  A    O  
ATOM    992  CB  ALA A 150      23.813  -5.351 -30.741  1.00 78.69      A    C  
ANISOU  992  CB  ALA A 150     5630  18671   5598   -267     74   1834  A    C  
ATOM    993  N   LEU A 151      25.929  -4.211 -32.774  1.00 81.00      A    N  
ANISOU  993  N   LEU A 151     5461  19654   5660   -618     65   1968  A    N  
ATOM    994  CA  LEU A 151      26.323  -3.288 -33.846  1.00 81.90      A    C  
ANISOU  994  CA  LEU A 151     5539  19868   5711   -902     60   1960  A    C  
ATOM    995  C   LEU A 151      26.988  -4.002 -35.047  1.00 88.25      A    C  
ANISOU  995  C   LEU A 151     6099  20931   6501   -640    180   2043  A    C  
ATOM    996  O   LEU A 151      26.766  -3.601 -36.195  1.00 85.75      A    O  
ANISOU  996  O   LEU A 151     5866  20495   6221   -726    230   1988  A    O  
ATOM    997  CB  LEU A 151      27.193  -2.130 -33.314  1.00 84.05      A    C  
ANISOU  997  CB  LEU A 151     5695  20472   5769  -1388    -81   2024  A    C  
ATOM    998  CG  LEU A 151      26.485  -1.106 -32.407  1.00 87.40      A    C  
ANISOU  998  CG  LEU A 151     6468  20557   6183  -1727   -189   1898  A    C  
ATOM    999  CD1 LEU A 151      27.478  -0.348 -31.557  1.00 90.06      A    C  
ANISOU  999  CD1 LEU A 151     6665  21277   6275  -2151   -335   1976  A    C  
ATOM   1000  CD2 LEU A 151      25.618  -0.136 -33.201  1.00 87.79      A    C  
ANISOU 1000  CD2 LEU A 151     6861  20185   6309  -1917   -171   1769  A    C  
ATOM   1001  N   VAL A 152      27.755  -5.087 -34.774  1.00 88.45      A    N  
ANISOU 1001  N   VAL A 152     5845  21297   6463   -288    233   2177  A    N  
ATOM   1002  CA  VAL A 152      28.406  -5.922 -35.790  1.00 90.36      A    C  
ANISOU 1002  CA  VAL A 152     5869  21793   6670     57    367   2258  A    C  
ATOM   1003  C   VAL A 152      27.330  -6.721 -36.554  1.00 92.98      A    C  
ANISOU 1003  C   VAL A 152     6512  21611   7204    377    495   2117  A    C  
ATOM   1004  O   VAL A 152      27.366  -6.767 -37.786  1.00 92.01      A    O  
ANISOU 1004  O   VAL A 152     6392  21474   7092    443    586   2080  A    O  
ATOM   1005  CB  VAL A 152      29.508  -6.837 -35.186  1.00 97.79      A    C  
ANISOU 1005  CB  VAL A 152     6447  23251   7457    386    389   2452  A    C  
ATOM   1006  CG1 VAL A 152      30.191  -7.679 -36.265  1.00 99.52      A    C  
ANISOU 1006  CG1 VAL A 152     6484  23701   7629    820    552   2525  A    C  
ATOM   1007  CG2 VAL A 152      30.548  -6.023 -34.421  1.00100.41      A    C  
ANISOU 1007  CG2 VAL A 152     6431  24163   7557     14    250   2596  A    C  
ATOM   1008  N   LEU A 153      26.355  -7.308 -35.820  1.00 89.39      A    N  
ANISOU 1008  N   LEU A 153     6323  20751   6891    531    495   2037  A    N  
ATOM   1009  CA  LEU A 153      25.247  -8.073 -36.407  1.00 87.89      A    C  
ANISOU 1009  CA  LEU A 153     6444  20074   6875    765    596   1902  A    C  
ATOM   1010  C   LEU A 153      24.349  -7.212 -37.283  1.00 92.14      A    C  
ANISOU 1010  C   LEU A 153     7196  20305   7507    503    585   1752  A    C  
ATOM   1011  O   LEU A 153      23.896  -7.670 -38.334  1.00 92.17      A    O  
ANISOU 1011  O   LEU A 153     7337  20098   7586    659    680   1667  A    O  
ATOM   1012  CB  LEU A 153      24.437  -8.812 -35.343  1.00 86.65      A    C  
ANISOU 1012  CB  LEU A 153     6498  19607   6818    910    586   1873  A    C  
ATOM   1013  CG  LEU A 153      25.055 -10.116 -34.850  1.00 93.39      A    C  
ANISOU 1013  CG  LEU A 153     7264  20605   7616   1329    656   2003  A    C  
ATOM   1014  CD1 LEU A 153      24.398 -10.580 -33.543  1.00 92.65      A    C  
ANISOU 1014  CD1 LEU A 153     7329  20300   7575   1362    607   2016  A    C  
ATOM   1015  CD2 LEU A 153      25.019 -11.207 -35.938  1.00 95.65      A    C  
ANISOU 1015  CD2 LEU A 153     7686  20713   7943   1703    816   1964  A    C  
ATOM   1016  N   LEU A 154      24.153  -5.943 -36.882  1.00 87.91      A    N  
ANISOU 1016  N   LEU A 154     6701  19755   6946    112    469   1726  A    N  
ATOM   1017  CA  LEU A 154      23.397  -4.943 -37.630  1.00 85.92      A    C  
ANISOU 1017  CA  LEU A 154     6653  19244   6748   -141    445   1613  A    C  
ATOM   1018  C   LEU A 154      24.190  -4.531 -38.895  1.00 90.95      A    C  
ANISOU 1018  C   LEU A 154     7132  20135   7290   -228    490   1662  A    C  
ATOM   1019  O   LEU A 154      23.585  -4.135 -39.893  1.00 89.02      A    O  
ANISOU 1019  O   LEU A 154     7047  19678   7100   -286    522   1578  A    O  
ATOM   1020  CB  LEU A 154      23.154  -3.736 -36.714  1.00 85.74      A    C  
ANISOU 1020  CB  LEU A 154     6745  19147   6683   -498    316   1589  A    C  
ATOM   1021  CG  LEU A 154      21.792  -3.023 -36.754  1.00 88.73      A    C  
ANISOU 1021  CG  LEU A 154     7460  19088   7164   -619    288   1448  A    C  
ATOM   1022  CD1 LEU A 154      20.604  -4.004 -36.779  1.00 86.91      A    C  
ANISOU 1022  CD1 LEU A 154     7387  18543   7091   -340    354   1357  A    C  
ATOM   1023  CD2 LEU A 154      21.651  -2.101 -35.553  1.00 91.86      A    C  
ANISOU 1023  CD2 LEU A 154     7983  19432   7487   -900    174   1430  A    C  
ATOM   1024  N   GLY A 155      25.524  -4.670 -38.836  1.00 90.11      A    N  
ANISOU 1024  N   GLY A 155     6694  20517   7027   -222    494   1809  A    N  
ATOM   1025  CA  GLY A 155      26.451  -4.372 -39.924  1.00 91.26      A    C  
ANISOU 1025  CA  GLY A 155     6617  21015   7042   -296    544   1890  A    C  
ATOM   1026  C   GLY A 155      26.369  -5.357 -41.077  1.00 94.34      A    C  
ANISOU 1026  C   GLY A 155     7008  21361   7475     80    697   1852  A    C  
ATOM   1027  O   GLY A 155      26.382  -4.942 -42.237  1.00 92.75      A    O  
ANISOU 1027  O   GLY A 155     6826  21171   7245    -12    743   1827  A    O  
ATOM   1028  N   ILE A 156      26.283  -6.675 -40.763  1.00 92.00      A    N  
ANISOU 1028  N   ILE A 156     6727  20998   7233    501    778   1848  A    N  
ATOM   1029  CA  ILE A 156      26.179  -7.790 -41.731  1.00 92.21      A    C  
ANISOU 1029  CA  ILE A 156     6826  20925   7285    902    931   1795  A    C  
ATOM   1030  C   ILE A 156      24.843  -7.701 -42.490  1.00 93.99      A    C  
ANISOU 1030  C   ILE A 156     7400  20654   7657    834    947   1613  A    C  
ATOM   1031  O   ILE A 156      24.805  -7.885 -43.712  1.00 93.77      A    O  
ANISOU 1031  O   ILE A 156     7413  20613   7603    923   1037   1559  A    O  
ATOM   1032  CB  ILE A 156      26.338  -9.191 -41.039  1.00 96.27      A    C  
ANISOU 1032  CB  ILE A 156     7358  21406   7812   1345   1002   1836  A    C  
ATOM   1033  CG1 ILE A 156      27.522  -9.234 -40.040  1.00 98.99      A    C  
ANISOU 1033  CG1 ILE A 156     7348  22257   8005   1411    958   2032  A    C  
ATOM   1034  CG2 ILE A 156      26.434 -10.330 -42.079  1.00 97.89      A    C  
ANISOU 1034  CG2 ILE A 156     7671  21525   7999   1769   1173   1785  A    C  
ATOM   1035  CD1 ILE A 156      27.344 -10.191 -38.880  1.00102.91      A    C  
ANISOU 1035  CD1 ILE A 156     7929  22629   8544   1679    950   2078  A    C  
ATOM   1036  N   MET A 157      23.751  -7.429 -41.745  1.00 88.52      A    N  
ANISOU 1036  N   MET A 157     6940  19594   7098    684    861   1527  A    N  
ATOM   1037  CA  MET A 157      22.396  -7.302 -42.263  1.00 85.89      A    C  
ANISOU 1037  CA  MET A 157     6905  18839   6892    607    856   1373  A    C  
ATOM   1038  C   MET A 157      22.308  -6.198 -43.329  1.00 89.39      A    C  
ANISOU 1038  C   MET A 157     7358  19313   7294    356    835   1348  A    C  
ATOM   1039  O   MET A 157      21.906  -6.494 -44.453  1.00 88.81      A    O  
ANISOU 1039  O   MET A 157     7392  19120   7233    443    903   1265  A    O  
ATOM   1040  CB  MET A 157      21.423  -7.084 -41.101  1.00 86.38      A    C  
ANISOU 1040  CB  MET A 157     7136  18623   7062    485    764   1324  A    C  
ATOM   1041  CG  MET A 157      19.972  -7.194 -41.485  1.00 88.03      A    C  
ANISOU 1041  CG  MET A 157     7613  18446   7388    468    768   1181  A    C  
ATOM   1042  SD  MET A 157      19.321  -5.600 -42.019  1.00 91.38      A    S  
ANISOU 1042  SD  MET A 157     8132  18775   7812    150    686   1132  A    S  
ATOM   1043  CE  MET A 157      19.352  -4.685 -40.475  1.00 87.66      A    C  
ANISOU 1043  CE  MET A 157     7673  18300   7335    -64    566   1178  A    C  
ATOM   1044  N   TRP A 158      22.727  -4.955 -42.995  1.00 86.64      A    N  
ANISOU 1044  N   TRP A 158     6917  19126   6875     37    741   1423  A    N  
ATOM   1045  CA  TRP A 158      22.738  -3.806 -43.913  1.00 87.05      A    C  
ANISOU 1045  CA  TRP A 158     7008  19203   6866   -231    715   1429  A    C  
ATOM   1046  C   TRP A 158      23.534  -4.088 -45.195  1.00 92.80      A    C  
ANISOU 1046  C   TRP A 158     7565  20211   7483   -130    820   1476  A    C  
ATOM   1047  O   TRP A 158      23.105  -3.681 -46.279  1.00 91.89      A    O  
ANISOU 1047  O   TRP A 158     7566  19988   7360   -198    844   1428  A    O  
ATOM   1048  CB  TRP A 158      23.256  -2.536 -43.217  1.00 87.09      A    C  
ANISOU 1048  CB  TRP A 158     6974  19331   6783   -607    600   1514  A    C  
ATOM   1049  CG  TRP A 158      22.193  -1.784 -42.469  1.00 86.96      A    C  
ANISOU 1049  CG  TRP A 158     7243  18945   6854   -758    507   1431  A    C  
ATOM   1050  CD1 TRP A 158      21.895  -1.885 -41.139  1.00 89.29      A    C  
ANISOU 1050  CD1 TRP A 158     7594  19132   7200   -747    446   1409  A    C  
ATOM   1051  CD2 TRP A 158      21.253  -0.850 -43.023  1.00 85.91      A    C  
ANISOU 1051  CD2 TRP A 158     7380  18510   6752   -894    475   1364  A    C  
ATOM   1053  CE2 TRP A 158      20.416  -0.420 -41.967  1.00 88.65      A    C  
ANISOU 1053  CE2 TRP A 158     7934  18585   7164   -939    403   1299  A    C  
ATOM   1054  CE3 TRP A 158      21.040  -0.326 -44.310  1.00 87.26      A    C  
ANISOU 1054  CE3 TRP A 158     7639  18630   6886   -963    505   1362  A    C  
ATOM   1052  NE1 TRP A 158      20.828  -1.069 -40.829  1.00 87.41      A    N  
ANISOU 1052  NE1 TRP A 158     7640  18553   7018   -862    386   1324  A    N  
ATOM   1055  CZ2 TRP A 158      19.392   0.518 -42.159  1.00 87.07      A    C  
ANISOU 1055  CZ2 TRP A 158     8022  18073   6987  -1018    365   1236  A    C  
ATOM   1056  CZ3 TRP A 158      20.018   0.594 -44.498  1.00 87.66      A    C  
ANISOU 1056  CZ3 TRP A 158     7980  18361   6965  -1051    459   1307  A    C  
ATOM   1057  CH2 TRP A 158      19.210   1.009 -43.432  1.00 87.24      A    C  
ANISOU 1057  CH2 TRP A 158     8125  18049   6972  -1063    392   1246  A    C  
ATOM   1058  N   VAL A 159      24.665  -4.823 -45.068  1.00 91.17      A    N  
ANISOU 1058  N   VAL A 159     7082  20379   7178     67    890   1574  A    N  
ATOM   1059  CA  VAL A 159      25.535  -5.221 -46.177  1.00 92.80      A    C  
ANISOU 1059  CA  VAL A 159     7090  20917   7252    234   1012   1629  A    C  
ATOM   1060  C   VAL A 159      24.814  -6.254 -47.067  1.00 98.13      A    C  
ANISOU 1060  C   VAL A 159     7972  21316   7995    557   1124   1486  A    C  
ATOM   1061  O   VAL A 159      24.712  -6.021 -48.275  1.00 97.78      A    O  
ANISOU 1061  O   VAL A 159     7971  21283   7896    522   1178   1448  A    O  
ATOM   1062  CB  VAL A 159      26.949  -5.654 -45.688  1.00 98.39      A    C  
ANISOU 1062  CB  VAL A 159     7424  22148   7811    385   1053   1789  A    C  
ATOM   1063  CG1 VAL A 159      27.674  -6.534 -46.704  1.00100.27      A    C  
ANISOU 1063  CG1 VAL A 159     7498  22672   7927    746   1220   1817  A    C  
ATOM   1064  CG2 VAL A 159      27.791  -4.433 -45.349  1.00 99.35      A    C  
ANISOU 1064  CG2 VAL A 159     7310  22642   7795    -44    951   1935  A    C  
ATOM   1065  N   LEU A 160      24.249  -7.339 -46.469  1.00 95.36      A    N  
ANISOU 1065  N   LEU A 160     7783  20697   7754    827   1151   1405  A    N  
ATOM   1066  CA  LEU A 160      23.484  -8.365 -47.204  1.00 94.95      A    C  
ANISOU 1066  CA  LEU A 160     7985  20336   7756   1080   1244   1256  A    C  
ATOM   1067  C   LEU A 160      22.323  -7.737 -47.954  1.00 96.59      A    C  
ANISOU 1067  C   LEU A 160     8409  20260   8030    853   1192   1138  A    C  
ATOM   1068  O   LEU A 160      22.088  -8.100 -49.111  1.00 96.89      A    O  
ANISOU 1068  O   LEU A 160     8548  20248   8019    951   1271   1052  A    O  
ATOM   1069  CB  LEU A 160      22.962  -9.476 -46.284  1.00 94.81      A    C  
ANISOU 1069  CB  LEU A 160     8149  20031   7844   1299   1253   1202  A    C  
ATOM   1070  CG  LEU A 160      23.991 -10.502 -45.814  1.00102.90      A    C  
ANISOU 1070  CG  LEU A 160     9047  21262   8788   1672   1347   1297  A    C  
ATOM   1071  CD1 LEU A 160      23.546 -11.161 -44.511  1.00102.49      A    C  
ANISOU 1071  CD1 LEU A 160     9124  20976   8839   1751   1300   1307  A    C  
ATOM   1072  CD2 LEU A 160      24.284 -11.542 -46.894  1.00107.30      A    C  
ANISOU 1072  CD2 LEU A 160     9729  21784   9256   2036   1512   1224  A    C  
ATOM   1073  N   SER A 161      21.631  -6.761 -47.307  1.00 90.67      A    N  
ANISOU 1073  N   SER A 161     7732  19350   7369    566   1063   1140  A    N  
ATOM   1074  CA  SER A 161      20.518  -6.001 -47.886  1.00 88.58      A    C  
ANISOU 1074  CA  SER A 161     7654  18850   7152    367   1000   1059  A    C  
ATOM   1075  C   SER A 161      20.963  -5.269 -49.163  1.00 92.83      A    C  
ANISOU 1075  C   SER A 161     8121  19584   7568    247   1030   1102  A    C  
ATOM   1076  O   SER A 161      20.260  -5.320 -50.170  1.00 92.16      A    O  
ANISOU 1076  O   SER A 161     8174  19371   7473    257   1050   1015  A    O  
ATOM   1077  CB  SER A 161      19.963  -5.004 -46.873  1.00 90.80      A    C  
ANISOU 1077  CB  SER A 161     8005  18985   7510    132    873   1083  A    C  
ATOM   1078  OG  SER A 161      19.110  -5.631 -45.928  1.00 99.45      A    O  
ANISOU 1078  OG  SER A 161     9221  19843   8723    225    847   1016  A    O  
ATOM   1079  N   ALA A 162      22.161  -4.651 -49.137  1.00 89.79      A    N  
ANISOU 1079  N   ALA A 162     7508  19541   7068    124   1033   1242  A    N  
ATOM   1080  CA  ALA A 162      22.722  -3.948 -50.282  1.00 90.12      A    C  
ANISOU 1080  CA  ALA A 162     7457  19815   6969    -20   1067   1312  A    C  
ATOM   1081  C   ALA A 162      23.173  -4.914 -51.382  1.00 96.24      A    C  
ANISOU 1081  C   ALA A 162     8154  20770   7643    258   1214   1273  A    C  
ATOM   1082  O   ALA A 162      23.145  -4.541 -52.554  1.00 96.77      A    O  
ANISOU 1082  O   ALA A 162     8242  20909   7615    190   1252   1271  A    O  
ATOM   1083  CB  ALA A 162      23.871  -3.062 -49.843  1.00 92.15      A    C  
ANISOU 1083  CB  ALA A 162     7486  20413   7114   -276   1025   1480  A    C  
ATOM   1084  N   LEU A 163      23.562  -6.156 -51.019  1.00 93.77      A    N  
ANISOU 1084  N   LEU A 163     7783  20510   7336    588   1301   1241  A    N  
ATOM   1085  CA  LEU A 163      24.011  -7.171 -51.987  1.00 95.47      A    C  
ANISOU 1085  CA  LEU A 163     7973  20863   7438    913   1458   1190  A    C  
ATOM   1086  C   LEU A 163      22.844  -7.700 -52.830  1.00 98.74      A    C  
ANISOU 1086  C   LEU A 163     8700  20920   7898    990   1482   1004  A    C  
ATOM   1087  O   LEU A 163      22.988  -7.871 -54.043  1.00100.17      A    O  
ANISOU 1087  O   LEU A 163     8903  21205   7954   1079   1574    956  A    O  
ATOM   1088  CB  LEU A 163      24.737  -8.333 -51.275  1.00 96.96      A    C  
ANISOU 1088  CB  LEU A 163     8061  21172   7607   1275   1545   1220  A    C  
ATOM   1089  CG  LEU A 163      25.479  -9.335 -52.165  1.00103.98      A    C  
ANISOU 1089  CG  LEU A 163     8904  22268   8338   1673   1728   1196  A    C  
ATOM   1090  CD1 LEU A 163      26.931  -8.937 -52.338  1.00107.30      A    C  
ANISOU 1090  CD1 LEU A 163     8915  23287   8567   1700   1793   1382  A    C  
ATOM   1091  CD2 LEU A 163      25.400 -10.734 -51.590  1.00106.25      A    C  
ANISOU 1091  CD2 LEU A 163     9355  22349   8665   2071   1804   1133  A    C  
ATOM   1092  N   VAL A 164      21.699  -7.951 -52.180  1.00 92.82      A    N  
ANISOU 1092  N   VAL A 164     8176  19786   7306    939   1398    904  A    N  
ATOM   1093  CA  VAL A 164      20.477  -8.467 -52.796  1.00 91.80      A    C  
ANISOU 1093  CA  VAL A 164     8328  19336   7215    957   1396    733  A    C  
ATOM   1094  C   VAL A 164      19.809  -7.400 -53.685  1.00 94.74      A    C  
ANISOU 1094  C   VAL A 164     8743  19695   7560    700   1322    726  A    C  
ATOM   1095  O   VAL A 164      19.455  -7.691 -54.832  1.00 94.54      A    O  
ANISOU 1095  O   VAL A 164     8827  19652   7443    740   1369    632  A    O  
ATOM   1096  CB  VAL A 164      19.529  -9.032 -51.691  1.00 94.47      A    C  
ANISOU 1096  CB  VAL A 164     8845  19336   7712    964   1331    659  A    C  
ATOM   1097  CG1 VAL A 164      18.081  -9.162 -52.169  1.00 93.22      A    C  
ANISOU 1097  CG1 VAL A 164     8930  18897   7593    857   1283    510  A    C  
ATOM   1098  CG2 VAL A 164      20.048 -10.364 -51.150  1.00 95.74      A    C  
ANISOU 1098  CG2 VAL A 164     9052  19457   7869   1272   1430    647  A    C  
ATOM   1099  N   SER A 165      19.659  -6.170 -53.148  1.00 89.98      A    N  
ANISOU 1099  N   SER A 165     8078  19096   7015    451   1208    828  A    N  
ATOM   1100  CA  SER A 165      19.009  -5.022 -53.792  1.00 88.59      A    C  
ANISOU 1100  CA  SER A 165     7972  18873   6814    226   1127    853  A    C  
ATOM   1101  C   SER A 165      19.754  -4.408 -54.990  1.00 93.28      A    C  
ANISOU 1101  C   SER A 165     8464  19735   7241    148   1181    937  A    C  
ATOM   1102  O   SER A 165      19.092  -3.975 -55.937  1.00 92.48      A    O  
ANISOU 1102  O   SER A 165     8474  19583   7082     76   1158    908  A    O  
ATOM   1103  CB  SER A 165      18.725  -3.935 -52.762  1.00 89.96      A    C  
ANISOU 1103  CB  SER A 165     8161  18938   7080     21   1006    937  A    C  
ATOM   1104  OG  SER A 165      18.141  -4.480 -51.591  1.00 92.00      A    O  
ANISOU 1104  OG  SER A 165     8484  18994   7476     92    966    876  A    O  
ATOM   1105  N   TYR A 166      21.112  -4.327 -54.935  1.00 91.14      A    N  
ANISOU 1105  N   TYR A 166     7968  19784   6875    151   1248   1056  A    N  
ATOM   1106  CA  TYR A 166      21.922  -3.723 -56.007  1.00 92.33      A    C  
ANISOU 1106  CA  TYR A 166     7989  20246   6847     48   1308   1160  A    C  
ATOM   1107  C   TYR A 166      22.382  -4.720 -57.089  1.00 98.13      A    C  
ANISOU 1107  C   TYR A 166     8668  21176   7440    313   1461   1088  A    C  
ATOM   1108  O   TYR A 166      23.197  -4.362 -57.942  1.00 99.05      A    O  
ANISOU 1108  O   TYR A 166     8631  21618   7385    268   1537   1181  A    O  
ATOM   1109  CB  TYR A 166      23.107  -2.927 -55.438  1.00 94.55      A    C  
ANISOU 1109  CB  TYR A 166     8037  20825   7062   -161   1290   1347  A    C  
ATOM   1110  CG  TYR A 166      22.695  -1.671 -54.700  1.00 95.42      A    C  
ANISOU 1110  CG  TYR A 166     8267  20741   7246   -484   1146   1422  A    C  
ATOM   1111  CD1 TYR A 166      22.253  -0.544 -55.390  1.00 97.89      A    C  
ANISOU 1111  CD1 TYR A 166     8734  20963   7497   -723   1092   1485  A    C  
ATOM   1112  CD2 TYR A 166      22.767  -1.600 -53.310  1.00 94.80      A    C  
ANISOU 1112  CD2 TYR A 166     8175  20565   7280   -538   1070   1437  A    C  
ATOM   1113  CE1 TYR A 166      21.863   0.613 -54.712  1.00 98.60      A    C  
ANISOU 1113  CE1 TYR A 166     8997  20831   7635   -985    972   1549  A    C  
ATOM   1114  CE2 TYR A 166      22.383  -0.449 -52.623  1.00 94.70      A    C  
ANISOU 1114  CE2 TYR A 166     8316  20352   7313   -818    947   1489  A    C  
ATOM   1115  CZ  TYR A 166      21.936   0.657 -53.327  1.00102.00      A    C  
ANISOU 1115  CZ  TYR A 166     9426  21156   8173  -1033    902   1542  A    C  
ATOM   1116  OH  TYR A 166      21.559   1.792 -52.650  1.00101.33      A    O  
ANISOU 1116  OH  TYR A 166     9551  20834   8114  -1275    793   1589  A    O  
ATOM   1117  N   LEU A 167      21.804  -5.938 -57.094  1.00 95.42      A    N  
ANISOU 1117  N   LEU A 167     8483  20622   7152    572   1509    918  A    N  
ATOM   1118  CA  LEU A 167      22.065  -6.988 -58.082  1.00 97.62      A    C  
ANISOU 1118  CA  LEU A 167     8809  20989   7292    850   1656    805  A    C  
ATOM   1119  C   LEU A 167      21.744  -6.555 -59.538  1.00103.68      A    C  
ANISOU 1119  C   LEU A 167     9648  21835   7909    755   1676    774  A    C  
ATOM   1120  O   LEU A 167      22.585  -6.827 -60.399  1.00105.83      A    O  
ANISOU 1120  O   LEU A 167     9809  22403   7997    897   1810    792  A    O  
ATOM   1121  CB  LEU A 167      21.347  -8.294 -57.698  1.00 97.27      A    C  
ANISOU 1121  CB  LEU A 167     9008  20612   7339   1073   1678    623  A    C  
ATOM   1122  CG  LEU A 167      22.183  -9.586 -57.666  1.00104.60      A    C  
ANISOU 1122  CG  LEU A 167     9944  21622   8176   1461   1843    567  A    C  
ATOM   1123  CD1 LEU A 167      23.564  -9.372 -57.051  1.00106.32      A    C  
ANISOU 1123  CD1 LEU A 167     9828  22230   8340   1578   1906    752  A    C  
ATOM   1124  CD2 LEU A 167      21.470 -10.664 -56.880  1.00106.86      A    C  
ANISOU 1124  CD2 LEU A 167    10489  21523   8589   1601   1831    436  A    C  
ATOM   1125  N   PRO A 168      20.624  -5.833 -59.862  1.00 99.34      A    N  
ANISOU 1125  N   PRO A 168     9256  21083   7406    534   1555    748  A    N  
ATOM   1126  CA  PRO A 168      20.423  -5.394 -61.256  1.00100.05      A    C  
ANISOU 1126  CA  PRO A 168     9392  21298   7326    456   1576    745  A    C  
ATOM   1127  C   PRO A 168      21.481  -4.383 -61.714  1.00106.52      A    C  
ANISOU 1127  C   PRO A 168     9996  22473   8003    307   1618    945  A    C  
ATOM   1128  O   PRO A 168      21.822  -4.365 -62.898  1.00108.51      A    O  
ANISOU 1128  O   PRO A 168    10216  22950   8062    343   1707    950  A    O  
ATOM   1129  CB  PRO A 168      19.027  -4.766 -61.236  1.00 99.68      A    C  
ANISOU 1129  CB  PRO A 168     9522  20982   7369    272   1421    717  A    C  
ATOM   1130  CG  PRO A 168      18.381  -5.289 -60.020  1.00102.63      A    C  
ANISOU 1130  CG  PRO A 168     9980  21076   7940    315   1353    635  A    C  
ATOM   1131  CD  PRO A 168      19.486  -5.398 -59.025  1.00 98.53      A    C  
ANISOU 1131  CD  PRO A 168     9288  20665   7485    379   1402    727  A    C  
ATOM   1132  N   LEU A 169      22.021  -3.565 -60.775  1.00102.65      A    N  
ANISOU 1132  N   LEU A 169     9365  22048   7590    121   1556   1108  A    N  
ATOM   1133  CA  LEU A 169      23.081  -2.580 -61.038  1.00104.28      A    C  
ANISOU 1133  CA  LEU A 169     9365  22597   7658    -96   1583   1315  A    C  
ATOM   1134  C   LEU A 169      24.417  -3.279 -61.383  1.00111.76      A    C  
ANISOU 1134  C   LEU A 169    10037  23985   8440    107   1753   1354  A    C  
ATOM   1135  O   LEU A 169      25.253  -2.688 -62.067  1.00113.36      A    O  
ANISOU 1135  O   LEU A 169    10057  24556   8458    -33   1816   1503  A    O  
ATOM   1136  CB  LEU A 169      23.233  -1.605 -59.837  1.00103.11      A    C  
ANISOU 1136  CB  LEU A 169     9186  22362   7629   -369   1461   1450  A    C  
ATOM   1137  CG  LEU A 169      24.288  -0.482 -59.924  1.00109.27      A    C  
ANISOU 1137  CG  LEU A 169     9795  23452   8270   -698   1458   1674  A    C  
ATOM   1138  CD1 LEU A 169      23.909   0.577 -60.946  1.00110.11      A    C  
ANISOU 1138  CD1 LEU A 169    10067  23506   8262   -935   1421   1764  A    C  
ATOM   1139  CD2 LEU A 169      24.485   0.174 -58.592  1.00110.27      A    C  
ANISOU 1139  CD2 LEU A 169     9913  23476   8509   -926   1346   1758  A    C  
ATOM   1140  N   MET A 170      24.589  -4.546 -60.944  1.00109.54      A    N  
ANISOU 1140  N   MET A 170     9741  23672   8207    451   1835   1228  A    N  
ATOM   1141  CA  MET A 170      25.774  -5.369 -61.201  1.00112.72      A    C  
ANISOU 1141  CA  MET A 170     9913  24467   8450    754   2011   1249  A    C  
ATOM   1142  C   MET A 170      25.723  -6.059 -62.577  1.00119.59      A    C  
ANISOU 1142  C   MET A 170    10884  25425   9131    996   2155   1122  A    C  
ATOM   1143  O   MET A 170      26.707  -6.684 -62.986  1.00122.57      A    O  
ANISOU 1143  O   MET A 170    11081  26160   9330   1278   2325   1140  A    O  
ATOM   1144  CB  MET A 170      26.000  -6.403 -60.077  1.00115.02      A    C  
ANISOU 1144  CB  MET A 170    10186  24657   8860   1050   2039   1186  A    C  
ATOM   1145  CG  MET A 170      26.129  -5.799 -58.687  1.00117.78      A    C  
ANISOU 1145  CG  MET A 170    10413  24973   9365    836   1908   1310  A    C  
ATOM   1146  SD  MET A 170      27.384  -4.504 -58.538  1.00124.64      A    S  
ANISOU 1146  SD  MET A 170    10877  26398  10085    500   1892   1589  A    S  
ATOM   1147  CE  MET A 170      26.575  -3.432 -57.374  1.00118.72      A    C  
ANISOU 1147  CE  MET A 170    10348  25275   9483     -2   1682   1632  A    C  
ATOM   1148  N   GLY A 171      24.590  -5.929 -63.273  1.00114.49      A    N  
ANISOU 1148  N   GLY A 171    10516  24482   8503    895   2089    998  A    N  
ATOM   1149  CA  GLY A 171      24.391  -6.496 -64.602  1.00115.59      A    C  
ANISOU 1149  CA  GLY A 171    10794  24671   8452   1066   2199    861  A    C  
ATOM   1150  C   GLY A 171      23.216  -7.443 -64.747  1.00117.95      A    C  
ANISOU 1150  C   GLY A 171    11452  24540   8823   1182   2161    612  A    C  
ATOM   1151  O   GLY A 171      23.080  -8.079 -65.795  1.00119.41      A    O  
ANISOU 1151  O   GLY A 171    11792  24743   8836   1306   2243    473  A    O  
ATOM   1152  N   TRP A 172      22.354  -7.553 -63.712  1.00111.39      A    N  
ANISOU 1152  N   TRP A 172    10758  23339   8227   1119   2034    553  A    N  
ATOM   1153  CA  TRP A 172      21.187  -8.434 -63.773  1.00109.67      A    C  
ANISOU 1153  CA  TRP A 172    10865  22730   8073   1168   1984    331  A    C  
ATOM   1154  C   TRP A 172      19.924  -7.656 -64.183  1.00111.47      A    C  
ANISOU 1154  C   TRP A 172    11209  22805   8338    869   1821    323  A    C  
ATOM   1155  O   TRP A 172      18.944  -7.580 -63.439  1.00108.77      A    O  
ANISOU 1155  O   TRP A 172    10972  22185   8172    745   1687    288  A    O  
ATOM   1156  CB  TRP A 172      21.009  -9.261 -62.478  1.00106.97      A    C  
ANISOU 1156  CB  TRP A 172    10618  22101   7925   1295   1960    265  A    C  
ATOM   1157  CG  TRP A 172      20.073 -10.441 -62.596  1.00107.96      A    C  
ANISOU 1157  CG  TRP A 172    11093  21868   8059   1390   1964     27  A    C  
ATOM   1158  CD1 TRP A 172      19.442 -10.887 -63.722  1.00111.91      A    C  
ANISOU 1158  CD1 TRP A 172    11825  22292   8405   1369   1982   -144  A    C  
ATOM   1159  CD2 TRP A 172      19.669 -11.320 -61.537  1.00107.15      A    C  
ANISOU 1159  CD2 TRP A 172    11162  21440   8109   1481   1943    -58  A    C  
ATOM   1161  CE2 TRP A 172      18.781 -12.269 -62.094  1.00111.93      A    C  
ANISOU 1161  CE2 TRP A 172    12117  21771   8642   1481   1949   -283  A    C  
ATOM   1162  CE3 TRP A 172      19.971 -11.401 -60.165  1.00107.23      A    C  
ANISOU 1162  CE3 TRP A 172    11074  21373   8295   1542   1917     37  A    C  
ATOM   1160  NE1 TRP A 172      18.655 -11.975 -63.426  1.00111.39      A    N  
ANISOU 1160  NE1 TRP A 172    12072  21868   8382   1409   1968   -337  A    N  
ATOM   1163  CZ2 TRP A 172      18.183 -13.278 -61.325  1.00111.23      A    C  
ANISOU 1163  CZ2 TRP A 172    12292  21316   8653   1519   1933   -405  A    C  
ATOM   1164  CZ3 TRP A 172      19.375 -12.397 -59.404  1.00108.35      A    C  
ANISOU 1164  CZ3 TRP A 172    11466  21159   8542   1613   1903    -80  A    C  
ATOM   1165  CH2 TRP A 172      18.493 -13.321 -59.982  1.00109.95      A    C  
ANISOU 1165  CH2 TRP A 172    12027  21077   8672   1593   1914   -294  A    C  
ATOM   1166  N   THR A 173      19.970  -7.085 -65.395  1.00109.42      A    N  
ANISOU 1166  N   THR A 173    10920  22762   7892    779   1841    367  A    N  
ATOM   1167  CA  THR A 173      18.870  -6.348 -66.025  1.00108.42      A    C  
ANISOU 1167  CA  THR A 173    10894  22562   7737    551   1706    378  A    C  
ATOM   1168  C   THR A 173      18.258  -7.220 -67.125  1.00114.54      A    C  
ANISOU 1168  C   THR A 173    11887  23296   8338    630   1742    165  A    C  
ATOM   1169  O   THR A 173      18.876  -8.206 -67.531  1.00115.66      A    O  
ANISOU 1169  O   THR A 173    12099  23495   8352    856   1892     34  A    O  
ATOM   1170  CB  THR A 173      19.350  -4.996 -66.566  1.00114.69      A    C  
ANISOU 1170  CB  THR A 173    11529  23621   8429    370   1693    603  A    C  
ATOM   1172  CG2 THR A 173      19.618  -3.984 -65.462  1.00111.44      A    C  
ANISOU 1172  CG2 THR A 173    10988  23168   8187    196   1608    799  A    C  
ATOM   1171  OG1 THR A 173      20.520  -5.196 -67.359  1.00115.97      A    O  
ANISOU 1171  OG1 THR A 173    11558  24127   8380    495   1863    637  A    O  
ATOM   1173  N   CYS A 174      17.052  -6.873 -67.602  1.00112.27      A    N  
ANISOU 1173  N   CYS A 174    11714  22921   8023    457   1607    128  A    N  
ATOM   1174  CA  CYS A 174      16.387  -7.659 -68.640  1.00114.91      A    C  
ANISOU 1174  CA  CYS A 174    12255  23238   8168    474   1617    -78  A    C  
ATOM   1175  C   CYS A 174      16.878  -7.332 -70.069  1.00122.78      A    C  
ANISOU 1175  C   CYS A 174    13221  24547   8883    498   1708    -49  A    C  
ATOM   1176  O   CYS A 174      16.145  -6.730 -70.856  1.00122.49      A    O  
ANISOU 1176  O   CYS A 174    13213  24605   8722    350   1614    -17  A    O  
ATOM   1177  CB  CYS A 174      14.867  -7.572 -68.520  1.00114.24      A    C  
ANISOU 1177  CB  CYS A 174    12276  22988   8140    284   1433   -138  A    C  
ATOM   1178  SG  CYS A 174      14.190  -5.892 -68.576  1.00116.87      A    S  
ANISOU 1178  SG  CYS A 174    12463  23429   8514     93   1269    116  A    S  
ATOM   1179  N   CYS A 175      18.115  -7.754 -70.409  1.00123.13      A    N  
ANISOU 1179  N   CYS A 175    13196  24780   8807    706   1897    -53  A    N  
ATOM   1180  CA  CYS A 175      18.655  -7.527 -71.758  1.00126.80      A    C  
ANISOU 1180  CA  CYS A 175    13621  25574   8983    752   2009    -29  A    C  
ATOM   1181  C   CYS A 175      17.972  -8.536 -72.745  1.00132.77      A    C  
ANISOU 1181  C   CYS A 175    14667  26259   9520    816   2040   -304  A    C  
ATOM   1182  O   CYS A 175      17.010  -8.112 -73.397  1.00132.12      A    O  
ANISOU 1182  O   CYS A 175    14654  26214   9332    627   1919   -315  A    O  
ATOM   1183  CB  CYS A 175      20.185  -7.595 -71.788  1.00129.22      A    C  
ANISOU 1183  CB  CYS A 175    13717  26170   9209    955   2204     76  A    C  
ATOM   1184  SG  CYS A 175      21.002  -6.685 -70.447  1.00131.35      A    S  
ANISOU 1184  SG  CYS A 175    13672  26517   9717    839   2160    363  A    S  
ATOM   1185  N   PRO A 176      18.302  -9.864 -72.787  1.00130.90      A    N  
ANISOU 1185  N   PRO A 176    14637  25886   9214   1059   2177   -531  A    N  
ATOM   1186  CA  PRO A 176      17.512 -10.778 -73.632  1.00132.25      A    C  
ANISOU 1186  CA  PRO A 176    15143  25934   9171   1049   2180   -805  A    C  
ATOM   1187  C   PRO A 176      16.312 -11.379 -72.867  1.00133.64      A    C  
ANISOU 1187  C   PRO A 176    15547  25725   9504    878   2026   -963  A    C  
ATOM   1188  O   PRO A 176      15.314 -11.748 -73.491  1.00134.40      A    O  
ANISOU 1188  O   PRO A 176    15885  25743   9436    730   1957  -1154  A    O  
ATOM   1189  CB  PRO A 176      18.525 -11.857 -74.026  1.00137.07      A    C  
ANISOU 1189  CB  PRO A 176    15900  26578   9603   1417   2424   -957  A    C  
ATOM   1190  CG  PRO A 176      19.635 -11.772 -72.997  1.00140.84      A    C  
ANISOU 1190  CG  PRO A 176    16136  27095  10281   1627   2516   -788  A    C  
ATOM   1191  CD  PRO A 176      19.367 -10.610 -72.079  1.00133.17      A    C  
ANISOU 1191  CD  PRO A 176    14896  26116   9585   1358   2334   -549  A    C  
ATOM   1192  N   ARG A 177      16.420 -11.474 -71.514  1.00126.83      A    N  
ANISOU 1192  N   ARG A 177    14599  24652   8939    878   1971   -878  A    N  
ATOM   1193  CA  ARG A 177      15.420 -12.017 -70.585  1.00124.74      A    C  
ANISOU 1193  CA  ARG A 177    14502  24044   8850    723   1839   -987  A    C  
ATOM   1194  C   ARG A 177      14.145 -11.155 -70.531  1.00125.33      A    C  
ANISOU 1194  C   ARG A 177    14456  24161   9003    402   1613   -891  A    C  
ATOM   1195  O   ARG A 177      14.257  -9.936 -70.663  1.00123.88      A    O  
ANISOU 1195  O   ARG A 177    14019  24195   8854    346   1557   -671  A    O  
ATOM   1196  CB  ARG A 177      16.022 -12.164 -69.181  1.00123.54      A    C  
ANISOU 1196  CB  ARG A 177    14279  23700   8961    877   1884   -910  A    C  
ATOM   1197  CG  ARG A 177      16.939 -13.368 -69.026  1.00137.05      A    C  
ANISOU 1197  CG  ARG A 177    16220  25259  10595   1205   2083  -1062  A    C  
ATOM   1198  CD  ARG A 177      17.306 -13.583 -67.568  1.00145.96      A    C  
ANISOU 1198  CD  ARG A 177    17259  26229  11971   1362   2113   -961  A    C  
ATOM   1199  NE  ARG A 177      18.745 -13.449 -67.327  1.00153.01      A    N  
ANISOU 1199  NE  ARG A 177    17891  27401  12844   1652   2266   -801  A    N  
ATOM   1200  CZ  ARG A 177      19.362 -12.302 -67.056  1.00163.74      A    C  
ANISOU 1200  CZ  ARG A 177    18871  29034  14308   1569   2219   -553  A    C  
ATOM   1201  NH1 ARG A 177      18.675 -11.167 -67.002  1.00149.28      A    N1+
ANISOU 1201  NH1 ARG A 177    16910  27195  12616   1249   2034   -439  A    N1+
ATOM   1202  NH2 ARG A 177      20.670 -12.280 -66.845  1.00150.18      A    N  
ANISOU 1202  NH2 ARG A 177    16910  27612  12538   1804   2360   -413  A    N  
ATOM   1203  N   PRO A 178      12.934 -11.746 -70.336  1.00120.72      A    N  
ANISOU 1203  N   PRO A 178    14051  23386   8429    192   1484  -1040  A    N  
ATOM   1204  CA  PRO A 178      11.705 -10.925 -70.323  1.00118.85      A    C  
ANISOU 1204  CA  PRO A 178    13663  23261   8234    -68   1275   -934  A    C  
ATOM   1205  C   PRO A 178      11.619  -9.895 -69.198  1.00118.89      A    C  
ANISOU 1205  C   PRO A 178    13412  23241   8519    -76   1189   -700  A    C  
ATOM   1206  O   PRO A 178      11.890 -10.220 -68.040  1.00117.04      A    O  
ANISOU 1206  O   PRO A 178    13184  22787   8497    -10   1218   -696  A    O  
ATOM   1207  CB  PRO A 178      10.578 -11.962 -70.247  1.00121.73      A    C  
ANISOU 1207  CB  PRO A 178    14268  23453   8530   -288   1182  -1155  A    C  
ATOM   1208  CG  PRO A 178      11.207 -13.172 -69.671  1.00127.04      A    C  
ANISOU 1208  CG  PRO A 178    15208  23802   9258   -146   1322  -1321  A    C  
ATOM   1209  CD  PRO A 178      12.614 -13.182 -70.185  1.00123.73      A    C  
ANISOU 1209  CD  PRO A 178    14793  23469   8751    170   1523  -1304  A    C  
ATOM   1210  N   CYS A 179      11.243  -8.650 -69.558  1.00114.20      A    N  
ANISOU 1210  N   CYS A 179    12622  22862   7907   -150   1086   -504  A    N  
ATOM   1211  CA  CYS A 179      11.105  -7.509 -68.644  1.00111.66      A    C  
ANISOU 1211  CA  CYS A 179    12101  22517   7806   -158   1002   -278  A    C  
ATOM   1212  C   CYS A 179       9.808  -7.531 -67.836  1.00111.48      A    C  
ANISOU 1212  C   CYS A 179    12060  22390   7908   -293    847   -293  A    C  
ATOM   1213  O   CYS A 179       8.795  -8.040 -68.320  1.00112.15      A    O  
ANISOU 1213  O   CYS A 179    12218  22544   7851   -439    760   -418  A    O  
ATOM   1214  CB  CYS A 179      11.262  -6.194 -69.400  1.00112.82      A    C  
ANISOU 1214  CB  CYS A 179    12114  22896   7855   -163    968    -62  A    C  
ATOM   1215  SG  CYS A 179      12.894  -5.959 -70.147  1.00118.67      A    S  
ANISOU 1215  SG  CYS A 179    12817  23816   8456    -35   1155     10  A    S  
ATOM   1216  N   SER A 180       9.832  -6.948 -66.619  1.00103.68      A    N  
ANISOU 1216  N   SER A 180    10964  21270   7160   -257    813   -162  A    N  
ATOM   1217  CA  SER A 180       8.646  -6.884 -65.762  1.00101.57      A    C  
ANISOU 1217  CA  SER A 180    10647  20935   7009   -356    681   -153  A    C  
ATOM   1218  C   SER A 180       7.631  -5.828 -66.240  1.00103.88      A    C  
ANISOU 1218  C   SER A 180    10818  21446   7206   -402    539    -10  A    C  
ATOM   1219  O   SER A 180       7.971  -4.949 -67.038  1.00103.16      A    O  
ANISOU 1219  O   SER A 180    10689  21501   7005   -346    544    124  A    O  
ATOM   1220  CB  SER A 180       9.027  -6.681 -64.296  1.00102.21      A    C  
ANISOU 1220  CB  SER A 180    10672  20807   7355   -283    702    -73  A    C  
ATOM   1221  OG  SER A 180       9.661  -5.436 -64.059  1.00107.46      A    O  
ANISOU 1221  OG  SER A 180    11236  21499   8097   -197    715    130  A    O  
ATOM   1222  N   GLU A 181       6.382  -5.939 -65.756  1.00 99.64      A    N  
ANISOU 1222  N   GLU A 181    10217  20951   6691   -496    418    -27  A    N  
ATOM   1223  CA  GLU A 181       5.277  -5.047 -66.098  1.00 99.71      A    C  
ANISOU 1223  CA  GLU A 181    10088  21201   6594   -497    280    110  A    C  
ATOM   1224  C   GLU A 181       5.336  -3.707 -65.362  1.00 99.95      A    C  
ANISOU 1224  C   GLU A 181    10038  21165   6773   -333    256    336  A    C  
ATOM   1225  O   GLU A 181       5.170  -2.655 -65.988  1.00 99.69      A    O  
ANISOU 1225  O   GLU A 181     9971  21274   6631   -242    208    503  A    O  
ATOM   1226  CB  GLU A 181       3.936  -5.742 -65.795  1.00102.21      A    C  
ANISOU 1226  CB  GLU A 181    10337  21642   6857   -664    168      9  A    C  
ATOM   1227  CG  GLU A 181       3.436  -6.641 -66.908  1.00117.08      A    C  
ANISOU 1227  CG  GLU A 181    12284  23723   8478   -865    125   -160  A    C  
ATOM   1228  CD  GLU A 181       2.738  -5.886 -68.017  1.00145.55      A    C  
ANISOU 1228  CD  GLU A 181    15756  27702  11844   -857      8    -43  A    C  
ATOM   1229  OE1 GLU A 181       1.495  -5.761 -67.950  1.00146.23      A    O  
ANISOU 1229  OE1 GLU A 181    15685  28050  11828   -962   -125    -22  A    O  
ATOM   1230  OE2 GLU A 181       3.431  -5.408 -68.944  1.00145.14      A    O1-
ANISOU 1230  OE2 GLU A 181    15744  27711  11693   -743     51     41  A    O1-
ATOM   1231  N   LEU A 182       5.557  -3.758 -64.029  1.00 93.51      A    N  
ANISOU 1231  N   LEU A 182     9221  20120   6189   -296    290    340  A    N  
ATOM   1232  CA  LEU A 182       5.557  -2.609 -63.120  1.00 91.45      A    C  
ANISOU 1232  CA  LEU A 182     8925  19748   6072   -160    269    519  A    C  
ATOM   1233  C   LEU A 182       6.888  -1.853 -62.974  1.00 91.74      A    C  
ANISOU 1233  C   LEU A 182     9044  19622   6193    -94    357    632  A    C  
ATOM   1234  O   LEU A 182       6.858  -0.640 -62.743  1.00 91.09      A    O  
ANISOU 1234  O   LEU A 182     8989  19492   6126     -1    326    807  A    O  
ATOM   1235  CB  LEU A 182       5.066  -3.037 -61.714  1.00 90.48      A    C  
ANISOU 1235  CB  LEU A 182     8756  19490   6133   -174    253    465  A    C  
ATOM   1236  CG  LEU A 182       3.699  -3.732 -61.598  1.00 96.37      A    C  
ANISOU 1236  CG  LEU A 182     9390  20419   6807   -272    159    387  A    C  
ATOM   1237  CD1 LEU A 182       3.652  -4.628 -60.372  1.00 95.22      A    C  
ANISOU 1237  CD1 LEU A 182     9250  20100   6829   -356    188    282  A    C  
ATOM   1238  CD2 LEU A 182       2.561  -2.723 -61.553  1.00100.11      A    C  
ANISOU 1238  CD2 LEU A 182     9733  21101   7202   -134     56    551  A    C  
ATOM   1239  N   PHE A 183       8.037  -2.553 -63.039  1.00 85.88      A    N  
ANISOU 1239  N   PHE A 183     8345  18796   5489   -139    468    540  A    N  
ATOM   1240  CA  PHE A 183       9.333  -1.912 -62.811  1.00 84.56      A    C  
ANISOU 1240  CA  PHE A 183     8207  18533   5388   -114    551    652  A    C  
ATOM   1241  C   PHE A 183      10.251  -1.883 -64.035  1.00 90.47      A    C  
ANISOU 1241  C   PHE A 183     8974  19430   5970   -137    632    670  A    C  
ATOM   1242  O   PHE A 183      10.638  -2.945 -64.530  1.00 90.73      A    O  
ANISOU 1242  O   PHE A 183     9017  19524   5932   -145    705    517  A    O  
ATOM   1243  CB  PHE A 183      10.051  -2.545 -61.607  1.00 84.54      A    C  
ANISOU 1243  CB  PHE A 183     8191  18351   5578   -110    619    585  A    C  
ATOM   1244  CG  PHE A 183       9.262  -2.527 -60.318  1.00 84.16      A    C  
ANISOU 1244  CG  PHE A 183     8125  18161   5690    -92    551    580  A    C  
ATOM   1245  CD1 PHE A 183       9.293  -1.417 -59.479  1.00 86.38      A    C  
ANISOU 1245  CD1 PHE A 183     8425  18329   6066    -58    515    722  A    C  
ATOM   1246  CD2 PHE A 183       8.507  -3.625 -59.932  1.00 85.54      A    C  
ANISOU 1246  CD2 PHE A 183     8286  18312   5904   -124    528    432  A    C  
ATOM   1247  CE1 PHE A 183       8.565  -1.398 -58.290  1.00 86.05      A    C  
ANISOU 1247  CE1 PHE A 183     8368  18175   6151    -20    464    713  A    C  
ATOM   1248  CE2 PHE A 183       7.767  -3.600 -58.748  1.00 87.51      A    C  
ANISOU 1248  CE2 PHE A 183     8500  18467   6282   -114    473    439  A    C  
ATOM   1249  CZ  PHE A 183       7.808  -2.490 -57.929  1.00 84.85      A    C  
ANISOU 1249  CZ  PHE A 183     8162  18040   6036    -44    445    578  A    C  
ATOM   1250  N   PRO A 184      10.645  -0.672 -64.509  1.00 88.19      A    N  
ANISOU 1250  N   PRO A 184     8716  19189   5604   -145    630    859  A    N  
ATOM   1251  CA  PRO A 184      11.538  -0.586 -65.684  1.00 89.49      A    C  
ANISOU 1251  CA  PRO A 184     8882  19531   5590   -182    714    899  A    C  
ATOM   1252  C   PRO A 184      12.948  -1.141 -65.461  1.00 93.49      A    C  
ANISOU 1252  C   PRO A 184     9327  20056   6137   -194    852    857  A    C  
ATOM   1253  O   PRO A 184      13.547  -0.898 -64.415  1.00 91.98      A    O  
ANISOU 1253  O   PRO A 184     9102  19746   6099   -216    872    918  A    O  
ATOM   1254  CB  PRO A 184      11.580   0.917 -66.001  1.00 92.05      A    C  
ANISOU 1254  CB  PRO A 184     9281  19854   5839   -212    670   1138  A    C  
ATOM   1255  CG  PRO A 184      10.467   1.533 -65.214  1.00 95.63      A    C  
ANISOU 1255  CG  PRO A 184     9792  20149   6396   -141    554   1198  A    C  
ATOM   1256  CD  PRO A 184      10.267   0.670 -64.022  1.00 89.48      A    C  
ANISOU 1256  CD  PRO A 184     8947  19237   5816   -123    556   1048  A    C  
ATOM   1257  N   LEU A 185      13.461  -1.897 -66.469  1.00 92.01      A    N  
ANISOU 1257  N   LEU A 185     9122  20046   5789   -165    949    753  A    N  
ATOM   1258  CA  LEU A 185      14.784  -2.551 -66.600  1.00 92.36      A    C  
ANISOU 1258  CA  LEU A 185     9095  20203   5795   -112   1104    705  A    C  
ATOM   1259  C   LEU A 185      14.961  -3.857 -65.791  1.00 96.14      A    C  
ANISOU 1259  C   LEU A 185     9577  20547   6403      2   1165    521  A    C  
ATOM   1260  O   LEU A 185      15.903  -4.600 -66.077  1.00 97.11      A    O  
ANISOU 1260  O   LEU A 185     9665  20778   6454    113   1302    453  A    O  
ATOM   1261  CB  LEU A 185      15.968  -1.600 -66.314  1.00 92.53      A    C  
ANISOU 1261  CB  LEU A 185     9015  20316   5827   -193   1159    913  A    C  
ATOM   1262  CG  LEU A 185      16.092  -0.339 -67.163  1.00 98.54      A    C  
ANISOU 1262  CG  LEU A 185     9804  21210   6426   -322   1136   1114  A    C  
ATOM   1263  CD1 LEU A 185      16.937   0.692 -66.459  1.00 98.67      A    C  
ANISOU 1263  CD1 LEU A 185     9786  21194   6510   -477   1134   1320  A    C  
ATOM   1264  CD2 LEU A 185      16.658  -0.646 -68.547  1.00103.51      A    C  
ANISOU 1264  CD2 LEU A 185    10388  22134   6807   -294   1251   1095  A    C  
ATOM   1265  N   ILE A 186      14.070  -4.151 -64.820  1.00 91.39      A    N  
ANISOU 1265  N   ILE A 186     9028  19726   5970     -7   1071    448  A    N  
ATOM   1266  CA  ILE A 186      14.149  -5.348 -63.973  1.00 90.71      A    C  
ANISOU 1266  CA  ILE A 186     8983  19476   6008     83   1119    294  A    C  
ATOM   1267  C   ILE A 186      13.422  -6.564 -64.624  1.00 96.11      A    C  
ANISOU 1267  C   ILE A 186     9827  20116   6575    102   1130     67  A    C  
ATOM   1268  O   ILE A 186      12.285  -6.423 -65.081  1.00 95.98      A    O  
ANISOU 1268  O   ILE A 186     9861  20117   6492     -9   1020     26  A    O  
ATOM   1269  CB  ILE A 186      13.680  -5.016 -62.516  1.00 91.79      A    C  
ANISOU 1269  CB  ILE A 186     9093  19409   6374     42   1025    348  A    C  
ATOM   1270  CG1 ILE A 186      14.825  -4.307 -61.746  1.00 92.01      A    C  
ANISOU 1270  CG1 ILE A 186     8998  19462   6499     36   1060    517  A    C  
ATOM   1271  CG2 ILE A 186      13.201  -6.254 -61.732  1.00 91.42      A    C  
ANISOU 1271  CG2 ILE A 186     9134  19167   6434     92   1034    181  A    C  
ATOM   1272  CD1 ILE A 186      14.408  -3.207 -60.817  1.00100.51      A    C  
ANISOU 1272  CD1 ILE A 186    10070  20409   7710    -57    946    642  A    C  
ATOM   1273  N   PRO A 187      14.076  -7.754 -64.693  1.00 94.12      A    N  
ANISOU 1273  N   PRO A 187     9669  19818   6274    241   1263    -78  A    N  
ATOM   1274  CA  PRO A 187      13.415  -8.928 -65.297  1.00 95.69      A    C  
ANISOU 1274  CA  PRO A 187    10091  19926   6341    229   1278   -309  A    C  
ATOM   1275  C   PRO A 187      12.574  -9.735 -64.312  1.00 99.85      A    C  
ANISOU 1275  C   PRO A 187    10743  20186   7009    154   1209   -420  A    C  
ATOM   1276  O   PRO A 187      12.814  -9.672 -63.102  1.00 97.71      A    O  
ANISOU 1276  O   PRO A 187    10402  19783   6939    199   1203   -344  A    O  
ATOM   1277  CB  PRO A 187      14.584  -9.769 -65.805  1.00 99.42      A    C  
ANISOU 1277  CB  PRO A 187    10648  20438   6688    453   1467   -401  A    C  
ATOM   1278  CG  PRO A 187      15.762  -9.354 -64.973  1.00102.91      A    C  
ANISOU 1278  CG  PRO A 187    10900  20922   7278    593   1538   -241  A    C  
ATOM   1279  CD  PRO A 187      15.436  -8.090 -64.226  1.00 96.13      A    C  
ANISOU 1279  CD  PRO A 187     9846  20110   6569    426   1407    -35  A    C  
ATOM   1280  N   ASN A 188      11.625 -10.538 -64.843  1.00 98.30      A    N  
ANISOU 1280  N   ASN A 188    10740  19926   6685     17   1159   -601  A    N  
ATOM   1281  CA  ASN A 188      10.723 -11.385 -64.056  1.00 98.04      A    C  
ANISOU 1281  CA  ASN A 188    10848  19666   6737   -121   1091   -716  A    C  
ATOM   1282  C   ASN A 188      11.435 -12.469 -63.232  1.00103.83      A    C  
ANISOU 1282  C   ASN A 188    11756  20119   7575     34   1210   -796  A    C  
ATOM   1283  O   ASN A 188      10.922 -12.834 -62.169  1.00102.94      A    O  
ANISOU 1283  O   ASN A 188    11664  19828   7620    -43   1156   -787  A    O  
ATOM   1284  CB  ASN A 188       9.626 -11.991 -64.922  1.00 98.61      A    C  
ANISOU 1284  CB  ASN A 188    11096  19770   6601   -346   1016   -894  A    C  
ATOM   1285  CG  ASN A 188       8.640 -10.964 -65.404  1.00120.60      A    C  
ANISOU 1285  CG  ASN A 188    13681  22830   9313   -515    857   -791  A    C  
ATOM   1287  ND2 ASN A 188       8.938 -10.313 -66.522  1.00110.06      A    N  
ANISOU 1287  ND2 ASN A 188    12222  21502   8091   -656    728   -724  A    N  
ATOM   1286  OD1 ASN A 188       7.596 -10.750 -64.790  1.00119.96      A    O  
ANISOU 1286  OD1 ASN A 188    13549  22972   9057   -500    854   -762  A    O  
ATOM   1288  N   ASP A 189      12.613 -12.963 -63.688  1.00102.60      A    N  
ANISOU 1288  N   ASP A 189    11719  19942   7321    276   1377   -858  A    N  
ATOM   1289  CA  ASP A 189      13.369 -13.969 -62.934  1.00103.53      A    C  
ANISOU 1289  CA  ASP A 189    12013  19811   7512    494   1505   -913  A    C  
ATOM   1290  C   ASP A 189      13.998 -13.355 -61.665  1.00104.93      A    C  
ANISOU 1290  C   ASP A 189    11934  20012   7922    617   1504   -711  A    C  
ATOM   1291  O   ASP A 189      14.131 -14.059 -60.661  1.00103.95      A    O  
ANISOU 1291  O   ASP A 189    11918  19659   7918    697   1533   -723  A    O  
ATOM   1292  CB  ASP A 189      14.382 -14.753 -63.805  1.00108.69      A    C  
ANISOU 1292  CB  ASP A 189    12874  20461   7963    770   1694  -1037  A    C  
ATOM   1293  CG  ASP A 189      15.585 -13.996 -64.344  1.00123.31      A    C  
ANISOU 1293  CG  ASP A 189    14464  22641   9746    993   1798   -900  A    C  
ATOM   1294  OD1 ASP A 189      15.410 -12.853 -64.812  1.00123.23      A    O  
ANISOU 1294  OD1 ASP A 189    14169  22884   9770    853   1708   -743  A    O  
ATOM   1295  OD2 ASP A 189      16.697 -14.567 -64.337  1.00132.67      A    O1-
ANISOU 1295  OD2 ASP A 189    15744  23839  10825   1310   1975   -944  A    O1-
ATOM   1296  N   TYR A 190      14.293 -12.031 -61.684  1.00100.19      A    N  
ANISOU 1296  N   TYR A 190    11020  19675   7372    596   1458   -524  A    N  
ATOM   1297  CA  TYR A 190      14.809 -11.313 -60.513  1.00 98.25      A    C  
ANISOU 1297  CA  TYR A 190    10539  19470   7322    645   1434   -335  A    C  
ATOM   1298  C   TYR A 190      13.671 -11.033 -59.532  1.00 99.44      A    C  
ANISOU 1298  C   TYR A 190    10667  19473   7644    444   1285   -303  A    C  
ATOM   1299  O   TYR A 190      13.864 -11.196 -58.327  1.00 97.84      A    O  
ANISOU 1299  O   TYR A 190    10431  19146   7597    497   1283   -246  A    O  
ATOM   1300  CB  TYR A 190      15.495  -9.983 -60.900  1.00 99.31      A    C  
ANISOU 1300  CB  TYR A 190    10402  19903   7427    633   1429   -153  A    C  
ATOM   1301  CG  TYR A 190      15.991  -9.192 -59.700  1.00100.10      A    C  
ANISOU 1301  CG  TYR A 190    10290  20038   7703    622   1388     30  A    C  
ATOM   1302  CD1 TYR A 190      17.258  -9.414 -59.167  1.00103.04      A    C  
ANISOU 1302  CD1 TYR A 190    10545  20509   8096    814   1494    108  A    C  
ATOM   1303  CD2 TYR A 190      15.180  -8.241 -59.079  1.00 98.45      A    C  
ANISOU 1303  CD2 TYR A 190    10009  19777   7621    431   1244    123  A    C  
ATOM   1304  CE1 TYR A 190      17.711  -8.707 -58.053  1.00102.02      A    C  
ANISOU 1304  CE1 TYR A 190    10227  20431   8105    767   1445    268  A    C  
ATOM   1305  CE2 TYR A 190      15.623  -7.529 -57.964  1.00 97.52      A    C  
ANISOU 1305  CE2 TYR A 190     9743  19667   7643    406   1206    270  A    C  
ATOM   1306  CZ  TYR A 190      16.893  -7.759 -57.462  1.00105.00      A    C  
ANISOU 1306  CZ  TYR A 190    10573  20719   8604    549   1300    340  A    C  
ATOM   1307  OH  TYR A 190      17.344  -7.058 -56.372  1.00106.22      A    O  
ANISOU 1307  OH  TYR A 190    10582  20905   8871    488   1252    479  A    O  
ATOM   1308  N   LEU A 191      12.523 -10.531 -60.053  1.00 95.43      A    N  
ANISOU 1308  N   LEU A 191    10149  19023   7087    230   1162   -323  A    N  
ATOM   1309  CA  LEU A 191      11.317 -10.167 -59.311  1.00 93.77      A    C  
ANISOU 1309  CA  LEU A 191     9887  18752   6991     50   1022   -288  A    C  
ATOM   1310  C   LEU A 191      10.813 -11.352 -58.496  1.00 98.71      A    C  
ANISOU 1310  C   LEU A 191    10693  19129   7682     -1   1026   -404  A    C  
ATOM   1311  O   LEU A 191      10.553 -11.193 -57.297  1.00 97.37      A    O  
ANISOU 1311  O   LEU A 191    10451  18875   7669    -41    971   -333  A    O  
ATOM   1312  CB  LEU A 191      10.226  -9.648 -60.272  1.00 94.40      A    C  
ANISOU 1312  CB  LEU A 191     9934  18998   6937   -122    911   -303  A    C  
ATOM   1313  CG  LEU A 191       9.023  -8.925 -59.635  1.00 98.17      A    C  
ANISOU 1313  CG  LEU A 191    10278  19522   7500   -250    767   -213  A    C  
ATOM   1314  CD1 LEU A 191       9.329  -7.457 -59.380  1.00 97.29      A    C  
ANISOU 1314  CD1 LEU A 191     9994  19516   7456   -178    731    -15  A    C  
ATOM   1315  CD2 LEU A 191       7.803  -9.013 -60.528  1.00101.74      A    C  
ANISOU 1315  CD2 LEU A 191    10742  20130   7786   -424    667   -285  A    C  
ATOM   1316  N   LEU A 192      10.737 -12.548 -59.131  1.00 96.97      A    N  
ANISOU 1316  N   LEU A 192    10738  18777   7328     -3   1098   -583  A    N  
ATOM   1317  CA  LEU A 192      10.323 -13.804 -58.499  1.00 97.66      A    C  
ANISOU 1317  CA  LEU A 192    11082  18583   7443    -70   1118   -703  A    C  
ATOM   1318  C   LEU A 192      11.331 -14.231 -57.419  1.00101.13      A    C  
ANISOU 1318  C   LEU A 192    11549  18852   8023    172   1219   -635  A    C  
ATOM   1319  O   LEU A 192      10.928 -14.755 -56.384  1.00100.11      A    O  
ANISOU 1319  O   LEU A 192    11493  18537   8005    109   1194   -625  A    O  
ATOM   1320  CB  LEU A 192      10.157 -14.903 -59.564  1.00100.66      A    C  
ANISOU 1320  CB  LEU A 192    11798  18841   7607   -130   1179   -918  A    C  
ATOM   1321  CG  LEU A 192       9.688 -16.284 -59.083  1.00106.87      A    C  
ANISOU 1321  CG  LEU A 192    12941  19292   8371   -260   1200  -1063  A    C  
ATOM   1322  CD1 LEU A 192       8.187 -16.306 -58.813  1.00106.47      A    C  
ANISOU 1322  CD1 LEU A 192    12855  19291   8308   -651   1042  -1089  A    C  
ATOM   1323  CD2 LEU A 192      10.083 -17.363 -60.079  1.00112.22      A    C  
ANISOU 1323  CD2 LEU A 192    14019  19786   8834   -188   1319  -1268  A    C  
ATOM   1324  N   SER A 193      12.633 -13.983 -57.657  1.00 98.46      A    N  
ANISOU 1324  N   SER A 193    11126  18619   7664    444   1331   -571  A    N  
ATOM   1325  CA  SER A 193      13.713 -14.304 -56.717  1.00 98.03      A    C  
ANISOU 1325  CA  SER A 193    11041  18496   7709    709   1428   -482  A    C  
ATOM   1326  C   SER A 193      13.703 -13.407 -55.468  1.00100.08      A    C  
ANISOU 1326  C   SER A 193    11034  18827   8163    656   1339   -305  A    C  
ATOM   1327  O   SER A 193      13.994 -13.896 -54.371  1.00 99.11      A    O  
ANISOU 1327  O   SER A 193    10945  18567   8144    764   1367   -257  A    O  
ATOM   1328  CB  SER A 193      15.064 -14.263 -57.419  1.00100.77      A    C  
ANISOU 1328  CB  SER A 193    11311  19034   7944    992   1565   -449  A    C  
ATOM   1329  OG  SER A 193      15.103 -15.275 -58.410  1.00108.16      A    O  
ANISOU 1329  OG  SER A 193    12548  19859   8687   1086   1669   -630  A    O  
ATOM   1330  N   TRP A 194      13.345 -12.111 -55.632  1.00 95.47      A    N  
ANISOU 1330  N   TRP A 194    10217  18443   7612    499   1233   -211  A    N  
ATOM   1331  CA  TRP A 194      13.260 -11.153 -54.525  1.00 93.16      A    C  
ANISOU 1331  CA  TRP A 194     9716  18203   7476    435   1145    -60  A    C  
ATOM   1332  C   TRP A 194      12.013 -11.413 -53.660  1.00 94.09      A    C  
ANISOU 1332  C   TRP A 194     9906  18154   7690    269   1054    -93  A    C  
ATOM   1333  O   TRP A 194      12.088 -11.298 -52.437  1.00 92.04      A    O  
ANISOU 1333  O   TRP A 194     9584  17829   7558    293   1033    -12  A    O  
ATOM   1334  CB  TRP A 194      13.311  -9.694 -55.032  1.00 91.08      A    C  
ANISOU 1334  CB  TRP A 194     9253  18164   7190    344   1076     51  A    C  
ATOM   1335  CG  TRP A 194      13.323  -8.668 -53.928  1.00 90.38      A    C  
ANISOU 1335  CG  TRP A 194     9005  18101   7234    294   1001    196  A    C  
ATOM   1336  CD1 TRP A 194      14.402  -8.260 -53.198  1.00 93.02      A    C  
ANISOU 1336  CD1 TRP A 194     9209  18512   7622    373   1034    313  A    C  
ATOM   1337  CD2 TRP A 194      12.192  -7.951 -53.409  1.00 88.81      A    C  
ANISOU 1337  CD2 TRP A 194     8774  17861   7108    156    884    233  A    C  
ATOM   1339  CE2 TRP A 194      12.665  -7.116 -52.371  1.00 91.63      A    C  
ANISOU 1339  CE2 TRP A 194     9023  18230   7562    162    856    359  A    C  
ATOM   1340  CE3 TRP A 194      10.822  -7.924 -53.727  1.00 89.95      A    C  
ANISOU 1340  CE3 TRP A 194     8961  17992   7224     36    802    177  A    C  
ATOM   1338  NE1 TRP A 194      14.014  -7.339 -52.252  1.00 90.91      A    N  
ANISOU 1338  NE1 TRP A 194     8867  18217   7456    270    941    405  A    N  
ATOM   1341  CZ2 TRP A 194      11.817  -6.267 -51.649  1.00 89.74      A    C  
ANISOU 1341  CZ2 TRP A 194     8758  17947   7392     80    761    416  A    C  
ATOM   1342  CZ3 TRP A 194       9.985  -7.080 -53.015  1.00 90.35      A    C  
ANISOU 1342  CZ3 TRP A 194     8940  18045   7344    -22    710    252  A    C  
ATOM   1343  CH2 TRP A 194      10.482  -6.267 -51.986  1.00 89.98      A    C  
ANISOU 1343  CH2 TRP A 194     8826  17967   7394     14    696    364  A    C  
ATOM   1344  N   LEU A 195      10.882 -11.772 -54.300  1.00 90.59      A    N  
ANISOU 1344  N   LEU A 195     9579  17677   7164     90   1000   -206  A    N  
ATOM   1345  CA  LEU A 195       9.616 -12.075 -53.623  1.00 89.76      A    C  
ANISOU 1345  CA  LEU A 195     9518  17479   7107   -105    915   -238  A    C  
ATOM   1346  C   LEU A 195       9.714 -13.367 -52.812  1.00 94.19      A    C  
ANISOU 1346  C   LEU A 195    10300  17775   7712    -80    980   -297  A    C  
ATOM   1347  O   LEU A 195       9.180 -13.427 -51.701  1.00 92.66      A    O  
ANISOU 1347  O   LEU A 195    10074  17512   7621   -159    936   -244  A    O  
ATOM   1348  CB  LEU A 195       8.448 -12.147 -54.622  1.00 90.78      A    C  
ANISOU 1348  CB  LEU A 195     9690  17709   7094   -326    840   -338  A    C  
ATOM   1349  CG  LEU A 195       7.864 -10.807 -55.080  1.00 94.43      A    C  
ANISOU 1349  CG  LEU A 195     9922  18432   7523   -381    736   -247  A    C  
ATOM   1350  CD1 LEU A 195       7.293 -10.915 -56.474  1.00 96.30      A    C  
ANISOU 1350  CD1 LEU A 195    10208  18812   7570   -531    689   -347  A    C  
ATOM   1351  CD2 LEU A 195       6.792 -10.308 -54.125  1.00 94.64      A    C  
ANISOU 1351  CD2 LEU A 195     9796  18518   7647   -459    643   -155  A    C  
ATOM   1352  N   LEU A 196      10.413 -14.386 -53.359  1.00 92.60      A    N  
ANISOU 1352  N   LEU A 196    10343  17422   7420     49   1094   -399  A    N  
ATOM   1353  CA  LEU A 196      10.646 -15.669 -52.694  1.00 93.90      A    C  
ANISOU 1353  CA  LEU A 196    10790  17290   7599    126   1177   -451  A    C  
ATOM   1354  C   LEU A 196      11.576 -15.486 -51.486  1.00 96.89      A    C  
ANISOU 1354  C   LEU A 196    11043  17653   8118    360   1219   -301  A    C  
ATOM   1355  O   LEU A 196      11.378 -16.147 -50.461  1.00 96.65      A    O  
ANISOU 1355  O   LEU A 196    11141  17427   8154    351   1228   -277  A    O  
ATOM   1356  CB  LEU A 196      11.233 -16.700 -53.683  1.00 96.71      A    C  
ANISOU 1356  CB  LEU A 196    11469  17485   7791    265   1301   -599  A    C  
ATOM   1357  CG  LEU A 196      10.295 -17.788 -54.257  1.00103.98      A    C  
ANISOU 1357  CG  LEU A 196    12767  18170   8569     12   1294   -786  A    C  
ATOM   1358  CD1 LEU A 196       9.792 -18.738 -53.180  1.00107.33      A    C  
ANISOU 1358  CD1 LEU A 196    13389  18330   9062   -151   1272   -779  A    C  
ATOM   1359  CD2 LEU A 196       9.144 -17.201 -55.071  1.00104.11      A    C  
ANISOU 1359  CD2 LEU A 196    12672  18406   8478   -293   1178   -859  A    C  
ATOM   1360  N   PHE A 197      12.576 -14.573 -51.606  1.00 92.27      A    N  
ANISOU 1360  N   PHE A 197    10201  17297   7560    538   1238   -193  A    N  
ATOM   1361  CA  PHE A 197      13.524 -14.244 -50.537  1.00 90.89      A    C  
ANISOU 1361  CA  PHE A 197     9854  17191   7489    725   1260    -42  A    C  
ATOM   1362  C   PHE A 197      12.802 -13.549 -49.374  1.00 91.63      A    C  
ANISOU 1362  C   PHE A 197     9795  17302   7717    549   1145     48  A    C  
ATOM   1363  O   PHE A 197      13.043 -13.901 -48.214  1.00 91.14      A    O  
ANISOU 1363  O   PHE A 197     9744  17150   7734    625   1154    120  A    O  
ATOM   1364  CB  PHE A 197      14.707 -13.394 -51.062  1.00 92.44      A    C  
ANISOU 1364  CB  PHE A 197     9806  17672   7643    879   1298     48  A    C  
ATOM   1365  CG  PHE A 197      15.580 -12.766 -49.991  1.00 93.10      A    C  
ANISOU 1365  CG  PHE A 197     9643  17916   7816    966   1279    217  A    C  
ATOM   1366  CD1 PHE A 197      16.350 -13.556 -49.143  1.00 97.38      A    C  
ANISOU 1366  CD1 PHE A 197    10214  18409   8378   1196   1349    280  A    C  
ATOM   1367  CD2 PHE A 197      15.618 -11.388 -49.822  1.00 93.73      A    C  
ANISOU 1367  CD2 PHE A 197     9484  18193   7937    815   1188    314  A    C  
ATOM   1368  CE1 PHE A 197      17.139 -12.975 -48.143  1.00 97.62      A    C  
ANISOU 1368  CE1 PHE A 197     9998  18627   8464   1247   1318    437  A    C  
ATOM   1369  CE2 PHE A 197      16.413 -10.808 -48.826  1.00 95.91      A    C  
ANISOU 1369  CE2 PHE A 197     9559  18613   8269    846   1161    457  A    C  
ATOM   1370  CZ  PHE A 197      17.173 -11.606 -47.999  1.00 94.97      A    C  
ANISOU 1370  CZ  PHE A 197     9432  18488   8163   1050   1221    516  A    C  
ATOM   1371  N   ILE A 198      11.915 -12.577 -49.697  1.00 85.74      A    N  
ANISOU 1371  N   ILE A 198     8921  16679   6978    341   1042     45  A    N  
ATOM   1372  CA  ILE A 198      11.112 -11.822 -48.730  1.00 83.98      A    C  
ANISOU 1372  CA  ILE A 198     8564  16494   6851    198    939    117  A    C  
ATOM   1373  C   ILE A 198      10.088 -12.757 -48.025  1.00 90.00      A    C  
ANISOU 1373  C   ILE A 198     9482  17078   7638     61    923     66  A    C  
ATOM   1374  O   ILE A 198       9.863 -12.615 -46.820  1.00 88.50      A    O  
ANISOU 1374  O   ILE A 198     9232  16859   7535     46    893    142  A    O  
ATOM   1375  CB  ILE A 198      10.488 -10.548 -49.398  1.00 85.42      A    C  
ANISOU 1375  CB  ILE A 198     8594  16862   7001     79    851    136  A    C  
ATOM   1376  CG1 ILE A 198      11.555  -9.435 -49.626  1.00 84.27      A    C  
ANISOU 1376  CG1 ILE A 198     8292  16873   6855    174    856    238  A    C  
ATOM   1377  CG2 ILE A 198       9.236 -10.005 -48.670  1.00 84.92      A    C  
ANISOU 1377  CG2 ILE A 198     8451  16830   6984    -62    756    167  A    C  
ATOM   1378  CD1 ILE A 198      12.248  -8.788 -48.368  1.00 84.03      A    C  
ANISOU 1378  CD1 ILE A 198     8140  16869   6919    226    838    363  A    C  
ATOM   1379  N   ALA A 199       9.529 -13.741 -48.771  1.00 89.16      A    N  
ANISOU 1379  N   ALA A 199     9590  16853   7435    -55    946    -63  A    N  
ATOM   1380  CA  ALA A 199       8.589 -14.745 -48.258  1.00 90.21      A    C  
ANISOU 1380  CA  ALA A 199     9913  16809   7553   -246    936   -119  A    C  
ATOM   1381  C   ALA A 199       9.270 -15.657 -47.234  1.00 94.70      A    C  
ANISOU 1381  C   ALA A 199    10653  17144   8182    -96   1015    -70  A    C  
ATOM   1382  O   ALA A 199       8.626 -16.062 -46.264  1.00 94.30      A    O  
ANISOU 1382  O   ALA A 199    10651  17004   8176   -225    991    -33  A    O  
ATOM   1383  CB  ALA A 199       8.031 -15.574 -49.402  1.00 93.17      A    C  
ANISOU 1383  CB  ALA A 199    10525  17096   7780   -414    950   -276  A    C  
ATOM   1384  N   PHE A 200      10.570 -15.970 -47.457  1.00 92.41      A    N  
ANISOU 1384  N   PHE A 200    10440  16791   7880    192   1114    -57  A    N  
ATOM   1385  CA APHE A 200      11.328 -16.814 -46.539  0.50 93.34      A    C  
ANISOU 1385  CA APHE A 200    10711  16721   8035    404   1195     10  A    C  
ATOM   1386  CA BPHE A 200      11.407 -16.801 -46.586  0.50 93.22      A    C  
ANISOU 1386  CA BPHE A 200    10692  16711   8016    421   1200     10  A    C  
ATOM   1387  C   PHE A 200      11.694 -16.072 -45.255  1.00 95.02      A    C  
ANISOU 1387  C   PHE A 200    10660  17077   8365    481   1149    169  A    C  
ATOM   1388  O   PHE A 200      11.606 -16.675 -44.177  1.00 94.74      A    O  
ANISOU 1388  O   PHE A 200    10726  16898   8372    502   1162    234  A    O  
ATOM   1389  CB APHE A 200      12.538 -17.467 -47.219  0.50 97.14      A    C  
ANISOU 1389  CB APHE A 200    11356  17125   8430    723   1324    -23  A    C  
ATOM   1390  CB BPHE A 200      12.706 -17.187 -47.334  0.50 96.52      A    C  
ANISOU 1390  CB BPHE A 200    11202  17116   8353    746   1320    -12  A    C  
ATOM   1391  CG APHE A 200      12.226 -18.864 -47.704  0.50101.78      A    C  
ANISOU 1391  CG APHE A 200    12401  17366   8905    706   1407   -157  A    C  
ATOM   1392  CG BPHE A 200      13.958 -17.389 -46.512  0.50 98.60      A    C  
ANISOU 1392  CG BPHE A 200    11401  17413   8650   1085   1392    123  A    C  
ATOM   1393  CD1APHE A 200      12.481 -19.971 -46.901  0.50106.74      A    C  
ANISOU 1393  CD1APHE A 200    13324  17700   9532    846   1482   -117  A    C  
ATOM   1394  CD1BPHE A 200      14.173 -18.575 -45.820  0.50103.62      A    C  
ANISOU 1394  CD1BPHE A 200    12320  17778   9274   1244   1467    152  A    C  
ATOM   1395  CD2APHE A 200      11.640 -19.073 -48.948  0.50105.37      A    C  
ANISOU 1395  CD2APHE A 200    13024  17774   9237    534   1407   -323  A    C  
ATOM   1396  CD2BPHE A 200      14.949 -16.413 -46.474  0.50 99.89      A    C  
ANISOU 1396  CD2BPHE A 200    11230  17893   8832   1244   1387    229  A    C  
ATOM   1397  CE1APHE A 200      12.177 -21.263 -47.343  0.50110.83      A    C  
ANISOU 1397  CE1APHE A 200    14339  17843   9928    812   1563   -245  A    C  
ATOM   1398  CE1BPHE A 200      15.340 -18.767 -45.074  0.50105.33      A    C  
ANISOU 1398  CE1BPHE A 200    12452  18070   9498   1590   1531    294  A    C  
ATOM   1399  CE2APHE A 200      11.335 -20.365 -49.390  0.50111.24      A    C  
ANISOU 1399  CE2APHE A 200    14245  18168   9853    479   1481   -463  A    C  
ATOM   1400  CE2BPHE A 200      16.117 -16.608 -45.730  0.50103.49      A    C  
ANISOU 1400  CE2BPHE A 200    11585  18447   9288   1544   1446    364  A    C  
ATOM   1401  CZ APHE A 200      11.606 -21.451 -48.584  0.50111.25      A    C  
ANISOU 1401  CZ APHE A 200    14575  17840   9855    615   1561   -426  A    C  
ATOM   1402  CZ BPHE A 200      16.305 -17.784 -45.036  0.50103.37      A    C  
ANISOU 1402  CZ BPHE A 200    11823  18191   9262   1736   1516    399  A    C  
ATOM   1403  N   LEU A 201      12.034 -14.758 -45.350  1.00 88.79      A    N  
ANISOU 1403  N   LEU A 201     9563  16559   7615    494   1090    231  A    N  
ATOM   1404  CA  LEU A 201      12.332 -13.894 -44.201  1.00 86.09      A    C  
ANISOU 1404  CA  LEU A 201     8989  16362   7361    518   1032    362  A    C  
ATOM   1405  C   LEU A 201      11.094 -13.762 -43.312  1.00 87.96      A    C  
ANISOU 1405  C   LEU A 201     9217  16553   7652    307    957    373  A    C  
ATOM   1406  O   LEU A 201      11.232 -13.810 -42.097  1.00 87.44      A    O  
ANISOU 1406  O   LEU A 201     9110  16475   7639    346    945    463  A    O  
ATOM   1407  CB  LEU A 201      12.786 -12.490 -44.641  1.00 84.57      A    C  
ANISOU 1407  CB  LEU A 201     8544  16420   7168    508    981    404  A    C  
ATOM   1408  CG  LEU A 201      14.134 -12.330 -45.355  1.00 89.50      A    C  
ANISOU 1408  CG  LEU A 201     9070  17199   7735    702   1045    447  A    C  
ATOM   1409  CD1 LEU A 201      14.334 -10.889 -45.757  1.00 88.29      A    C  
ANISOU 1409  CD1 LEU A 201     8712  17263   7572    600    981    490  A    C  
ATOM   1410  CD2 LEU A 201      15.312 -12.771 -44.478  1.00 91.88      A    C  
ANISOU 1410  CD2 LEU A 201     9305  17558   8050    908   1088    563  A    C  
ATOM   1411  N   PHE A 202       9.891 -13.615 -43.921  1.00 83.96      A    N  
ANISOU 1411  N   PHE A 202     8731  16059   7111     89    909    288  A    N  
ATOM   1412  CA  PHE A 202       8.602 -13.501 -43.228  1.00 83.01      A    C  
ANISOU 1412  CA  PHE A 202     8569  15963   7009   -116    845    298  A    C  
ATOM   1413  C   PHE A 202       8.258 -14.775 -42.447  1.00 89.01      A    C  
ANISOU 1413  C   PHE A 202     9545  16510   7766   -189    888    304  A    C  
ATOM   1414  O   PHE A 202       7.793 -14.671 -41.311  1.00 88.89      A    O  
ANISOU 1414  O   PHE A 202     9465  16518   7790   -249    862    378  A    O  
ATOM   1415  CB  PHE A 202       7.471 -13.144 -44.205  1.00 84.72      A    C  
ANISOU 1415  CB  PHE A 202     8732  16304   7153   -312    787    217  A    C  
ATOM   1416  CG  PHE A 202       7.265 -11.684 -44.566  1.00 84.92      A    C  
ANISOU 1416  CG  PHE A 202     8530  16556   7179   -284    719    250  A    C  
ATOM   1417  CD1 PHE A 202       8.062 -10.689 -44.008  1.00 86.92      A    C  
ANISOU 1417  CD1 PHE A 202     8663  16870   7494   -133    709    336  A    C  
ATOM   1418  CD2 PHE A 202       6.269 -11.306 -45.461  1.00 87.29      A    C  
ANISOU 1418  CD2 PHE A 202     8759  17010   7398   -416    663    201  A    C  
ATOM   1419  CE1 PHE A 202       7.873  -9.343 -44.352  1.00 87.09      A    C  
ANISOU 1419  CE1 PHE A 202     8547  17043   7499   -114    652    368  A    C  
ATOM   1420  CE2 PHE A 202       6.075  -9.960 -45.795  1.00 89.14      A    C  
ANISOU 1420  CE2 PHE A 202     8825  17426   7618   -352    607    247  A    C  
ATOM   1421  CZ  PHE A 202       6.879  -8.988 -45.241  1.00 86.11      A    C  
ANISOU 1421  CZ  PHE A 202     8375  17042   7300   -201    606    328  A    C  
ATOM   1422  N   SER A 203       8.518 -15.968 -43.034  1.00 87.05      A    N  
ANISOU 1422  N   SER A 203     9580  16039   7456   -176    961    228  A    N  
ATOM   1423  CA  SER A 203       8.295 -17.276 -42.399  1.00 88.53      A    C  
ANISOU 1423  CA  SER A 203    10065  15954   7619   -241   1015    234  A    C  
ATOM   1424  C   SER A 203       9.195 -17.432 -41.161  1.00 91.76      A    C  
ANISOU 1424  C   SER A 203    10466  16301   8097     -8   1054    370  A    C  
ATOM   1425  O   SER A 203       8.738 -17.934 -40.132  1.00 91.74      A    O  
ANISOU 1425  O   SER A 203    10553  16197   8106   -109   1053    436  A    O  
ATOM   1426  CB  SER A 203       8.574 -18.406 -43.384  1.00 94.65      A    C  
ANISOU 1426  CB  SER A 203    11195  16473   8296   -211   1098    118  A    C  
ATOM   1427  OG  SER A 203       7.870 -18.224 -44.600  1.00104.77      A    O  
ANISOU 1427  OG  SER A 203    12478  17837   9491   -428   1056    -12  A    O  
ATOM   1428  N   GLY A 204      10.448 -16.971 -41.281  1.00 87.35      A    N  
ANISOU 1428  N   GLY A 204     9780  15843   7566    281   1081    421  A    N  
ATOM   1429  CA  GLY A 204      11.446 -16.968 -40.216  1.00 86.70      A    C  
ANISOU 1429  CA  GLY A 204     9625  15792   7526    520   1104    560  A    C  
ATOM   1430  C   GLY A 204      11.027 -16.105 -39.042  1.00 87.68      A    C  
ANISOU 1430  C   GLY A 204     9514  16086   7714    408   1019    648  A    C  
ATOM   1431  O   GLY A 204      11.199 -16.506 -37.890  1.00 87.63      A    O  
ANISOU 1431  O   GLY A 204     9550  16025   7723    465   1028    749  A    O  
ATOM   1432  N   ILE A 205      10.445 -14.921 -39.333  1.00 82.08      A    N  
ANISOU 1432  N   ILE A 205     8584  15578   7026    263    942    609  A    N  
ATOM   1433  CA  ILE A 205       9.921 -13.986 -38.331  1.00 80.55      A    C  
ANISOU 1433  CA  ILE A 205     8197  15540   6870    168    868    667  A    C  
ATOM   1434  C   ILE A 205       8.694 -14.625 -37.643  1.00 85.75      A    C  
ANISOU 1434  C   ILE A 205     8954  16112   7514    -32    864    670  A    C  
ATOM   1435  O   ILE A 205       8.607 -14.591 -36.411  1.00 85.17      A    O  
ANISOU 1435  O   ILE A 205     8841  16065   7456    -30    853    757  A    O  
ATOM   1436  CB  ILE A 205       9.610 -12.571 -38.929  1.00 82.00      A    C  
ANISOU 1436  CB  ILE A 205     8179  15922   7057    105    800    625  A    C  
ATOM   1437  CG1 ILE A 205      10.875 -11.907 -39.513  1.00 81.31      A    C  
ANISOU 1437  CG1 ILE A 205     7986  15939   6969    259    802    650  A    C  
ATOM   1438  CG2 ILE A 205       8.961 -11.651 -37.882  1.00 82.36      A    C  
ANISOU 1438  CG2 ILE A 205     8088  16090   7114     26    739    666  A    C  
ATOM   1439  CD1 ILE A 205      10.642 -10.594 -40.247  1.00 82.97      A    C  
ANISOU 1439  CD1 ILE A 205     8070  16289   7164    196    748    614  A    C  
ATOM   1440  N   ILE A 206       7.771 -15.226 -38.440  1.00 83.34      A    N  
ANISOU 1440  N   ILE A 206     8777  15727   7161   -224    874    580  A    N  
ATOM   1441  CA  ILE A 206       6.561 -15.896 -37.936  1.00 84.20      A    C  
ANISOU 1441  CA  ILE A 206     8973  15791   7227   -478    871    583  A    C  
ATOM   1442  C   ILE A 206       6.922 -17.062 -37.000  1.00 88.84      A    C  
ANISOU 1442  C   ILE A 206     9807  16138   7811   -444    934    665  A    C  
ATOM   1443  O   ILE A 206       6.420 -17.096 -35.878  1.00 88.14      A    O  
ANISOU 1443  O   ILE A 206     9678  16094   7718   -542    924    747  A    O  
ATOM   1444  CB  ILE A 206       5.573 -16.308 -39.080  1.00 88.63      A    C  
ANISOU 1444  CB  ILE A 206     9613  16356   7708   -733    856    467  A    C  
ATOM   1445  CG1 ILE A 206       4.992 -15.077 -39.843  1.00 88.03      A    C  
ANISOU 1445  CG1 ILE A 206     9259  16571   7616   -768    783    422  A    C  
ATOM   1446  CG2 ILE A 206       4.450 -17.246 -38.589  1.00 90.79      A    C  
ANISOU 1446  CG2 ILE A 206    10030  16558   7906  -1048    863    478  A    C  
ATOM   1447  CD1 ILE A 206       4.242 -13.961 -38.989  1.00 97.41      A    C  
ANISOU 1447  CD1 ILE A 206    10168  18028   8816   -775    729    495  A    C  
ATOM   1448  N   TYR A 207       7.817 -17.981 -37.444  1.00 86.71      A    N  
ANISOU 1448  N   TYR A 207     9795  15622   7528   -274   1005    652  A    N  
ATOM   1449  CA  TYR A 207       8.265 -19.132 -36.647  1.00 88.15      A    C  
ANISOU 1449  CA  TYR A 207    10262  15540   7691   -176   1075    742  A    C  
ATOM   1450  C   TYR A 207       8.804 -18.702 -35.287  1.00 91.23      A    C  
ANISOU 1450  C   TYR A 207    10483  16053   8127     -6   1058    891  A    C  
ATOM   1451  O   TYR A 207       8.408 -19.279 -34.270  1.00 92.07      A    O  
ANISOU 1451  O   TYR A 207    10705  16065   8210    -94   1073    983  A    O  
ATOM   1452  CB  TYR A 207       9.310 -19.976 -37.402  1.00 90.71      A    C  
ANISOU 1452  CB  TYR A 207    10871  15617   7979     78   1164    705  A    C  
ATOM   1453  CG  TYR A 207       9.736 -21.223 -36.651  1.00 94.58      A    C  
ANISOU 1453  CG  TYR A 207    11709  15798   8427    224   1247    806  A    C  
ATOM   1454  CD1 TYR A 207       8.972 -22.386 -36.702  1.00 98.96      A    C  
ANISOU 1454  CD1 TYR A 207    12665  16030   8906    -16   1290    776  A    C  
ATOM   1455  CD2 TYR A 207      10.900 -21.240 -35.889  1.00 95.31      A    C  
ANISOU 1455  CD2 TYR A 207    11742  15934   8540    592   1279    943  A    C  
ATOM   1456  CE1 TYR A 207       9.360 -23.537 -36.018  1.00101.94      A    C  
ANISOU 1456  CE1 TYR A 207    13419  16081   9234    130   1372    882  A    C  
ATOM   1457  CE2 TYR A 207      11.296 -22.384 -35.199  1.00 98.69      A    C  
ANISOU 1457  CE2 TYR A 207    12499  16083   8915    771   1356   1057  A    C  
ATOM   1458  CZ  TYR A 207      10.524 -23.532 -35.268  1.00108.93      A    C  
ANISOU 1458  CZ  TYR A 207    14237  17008  10142    551   1407   1027  A    C  
ATOM   1459  OH  TYR A 207      10.908 -24.664 -34.588  1.00113.59      A    O  
ANISOU 1459  OH  TYR A 207    15207  17284  10670    738   1489   1152  A    O  
ATOM   1460  N   THR A 208       9.690 -17.685 -35.271  1.00 85.80      A    N  
ANISOU 1460  N   THR A 208     9531  15583   7484    207   1023    916  A    N  
ATOM   1461  CA  THR A 208      10.270 -17.165 -34.035  1.00 84.82      A    C  
ANISOU 1461  CA  THR A 208     9231  15614   7381    344    991   1044  A    C  
ATOM   1462  C   THR A 208       9.191 -16.501 -33.184  1.00 87.80      A    C  
ANISOU 1462  C   THR A 208     9457  16141   7763    123    932   1060  A    C  
ATOM   1463  O   THR A 208       9.064 -16.868 -32.014  1.00 88.12      A    O  
ANISOU 1463  O   THR A 208     9542  16160   7782    116    940   1165  A    O  
ATOM   1464  CB  THR A 208      11.497 -16.277 -34.302  1.00 89.63      A    C  
ANISOU 1464  CB  THR A 208     9611  16436   8010    559    962   1060  A    C  
ATOM   1466  CG2 THR A 208      12.305 -15.999 -33.041  1.00 86.00      A    C  
ANISOU 1466  CG2 THR A 208     9012  16129   7537    705    931   1199  A    C  
ATOM   1465  OG1 THR A 208      12.340 -16.913 -35.261  1.00 91.71      A    O  
ANISOU 1465  OG1 THR A 208     9999  16599   8249    761   1031   1033  A    O  
ATOM   1467  N   TYR A 209       8.360 -15.600 -33.783  1.00 83.11      A    N  
ANISOU 1467  N   TYR A 209     8701  15699   7178    -41    883    963  A    N  
ATOM   1468  CA  TYR A 209       7.295 -14.905 -33.044  1.00 81.96      A    C  
ANISOU 1468  CA  TYR A 209     8397  15732   7014   -201    841    975  A    C  
ATOM   1469  C   TYR A 209       6.205 -15.860 -32.512  1.00 85.52      A    C  
ANISOU 1469  C   TYR A 209     8979  16102   7411   -426    874   1011  A    C  
ATOM   1470  O   TYR A 209       5.517 -15.514 -31.554  1.00 84.88      A    O  
ANISOU 1470  O   TYR A 209     8783  16170   7297   -508    860   1066  A    O  
ATOM   1471  CB  TYR A 209       6.685 -13.704 -33.805  1.00 82.23      A    C  
ANISOU 1471  CB  TYR A 209     8235  15959   7049   -261    788    882  A    C  
ATOM   1472  CG  TYR A 209       5.987 -12.765 -32.846  1.00 84.70      A    C  
ANISOU 1472  CG  TYR A 209     8375  16474   7333   -287    753    912  A    C  
ATOM   1473  CD1 TYR A 209       6.708 -12.035 -31.905  1.00 86.14      A    C  
ANISOU 1473  CD1 TYR A 209     8485  16725   7520   -146    726    962  A    C  
ATOM   1474  CD2 TYR A 209       4.598 -12.726 -32.770  1.00 86.85      A    C  
ANISOU 1474  CD2 TYR A 209     8569  16885   7546   -456    752    899  A    C  
ATOM   1475  CE1 TYR A 209       6.067 -11.257 -30.941  1.00 86.84      A    C  
ANISOU 1475  CE1 TYR A 209     8466  16971   7559   -154    706    980  A    C  
ATOM   1476  CE2 TYR A 209       3.945 -11.947 -31.813  1.00 87.84      A    C  
ANISOU 1476  CE2 TYR A 209     8548  17206   7621   -436    740    931  A    C  
ATOM   1477  CZ  TYR A 209       4.684 -11.227 -30.890  1.00 94.19      A    C  
ANISOU 1477  CZ  TYR A 209     9325  18030   8434   -275    721    964  A    C  
ATOM   1478  OH  TYR A 209       4.041 -10.447 -29.954  1.00 94.55      A    O  
ANISOU 1478  OH  TYR A 209     9267  18250   8409   -238    717    980  A    O  
ATOM   1479  N   GLY A 210       6.120 -17.064 -33.077  1.00 83.31      A    N  
ANISOU 1479  N   GLY A 210     8961  15585   7108   -525    923    987  A    N  
ATOM   1480  CA  GLY A 210       5.211 -18.107 -32.615  1.00 85.25      A    C  
ANISOU 1480  CA  GLY A 210     9398  15709   7285   -784    959   1031  A    C  
ATOM   1481  C   GLY A 210       5.660 -18.642 -31.264  1.00 89.97      A    C  
ANISOU 1481  C   GLY A 210    10108  16205   7871   -689    994   1180  A    C  
ATOM   1482  O   GLY A 210       4.840 -18.845 -30.362  1.00 89.49      A    O  
ANISOU 1482  O   GLY A 210    10044  16205   7752   -887   1002   1256  A    O  
ATOM   1483  N   HIS A 211       6.987 -18.832 -31.112  1.00 87.01      A    N  
ANISOU 1483  N   HIS A 211     9806  15720   7535   -374   1013   1236  A    N  
ATOM   1484  CA  HIS A 211       7.614 -19.291 -29.870  1.00 87.61      A    C  
ANISOU 1484  CA  HIS A 211     9970  15731   7589   -217   1038   1394  A    C  
ATOM   1485  C   HIS A 211       7.743 -18.143 -28.858  1.00 90.26      A    C  
ANISOU 1485  C   HIS A 211     9990  16372   7931   -141    977   1446  A    C  
ATOM   1486  O   HIS A 211       7.618 -18.390 -27.657  1.00 90.09      A    O  
ANISOU 1486  O   HIS A 211     9990  16380   7862   -150    984   1567  A    O  
ATOM   1487  CB  HIS A 211       8.980 -19.942 -30.144  1.00 89.00      A    C  
ANISOU 1487  CB  HIS A 211    10339  15706   7772    114   1086   1444  A    C  
ATOM   1488  CG  HIS A 211       8.892 -21.226 -30.909  1.00 94.47      A    C  
ANISOU 1488  CG  HIS A 211    11439  16030   8425     75   1165   1407  A    C  
ATOM   1490  CD2 HIS A 211       9.223 -21.492 -32.193  1.00 96.63      A    C  
ANISOU 1490  CD2 HIS A 211    11851  16161   8702    139   1199   1285  A    C  
ATOM   1489  ND1 HIS A 211       8.432 -22.388 -30.319  1.00 98.66      A    N  
ANISOU 1489  ND1 HIS A 211    12316  16285   8887    -51   1222   1500  A    N  
ATOM   1491  CE1 HIS A 211       8.486 -23.316 -31.260  1.00100.14      A    C  
ANISOU 1491  CE1 HIS A 211    12869  16144   9036    -67   1287   1422  A    C  
ATOM   1492  NE2 HIS A 211       8.956 -22.824 -32.405  1.00 99.30      A    N  
ANISOU 1492  NE2 HIS A 211    12647  16114   8969     54   1276   1287  A    N  
ATOM   1493  N   VAL A 212       7.973 -16.892 -29.347  1.00 85.38      A    N  
ANISOU 1493  N   VAL A 212     9115  15967   7358    -80    918   1353  A    N  
ATOM   1494  CA  VAL A 212       8.099 -15.673 -28.532  1.00 83.93      A    C  
ANISOU 1494  CA  VAL A 212     8682  16044   7165    -25    857   1368  A    C  
ATOM   1495  C   VAL A 212       6.827 -15.442 -27.695  1.00 88.54      A    C  
ANISOU 1495  C   VAL A 212     9189  16764   7690   -219    858   1386  A    C  
ATOM   1496  O   VAL A 212       6.937 -15.202 -26.494  1.00 87.64      A    O  
ANISOU 1496  O   VAL A 212     9015  16759   7524   -174    846   1467  A    O  
ATOM   1497  CB  VAL A 212       8.528 -14.432 -29.373  1.00 86.00      A    C  
ANISOU 1497  CB  VAL A 212     8760  16445   7470     47    803   1262  A    C  
ATOM   1498  CG1 VAL A 212       8.320 -13.123 -28.612  1.00 84.79      A    C  
ANISOU 1498  CG1 VAL A 212     8420  16514   7284     42    745   1248  A    C  
ATOM   1499  CG2 VAL A 212       9.981 -14.551 -29.811  1.00 85.89      A    C  
ANISOU 1499  CG2 VAL A 212     8760  16393   7483    260    802   1287  A    C  
ATOM   1500  N   LEU A 213       5.636 -15.572 -28.323  1.00 86.81      A    N  
ANISOU 1500  N   LEU A 213     8962  16566   7455   -436    874   1317  A    N  
ATOM   1501  CA  LEU A 213       4.324 -15.425 -27.682  1.00 87.97      A    C  
ANISOU 1501  CA  LEU A 213     9001  16901   7523   -629    886   1340  A    C  
ATOM   1502  C   LEU A 213       4.148 -16.430 -26.533  1.00 94.60      A    C  
ANISOU 1502  C   LEU A 213     9988  17659   8297   -724    934   1481  A    C  
ATOM   1503  O   LEU A 213       3.808 -16.031 -25.419  1.00 94.01      A    O  
ANISOU 1503  O   LEU A 213     9798  17768   8153   -726    937   1545  A    O  
ATOM   1504  CB  LEU A 213       3.208 -15.637 -28.718  1.00 88.92      A    C  
ANISOU 1504  CB  LEU A 213     9089  17075   7620   -862    892   1259  A    C  
ATOM   1505  CG  LEU A 213       2.612 -14.402 -29.383  1.00 92.95      A    C  
ANISOU 1505  CG  LEU A 213     9357  17831   8126   -823    849   1157  A    C  
ATOM   1506  CD1 LEU A 213       2.022 -14.760 -30.736  1.00 94.21      A    C  
ANISOU 1506  CD1 LEU A 213     9528  17992   8275  -1009    841   1075  A    C  
ATOM   1507  CD2 LEU A 213       1.534 -13.759 -28.510  1.00 95.27      A    C  
ANISOU 1507  CD2 LEU A 213     9438  18434   8325   -844    857   1190  A    C  
ATOM   1508  N   TRP A 214       4.399 -17.728 -26.827  1.00 94.16      A    N  
ANISOU 1508  N   TRP A 214    10217  17312   8249   -791    977   1530  A    N  
ATOM   1509  CA  TRP A 214       4.335 -18.903 -25.949  1.00 96.98      A    C  
ANISOU 1509  CA  TRP A 214    10816  17493   8541   -882   1031   1677  A    C  
ATOM   1510  C   TRP A 214       5.134 -18.657 -24.657  1.00 99.78      A    C  
ANISOU 1510  C   TRP A 214    11119  17923   8871   -655   1020   1800  A    C  
ATOM   1511  O   TRP A 214       4.608 -18.875 -23.563  1.00 99.94      A    O  
ANISOU 1511  O   TRP A 214    11137  18033   8804   -763   1044   1910  A    O  
ATOM   1512  CB  TRP A 214       4.896 -20.112 -26.727  1.00 98.16      A    C  
ANISOU 1512  CB  TRP A 214    11328  17253   8714   -859   1075   1680  A    C  
ATOM   1513  CG  TRP A 214       4.703 -21.494 -26.155  1.00102.78      A    C  
ANISOU 1513  CG  TRP A 214    12274  17558   9219  -1009   1141   1814  A    C  
ATOM   1514  CD1 TRP A 214       4.540 -21.841 -24.842  1.00107.02      A    C  
ANISOU 1514  CD1 TRP A 214    12856  18127   9678  -1054   1166   1978  A    C  
ATOM   1515  CD2 TRP A 214       4.828 -22.727 -26.882  1.00105.30      A    C  
ANISOU 1515  CD2 TRP A 214    13015  17477   9518  -1091   1197   1802  A    C  
ATOM   1517  CE2 TRP A 214       4.670 -23.781 -25.953  1.00112.10      A    C  
ANISOU 1517  CE2 TRP A 214    14182  18123  10287  -1207   1254   1969  A    C  
ATOM   1518  CE3 TRP A 214       5.053 -23.044 -28.239  1.00106.91      A    C  
ANISOU 1518  CE3 TRP A 214    13396  17470   9755  -1080   1209   1663  A    C  
ATOM   1516  NE1 TRP A 214       4.491 -23.212 -24.716  1.00109.64      A    N  
ANISOU 1516  NE1 TRP A 214    13613  18100   9944  -1184   1232   2080  A    N  
ATOM   1519  CZ2 TRP A 214       4.706 -25.131 -26.340  1.00114.65      A    C  
ANISOU 1519  CZ2 TRP A 214    15016  17995  10549  -1320   1323   1998  A    C  
ATOM   1520  CZ3 TRP A 214       5.084 -24.378 -28.620  1.00111.49      A    C  
ANISOU 1520  CZ3 TRP A 214    14470  17621  10271  -1185   1277   1677  A    C  
ATOM   1521  CH2 TRP A 214       4.912 -25.404 -27.679  1.00115.00      A    C  
ANISOU 1521  CH2 TRP A 214    15247  17824  10624  -1305   1334   1841  A    C  
ATOM   1522  N   LYS A 215       6.383 -18.170 -24.788  1.00 95.03      A    N  
ANISOU 1522  N   LYS A 215    10455  17325   8329   -362    980   1783  A    N  
ATOM   1523  CA  LYS A 215       7.231 -17.864 -23.643  1.00 94.70      A    C  
ANISOU 1523  CA  LYS A 215    10338  17399   8245   -160    950   1891  A    C  
ATOM   1524  C   LYS A 215       6.765 -16.603 -22.915  1.00 98.43      A    C  
ANISOU 1524  C   LYS A 215    10547  18184   8668   -201    906   1846  A    C  
ATOM   1525  O   LYS A 215       6.566 -16.666 -21.697  1.00 99.67      A    O  
ANISOU 1525  O   LYS A 215    10690  18448   8732   -212    912   1950  A    O  
ATOM   1526  CB  LYS A 215       8.720 -17.816 -24.020  1.00 96.24      A    C  
ANISOU 1526  CB  LYS A 215    10531  17547   8487    133    920   1902  A    C  
ATOM   1527  CG  LYS A 215       9.319 -19.194 -24.324  1.00109.10      A    C  
ANISOU 1527  CG  LYS A 215    12463  18871  10119    274    983   1995  A    C  
ATOM   1528  CD  LYS A 215       9.490 -20.077 -23.077  1.00118.27      A    C  
ANISOU 1528  CD  LYS A 215    13808  19941  11188    343   1018   2196  A    C  
ATOM   1529  CE  LYS A 215       9.733 -21.532 -23.408  1.00128.85      A    C  
ANISOU 1529  CE  LYS A 215    15545  20900  12513    436   1102   2280  A    C  
ATOM   1530  NZ  LYS A 215       8.510 -22.207 -23.926  1.00137.26      A    N1+
ANISOU 1530  NZ  LYS A 215    16847  21729  13575     97   1157   2216  A    N1+
ATOM   1531  N   ALA A 216       6.510 -15.492 -23.658  1.00 92.78      A    N  
ANISOU 1531  N   ALA A 216     9654  17602   7996   -219    869   1695  A    N  
ATOM   1532  CA  ALA A 216       6.015 -14.220 -23.103  1.00 91.33      A    C  
ANISOU 1532  CA  ALA A 216     9271  17677   7753   -224    838   1630  A    C  
ATOM   1533  C   ALA A 216       4.768 -14.411 -22.235  1.00 95.87      A    C  
ANISOU 1533  C   ALA A 216     9809  18397   8222   -384    890   1686  A    C  
ATOM   1534  O   ALA A 216       4.600 -13.697 -21.246  1.00 95.48      A    O  
ANISOU 1534  O   ALA A 216     9663  18537   8077   -335    883   1697  A    O  
ATOM   1535  CB  ALA A 216       5.728 -13.227 -24.216  1.00 90.47      A    C  
ANISOU 1535  CB  ALA A 216     9046  17628   7701   -221    809   1476  A    C  
ATOM   1536  N   HIS A 217       3.934 -15.409 -22.585  1.00 93.76      A    N  
ANISOU 1536  N   HIS A 217     9628  18046   7950   -592    945   1725  A    N  
ATOM   1537  CA  HIS A 217       2.712 -15.785 -21.868  1.00 95.69      A    C  
ANISOU 1537  CA  HIS A 217     9831  18448   8078   -805   1003   1801  A    C  
ATOM   1538  C   HIS A 217       3.035 -16.463 -20.525  1.00 99.09      A    C  
ANISOU 1538  C   HIS A 217    10384  18841   8424   -796   1031   1968  A    C  
ATOM   1539  O   HIS A 217       2.379 -16.179 -19.526  1.00 99.20      A    O  
ANISOU 1539  O   HIS A 217    10289  19085   8315   -858   1064   2024  A    O  
ATOM   1540  CB  HIS A 217       1.846 -16.708 -22.750  1.00 98.57      A    C  
ANISOU 1540  CB  HIS A 217    10285  18715   8451  -1084   1040   1797  A    C  
ATOM   1541  CG  HIS A 217       0.573 -17.167 -22.104  1.00104.80      A    C  
ANISOU 1541  CG  HIS A 217    11027  19688   9104  -1368   1099   1894  A    C  
ATOM   1543  CD2 HIS A 217      -0.661 -16.612 -22.134  1.00107.52      A    C  
ANISOU 1543  CD2 HIS A 217    11115  20390   9349  -1505   1122   1868  A    C  
ATOM   1542  ND1 HIS A 217       0.522 -18.331 -21.350  1.00109.04      A    N  
ANISOU 1542  ND1 HIS A 217    11798  20054   9580  -1533   1147   2051  A    N  
ATOM   1544  CE1 HIS A 217      -0.731 -18.436 -20.937  1.00110.37      A    C  
ANISOU 1544  CE1 HIS A 217    11836  20486   9614  -1804   1195   2113  A    C  
ATOM   1545  NE2 HIS A 217      -1.482 -17.429 -21.388  1.00109.88      A    N  
ANISOU 1545  NE2 HIS A 217    11457  20771   9520  -1787   1183   2008  A    N  
ATOM   1546  N   GLN A 218       4.037 -17.357 -20.506  1.00 95.05      A    N  
ANISOU 1546  N   GLN A 218    10096  18057   7960   -696   1025   2056  A    N  
ATOM   1547  CA  GLN A 218       4.463 -18.101 -19.313  1.00 95.69      A    C  
ANISOU 1547  CA  GLN A 218    10325  18075   7957   -650   1048   2238  A    C  
ATOM   1548  C   GLN A 218       5.090 -17.205 -18.217  1.00 96.70      A    C  
ANISOU 1548  C   GLN A 218    10302  18427   8014   -452    998   2259  A    C  
ATOM   1549  O   GLN A 218       5.291 -17.665 -17.086  1.00 96.78      A    O  
ANISOU 1549  O   GLN A 218    10385  18470   7919   -427   1013   2411  A    O  
ATOM   1550  CB  GLN A 218       5.428 -19.232 -19.714  1.00 98.11      A    C  
ANISOU 1550  CB  GLN A 218    10927  18027   8322   -538   1060   2328  A    C  
ATOM   1551  CG  GLN A 218       4.774 -20.349 -20.537  1.00107.43      A    C  
ANISOU 1551  CG  GLN A 218    12363  18933   9520   -783   1122   2335  A    C  
ATOM   1552  CD  GLN A 218       5.730 -21.449 -20.947  1.00118.94      A    C  
ANISOU 1552  CD  GLN A 218    14168  20004  11019   -623   1150   2407  A    C  
ATOM   1554  NE2 GLN A 218       5.178 -22.591 -21.333  1.00109.73      A    N  
ANISOU 1554  NE2 GLN A 218    13322  18546   9823   -855   1213   2443  A    N  
ATOM   1553  OE1 GLN A 218       6.960 -21.298 -20.931  1.00112.10      A    O  
ANISOU 1553  OE1 GLN A 218    13297  19105  10193   -293   1118   2432  A    O  
ATOM   1555  N   HIS A 219       5.382 -15.930 -18.558  1.00 90.43      A    N  
ANISOU 1555  N   HIS A 219     9322  17780   7258   -330    937   2107  A    N  
ATOM   1556  CA  HIS A 219       5.985 -14.944 -17.663  1.00 89.25      A    C  
ANISOU 1556  CA  HIS A 219     9055  17827   7027   -183    878   2087  A    C  
ATOM   1557  C   HIS A 219       4.976 -14.205 -16.779  1.00 91.21      A    C  
ANISOU 1557  C   HIS A 219     9177  18340   7139   -252    909   2049  A    C  
ATOM   1558  O   HIS A 219       5.292 -13.933 -15.619  1.00 91.49      A    O  
ANISOU 1558  O   HIS A 219     9199  18517   7048   -187    890   2104  A    O  
ATOM   1559  CB  HIS A 219       6.852 -13.966 -18.459  1.00 88.52      A    C  
ANISOU 1559  CB  HIS A 219     8881  17732   7021    -50    799   1949  A    C  
ATOM   1560  CG  HIS A 219       8.235 -14.482 -18.723  1.00 92.02      A    C  
ANISOU 1560  CG  HIS A 219     9392  18055   7517    101    754   2027  A    C  
ATOM   1562  CD2 HIS A 219       8.660 -15.403 -19.619  1.00 93.81      A    C  
ANISOU 1562  CD2 HIS A 219     9739  18061   7843    156    778   2069  A    C  
ATOM   1561  ND1 HIS A 219       9.317 -14.056 -17.975  1.00 93.99      A    N  
ANISOU 1561  ND1 HIS A 219     9578  18449   7685    224    679   2074  A    N  
ATOM   1563  CE1 HIS A 219      10.362 -14.716 -18.446  1.00 93.73      A    C  
ANISOU 1563  CE1 HIS A 219     9591  18317   7706    367    661   2157  A    C  
ATOM   1564  NE2 HIS A 219      10.015 -15.539 -19.434  1.00 94.06      A    N  
ANISOU 1564  NE2 HIS A 219     9759  18122   7858    352    727   2152  A    N  
ATOM   1565  N   VAL A 220       3.771 -13.888 -17.313  1.00 85.75      A    N  
ANISOU 1565  N   VAL A 220     8386  17743   6452   -366    959   1960  A    N  
ATOM   1566  CA  VAL A 220       2.695 -13.209 -16.566  1.00 84.81      A    C  
ANISOU 1566  CA  VAL A 220     8126  17912   6184   -390   1010   1925  A    C  
ATOM   1567  C   VAL A 220       1.983 -14.153 -15.592  1.00 87.97      A    C  
ANISOU 1567  C   VAL A 220     8548  18422   6455   -550   1088   2093  A    C  
ATOM   1568  O   VAL A 220       1.736 -15.321 -15.915  1.00 88.08      A    O  
ANISOU 1568  O   VAL A 220     8669  18289   6510   -731   1123   2204  A    O  
ATOM   1569  CB  VAL A 220       1.669 -12.435 -17.439  1.00 88.01      A    C  
ANISOU 1569  CB  VAL A 220     8380  18451   6608   -402   1036   1788  A    C  
ATOM   1570  CG1 VAL A 220       2.161 -11.041 -17.786  1.00 86.05      A    C  
ANISOU 1570  CG1 VAL A 220     8117  18166   6412   -212    970   1624  A    C  
ATOM   1571  CG2 VAL A 220       1.290 -13.205 -18.697  1.00 88.32      A    C  
ANISOU 1571  CG2 VAL A 220     8426  18383   6749   -593   1059   1806  A    C  
ATOM   1572  N   ALA A 221       1.637 -13.619 -14.406  1.00 83.45      A    N  
ANISOU 1572  N   ALA A 221     7896  18102   5709   -493   1119   2107  A    N  
ATOM   1573  CA  ALA A 221       0.929 -14.322 -13.347  1.00 84.39      A    C  
ANISOU 1573  CA  ALA A 221     8006  18391   5667   -635   1200   2266  A    C  
ATOM   1574  C   ALA A 221      -0.515 -14.633 -13.766  1.00 88.03      A    C  
ANISOU 1574  C   ALA A 221     8324  19037   6084   -850   1289   2285  A    C  
ATOM   1575  O   ALA A 221      -1.100 -13.893 -14.556  1.00 85.71      A    O  
ANISOU 1575  O   ALA A 221     7880  18861   5825   -805   1293   2150  A    O  
ATOM   1576  CB  ALA A 221       0.939 -13.475 -12.088  1.00 85.69      A    C  
ANISOU 1576  CB  ALA A 221     8110  18805   5642   -488   1211   2239  A    C  
ATOM   1577  N   SER A 222      -1.081 -15.734 -13.244  1.00 87.29      A    N  
ANISOU 1577  N   SER A 222     8281  18987   5900  -1096   1357   2466  A    N  
ATOM   1578  CA  SER A 222      -2.456 -16.170 -13.527  1.00 89.00      A    C  
ANISOU 1578  CA  SER A 222     8351  19430   6034  -1379   1439   2521  A    C  
ATOM   1579  C   SER A 222      -3.119 -16.728 -12.253  1.00 96.66      A    C  
ANISOU 1579  C   SER A 222     9288  20650   6788  -1549   1530   2706  A    C  
ATOM   1580  O   SER A 222      -4.179 -17.359 -12.322  1.00 98.62      A    O  
ANISOU 1580  O   SER A 222     9447  21083   6940  -1862   1601   2808  A    O  
ATOM   1581  CB  SER A 222      -2.454 -17.225 -14.631  1.00 91.74      A    C  
ANISOU 1581  CB  SER A 222     8864  19474   6518  -1635   1419   2558  A    C  
ATOM   1582  OG  SER A 222      -1.760 -18.395 -14.227  1.00 98.81      A    O  
ANISOU 1582  OG  SER A 222    10067  20042   7432  -1731   1417   2720  A    O  
ATOM   2854  N   ALA A 235       4.196  -9.477 -13.361  1.00 87.84      A    N  
ANISOU 2854  N   ALA A 235     8536  18744   6094     74    872   1667  A    N  
ATOM   2855  CA  ALA A 235       5.035 -10.228 -14.307  1.00 86.67      A    C  
ANISOU 2855  CA  ALA A 235     8412  18382   6138     27    817   1733  A    C  
ATOM   2856  C   ALA A 235       6.528 -10.075 -14.032  1.00 91.10      A    C  
ANISOU 2856  C   ALA A 235     9027  18894   6692     74    705   1754  A    C  
ATOM   2857  O   ALA A 235       6.989  -8.965 -13.747  1.00 90.67      A    O  
ANISOU 2857  O   ALA A 235     9002  18900   6548    110    642   1635  A    O  
ATOM   2858  CB  ALA A 235       4.752  -9.766 -15.735  1.00 85.69      A    C  
ANISOU 2858  CB  ALA A 235     8252  18139   6168     36    816   1611  A    C  
ATOM   2859  N   ARG A 236       7.294 -11.175 -14.181  1.00 88.58      A    N  
ANISOU 2859  N   ARG A 236     8733  18470   6454     73    680   1906  A    N  
ATOM   2860  CA  ARG A 236       8.754 -11.117 -14.073  1.00 89.03      A    C  
ANISOU 2860  CA  ARG A 236     8789  18535   6504    138    574   1951  A    C  
ATOM   2861  C   ARG A 236       9.272 -10.575 -15.416  1.00 91.64      A    C  
ANISOU 2861  C   ARG A 236     9090  18744   6986    152    529   1833  A    C  
ATOM   2862  O   ARG A 236       8.786 -11.011 -16.470  1.00 89.81      A    O  
ANISOU 2862  O   ARG A 236     8867  18355   6903    141    582   1815  A    O  
ATOM   2863  CB  ARG A 236       9.385 -12.472 -13.670  1.00 91.55      A    C  
ANISOU 2863  CB  ARG A 236     9149  18814   6820    197    576   2175  A    C  
ATOM   2864  CG  ARG A 236       9.009 -13.681 -14.518  1.00105.28      A    C  
ANISOU 2864  CG  ARG A 236    10975  20319   8709    189    656   2262  A    C  
ATOM   2865  CD  ARG A 236       9.601 -14.956 -13.946  1.00122.42      A    C  
ANISOU 2865  CD  ARG A 236    13252  22422  10840    283    667   2491  A    C  
ATOM   2866  NE  ARG A 236       9.218 -16.134 -14.726  1.00138.07      A    N  
ANISOU 2866  NE  ARG A 236    15391  24126  12944    262    749   2561  A    N  
ATOM   2867  CZ  ARG A 236       9.215 -17.380 -14.260  1.00155.63      A    C  
ANISOU 2867  CZ  ARG A 236    17799  26203  15131    301    800   2760  A    C  
ATOM   2868  NH1 ARG A 236       9.570 -17.629 -13.005  1.00144.61      A    N1+
ANISOU 2868  NH1 ARG A 236    16422  24942  13583    384    777   2927  A    N1+
ATOM   2869  NH2 ARG A 236       8.850 -18.387 -15.043  1.00143.60      A    N  
ANISOU 2869  NH2 ARG A 236    16469  24387  13705    251    874   2794  A    N  
ATOM   2870  N   MET A 237      10.180  -9.564 -15.377  1.00 88.81      A    N  
ANISOU 2870  N   MET A 237     8705  18470   6568    146    430   1745  A    N  
ATOM   2871  CA  MET A 237      10.719  -8.861 -16.567  1.00 87.62      A    C  
ANISOU 2871  CA  MET A 237     8529  18237   6526    131    381   1632  A    C  
ATOM   2872  C   MET A 237       9.532  -8.297 -17.351  1.00 87.92      A    C  
ANISOU 2872  C   MET A 237     8606  18157   6643    113    450   1489  A    C  
ATOM   2873  O   MET A 237       9.301  -8.733 -18.475  1.00 86.49      A    O  
ANISOU 2873  O   MET A 237     8405  17844   6615    126    487   1484  A    O  
ATOM   2874  CB  MET A 237      11.539  -9.798 -17.490  1.00 90.13      A    C  
ANISOU 2874  CB  MET A 237     8791  18472   6982    204    374   1739  A    C  
ATOM   2875  CG  MET A 237      12.767 -10.412 -16.858  1.00 96.33      A    C  
ANISOU 2875  CG  MET A 237     9517  19400   7685    287    317   1913  A    C  
ATOM   2876  SD  MET A 237      13.211 -12.016 -17.605  1.00102.00      A    S  
ANISOU 2876  SD  MET A 237    10249  19963   8543    464    376   2073  A    S  
ATOM   2877  CE  MET A 237      13.542 -11.545 -19.287  1.00 97.19      A    C  
ANISOU 2877  CE  MET A 237     9549  19332   8048    462    339   1958  A    C  
ATOM   2878  N   ARG A 238       8.735  -7.396 -16.747  1.00 83.01      A    N  
ANISOU 2878  N   ARG A 238     8043  17597   5898    106    473   1381  A    N  
ATOM   2879  CA  ARG A 238       7.546  -6.917 -17.443  1.00 81.66      A    C  
ANISOU 2879  CA  ARG A 238     7886  17367   5774    140    547   1270  A    C  
ATOM   2880  C   ARG A 238       7.840  -5.901 -18.583  1.00 83.99      A    C  
ANISOU 2880  C   ARG A 238     8229  17540   6141    143    503   1138  A    C  
ATOM   2881  O   ARG A 238       7.053  -5.871 -19.531  1.00 83.01      A    O  
ANISOU 2881  O   ARG A 238     8076  17351   6111    181    555   1092  A    O  
ATOM   2882  CB  ARG A 238       6.452  -6.415 -16.488  1.00 81.47      A    C  
ANISOU 2882  CB  ARG A 238     7899  17473   5583    193    616   1217  A    C  
ATOM   2883  CG  ARG A 238       6.803  -5.219 -15.652  1.00 86.03      A    C  
ANISOU 2883  CG  ARG A 238     8615  18095   5977    210    566   1105  A    C  
ATOM   2884  CD  ARG A 238       5.535  -4.554 -15.187  1.00 86.38      A    C  
ANISOU 2884  CD  ARG A 238     8713  18231   5878    331    662   1016  A    C  
ATOM   2885  NE  ARG A 238       5.653  -3.108 -15.311  1.00 91.82      A    N  
ANISOU 2885  NE  ARG A 238     9599  18818   6470    395    635    842  A    N  
ATOM   2886  CZ  ARG A 238       5.214  -2.411 -16.351  1.00108.77      A    C  
ANISOU 2886  CZ  ARG A 238    11794  20846   8687    487    661    751  A    C  
ATOM   2887  NH1 ARG A 238       5.382  -1.098 -16.394  1.00100.28      A    N1+
ANISOU 2887  NH1 ARG A 238    10959  19639   7504    545    638    603  A    N1+
ATOM   2888  NH2 ARG A 238       4.596  -3.021 -17.354  1.00 96.12      A    N  
ANISOU 2888  NH2 ARG A 238    10024  19250   7247    513    708    810  A    N  
ATOM   2889  N   LEU A 239       8.959  -5.130 -18.536  1.00 79.81      A    N  
ANISOU 2889  N   LEU A 239     7766  16998   5559     81    405   1090  A    N  
ATOM   2890  CA  LEU A 239       9.310  -4.194 -19.625  1.00 78.33      A    C  
ANISOU 2890  CA  LEU A 239     7645  16689   5430     48    362    987  A    C  
ATOM   2891  C   LEU A 239       9.855  -4.925 -20.854  1.00 80.86      A    C  
ANISOU 2891  C   LEU A 239     7847  16945   5932     36    355   1053  A    C  
ATOM   2892  O   LEU A 239       9.775  -4.412 -21.979  1.00 78.84      A    O  
ANISOU 2892  O   LEU A 239     7617  16584   5754     34    353    983  A    O  
ATOM   2893  CB  LEU A 239      10.235  -3.044 -19.189  1.00 79.38      A    C  
ANISOU 2893  CB  LEU A 239     7909  16833   5418    -73    262    912  A    C  
ATOM   2894  CG  LEU A 239       9.679  -2.041 -18.145  1.00 85.71      A    C  
ANISOU 2894  CG  LEU A 239     8918  17635   6014    -58    271    794  A    C  
ATOM   2895  CD1 LEU A 239      10.728  -1.017 -17.775  1.00 87.29      A    C  
ANISOU 2895  CD1 LEU A 239     9261  17852   6055   -247    155    734  A    C  
ATOM   2896  CD2 LEU A 239       8.427  -1.313 -18.639  1.00 87.35      A    C  
ANISOU 2896  CD2 LEU A 239     9272  17698   6220     83    350    670  A    C  
ATOM   2897  N   ASP A 240      10.372  -6.145 -20.632  1.00 78.51      A    N  
ANISOU 2897  N   ASP A 240     7441  16702   5685     50    358   1191  A    N  
ATOM   2898  CA  ASP A 240      10.858  -7.038 -21.674  1.00 77.90      A    C  
ANISOU 2898  CA  ASP A 240     7282  16558   5758     81    372   1259  A    C  
ATOM   2899  C   ASP A 240       9.676  -7.783 -22.295  1.00 81.02      A    C  
ANISOU 2899  C   ASP A 240     7680  16848   6258    118    466   1256  A    C  
ATOM   2900  O   ASP A 240       9.648  -7.951 -23.514  1.00 80.19      A    O  
ANISOU 2900  O   ASP A 240     7558  16645   6266    124    483   1227  A    O  
ATOM   2901  CB  ASP A 240      11.927  -8.001 -21.129  1.00 81.08      A    C  
ANISOU 2901  CB  ASP A 240     7609  17056   6142    124    342   1414  A    C  
ATOM   2902  CG  ASP A 240      13.359  -7.509 -21.319  1.00 99.17      A    C  
ANISOU 2902  CG  ASP A 240     9820  19487   8375     78    244   1435  A    C  
ATOM   2903  OD1 ASP A 240      13.598  -6.694 -22.253  1.00100.85      A    O  
ANISOU 2903  OD1 ASP A 240    10035  19665   8617      3    213   1344  A    O  
ATOM   2904  OD2 ASP A 240      14.244  -7.949 -20.554  1.00107.73      A    O1-
ANISOU 2904  OD2 ASP A 240    10827  20737   9369    109    198   1557  A    O1-
ATOM   2905  N   VAL A 241       8.678  -8.182 -21.467  1.00 77.98      A    N  
ANISOU 2905  N   VAL A 241     7308  16509   5813    119    525   1285  A    N  
ATOM   2906  CA  VAL A 241       7.445  -8.846 -21.928  1.00 77.58      A    C  
ANISOU 2906  CA  VAL A 241     7239  16418   5820     97    608   1288  A    C  
ATOM   2907  C   VAL A 241       6.572  -7.848 -22.714  1.00 81.57      A    C  
ANISOU 2907  C   VAL A 241     7729  16932   6331    118    622   1157  A    C  
ATOM   2908  O   VAL A 241       6.089  -8.189 -23.799  1.00 80.60      A    O  
ANISOU 2908  O   VAL A 241     7570  16756   6297     93    650   1135  A    O  
ATOM   2909  CB  VAL A 241       6.660  -9.593 -20.805  1.00 81.80      A    C  
ANISOU 2909  CB  VAL A 241     7770  17042   6267     61    670   1382  A    C  
ATOM   2910  CG1 VAL A 241       5.336 -10.149 -21.324  1.00 81.62      A    C  
ANISOU 2910  CG1 VAL A 241     7704  17033   6276    -19    748   1382  A    C  
ATOM   2911  CG2 VAL A 241       7.493 -10.724 -20.214  1.00 82.21      A    C  
ANISOU 2911  CG2 VAL A 241     7868  17048   6320     65    662   1534  A    C  
ATOM   2912  N   GLU A 242       6.435  -6.606 -22.203  1.00 79.33      A    N  
ANISOU 2912  N   GLU A 242     7498  16704   5939    173    598   1071  A    N  
ATOM   2913  CA  GLU A 242       5.657  -5.561 -22.871  1.00 79.98      A    C  
ANISOU 2913  CA  GLU A 242     7609  16779   6001    248    615    959  A    C  
ATOM   2914  C   GLU A 242       6.262  -5.143 -24.241  1.00 82.72      A    C  
ANISOU 2914  C   GLU A 242     7977  16994   6460    233    569    911  A    C  
ATOM   2915  O   GLU A 242       5.506  -4.752 -25.130  1.00 80.19      A    O  
ANISOU 2915  O   GLU A 242     7633  16669   6168    285    597    862  A    O  
ATOM   2916  CB  GLU A 242       5.394  -4.351 -21.948  1.00 82.69      A    C  
ANISOU 2916  CB  GLU A 242     8078  17164   6178    335    612    875  A    C  
ATOM   2917  CG  GLU A 242       6.561  -3.388 -21.788  1.00 96.08      A    C  
ANISOU 2917  CG  GLU A 242     9929  18747   7831    287    523    809  A    C  
ATOM   2918  CD  GLU A 242       6.202  -1.923 -21.634  1.00123.66      A    C  
ANISOU 2918  CD  GLU A 242    13631  22188  11167    378    527    685  A    C  
ATOM   2919  OE1 GLU A 242       5.383  -1.595 -20.745  1.00124.68      A    O  
ANISOU 2919  OE1 GLU A 242    13798  22415  11159    486    588    660  A    O  
ATOM   2920  OE2 GLU A 242       6.762  -1.099 -22.393  1.00116.57      A    O1-
ANISOU 2920  OE2 GLU A 242    12883  21142  10267    340    473    616  A    O1-
ATOM   2921  N   LEU A 243       7.610  -5.240 -24.409  1.00 81.06      A    N  
ANISOU 2921  N   LEU A 243     7788  16716   6295    165    502    937  A    N  
ATOM   2922  CA  LEU A 243       8.287  -4.925 -25.679  1.00 80.48      A    C  
ANISOU 2922  CA  LEU A 243     7717  16550   6311    136    465    908  A    C  
ATOM   2923  C   LEU A 243       8.002  -6.003 -26.723  1.00 82.34      A    C  
ANISOU 2923  C   LEU A 243     7864  16748   6674    133    508    946  A    C  
ATOM   2924  O   LEU A 243       7.816  -5.677 -27.893  1.00 79.84      A    O  
ANISOU 2924  O   LEU A 243     7543  16380   6412    140    509    897  A    O  
ATOM   2925  CB  LEU A 243       9.798  -4.713 -25.499  1.00 81.22      A    C  
ANISOU 2925  CB  LEU A 243     7818  16657   6385     57    388    940  A    C  
ATOM   2926  CG  LEU A 243      10.291  -3.257 -25.577  1.00 87.51      A    C  
ANISOU 2926  CG  LEU A 243     8753  17427   7072    -15    323    862  A    C  
ATOM   2927  CD1 LEU A 243      11.587  -3.064 -24.799  1.00 88.72      A    C  
ANISOU 2927  CD1 LEU A 243     8876  17688   7146   -138    240    916  A    C  
ATOM   2928  CD2 LEU A 243      10.485  -2.808 -27.016  1.00 90.66      A    C  
ANISOU 2928  CD2 LEU A 243     9209  17718   7519    -34    312    805  A    C  
ATOM   2929  N   ALA A 244       7.911  -7.282 -26.278  1.00 80.07      A    N  
ANISOU 2929  N   ALA A 244     7536  16474   6412    116    545   1032  A    N  
ATOM   2930  CA  ALA A 244       7.559  -8.440 -27.111  1.00 79.82      A    C  
ANISOU 2930  CA  ALA A 244     7484  16371   6471     84    592   1063  A    C  
ATOM   2931  C   ALA A 244       6.093  -8.316 -27.544  1.00 83.22      A    C  
ANISOU 2931  C   ALA A 244     7872  16858   6889     50    634   1012  A    C  
ATOM   2932  O   ALA A 244       5.731  -8.773 -28.626  1.00 82.56      A    O  
ANISOU 2932  O   ALA A 244     7775  16730   6865      2    650    987  A    O  
ATOM   2933  CB  ALA A 244       7.769  -9.735 -26.337  1.00 81.39      A    C  
ANISOU 2933  CB  ALA A 244     7715  16543   6667     70    623   1176  A    C  
ATOM   2934  N   LYS A 245       5.256  -7.681 -26.697  1.00 80.09      A    N  
ANISOU 2934  N   LYS A 245     7446  16591   6393     83    653    998  A    N  
ATOM   2935  CA  LYS A 245       3.841  -7.419 -26.990  1.00 79.79      A    C  
ANISOU 2935  CA  LYS A 245     7321  16692   6304     90    695    965  A    C  
ATOM   2936  C   LYS A 245       3.701  -6.281 -28.023  1.00 81.78      A    C  
ANISOU 2936  C   LYS A 245     7576  16935   6560    187    668    879  A    C  
ATOM   2937  O   LYS A 245       2.732  -6.279 -28.774  1.00 82.33      A    O  
ANISOU 2937  O   LYS A 245     7555  17108   6620    184    688    862  A    O  
ATOM   2938  CB  LYS A 245       3.071  -7.060 -25.704  1.00 82.59      A    C  
ANISOU 2938  CB  LYS A 245     7639  17218   6525    147    736    984  A    C  
ATOM   2939  CG  LYS A 245       2.405  -8.236 -24.999  1.00 86.77      A    C  
ANISOU 2939  CG  LYS A 245     8102  17849   7019     17    792   1080  A    C  
ATOM   2940  CD  LYS A 245       1.692  -7.781 -23.728  1.00 90.48      A    C  
ANISOU 2940  CD  LYS A 245     8520  18524   7335     92    841   1099  A    C  
ATOM   2941  CE  LYS A 245       0.654  -8.763 -23.237  1.00 97.26      A    C  
ANISOU 2941  CE  LYS A 245     9267  19560   8126    -58    909   1196  A    C  
ATOM   2942  NZ  LYS A 245      -0.100  -8.238 -22.058  1.00101.91      A    N1+
ANISOU 2942  NZ  LYS A 245     9777  20401   8543     43    970   1212  A    N1+
ATOM   2943  N   THR A 246       4.651  -5.313 -28.044  1.00 76.45      A    N  
ANISOU 2943  N   THR A 246     7013  16154   5881    256    619    834  A    N  
ATOM   2944  CA  THR A 246       4.637  -4.157 -28.954  1.00 75.74      A    C  
ANISOU 2944  CA  THR A 246     6986  16012   5780    343    592    767  A    C  
ATOM   2945  C   THR A 246       5.087  -4.551 -30.379  1.00 80.00      A    C  
ANISOU 2945  C   THR A 246     7494  16475   6427    274    569    763  A    C  
ATOM   2946  O   THR A 246       4.505  -4.084 -31.363  1.00 79.64      A    O  
ANISOU 2946  O   THR A 246     7427  16460   6374    327    570    732  A    O  
ATOM   2947  CB  THR A 246       5.431  -2.988 -28.345  1.00 77.42      A    C  
ANISOU 2947  CB  THR A 246     7370  16125   5922    382    550    726  A    C  
ATOM   2949  CG2 THR A 246       5.321  -1.699 -29.162  1.00 74.19      A    C  
ANISOU 2949  CG2 THR A 246     7092  15626   5472    475    531    664  A    C  
ATOM   2948  OG1 THR A 246       4.933  -2.742 -27.033  1.00 77.86      A    O  
ANISOU 2948  OG1 THR A 246     7463  16258   5862    447    579    720  A    O  
ATOM   2950  N   LEU A 247       6.108  -5.421 -30.467  1.00 76.47      A    N  
ANISOU 2950  N   LEU A 247     7047  15947   6061    181    554    800  A    N  
ATOM   2951  CA  LEU A 247       6.678  -5.951 -31.701  1.00 75.88      A    C  
ANISOU 2951  CA  LEU A 247     6958  15801   6073    131    547    797  A    C  
ATOM   2952  C   LEU A 247       5.617  -6.725 -32.495  1.00 79.67      A    C  
ANISOU 2952  C   LEU A 247     7370  16328   6572     81    582    784  A    C  
ATOM   2953  O   LEU A 247       5.575  -6.607 -33.727  1.00 79.47      A    O  
ANISOU 2953  O   LEU A 247     7336  16287   6571     73    572    747  A    O  
ATOM   2954  CB  LEU A 247       7.911  -6.834 -31.375  1.00 76.16      A    C  
ANISOU 2954  CB  LEU A 247     7005  15776   6157     99    543    856  A    C  
ATOM   2955  CG  LEU A 247       8.394  -7.814 -32.457  1.00 81.28      A    C  
ANISOU 2955  CG  LEU A 247     7652  16352   6878     85    565    861  A    C  
ATOM   2956  CD1 LEU A 247       9.179  -7.107 -33.537  1.00 81.00      A    C  
ANISOU 2956  CD1 LEU A 247     7611  16312   6854    100    534    834  A    C  
ATOM   2957  CD2 LEU A 247       9.205  -8.935 -31.853  1.00 85.56      A    C  
ANISOU 2957  CD2 LEU A 247     8221  16847   7443    110    590    939  A    C  
ATOM   2958  N   GLY A 248       4.775  -7.481 -31.779  1.00 75.61      A    N  
ANISOU 2958  N   GLY A 248     6810  15889   6028     24    619    818  A    N  
ATOM   2959  CA  GLY A 248       3.686  -8.263 -32.356  1.00 75.69      A    C  
ANISOU 2959  CA  GLY A 248     6751  15983   6024    -89    646    813  A    C  
ATOM   2960  C   GLY A 248       2.650  -7.413 -33.057  1.00 78.51      A    C  
ANISOU 2960  C   GLY A 248     7002  16513   6315    -34    634    774  A    C  
ATOM   2961  O   GLY A 248       2.132  -7.805 -34.107  1.00 78.52      A    O  
ANISOU 2961  O   GLY A 248     6951  16573   6310   -124    627    749  A    O  
ATOM   2962  N   LEU A 249       2.360  -6.226 -32.491  1.00 73.90      A    N  
ANISOU 2962  N   LEU A 249     6406  16011   5663    130    631    769  A    N  
ATOM   2963  CA  LEU A 249       1.410  -5.284 -33.088  1.00 73.60      A    C  
ANISOU 2963  CA  LEU A 249     6289  16136   5540    263    626    748  A    C  
ATOM   2964  C   LEU A 249       2.025  -4.567 -34.315  1.00 75.54      A    C  
ANISOU 2964  C   LEU A 249     6619  16258   5825    324    583    710  A    C  
ATOM   2965  O   LEU A 249       1.309  -4.253 -35.261  1.00 74.87      A    O  
ANISOU 2965  O   LEU A 249     6457  16299   5691    374    571    704  A    O  
ATOM   2966  CB  LEU A 249       0.867  -4.302 -32.029  1.00 74.13      A    C  
ANISOU 2966  CB  LEU A 249     6362  16308   5496    457    655    755  A    C  
ATOM   2967  CG  LEU A 249       0.153  -4.951 -30.815  1.00 79.26      A    C  
ANISOU 2967  CG  LEU A 249     6899  17141   6077    407    709    803  A    C  
ATOM   2968  CD1 LEU A 249      -0.137  -3.938 -29.727  1.00 79.58      A    C  
ANISOU 2968  CD1 LEU A 249     6996  17239   6001    623    744    794  A    C  
ATOM   2969  CD2 LEU A 249      -1.124  -5.674 -31.225  1.00 82.32      A    C  
ANISOU 2969  CD2 LEU A 249     7059  17822   6397    304    732    843  A    C  
ATOM   2970  N   VAL A 250       3.361  -4.371 -34.307  1.00 70.88      A    N  
ANISOU 2970  N   VAL A 250     6169  15455   5307    304    559    697  A    N  
ATOM   2971  CA  VAL A 250       4.147  -3.754 -35.382  1.00 69.87      A    C  
ANISOU 2971  CA  VAL A 250     6127  15211   5210    320    523    676  A    C  
ATOM   2972  C   VAL A 250       4.212  -4.724 -36.580  1.00 73.62      A    C  
ANISOU 2972  C   VAL A 250     6537  15695   5740    203    522    662  A    C  
ATOM   2973  O   VAL A 250       4.014  -4.296 -37.724  1.00 73.39      A    O  
ANISOU 2973  O   VAL A 250     6500  15697   5688    232    502    646  A    O  
ATOM   2974  CB  VAL A 250       5.551  -3.318 -34.866  1.00 72.78      A    C  
ANISOU 2974  CB  VAL A 250     6626  15418   5610    294    498    680  A    C  
ATOM   2975  CG1 VAL A 250       6.480  -2.895 -36.004  1.00 72.02      A    C  
ANISOU 2975  CG1 VAL A 250     6593  15235   5537    262    468    675  A    C  
ATOM   2976  CG2 VAL A 250       5.433  -2.199 -33.835  1.00 73.09      A    C  
ANISOU 2976  CG2 VAL A 250     6781  15428   5563    390    493    672  A    C  
ATOM   2977  N   LEU A 251       4.452  -6.029 -36.299  1.00 69.86      A    N  
ANISOU 2977  N   LEU A 251     6042  15183   5319     79    547    668  A    N  
ATOM   2978  CA  LEU A 251       4.503  -7.117 -37.278  1.00 69.75      A    C  
ANISOU 2978  CA  LEU A 251     6027  15137   5337    -40    559    640  A    C  
ATOM   2979  C   LEU A 251       3.144  -7.297 -37.977  1.00 76.09      A    C  
ANISOU 2979  C   LEU A 251     6724  16123   6066   -112    550    619  A    C  
ATOM   2980  O   LEU A 251       3.110  -7.469 -39.201  1.00 77.57      A    O  
ANISOU 2980  O   LEU A 251     6912  16321   6238   -166    535    578  A    O  
ATOM   2981  CB  LEU A 251       4.971  -8.428 -36.604  1.00 70.00      A    C  
ANISOU 2981  CB  LEU A 251     6125  15053   5418   -128    596    663  A    C  
ATOM   2982  CG  LEU A 251       4.869  -9.743 -37.399  1.00 76.00      A    C  
ANISOU 2982  CG  LEU A 251     6959  15733   6186   -262    624    626  A    C  
ATOM   2983  CD1 LEU A 251       5.841  -9.774 -38.568  1.00 76.55      A    C  
ANISOU 2983  CD1 LEU A 251     7093  15709   6283   -210    626    582  A    C  
ATOM   2984  CD2 LEU A 251       5.148 -10.926 -36.523  1.00 79.28      A    C  
ANISOU 2984  CD2 LEU A 251     7484  16010   6627   -318    667    668  A    C  
ATOM   2985  N   ALA A 252       2.036  -7.229 -37.209  1.00 72.65      A    N  
ANISOU 2985  N   ALA A 252     6177  15867   5560   -114    559    650  A    N  
ATOM   2986  CA  ALA A 252       0.668  -7.368 -37.723  1.00 73.36      A    C  
ANISOU 2986  CA  ALA A 252     6105  16221   5546   -189    547    652  A    C  
ATOM   2987  C   ALA A 252       0.324  -6.264 -38.735  1.00 76.93      A    C  
ANISOU 2987  C   ALA A 252     6497  16797   5935    -36    509    645  A    C  
ATOM   2988  O   ALA A 252      -0.155  -6.580 -39.824  1.00 77.68      A    O  
ANISOU 2988  O   ALA A 252     6521  17015   5977   -136    480    622  A    O  
ATOM   2989  CB  ALA A 252      -0.326  -7.372 -36.572  1.00 75.02      A    C  
ANISOU 2989  CB  ALA A 252     6183  16643   5678   -182    575    706  A    C  
ATOM   2990  N   VAL A 253       0.616  -4.988 -38.395  1.00 72.68      A    N  
ANISOU 2990  N   VAL A 253     6020  16205   5391    196    507    665  A    N  
ATOM   2991  CA  VAL A 253       0.402  -3.822 -39.260  1.00 73.10      A    C  
ANISOU 2991  CA  VAL A 253     6082  16316   5377    379    478    677  A    C  
ATOM   2992  C   VAL A 253       1.206  -3.986 -40.583  1.00 80.26      A    C  
ANISOU 2992  C   VAL A 253     7067  17096   6332    290    448    643  A    C  
ATOM   2993  O   VAL A 253       0.640  -3.759 -41.660  1.00 80.58      A    O  
ANISOU 2993  O   VAL A 253     7035  17288   6295    318    417    649  A    O  
ATOM   2994  CB  VAL A 253       0.696  -2.487 -38.513  1.00 75.63      A    C  
ANISOU 2994  CB  VAL A 253     6545  16518   5672    616    490    699  A    C  
ATOM   2995  CG1 VAL A 253       0.747  -1.299 -39.464  1.00 76.00      A    C  
ANISOU 2995  CG1 VAL A 253     6686  16537   5654    796    463    720  A    C  
ATOM   2996  CG2 VAL A 253      -0.330  -2.233 -37.422  1.00 76.04      A    C  
ANISOU 2996  CG2 VAL A 253     6505  16754   5634    751    529    728  A    C  
ATOM   2997  N   LEU A 254       2.487  -4.448 -40.490  1.00 78.17      A    N  
ANISOU 2997  N   LEU A 254     6928  16596   6176    192    461    613  A    N  
ATOM   2998  CA  LEU A 254       3.392  -4.699 -41.628  1.00 78.81      A    C  
ANISOU 2998  CA  LEU A 254     7081  16566   6297    121    452    581  A    C  
ATOM   2999  C   LEU A 254       2.775  -5.687 -42.623  1.00 85.11      A    C  
ANISOU 2999  C   LEU A 254     7804  17484   7049    -28    443    534  A    C  
ATOM   3000  O   LEU A 254       2.665  -5.370 -43.810  1.00 85.27      A    O  
ANISOU 3000  O   LEU A 254     7809  17581   7009    -14    416    524  A    O  
ATOM   3001  CB  LEU A 254       4.778  -5.198 -41.145  1.00 78.34      A    C  
ANISOU 3001  CB  LEU A 254     7123  16303   6338     68    481    572  A    C  
ATOM   3002  CG  LEU A 254       5.875  -5.381 -42.222  1.00 83.78      A    C  
ANISOU 3002  CG  LEU A 254     7873  16906   7053     33    491    549  A    C  
ATOM   3003  CD1 LEU A 254       6.739  -4.126 -42.373  1.00 83.87      A    C  
ANISOU 3003  CD1 LEU A 254     7947  16864   7055    105    472    591  A    C  
ATOM   3004  CD2 LEU A 254       6.775  -6.563 -41.890  1.00 86.47      A    C  
ANISOU 3004  CD2 LEU A 254     8262  17130   7463    -20    536    533  A    C  
ATOM   3005  N   LEU A 255       2.324  -6.853 -42.122  1.00 82.80      A    N  
ANISOU 3005  N   LEU A 255     7484  17212   6765   -186    464    510  A    N  
ATOM   3006  CA  LEU A 255       1.701  -7.915 -42.915  1.00 83.79      A    C  
ANISOU 3006  CA  LEU A 255     7584  17426   6828   -394    454    455  A    C  
ATOM   3007  C   LEU A 255       0.338  -7.514 -43.510  1.00 87.43      A    C  
ANISOU 3007  C   LEU A 255     7855  18217   7149   -418    402    474  A    C  
ATOM   3008  O   LEU A 255      -0.079  -8.102 -44.511  1.00 88.64      A    O  
ANISOU 3008  O   LEU A 255     7986  18473   7218   -584    373    423  A    O  
ATOM   3009  CB  LEU A 255       1.601  -9.209 -42.088  1.00 84.76      A    C  
ANISOU 3009  CB  LEU A 255     7772  17451   6980   -576    492    441  A    C  
ATOM   3010  CG  LEU A 255       2.735 -10.249 -42.224  1.00 89.71      A    C  
ANISOU 3010  CG  LEU A 255     8619  17785   7683   -631    541    391  A    C  
ATOM   3011  CD1 LEU A 255       4.113  -9.646 -41.968  1.00 88.98      A    C  
ANISOU 3011  CD1 LEU A 255     8590  17532   7688   -422    565    420  A    C  
ATOM   3012  CD2 LEU A 255       2.528 -11.392 -41.246  1.00 92.84      A    C  
ANISOU 3012  CD2 LEU A 255     9109  18073   8092   -785    579    404  A    C  
ATOM   3013  N   ILE A 256      -0.347  -6.509 -42.913  1.00 81.94      A    N  
ANISOU 3013  N   ILE A 256     7026  17702   6405   -238    392    548  A    N  
ATOM   3014  CA  ILE A 256      -1.630  -6.012 -43.435  1.00 81.82      A    C  
ANISOU 3014  CA  ILE A 256     6799  18054   6236   -183    347    593  A    C  
ATOM   3015  C   ILE A 256      -1.355  -5.047 -44.609  1.00 84.66      A    C  
ANISOU 3015  C   ILE A 256     7197  18417   6554     -8    311    608  A    C  
ATOM   3016  O   ILE A 256      -1.944  -5.212 -45.673  1.00 84.83      A    O  
ANISOU 3016  O   ILE A 256     7114  18655   6461    -86    263    601  A    O  
ATOM   3017  CB  ILE A 256      -2.541  -5.397 -42.306  1.00 84.36      A    C  
ANISOU 3017  CB  ILE A 256     6966  18591   6495    -12    369    673  A    C  
ATOM   3018  CG1 ILE A 256      -3.107  -6.489 -41.367  1.00 84.98      A    C  
ANISOU 3018  CG1 ILE A 256     6946  18784   6559   -252    396    675  A    C  
ATOM   3019  CG2 ILE A 256      -3.673  -4.516 -42.855  1.00 84.52      A    C  
ANISOU 3019  CG2 ILE A 256     6784  18984   6348    198    334    747  A    C  
ATOM   3020  CD1 ILE A 256      -3.486  -5.999 -39.934  1.00 85.78      A    C  
ANISOU 3020  CD1 ILE A 256     6981  18962   6649    -85    448    738  A    C  
ATOM   3021  N   CYS A 257      -0.441  -4.072 -44.410  1.00 80.28      A    N  
ANISOU 3021  N   CYS A 257     6803  17624   6075    197    332    632  A    N  
ATOM   3022  CA  CYS A 257      -0.097  -3.007 -45.357  1.00 80.80      A    C  
ANISOU 3022  CA  CYS A 257     6955  17647   6100    368    307    669  A    C  
ATOM   3023  C   CYS A 257       0.665  -3.464 -46.601  1.00 84.82      A    C  
ANISOU 3023  C   CYS A 257     7541  18064   6624    225    293    615  A    C  
ATOM   3024  O   CYS A 257       0.456  -2.895 -47.679  1.00 84.60      A    O  
ANISOU 3024  O   CYS A 257     7504  18138   6501    306    257    650  A    O  
ATOM   3025  CB  CYS A 257       0.650  -1.888 -44.644  1.00 80.78      A    C  
ANISOU 3025  CB  CYS A 257     7136  17400   6156    559    334    708  A    C  
ATOM   3026  SG  CYS A 257      -0.312  -1.071 -43.348  1.00 86.10      A    S  
ANISOU 3026  SG  CYS A 257     7768  18194   6753    823    357    772  A    S  
ATOM   3027  N   TRP A 258       1.567  -4.449 -46.454  1.00 81.02      A    N  
ANISOU 3027  N   TRP A 258     7148  17392   6244     46    327    539  A    N  
ATOM   3028  CA  TRP A 258       2.368  -4.951 -47.573  1.00 80.92      A    C  
ANISOU 3028  CA  TRP A 258     7225  17288   6234    -60    335    478  A    C  
ATOM   3029  C   TRP A 258       1.657  -6.029 -48.412  1.00 87.58      A    C  
ANISOU 3029  C   TRP A 258     8006  18289   6980   -266    310    400  A    C  
ATOM   3030  O   TRP A 258       1.999  -6.184 -49.586  1.00 87.79      A    O  
ANISOU 3030  O   TRP A 258     8088  18321   6949   -315    303    355  A    O  
ATOM   3031  CB  TRP A 258       3.752  -5.435 -47.094  1.00 78.21      A    C  
ANISOU 3031  CB  TRP A 258     7021  16675   6021    -90    394    445  A    C  
ATOM   3032  CG  TRP A 258       4.756  -4.348 -46.795  1.00 77.94      A    C  
ANISOU 3032  CG  TRP A 258     7069  16506   6040     42    407    511  A    C  
ATOM   3033  CD1 TRP A 258       4.497  -3.063 -46.411  1.00 80.88      A    C  
ANISOU 3033  CD1 TRP A 258     7461  16885   6384    184    381    588  A    C  
ATOM   3034  CD2 TRP A 258       6.181  -4.493 -46.768  1.00 76.88      A    C  
ANISOU 3034  CD2 TRP A 258     7020  16215   5976     28    450    507  A    C  
ATOM   3036  CE2 TRP A 258       6.724  -3.242 -46.393  1.00 80.37      A    C  
ANISOU 3036  CE2 TRP A 258     7520  16590   6425    108    436    584  A    C  
ATOM   3037  CE3 TRP A 258       7.057  -5.561 -47.027  1.00 77.89      A    C  
ANISOU 3037  CE3 TRP A 258     7189  16264   6143    -34    503    451  A    C  
ATOM   3035  NE1 TRP A 258       5.674  -2.386 -46.191  1.00 79.54      A    N  
ANISOU 3035  NE1 TRP A 258     7408  16553   6261    207    397    625  A    N  
ATOM   3038  CZ2 TRP A 258       8.103  -3.026 -46.284  1.00 79.08      A    C  
ANISOU 3038  CZ2 TRP A 258     7411  16335   6302     80    463    613  A    C  
ATOM   3039  CZ3 TRP A 258       8.423  -5.340 -46.935  1.00 78.74      A    C  
ANISOU 3039  CZ3 TRP A 258     7330  16298   6290      3    539    487  A    C  
ATOM   3040  CH2 TRP A 258       8.934  -4.089 -46.562  1.00 78.92      A    C  
ANISOU 3040  CH2 TRP A 258     7365  16305   6315     36    514    570  A    C  
ATOM   3041  N   PHE A 259       0.670  -6.752 -47.829  1.00 85.95      A    N  
ANISOU 3041  N   PHE A 259     7697  18223   6738   -411    296    384  A    N  
ATOM   3042  CA  PHE A 259      -0.079  -7.815 -48.512  1.00 87.99      A    C  
ANISOU 3042  CA  PHE A 259     7917  18637   6880   -678    263    306  A    C  
ATOM   3043  C   PHE A 259      -0.694  -7.371 -49.859  1.00 93.02      A    C  
ANISOU 3043  C   PHE A 259     8444  19549   7351   -680    192    313  A    C  
ATOM   3044  O   PHE A 259      -0.352  -8.029 -50.842  1.00 93.39      A    O  
ANISOU 3044  O   PHE A 259     8606  19534   7345   -825    191    219  A    O  
ATOM   3045  CB  PHE A 259      -1.135  -8.486 -47.601  1.00 91.34      A    C  
ANISOU 3045  CB  PHE A 259     8216  19226   7264   -858    252    320  A    C  
ATOM   3046  CG  PHE A 259      -2.169  -9.319 -48.326  1.00 95.88      A    C  
ANISOU 3046  CG  PHE A 259     8705  20060   7667  -1172    194    264  A    C  
ATOM   3047  CD1 PHE A 259      -1.833 -10.550 -48.878  1.00100.30      A    C  
ANISOU 3047  CD1 PHE A 259     9482  20425   8202  -1445    209    139  A    C  
ATOM   3048  CD2 PHE A 259      -3.476  -8.869 -48.463  1.00100.98      A    C  
ANISOU 3048  CD2 PHE A 259     9059  21157   8150  -1195    124    338  A    C  
ATOM   3049  CE1 PHE A 259      -2.781 -11.311 -49.569  1.00104.23      A    C  
ANISOU 3049  CE1 PHE A 259     9935  21152   8516  -1787    147     75  A    C  
ATOM   3050  CE2 PHE A 259      -4.428  -9.630 -49.155  1.00106.97      A    C  
ANISOU 3050  CE2 PHE A 259     9714  22208   8723  -1533     56    292  A    C  
ATOM   3051  CZ  PHE A 259      -4.073 -10.846 -49.703  1.00105.88      A    C  
ANISOU 3051  CZ  PHE A 259     9821  21846   8561  -1855     64    154  A    C  
ATOM   3052  N   PRO A 260      -1.573  -6.320 -49.974  1.00 89.68      A    N  
ANISOU 3052  N   PRO A 260     7819  19429   6827   -506    139    420  A    N  
ATOM   3053  CA  PRO A 260      -2.119  -5.972 -51.310  1.00 90.21      A    C  
ANISOU 3053  CA  PRO A 260     7784  19775   6718   -502     67    438  A    C  
ATOM   3054  C   PRO A 260      -1.047  -5.601 -52.335  1.00 90.37      A    C  
ANISOU 3054  C   PRO A 260     7983  19597   6759   -420     85    413  A    C  
ATOM   3055  O   PRO A 260      -1.143  -6.032 -53.480  1.00 90.01      A    O  
ANISOU 3055  O   PRO A 260     7948  19661   6589   -567     49    348  A    O  
ATOM   3056  CB  PRO A 260      -3.097  -4.822 -51.032  1.00 93.03      A    C  
ANISOU 3056  CB  PRO A 260     7926  20441   6980   -233     28    584  A    C  
ATOM   3057  CG  PRO A 260      -2.702  -4.288 -49.704  1.00 96.43      A    C  
ANISOU 3057  CG  PRO A 260     8430  20649   7562    -41     94    630  A    C  
ATOM   3058  CD  PRO A 260      -2.123  -5.429 -48.928  1.00 90.93      A    C  
ANISOU 3058  CD  PRO A 260     7846  19702   7001   -281    145    531  A    C  
ATOM   3059  N   VAL A 261       0.011  -4.877 -51.896  1.00 84.29      A    N  
ANISOU 3059  N   VAL A 261     7357  18541   6130   -221    142    457  A    N  
ATOM   3060  CA  VAL A 261       1.164  -4.481 -52.727  1.00 82.31      A    C  
ANISOU 3060  CA  VAL A 261     7264  18109   5901   -155    173    453  A    C  
ATOM   3061  C   VAL A 261       1.922  -5.732 -53.236  1.00 85.11      A    C  
ANISOU 3061  C   VAL A 261     7749  18314   6274   -359    218    312  A    C  
ATOM   3062  O   VAL A 261       2.149  -5.845 -54.440  1.00 85.71      A    O  
ANISOU 3062  O   VAL A 261     7869  18452   6245   -403    210    272  A    O  
ATOM   3063  CB  VAL A 261       2.096  -3.449 -52.028  1.00 83.75      A    C  
ANISOU 3063  CB  VAL A 261     7564  18047   6210     40    219    537  A    C  
ATOM   3064  CG1 VAL A 261       3.129  -2.892 -53.001  1.00 83.32      A    C  
ANISOU 3064  CG1 VAL A 261     7630  17898   6128     87    238    569  A    C  
ATOM   3065  CG2 VAL A 261       1.292  -2.306 -51.408  1.00 83.73      A    C  
ANISOU 3065  CG2 VAL A 261     7498  18139   6178    257    189    655  A    C  
ATOM   3066  N   LEU A 262       2.240  -6.691 -52.339  1.00 80.40      A    N  
ANISOU 3066  N   LEU A 262     7227  17531   5789   -466    270    239  A    N  
ATOM   3067  CA  LEU A 262       2.919  -7.946 -52.693  1.00 80.49      A    C  
ANISOU 3067  CA  LEU A 262     7410  17363   5809   -613    328    107  A    C  
ATOM   3068  C   LEU A 262       2.061  -8.886 -53.567  1.00 86.39      A    C  
ANISOU 3068  C   LEU A 262     8172  18263   6388   -863    282     -5  A    C  
ATOM   3069  O   LEU A 262       2.586  -9.511 -54.492  1.00 85.65      A    O  
ANISOU 3069  O   LEU A 262     8236  18086   6222   -935    316   -112  A    O  
ATOM   3070  CB  LEU A 262       3.413  -8.680 -51.436  1.00 79.71      A    C  
ANISOU 3070  CB  LEU A 262     7409  17017   5859   -626    394     85  A    C  
ATOM   3071  CG  LEU A 262       4.496  -7.972 -50.588  1.00 82.93      A    C  
ANISOU 3071  CG  LEU A 262     7830  17263   6416   -425    442    173  A    C  
ATOM   3072  CD1 LEU A 262       4.569  -8.555 -49.183  1.00 82.25      A    C  
ANISOU 3072  CD1 LEU A 262     7775  17030   6447   -442    475    181  A    C  
ATOM   3073  CD2 LEU A 262       5.870  -8.000 -51.263  1.00 84.68      A    C  
ANISOU 3073  CD2 LEU A 262     8157  17367   6651   -334    509    154  A    C  
ATOM   3074  N   ALA A 263       0.744  -8.970 -53.282  1.00 85.39      A    N  
ANISOU 3074  N   ALA A 263     7880  18385   6179  -1001    206     21  A    N  
ATOM   3075  CA  ALA A 263      -0.207  -9.816 -54.012  1.00 88.10      A    C  
ANISOU 3075  CA  ALA A 263     8203  18935   6334  -1302    141    -73  A    C  
ATOM   3076  C   ALA A 263      -0.368  -9.396 -55.478  1.00 94.91      A    C  
ANISOU 3076  C   ALA A 263     9022  20022   7018  -1302     83    -89  A    C  
ATOM   3077  O   ALA A 263      -0.627 -10.248 -56.333  1.00 96.35      A    O  
ANISOU 3077  O   ALA A 263     9309  20255   7046  -1553     58   -217  A    O  
ATOM   3078  CB  ALA A 263      -1.554  -9.818 -53.313  1.00 89.78      A    C  
ANISOU 3078  CB  ALA A 263     8179  19448   6483  -1432     72     -4  A    C  
ATOM   3079  N   LEU A 264      -0.204  -8.088 -55.763  1.00 91.35      A    N  
ANISOU 3079  N   LEU A 264     8449  19688   6573  -1029     64     41  A    N  
ATOM   3080  CA  LEU A 264      -0.291  -7.532 -57.113  1.00 92.07      A    C  
ANISOU 3080  CA  LEU A 264     8499  19990   6495   -983     13     61  A    C  
ATOM   3081  C   LEU A 264       0.975  -7.838 -57.900  1.00 94.54      A    C  
ANISOU 3081  C   LEU A 264     9044  20053   6825   -957     94    -31  A    C  
ATOM   3082  O   LEU A 264       0.887  -8.120 -59.091  1.00 95.82      A    O  
ANISOU 3082  O   LEU A 264     9254  20342   6812  -1065     67   -106  A    O  
ATOM   3083  CB  LEU A 264      -0.582  -6.022 -57.082  1.00 91.84      A    C  
ANISOU 3083  CB  LEU A 264     8302  20140   6452   -688    -29    250  A    C  
ATOM   3084  CG  LEU A 264      -2.018  -5.641 -56.698  1.00 98.11      A    C  
ANISOU 3084  CG  LEU A 264     8831  21277   7169   -645   -108    357  A    C  
ATOM   3085  CD1 LEU A 264      -2.074  -4.260 -56.093  1.00 97.60      A    C  
ANISOU 3085  CD1 LEU A 264     8715  21206   7163   -281   -100    532  A    C  
ATOM   3086  CD2 LEU A 264      -2.949  -5.724 -57.887  1.00104.43      A    C  
ANISOU 3086  CD2 LEU A 264     9442  22528   7709   -807   -219    354  A    C  
ATOM   3087  N   MET A 265       2.141  -7.818 -57.226  1.00 89.12      A    N  
ANISOU 3087  N   MET A 265     8487  19045   6329   -816    195    -23  A    N  
ATOM   3088  CA  MET A 265       3.454  -8.131 -57.802  1.00 88.66      A    C  
ANISOU 3088  CA  MET A 265     8617  18776   6294   -752    293    -92  A    C  
ATOM   3089  C   MET A 265       3.543  -9.610 -58.192  1.00 93.78      A    C  
ANISOU 3089  C   MET A 265     9473  19297   6863   -951    338   -286  A    C  
ATOM   3090  O   MET A 265       4.164  -9.936 -59.201  1.00 94.51      A    O  
ANISOU 3090  O   MET A 265     9703  19359   6849   -942    389   -373  A    O  
ATOM   3091  CB  MET A 265       4.568  -7.801 -56.808  1.00 89.29      A    C  
ANISOU 3091  CB  MET A 265     8738  18608   6580   -574    378    -22  A    C  
ATOM   3092  CG  MET A 265       4.792  -6.318 -56.601  1.00 92.38      A    C  
ANISOU 3092  CG  MET A 265     9023  19054   7023   -389    355    150  A    C  
ATOM   3093  SD  MET A 265       6.017  -6.011 -55.294  1.00 95.20      A    S  
ANISOU 3093  SD  MET A 265     9425  19151   7597   -256    436    220  A    S  
ATOM   3094  CE  MET A 265       7.534  -6.295 -56.180  1.00 92.03      A    C  
ANISOU 3094  CE  MET A 265     9125  18682   7158   -213    541    179  A    C  
ATOM   3095  N   ALA A 266       2.925 -10.502 -57.393  1.00 90.85      A    N  
ANISOU 3095  N   ALA A 266     9153  18840   6525  -1131    325   -353  A    N  
ATOM   3096  CA  ALA A 266       2.875 -11.944 -57.659  1.00 92.37      A    C  
ANISOU 3096  CA  ALA A 266     9608  18862   6627  -1355    362   -538  A    C  
ATOM   3097  C   ALA A 266       1.941 -12.218 -58.847  1.00 97.72      A    C  
ANISOU 3097  C   ALA A 266    10281  19800   7050  -1613    269   -633  A    C  
ATOM   3098  O   ALA A 266       2.193 -13.143 -59.622  1.00 99.33      A    O  
ANISOU 3098  O   ALA A 266    10747  19876   7116  -1748    309   -802  A    O  
ATOM   3099  CB  ALA A 266       2.391 -12.686 -56.423  1.00 93.29      A    C  
ANISOU 3099  CB  ALA A 266     9779  18826   6841  -1503    365   -549  A    C  
ATOM   3100  N   HIS A 267       0.880 -11.389 -58.995  1.00 93.90      A    N  
ANISOU 3100  N   HIS A 267     9502  19693   6483  -1662    146   -521  A    N  
ATOM   3101  CA  HIS A 267      -0.098 -11.432 -60.090  1.00 96.03      A    C  
ANISOU 3101  CA  HIS A 267     9677  20319   6491  -1889     31   -567  A    C  
ATOM   3102  C   HIS A 267       0.534 -10.880 -61.382  1.00 99.81      A    C  
ANISOU 3102  C   HIS A 267    10188  20881   6853  -1733     45   -570  A    C  
ATOM   3103  O   HIS A 267       0.128 -11.258 -62.483  1.00101.78      A    O  
ANISOU 3103  O   HIS A 267    10492  21315   6866  -1930    -12   -673  A    O  
ATOM   3104  CB  HIS A 267      -1.347 -10.617 -59.711  1.00 96.91      A    C  
ANISOU 3104  CB  HIS A 267     9423  20840   6557  -1901    -92   -406  A    C  
ATOM   3105  CG  HIS A 267      -2.476 -10.723 -60.690  1.00103.17      A    C  
ANISOU 3105  CG  HIS A 267    10064  22075   7062  -2162   -225   -433  A    C  
ATOM   3107  CD2 HIS A 267      -3.371 -11.723 -60.875  1.00107.53      A    C  
ANISOU 3107  CD2 HIS A 267    10625  22798   7434  -2583   -302   -543  A    C  
ATOM   3106  ND1 HIS A 267      -2.754  -9.704 -61.581  1.00105.43      A    N  
ANISOU 3106  ND1 HIS A 267    10162  22692   7204  -2003   -298   -327  A    N  
ATOM   3108  CE1 HIS A 267      -3.805 -10.111 -62.276  1.00107.71      A    C  
ANISOU 3108  CE1 HIS A 267    10323  23373   7228  -2310   -420   -374  A    C  
ATOM   3109  NE2 HIS A 267      -4.213 -11.319 -61.884  1.00109.47      A    N  
ANISOU 3109  NE2 HIS A 267    10656  23523   7417  -2688   -430   -508  A    N  
ATOM   3110  N   SER A 268       1.524  -9.979 -61.221  1.00 93.71      A    N  
ANISOU 3110  N   SER A 268     9388  19985   6234  -1406    119   -452  A    N  
ATOM   3111  CA  SER A 268       2.315  -9.331 -62.266  1.00 93.40      A    C  
ANISOU 3111  CA  SER A 268     9376  19996   6118  -1230    156   -416  A    C  
ATOM   3112  C   SER A 268       3.179 -10.358 -63.032  1.00 99.46      A    C  
ANISOU 3112  C   SER A 268    10436  20567   6788  -1293    259   -611  A    C  
ATOM   3113  O   SER A 268       3.450 -10.163 -64.217  1.00 99.90      A    O  
ANISOU 3113  O   SER A 268    10528  20761   6667  -1273    262   -641  A    O  
ATOM   3114  CB  SER A 268       3.170  -8.223 -61.648  1.00 93.58      A    C  
ANISOU 3114  CB  SER A 268     9325  19891   6339   -932    219   -245  A    C  
ATOM   3115  OG  SER A 268       4.235  -7.776 -62.467  1.00103.59      A    O  
ANISOU 3115  OG  SER A 268    10642  21168   7548   -787    278   -203  A    O  
ATOM   3116  N   LEU A 269       3.583 -11.454 -62.350  1.00 96.92      A    N  
ANISOU 3116  N   LEU A 269    10337  19925   6564  -1349    346   -738  A    N  
ATOM   3117  CA  LEU A 269       4.391 -12.557 -62.890  1.00 98.48      A    C  
ANISOU 3117  CA  LEU A 269    10868  19877   6674  -1359    465   -931  A    C  
ATOM   3118  C   LEU A 269       3.521 -13.596 -63.613  1.00107.01      A    C  
ANISOU 3118  C   LEU A 269    12154  21000   7507  -1703    403  -1133  A    C  
ATOM   3119  O   LEU A 269       4.002 -14.266 -64.531  1.00108.29      A    O  
ANISOU 3119  O   LEU A 269    12579  21068   7497  -1714    476  -1297  A    O  
ATOM   3120  CB  LEU A 269       5.148 -13.266 -61.746  1.00 97.37      A    C  
ANISOU 3120  CB  LEU A 269    10900  19362   6735  -1240    582   -959  A    C  
ATOM   3121  CG  LEU A 269       6.222 -12.470 -60.989  1.00 99.00      A    C  
ANISOU 3121  CG  LEU A 269    10960  19493   7163   -923    662   -793  A    C  
ATOM   3122  CD1 LEU A 269       6.234 -12.846 -59.530  1.00 97.72      A    C  
ANISOU 3122  CD1 LEU A 269    10828  19098   7205   -900    688   -756  A    C  
ATOM   3123  CD2 LEU A 269       7.607 -12.685 -61.590  1.00100.75      A    C  
ANISOU 3123  CD2 LEU A 269    11313  19628   7339   -685    809   -835  A    C  
ATOM   3124  N   ALA A 270       2.258 -13.753 -63.168  1.00105.72      A    N  
ANISOU 3124  N   ALA A 270    11878  20982   7307  -1995    276  -1125  A    N  
ATOM   3125  CA  ALA A 270       1.304 -14.734 -63.691  1.00109.25      A    C  
ANISOU 3125  CA  ALA A 270    12503  21498   7509  -2411    196  -1304  A    C  
ATOM   3126  C   ALA A 270       0.604 -14.322 -64.986  1.00115.55      A    C  
ANISOU 3126  C   ALA A 270    13149  22727   8029  -2572     70  -1317  A    C  
ATOM   3127  O   ALA A 270       0.548 -15.124 -65.918  1.00118.12      A    O  
ANISOU 3127  O   ALA A 270    13742  23030   8110  -2801     65  -1515  A    O  
ATOM   3128  CB  ALA A 270       0.276 -15.085 -62.620  1.00110.36      A    C  
ANISOU 3128  CB  ALA A 270    12561  21659   7711  -2688    116  -1273  A    C  
ATOM   3129  N   THR A 271       0.036 -13.099 -65.035  1.00111.18      A    N  
ANISOU 3129  N   THR A 271    12193  22560   7491  -2451    -34  -1109  A    N  
ATOM   3130  CA  THR A 271      -0.707 -12.596 -66.197  1.00112.94      A    C  
ANISOU 3130  CA  THR A 271    12220  23247   7445  -2563   -167  -1075  A    C  
ATOM   3131  C   THR A 271      -0.368 -11.153 -66.562  1.00114.75      A    C  
ANISOU 3131  C   THR A 271    12200  23676   7724  -2195   -172   -859  A    C  
ATOM   3132  O   THR A 271       0.055 -10.375 -65.699  1.00111.75      A    O  
ANISOU 3132  O   THR A 271    11713  23152   7594  -1908   -113   -701  A    O  
ATOM   3133  CB  THR A 271      -2.225 -12.743 -65.990  1.00124.12      A    C  
ANISOU 3133  CB  THR A 271    13383  25055   8721  -2899   -337  -1034  A    C  
ATOM   3135  CG2 THR A 271      -2.733 -14.149 -66.293  1.00126.58      A    C  
ANISOU 3135  CG2 THR A 271    13967  25306   8822  -3398   -378  -1272  A    C  
ATOM   3134  OG1 THR A 271      -2.575 -12.343 -64.660  1.00121.27      A    O  
ANISOU 3134  OG1 THR A 271    12806  24673   8598  -2778   -337   -874  A    O  
ATOM   3136  N   THR A 272      -0.594 -10.805 -67.852  1.00112.54      A    N  
ANISOU 3136  N   THR A 272    11849  23728   7184  -2230   -248   -850  A    N  
ATOM   3137  CA  THR A 272      -0.392  -9.485 -68.461  1.00111.14      A    C  
ANISOU 3137  CA  THR A 272    11474  23775   6979  -1930   -268   -643  A    C  
ATOM   3138  C   THR A 272      -1.349  -8.491 -67.797  1.00113.42      A    C  
ANISOU 3138  C   THR A 272    11410  24353   7332  -1810   -381   -408  A    C  
ATOM   3139  O   THR A 272      -2.551  -8.764 -67.708  1.00114.99      A    O  
ANISOU 3139  O   THR A 272    11423  24883   7385  -2039   -512   -409  A    O  
ATOM   3140  CB  THR A 272      -0.638  -9.565 -69.983  1.00123.36      A    C  
ANISOU 3140  CB  THR A 272    13054  25632   8186  -2055   -336   -712  A    C  
ATOM   3142  CG2 THR A 272      -0.012  -8.401 -70.743  1.00121.34      A    C  
ANISOU 3142  CG2 THR A 272    12718  25484   7901  -1738   -305   -528  A    C  
ATOM   3141  OG1 THR A 272      -0.150 -10.810 -70.490  1.00124.91      A    O  
ANISOU 3141  OG1 THR A 272    13602  25594   8263  -2261   -254   -986  A    O  
ATOM   3143  N   LEU A 273      -0.812  -7.361 -67.308  1.00106.94      A    N  
ANISOU 3143  N   LEU A 273    10507  23414   6711  -1458   -326   -207  A    N  
ATOM   3144  CA  LEU A 273      -1.609  -6.350 -66.610  1.00106.02      A    C  
ANISOU 3144  CA  LEU A 273    10114  23505   6662  -1267   -404     16  A    C  
ATOM   3145  C   LEU A 273      -2.147  -5.262 -67.526  1.00112.55      A    C  
ANISOU 3145  C   LEU A 273    10760  24723   7280  -1086   -502    210  A    C  
ATOM   3146  O   LEU A 273      -1.456  -4.805 -68.437  1.00112.06      A    O  
ANISOU 3146  O   LEU A 273    10810  24631   7136   -974   -465    248  A    O  
ATOM   3147  CB  LEU A 273      -0.841  -5.719 -65.425  1.00102.59      A    C  
ANISOU 3147  CB  LEU A 273     9731  22703   6544   -999   -298    123  A    C  
ATOM   3148  CG  LEU A 273      -0.433  -6.640 -64.269  1.00104.84      A    C  
ANISOU 3148  CG  LEU A 273    10151  22628   7054  -1114   -209    -14  A    C  
ATOM   3149  CD1 LEU A 273       0.575  -5.963 -63.381  1.00101.91      A    C  
ANISOU 3149  CD1 LEU A 273     9858  21916   6947   -853   -101     85  A    C  
ATOM   3150  CD2 LEU A 273      -1.625  -7.064 -63.449  1.00107.64      A    C  
ANISOU 3150  CD2 LEU A 273    10334  23156   7409  -1286   -289    -24  A    C  
ATOM   3151  N   SER A 274      -3.388  -4.835 -67.251  1.00111.61      A    N  
ANISOU 3151  N   SER A 274    10353  24990   7065  -1037   -623    349  A    N  
ATOM   3152  CA  SER A 274      -4.090  -3.766 -67.958  1.00113.80      A    C  
ANISOU 3152  CA  SER A 274    10424  25683   7131   -808   -726    569  A    C  
ATOM   3153  C   SER A 274      -3.543  -2.410 -67.488  1.00116.67      A    C  
ANISOU 3153  C   SER A 274    10857  25806   7668   -377   -654    791  A    C  
ATOM   3154  O   SER A 274      -2.834  -2.347 -66.476  1.00113.66      A    O  
ANISOU 3154  O   SER A 274    10615  25010   7562   -296   -547    771  A    O  
ATOM   3155  CB  SER A 274      -5.590  -3.861 -67.681  1.00120.05      A    C  
ANISOU 3155  CB  SER A 274    10865  26993   7755   -884   -866    641  A    C  
ATOM   3156  OG  SER A 274      -6.310  -2.734 -68.154  1.00131.89      A    O  
ANISOU 3156  OG  SER A 274    12145  28912   9055   -580   -960    887  A    O  
ATOM   3157  N   ASP A 275      -3.881  -1.327 -68.213  1.00115.26      A    N  
ANISOU 3157  N   ASP A 275    10600  25886   7309   -112   -716   1006  A    N  
ATOM   3158  CA  ASP A 275      -3.451   0.026 -67.862  1.00114.20      A    C  
ANISOU 3158  CA  ASP A 275    10582  25524   7285    285   -658   1232  A    C  
ATOM   3159  C   ASP A 275      -4.076   0.496 -66.531  1.00115.97      A    C  
ANISOU 3159  C   ASP A 275    10695  25707   7661    511   -653   1333  A    C  
ATOM   3160  O   ASP A 275      -3.365   1.066 -65.701  1.00113.49      A    O  
ANISOU 3160  O   ASP A 275    10574  24970   7575    674   -554   1378  A    O  
ATOM   3161  CB  ASP A 275      -3.757   1.011 -69.002  1.00119.08      A    C  
ANISOU 3161  CB  ASP A 275    11160  26452   7632    516   -735   1447  A    C  
ATOM   3162  CG  ASP A 275      -2.686   2.067 -69.207  1.00132.33      A    C  
ANISOU 3162  CG  ASP A 275    13107  27789   9384    808   -652   1638  A    C  
ATOM   3163  OD1 ASP A 275      -2.286   2.711 -68.214  1.00130.71      A    O  
ANISOU 3163  OD1 ASP A 275    13093  27128   9442    858   -544   1623  A    O  
ATOM   3164  OD2 ASP A 275      -2.255   2.259 -70.367  1.00142.09      A    O1-
ANISOU 3164  OD2 ASP A 275    14370  29221  10397    968   -700   1810  A    O1-
ATOM   3165  N   GLN A 276      -5.385   0.217 -66.322  1.00113.13      A    N  
ANISOU 3165  N   GLN A 276    10017  25808   7157    494   -757   1360  A    N  
ATOM   3166  CA  GLN A 276      -6.144   0.574 -65.112  1.00112.22      A    C  
ANISOU 3166  CA  GLN A 276     9741  25764   7134    710   -755   1454  A    C  
ATOM   3167  C   GLN A 276      -5.633  -0.111 -63.839  1.00110.92      A    C  
ANISOU 3167  C   GLN A 276     9680  25200   7265    535   -659   1290  A    C  
ATOM   3168  O   GLN A 276      -5.727   0.474 -62.760  1.00109.55      A    O  
ANISOU 3168  O   GLN A 276     9529  24855   7239    786   -604   1375  A    O  
ATOM   3169  CB  GLN A 276      -7.660   0.337 -65.295  1.00117.06      A    C  
ANISOU 3169  CB  GLN A 276     9937  27060   7481    690   -890   1525  A    C  
ATOM   3170  CG  GLN A 276      -8.047  -1.076 -65.751  1.00134.42      A    C  
ANISOU 3170  CG  GLN A 276    11976  29551   9546    160   -972   1314  A    C  
ATOM   3171  CD  GLN A 276      -9.484  -1.419 -65.451  1.00154.47      A    C  
ANISOU 3171  CD  GLN A 276    14084  32728  11879     74  -1087   1373  A    C  
ATOM   3173  NE2 GLN A 276      -9.711  -2.620 -64.939  1.00143.35      A    N  
ANISOU 3173  NE2 GLN A 276    12599  31345  10523   -352  -1094   1190  A    N  
ATOM   3172  OE1 GLN A 276     -10.403  -0.630 -65.682  1.00153.89      A    O  
ANISOU 3172  OE1 GLN A 276    13740  33150  11581    384  -1169   1591  A    O  
ATOM   3174  N   VAL A 277      -5.102  -1.345 -63.969  1.00104.68      A    N  
ANISOU 3174  N   VAL A 277     8974  24258   6541    125   -635   1057  A    N  
ATOM   3175  CA  VAL A 277      -4.545  -2.136 -62.863  1.00101.12      A    C  
ANISOU 3175  CA  VAL A 277     8645  23426   6350    -62   -544    896  A    C  
ATOM   3176  C   VAL A 277      -3.221  -1.502 -62.417  1.00102.72      A    C  
ANISOU 3176  C   VAL A 277     9144  23091   6793    124   -420    921  A    C  
ATOM   3177  O   VAL A 277      -2.961  -1.435 -61.216  1.00101.28      A    O  
ANISOU 3177  O   VAL A 277     9019  22640   6822    191   -353    913  A    O  
ATOM   3178  CB  VAL A 277      -4.385  -3.639 -63.224  1.00104.64      A    C  
ANISOU 3178  CB  VAL A 277     9146  23857   6757   -522   -552    650  A    C  
ATOM   3179  CG1 VAL A 277      -4.044  -4.474 -61.995  1.00102.13      A    C  
ANISOU 3179  CG1 VAL A 277     8934  23195   6678   -686   -469    515  A    C  
ATOM   3180  CG2 VAL A 277      -5.639  -4.183 -63.898  1.00107.80      A    C  
ANISOU 3180  CG2 VAL A 277     9274  24820   6865   -768   -692    629  A    C  
ATOM   3181  N   LYS A 278      -2.402  -1.013 -63.387  1.00 98.62      A    N  
ANISOU 3181  N   LYS A 278     8799  22452   6219    188   -394    961  A    N  
ATOM   3182  CA  LYS A 278      -1.126  -0.328 -63.147  1.00 95.94      A    C  
ANISOU 3182  CA  LYS A 278     8722  21677   6055    321   -287   1009  A    C  
ATOM   3183  C   LYS A 278      -1.376   0.982 -62.395  1.00100.04      A    C  
ANISOU 3183  C   LYS A 278     9285  22085   6642    665   -277   1207  A    C  
ATOM   3184  O   LYS A 278      -0.575   1.354 -61.535  1.00 98.67      A    O  
ANISOU 3184  O   LYS A 278     9286  21535   6669    719   -194   1210  A    O  
ATOM   3185  CB  LYS A 278      -0.375  -0.066 -64.459  1.00 99.00      A    C  
ANISOU 3185  CB  LYS A 278     9243  22062   6309    298   -272   1036  A    C  
ATOM   3186  CG  LYS A 278       0.185  -1.324 -65.114  1.00114.27      A    C  
ANISOU 3186  CG  LYS A 278    11227  23988   8202     -8   -240    817  A    C  
ATOM   3187  CD  LYS A 278       1.327  -0.992 -66.068  1.00126.12      A    C  
ANISOU 3187  CD  LYS A 278    12903  25372   9644      2   -170    843  A    C  
ATOM   3188  CE  LYS A 278       1.641  -2.101 -67.044  1.00138.80      A    C  
ANISOU 3188  CE  LYS A 278    14558  27055  11123   -243   -146    639  A    C  
ATOM   3189  NZ  LYS A 278       0.693  -2.112 -68.191  1.00151.17      A    N1+
ANISOU 3189  NZ  LYS A 278    16007  29040  12391   -315   -263    645  A    N1+
ATOM   3190  N   LYS A 279      -2.511   1.651 -62.695  1.00 98.51      A    N  
ANISOU 3190  N   LYS A 279     8938  22232   6260    904   -361   1369  A    N  
ATOM   3191  CA  LYS A 279      -2.977   2.871 -62.027  1.00 98.96      A    C  
ANISOU 3191  CA  LYS A 279     9047  22225   6326   1291   -353   1559  A    C  
ATOM   3192  C   LYS A 279      -3.299   2.547 -60.546  1.00102.57      A    C  
ANISOU 3192  C   LYS A 279     9424  22588   6959   1299   -317   1489  A    C  
ATOM   3193  O   LYS A 279      -2.951   3.331 -59.662  1.00101.57      A    O  
ANISOU 3193  O   LYS A 279     9488  22140   6964   1498   -252   1551  A    O  
ATOM   3194  CB  LYS A 279      -4.233   3.439 -62.727  1.00104.03      A    C  
ANISOU 3194  CB  LYS A 279     9487  23348   6690   1562   -454   1739  A    C  
ATOM   3195  CG  LYS A 279      -3.987   4.029 -64.107  1.00111.45      A    C  
ANISOU 3195  CG  LYS A 279    10521  24395   7430   1626   -494   1856  A    C  
ATOM   3196  CD  LYS A 279      -5.256   4.626 -64.696  1.00120.67      A    C  
ANISOU 3196  CD  LYS A 279    11460  26078   8309   1925   -599   2049  A    C  
ATOM   3197  CE  LYS A 279      -4.999   5.317 -66.015  1.00129.83      A    C  
ANISOU 3197  CE  LYS A 279    12718  27356   9253   1997   -643   2181  A    C  
ATOM   3198  NZ  LYS A 279      -6.235   5.903 -66.596  1.00140.04      A    N1+
ANISOU 3198  NZ  LYS A 279    13784  29177  10248   2334   -748   2395  A    N1+
ATOM   3199  N   ALA A 280      -3.940   1.382 -60.285  1.00 99.18      A    N  
ANISOU 3199  N   ALA A 280     8735  22436   6513   1056   -359   1358  A    N  
ATOM   3200  CA  ALA A 280      -4.288   0.927 -58.940  1.00 97.87      A    C  
ANISOU 3200  CA  ALA A 280     8466  22234   6487   1014   -327   1290  A    C  
ATOM   3201  C   ALA A 280      -3.047   0.672 -58.099  1.00 98.47      A    C  
ANISOU 3201  C   ALA A 280     8787  21795   6834    887   -225   1175  A    C  
ATOM   3202  O   ALA A 280      -3.064   1.034 -56.925  1.00 97.11      A    O  
ANISOU 3202  O   ALA A 280     8657  21455   6785   1032   -177   1202  A    O  
ATOM   3203  CB  ALA A 280      -5.147  -0.325 -59.001  1.00 99.85      A    C  
ANISOU 3203  CB  ALA A 280     8424  22875   6637    699   -396   1176  A    C  
ATOM   3204  N   PHE A 281      -1.963   0.096 -58.702  1.00 93.09      A    N  
ANISOU 3204  N   PHE A 281     8264  20886   6222    646   -189   1058  A    N  
ATOM   3205  CA  PHE A 281      -0.690  -0.179 -58.014  1.00 89.98      A    C  
ANISOU 3205  CA  PHE A 281     8074  20056   6058    535    -93    963  A    C  
ATOM   3206  C   PHE A 281       0.029   1.096 -57.550  1.00 92.01      A    C  
ANISOU 3206  C   PHE A 281     8555  19997   6406    766    -40   1087  A    C  
ATOM   3207  O   PHE A 281       0.629   1.082 -56.475  1.00 89.52      A    O  
ANISOU 3207  O   PHE A 281     8341  19404   6269    746     20   1047  A    O  
ATOM   3208  CB  PHE A 281       0.249  -1.075 -58.848  1.00 91.18      A    C  
ANISOU 3208  CB  PHE A 281     8320  20106   6218    276    -59    823  A    C  
ATOM   3209  CG  PHE A 281       1.516  -1.519 -58.135  1.00 90.55      A    C  
ANISOU 3209  CG  PHE A 281     8399  19656   6349    176     39    729  A    C  
ATOM   3210  CD1 PHE A 281       1.515  -2.638 -57.307  1.00 92.68      A    C  
ANISOU 3210  CD1 PHE A 281     8638  19843   6732      8     67    594  A    C  
ATOM   3211  CD2 PHE A 281       2.715  -0.827 -58.308  1.00 91.64      A    C  
ANISOU 3211  CD2 PHE A 281     8712  19554   6552    240    101    790  A    C  
ATOM   3212  CE1 PHE A 281       2.690  -3.053 -56.661  1.00 91.85      A    C  
ANISOU 3212  CE1 PHE A 281     8667  19429   6802    -46    156    526  A    C  
ATOM   3213  CE2 PHE A 281       3.882  -1.229 -57.645  1.00 92.48      A    C  
ANISOU 3213  CE2 PHE A 281     8919  19391   6828    157    186    720  A    C  
ATOM   3214  CZ  PHE A 281       3.865  -2.344 -56.833  1.00 89.69      A    C  
ANISOU 3214  CZ  PHE A 281     8525  18969   6585     37    212    590  A    C  
ATOM   3215  N   ALA A 282      -0.014   2.181 -58.358  1.00 89.90      A    N  
ANISOU 3215  N   ALA A 282     8388  19767   6004    964    -64   1239  A    N  
ATOM   3216  CA  ALA A 282       0.616   3.463 -58.015  1.00 89.63      A    C  
ANISOU 3216  CA  ALA A 282     8626  19414   6017   1154    -20   1368  A    C  
ATOM   3217  C   ALA A 282      -0.002   4.047 -56.735  1.00 94.05      A    C  
ANISOU 3217  C   ALA A 282     9214  19892   6631   1390     -8   1420  A    C  
ATOM   3218  O   ALA A 282       0.730   4.492 -55.843  1.00 91.91      A    O  
ANISOU 3218  O   ALA A 282     9151  19278   6492   1397     48   1417  A    O  
ATOM   3219  CB  ALA A 282       0.482   4.444 -59.167  1.00 92.33      A    C  
ANISOU 3219  CB  ALA A 282     9078  19836   6166   1325    -54   1534  A    C  
ATOM   3220  N   PHE A 283      -1.345   3.998 -56.634  1.00 92.67      A    N  
ANISOU 3220  N   PHE A 283     8812  20064   6335   1571    -60   1464  A    N  
ATOM   3221  CA  PHE A 283      -2.087   4.459 -55.464  1.00 93.30      A    C  
ANISOU 3221  CA  PHE A 283     8866  20157   6428   1830    -42   1511  A    C  
ATOM   3222  C   PHE A 283      -1.982   3.438 -54.322  1.00 97.00      A    C  
ANISOU 3222  C   PHE A 283     9209  20578   7069   1613     -9   1358  A    C  
ATOM   3223  O   PHE A 283      -2.018   3.830 -53.161  1.00 95.54      A    O  
ANISOU 3223  O   PHE A 283     9115  20222   6965   1749     37   1363  A    O  
ATOM   3224  CB  PHE A 283      -3.558   4.727 -55.823  1.00 97.54      A    C  
ANISOU 3224  CB  PHE A 283     9148  21171   6742   2108   -105   1629  A    C  
ATOM   3225  CG  PHE A 283      -3.786   5.966 -56.658  1.00101.21      A    C  
ANISOU 3225  CG  PHE A 283     9783  21649   7022   2460   -125   1824  A    C  
ATOM   3226  CD1 PHE A 283      -3.917   7.215 -56.060  1.00105.56      A    C  
ANISOU 3226  CD1 PHE A 283    10575  22002   7529   2868    -79   1952  A    C  
ATOM   3227  CD2 PHE A 283      -3.903   5.882 -58.040  1.00103.85      A    C  
ANISOU 3227  CD2 PHE A 283    10061  22191   7207   2399   -187   1883  A    C  
ATOM   3228  CE1 PHE A 283      -4.142   8.360 -56.834  1.00108.77      A    C  
ANISOU 3228  CE1 PHE A 283    11190  22390   7749   3220    -92   2146  A    C  
ATOM   3229  CE2 PHE A 283      -4.124   7.027 -58.813  1.00108.76      A    C  
ANISOU 3229  CE2 PHE A 283    10857  22824   7644   2739   -206   2084  A    C  
ATOM   3230  CZ  PHE A 283      -4.236   8.259 -58.205  1.00108.36      A    C  
ANISOU 3230  CZ  PHE A 283    11068  22548   7557   3153   -157   2220  A    C  
ATOM   3231  N   CYS A 284      -1.848   2.136 -54.661  1.00 94.81      A    N  
ANISOU 3231  N   CYS A 284     8754  20439   6831   1279    -30   1225  A    N  
ATOM   3232  CA  CYS A 284      -1.732   1.006 -53.725  1.00 93.83      A    C  
ANISOU 3232  CA  CYS A 284     8529  20269   6851   1037     -1   1083  A    C  
ATOM   3233  C   CYS A 284      -0.453   1.077 -52.927  1.00 93.13      A    C  
ANISOU 3233  C   CYS A 284     8677  19741   6966    953     72   1023  A    C  
ATOM   3234  O   CYS A 284      -0.465   0.782 -51.739  1.00 91.98      A    O  
ANISOU 3234  O   CYS A 284     8516  19498   6935    919    108    973  A    O  
ATOM   3235  CB  CYS A 284      -1.823  -0.318 -54.474  1.00 95.41      A    C  
ANISOU 3235  CB  CYS A 284     8571  20675   7006    711    -40    963  A    C  
ATOM   3236  SG  CYS A 284      -2.980  -1.502 -53.755  1.00100.15      A    S  
ANISOU 3236  SG  CYS A 284     8932  21492   7628    479    -51    863  A    S  
ATOM   3237  N   SER A 285       0.657   1.440 -53.591  1.00 87.52      A    N  
ANISOU 3237  N   SER A 285     8167  18803   6281    907     94   1039  A    N  
ATOM   3238  CA  SER A 285       1.978   1.566 -52.993  1.00 84.97      A    C  
ANISOU 3238  CA  SER A 285     8042  18126   6116    808    155   1003  A    C  
ATOM   3239  C   SER A 285       2.032   2.612 -51.883  1.00 88.02      A    C  
ANISOU 3239  C   SER A 285     8604  18290   6550    991    180   1072  A    C  
ATOM   3240  O   SER A 285       2.971   2.593 -51.083  1.00 86.40      A    O  
ANISOU 3240  O   SER A 285     8520  17838   6472    884    221   1032  A    O  
ATOM   3241  CB  SER A 285       3.035   1.829 -54.061  1.00 88.28      A    C  
ANISOU 3241  CB  SER A 285     8594  18442   6506    711    170   1027  A    C  
ATOM   3242  OG  SER A 285       2.690   2.889 -54.936  1.00 99.15      A    O  
ANISOU 3242  OG  SER A 285    10088  19844   7740    890    141   1168  A    O  
ATOM   3243  N   MET A 286       0.998   3.478 -51.785  1.00 86.11      A    N  
ANISOU 3243  N   MET A 286     8375  18155   6190   1278    158   1173  A    N  
ATOM   3244  CA  MET A 286       0.891   4.492 -50.731  1.00 86.85      A    C  
ANISOU 3244  CA  MET A 286     8674  18035   6292   1496    189   1227  A    C  
ATOM   3245  C   MET A 286       0.729   3.850 -49.338  1.00 90.82      A    C  
ANISOU 3245  C   MET A 286     9074  18523   6911   1439    219   1134  A    C  
ATOM   3246  O   MET A 286       0.953   4.521 -48.330  1.00 90.00      A    O  
ANISOU 3246  O   MET A 286     9168  18183   6843   1531    253   1139  A    O  
ATOM   3247  CB  MET A 286      -0.234   5.505 -51.014  1.00 91.63      A    C  
ANISOU 3247  CB  MET A 286     9321  18782   6714   1879    171   1361  A    C  
ATOM   3248  CG  MET A 286      -0.024   6.356 -52.268  1.00 96.88      A    C  
ANISOU 3248  CG  MET A 286    10163  19402   7247   1980    146   1485  A    C  
ATOM   3249  SD  MET A 286       1.597   7.156 -52.478  1.00100.73      A    S  
ANISOU 3249  SD  MET A 286    11064  19417   7793   1791    177   1517  A    S  
ATOM   3250  CE  MET A 286       1.580   8.275 -51.127  1.00 98.49      A    C  
ANISOU 3250  CE  MET A 286    11133  18777   7513   1998    222   1541  A    C  
ATOM   3251  N   LEU A 287       0.384   2.539 -49.300  1.00 87.91      A    N  
ANISOU 3251  N   LEU A 287     8426  18389   6587   1260    207   1048  A    N  
ATOM   3252  CA  LEU A 287       0.237   1.732 -48.088  1.00 87.37      A    C  
ANISOU 3252  CA  LEU A 287     8244  18331   6621   1158    235    967  A    C  
ATOM   3253  C   LEU A 287       1.583   1.490 -47.394  1.00 90.67      A    C  
ANISOU 3253  C   LEU A 287     8823  18427   7200    976    273    901  A    C  
ATOM   3254  O   LEU A 287       1.613   1.303 -46.176  1.00 88.88      A    O  
ANISOU 3254  O   LEU A 287     8604  18123   7045    971    301    867  A    O  
ATOM   3255  CB  LEU A 287      -0.469   0.402 -48.398  1.00 87.54      A    C  
ANISOU 3255  CB  LEU A 287     7982  18655   6625    963    209    902  A    C  
ATOM   3256  CG  LEU A 287      -1.973   0.370 -48.106  1.00 93.91      A    C  
ANISOU 3256  CG  LEU A 287     8540  19843   7300   1101    187    951  A    C  
ATOM   3257  CD1 LEU A 287      -2.781   0.865 -49.294  1.00 96.20      A    C  
ANISOU 3257  CD1 LEU A 287     8713  20436   7403   1252    130   1040  A    C  
ATOM   3258  CD2 LEU A 287      -2.425  -1.025 -47.747  1.00 95.68      A    C  
ANISOU 3258  CD2 LEU A 287     8553  20248   7553    821    183    868  A    C  
ATOM   3259  N   CYS A 288       2.693   1.516 -48.169  1.00 88.64      A    N  
ANISOU 3259  N   CYS A 288     8679  18020   6980    833    274    894  A    N  
ATOM   3260  CA  CYS A 288       4.068   1.361 -47.673  1.00 87.90      A    C  
ANISOU 3260  CA  CYS A 288     8704  17686   7006    667    305    856  A    C  
ATOM   3261  C   CYS A 288       4.461   2.611 -46.892  1.00 92.71      A    C  
ANISOU 3261  C   CYS A 288     9556  18065   7606    764    313    910  A    C  
ATOM   3262  O   CYS A 288       5.317   2.537 -46.007  1.00 92.50      A    O  
ANISOU 3262  O   CYS A 288     9595  17890   7663    654    331    878  A    O  
ATOM   3263  CB  CYS A 288       5.043   1.103 -48.819  1.00 88.41      A    C  
ANISOU 3263  CB  CYS A 288     8790  17732   7070    517    311    852  A    C  
ATOM   3264  SG  CYS A 288       4.717  -0.411 -49.758  1.00 92.37      A    S  
ANISOU 3264  SG  CYS A 288     9086  18448   7561    382    310    758  A    S  
ATOM   3265  N   LEU A 289       3.830   3.759 -47.227  1.00 89.95      A    N  
ANISOU 3265  N   LEU A 289     9360  17684   7134    973    299    995  A    N  
ATOM   3266  CA  LEU A 289       4.056   5.049 -46.581  1.00 90.26      A    C  
ANISOU 3266  CA  LEU A 289     9710  17463   7123   1087    309   1045  A    C  
ATOM   3267  C   LEU A 289       3.201   5.239 -45.309  1.00 93.68      A    C  
ANISOU 3267  C   LEU A 289    10157  17899   7537   1290    330   1019  A    C  
ATOM   3268  O   LEU A 289       3.662   5.894 -44.373  1.00 93.11      A    O  
ANISOU 3268  O   LEU A 289    10321  17589   7466   1283    346   1004  A    O  
ATOM   3269  CB  LEU A 289       3.870   6.196 -47.593  1.00 92.01      A    C  
ANISOU 3269  CB  LEU A 289    10151  17604   7203   1241    294   1157  A    C  
ATOM   3270  CG  LEU A 289       4.869   7.370 -47.545  1.00 97.36      A    C  
ANISOU 3270  CG  LEU A 289    11216  17939   7837   1146    298   1213  A    C  
ATOM   3271  CD1 LEU A 289       6.328   6.897 -47.508  1.00 95.66      A    C  
ANISOU 3271  CD1 LEU A 289    10960  17665   7721    777    298   1175  A    C  
ATOM   3272  CD2 LEU A 289       4.676   8.290 -48.741  1.00101.98      A    C  
ANISOU 3272  CD2 LEU A 289    12005  18465   8278   1282    286   1339  A    C  
ATOM   3273  N   ILE A 290       1.989   4.641 -45.254  1.00 90.65      A    N  
ANISOU 3273  N   ILE A 290     9516  17808   7120   1444    332   1013  A    N  
ATOM   3274  CA  ILE A 290       1.148   4.741 -44.055  1.00 91.66      A    C  
ANISOU 3274  CA  ILE A 290     9613  18002   7213   1641    365    996  A    C  
ATOM   3275  C   ILE A 290       1.684   3.816 -42.944  1.00 94.74      A    C  
ANISOU 3275  C   ILE A 290     9902  18357   7737   1419    382    906  A    C  
ATOM   3276  O   ILE A 290       1.621   4.174 -41.771  1.00 94.50      A    O  
ANISOU 3276  O   ILE A 290     9978  18233   7694   1509    413    881  A    O  
ATOM   3277  CB  ILE A 290      -0.386   4.579 -44.297  1.00 96.47      A    C  
ANISOU 3277  CB  ILE A 290     9968  18989   7699   1899    366   1047  A    C  
ATOM   3278  CG1 ILE A 290      -0.784   3.143 -44.699  1.00 96.09      A    C  
ANISOU 3278  CG1 ILE A 290     9544  19264   7701   1675    339   1005  A    C  
ATOM   3279  CG2 ILE A 290      -0.932   5.607 -45.291  1.00 99.31      A    C  
ANISOU 3279  CG2 ILE A 290    10446  19388   7899   2188    350   1159  A    C  
ATOM   3280  CD1 ILE A 290      -1.486   2.373 -43.592  1.00100.51      A    C  
ANISOU 3280  CD1 ILE A 290     9883  20034   8271   1663    368    968  A    C  
ATOM   3281  N   ASN A 291       2.221   2.638 -43.330  1.00 90.40      A    N  
ANISOU 3281  N   ASN A 291     9172  17876   7299   1148    367    859  A    N  
ATOM   3282  CA  ASN A 291       2.808   1.631 -42.442  1.00 88.85      A    C  
ANISOU 3282  CA  ASN A 291     8887  17645   7226    943    383    791  A    C  
ATOM   3283  C   ASN A 291       3.933   2.264 -41.612  1.00 93.95      A    C  
ANISOU 3283  C   ASN A 291     9768  18017   7911    871    388    780  A    C  
ATOM   3284  O   ASN A 291       3.980   2.097 -40.392  1.00 93.67      A    O  
ANISOU 3284  O   ASN A 291     9740  17946   7905    857    406    748  A    O  
ATOM   3285  CB  ASN A 291       3.343   0.458 -43.282  1.00 86.92      A    C  
ANISOU 3285  CB  ASN A 291     8495  17468   7064    716    372    754  A    C  
ATOM   3286  CG  ASN A 291       4.158  -0.559 -42.519  1.00 94.82      A    C  
ANISOU 3286  CG  ASN A 291     9456  18387   8183    532    393    703  A    C  
ATOM   3288  ND2 ASN A 291       5.465  -0.519 -42.692  1.00 84.39      A    N  
ANISOU 3288  ND2 ASN A 291     8008  17171   6885    506    411    678  A    N  
ATOM   3287  OD1 ASN A 291       3.628  -1.381 -41.765  1.00 81.64      A    O  
ANISOU 3287  OD1 ASN A 291     7863  16584   6571    416    395    699  A    O  
ATOM   3289  N   SER A 292       4.805   3.031 -42.291  1.00 90.91      A    N  
ANISOU 3289  N   SER A 292     9575  17462   7503    809    368    813  A    N  
ATOM   3290  CA  SER A 292       5.937   3.757 -41.722  1.00 90.39      A    C  
ANISOU 3290  CA  SER A 292     9745  17162   7438    681    359    814  A    C  
ATOM   3291  C   SER A 292       5.470   4.905 -40.813  1.00 94.60      A    C  
ANISOU 3291  C   SER A 292    10549  17527   7867    858    369    813  A    C  
ATOM   3292  O   SER A 292       6.258   5.394 -40.012  1.00 94.37      A    O  
ANISOU 3292  O   SER A 292    10721  17315   7822    730    358    792  A    O  
ATOM   3293  CB  SER A 292       6.825   4.289 -42.843  1.00 94.49      A    C  
ANISOU 3293  CB  SER A 292    10383  17588   7929    547    338    867  A    C  
ATOM   3294  OG  SER A 292       7.048   3.309 -43.846  1.00101.88      A    O  
ANISOU 3294  OG  SER A 292    11092  18696   8924    458    341    865  A    O  
ATOM   3295  N   MET A 293       4.199   5.335 -40.948  1.00 92.33      A    N  
ANISOU 3295  N   MET A 293    10271  17322   7489   1157    392    836  A    N  
ATOM   3296  CA  MET A 293       3.581   6.389 -40.142  1.00 94.29      A    C  
ANISOU 3296  CA  MET A 293    10782  17434   7610   1416    423    834  A    C  
ATOM   3297  C   MET A 293       2.879   5.808 -38.913  1.00 97.08      A    C  
ANISOU 3297  C   MET A 293    10968  17947   7972   1518    460    782  A    C  
ATOM   3298  O   MET A 293       2.761   6.501 -37.900  1.00 98.26      A    O  
ANISOU 3298  O   MET A 293    11347  17950   8036   1641    489    747  A    O  
ATOM   3299  CB  MET A 293       2.566   7.181 -40.972  1.00 98.96      A    C  
ANISOU 3299  CB  MET A 293    11466  18067   8068   1747    438    911  A    C  
ATOM   3300  CG  MET A 293       3.170   8.326 -41.743  1.00104.63      A    C  
ANISOU 3300  CG  MET A 293    12558  18491   8705   1732    419    971  A    C  
ATOM   3301  SD  MET A 293       1.927   9.362 -42.559  1.00112.23      A    S  
ANISOU 3301  SD  MET A 293    13663  19496   9486   2191    441   1086  A    S  
ATOM   3302  CE  MET A 293       1.184  10.189 -41.134  1.00111.22      A    C  
ANISOU 3302  CE  MET A 293    13802  19245   9211   2586    513   1050  A    C  
ATOM   3303  N   VAL A 294       2.403   4.546 -39.001  1.00 91.01      A    N  
ANISOU 3303  N   VAL A 294     9825  17471   7285   1456    463    776  A    N  
ATOM   3304  CA  VAL A 294       1.704   3.862 -37.905  1.00 89.93      A    C  
ANISOU 3304  CA  VAL A 294     9494  17523   7151   1508    501    745  A    C  
ATOM   3305  C   VAL A 294       2.704   3.427 -36.804  1.00 91.51      A    C  
ANISOU 3305  C   VAL A 294     9746  17588   7438   1276    494    690  A    C  
ATOM   3306  O   VAL A 294       2.401   3.616 -35.624  1.00 91.98      A    O  
ANISOU 3306  O   VAL A 294     9869  17640   7438   1370    528    659  A    O  
ATOM   3307  CB  VAL A 294       0.783   2.717 -38.428  1.00 92.92      A    C  
ANISOU 3307  CB  VAL A 294     9494  18256   7558   1481    502    769  A    C  
ATOM   3308  CG1 VAL A 294       0.272   1.821 -37.303  1.00 92.24      A    C  
ANISOU 3308  CG1 VAL A 294     9207  18355   7485   1436    539    747  A    C  
ATOM   3309  CG2 VAL A 294      -0.396   3.290 -39.210  1.00 94.41      A    C  
ANISOU 3309  CG2 VAL A 294     9608  18655   7609   1763    508    835  A    C  
ATOM   3310  N   ASN A 295       3.898   2.907 -37.196  1.00 85.71      A    N  
ANISOU 3310  N   ASN A 295     8984  16764   6817   1001    454    684  A    N  
ATOM   3311  CA  ASN A 295       4.996   2.450 -36.316  1.00 84.16      A    C  
ANISOU 3311  CA  ASN A 295     8801  16483   6694    780    437    655  A    C  
ATOM   3312  C   ASN A 295       5.475   3.468 -35.237  1.00 88.83      A    C  
ANISOU 3312  C   ASN A 295     9682  16875   7195    779    429    622  A    C  
ATOM   3313  O   ASN A 295       5.552   3.054 -34.078  1.00 87.45      A    O  
ANISOU 3313  O   ASN A 295     9463  16741   7022    738    438    595  A    O  
ATOM   3314  CB  ASN A 295       6.202   1.967 -37.138  1.00 82.25      A    C  
ANISOU 3314  CB  ASN A 295     8499  16207   6547    552    403    673  A    C  
ATOM   3315  CG  ASN A 295       6.079   0.581 -37.726  1.00 99.46      A    C  
ANISOU 3315  CG  ASN A 295    10415  18550   8826    481    416    677  A    C  
ATOM   3317  ND2 ASN A 295       7.207   0.039 -38.148  1.00 85.20      A    N  
ANISOU 3317  ND2 ASN A 295     8558  16722   7090    318    403    686  A    N  
ATOM   3316  OD1 ASN A 295       4.995  -0.017 -37.816  1.00 97.11      A    O  
ANISOU 3316  OD1 ASN A 295     9966  18405   8525    563    440    673  A    O  
ATOM   3318  N   PRO A 296       5.814   4.760 -35.543  1.00 87.43      A    N  
ANISOU 3318  N   PRO A 296     9823  16474   6920    802    411    622  A    N  
ATOM   3319  CA  PRO A 296       6.283   5.669 -34.472  1.00 88.90      A    C  
ANISOU 3319  CA  PRO A 296    10326  16454   6998    755    399    572  A    C  
ATOM   3320  C   PRO A 296       5.204   6.128 -33.492  1.00 95.20      A    C  
ANISOU 3320  C   PRO A 296    11247  17248   7676   1040    457    526  A    C  
ATOM   3321  O   PRO A 296       5.538   6.727 -32.475  1.00 95.63      A    O  
ANISOU 3321  O   PRO A 296    11540  17160   7635    995    453    467  A    O  
ATOM   3322  CB  PRO A 296       6.891   6.856 -35.240  1.00 91.86      A    C  
ANISOU 3322  CB  PRO A 296    11036  16574   7291    673    367    593  A    C  
ATOM   3323  CG  PRO A 296       6.943   6.424 -36.681  1.00 94.87      A    C  
ANISOU 3323  CG  PRO A 296    11221  17063   7761    647    358    662  A    C  
ATOM   3324  CD  PRO A 296       5.827   5.457 -36.843  1.00 89.28      A    C  
ANISOU 3324  CD  PRO A 296    10184  16616   7122    846    398    668  A    C  
ATOM   3325  N   VAL A 297       3.922   5.862 -33.798  1.00 93.56      A    N  
ANISOU 3325  N   VAL A 297    10871  17226   7452   1329    512    553  A    N  
ATOM   3326  CA  VAL A 297       2.775   6.201 -32.942  1.00 95.60      A    C  
ANISOU 3326  CA  VAL A 297    11174  17570   7580   1650    585    527  A    C  
ATOM   3327  C   VAL A 297       2.594   5.065 -31.926  1.00100.24      A    C  
ANISOU 3327  C   VAL A 297    11473  18389   8225   1560    605    512  A    C  
ATOM   3328  O   VAL A 297       2.327   5.334 -30.753  1.00101.06      A    O  
ANISOU 3328  O   VAL A 297    11691  18483   8222   1665    645    463  A    O  
ATOM   3329  CB  VAL A 297       1.485   6.494 -33.761  1.00100.60      A    C  
ANISOU 3329  CB  VAL A 297    11712  18373   8138   2003    633    587  A    C  
ATOM   3330  CG1 VAL A 297       0.296   6.799 -32.853  1.00102.26      A    C  
ANISOU 3330  CG1 VAL A 297    11925  18738   8192   2367    721    572  A    C  
ATOM   3331  CG2 VAL A 297       1.705   7.638 -34.753  1.00101.71      A    C  
ANISOU 3331  CG2 VAL A 297    12175  18260   8211   2103    614    620  A    C  
ATOM   3332  N   ILE A 298       2.788   3.801 -32.375  1.00 96.10      A    N  
ANISOU 3332  N   ILE A 298    10611  18049   7854   1361    579    553  A    N  
ATOM   3333  CA  ILE A 298       2.714   2.594 -31.539  1.00 95.31      A    C  
ANISOU 3333  CA  ILE A 298    10257  18138   7818   1238    594    560  A    C  
ATOM   3334  C   ILE A 298       3.840   2.617 -30.485  1.00100.80      A    C  
ANISOU 3334  C   ILE A 298    11102  18685   8512   1052    561    520  A    C  
ATOM   3335  O   ILE A 298       3.573   2.364 -29.309  1.00101.46      A    O  
ANISOU 3335  O   ILE A 298    11163  18854   8534   1091    595    503  A    O  
ATOM   3336  CB  ILE A 298       2.727   1.285 -32.394  1.00 96.48      A    C  
ANISOU 3336  CB  ILE A 298    10103  18441   8115   1059    574    608  A    C  
ATOM   3337  CG1 ILE A 298       1.509   1.213 -33.353  1.00 96.98      A    C  
ANISOU 3337  CG1 ILE A 298     9987  18718   8145   1213    599    646  A    C  
ATOM   3338  CG2 ILE A 298       2.812   0.027 -31.499  1.00 96.70      A    C  
ANISOU 3338  CG2 ILE A 298     9948  18589   8205    904    589    625  A    C  
ATOM   3339  CD1 ILE A 298       1.475  -0.013 -34.307  1.00 99.62      A    C  
ANISOU 3339  CD1 ILE A 298    10079  19179   8594   1016    575    674  A    C  
ATOM   3340  N   TYR A 299       5.084   2.940 -30.904  1.00 97.89      A    N  
ANISOU 3340  N   TYR A 299    10873  18131   8189    845    494    514  A    N  
ATOM   3341  CA  TYR A 299       6.250   3.000 -30.018  1.00 98.25      A    C  
ANISOU 3341  CA  TYR A 299    11033  18085   8213    633    444    490  A    C  
ATOM   3342  C   TYR A 299       6.196   4.152 -28.994  1.00105.13      A    C  
ANISOU 3342  C   TYR A 299    12241  18799   8903    712    452    413  A    C  
ATOM   3343  O   TYR A 299       6.724   4.002 -27.888  1.00104.85      A    O  
ANISOU 3343  O   TYR A 299    12240  18785   8814    598    431    386  A    O  
ATOM   3344  CB  TYR A 299       7.563   3.018 -30.821  1.00 98.69      A    C  
ANISOU 3344  CB  TYR A 299    11101  18056   8339    381    373    519  A    C  
ATOM   3345  CG  TYR A 299       8.004   1.636 -31.264  1.00 98.68      A    C  
ANISOU 3345  CG  TYR A 299    10786  18216   8492    271    366    582  A    C  
ATOM   3346  CD1 TYR A 299       8.293   0.642 -30.331  1.00 99.74      A    C  
ANISOU 3346  CD1 TYR A 299    10765  18469   8662    195    363    610  A    C  
ATOM   3347  CD2 TYR A 299       8.162   1.332 -32.611  1.00 99.14      A    C  
ANISOU 3347  CD2 TYR A 299    10737  18292   8640    256    367    615  A    C  
ATOM   3348  CE1 TYR A 299       8.681  -0.637 -30.730  1.00 98.61      A    C  
ANISOU 3348  CE1 TYR A 299    10394  18432   8643    133    368    669  A    C  
ATOM   3349  CE2 TYR A 299       8.578   0.062 -33.022  1.00 99.14      A    C  
ANISOU 3349  CE2 TYR A 299    10503  18407   8759    178    372    659  A    C  
ATOM   3350  CZ  TYR A 299       8.828  -0.923 -32.076  1.00105.56      A    C  
ANISOU 3350  CZ  TYR A 299    11194  19308   9607    128    376    685  A    C  
ATOM   3351  OH  TYR A 299       9.234  -2.181 -32.464  1.00105.04      A    O  
ANISOU 3351  OH  TYR A 299    10954  19314   9641     88    392    730  A    O  
ATOM   3352  N   ALA A 300       5.531   5.272 -29.349  1.00103.89      A    N  
ANISOU 3352  N   ALA A 300    12350  18486   8636    926    486    378  A    N  
ATOM   3353  CA  ALA A 300       5.366   6.439 -28.480  1.00106.14      A    C  
ANISOU 3353  CA  ALA A 300    13035  18569   8724   1052    511    291  A    C  
ATOM   3354  C   ALA A 300       4.147   6.315 -27.551  1.00111.06      A    C  
ANISOU 3354  C   ALA A 300    13600  19355   9244   1364    605    262  A    C  
ATOM   3355  O   ALA A 300       3.968   7.154 -26.664  1.00112.75      A    O  
ANISOU 3355  O   ALA A 300    14139  19426   9277   1495    640    178  A    O  
ATOM   3356  CB  ALA A 300       5.267   7.705 -29.317  1.00108.55      A    C  
ANISOU 3356  CB  ALA A 300    13701  18602   8940   1172    515    280  A    C  
ATOM   3357  N   LEU A 301       3.320   5.271 -27.743  1.00106.55      A    N  
ANISOU 3357  N   LEU A 301    12627  19088   8767   1466    650    330  A    N  
ATOM   3358  CA  LEU A 301       2.131   5.039 -26.918  1.00107.60      A    C  
ANISOU 3358  CA  LEU A 301    12627  19457   8798   1731    745    328  A    C  
ATOM   3359  C   LEU A 301       2.174   3.752 -26.085  1.00109.80      A    C  
ANISOU 3359  C   LEU A 301    12590  19979   9150   1559    748    368  A    C  
ATOM   3360  O   LEU A 301       1.406   3.636 -25.124  1.00110.68      A    O  
ANISOU 3360  O   LEU A 301    12637  20270   9146   1718    822    360  A    O  
ATOM   3361  CB  LEU A 301       0.843   5.087 -27.758  1.00108.53      A    C  
ANISOU 3361  CB  LEU A 301    12568  19776   8893   2040    811    386  A    C  
ATOM   3362  CG  LEU A 301       0.338   6.468 -28.191  1.00116.22      A    C  
ANISOU 3362  CG  LEU A 301    13880  20570   9707   2388    855    357  A    C  
ATOM   3363  CD1 LEU A 301      -0.780   6.335 -29.199  1.00117.03      A    C  
ANISOU 3363  CD1 LEU A 301    13731  20920   9816   2632    890    446  A    C  
ATOM   3364  CD2 LEU A 301      -0.161   7.288 -27.003  1.00121.96      A    C  
ANISOU 3364  CD2 LEU A 301    14865  21267  10209   2693    947    281  A    C  
ATOM   3365  N   ARG A 302       3.058   2.795 -26.437  1.00103.45      A    N  
ANISOU 3365  N   ARG A 302    11606  19182   8519   1255    676    419  A    N  
ATOM   3366  CA  ARG A 302       3.143   1.524 -25.716  1.00101.79      A    C  
ANISOU 3366  CA  ARG A 302    11138  19158   8377   1099    678    475  A    C  
ATOM   3367  C   ARG A 302       4.445   1.330 -24.943  1.00105.34      A    C  
ANISOU 3367  C   ARG A 302    11682  19507   8834    861    607    465  A    C  
ATOM   3368  O   ARG A 302       4.386   0.854 -23.809  1.00105.79      A    O  
ANISOU 3368  O   ARG A 302    11682  19682   8833    835    627    480  A    O  
ATOM   3369  CB  ARG A 302       2.865   0.333 -26.638  1.00 98.86      A    C  
ANISOU 3369  CB  ARG A 302    10463  18928   8172    995    675    558  A    C  
ATOM   3370  CG  ARG A 302       1.397   0.251 -27.043  1.00104.12      A    C  
ANISOU 3370  CG  ARG A 302    10935  19837   8791   1184    749    591  A    C  
ATOM   3371  CD  ARG A 302       0.943  -1.165 -27.310  1.00108.31      A    C  
ANISOU 3371  CD  ARG A 302    11169  20564   9420   1015    762    671  A    C  
ATOM   3372  NE  ARG A 302       0.805  -1.931 -26.073  1.00114.78      A    N  
ANISOU 3372  NE  ARG A 302    11924  21485  10201    928    793    708  A    N  
ATOM   3373  CZ  ARG A 302       1.287  -3.155 -25.894  1.00129.99      A    C  
ANISOU 3373  CZ  ARG A 302    13741  23423  12228    708    778    773  A    C  
ATOM   3374  NH1 ARG A 302       1.124  -3.774 -24.733  1.00120.49      A    N1+
ANISOU 3374  NH1 ARG A 302    12505  22308  10969    649    809    820  A    N1+
ATOM   3375  NH2 ARG A 302       1.935  -3.770 -26.874  1.00115.40      A    N  
ANISOU 3375  NH2 ARG A 302    11839  21486  10521    561    738    795  A    N  
ATOM   3376  N   SER A 303       5.603   1.692 -25.523  1.00101.47      A    N  
ANISOU 3376  N   SER A 303    11317  18840   8398    683    524    451  A    N  
ATOM   3377  CA  SER A 303       6.884   1.550 -24.827  1.00101.55      A    C  
ANISOU 3377  CA  SER A 303    11376  18818   8390    446    445    456  A    C  
ATOM   3378  C   SER A 303       7.096   2.671 -23.805  1.00108.73      A    C  
ANISOU 3378  C   SER A 303    12605  19613   9096    441    427    358  A    C  
ATOM   3379  O   SER A 303       7.204   3.842 -24.174  1.00109.45      A    O  
ANISOU 3379  O   SER A 303    12995  19495   9097    461    414    283  A    O  
ATOM   3380  CB  SER A 303       8.047   1.472 -25.808  1.00103.95      A    C  
ANISOU 3380  CB  SER A 303    11649  19047   8800    244    367    492  A    C  
ATOM   3381  OG  SER A 303       9.270   1.252 -25.123  1.00111.77      A    O  
ANISOU 3381  OG  SER A 303    12633  20083   9752     23    288    516  A    O  
ATOM   3382  N   GLU A 304       7.141   2.294 -22.517  1.00107.00      A    N  
ANISOU 3382  N   GLU A 304    12350  19517   8787    408    429    360  A    N  
ATOM   3383  CA  GLU A 304       7.322   3.203 -21.382  1.00109.42      A    C  
ANISOU 3383  CA  GLU A 304    12954  19745   8874    386    413    259  A    C  
ATOM   3384  C   GLU A 304       8.684   3.893 -21.363  1.00115.37      A    C  
ANISOU 3384  C   GLU A 304    13913  20366   9557     85    293    220  A    C  
ATOM   3385  O   GLU A 304       8.768   5.047 -20.939  1.00117.33      A    O  
ANISOU 3385  O   GLU A 304    14537  20424   9619     55    278    103  A    O  
ATOM   3386  CB  GLU A 304       7.076   2.472 -20.054  1.00111.02      A    C  
ANISOU 3386  CB  GLU A 304    13022  20159   9000    409    442    291  A    C  
ATOM   3387  CG  GLU A 304       5.604   2.302 -19.716  1.00120.13      A    C  
ANISOU 3387  CG  GLU A 304    14110  21435  10097    705    572    285  A    C  
ATOM   3388  CD  GLU A 304       5.305   1.318 -18.601  1.00133.22      A    C  
ANISOU 3388  CD  GLU A 304    15555  23340  11722    701    610    362  A    C  
ATOM   3389  OE1 GLU A 304       5.975   1.385 -17.544  1.00129.54      A    O  
ANISOU 3389  OE1 GLU A 304    15179  22909  11132    572    558    346  A    O  
ATOM   3390  OE2 GLU A 304       4.391   0.481 -18.782  1.00119.35      A    O1-
ANISOU 3390  OE2 GLU A 304    13547  21754  10048    808    689    447  A    O1-
ATOM   3391  N   GLU A 305       9.745   3.193 -21.807  1.00111.21      A    N  
ANISOU 3391  N   GLU A 305    13151  19950   9155   -140    212    318  A    N  
ATOM   3392  CA  GLU A 305      11.105   3.742 -21.843  1.00112.39      A    C  
ANISOU 3392  CA  GLU A 305    13407  20066   9228   -464     93    311  A    C  
ATOM   3393  C   GLU A 305      11.257   4.852 -22.901  1.00117.23      A    C  
ANISOU 3393  C   GLU A 305    14287  20426   9828   -536     77    254  A    C  
ATOM   3394  O   GLU A 305      12.004   5.807 -22.668  1.00118.55      A    O  
ANISOU 3394  O   GLU A 305    14742  20468   9833   -783      1    187  A    O  
ATOM   3395  CB  GLU A 305      12.153   2.636 -22.026  1.00112.62      A    C  
ANISOU 3395  CB  GLU A 305    13072  20336   9382   -616     30    452  A    C  
ATOM   3396  CG  GLU A 305      12.224   1.639 -20.883  1.00123.26      A    C  
ANISOU 3396  CG  GLU A 305    14221  21915  10695   -598     21    524  A    C  
ATOM   3397  CD  GLU A 305      13.253   0.548 -21.090  1.00143.83      A    C  
ANISOU 3397  CD  GLU A 305    16499  24746  13404   -686    -31    675  A    C  
ATOM   3398  OE1 GLU A 305      14.425   0.757 -20.702  1.00141.05      A    O  
ANISOU 3398  OE1 GLU A 305    16110  24543  12941   -920   -137    709  A    O  
ATOM   3399  OE2 GLU A 305      12.891  -0.515 -21.645  1.00134.81      A    O1-
ANISOU 3399  OE2 GLU A 305    15144  23641  12435   -520     35    761  A    O1-
ATOM   3400  N   ILE A 306      10.533   4.739 -24.042  1.00112.62      A    N  
ANISOU 3400  N   ILE A 306    13627  19770   9395   -337    146    283  A    N  
ATOM   3401  CA  ILE A 306      10.523   5.760 -25.099  1.00113.37      A    C  
ANISOU 3401  CA  ILE A 306    13975  19622   9478   -352    145    248  A    C  
ATOM   3402  C   ILE A 306       9.641   6.936 -24.617  1.00121.00      A    C  
ANISOU 3402  C   ILE A 306    15380  20331  10262   -152    203    124  A    C  
ATOM   3403  O   ILE A 306       9.943   8.093 -24.918  1.00122.24      A    O  
ANISOU 3403  O   ILE A 306    15927  20221  10298   -264    174     64  A    O  
ATOM   3404  CB  ILE A 306      10.107   5.194 -26.506  1.00114.20      A    C  
ANISOU 3404  CB  ILE A 306    13831  19774   9787   -211    190    331  A    C  
ATOM   3405  CG1 ILE A 306      11.039   4.033 -26.951  1.00112.80      A    C  
ANISOU 3405  CG1 ILE A 306    13279  19821   9758   -390    142    440  A    C  
ATOM   3406  CG2 ILE A 306      10.086   6.298 -27.586  1.00115.35      A    C  
ANISOU 3406  CG2 ILE A 306    14254  19671   9901   -206    192    308  A    C  
ATOM   3407  CD1 ILE A 306      10.519   3.140 -28.111  1.00115.28      A    C  
ANISOU 3407  CD1 ILE A 306    13317  20218  10265   -239    197    510  A    C  
ATOM   3408  N   ARG A 307       8.584   6.628 -23.830  1.00119.32      A    N  
ANISOU 3408  N   ARG A 307    15121  20206  10009    141    292     91  A    N  
ATOM   3409  CA  ARG A 307       7.645   7.603 -23.263  1.00122.29      A    C  
ANISOU 3409  CA  ARG A 307    15874  20397  10194    417    373    -22  A    C  
ATOM   3410  C   ARG A 307       8.307   8.548 -22.253  1.00131.41      A    C  
ANISOU 3410  C   ARG A 307    17460  21361  11109    210    316   -144  A    C  
ATOM   3411  O   ARG A 307       8.088   9.760 -22.315  1.00132.97      A    O  
ANISOU 3411  O   ARG A 307    18142  21239  11140    288    340   -243  A    O  
ATOM   3412  CB  ARG A 307       6.435   6.896 -22.625  1.00121.43      A    C  
ANISOU 3412  CB  ARG A 307    15528  20521  10088    748    482     -7  A    C  
ATOM   3413  CG  ARG A 307       5.351   6.512 -23.621  1.00129.31      A    C  
ANISOU 3413  CG  ARG A 307    16300  21622  11210   1048    566     64  A    C  
ATOM   3414  CD  ARG A 307       4.133   5.930 -22.936  1.00139.83      A    C  
ANISOU 3414  CD  ARG A 307    17419  23215  12495   1344    676     80  A    C  
ATOM   3415  NE  ARG A 307       3.296   6.967 -22.328  1.00153.04      A    N  
ANISOU 3415  NE  ARG A 307    19438  24775  13934   1674    769    -21  A    N  
ATOM   3416  CZ  ARG A 307       2.197   7.470 -22.883  1.00169.53      A    C  
ANISOU 3416  CZ  ARG A 307    21589  26863  15963   2053    861    -17  A    C  
ATOM   3417  NH1 ARG A 307       1.778   7.031 -24.064  1.00156.12      A    N1+
ANISOU 3417  NH1 ARG A 307    19613  25285  14419   2116    862     83  A    N1+
ATOM   3418  NH2 ARG A 307       1.503   8.412 -22.257  1.00159.42      A    N  
ANISOU 3418  NH2 ARG A 307    20650  25475  14446   2391    955   -109  A    N  
ATOM   3419  N   SER A 308       9.111   7.993 -21.329  1.00130.64      A    N  
ANISOU 3419  N   SER A 308    17209  21453  10977    -53    240   -134  A    N  
ATOM   3420  CA  SER A 308       9.808   8.760 -20.294  1.00134.47      A    C  
ANISOU 3420  CA  SER A 308    18053  21823  11216   -310    167   -248  A    C  
ATOM   3421  C   SER A 308      11.015   9.526 -20.832  1.00142.25      A    C  
ANISOU 3421  C   SER A 308    19284  22628  12139   -732     47   -262  A    C  
ATOM   3422  O   SER A 308      11.354  10.578 -20.288  1.00144.67      A    O  
ANISOU 3422  O   SER A 308    20077  22685  12205   -911      7   -389  A    O  
ATOM   3423  CB  SER A 308      10.207   7.863 -19.128  1.00137.99      A    C  
ANISOU 3423  CB  SER A 308    18210  22587  11633   -439    121   -210  A    C  
ATOM   3424  OG  SER A 308       9.060   7.466 -18.395  1.00147.68      A    O  
ANISOU 3424  OG  SER A 308    19328  23942  12841    -85    238   -221  A    O  
ATOM   3425  N   SER A 309      11.647   9.011 -21.908  1.00139.07      A    N  
ANISOU 3425  N   SER A 309    18561  22349  11931   -902     -7   -133  A    N  
ATOM   3426  CA  SER A 309      12.799   9.642 -22.558  1.00141.11      A    C  
ANISOU 3426  CA  SER A 309    18969  22508  12140  -1319   -115   -113  A    C  
ATOM   3427  C   SER A 309      12.396  10.948 -23.258  1.00148.65      A    C  
ANISOU 3427  C   SER A 309    20454  23029  12999  -1265    -75   -190  A    C  
ATOM   3428  O   SER A 309      13.198  11.879 -23.322  1.00150.48      A    O  
ANISOU 3428  O   SER A 309    21042  23066  13067  -1644   -159   -233  A    O  
ATOM   3429  CB  SER A 309      13.455   8.681 -23.543  1.00142.95      A    C  
ANISOU 3429  CB  SER A 309    18700  23015  12600  -1430   -153     49  A    C  
ATOM   3430  OG  SER A 309      12.634   8.418 -24.668  1.00151.86      A    O  
ANISOU 3430  OG  SER A 309    19696  24081  13923  -1115    -59    102  A    O  
ATOM   3431  N   ALA A 310      11.146  11.010 -23.765  1.00146.18      A    N  
ANISOU 3431  N   ALA A 310    20197  22578  12766   -800     50   -197  A    N  
ATOM   3432  CA  ALA A 310      10.566  12.182 -24.425  1.00148.78      A    C  
ANISOU 3432  CA  ALA A 310    21026  22501  13002   -625    110   -250  A    C  
ATOM   3433  C   ALA A 310      10.248  13.280 -23.399  1.00158.32      A    C  
ANISOU 3433  C   ALA A 310    22858  23378  13917   -566    140   -421  A    C  
ATOM   3434  O   ALA A 310      10.317  14.465 -23.745  1.00160.73      A    O  
ANISOU 3434  O   ALA A 310    23729  23276  14066   -631    141   -482  A    O  
ATOM   3435  CB  ALA A 310       9.308  11.787 -25.182  1.00147.70      A    C  
ANISOU 3435  CB  ALA A 310    20679  22418  13022   -117    231   -189  A    C  
ATOM   3436  N   HIS A 311       9.903  12.873 -22.145  1.00156.49      A    N  
ANISOU 3436  N   HIS A 311    22546  23313  13598   -441    168   -496  A    N  
ATOM   3437  CA AHIS A 311       9.591  13.792 -21.049  0.50160.28      A    C  
ANISOU 3437  CA AHIS A 311    23594  23522  13782   -363    205   -673  A    C  
ATOM   3438  CA BHIS A 311       9.588  13.774 -21.031  0.50160.06      A    C  
ANISOU 3438  CA BHIS A 311    23557  23503  13755   -361    206   -673  A    C  
ATOM   3439  C   HIS A 311      10.857  14.471 -20.524  1.00167.48      A    C  
ANISOU 3439  C   HIS A 311    24872  24281  14482   -952     63   -759  A    C  
ATOM   3440  O   HIS A 311      10.833  15.673 -20.255  1.00170.78      A    O  
ANISOU 3440  O   HIS A 311    25971  24272  14645  -1008     74   -899  A    O  
ATOM   3441  CB AHIS A 311       8.845  13.074 -19.914  0.50160.44      A    C  
ANISOU 3441  CB AHIS A 311    23368  23821  13771    -56    284   -712  A    C  
ATOM   3442  CB BHIS A 311       8.877  13.001 -19.899  0.50159.89      A    C  
ANISOU 3442  CB BHIS A 311    23257  23781  13713    -73    279   -705  A    C  
ATOM   3443  CG AHIS A 311       7.378  12.921 -20.163  0.50163.19      A    C  
ANISOU 3443  CG AHIS A 311    23592  24224  14188    554    448   -684  A    C  
ATOM   3444  CG BHIS A 311       8.872  13.697 -18.570  0.50166.55      A    C  
ANISOU 3444  CG BHIS A 311    24572  24466  14243   -116    284   -884  A    C  
ATOM   3447  CD2AHIS A 311       6.359  13.764 -19.875  0.50167.62      A    C  
ANISOU 3447  CD2AHIS A 311    24575  24550  14563   1011    582   -783  A    C  
ATOM   3448  CD2BHIS A 311       9.614  13.453 -17.465  0.50168.88      A    C  
ANISOU 3448  CD2BHIS A 311    24822  24939  14408   -458    189   -938  A    C  
ATOM   3445  ND1AHIS A 311       6.864  11.792 -20.773  0.50161.55      A    N  
ANISOU 3445  ND1AHIS A 311    22764  24374  14243    728    484   -534  A    N  
ATOM   3446  ND1BHIS A 311       8.022  14.755 -18.312  0.50171.57      A    N  
ANISOU 3446  ND1BHIS A 311    25805  24734  14650    243    402  -1028  A    N  
ATOM   3449  CE1AHIS A 311       5.556  11.982 -20.837  0.50161.62      A    C  
ANISOU 3449  CE1AHIS A 311    22800  24393  14217   1248    627   -540  A    C  
ATOM   3450  CE1BHIS A 311       8.277  15.125 -17.068  0.50173.51      A    C  
ANISOU 3450  CE1BHIS A 311    26370  24922  14633     92    377  -1180  A    C  
ATOM   3451  NE2AHIS A 311       5.206  13.155 -20.309  0.50165.59      A    N  
ANISOU 3451  NE2AHIS A 311    23905  24560  14453   1465    696   -681  A    N  
ATOM   3452  NE2BHIS A 311       9.227  14.370 -16.517  0.50172.33      A    N  
ANISOU 3452  NE2BHIS A 311    25842  25106  14531   -343    244  -1130  A    N  
ATOM   3453  N   HIS A 312      11.962  13.708 -20.392  1.00163.88      A    N  
ANISOU 3453  N   HIS A 312    23979  24179  14111  -1391    -69   -670  A    N  
ATOM   3454  CA  HIS A 312      13.249  14.217 -19.916  1.00167.09      A    C  
ANISOU 3454  CA  HIS A 312    24610  24564  14311  -2006   -225   -722  A    C  
ATOM   3455  C   HIS A 312      13.967  15.096 -20.953  1.00172.23      A    C  
ANISOU 3455  C   HIS A 312    25584  24935  14922  -2376   -291   -691  A    C  
ATOM   3456  O   HIS A 312      14.778  15.942 -20.570  1.00174.40      A    O  
ANISOU 3456  O   HIS A 312    26302  25020  14940  -2857   -392   -781  A    O  
ATOM   3457  CB  HIS A 312      14.150  13.071 -19.425  1.00166.63      A    C  
ANISOU 3457  CB  HIS A 312    23930  25041  14340  -2291   -337   -610  A    C  
ATOM   3458  CG  HIS A 312      13.722  12.481 -18.113  1.00170.32      A    C  
ANISOU 3458  CG  HIS A 312    24238  25736  14741  -2085   -306   -662  A    C  
ATOM   3460  CD2 HIS A 312      13.170  11.273 -17.846  1.00169.49      A    C  
ANISOU 3460  CD2 HIS A 312    23616  25955  14826  -1745   -237   -566  A    C  
ATOM   3459  ND1 HIS A 312      13.894  13.165 -16.920  1.00175.73      A    N  
ANISOU 3459  ND1 HIS A 312    25344  26314  15112  -2270   -350   -825  A    N  
ATOM   3461  CE1 HIS A 312      13.426  12.364 -15.976  1.00174.11      A    C  
ANISOU 3461  CE1 HIS A 312    24845  26387  14921  -2014   -302   -817  A    C  
ATOM   3462  NE2 HIS A 312      12.980  11.215 -16.484  1.00170.69      A    N  
ANISOU 3462  NE2 HIS A 312    23852  26213  14788  -1703   -233   -657  A    N  
ATOM   3463  N   CYS A 313      13.659  14.903 -22.257  1.00167.86      A    N  
ANISOU 3463  N   CYS A 313    24819  24361  14599  -2178   -236   -564  A    N  
ATOM   3464  CA  CYS A 313      14.226  15.670 -23.374  1.00169.56      A    C  
ANISOU 3464  CA  CYS A 313    25302  24326  14797  -2476   -279   -506  A    C  
ATOM   3465  C   CYS A 313      13.548  17.032 -23.538  1.00178.04      A    C  
ANISOU 3465  C   CYS A 313    27183  24790  15673  -2294   -199   -626  A    C  
ATOM   3466  O   CYS A 313      14.209  17.996 -23.929  1.00180.48      A    O  
ANISOU 3466  O   CYS A 313    27970  24787  15816  -2709   -264   -643  A    O  
ATOM   3467  CB  CYS A 313      14.184  14.866 -24.670  1.00166.24      A    C  
ANISOU 3467  CB  CYS A 313    24340  24143  14681  -2320   -249   -325  A    C  
ATOM   3468  SG  CYS A 313      15.560  13.705 -24.869  1.00167.71      A    S  
ANISOU 3468  SG  CYS A 313    23772  24932  15019  -2745   -375   -163  A    S  
ATOM   3469  N   LEU A 314      12.234  17.108 -23.232  1.00175.61      A    N  
ANISOU 3469  N   LEU A 314    27031  24326  15365  -1670    -53   -699  A    N  
ATOM   3470  CA  LEU A 314      11.422  18.328 -23.306  1.00179.36      A    C  
ANISOU 3470  CA  LEU A 314    28263  24244  15643  -1338     54   -809  A    C  
ATOM   3471  C   LEU A 314      11.837  19.353 -22.234  1.00189.26      A    C  
ANISOU 3471  C   LEU A 314    30249  25126  16536  -1661      6  -1006  A    C  
ATOM   3472  O   LEU A 314      11.606  20.549 -22.416  1.00192.77      A    O  
ANISOU 3472  O   LEU A 314    31453  25020  16771  -1645     45  -1085  A    O  
ATOM   3473  CB  LEU A 314       9.926  17.979 -23.176  1.00177.99      A    C  
ANISOU 3473  CB  LEU A 314    27935  24142  15549   -568    222   -820  A    C  
ATOM   3474  CG  LEU A 314       8.927  18.983 -23.758  1.00185.71      A    C  
ANISOU 3474  CG  LEU A 314    29559  24635  16368    -45    364   -879  A    C  
ATOM   3475  CD1 LEU A 314       8.720  18.757 -25.247  1.00185.27      A    C  
ANISOU 3475  CD1 LEU A 314    29511  24435  16449     41    377   -726  A    C  
ATOM   3476  CD2 LEU A 314       7.593  18.886 -23.047  1.00187.34      A    C  
ANISOU 3476  CD2 LEU A 314    29574  25025  16580    652    519   -913  A    C  
ATOM   3477  N   ALA A 315      12.454  18.880 -21.129  1.00186.72      A    N  
ANISOU 3477  N   ALA A 315    29722  25098  16126  -1963    -80  -1080  A    N  
ATOM   3478  CA  ALA A 315      12.948  19.711 -20.027  1.00191.51      A    C  
ANISOU 3478  CA  ALA A 315    30950  25438  16375  -2342   -148  -1274  A    C  
ATOM   3479  C   ALA A 315      14.147  20.563 -20.467  1.00200.34      A    C  
ANISOU 3479  C   ALA A 315    32478  26313  17330  -3080   -293  -1269  A    C  
ATOM   3480  O   ALA A 315      14.261  21.716 -20.045  1.00202.94      A    O  
ANISOU 3480  O   ALA A 315    33272  26286  17551  -3098   -316  -1431  A    O  
ATOM   3481  CB  ALA A 315      13.330  18.837 -18.842  1.00190.87      A    C  
ANISOU 3481  CB  ALA A 315    30419  25834  16268  -2505   -222  -1312  A    C  
ATOM   3482  N   HIS A 316      15.029  19.995 -21.319  1.00194.99      A    N  
ANISOU 3482  N   HIS A 316    31250  25979  16858  -3447   -393  -1078  A    N  
ATOM   3483  CA  HIS A 316      16.214  20.669 -21.862  1.00197.95      A    C  
ANISOU 3483  CA  HIS A 316    31870  26239  17101  -4172   -530  -1026  A    C  
ATOM   3484  C   HIS A 316      15.862  21.561 -23.063  1.00202.42      A    C  
ANISOU 3484  C   HIS A 316    32290  26494  18128  -3521   -452   -972  A    C  
ATOM   3485  O   HIS A 316      16.558  22.549 -23.308  1.00201.85      A    O  
ANISOU 3485  O   HIS A 316    32114  26287  18291  -3533   -521   -999  A    O  
ATOM   3486  CB  HIS A 316      17.294  19.647 -22.253  1.00195.27      A    C  
ANISOU 3486  CB  HIS A 316    30679  26555  16959  -4569   -655   -834  A    C  
ATOM   3487  CG  HIS A 316      17.924  18.956 -21.084  1.00197.87      A    C  
ANISOU 3487  CG  HIS A 316    30598  27373  17212  -4836   -766   -867  A    C  
ATOM   3489  CD2 HIS A 316      17.631  17.759 -20.526  1.00195.88      A    C  
ANISOU 3489  CD2 HIS A 316    29721  27569  17136  -4481   -738   -828  A    C  
ATOM   3488  ND1 HIS A 316      18.982  19.522 -20.399  1.00198.77      A    N  
ANISOU 3488  ND1 HIS A 316    30428  27518  17577  -4757   -914   -945  A    N  
ATOM   3490  CE1 HIS A 316      19.292  18.661 -19.443  1.00197.57      A    C  
ANISOU 3490  CE1 HIS A 316    29933  27816  17318  -4923   -985   -940  A    C  
ATOM   3491  NE2 HIS A 316      18.507  17.585 -19.481  1.00197.10      A    N  
ANISOU 3491  NE2 HIS A 316    29729  28064  17095  -4945   -881   -865  A    N  
ATOM   3492  N   TRP A 317      14.786  21.209 -23.804  1.00201.40      A    N  
ANISOU 3492  N   TRP A 317    32618  26122  17784  -3352   -305   -892  A    N  
ATOM   3493  CA  TRP A 317      14.294  21.942 -24.976  1.00203.15      A    C  
ANISOU 3493  CA  TRP A 317    33260  25901  18028  -3109   -217   -818  A    C  
ATOM   3494  C   TRP A 317      13.566  23.241 -24.615  1.00206.28      A    C  
ANISOU 3494  C   TRP A 317    33109  26264  19005  -2132   -140   -979  A    C  
ATOM   3495  O   TRP A 317      13.650  24.211 -25.370  1.00206.02      A    O  
ANISOU 3495  O   TRP A 317    33034  26043  19200  -2037   -136   -949  A    O  
ATOM   3496  CB  TRP A 317      13.378  21.051 -25.824  1.00197.69      A    C  
ANISOU 3496  CB  TRP A 317    31953  25490  17672  -2468   -107   -671  A    C  
ATOM   3497  CG  TRP A 317      14.092  20.296 -26.904  1.00195.96      A    C  
ANISOU 3497  CG  TRP A 317    31067  25689  17702  -2749   -179   -470  A    C  
ATOM   3498  CD1 TRP A 317      14.356  18.959 -26.931  1.00194.64      A    C  
ANISOU 3498  CD1 TRP A 317    30043  26129  17782  -2755   -218   -377  A    C  
ATOM   3499  CD2 TRP A 317      14.612  20.834 -28.128  1.00197.29      A    C  
ANISOU 3499  CD2 TRP A 317    31398  25686  17878  -3041   -210   -335  A    C  
ATOM   3501  CE2 TRP A 317      15.186  19.761 -28.846  1.00197.52      A    C  
ANISOU 3501  CE2 TRP A 317    30619  26269  18162  -3200   -263   -173  A    C  
ATOM   3502  CE3 TRP A 317      14.654  22.123 -28.687  1.00202.87      A    C  
ANISOU 3502  CE3 TRP A 317    32884  25813  18386  -3179   -192   -331  A    C  
ATOM   3500  NE1 TRP A 317      15.015  18.629 -28.092  1.00192.66      A    N  
ANISOU 3500  NE1 TRP A 317    29412  26101  17688  -3010   -266   -205  A    N  
ATOM   3503  CZ2 TRP A 317      15.795  19.937 -30.095  1.00197.00      A    C  
ANISOU 3503  CZ2 TRP A 317    30466  26231  18154  -3490   -296    -11  A    C  
ATOM   3504  CZ3 TRP A 317      15.259  22.295 -29.923  1.00204.26      A    C  
ANISOU 3504  CZ3 TRP A 317    32977  26008  18625  -3493   -231   -158  A    C  
ATOM   3505  CH2 TRP A 317      15.821  21.212 -30.613  1.00200.91      A    C  
ANISOU 3505  CH2 TRP A 317    31707  26177  18453  -3646   -281     -2  A    C  
ATOM   3506  N   LYS A 318      12.834  23.249 -23.481  1.00203.53      A    N  
ANISOU 3506  N   LYS A 318    32832  25935  18566  -1780    -69  -1144  A    N  
ATOM   3507  CA  LYS A 318      12.070  24.403 -22.992  1.00204.46      A    C  
ANISOU 3507  CA  LYS A 318    32924  25906  18856  -1307     15  -1318  A    C  
ATOM   3508  C   LYS A 318      12.916  25.351 -22.132  1.00207.82      A    C  
ANISOU 3508  C   LYS A 318    32715  26563  19684  -1364   -114  -1499  A    C  
ATOM   3509  O   LYS A 318      12.858  26.565 -22.336  1.00208.85      A    O  
ANISOU 3509  O   LYS A 318    32759  26525  20069  -1248   -103  -1568  A    O  
ATOM   3510  CB  LYS A 318      10.813  23.950 -22.227  1.00206.42      A    C  
ANISOU 3510  CB  LYS A 318    33059  26319  19051   -799    151  -1411  A    C  
ATOM   3511  CG  LYS A 318       9.680  23.460 -23.128  1.00210.57      A    C  
ANISOU 3511  CG  LYS A 318    32570  27338  20100   -257    257  -1259  A    C  
ATOM   3512  CD  LYS A 318       8.461  22.995 -22.332  1.00213.22      A    C  
ANISOU 3512  CD  LYS A 318    32176  28161  20678    108    366  -1346  A    C  
ATOM   3513  CE  LYS A 318       7.460  24.100 -22.079  1.00225.90      A    C  
ANISOU 3513  CE  LYS A 318    32766  30127  22939    241    431  -1481  A    C  
ATOM   3514  NZ  LYS A 318       6.287  23.610 -21.309  1.00235.59      A    N1+
ANISOU 3514  NZ  LYS A 318    33104  31893  24518    233    526  -1568  A    N1+
ATOM   3515  N   LYS A 319      13.690  24.801 -21.172  1.00205.31      A    N  
ANISOU 3515  N   LYS A 319    32511  26368  19130  -1722   -226  -1573  A    N  
ATOM   3516  CA  LYS A 319      14.546  25.578 -20.273  1.00220.98      A    C  
ANISOU 3516  CA  LYS A 319    31905  29440  22618   -765   -398  -1739  A    C  
ATOM   3517  C   LYS A 319      15.950  25.778 -20.845  1.00231.84      A    C  
ANISOU 3517  C   LYS A 319    30999  30746  26343    -93   -379  -1152  A    C  
ATOM   3518  O   LYS A 319      16.575  24.830 -21.317  1.00213.34      A    O  
ANISOU 3518  O   LYS A 319    31497  28205  21357  -1576   -572  -1472  A    O  
ATOM   3519  CB  LYS A 319      14.609  24.931 -18.877  1.00222.57      A    C  
ANISOU 3519  CB  LYS A 319    31864  29953  22749   -629   -459  -1871  A    C  
ATOM   3520  CG  LYS A 319      13.359  25.154 -18.019  1.00232.05      A    C  
ANISOU 3520  CG  LYS A 319    31969  31494  24707    -88   -338  -1891  A    C  
ATOM   3521  CD  LYS A 319      13.369  26.489 -17.261  1.00232.20      A    C  
ANISOU 3521  CD  LYS A 319    31308  30862  26054    -77   -260  -1556  A    C  
ATOM   3522  CE  LYS A 319      14.104  26.421 -15.943  1.00234.79      A    C  
ANISOU 3522  CE  LYS A 319    31317  30925  26970    -86   -280  -1337  A    C  
ATOM   3523  NZ  LYS A 319      14.198  27.756 -15.303  1.00236.41      A    N1+
ANISOU 3523  NZ  LYS A 319    31168  30796  27860    -78   -227  -1136  A    N1+
ATOM   1583  N   ASN A1001      -2.490 -16.463 -11.094  1.00 61.05      A    N  
ANISOU 1583  N   ASN A1001     5803  13013   4380   -280    193    696  A    N  
ATOM   1584  CA  ASN A1001      -2.868 -16.945  -9.764  1.00 60.84      A    C  
ANISOU 1584  CA  ASN A1001     5755  12971   4390   -249    190    626  A    C  
ATOM   1585  C   ASN A1001      -2.704 -15.879  -8.718  1.00 67.43      A    C  
ANISOU 1585  C   ASN A1001     6643  13705   5272   -260    210    601  A    C  
ATOM   1586  O   ASN A1001      -1.963 -14.922  -8.932  1.00 69.59      A    O  
ANISOU 1586  O   ASN A1001     6965  13918   5558   -317    231    619  A    O  
ATOM   1587  CB  ASN A1001      -1.881 -18.049  -9.355  1.00 60.68      A    C  
ANISOU 1587  CB  ASN A1001     5683  13023   4349   -292    191    564  A    C  
ATOM   1588  CG  ASN A1001      -2.269 -19.434  -9.747  1.00 82.83      A    C  
ANISOU 1588  CG  ASN A1001     8428  15907   7136   -263    173    547  A    C  
ATOM   1590  ND2 ASN A1001      -1.300 -20.336  -9.763  1.00 76.35      A    N  
ANISOU 1590  ND2 ASN A1001     7569  15143   6297   -292    170    505  A    N  
ATOM   1589  OD1 ASN A1001      -3.429 -19.715 -10.018  1.00 76.08      A    O  
ANISOU 1589  OD1 ASN A1001     7558  15063   6286   -213    162    562  A    O  
ATOM   1591  N   ILE A1002      -3.273 -16.129  -7.529  1.00 63.04      A    N  
ANISOU 1591  N   ILE A1002     6071  13142   4740   -218    208    547  A    N  
ATOM   1592  CA  ILE A1002      -3.116 -15.312  -6.329  1.00 62.57      A    C  
ANISOU 1592  CA  ILE A1002     6041  13015   4718   -225    225    492  A    C  
ATOM   1593  C   ILE A1002      -1.735 -15.662  -5.745  1.00 68.40      A    C  
ANISOU 1593  C   ILE A1002     6756  13800   5433   -298    236    434  A    C  
ATOM   1594  O   ILE A1002      -1.042 -14.766  -5.264  1.00 70.03      A    O  
ANISOU 1594  O   ILE A1002     6990  13957   5663   -348    255    392  A    O  
ATOM   1595  CB  ILE A1002      -4.300 -15.520  -5.330  1.00 65.13      A    C  
ANISOU 1595  CB  ILE A1002     6343  13346   5056   -150    220    454  A    C  
ATOM   1596  CG1 ILE A1002      -4.125 -14.696  -4.046  1.00 65.92      A    C  
ANISOU 1596  CG1 ILE A1002     6466  13393   5188   -154    238    380  A    C  
ATOM   1597  CG2 ILE A1002      -4.571 -17.002  -5.019  1.00 65.01      A    C  
ANISOU 1597  CG2 ILE A1002     6267  13429   5005   -139    214    440  A    C  
ATOM   1598  CD1 ILE A1002      -5.360 -14.168  -3.483  1.00 73.32      A    C  
ANISOU 1598  CD1 ILE A1002     7404  14301   6155    -76    237    353  A    C  
ATOM   1599  N   PHE A1003      -1.321 -16.961  -5.837  1.00 64.10      A    N  
ANISOU 1599  N   PHE A1003     6158  13351   4846   -303    222    427  A    N  
ATOM   1600  CA  PHE A1003      -0.017 -17.491  -5.389  1.00 62.99      A    C  
ANISOU 1600  CA  PHE A1003     5982  13279   4674   -350    222    375  A    C  
ATOM   1601  C   PHE A1003       1.108 -16.803  -6.161  1.00 66.70      A    C  
ANISOU 1601  C   PHE A1003     6462  13746   5138   -434    238    375  A    C  
ATOM   1602  O   PHE A1003       2.088 -16.382  -5.554  1.00 66.46      A    O  
ANISOU 1602  O   PHE A1003     6420  13730   5102   -488    251    312  A    O  
ATOM   1603  CB  PHE A1003       0.044 -19.025  -5.585  1.00 64.06      A    C  
ANISOU 1603  CB  PHE A1003     6069  13494   4776   -319    202    381  A    C  
ATOM   1604  CG  PHE A1003       1.311 -19.711  -5.124  1.00 65.73      A    C  
ANISOU 1604  CG  PHE A1003     6240  13783   4952   -337    191    331  A    C  
ATOM   1605  CD1 PHE A1003       1.456 -20.130  -3.803  1.00 68.49      A    C  
ANISOU 1605  CD1 PHE A1003     6577  14165   5282   -303    184    295  A    C  
ATOM   1606  CD2 PHE A1003       2.352 -19.958  -6.012  1.00 67.93      A    C  
ANISOU 1606  CD2 PHE A1003     6487  14118   5207   -379    187    319  A    C  
ATOM   1607  CE1 PHE A1003       2.625 -20.770  -3.375  1.00 68.76      A    C  
ANISOU 1607  CE1 PHE A1003     6570  14280   5274   -299    166    252  A    C  
ATOM   1608  CE2 PHE A1003       3.528 -20.590  -5.579  1.00 70.39      A    C  
ANISOU 1608  CE2 PHE A1003     6750  14513   5483   -380    172    263  A    C  
ATOM   1609  CZ  PHE A1003       3.649 -20.997  -4.265  1.00 68.00      A    C  
ANISOU 1609  CZ  PHE A1003     6437  14236   5162   -333    158    232  A    C  
ATOM   1610  N   GLU A1004       0.945 -16.669  -7.498  1.00 63.27      A    N  
ANISOU 1610  N   GLU A1004     6041  13302   4695   -449    240    442  A    N  
ATOM   1611  CA  GLU A1004       1.909 -16.007  -8.380  1.00 63.07      A    C  
ANISOU 1611  CA  GLU A1004     6029  13279   4655   -538    264    462  A    C  
ATOM   1612  C   GLU A1004       1.935 -14.473  -8.184  1.00 68.73      A    C  
ANISOU 1612  C   GLU A1004     6821  13870   5422   -587    297    475  A    C  
ATOM   1613  O   GLU A1004       3.015 -13.883  -8.230  1.00 69.49      A    O  
ANISOU 1613  O   GLU A1004     6920  13964   5520   -686    328    443  A    O  
ATOM   1614  CB  GLU A1004       1.681 -16.409  -9.841  1.00 63.75      A    C  
ANISOU 1614  CB  GLU A1004     6105  13415   4703   -532    256    534  A    C  
ATOM   1615  CG  GLU A1004       1.934 -17.890 -10.088  1.00 66.24      A    C  
ANISOU 1615  CG  GLU A1004     6343  13848   4977   -505    231    496  A    C  
ATOM   1616  CD  GLU A1004       1.607 -18.415 -11.472  1.00 80.10      A    C  
ANISOU 1616  CD  GLU A1004     8072  15672   6692   -491    219    542  A    C  
ATOM   1617  OE1 GLU A1004       1.163 -17.619 -12.331  1.00 74.38      A    O  
ANISOU 1617  OE1 GLU A1004     7389  14917   5954   -500    229    621  A    O  
ATOM   1618  OE2 GLU A1004       1.796 -19.632 -11.699  1.00 69.69      A    O1-
ANISOU 1618  OE2 GLU A1004     6691  14437   5352   -467    200    498  A    O1-
ATOM   1619  N   MET A1005       0.754 -13.842  -7.925  1.00 64.65      A    N  
ANISOU 1619  N   MET A1005     6360  13250   4953   -518    292    511  A    N  
ATOM   1620  CA  MET A1005       0.590 -12.403  -7.636  1.00 64.31      A    C  
ANISOU 1620  CA  MET A1005     6398  13060   4977   -539    319    517  A    C  
ATOM   1621  C   MET A1005       1.289 -12.067  -6.302  1.00 69.10      A    C  
ANISOU 1621  C   MET A1005     6987  13657   5612   -589    337    397  A    C  
ATOM   1622  O   MET A1005       2.105 -11.145  -6.253  1.00 70.00      A    O  
ANISOU 1622  O   MET A1005     7135  13702   5759   -685    374    366  A    O  
ATOM   1623  CB  MET A1005      -0.913 -12.036  -7.557  1.00 65.94      A    C  
ANISOU 1623  CB  MET A1005     6646  13187   5222   -423    298    559  A    C  
ATOM   1624  CG  MET A1005      -1.201 -10.560  -7.295  1.00 69.63      A    C  
ANISOU 1624  CG  MET A1005     7205  13483   5770   -419    321    569  A    C  
ATOM   1625  SD  MET A1005      -2.792 -10.281  -6.453  1.00 72.32      A    S  
ANISOU 1625  SD  MET A1005     7551  13769   6158   -275    294    532  A    S  
ATOM   1626  CE  MET A1005      -3.618  -9.315  -7.656  1.00 70.29      A    C  
ANISOU 1626  CE  MET A1005     7402  13350   5955   -214    294    647  A    C  
ATOM   1627  N   LEU A1006       0.977 -12.829  -5.238  1.00 65.07      A    N  
ANISOU 1627  N   LEU A1006     6421  13221   5081   -530    313    329  A    N  
ATOM   1628  CA  LEU A1006       1.533 -12.624  -3.903  1.00 65.60      A    C  
ANISOU 1628  CA  LEU A1006     6458  13314   5154   -557    321    212  A    C  
ATOM   1629  C   LEU A1006       3.009 -13.056  -3.776  1.00 69.14      A    C  
ANISOU 1629  C   LEU A1006     6842  13876   5552   -641    326    147  A    C  
ATOM   1630  O   LEU A1006       3.652 -12.712  -2.784  1.00 68.86      A    O  
ANISOU 1630  O   LEU A1006     6777  13872   5516   -680    335     42  A    O  
ATOM   1631  CB  LEU A1006       0.648 -13.279  -2.825  1.00 65.34      A    C  
ANISOU 1631  CB  LEU A1006     6392  13333   5102   -460    296    178  A    C  
ATOM   1632  CG  LEU A1006      -0.601 -12.497  -2.418  1.00 70.83      A    C  
ANISOU 1632  CG  LEU A1006     7131  13926   5853   -394    301    170  A    C  
ATOM   1633  CD1 LEU A1006      -1.533 -13.356  -1.613  1.00 70.39      A    C  
ANISOU 1633  CD1 LEU A1006     7034  13947   5763   -305    281    164  A    C  
ATOM   1634  CD2 LEU A1006      -0.240 -11.269  -1.592  1.00 75.16      A    C  
ANISOU 1634  CD2 LEU A1006     7699  14408   6450   -438    326     62  A    C  
ATOM   1635  N   ARG A1007       3.548 -13.777  -4.781  1.00 65.52      A    N  
ANISOU 1635  N   ARG A1007     6354  13492   5049   -666    319    198  A    N  
ATOM   1636  CA  ARG A1007       4.964 -14.162  -4.826  1.00 65.24      A    C  
ANISOU 1636  CA  ARG A1007     6249  13574   4965   -740    323    134  A    C  
ATOM   1637  C   ARG A1007       5.773 -12.899  -5.178  1.00 70.26      A    C  
ANISOU 1637  C   ARG A1007     6915  14145   5637   -874    373    106  A    C  
ATOM   1638  O   ARG A1007       6.780 -12.632  -4.532  1.00 71.45      A    O  
ANISOU 1638  O   ARG A1007     7014  14358   5775   -947    387     -2  A    O  
ATOM   1639  CB  ARG A1007       5.218 -15.289  -5.842  1.00 63.98      A    C  
ANISOU 1639  CB  ARG A1007     6046  13511   4752   -720    302    186  A    C  
ATOM   1640  CG  ARG A1007       6.622 -15.858  -5.767  1.00 71.95      A    C  
ANISOU 1640  CG  ARG A1007     6967  14664   5706   -766    296    105  A    C  
ATOM   1641  CD  ARG A1007       6.762 -17.171  -6.504  1.00 82.43      A    C  
ANISOU 1641  CD  ARG A1007     8244  16088   6987   -712    265    133  A    C  
ATOM   1642  NE  ARG A1007       8.168 -17.579  -6.575  1.00 89.14      A    N  
ANISOU 1642  NE  ARG A1007     9006  17079   7785   -755    261     49  A    N  
ATOM   1643  CZ  ARG A1007       8.585 -18.812  -6.843  1.00101.88      A    C  
ANISOU 1643  CZ  ARG A1007    10556  18797   9358   -693    226     30  A    C  
ATOM   1644  NH1 ARG A1007       9.881 -19.085  -6.886  1.00 87.55      A    N1+
ANISOU 1644  NH1 ARG A1007     8652  17117   7495   -725    221    -57  A    N1+
ATOM   1645  NH2 ARG A1007       7.708 -19.787  -7.053  1.00 91.68      A    N  
ANISOU 1645  NH2 ARG A1007     9283  17476   8075   -597    197     88  A    N  
ATOM   1646  N   ILE A1008       5.300 -12.108  -6.170  1.00 65.66      A    N  
ANISOU 1646  N   ILE A1008     6416  13436   5097   -905    402    203  A    N  
ATOM   1647  CA  ILE A1008       5.880 -10.829  -6.589  1.00 65.89      A    C  
ANISOU 1647  CA  ILE A1008     6502  13360   5173  -1034    460    207  A    C  
ATOM   1648  C   ILE A1008       5.853  -9.781  -5.426  1.00 74.28      A    C  
ANISOU 1648  C   ILE A1008     7597  14314   6312  -1067    483    105  A    C  
ATOM   1649  O   ILE A1008       6.872  -9.134  -5.177  1.00 76.02      A    O  
ANISOU 1649  O   ILE A1008     7798  14535   6550  -1196    525     16  A    O  
ATOM   1650  CB  ILE A1008       5.163 -10.340  -7.878  1.00 68.14      A    C  
ANISOU 1650  CB  ILE A1008     6881  13534   5477  -1025    476    362  A    C  
ATOM   1651  CG1 ILE A1008       5.629 -11.176  -9.099  1.00 67.59      A    C  
ANISOU 1651  CG1 ILE A1008     6761  13599   5320  -1045    470    428  A    C  
ATOM   1652  CG2 ILE A1008       5.342  -8.826  -8.106  1.00 69.51      A    C  
ANISOU 1652  CG2 ILE A1008     7156  13527   5727  -1131    538    391  A    C  
ATOM   1653  CD1 ILE A1008       4.813 -11.112 -10.358  1.00 66.77      A    C  
ANISOU 1653  CD1 ILE A1008     6720  13453   5197   -996    465    579  A    C  
ATOM   1654  N   ASP A1009       4.715  -9.651  -4.703  1.00 72.02      A    N  
ANISOU 1654  N   ASP A1009     7348  13950   6067   -956    458    102  A    N  
ATOM   1655  CA  ASP A1009       4.534  -8.670  -3.618  1.00 73.67      A    C  
ANISOU 1655  CA  ASP A1009     7585  14056   6349   -969    477     -4  A    C  
ATOM   1656  C   ASP A1009       5.240  -9.035  -2.277  1.00 79.35      A    C  
ANISOU 1656  C   ASP A1009     8204  14919   7027   -986    463   -165  A    C  
ATOM   1657  O   ASP A1009       6.061  -8.244  -1.799  1.00 80.00      A    O  
ANISOU 1657  O   ASP A1009     8270  14986   7140  -1098    500   -281  A    O  
ATOM   1658  CB  ASP A1009       3.034  -8.363  -3.387  1.00 74.99      A    C  
ANISOU 1658  CB  ASP A1009     7819  14105   6570   -838    456     43  A    C  
ATOM   1659  CG  ASP A1009       2.367  -7.491  -4.449  1.00 78.20      A    C  
ANISOU 1659  CG  ASP A1009     8339  14331   7041   -823    474    175  A    C  
ATOM   1660  OD1 ASP A1009       3.089  -6.792  -5.190  1.00 77.93      A    O  
ANISOU 1660  OD1 ASP A1009     8358  14218   7033   -937    519    220  A    O  
ATOM   1661  OD2 ASP A1009       1.127  -7.488  -4.515  1.00 80.95      A    O1-
ANISOU 1661  OD2 ASP A1009     8724  14624   7409   -696    445    233  A    O1-
ATOM   1662  N   GLU A1010       4.911 -10.208  -1.675  1.00 75.20      A    N  
ANISOU 1662  N   GLU A1010     7613  14534   6428   -877    414   -172  A    N  
ATOM   1663  CA  GLU A1010       5.497 -10.694  -0.411  1.00 74.67      A    C  
ANISOU 1663  CA  GLU A1010     7451  14623   6297   -864    391   -300  A    C  
ATOM   1664  C   GLU A1010       6.917 -11.290  -0.599  1.00 78.07      A    C  
ANISOU 1664  C   GLU A1010     7794  15213   6657   -937    387   -349  A    C  
ATOM   1665  O   GLU A1010       7.821 -10.962   0.167  1.00 78.87      A    O  
ANISOU 1665  O   GLU A1010     7833  15392   6742  -1008    398   -485  A    O  
ATOM   1666  CB  GLU A1010       4.575 -11.730   0.267  1.00 74.95      A    C  
ANISOU 1666  CB  GLU A1010     7463  14740   6277   -723    346   -265  A    C  
ATOM   1667  CG  GLU A1010       3.170 -11.240   0.597  1.00 85.71      A    C  
ANISOU 1667  CG  GLU A1010     8885  15987   7693   -644    348   -240  A    C  
ATOM   1668  CD  GLU A1010       2.997 -10.376   1.834  1.00106.06      A    C  
ANISOU 1668  CD  GLU A1010    11455  18543  10301   -645    362   -375  A    C  
ATOM   1669  OE1 GLU A1010       3.791 -10.520   2.793  1.00100.64      A    O  
ANISOU 1669  OE1 GLU A1010    10695  17984   9559   -678    357   -492  A    O  
ATOM   1670  OE2 GLU A1010       2.042  -9.568   1.852  1.00102.35      A    O1-
ANISOU 1670  OE2 GLU A1010    11046  17940   9904   -604    375   -370  A    O1-
ATOM   1671  N   GLY A1011       7.083 -12.158  -1.599  1.00 73.01      A    N  
ANISOU 1671  N   GLY A1011     7140  14629   5973   -915    369   -252  A    N  
ATOM   1672  CA  GLY A1011       8.344 -12.826  -1.900  1.00 72.54      A    C  
ANISOU 1672  CA  GLY A1011     6991  14726   5845   -962    359   -294  A    C  
ATOM   1673  C   GLY A1011       8.414 -14.203  -1.280  1.00 76.17      A    C  
ANISOU 1673  C   GLY A1011     7382  15339   6222   -842    301   -300  A    C  
ATOM   1674  O   GLY A1011       8.504 -14.318  -0.047  1.00 77.84      A    O  
ANISOU 1674  O   GLY A1011     7551  15628   6396   -796    279   -381  A    O  
ATOM   1675  N   LEU A1012       8.371 -15.262  -2.123  1.00 69.84      A    N  
ANISOU 1675  N   LEU A1012     6568  14580   5388   -789    277   -215  A    N  
ATOM   1676  CA  LEU A1012       8.439 -16.649  -1.651  1.00 68.81      A    C  
ANISOU 1676  CA  LEU A1012     6386  14566   5191   -672    224   -206  A    C  
ATOM   1677  C   LEU A1012       9.832 -17.027  -1.162  1.00 73.73      A    C  
ANISOU 1677  C   LEU A1012     6905  15365   5744   -682    200   -315  A    C  
ATOM   1678  O   LEU A1012      10.772 -17.076  -1.962  1.00 75.74      A    O  
ANISOU 1678  O   LEU A1012     7107  15688   5982   -746    210   -346  A    O  
ATOM   1679  CB  LEU A1012       7.934 -17.661  -2.703  1.00 67.93      A    C  
ANISOU 1679  CB  LEU A1012     6297  14431   5082   -613    207    -98  A    C  
ATOM   1680  CG  LEU A1012       8.095 -19.170  -2.379  1.00 72.21      A    C  
ANISOU 1680  CG  LEU A1012     6798  15066   5572   -497    158    -84  A    C  
ATOM   1681  CD1 LEU A1012       7.298 -19.577  -1.136  1.00 72.81      A    C  
ANISOU 1681  CD1 LEU A1012     6902  15127   5635   -405    138    -60  A    C  
ATOM   1682  CD2 LEU A1012       7.664 -20.027  -3.549  1.00 72.97      A    C  
ANISOU 1682  CD2 LEU A1012     6910  15130   5685   -465    150     -4  A    C  
ATOM   1683  N   ARG A1013       9.957 -17.303   0.152  1.00 67.76      A    N  
ANISOU 1683  N   ARG A1013     6110  14700   4936   -613    169   -375  A    N  
ATOM   1684  CA  ARG A1013      11.206 -17.721   0.791  1.00 66.96      A    C  
ANISOU 1684  CA  ARG A1013     5901  14789   4752   -590    133   -482  A    C  
ATOM   1685  C   ARG A1013      10.907 -19.009   1.583  1.00 68.93      A    C  
ANISOU 1685  C   ARG A1013     6147  15108   4937   -428     76   -426  A    C  
ATOM   1686  O   ARG A1013       9.884 -19.076   2.264  1.00 67.89      A    O  
ANISOU 1686  O   ARG A1013     6075  14910   4811   -373     76   -369  A    O  
ATOM   1687  CB  ARG A1013      11.734 -16.595   1.698  1.00 67.51      A    C  
ANISOU 1687  CB  ARG A1013     5925  14915   4812   -675    154   -622  A    C  
ATOM   1688  CG  ARG A1013      13.255 -16.459   1.768  1.00 74.75      A    C  
ANISOU 1688  CG  ARG A1013     6717  16010   5673   -742    148   -765  A    C  
ATOM   1689  CD  ARG A1013      13.839 -15.632   0.632  1.00 74.80      A    C  
ANISOU 1689  CD  ARG A1013     6718  15965   5737   -907    208   -795  A    C  
ATOM   1690  NE  ARG A1013      14.459 -16.484  -0.384  1.00 76.86      A    N  
ANISOU 1690  NE  ARG A1013     6936  16297   5969   -886    192   -754  A    N  
ATOM   1691  CZ  ARG A1013      14.839 -16.070  -1.588  1.00 86.85      A    C  
ANISOU 1691  CZ  ARG A1013     8198  17535   7266  -1010    241   -747  A    C  
ATOM   1692  NH1 ARG A1013      15.370 -16.924  -2.451  1.00 70.88      A    N1+
ANISOU 1692  NH1 ARG A1013     6127  15599   5207   -976    222   -721  A    N1+
ATOM   1693  NH2 ARG A1013      14.686 -14.797  -1.941  1.00 71.45      A    N  
ANISOU 1693  NH2 ARG A1013     6297  15469   5383  -1168    311   -764  A    N  
ATOM   1694  N   LEU A1014      11.758 -20.049   1.441  1.00 64.45      A    N  
ANISOU 1694  N   LEU A1014     5514  14662   4312   -352     31   -435  A    N  
ATOM   1695  CA  LEU A1014      11.552 -21.361   2.086  1.00 62.91      A    C  
ANISOU 1695  CA  LEU A1014     5330  14512   4063   -193    -22   -365  A    C  
ATOM   1696  C   LEU A1014      12.309 -21.538   3.439  1.00 66.13      A    C  
ANISOU 1696  C   LEU A1014     5663  15101   4364   -114    -68   -442  A    C  
ATOM   1697  O   LEU A1014      12.204 -22.602   4.054  1.00 66.38      A    O  
ANISOU 1697  O   LEU A1014     5706  15176   4339     25   -113   -374  A    O  
ATOM   1698  CB  LEU A1014      11.866 -22.521   1.100  1.00 62.15      A    C  
ANISOU 1698  CB  LEU A1014     5225  14412   3978   -127    -48   -313  A    C  
ATOM   1699  CG  LEU A1014      11.164 -22.495  -0.287  1.00 65.44      A    C  
ANISOU 1699  CG  LEU A1014     5703  14680   4482   -189    -10   -239  A    C  
ATOM   1700  CD1 LEU A1014      11.788 -23.498  -1.233  1.00 65.68      A    C  
ANISOU 1700  CD1 LEU A1014     5693  14752   4512   -138    -36   -240  A    C  
ATOM   1701  CD2 LEU A1014       9.665 -22.773  -0.192  1.00 65.69      A    C  
ANISOU 1701  CD2 LEU A1014     5838  14559   4561   -153      6   -120  A    C  
ATOM   1702  N   LYS A1015      13.055 -20.498   3.892  1.00 61.53      A    N  
ANISOU 1702  N   LYS A1015     5004  14623   3752   -203    -55   -583  A    N  
ATOM   1703  CA  LYS A1015      13.773 -20.431   5.186  1.00 61.13      A    C  
ANISOU 1703  CA  LYS A1015     4865  14768   3592   -148    -96   -685  A    C  
ATOM   1704  C   LYS A1015      13.239 -19.212   5.961  1.00 62.50      A    C  
ANISOU 1704  C   LYS A1015     5055  14910   3781   -237    -55   -756  A    C  
ATOM   1705  O   LYS A1015      12.914 -18.199   5.338  1.00 61.87      A    O  
ANISOU 1705  O   LYS A1015     5016  14693   3798   -371      3   -780  A    O  
ATOM   1706  CB  LYS A1015      15.282 -20.219   4.980  1.00 64.65      A    C  
ANISOU 1706  CB  LYS A1015     5173  15402   3989   -190   -116   -837  A    C  
ATOM   1707  CG  LYS A1015      16.054 -21.397   4.397  1.00 76.31      A    C  
ANISOU 1707  CG  LYS A1015     6600  16963   5430    -80   -168   -810  A    C  
ATOM   1708  CD  LYS A1015      17.542 -21.055   4.187  1.00 76.36      A    C  
ANISOU 1708  CD  LYS A1015     6450  17178   5383   -133   -184   -983  A    C  
ATOM   1709  CE  LYS A1015      17.858 -20.540   2.795  1.00 86.12      A    C  
ANISOU 1709  CE  LYS A1015     7670  18353   6699   -293   -125  -1023  A    C  
ATOM   1710  NZ  LYS A1015      17.825 -21.613   1.755  1.00 87.81      A    N1+
ANISOU 1710  NZ  LYS A1015     7911  18510   6945   -220   -141   -931  A    N1+
ATOM   1711  N   ILE A1016      13.186 -19.285   7.299  1.00 58.29      A    N  
ANISOU 1711  N   ILE A1016     4490  14507   3152   -160    -86   -793  A    N  
ATOM   1712  CA  ILE A1016      12.731 -18.190   8.170  1.00 58.83      A    C  
ANISOU 1712  CA  ILE A1016     4558  14575   3221   -229    -53   -885  A    C  
ATOM   1713  C   ILE A1016      13.371 -16.837   7.753  1.00 63.65      A    C  
ANISOU 1713  C   ILE A1016     5114  15168   3901   -407     -5  -1050  A    C  
ATOM   1714  O   ILE A1016      14.568 -16.793   7.486  1.00 64.85      A    O  
ANISOU 1714  O   ILE A1016     5167  15451   4024   -451    -19  -1154  A    O  
ATOM   1715  CB  ILE A1016      13.008 -18.564   9.677  1.00 63.67      A    C  
ANISOU 1715  CB  ILE A1016     5102  15409   3680   -112   -106   -931  A    C  
ATOM   1716  CG1 ILE A1016      12.119 -19.755  10.155  1.00 63.77      A    C  
ANISOU 1716  CG1 ILE A1016     5197  15400   3635     46   -135   -742  A    C  
ATOM   1717  CG2 ILE A1016      12.895 -17.350  10.652  1.00 65.27      A    C  
ANISOU 1717  CG2 ILE A1016     5266  15668   3866   -189    -77  -1082  A    C  
ATOM   1718  CD1 ILE A1016      12.489 -20.382  11.594  1.00 67.49      A    C  
ANISOU 1718  CD1 ILE A1016     5606  16109   3926    190   -196   -747  A    C  
ATOM   1719  N   TYR A1017      12.572 -15.762   7.668  1.00 60.67      A    N  
ANISOU 1719  N   TYR A1017     4805  14625   3623   -508     54  -1073  A    N  
ATOM   1720  CA  TYR A1017      13.026 -14.403   7.352  1.00 62.21      A    C  
ANISOU 1720  CA  TYR A1017     4976  14758   3902   -683    110  -1217  A    C  
ATOM   1721  C   TYR A1017      12.375 -13.333   8.270  1.00 69.38      A    C  
ANISOU 1721  C   TYR A1017     5906  15610   4844   -728    143  -1317  A    C  
ATOM   1722  O   TYR A1017      11.522 -13.670   9.092  1.00 68.85      A    O  
ANISOU 1722  O   TYR A1017     5873  15556   4732   -623    124  -1263  A    O  
ATOM   1723  CB  TYR A1017      12.830 -14.083   5.866  1.00 63.36      A    C  
ANISOU 1723  CB  TYR A1017     5203  14701   4170   -781    160  -1127  A    C  
ATOM   1724  CG  TYR A1017      11.393 -13.933   5.391  1.00 66.59      A    C  
ANISOU 1724  CG  TYR A1017     5751  14879   4671   -757    188   -980  A    C  
ATOM   1725  CD1 TYR A1017      10.689 -15.020   4.874  1.00 67.61      A    C  
ANISOU 1725  CD1 TYR A1017     5940  14959   4790   -646    161   -810  A    C  
ATOM   1726  CD2 TYR A1017      10.786 -12.680   5.329  1.00 68.25      A    C  
ANISOU 1726  CD2 TYR A1017     6030  14915   4988   -851    244  -1018  A    C  
ATOM   1727  CE1 TYR A1017       9.388 -14.877   4.383  1.00 67.50      A    C  
ANISOU 1727  CE1 TYR A1017     6036  14754   4856   -627    187   -689  A    C  
ATOM   1728  CE2 TYR A1017       9.493 -12.522   4.819  1.00 68.25      A    C  
ANISOU 1728  CE2 TYR A1017     6147  14716   5069   -818    264   -889  A    C  
ATOM   1729  CZ  TYR A1017       8.798 -13.623   4.347  1.00 73.64      A    C  
ANISOU 1729  CZ  TYR A1017     6874  15379   5728   -708    235   -728  A    C  
ATOM   1730  OH  TYR A1017       7.529 -13.459   3.841  1.00 73.54      A    O  
ANISOU 1730  OH  TYR A1017     6959  15193   5788   -677    254   -615  A    O  
ATOM   1731  N   LYS A1018      12.792 -12.056   8.145  1.00 67.55      A    N  
ANISOU 1731  N   LYS A1018     5654  15318   4695   -888    196  -1468  A    N  
ATOM   1732  CA  LYS A1018      12.221 -10.935   8.898  1.00 67.71      A    C  
ANISOU 1732  CA  LYS A1018     5698  15258   4773   -941    233  -1585  A    C  
ATOM   1733  C   LYS A1018      11.512  -9.959   7.936  1.00 73.53      A    C  
ANISOU 1733  C   LYS A1018     6562  15696   5681  -1044    302  -1530  A    C  
ATOM   1734  O   LYS A1018      12.029  -9.675   6.844  1.00 72.72      A    O  
ANISOU 1734  O   LYS A1018     6484  15498   5648  -1153    337  -1499  A    O  
ATOM   1735  CB  LYS A1018      13.300 -10.193   9.690  1.00 71.07      A    C  
ANISOU 1735  CB  LYS A1018     5993  15853   5158  -1040    240  -1832  A    C  
ATOM   1736  CG  LYS A1018      13.725 -10.864  11.000  1.00 77.20      A    C  
ANISOU 1736  CG  LYS A1018     6645  16931   5755   -919    171  -1915  A    C  
ATOM   1737  CD  LYS A1018      14.106  -9.818  12.063  1.00 73.19      A    C  
ANISOU 1737  CD  LYS A1018     6038  16542   5231  -1007    188  -2174  A    C  
ATOM   1738  CE  LYS A1018      15.078 -10.322  13.100  1.00 69.80      A    C  
ANISOU 1738  CE  LYS A1018     5447  16461   4615   -927    120  -2296  A    C  
ATOM   1739  NZ  LYS A1018      15.546  -9.226  14.001  1.00 68.25      A    N1+
ANISOU 1739  NZ  LYS A1018     5139  16387   4407  -1033    141  -2575  A    N1+
ATOM   1740  N   ASP A1019      10.316  -9.462   8.335  1.00 71.55      A    N  
ANISOU 1740  N   ASP A1019     6390  15305   5489  -1001    319  -1513  A    N  
ATOM   1741  CA  ASP A1019       9.541  -8.500   7.538  1.00 71.28      A    C  
ANISOU 1741  CA  ASP A1019     6481  14986   5614  -1068    376  -1460  A    C  
ATOM   1742  C   ASP A1019       9.981  -7.043   7.857  1.00 77.14      A    C  
ANISOU 1742  C   ASP A1019     7215  15637   6458  -1218    432  -1659  A    C  
ATOM   1743  O   ASP A1019      10.882  -6.866   8.676  1.00 77.68      A    O  
ANISOU 1743  O   ASP A1019     7167  15885   6464  -1273    426  -1844  A    O  
ATOM   1744  CB  ASP A1019       8.015  -8.741   7.664  1.00 71.87      A    C  
ANISOU 1744  CB  ASP A1019     6645  14953   5710   -937    364  -1335  A    C  
ATOM   1745  CG  ASP A1019       7.352  -8.369   8.989  1.00 85.27      A    C  
ANISOU 1745  CG  ASP A1019     8311  16714   7375   -873    358  -1455  A    C  
ATOM   1746  OD1 ASP A1019       8.083  -8.080   9.961  1.00 89.85      A    O  
ANISOU 1746  OD1 ASP A1019     8792  17453   7895   -913    352  -1638  A    O  
ATOM   1747  OD2 ASP A1019       6.093  -8.372   9.051  1.00 84.29      A    O1-
ANISOU 1747  OD2 ASP A1019     8252  16496   7278   -782    358  -1374  A    O1-
ATOM   1748  N   THR A1020       9.364  -6.020   7.205  1.00 74.31      A    N  
ANISOU 1748  N   THR A1020     6979  15002   6255  -1280    487  -1624  A    N  
ATOM   1749  CA  THR A1020       9.673  -4.579   7.331  1.00 75.80      A    C  
ANISOU 1749  CA  THR A1020     7193  15033   6575  -1427    551  -1789  A    C  
ATOM   1750  C   THR A1020       9.598  -4.078   8.791  1.00 80.05      A    C  
ANISOU 1750  C   THR A1020     7651  15677   7088  -1410    544  -2014  A    C  
ATOM   1751  O   THR A1020      10.342  -3.162   9.160  1.00 80.23      A    O  
ANISOU 1751  O   THR A1020     7627  15689   7168  -1550    586  -2216  A    O  
ATOM   1752  CB  THR A1020       8.786  -3.766   6.350  1.00 86.59      A    C  
ANISOU 1752  CB  THR A1020     8727  16071   8103  -1443    598  -1660  A    C  
ATOM   1754  CG2 THR A1020       9.026  -2.259   6.417  1.00 86.98      A    C  
ANISOU 1754  CG2 THR A1020     8829  15910   8309  -1605    673  -1802  A    C  
ATOM   1753  OG1 THR A1020       9.077  -4.199   5.019  1.00 89.49      A    O  
ANISOU 1753  OG1 THR A1020     9148  16390   8465  -1459    600  -1461  A    O  
ATOM   1755  N   GLU A1021       8.716  -4.695   9.608  1.00 76.38      A    N  
ANISOU 1755  N   GLU A1021     7164  15327   6532  -1247    495  -1984  A    N  
ATOM   1756  CA  GLU A1021       8.509  -4.373  11.023  1.00 77.06      A    C  
ANISOU 1756  CA  GLU A1021     7167  15551   6563  -1204    481  -2180  A    C  
ATOM   1757  C   GLU A1021       9.420  -5.211  11.943  1.00 80.10      A    C  
ANISOU 1757  C   GLU A1021     7392  16283   6759  -1178    430  -2276  A    C  
ATOM   1758  O   GLU A1021       9.557  -4.894  13.130  1.00 81.01      A    O  
ANISOU 1758  O   GLU A1021     7411  16556   6812  -1177    422  -2478  A    O  
ATOM   1759  CB  GLU A1021       7.024  -4.534  11.401  1.00 77.91      A    C  
ANISOU 1759  CB  GLU A1021     7331  15608   6662  -1047    462  -2094  A    C  
ATOM   1760  CG  GLU A1021       6.078  -3.632  10.619  1.00 91.17      A    C  
ANISOU 1760  CG  GLU A1021     9156  16965   8521  -1047    504  -2022  A    C  
ATOM   1761  CD  GLU A1021       5.586  -2.386  11.332  1.00121.40      A    C  
ANISOU 1761  CD  GLU A1021    13001  20659  12466  -1074    541  -2224  A    C  
ATOM   1762  OE1 GLU A1021       6.421  -1.640  11.893  1.00123.12      A    O  
ANISOU 1762  OE1 GLU A1021    13158  20905  12718  -1199    570  -2437  A    O  
ATOM   1763  OE2 GLU A1021       4.357  -2.145  11.313  1.00119.76      A    O1-
ANISOU 1763  OE2 GLU A1021    12864  20319  12321   -971    543  -2178  A    O1-
ATOM   1764  N   GLY A1022      10.010  -6.272  11.389  1.00 75.10      A    N  
ANISOU 1764  N   GLY A1022     6733  15770   6033  -1145    394  -2135  A    N  
ATOM   1765  CA  GLY A1022      10.951  -7.145  12.087  1.00 75.14      A    C  
ANISOU 1765  CA  GLY A1022     6596  16095   5861  -1103    338  -2197  A    C  
ATOM   1766  C   GLY A1022      10.451  -8.471  12.636  1.00 76.96      A    C  
ANISOU 1766  C   GLY A1022     6807  16504   5931   -919    273  -2052  A    C  
ATOM   1767  O   GLY A1022      11.184  -9.136  13.370  1.00 77.77      A    O  
ANISOU 1767  O   GLY A1022     6796  16876   5879   -863    222  -2102  A    O  
ATOM   1768  N   TYR A1023       9.234  -8.884  12.296  1.00 70.51      A    N  
ANISOU 1768  N   TYR A1023     6098  15547   5147   -823    273  -1872  A    N  
ATOM   1769  CA  TYR A1023       8.692 -10.153  12.782  1.00 69.25      A    C  
ANISOU 1769  CA  TYR A1023     5934  15529   4847   -664    224  -1722  A    C  
ATOM   1770  C   TYR A1023       9.215 -11.341  11.986  1.00 71.08      A    C  
ANISOU 1770  C   TYR A1023     6175  15799   5032   -619    188  -1551  A    C  
ATOM   1771  O   TYR A1023       9.305 -11.256  10.762  1.00 69.11      A    O  
ANISOU 1771  O   TYR A1023     5991  15377   4890   -682    211  -1466  A    O  
ATOM   1772  CB  TYR A1023       7.153 -10.159  12.721  1.00 69.62      A    C  
ANISOU 1772  CB  TYR A1023     6083  15419   4950   -590    244  -1603  A    C  
ATOM   1773  CG  TYR A1023       6.492  -9.060  13.514  1.00 72.42      A    C  
ANISOU 1773  CG  TYR A1023     6431  15732   5353   -608    277  -1766  A    C  
ATOM   1774  CD1 TYR A1023       6.439  -9.112  14.907  1.00 75.22      A    C  
ANISOU 1774  CD1 TYR A1023     6694  16315   5571   -549    258  -1887  A    C  
ATOM   1775  CD2 TYR A1023       5.896  -7.977  12.875  1.00 73.44      A    C  
ANISOU 1775  CD2 TYR A1023     6649  15597   5660   -673    326  -1796  A    C  
ATOM   1776  CE1 TYR A1023       5.813  -8.108  15.647  1.00 76.49      A    C  
ANISOU 1776  CE1 TYR A1023     6841  16447   5775   -561    288  -2054  A    C  
ATOM   1777  CE2 TYR A1023       5.281  -6.959  13.605  1.00 75.94      A    C  
ANISOU 1777  CE2 TYR A1023     6960  15863   6032   -677    354  -1957  A    C  
ATOM   1778  CZ  TYR A1023       5.238  -7.030  14.992  1.00 83.58      A    C  
ANISOU 1778  CZ  TYR A1023     7826  17066   6865   -623    336  -2094  A    C  
ATOM   1779  OH  TYR A1023       4.610  -6.045  15.717  1.00 83.34      A    O  
ANISOU 1779  OH  TYR A1023     7782  16997   6886   -622    364  -2268  A    O  
ATOM   1780  N   TYR A1024       9.491 -12.468  12.686  1.00 67.81      A    N  
ANISOU 1780  N   TYR A1024     5702  15608   4456   -499    131  -1493  A    N  
ATOM   1781  CA  TYR A1024       9.926 -13.745  12.115  1.00 66.75      A    C  
ANISOU 1781  CA  TYR A1024     5574  15523   4264   -423     89  -1334  A    C  
ATOM   1782  C   TYR A1024       8.771 -14.326  11.284  1.00 69.80      A    C  
ANISOU 1782  C   TYR A1024     6087  15706   4728   -376    106  -1124  A    C  
ATOM   1783  O   TYR A1024       7.666 -14.497  11.796  1.00 70.20      A    O  
ANISOU 1783  O   TYR A1024     6185  15726   4763   -313    117  -1059  A    O  
ATOM   1784  CB  TYR A1024      10.392 -14.716  13.221  1.00 68.69      A    C  
ANISOU 1784  CB  TYR A1024     5738  16041   4319   -291     25  -1322  A    C  
ATOM   1785  CG  TYR A1024      11.806 -14.474  13.715  1.00 72.71      A    C  
ANISOU 1785  CG  TYR A1024     6105  16786   4735   -319    -10  -1504  A    C  
ATOM   1786  CD1 TYR A1024      12.888 -14.487  12.833  1.00 74.77      A    C  
ANISOU 1786  CD1 TYR A1024     6318  17056   5034   -385    -18  -1544  A    C  
ATOM   1787  CD2 TYR A1024      12.076 -14.313  15.073  1.00 74.97      A    C  
ANISOU 1787  CD2 TYR A1024     6293  17315   4879   -271    -39  -1636  A    C  
ATOM   1788  CE1 TYR A1024      14.194 -14.293  13.285  1.00 75.65      A    C  
ANISOU 1788  CE1 TYR A1024     6283  17407   5054   -410    -52  -1722  A    C  
ATOM   1789  CE2 TYR A1024      13.382 -14.131  15.536  1.00 77.02      A    C  
ANISOU 1789  CE2 TYR A1024     6406  17818   5041   -289    -77  -1813  A    C  
ATOM   1790  CZ  TYR A1024      14.437 -14.124  14.636  1.00 83.23      A    C  
ANISOU 1790  CZ  TYR A1024     7143  18606   5876   -359    -84  -1857  A    C  
ATOM   1791  OH  TYR A1024      15.725 -13.933  15.069  1.00 86.47      A    O  
ANISOU 1791  OH  TYR A1024     7394  19271   6189   -381   -121  -2045  A    O  
ATOM   1792  N   THR A1025       9.025 -14.562   9.990  1.00 65.37      A    N  
ANISOU 1792  N   THR A1025     5570  15018   4250   -416    113  -1033  A    N  
ATOM   1793  CA  THR A1025       8.063 -14.971   8.963  1.00 64.13      A    C  
ANISOU 1793  CA  THR A1025     5521  14664   4181   -396    132   -860  A    C  
ATOM   1794  C   THR A1025       8.659 -16.088   8.053  1.00 69.55      A    C  
ANISOU 1794  C   THR A1025     6208  15368   4849   -357    101   -746  A    C  
ATOM   1795  O   THR A1025       9.880 -16.237   7.978  1.00 69.98      A    O  
ANISOU 1795  O   THR A1025     6183  15552   4855   -374     75   -819  A    O  
ATOM   1796  CB  THR A1025       7.743 -13.688   8.127  1.00 70.27      A    C  
ANISOU 1796  CB  THR A1025     6358  15230   5110   -517    188   -903  A    C  
ATOM   1798  CG2 THR A1025       6.636 -13.874   7.116  1.00 67.58      A    C  
ANISOU 1798  CG2 THR A1025     6123  14694   4859   -495    208   -746  A    C  
ATOM   1797  OG1 THR A1025       7.414 -12.601   8.992  1.00 68.66      A    O  
ANISOU 1797  OG1 THR A1025     6139  15019   4930   -558    214  -1047  A    O  
ATOM   1799  N   ILE A1026       7.792 -16.840   7.338  1.00 65.57      A    N  
ANISOU 1799  N   ILE A1026     5786  14739   4389   -307    104   -584  A    N  
ATOM   1800  CA  ILE A1026       8.179 -17.898   6.389  1.00 64.33      A    C  
ANISOU 1800  CA  ILE A1026     5639  14570   4234   -269     80   -479  A    C  
ATOM   1801  C   ILE A1026       7.155 -17.995   5.222  1.00 66.69      A    C  
ANISOU 1801  C   ILE A1026     6030  14673   4637   -288    110   -358  A    C  
ATOM   1802  O   ILE A1026       6.016 -17.546   5.380  1.00 65.39      A    O  
ANISOU 1802  O   ILE A1026     5921  14408   4517   -289    138   -327  A    O  
ATOM   1803  CB  ILE A1026       8.399 -19.256   7.127  1.00 67.13      A    C  
ANISOU 1803  CB  ILE A1026     5971  15061   4474   -134     28   -409  A    C  
ATOM   1804  CG1 ILE A1026       9.316 -20.198   6.292  1.00 66.58      A    C  
ANISOU 1804  CG1 ILE A1026     5875  15024   4397    -95     -7   -368  A    C  
ATOM   1805  CG2 ILE A1026       7.048 -19.910   7.548  1.00 66.84      A    C  
ANISOU 1805  CG2 ILE A1026     6011  14956   4429    -60     40   -279  A    C  
ATOM   1806  CD1 ILE A1026       9.835 -21.448   6.962  1.00 70.98      A    C  
ANISOU 1806  CD1 ILE A1026     6397  15729   4844     41    -66   -329  A    C  
ATOM   1807  N   GLY A1027       7.579 -18.575   4.092  1.00 63.14      A    N  
ANISOU 1807  N   GLY A1027     5584  14191   4217   -298    101   -303  A    N  
ATOM   1808  CA  GLY A1027       6.762 -18.793   2.898  1.00 62.78      A    C  
ANISOU 1808  CA  GLY A1027     5607  13995   4251   -311    122   -197  A    C  
ATOM   1809  C   GLY A1027       6.324 -17.523   2.194  1.00 68.16      A    C  
ANISOU 1809  C   GLY A1027     6332  14541   5022   -409    166   -214  A    C  
ATOM   1810  O   GLY A1027       7.163 -16.694   1.826  1.00 69.45      A    O  
ANISOU 1810  O   GLY A1027     6470  14709   5208   -504    185   -291  A    O  
ATOM   1811  N   ILE A1028       5.002 -17.382   1.982  1.00 64.17      A    N  
ANISOU 1811  N   ILE A1028     5895  13916   4569   -385    185   -139  A    N  
ATOM   1812  CA  ILE A1028       4.386 -16.191   1.387  1.00 64.54      A    C  
ANISOU 1812  CA  ILE A1028     5997  13821   4703   -447    222   -138  A    C  
ATOM   1813  C   ILE A1028       3.706 -15.442   2.538  1.00 69.71      A    C  
ANISOU 1813  C   ILE A1028     6663  14457   5366   -428    235   -202  A    C  
ATOM   1814  O   ILE A1028       2.523 -15.659   2.828  1.00 68.39      A    O  
ANISOU 1814  O   ILE A1028     6526  14254   5206   -364    238   -152  A    O  
ATOM   1815  CB  ILE A1028       3.448 -16.451   0.146  1.00 66.97      A    C  
ANISOU 1815  CB  ILE A1028     6362  14020   5063   -430    228    -20  A    C  
ATOM   1816  CG1 ILE A1028       4.165 -17.281  -0.961  1.00 66.45      A    C  
ANISOU 1816  CG1 ILE A1028     6272  13996   4979   -447    214     25  A    C  
ATOM   1817  CG2 ILE A1028       2.901 -15.114  -0.422  1.00 68.48      A    C  
ANISOU 1817  CG2 ILE A1028     6616  14067   5337   -478    261    -14  A    C  
ATOM   1818  CD1 ILE A1028       3.436 -17.421  -2.327  1.00 67.25      A    C  
ANISOU 1818  CD1 ILE A1028     6415  14018   5120   -439    219    123  A    C  
ATOM   1819  N   GLY A1029       4.521 -14.653   3.241  1.00 68.55      A    N  
ANISOU 1819  N   GLY A1029     6478  14360   5208   -485    244   -328  A    N  
ATOM   1820  CA  GLY A1029       4.133 -13.822   4.380  1.00 69.24      A    C  
ANISOU 1820  CA  GLY A1029     6558  14450   5299   -480    258   -430  A    C  
ATOM   1821  C   GLY A1029       3.466 -14.477   5.576  1.00 72.57      A    C  
ANISOU 1821  C   GLY A1029     6954  14978   5640   -385    241   -426  A    C  
ATOM   1822  O   GLY A1029       2.716 -13.798   6.275  1.00 72.68      A    O  
ANISOU 1822  O   GLY A1029     6979  14963   5673   -368    258   -482  A    O  
ATOM   1823  N   HIS A1030       3.736 -15.774   5.853  1.00 69.14      A    N  
ANISOU 1823  N   HIS A1030     6488  14668   5114   -322    208   -362  A    N  
ATOM   1824  CA  HIS A1030       3.131 -16.474   7.000  1.00 69.35      A    C  
ANISOU 1824  CA  HIS A1030     6498  14801   5051   -237    198   -336  A    C  
ATOM   1825  C   HIS A1030       3.848 -16.134   8.303  1.00 72.45      A    C  
ANISOU 1825  C   HIS A1030     6819  15360   5350   -232    184   -463  A    C  
ATOM   1826  O   HIS A1030       5.007 -16.510   8.473  1.00 72.98      A    O  
ANISOU 1826  O   HIS A1030     6831  15549   5348   -227    152   -494  A    O  
ATOM   1827  CB  HIS A1030       3.057 -18.002   6.776  1.00 70.20      A    C  
ANISOU 1827  CB  HIS A1030     6620  14944   5109   -168    174   -198  A    C  
ATOM   1828  CG  HIS A1030       2.350 -18.738   7.877  1.00 74.77      A    C  
ANISOU 1828  CG  HIS A1030     7197  15615   5598    -93    174   -148  A    C  
ATOM   1830  CD2 HIS A1030       1.023 -18.916   8.091  1.00 77.26      A    C  
ANISOU 1830  CD2 HIS A1030     7544  15889   5921    -68    203    -90  A    C  
ATOM   1829  ND1 HIS A1030       3.052 -19.359   8.901  1.00 77.85      A    N  
ANISOU 1829  ND1 HIS A1030     7544  16167   5867    -37    144   -153  A    N  
ATOM   1831  CE1 HIS A1030       2.137 -19.884   9.705  1.00 77.93      A    C  
ANISOU 1831  CE1 HIS A1030     7572  16223   5815     14    160    -87  A    C  
ATOM   1832  NE2 HIS A1030       0.900 -19.645   9.258  1.00 77.92      A    N  
ANISOU 1832  NE2 HIS A1030     7611  16106   5889     -9    199    -54  A    N  
ATOM   1833  N   LEU A1031       3.159 -15.432   9.223  1.00 68.39      A    N  
ANISOU 1833  N   LEU A1031     6293  14866   4825   -227    205   -547  A    N  
ATOM   1834  CA  LEU A1031       3.713 -15.027  10.518  1.00 69.29      A    C  
ANISOU 1834  CA  LEU A1031     6331  15152   4844   -222    195   -686  A    C  
ATOM   1835  C   LEU A1031       3.862 -16.226  11.466  1.00 73.66      A    C  
ANISOU 1835  C   LEU A1031     6849  15896   5241   -128    163   -615  A    C  
ATOM   1836  O   LEU A1031       2.887 -16.953  11.689  1.00 73.55      A    O  
ANISOU 1836  O   LEU A1031     6876  15873   5198    -69    174   -496  A    O  
ATOM   1837  CB  LEU A1031       2.849 -13.922  11.163  1.00 69.91      A    C  
ANISOU 1837  CB  LEU A1031     6408  15193   4961   -237    229   -801  A    C  
ATOM   1838  CG  LEU A1031       3.576 -12.964  12.117  1.00 75.93      A    C  
ANISOU 1838  CG  LEU A1031     7090  16084   5677   -275    228  -1005  A    C  
ATOM   1839  CD1 LEU A1031       3.036 -11.558  11.995  1.00 76.60      A    C  
ANISOU 1839  CD1 LEU A1031     7199  16011   5893   -342    267  -1138  A    C  
ATOM   1840  CD2 LEU A1031       3.469 -13.426  13.547  1.00 79.42      A    C  
ANISOU 1840  CD2 LEU A1031     7472  16744   5962   -198    215  -1032  A    C  
ATOM   1841  N   LEU A1032       5.078 -16.410  12.040  1.00 69.73      A    N  
ANISOU 1841  N   LEU A1032     6276  15574   4643   -114    125   -688  A    N  
ATOM   1842  CA  LEU A1032       5.375 -17.502  12.974  1.00 69.74      A    C  
ANISOU 1842  CA  LEU A1032     6245  15767   4484    -11     87   -617  A    C  
ATOM   1843  C   LEU A1032       5.156 -17.128  14.450  1.00 76.53      A    C  
ANISOU 1843  C   LEU A1032     7045  16814   5219     21     89   -715  A    C  
ATOM   1844  O   LEU A1032       4.524 -17.889  15.180  1.00 76.42      A    O  
ANISOU 1844  O   LEU A1032     7050  16884   5103     98     91   -609  A    O  
ATOM   1845  CB  LEU A1032       6.795 -18.047  12.769  1.00 69.63      A    C  
ANISOU 1845  CB  LEU A1032     6176  15865   4414     14     34   -631  A    C  
ATOM   1846  CG  LEU A1032       7.106 -18.736  11.444  1.00 72.53      A    C  
ANISOU 1846  CG  LEU A1032     6591  16103   4866     10     23   -522  A    C  
ATOM   1847  CD1 LEU A1032       8.598 -18.807  11.223  1.00 72.72      A    C  
ANISOU 1847  CD1 LEU A1032     6531  16246   4853      4    -20   -610  A    C  
ATOM   1848  CD2 LEU A1032       6.485 -20.129  11.370  1.00 73.66      A    C  
ANISOU 1848  CD2 LEU A1032     6805  16206   4977    108     13   -326  A    C  
ATOM   1849  N   THR A1033       5.712 -15.977  14.894  1.00 74.79      A    N  
ANISOU 1849  N   THR A1033     6748  16667   5001    -42     92   -921  A    N  
ATOM   1850  CA  THR A1033       5.619 -15.480  16.272  1.00 75.73      A    C  
ANISOU 1850  CA  THR A1033     6791  16982   5001    -21     93  -1057  A    C  
ATOM   1851  C   THR A1033       5.766 -13.951  16.352  1.00 80.36      A    C  
ANISOU 1851  C   THR A1033     7331  17520   5682   -126    122  -1288  A    C  
ATOM   1852  O   THR A1033       6.276 -13.328  15.418  1.00 79.68      A    O  
ANISOU 1852  O   THR A1033     7264  17277   5733   -218    136  -1343  A    O  
ATOM   1853  CB  THR A1033       6.613 -16.224  17.197  1.00 87.46      A    C  
ANISOU 1853  CB  THR A1033     8193  18746   6293     65     34  -1060  A    C  
ATOM   1855  CG2 THR A1033       8.091 -15.894  16.903  1.00 85.32      A    C  
ANISOU 1855  CG2 THR A1033     7837  18557   6024     20     -4  -1196  A    C  
ATOM   1854  OG1 THR A1033       6.302 -15.910  18.556  1.00 93.85      A    O  
ANISOU 1854  OG1 THR A1033     8936  19759   6964    100     38  -1158  A    O  
ATOM   1856  N   LYS A1034       5.336 -13.365  17.485  1.00 78.74      A    N  
ANISOU 1856  N   LYS A1034     7066  17452   5398   -114    135  -1424  A    N  
ATOM   1857  CA  LYS A1034       5.420 -11.932  17.812  1.00 79.82      A    C  
ANISOU 1857  CA  LYS A1034     7151  17565   5611   -201    164  -1669  A    C  
ATOM   1858  C   LYS A1034       6.608 -11.640  18.787  1.00 85.05      A    C  
ANISOU 1858  C   LYS A1034     7676  18497   6142   -215    130  -1869  A    C  
ATOM   1859  O   LYS A1034       6.800 -10.486  19.201  1.00 85.52      A    O  
ANISOU 1859  O   LYS A1034     7675  18568   6249   -293    152  -2102  A    O  
ATOM   1860  CB  LYS A1034       4.090 -11.457  18.439  1.00 82.83      A    C  
ANISOU 1860  CB  LYS A1034     7550  17922   6001   -172    205  -1710  A    C  
ATOM   1861  CG  LYS A1034       2.969 -11.188  17.445  1.00 98.06      A    C  
ANISOU 1861  CG  LYS A1034     9591  19566   8103   -187    245  -1606  A    C  
ATOM   1862  CD  LYS A1034       1.704 -10.718  18.160  1.00109.11      A    C  
ANISOU 1862  CD  LYS A1034    10985  20976   9497   -148    281  -1671  A    C  
ATOM   1863  CE  LYS A1034       0.712 -10.049  17.234  1.00124.11      A    C  
ANISOU 1863  CE  LYS A1034    12974  22595  11588   -167    317  -1644  A    C  
ATOM   1864  NZ  LYS A1034      -0.046 -11.027  16.404  1.00134.33      A    N1+
ANISOU 1864  NZ  LYS A1034    14350  23782  12905   -124    319  -1403  A    N1+
ATOM   1865  N   SER A1035       7.384 -12.695  19.154  1.00 81.54      A    N  
ANISOU 1865  N   SER A1035     7181  18268   5533   -134     73  -1784  A    N  
ATOM   1866  CA  SER A1035       8.526 -12.623  20.076  1.00 83.10      A    C  
ANISOU 1866  CA  SER A1035     7237  18762   5573   -120     27  -1950  A    C  
ATOM   1867  C   SER A1035       9.885 -12.541  19.331  1.00 86.91      A    C  
ANISOU 1867  C   SER A1035     7671  19243   6110   -191      1  -2020  A    C  
ATOM   1868  O   SER A1035       9.959 -12.994  18.178  1.00 86.00      A    O  
ANISOU 1868  O   SER A1035     7637  18941   6099   -207      4  -1870  A    O  
ATOM   1869  CB  SER A1035       8.502 -13.793  21.062  1.00 87.07      A    C  
ANISOU 1869  CB  SER A1035     7710  19531   5844     31    -22  -1815  A    C  
ATOM   1870  OG  SER A1035       8.899 -15.020  20.471  1.00 95.27      A    O  
ANISOU 1870  OG  SER A1035     8812  20528   6860    109    -58  -1586  A    O  
ATOM   1871  N   PRO A1036      10.964 -11.985  19.957  1.00 83.73      A    N  
ANISOU 1871  N   PRO A1036     7124  19058   5631   -238    -23  -2254  A    N  
ATOM   1872  CA  PRO A1036      12.257 -11.867  19.236  1.00 83.18      A    C  
ANISOU 1872  CA  PRO A1036     6994  18999   5612   -320    -41  -2336  A    C  
ATOM   1873  C   PRO A1036      13.117 -13.136  19.139  1.00 86.31      A    C  
ANISOU 1873  C   PRO A1036     7351  19569   5872   -201   -114  -2199  A    C  
ATOM   1874  O   PRO A1036      14.199 -13.084  18.548  1.00 87.34      A    O  
ANISOU 1874  O   PRO A1036     7421  19727   6038   -261   -130  -2268  A    O  
ATOM   1875  CB  PRO A1036      12.990 -10.759  19.999  1.00 86.78      A    C  
ANISOU 1875  CB  PRO A1036     7302  19634   6036   -419    -35  -2656  A    C  
ATOM   1876  CG  PRO A1036      12.446 -10.831  21.379  1.00 92.69      A    C  
ANISOU 1876  CG  PRO A1036     7994  20615   6609   -314    -57  -2704  A    C  
ATOM   1877  CD  PRO A1036      11.040 -11.370  21.302  1.00 86.85      A    C  
ANISOU 1877  CD  PRO A1036     7398  19704   5896   -232    -31  -2475  A    C  
ATOM   1878  N   SER A1037      12.640 -14.268  19.687  1.00 81.33      A    N  
ANISOU 1878  N   SER A1037     6759  19049   5095    -34   -156  -2005  A    N  
ATOM   1879  CA  SER A1037      13.357 -15.544  19.692  1.00 80.47      A    C  
ANISOU 1879  CA  SER A1037     6629  19094   4853    110   -229  -1857  A    C  
ATOM   1880  C   SER A1037      13.207 -16.361  18.407  1.00 79.74      A    C  
ANISOU 1880  C   SER A1037     6657  18759   4881    128   -224  -1638  A    C  
ATOM   1881  O   SER A1037      12.109 -16.492  17.872  1.00 76.73      A    O  
ANISOU 1881  O   SER A1037     6408  18134   4611    110   -177  -1491  A    O  
ATOM   1882  CB  SER A1037      12.931 -16.385  20.889  1.00 85.76      A    C  
ANISOU 1882  CB  SER A1037     7299  19972   5312    277   -270  -1734  A    C  
ATOM   1883  OG  SER A1037      13.429 -17.710  20.803  1.00 97.51      A    O  
ANISOU 1883  OG  SER A1037     8803  21555   6693    431   -337  -1551  A    O  
ATOM   1884  N   LEU A1038      14.314 -16.963  17.959  1.00 76.07      A    N  
ANISOU 1884  N   LEU A1038     6135  18388   4380    176   -278  -1626  A    N  
ATOM   1885  CA  LEU A1038      14.334 -17.824  16.785  1.00 74.52      A    C  
ANISOU 1885  CA  LEU A1038     6031  18005   4278    209   -283  -1441  A    C  
ATOM   1886  C   LEU A1038      13.788 -19.209  17.143  1.00 79.71      A    C  
ANISOU 1886  C   LEU A1038     6776  18676   4833    392   -322  -1193  A    C  
ATOM   1887  O   LEU A1038      13.104 -19.831  16.326  1.00 77.82      A    O  
ANISOU 1887  O   LEU A1038     6663  18207   4697    405   -297  -1009  A    O  
ATOM   1888  CB  LEU A1038      15.756 -17.916  16.209  1.00 74.58      A    C  
ANISOU 1888  CB  LEU A1038     5928  18125   4282    191   -324  -1547  A    C  
ATOM   1889  CG  LEU A1038      15.957 -18.683  14.894  1.00 76.93      A    C  
ANISOU 1889  CG  LEU A1038     6296  18254   4680    212   -329  -1400  A    C  
ATOM   1890  CD1 LEU A1038      15.075 -18.142  13.790  1.00 75.88      A    C  
ANISOU 1890  CD1 LEU A1038     6275  17806   4749     62   -247  -1355  A    C  
ATOM   1891  CD2 LEU A1038      17.394 -18.614  14.460  1.00 78.48      A    C  
ANISOU 1891  CD2 LEU A1038     6354  18623   4840    206   -373  -1534  A    C  
ATOM   1892  N   ASN A1039      14.076 -19.673  18.375  1.00 78.21      A    N  
ANISOU 1892  N   ASN A1039     6520  18755   4440    528   -379  -1190  A    N  
ATOM   1893  CA  ASN A1039      13.628 -20.967  18.895  1.00 78.47      A    C  
ANISOU 1893  CA  ASN A1039     6637  18824   4354    704   -415   -952  A    C  
ATOM   1894  C   ASN A1039      12.100 -21.007  19.017  1.00 81.71      A    C  
ANISOU 1894  C   ASN A1039     7183  19045   4820    673   -345   -806  A    C  
ATOM   1895  O   ASN A1039      11.479 -22.028  18.691  1.00 80.52      A    O  
ANISOU 1895  O   ASN A1039     7154  18743   4698    743   -338   -582  A    O  
ATOM   1896  CB  ASN A1039      14.310 -21.264  20.223  1.00 81.70      A    C  
ANISOU 1896  CB  ASN A1039     6937  19584   4520    844   -487   -999  A    C  
ATOM   1897  CG  ASN A1039      15.810 -21.050  20.194  1.00111.50      A    C  
ANISOU 1897  CG  ASN A1039    10547  23590   8229    865   -555  -1190  A    C  
ATOM   1899  ND2 ASN A1039      16.328 -20.331  21.182  1.00 99.83      A    N  
ANISOU 1899  ND2 ASN A1039     8922  22390   6617    848   -578  -1399  A    N  
ATOM   1898  OD1 ASN A1039      16.516 -21.520  19.288  1.00112.80      A    O  
ANISOU 1898  OD1 ASN A1039    10703  23698   8459    894   -587  -1164  A    O  
ATOM   1900  N   ALA A1040      11.495 -19.870  19.438  1.00 77.91      A    N  
ANISOU 1900  N   ALA A1040     6674  18562   4365    560   -291   -949  A    N  
ATOM   1901  CA  ALA A1040      10.044 -19.697  19.535  1.00 76.05      A    C  
ANISOU 1901  CA  ALA A1040     6541  18164   4191    515   -221   -857  A    C  
ATOM   1902  C   ALA A1040       9.447 -19.789  18.125  1.00 77.16      A    C  
ANISOU 1902  C   ALA A1040     6796  17976   4546    436   -174   -754  A    C  
ATOM   1903  O   ALA A1040       8.444 -20.473  17.951  1.00 76.24      A    O  
ANISOU 1903  O   ALA A1040     6789  17720   4459    467   -144   -568  A    O  
ATOM   1904  CB  ALA A1040       9.711 -18.351  20.163  1.00 77.09      A    C  
ANISOU 1904  CB  ALA A1040     6600  18364   4325    413   -180  -1074  A    C  
ATOM   1905  N   ALA A1041      10.101 -19.160  17.114  1.00 72.24      A    N  
ANISOU 1905  N   ALA A1041     6143  17243   4061    334   -169   -872  A    N  
ATOM   1906  CA  ALA A1041       9.661 -19.194  15.711  1.00 69.95      A    C  
ANISOU 1906  CA  ALA A1041     5949  16669   3961    259   -130   -787  A    C  
ATOM   1907  C   ALA A1041       9.797 -20.603  15.123  1.00 72.90      A    C  
ANISOU 1907  C   ALA A1041     6391  16976   4332    362   -163   -585  A    C  
ATOM   1908  O   ALA A1041       8.909 -21.039  14.402  1.00 70.59      A    O  
ANISOU 1908  O   ALA A1041     6204  16477   4141    349   -128   -443  A    O  
ATOM   1909  CB  ALA A1041      10.447 -18.188  14.881  1.00 70.29      A    C  
ANISOU 1909  CB  ALA A1041     5935  16651   4122    128   -117   -958  A    C  
ATOM   1910  N   LYS A1042      10.888 -21.321  15.473  1.00 71.43      A    N  
ANISOU 1910  N   LYS A1042     6140  16973   4027    472   -233   -580  A    N  
ATOM   1911  CA  LYS A1042      11.182 -22.695  15.047  1.00 71.23      A    C  
ANISOU 1911  CA  LYS A1042     6170  16907   3987    595   -276   -407  A    C  
ATOM   1912  C   LYS A1042      10.161 -23.690  15.611  1.00 75.73      A    C  
ANISOU 1912  C   LYS A1042     6853  17423   4500    689   -261   -192  A    C  
ATOM   1913  O   LYS A1042       9.772 -24.622  14.911  1.00 75.32      A    O  
ANISOU 1913  O   LYS A1042     6897  17193   4526    723   -253    -34  A    O  
ATOM   1914  CB  LYS A1042      12.601 -23.106  15.481  1.00 74.94      A    C  
ANISOU 1914  CB  LYS A1042     6530  17622   4323    709   -360   -474  A    C  
ATOM   1915  CG  LYS A1042      13.716 -22.565  14.600  1.00 83.71      A    C  
ANISOU 1915  CG  LYS A1042     7541  18760   5506    630   -376   -642  A    C  
ATOM   1916  CD  LYS A1042      15.088 -22.951  15.137  1.00 87.13      A    C  
ANISOU 1916  CD  LYS A1042     7848  19466   5792    756   -464   -719  A    C  
ATOM   1917  CE  LYS A1042      16.211 -22.470  14.246  1.00 86.42      A    C  
ANISOU 1917  CE  LYS A1042     7646  19422   5767    670   -474   -892  A    C  
ATOM   1918  NZ  LYS A1042      17.518 -23.068  14.627  1.00 90.24      A    N1+
ANISOU 1918  NZ  LYS A1042     8010  20160   6116    818   -566   -946  A    N1+
ATOM   1919  N   SER A1043       9.737 -23.500  16.869  1.00 73.36      A    N  
ANISOU 1919  N   SER A1043     6534  17278   4061    723   -255   -192  A    N  
ATOM   1920  CA  SER A1043       8.748 -24.365  17.512  1.00 73.99      A    C  
ANISOU 1920  CA  SER A1043     6714  17330   4070    794   -230      9  A    C  
ATOM   1921  C   SER A1043       7.351 -24.171  16.897  1.00 77.77      A    C  
ANISOU 1921  C   SER A1043     7287  17568   4694    684   -146     73  A    C  
ATOM   1922  O   SER A1043       6.619 -25.150  16.721  1.00 77.32      A    O  
ANISOU 1922  O   SER A1043     7336  17381   4661    717   -120    261  A    O  
ATOM   1923  CB  SER A1043       8.724 -24.133  19.021  1.00 78.41      A    C  
ANISOU 1923  CB  SER A1043     7213  18154   4426    853   -243    -25  A    C  
ATOM   1924  OG  SER A1043       7.647 -24.842  19.610  1.00 86.43      A    O  
ANISOU 1924  OG  SER A1043     8328  19137   5374    897   -203    172  A    O  
ATOM   1925  N   GLU A1044       6.995 -22.915  16.556  1.00 74.06      A    N  
ANISOU 1925  N   GLU A1044     6779  17037   4324    554   -106    -86  A    N  
ATOM   1926  CA  GLU A1044       5.718 -22.585  15.916  1.00 72.93      A    C  
ANISOU 1926  CA  GLU A1044     6708  16679   4321    459    -35    -49  A    C  
ATOM   1927  C   GLU A1044       5.650 -23.177  14.493  1.00 75.57      A    C  
ANISOU 1927  C   GLU A1044     7115  16787   4810    436    -30     45  A    C  
ATOM   1928  O   GLU A1044       4.585 -23.598  14.054  1.00 75.13      A    O  
ANISOU 1928  O   GLU A1044     7142  16572   4833    409     15    158  A    O  
ATOM   1929  CB  GLU A1044       5.473 -21.061  15.903  1.00 74.10      A    C  
ANISOU 1929  CB  GLU A1044     6799  16817   4539    346     -2   -248  A    C  
ATOM   1930  CG  GLU A1044       5.295 -20.421  17.278  1.00 82.54      A    C  
ANISOU 1930  CG  GLU A1044     7793  18098   5469    357      4   -364  A    C  
ATOM   1931  CD  GLU A1044       4.000 -20.638  18.047  1.00109.03      A    C  
ANISOU 1931  CD  GLU A1044    11186  21484   8758    371     54   -284  A    C  
ATOM   1932  OE1 GLU A1044       3.836 -19.986  19.104  1.00110.43      A    O  
ANISOU 1932  OE1 GLU A1044    11292  21830   8838    365     65   -412  A    O  
ATOM   1933  OE2 GLU A1044       3.152 -21.451  17.607  1.00102.00      A    O1-
ANISOU 1933  OE2 GLU A1044    10386  20460   7908    382     86   -108  A    O1-
ATOM   1934  N   LEU A1045       6.800 -23.251  13.808  1.00 72.20      A    N  
ANISOU 1934  N   LEU A1045     6649  16367   4417    448    -78    -10  A    N  
ATOM   1935  CA  LEU A1045       6.952 -23.816  12.466  1.00 70.97      A    C  
ANISOU 1935  CA  LEU A1045     6541  16035   4388    435    -82     55  A    C  
ATOM   1936  C   LEU A1045       6.716 -25.340  12.464  1.00 75.25      A    C  
ANISOU 1936  C   LEU A1045     7169  16515   4909    539    -94    250  A    C  
ATOM   1937  O   LEU A1045       5.940 -25.828  11.647  1.00 74.09      A    O  
ANISOU 1937  O   LEU A1045     7098  16180   4872    505    -59    343  A    O  
ATOM   1938  CB  LEU A1045       8.343 -23.447  11.891  1.00 71.13      A    C  
ANISOU 1938  CB  LEU A1045     6475  16127   4423    423   -128    -75  A    C  
ATOM   1939  CG  LEU A1045       8.704 -23.959  10.480  1.00 75.10      A    C  
ANISOU 1939  CG  LEU A1045     7003  16487   5043    407   -136    -39  A    C  
ATOM   1940  CD1 LEU A1045       7.671 -23.528   9.435  1.00 74.31      A    C  
ANISOU 1940  CD1 LEU A1045     6966  16176   5092    294    -76    -20  A    C  
ATOM   1941  CD2 LEU A1045      10.100 -23.527  10.088  1.00 75.87      A    C  
ANISOU 1941  CD2 LEU A1045     6997  16701   5129    389   -176   -182  A    C  
ATOM   1942  N   ASP A1046       7.363 -26.075  13.387  1.00 73.71      A    N  
ANISOU 1942  N   ASP A1046     6961  16474   4572    666   -143    310  A    N  
ATOM   1943  CA  ASP A1046       7.231 -27.530  13.532  1.00 74.59      A    C  
ANISOU 1943  CA  ASP A1046     7162  16525   4654    779   -157    503  A    C  
ATOM   1944  C   ASP A1046       5.797 -27.960  13.914  1.00 79.74      A    C  
ANISOU 1944  C   ASP A1046     7913  17070   5314    745    -87    648  A    C  
ATOM   1945  O   ASP A1046       5.364 -29.055  13.544  1.00 80.02      A    O  
ANISOU 1945  O   ASP A1046     8044  16955   5403    777    -70    800  A    O  
ATOM   1946  CB  ASP A1046       8.286 -28.079  14.514  1.00 78.09      A    C  
ANISOU 1946  CB  ASP A1046     7565  17177   4928    934   -230    531  A    C  
ATOM   1947  CG  ASP A1046       9.750 -27.922  14.079  1.00 90.30      A    C  
ANISOU 1947  CG  ASP A1046     9010  18835   6464    987   -305    400  A    C  
ATOM   1948  OD1 ASP A1046      10.030 -27.082  13.182  1.00 89.40      A    O  
ANISOU 1948  OD1 ASP A1046     8836  18679   6454    876   -293    253  A    O  
ATOM   1949  OD2 ASP A1046      10.613 -28.630  14.638  1.00 99.26      A    O1-
ANISOU 1949  OD2 ASP A1046    10123  20108   7483   1139   -373    446  A    O1-
ATOM   1950  N   LYS A1047       5.050 -27.081  14.610  1.00 76.08      A    N  
ANISOU 1950  N   LYS A1047     7422  16680   4804    673    -42    589  A    N  
ATOM   1951  CA  LYS A1047       3.653 -27.329  14.964  1.00 75.94      A    C  
ANISOU 1951  CA  LYS A1047     7474  16590   4790    623     32    697  A    C  
ATOM   1952  C   LYS A1047       2.743 -27.079  13.743  1.00 78.75      A    C  
ANISOU 1952  C   LYS A1047     7865  16731   5327    510     83    678  A    C  
ATOM   1953  O   LYS A1047       1.784 -27.823  13.535  1.00 78.58      A    O  
ANISOU 1953  O   LYS A1047     7919  16586   5353    483    135    800  A    O  
ATOM   1954  CB  LYS A1047       3.225 -26.462  16.159  1.00 79.07      A    C  
ANISOU 1954  CB  LYS A1047     7811  17172   5060    600     56    620  A    C  
ATOM   1955  N   ALA A1048       3.064 -26.049  12.927  1.00 74.29      A    N  
ANISOU 1955  N   ALA A1048     7243  16126   4859    444     71    528  A    N  
ATOM   1956  CA  ALA A1048       2.318 -25.674  11.715  1.00 72.80      A    C  
ANISOU 1956  CA  ALA A1048     7077  15755   4830    349    109    501  A    C  
ATOM   1957  C   ALA A1048       2.426 -26.698  10.578  1.00 76.66      A    C  
ANISOU 1957  C   ALA A1048     7624  16084   5421    362    100    591  A    C  
ATOM   1958  O   ALA A1048       1.487 -26.830   9.790  1.00 75.80      A    O  
ANISOU 1958  O   ALA A1048     7552  15831   5417    300    141    624  A    O  
ATOM   1959  CB  ALA A1048       2.765 -24.300  11.222  1.00 72.71      A    C  
ANISOU 1959  CB  ALA A1048     6997  15754   4876    283     97    330  A    C  
ATOM   1960  N   ILE A1049       3.576 -27.390  10.476  1.00 73.88      A    N  
ANISOU 1960  N   ILE A1049     7267  15766   5037    448     43    615  A    N  
ATOM   1961  CA  ILE A1049       3.859 -28.377   9.427  1.00 73.44      A    C  
ANISOU 1961  CA  ILE A1049     7255  15574   5074    476     27    677  A    C  
ATOM   1962  C   ILE A1049       3.516 -29.818   9.876  1.00 77.60      A    C  
ANISOU 1962  C   ILE A1049     7873  16038   5573    553     36    848  A    C  
ATOM   1963  O   ILE A1049       3.052 -30.621   9.063  1.00 76.60      A    O  
ANISOU 1963  O   ILE A1049     7805  15748   5551    536     59    914  A    O  
ATOM   1964  CB  ILE A1049       5.330 -28.229   8.913  1.00 76.75      A    C  
ANISOU 1964  CB  ILE A1049     7606  16063   5492    521    -40    579  A    C  
ATOM   1965  CG1 ILE A1049       5.688 -26.752   8.524  1.00 76.52      A    C  
ANISOU 1965  CG1 ILE A1049     7494  16093   5488    427    -38    414  A    C  
ATOM   1966  CG2 ILE A1049       5.667 -29.215   7.782  1.00 77.32      A    C  
ANISOU 1966  CG2 ILE A1049     7710  16006   5662    552    -58    618  A    C  
ATOM   1967  CD1 ILE A1049       5.007 -26.120   7.247  1.00 85.38      A    C  
ANISOU 1967  CD1 ILE A1049     8629  17068   6745    309      5    375  A    C  
ATOM   1968  N   GLY A1050       3.774 -30.129  11.143  1.00 74.85      A    N  
ANISOU 1968  N   GLY A1050     7535  15821   5085    636     20    916  A    N  
ATOM   1969  CA  GLY A1050       3.504 -31.446  11.708  1.00 75.59      A    C  
ANISOU 1969  CA  GLY A1050     7725  15859   5135    713     33   1096  A    C  
ATOM   1970  C   GLY A1050       4.691 -32.386  11.772  1.00 80.01      A    C  
ANISOU 1970  C   GLY A1050     8306  16434   5660    863    -39   1153  A    C  
ATOM   1971  O   GLY A1050       4.506 -33.584  12.003  1.00 80.91      A    O  
ANISOU 1971  O   GLY A1050     8519  16442   5779    929    -29   1310  A    O  
ATOM   1972  N   ARG A1051       5.921 -31.851  11.578  1.00 75.64      A    N  
ANISOU 1972  N   ARG A1051     7656  16010   5072    917   -111   1023  A    N  
ATOM   1973  CA  ARG A1051       7.194 -32.593  11.630  1.00 76.02      A    C  
ANISOU 1973  CA  ARG A1051     7692  16115   5076   1074   -192   1039  A    C  
ATOM   1974  C   ARG A1051       8.375 -31.677  12.038  1.00 80.20      A    C  
ANISOU 1974  C   ARG A1051     8088  16889   5494   1116   -258    884  A    C  
ATOM   1975  O   ARG A1051       8.232 -30.453  11.993  1.00 79.43      A    O  
ANISOU 1975  O   ARG A1051     7915  16869   5397   1002   -236    750  A    O  
ATOM   1976  CB  ARG A1051       7.474 -33.308  10.288  1.00 74.98      A    C  
ANISOU 1976  CB  ARG A1051     7586  15805   5100   1082   -205   1024  A    C  
ATOM   1977  CG  ARG A1051       7.568 -32.395   9.063  1.00 77.92      A    C  
ANISOU 1977  CG  ARG A1051     7875  16154   5577    959   -195    857  A    C  
ATOM   1978  CD  ARG A1051       7.868 -33.187   7.805  1.00 78.33      A    C  
ANISOU 1978  CD  ARG A1051     7946  16055   5760    977   -208    844  A    C  
ATOM   1979  NE  ARG A1051       8.469 -32.352   6.761  1.00 76.02      A    N  
ANISOU 1979  NE  ARG A1051     7552  15812   5519    903   -222    680  A    N  
ATOM   1980  CZ  ARG A1051       9.773 -32.119   6.649  1.00 83.39      A    C  
ANISOU 1980  CZ  ARG A1051     8388  16893   6402    967   -285    572  A    C  
ATOM   1981  NH1 ARG A1051      10.627 -32.654   7.515  1.00 68.23      A    N1+
ANISOU 1981  NH1 ARG A1051     6452  15094   4376   1123   -348    603  A    N1+
ATOM   1982  NH2 ARG A1051      10.234 -31.346   5.673  1.00 63.83      A    N  
ANISOU 1982  NH2 ARG A1051     5825  14453   3974    877   -283    433  A    N  
ATOM   1983  N   ASN A1052       9.538 -32.262  12.408  1.00 77.37      A    N  
ANISOU 1983  N   ASN A1052     7698  16650   5048   1279   -340    894  A    N  
ATOM   1984  CA  ASN A1052      10.724 -31.485  12.793  1.00 77.38      A    C  
ANISOU 1984  CA  ASN A1052     7557  16903   4939   1322   -406    734  A    C  
ATOM   1985  C   ASN A1052      11.407 -30.892  11.543  1.00 79.29      A    C  
ANISOU 1985  C   ASN A1052     7707  17129   5292   1241   -418    558  A    C  
ATOM   1986  O   ASN A1052      12.354 -31.485  11.044  1.00 78.98      A    O  
ANISOU 1986  O   ASN A1052     7627  17117   5264   1342   -477    524  A    O  
ATOM   1987  CB  ASN A1052      11.716 -32.342  13.623  1.00 79.33      A    C  
ANISOU 1987  CB  ASN A1052     7794  17305   5041   1538   -493    807  A    C  
ATOM   1988  CG  ASN A1052      11.127 -33.042  14.839  1.00 95.03      A    C  
ANISOU 1988  CG  ASN A1052     9885  19317   6905   1630   -482   1006  A    C  
ATOM   1990  ND2 ASN A1052      11.621 -34.241  15.131  1.00 84.64      A    N  
ANISOU 1990  ND2 ASN A1052     8634  17990   5535   1820   -539   1148  A    N  
ATOM   1989  OD1 ASN A1052      10.243 -32.526  15.539  1.00 84.72      A    O  
ANISOU 1989  OD1 ASN A1052     8601  18044   5546   1537   -422   1037  A    O  
ATOM   1991  N   THR A1053      10.930 -29.726  11.044  1.00 74.64      A    N  
ANISOU 1991  N   THR A1053     7082  16498   4779   1064   -361    448  A    N  
ATOM   1992  CA  THR A1053      11.455 -29.068   9.823  1.00 73.75      A    C  
ANISOU 1992  CA  THR A1053     6895  16356   4771    960   -356    298  A    C  
ATOM   1993  C   THR A1053      12.924 -28.604   9.907  1.00 77.53      A    C  
ANISOU 1993  C   THR A1053     7229  17058   5172    997   -419    133  A    C  
ATOM   1994  O   THR A1053      13.671 -28.696   8.924  1.00 75.95      A    O  
ANISOU 1994  O   THR A1053     6973  16848   5035    985   -437     52  A    O  
ATOM   1995  CB  THR A1053      10.562 -27.890   9.388  1.00 82.01      A    C  
ANISOU 1995  CB  THR A1053     7947  17314   5901    775   -281    234  A    C  
ATOM   1997  CG2 THR A1053       9.161 -28.326   8.985  1.00 79.72      A    C  
ANISOU 1997  CG2 THR A1053     7776  16803   5712    724   -219    366  A    C  
ATOM   1996  OG1 THR A1053      10.517 -26.911  10.429  1.00 82.26      A    O  
ANISOU 1996  OG1 THR A1053     7927  17495   5833    739   -273    161  A    O  
ATOM   1998  N   ASN A1054      13.305 -28.080  11.079  1.00 75.51      A    N  
ANISOU 1998  N   ASN A1054     6903  17014   4774   1035   -448     74  A    N  
ATOM   1999  CA  ASN A1054      14.616 -27.520  11.422  1.00 76.04      A    C  
ANISOU 1999  CA  ASN A1054     6816  17334   4741   1062   -505   -100  A    C  
ATOM   2000  C   ASN A1054      14.862 -26.171  10.698  1.00 78.71      A    C  
ANISOU 2000  C   ASN A1054     7067  17680   5159    867   -460   -289  A    C  
ATOM   2001  O   ASN A1054      16.004 -25.798  10.433  1.00 79.57      A    O  
ANISOU 2001  O   ASN A1054     7048  17947   5238    851   -493   -445  A    O  
ATOM   2002  CB  ASN A1054      15.756 -28.540  11.242  1.00 75.50      A    C  
ANISOU 2002  CB  ASN A1054     6700  17357   4629   1237   -588    -93  A    C  
ATOM   2003  CG  ASN A1054      16.940 -28.275  12.122  1.00105.07      A    C  
ANISOU 2003  CG  ASN A1054    10302  21412   8209   1337   -664   -215  A    C  
ATOM   2005  ND2 ASN A1054      16.723 -28.256  13.435  1.00101.32      A    N  
ANISOU 2005  ND2 ASN A1054     9842  21068   7589   1431   -689   -147  A    N  
ATOM   2004  OD1 ASN A1054      18.059 -28.083  11.638  1.00101.97      A    O  
ANISOU 2004  OD1 ASN A1054     9776  21158   7809   1328   -699   -377  A    O  
ATOM   2006  N   GLY A1055      13.775 -25.434  10.456  1.00 73.42      A    N  
ANISOU 2006  N   GLY A1055     6467  16847   4581    721   -383   -272  A    N  
ATOM   2007  CA  GLY A1055      13.796 -24.109   9.848  1.00 72.23      A    C  
ANISOU 2007  CA  GLY A1055     6267  16662   4515    535   -331   -419  A    C  
ATOM   2008  C   GLY A1055      13.713 -24.062   8.340  1.00 74.62      A    C  
ANISOU 2008  C   GLY A1055     6603  16787   4963    439   -293   -412  A    C  
ATOM   2009  O   GLY A1055      13.734 -22.969   7.769  1.00 74.31      A    O  
ANISOU 2009  O   GLY A1055     6541  16695   4997    283   -243   -509  A    O  
ATOM   2010  N   VAL A1056      13.633 -25.241   7.683  1.00 70.10      A    N  
ANISOU 2010  N   VAL A1056     6084  16120   4430    531   -315   -299  A    N  
ATOM   2011  CA  VAL A1056      13.561 -25.357   6.222  1.00 68.49      A    C  
ANISOU 2011  CA  VAL A1056     5905  15768   4349    458   -286   -289  A    C  
ATOM   2012  C   VAL A1056      12.348 -26.189   5.780  1.00 72.19      A    C  
ANISOU 2012  C   VAL A1056     6507  16023   4900    487   -258   -122  A    C  
ATOM   2013  O   VAL A1056      12.137 -27.294   6.285  1.00 72.51      A    O  
ANISOU 2013  O   VAL A1056     6604  16042   4905    620   -289     -8  A    O  
ATOM   2014  CB  VAL A1056      14.874 -25.885   5.573  1.00 72.00      A    C  
ANISOU 2014  CB  VAL A1056     6253  16325   4777    516   -334   -369  A    C  
ATOM   2015  CG1 VAL A1056      14.833 -25.736   4.055  1.00 70.43      A    C  
ANISOU 2015  CG1 VAL A1056     6062  16007   4692    407   -293   -387  A    C  
ATOM   2016  CG2 VAL A1056      16.100 -25.178   6.133  1.00 72.94      A    C  
ANISOU 2016  CG2 VAL A1056     6226  16688   4801    496   -365   -542  A    C  
ATOM   2017  N   ILE A1057      11.579 -25.660   4.808  1.00 67.11      A    N  
ANISOU 2017  N   ILE A1057     5911  15222   4366    362   -200   -109  A    N  
ATOM   2018  CA  ILE A1057      10.414 -26.330   4.247  1.00 66.01      A    C  
ANISOU 2018  CA  ILE A1057     5879  14891   4311    365   -169     21  A    C  
ATOM   2019  C   ILE A1057      10.541 -26.504   2.730  1.00 70.27      A    C  
ANISOU 2019  C   ILE A1057     6414  15342   4943    312   -155      5  A    C  
ATOM   2020  O   ILE A1057      11.362 -25.854   2.062  1.00 70.83      A    O  
ANISOU 2020  O   ILE A1057     6409  15485   5020    239   -153   -100  A    O  
ATOM   2021  CB  ILE A1057       9.057 -25.687   4.654  1.00 68.61      A    C  
ANISOU 2021  CB  ILE A1057     6278  15122   4667    291   -115     73  A    C  
ATOM   2022  CG1 ILE A1057       8.858 -24.286   4.008  1.00 68.60      A    C  
ANISOU 2022  CG1 ILE A1057     6256  15079   4728    143    -70    -13  A    C  
ATOM   2023  CG2 ILE A1057       8.873 -25.667   6.177  1.00 70.43      A    C  
ANISOU 2023  CG2 ILE A1057     6513  15454   4794    355   -127     95  A    C  
ATOM   2024  CD1 ILE A1057       7.479 -23.587   4.280  1.00 73.72      A    C  
ANISOU 2024  CD1 ILE A1057     6973  15617   5422     80    -18     30  A    C  
ATOM   2025  N   THR A1058       9.692 -27.400   2.213  1.00 64.07      A    N  
ANISOU 2025  N   THR A1058     5708  14410   4226    342   -141    107  A    N  
ATOM   2026  CA  THR A1058       9.510 -27.827   0.837  1.00 61.51      A    C  
ANISOU 2026  CA  THR A1058     5394  13989   3988    309   -127    112  A    C  
ATOM   2027  C   THR A1058       8.556 -26.809   0.171  1.00 65.04      A    C  
ANISOU 2027  C   THR A1058     5870  14347   4495    174    -70    116  A    C  
ATOM   2028  O   THR A1058       7.779 -26.167   0.890  1.00 64.52      A    O  
ANISOU 2028  O   THR A1058     5842  14252   4421    138    -43    145  A    O  
ATOM   2029  CB  THR A1058       8.957 -29.269   0.966  1.00 62.21      A    C  
ANISOU 2029  CB  THR A1058     5559  13968   4111    414   -139    218  A    C  
ATOM   2031  CG2 THR A1058       7.675 -29.515   0.231  1.00 60.15      A    C  
ANISOU 2031  CG2 THR A1058     5366  13547   3941    351    -92    281  A    C  
ATOM   2030  OG1 THR A1058       9.937 -30.231   0.613  1.00 57.53      A    O  
ANISOU 2030  OG1 THR A1058     4928  13413   3515    517   -188    186  A    O  
ATOM   2032  N   LYS A1059       8.596 -26.664  -1.187  1.00 62.05      A    N  
ANISOU 2032  N   LYS A1059     5473  13932   4171    108    -54     87  A    N  
ATOM   2033  CA  LYS A1059       7.689 -25.754  -1.922  1.00 60.62      A    C  
ANISOU 2033  CA  LYS A1059     5324  13667   4042     -2     -6    105  A    C  
ATOM   2034  C   LYS A1059       6.232 -26.194  -1.762  1.00 64.30      A    C  
ANISOU 2034  C   LYS A1059     5869  14008   4554     13     17    199  A    C  
ATOM   2035  O   LYS A1059       5.356 -25.347  -1.534  1.00 64.48      A    O  
ANISOU 2035  O   LYS A1059     5925  13984   4591    -40     49    221  A    O  
ATOM   2036  CB  LYS A1059       8.060 -25.643  -3.406  1.00 62.18      A    C  
ANISOU 2036  CB  LYS A1059     5484  13873   4270    -62      4     68  A    C  
ATOM   2037  CG  LYS A1059       7.291 -24.550  -4.159  1.00 64.39      A    C  
ANISOU 2037  CG  LYS A1059     5794  14088   4585   -169     48     90  A    C  
ATOM   2038  CD  LYS A1059       7.771 -24.412  -5.586  1.00 70.82      A    C  
ANISOU 2038  CD  LYS A1059     6571  14929   5408   -223     58     67  A    C  
ATOM   2039  CE  LYS A1059       6.785 -23.674  -6.445  1.00 82.53      A    C  
ANISOU 2039  CE  LYS A1059     8097  16338   6922   -302     95    117  A    C  
ATOM   2040  NZ  LYS A1059       6.802 -24.184  -7.841  1.00 93.91      A    N1+
ANISOU 2040  NZ  LYS A1059     9514  17801   8368   -323     99    120  A    N1+
ATOM   2041  N   ASP A1060       5.976 -27.518  -1.852  1.00 59.88      A    N  
ANISOU 2041  N   ASP A1060     5336  13393   4021     86      4    247  A    N  
ATOM   2042  CA  ASP A1060       4.636 -28.074  -1.656  1.00 58.69      A    C  
ANISOU 2042  CA  ASP A1060     5253  13132   3914     92     31    329  A    C  
ATOM   2043  C   ASP A1060       4.112 -27.800  -0.253  1.00 61.94      A    C  
ANISOU 2043  C   ASP A1060     5702  13550   4282    110     45    377  A    C  
ATOM   2044  O   ASP A1060       2.945 -27.442  -0.123  1.00 61.31      A    O  
ANISOU 2044  O   ASP A1060     5655  13413   4226     67     81    414  A    O  
ATOM   2045  CB  ASP A1060       4.563 -29.562  -2.039  1.00 60.75      A    C  
ANISOU 2045  CB  ASP A1060     5538  13324   4222    156     20    360  A    C  
ATOM   2046  CG  ASP A1060       4.399 -29.805  -3.542  1.00 68.88      A    C  
ANISOU 2046  CG  ASP A1060     6541  14321   5311    115     26    318  A    C  
ATOM   2047  OD1 ASP A1060       4.151 -28.819  -4.287  1.00 68.47      A    O  
ANISOU 2047  OD1 ASP A1060     6462  14294   5260     36     43    290  A    O  
ATOM   2048  OD2 ASP A1060       4.508 -30.977  -3.971  1.00 73.31      A    O1-
ANISOU 2048  OD2 ASP A1060     7109  14829   5917    163     14    314  A    O1-
ATOM   2049  N   GLU A1061       4.990 -27.868   0.781  1.00 59.98      A    N  
ANISOU 2049  N   GLU A1061     5436  13395   3960    173     14    365  A    N  
ATOM   2050  CA  GLU A1061       4.655 -27.552   2.183  1.00 60.13      A    C  
ANISOU 2050  CA  GLU A1061     5475  13459   3912    195     22    398  A    C  
ATOM   2051  C   GLU A1061       4.336 -26.054   2.359  1.00 63.46      A    C  
ANISOU 2051  C   GLU A1061     5875  13912   4326    111     48    337  A    C  
ATOM   2052  O   GLU A1061       3.435 -25.724   3.124  1.00 62.95      A    O  
ANISOU 2052  O   GLU A1061     5837  13835   4244     99     76    365  A    O  
ATOM   2053  CB  GLU A1061       5.773 -27.979   3.135  1.00 62.28      A    C  
ANISOU 2053  CB  GLU A1061     5722  13847   4094    292    -25    390  A    C  
ATOM   2054  CG  GLU A1061       5.692 -29.439   3.550  1.00 72.35      A    C  
ANISOU 2054  CG  GLU A1061     7054  15070   5363    395    -40    492  A    C  
ATOM   2055  CD  GLU A1061       6.859 -30.014   4.341  1.00 88.36      A    C  
ANISOU 2055  CD  GLU A1061     9061  17210   7302    521    -98    498  A    C  
ATOM   2056  OE1 GLU A1061       7.871 -29.303   4.556  1.00 73.06      A    O  
ANISOU 2056  OE1 GLU A1061     7041  15418   5301    529   -133    400  A    O  
ATOM   2057  OE2 GLU A1061       6.757 -31.198   4.736  1.00 78.96      A    O1-
ANISOU 2057  OE2 GLU A1061     7935  15959   6107    614   -108    601  A    O1-
ATOM   2058  N   ALA A1062       5.062 -25.162   1.638  1.00 59.53      A    N  
ANISOU 2058  N   ALA A1062     5328  13448   3843     52     41    251  A    N  
ATOM   2059  CA  ALA A1062       4.852 -23.709   1.638  1.00 58.80      A    C  
ANISOU 2059  CA  ALA A1062     5224  13353   3763    -33     68    190  A    C  
ATOM   2060  C   ALA A1062       3.495 -23.339   1.008  1.00 62.54      A    C  
ANISOU 2060  C   ALA A1062     5746  13708   4309    -79    106    237  A    C  
ATOM   2061  O   ALA A1062       2.807 -22.462   1.538  1.00 62.62      A    O  
ANISOU 2061  O   ALA A1062     5771  13697   4325   -106    130    221  A    O  
ATOM   2062  CB  ALA A1062       5.990 -23.013   0.893  1.00 59.55      A    C  
ANISOU 2062  CB  ALA A1062     5265  13499   3864    -95     60    104  A    C  
ATOM   2063  N   GLU A1063       3.113 -24.004  -0.118  1.00 58.06      A    N  
ANISOU 2063  N   GLU A1063     5194  13073   3794    -81    108    282  A    N  
ATOM   2064  CA  GLU A1063       1.827 -23.788  -0.799  1.00 57.25      A    C  
ANISOU 2064  CA  GLU A1063     5123  12880   3750   -112    137    323  A    C  
ATOM   2065  C   GLU A1063       0.643 -24.266   0.049  1.00 59.96      A    C  
ANISOU 2065  C   GLU A1063     5499  13193   4091    -81    159    376  A    C  
ATOM   2066  O   GLU A1063      -0.419 -23.652  -0.021  1.00 60.38      A    O  
ANISOU 2066  O   GLU A1063     5565  13204   4172   -105    184    383  A    O  
ATOM   2067  CB  GLU A1063       1.802 -24.499  -2.151  1.00 58.41      A    C  
ANISOU 2067  CB  GLU A1063     5262  12994   3938   -119    130    340  A    C  
ATOM   2068  CG  GLU A1063       0.745 -23.974  -3.103  1.00 66.25      A    C  
ANISOU 2068  CG  GLU A1063     6269  13926   4977   -158    151    361  A    C  
ATOM   2069  CD  GLU A1063       0.893 -24.410  -4.548  1.00 84.93      A    C  
ANISOU 2069  CD  GLU A1063     8613  16289   7368   -173    143    361  A    C  
ATOM   2070  OE1 GLU A1063       2.019 -24.787  -4.951  1.00 85.46      A    O  
ANISOU 2070  OE1 GLU A1063     8648  16405   7417   -172    123    327  A    O  
ATOM   2071  OE2 GLU A1063      -0.121 -24.362  -5.283  1.00 74.57      A    O1-
ANISOU 2071  OE2 GLU A1063     7306  14942   6086   -184    155    385  A    O1-
ATOM   2072  N   LYS A1064       0.822 -25.360   0.832  1.00 54.83      A    N  
ANISOU 2072  N   LYS A1064     4862  12566   3405    -27    150    418  A    N  
ATOM   2073  CA  LYS A1064      -0.201 -25.939   1.718  1.00 53.76      A    C  
ANISOU 2073  CA  LYS A1064     4760  12412   3256     -7    179    480  A    C  
ATOM   2074  C   LYS A1064      -0.540 -24.972   2.849  1.00 58.43      A    C  
ANISOU 2074  C   LYS A1064     5343  13061   3795    -13    196    452  A    C  
ATOM   2075  O   LYS A1064      -1.707 -24.841   3.221  1.00 57.44      A    O  
ANISOU 2075  O   LYS A1064     5229  12919   3677    -29    231    472  A    O  
ATOM   2076  CB  LYS A1064       0.250 -27.304   2.269  1.00 54.88      A    C  
ANISOU 2076  CB  LYS A1064     4928  12556   3366     55    167    544  A    C  
ATOM   2077  CG  LYS A1064      -0.895 -28.177   2.754  1.00 56.90      A    C  
ANISOU 2077  CG  LYS A1064     5230  12759   3631     52    209    627  A    C  
ATOM   2078  CD  LYS A1064      -0.392 -29.494   3.323  1.00 67.99      A    C  
ANISOU 2078  CD  LYS A1064     6680  14152   5003    120    198    707  A    C  
ATOM   2079  CE  LYS A1064      -1.263 -30.047   4.430  1.00 71.92      A    C  
ANISOU 2079  CE  LYS A1064     7225  14636   5466    114    247    799  A    C  
ATOM   2080  NZ  LYS A1064      -1.901 -31.335   4.049  1.00 80.50      A    N1+
ANISOU 2080  NZ  LYS A1064     8362  15596   6629     93    281    866  A    N1+
ATOM   2081  N   LEU A1065       0.482 -24.269   3.357  1.00 56.71      A    N  
ANISOU 2081  N   LEU A1065     5098  12923   3528     -5    171    390  A    N  
ATOM   2082  CA  LEU A1065       0.385 -23.258   4.408  1.00 57.80      A    C  
ANISOU 2082  CA  LEU A1065     5216  13129   3615    -12    181    331  A    C  
ATOM   2083  C   LEU A1065      -0.317 -22.005   3.853  1.00 61.86      A    C  
ANISOU 2083  C   LEU A1065     5730  13578   4196    -66    204    278  A    C  
ATOM   2084  O   LEU A1065      -1.217 -21.465   4.513  1.00 60.19      A    O  
ANISOU 2084  O   LEU A1065     5518  13375   3975    -66    230    257  A    O  
ATOM   2085  CB  LEU A1065       1.802 -22.929   4.872  1.00 58.83      A    C  
ANISOU 2085  CB  LEU A1065     5306  13362   3685      3    146    261  A    C  
ATOM   2086  CG  LEU A1065       1.976 -22.186   6.170  1.00 65.69      A    C  
ANISOU 2086  CG  LEU A1065     6144  14339   4478      9    147    189  A    C  
ATOM   2087  CD1 LEU A1065       1.555 -23.054   7.382  1.00 67.28      A    C  
ANISOU 2087  CD1 LEU A1065     6358  14620   4584     75    152    261  A    C  
ATOM   2088  CD2 LEU A1065       3.422 -21.755   6.323  1.00 68.35      A    C  
ANISOU 2088  CD2 LEU A1065     6424  14773   4775      2    112     93  A    C  
ATOM   2089  N   PHE A1066       0.051 -21.596   2.602  1.00 58.70      A    N  
ANISOU 2089  N   PHE A1066     5331  13112   3860   -104    195    263  A    N  
ATOM   2090  CA  PHE A1066      -0.541 -20.455   1.894  1.00 58.80      A    C  
ANISOU 2090  CA  PHE A1066     5356  13046   3938   -144    212    235  A    C  
ATOM   2091  C   PHE A1066      -2.048 -20.647   1.672  1.00 63.66      A    C  
ANISOU 2091  C   PHE A1066     5988  13610   4588   -127    235    282  A    C  
ATOM   2092  O   PHE A1066      -2.810 -19.693   1.876  1.00 64.89      A    O  
ANISOU 2092  O   PHE A1066     6149  13737   4769   -126    251    248  A    O  
ATOM   2093  CB  PHE A1066       0.184 -20.207   0.565  1.00 60.58      A    C  
ANISOU 2093  CB  PHE A1066     5583  13230   4206   -186    199    235  A    C  
ATOM   2094  CG  PHE A1066      -0.398 -19.128  -0.319  1.00 61.97      A    C  
ANISOU 2094  CG  PHE A1066     5785  13315   4444   -219    214    234  A    C  
ATOM   2095  CD1 PHE A1066      -0.201 -17.783  -0.026  1.00 65.59      A    C  
ANISOU 2095  CD1 PHE A1066     6257  13739   4926   -253    227    172  A    C  
ATOM   2096  CD2 PHE A1066      -1.108 -19.456  -1.466  1.00 63.99      A    C  
ANISOU 2096  CD2 PHE A1066     6055  13522   4737   -213    214    294  A    C  
ATOM   2097  CE1 PHE A1066      -0.718 -16.787  -0.856  1.00 67.01      A    C  
ANISOU 2097  CE1 PHE A1066     6476  13817   5169   -272    240    187  A    C  
ATOM   2098  CE2 PHE A1066      -1.643 -18.458  -2.289  1.00 67.30      A    C  
ANISOU 2098  CE2 PHE A1066     6503  13866   5203   -227    223    308  A    C  
ATOM   2099  CZ  PHE A1066      -1.440 -17.130  -1.983  1.00 66.12      A    C  
ANISOU 2099  CZ  PHE A1066     6378  13664   5079   -252    235    262  A    C  
ATOM   2100  N   ASN A1067      -2.477 -21.883   1.283  1.00 58.44      A    N  
ANISOU 2100  N   ASN A1067     5331  12940   3931   -112    237    349  A    N  
ATOM   2101  CA  ASN A1067      -3.890 -22.249   1.068  1.00 56.94      A    C  
ANISOU 2101  CA  ASN A1067     5143  12722   3771   -107    262    384  A    C  
ATOM   2102  C   ASN A1067      -4.694 -22.184   2.363  1.00 60.61      A    C  
ANISOU 2102  C   ASN A1067     5600  13236   4193    -90    291    376  A    C  
ATOM   2103  O   ASN A1067      -5.885 -21.937   2.303  1.00 60.25      A    O  
ANISOU 2103  O   ASN A1067     5540  13182   4170    -89    314    371  A    O  
ATOM   2104  CB  ASN A1067      -4.016 -23.639   0.457  1.00 54.70      A    C  
ANISOU 2104  CB  ASN A1067     4863  12418   3504   -110    262    440  A    C  
ATOM   2105  CG  ASN A1067      -3.679 -23.771  -1.012  1.00 68.00      A    C  
ANISOU 2105  CG  ASN A1067     6540  14064   5232   -126    240    440  A    C  
ATOM   2107  ND2 ASN A1067      -3.500 -25.014  -1.420  1.00 61.23      A    N  
ANISOU 2107  ND2 ASN A1067     5683  13194   4387   -125    236    468  A    N  
ATOM   2106  OD1 ASN A1067      -3.593 -22.799  -1.794  1.00 53.12      A    O  
ANISOU 2106  OD1 ASN A1067     4652  12161   3368   -139    230    418  A    O  
ATOM   2108  N   GLN A1068      -4.054 -22.407   3.529  1.00 58.11      A    N  
ANISOU 2108  N   GLN A1068     5283  12989   3806    -75    290    372  A    N  
ATOM   2109  CA  GLN A1068      -4.713 -22.286   4.831  1.00 58.64      A    C  
ANISOU 2109  CA  GLN A1068     5338  13131   3814    -61    320    359  A    C  
ATOM   2110  C   GLN A1068      -4.878 -20.803   5.176  1.00 64.30      A    C  
ANISOU 2110  C   GLN A1068     6034  13859   4539    -58    321    261  A    C  
ATOM   2111  O   GLN A1068      -5.890 -20.435   5.770  1.00 64.78      A    O  
ANISOU 2111  O   GLN A1068     6073  13955   4586    -48    350    231  A    O  
ATOM   2112  CB  GLN A1068      -3.922 -23.005   5.936  1.00 60.39      A    C  
ANISOU 2112  CB  GLN A1068     5565  13437   3941    -36    313    393  A    C  
ATOM   2113  CG  GLN A1068      -4.033 -24.534   5.906  1.00 67.84      A    C  
ANISOU 2113  CG  GLN A1068     6542  14358   4874    -28    325    501  A    C  
ATOM   2114  CD  GLN A1068      -2.814 -25.235   6.470  1.00 81.66      A    C  
ANISOU 2114  CD  GLN A1068     8310  16168   6550     18    296    542  A    C  
ATOM   2116  NE2 GLN A1068      -2.937 -26.526   6.726  1.00 68.15      A    N  
ANISOU 2116  NE2 GLN A1068     6641  14417   4837     36    303    641  A    N  
ATOM   2115  OE1 GLN A1068      -1.744 -24.646   6.662  1.00 80.05      A    O  
ANISOU 2115  OE1 GLN A1068     8080  16046   6291     42    266    482  A    O  
ATOM   2117  N   ASP A1069      -3.890 -19.956   4.792  1.00 62.02      A    N  
ANISOU 2117  N   ASP A1069     5749  13538   4278    -71    294    204  A    N  
ATOM   2118  CA  ASP A1069      -3.902 -18.503   5.013  1.00 62.61      A    C  
ANISOU 2118  CA  ASP A1069     5816  13590   4382    -77    296    105  A    C  
ATOM   2119  C   ASP A1069      -5.001 -17.797   4.205  1.00 65.30      A    C  
ANISOU 2119  C   ASP A1069     6169  13836   4805    -66    306    101  A    C  
ATOM   2120  O   ASP A1069      -5.700 -16.955   4.770  1.00 65.78      A    O  
ANISOU 2120  O   ASP A1069     6216  13900   4877    -42    321     34  A    O  
ATOM   2121  CB  ASP A1069      -2.526 -17.872   4.716  1.00 65.25      A    C  
ANISOU 2121  CB  ASP A1069     6154  13907   4731   -113    272     52  A    C  
ATOM   2122  CG  ASP A1069      -1.415 -18.090   5.748  1.00 80.10      A    C  
ANISOU 2122  CG  ASP A1069     8002  15907   6524   -113    258      0  A    C  
ATOM   2123  OD1 ASP A1069      -1.738 -18.315   6.945  1.00 81.13      A    O  
ANISOU 2123  OD1 ASP A1069     8108  16138   6577    -80    269    -13  A    O  
ATOM   2124  OD2 ASP A1069      -0.224 -18.008   5.363  1.00 88.08      A    O1-
ANISOU 2124  OD2 ASP A1069     9003  16927   7537   -145    237    -30  A    O1-
ATOM   2125  N   VAL A1070      -5.162 -18.146   2.903  1.00 59.92      A    N  
ANISOU 2125  N   VAL A1070     5508  13084   4174    -75    294    168  A    N  
ATOM   2126  CA  VAL A1070      -6.191 -17.599   1.996  1.00 59.25      A    C  
ANISOU 2126  CA  VAL A1070     5432  12926   4155    -51    295    181  A    C  
ATOM   2127  C   VAL A1070      -7.619 -17.894   2.532  1.00 64.37      A    C  
ANISOU 2127  C   VAL A1070     6043  13626   4788    -14    319    173  A    C  
ATOM   2128  O   VAL A1070      -8.471 -16.999   2.548  1.00 64.91      A    O  
ANISOU 2128  O   VAL A1070     6103  13667   4892     28    322    126  A    O  
ATOM   2129  CB  VAL A1070      -6.001 -18.087   0.530  1.00 61.92      A    C  
ANISOU 2129  CB  VAL A1070     5786  13217   4524    -68    276    254  A    C  
ATOM   2130  CG1 VAL A1070      -7.104 -17.561  -0.374  1.00 61.52      A    C  
ANISOU 2130  CG1 VAL A1070     5735  13118   4521    -30    271    271  A    C  
ATOM   2131  CG2 VAL A1070      -4.635 -17.683  -0.023  1.00 61.53      A    C  
ANISOU 2131  CG2 VAL A1070     5764  13128   4485   -112    259    252  A    C  
ATOM   2132  N   ASP A1071      -7.864 -19.137   2.987  1.00 60.98      A    N  
ANISOU 2132  N   ASP A1071     5593  13270   4308    -29    338    216  A    N  
ATOM   2133  CA  ASP A1071      -9.142 -19.539   3.576  1.00 61.55      A    C  
ANISOU 2133  CA  ASP A1071     5622  13409   4354    -17    373    210  A    C  
ATOM   2134  C   ASP A1071      -9.495 -18.645   4.765  1.00 67.84      A    C  
ANISOU 2134  C   ASP A1071     6393  14264   5119     12    391    123  A    C  
ATOM   2135  O   ASP A1071     -10.626 -18.151   4.826  1.00 68.70      A    O  
ANISOU 2135  O   ASP A1071     6464  14392   5247     48    405     75  A    O  
ATOM   2136  CB  ASP A1071      -9.121 -21.023   3.985  1.00 63.14      A    C  
ANISOU 2136  CB  ASP A1071     5822  13663   4504    -54    399    282  A    C  
ATOM   2137  CG  ASP A1071      -9.020 -21.970   2.811  1.00 72.32      A    C  
ANISOU 2137  CG  ASP A1071     7000  14770   5709    -81    388    347  A    C  
ATOM   2138  OD1 ASP A1071      -8.732 -21.499   1.697  1.00 73.92      A    O  
ANISOU 2138  OD1 ASP A1071     7213  14910   5962    -72    355    342  A    O  
ATOM   2139  OD2 ASP A1071      -9.231 -23.186   3.007  1.00 76.20      A    O1-
ANISOU 2139  OD2 ASP A1071     7493  15278   6181   -112    415    402  A    O1-
ATOM   2140  N   ALA A1072      -8.514 -18.398   5.676  1.00 64.12      A    N  
ANISOU 2140  N   ALA A1072     5932  13832   4598      3    387     88  A    N  
ATOM   2141  CA  ALA A1072      -8.690 -17.529   6.838  1.00 64.58      A    C  
ANISOU 2141  CA  ALA A1072     5961  13958   4620     27    402    -15  A    C  
ATOM   2142  C   ALA A1072      -8.921 -16.062   6.437  1.00 68.64      A    C  
ANISOU 2142  C   ALA A1072     6483  14379   5220     64    386   -106  A    C  
ATOM   2143  O   ALA A1072      -9.695 -15.376   7.096  1.00 69.34      A    O  
ANISOU 2143  O   ALA A1072     6534  14506   5305    104    403   -196  A    O  
ATOM   2144  CB  ALA A1072      -7.501 -17.645   7.768  1.00 65.57      A    C  
ANISOU 2144  CB  ALA A1072     6090  14155   4670      9    394    -36  A    C  
ATOM   2145  N   ALA A1073      -8.289 -15.593   5.346  1.00 64.89      A    N  
ANISOU 2145  N   ALA A1073     6058  13778   4820     54    357    -80  A    N  
ATOM   2146  CA  ALA A1073      -8.481 -14.221   4.856  1.00 65.04      A    C  
ANISOU 2146  CA  ALA A1073     6105  13677   4929     89    344   -140  A    C  
ATOM   2147  C   ALA A1073      -9.933 -14.025   4.391  1.00 69.86      A    C  
ANISOU 2147  C   ALA A1073     6694  14272   5579    157    345   -135  A    C  
ATOM   2148  O   ALA A1073     -10.604 -13.116   4.890  1.00 71.24      A    O  
ANISOU 2148  O   ALA A1073     6850  14435   5783    216    351   -226  A    O  
ATOM   2149  CB  ALA A1073      -7.505 -13.907   3.727  1.00 64.98      A    C  
ANISOU 2149  CB  ALA A1073     6159  13553   4979     50    320    -88  A    C  
ATOM   2150  N   VAL A1074     -10.430 -14.929   3.505  1.00 64.08      A    N  
ANISOU 2150  N   VAL A1074     5951  13556   4841    153    340    -41  A    N  
ATOM   2151  CA  VAL A1074     -11.788 -14.932   2.941  1.00 63.09      A    C  
ANISOU 2151  CA  VAL A1074     5787  13446   4739    213    337    -34  A    C  
ATOM   2152  C   VAL A1074     -12.867 -15.041   4.035  1.00 65.88      A    C  
ANISOU 2152  C   VAL A1074     6064  13922   5047    242    371   -111  A    C  
ATOM   2153  O   VAL A1074     -13.777 -14.211   4.045  1.00 66.42      A    O  
ANISOU 2153  O   VAL A1074     6103  13983   5151    322    365   -179  A    O  
ATOM   2154  CB  VAL A1074     -11.924 -16.002   1.829  1.00 65.65      A    C  
ANISOU 2154  CB  VAL A1074     6107  13782   5057    182    328     65  A    C  
ATOM   2155  CG1 VAL A1074     -13.380 -16.371   1.553  1.00 65.42      A    C  
ANISOU 2155  CG1 VAL A1074     6006  13828   5023    222    336     55  A    C  
ATOM   2156  CG2 VAL A1074     -11.218 -15.546   0.554  1.00 64.86      A    C  
ANISOU 2156  CG2 VAL A1074     6069  13569   5007    181    292    125  A    C  
ATOM   2157  N   ARG A1075     -12.741 -16.010   4.977  1.00 61.48      A    N  
ANISOU 2157  N   ARG A1075     5476  13476   4406    184    407   -101  A    N  
ATOM   2158  CA  ARG A1075     -13.671 -16.165   6.113  1.00 61.36      A    C  
ANISOU 2158  CA  ARG A1075     5386  13599   4327    194    450   -167  A    C  
ATOM   2159  C   ARG A1075     -13.770 -14.873   6.930  1.00 66.70      A    C  
ANISOU 2159  C   ARG A1075     6047  14281   5017    255    448   -299  A    C  
ATOM   2160  O   ARG A1075     -14.859 -14.527   7.361  1.00 68.17      A    O  
ANISOU 2160  O   ARG A1075     6163  14545   5192    306    468   -380  A    O  
ATOM   2161  CB  ARG A1075     -13.280 -17.339   7.023  1.00 59.39      A    C  
ANISOU 2161  CB  ARG A1075     5131  13456   3980    118    488   -112  A    C  
ATOM   2162  CG  ARG A1075     -13.669 -18.702   6.469  1.00 65.50      A    C  
ANISOU 2162  CG  ARG A1075     5897  14249   4741     62    510    -10  A    C  
ATOM   2163  CD  ARG A1075     -13.060 -19.825   7.294  1.00 75.04      A    C  
ANISOU 2163  CD  ARG A1075     7126  15522   5864     -4    544     66  A    C  
ATOM   2164  NE  ARG A1075     -13.359 -21.143   6.728  1.00 83.22      A    N  
ANISOU 2164  NE  ARG A1075     8169  16542   6908    -63    567    162  A    N  
ATOM   2165  CZ  ARG A1075     -14.146 -22.051   7.300  1.00 97.19      A    C  
ANISOU 2165  CZ  ARG A1075     9907  18397   8623   -119    628    199  A    C  
ATOM   2166  NH1 ARG A1075     -14.706 -21.807   8.478  1.00 86.97      A    N1+
ANISOU 2166  NH1 ARG A1075     8567  17230   7246   -121    672    156  A    N1+
ATOM   2167  NH2 ARG A1075     -14.375 -23.212   6.701  1.00 81.36      A    N  
ANISOU 2167  NH2 ARG A1075     7915  16353   6646   -180    650    275  A    N  
ATOM   2168  N   GLY A1076     -12.653 -14.152   7.078  1.00 63.24      A    N  
ANISOU 2168  N   GLY A1076     5664  13757   4606    248    426   -332  A    N  
ATOM   2169  CA  GLY A1076     -12.593 -12.864   7.768  1.00 64.29      A    C  
ANISOU 2169  CA  GLY A1076     5793  13864   4772    297    424   -470  A    C  
ATOM   2170  C   GLY A1076     -13.399 -11.765   7.092  1.00 69.82      A    C  
ANISOU 2170  C   GLY A1076     6501  14452   5576    393    400   -523  A    C  
ATOM   2171  O   GLY A1076     -14.155 -11.049   7.761  1.00 70.82      A    O  
ANISOU 2171  O   GLY A1076     6578  14619   5712    462    411   -646  A    O  
ATOM   2172  N   ILE A1077     -13.248 -11.646   5.748  1.00 65.86      A    N  
ANISOU 2172  N   ILE A1077     6061  13816   5146    406    367   -428  A    N  
ATOM   2173  CA  ILE A1077     -13.948 -10.721   4.847  1.00 66.09      A    C  
ANISOU 2173  CA  ILE A1077     6115  13727   5269    507    335   -434  A    C  
ATOM   2174  C   ILE A1077     -15.465 -10.965   4.935  1.00 71.73      A    C  
ANISOU 2174  C   ILE A1077     6733  14563   5957    585    342   -473  A    C  
ATOM   2175  O   ILE A1077     -16.227  -9.995   5.006  1.00 73.64      A    O  
ANISOU 2175  O   ILE A1077     6957  14771   6253    695    328   -564  A    O  
ATOM   2176  CB  ILE A1077     -13.417 -10.868   3.385  1.00 68.27      A    C  
ANISOU 2176  CB  ILE A1077     6468  13882   5589    486    303   -297  A    C  
ATOM   2177  CG1 ILE A1077     -11.930 -10.438   3.258  1.00 67.89      A    C  
ANISOU 2177  CG1 ILE A1077     6508  13708   5578    411    300   -279  A    C  
ATOM   2178  CG2 ILE A1077     -14.301 -10.122   2.366  1.00 70.06      A    C  
ANISOU 2178  CG2 ILE A1077     6712  14022   5886    603    267   -273  A    C  
ATOM   2179  CD1 ILE A1077     -11.167 -11.141   2.178  1.00 67.05      A    C  
ANISOU 2179  CD1 ILE A1077     6447  13568   5460    340    287   -149  A    C  
ATOM   2180  N   LEU A1078     -15.902 -12.255   4.946  1.00 66.88      A    N  
ANISOU 2180  N   LEU A1078     6056  14091   5263    528    366   -415  A    N  
ATOM   2181  CA  LEU A1078     -17.328 -12.631   5.063  1.00 66.55      A    C  
ANISOU 2181  CA  LEU A1078     5907  14192   5186    574    383   -459  A    C  
ATOM   2182  C   LEU A1078     -17.919 -12.209   6.414  1.00 70.28      A    C  
ANISOU 2182  C   LEU A1078     6303  14782   5617    607    419   -602  A    C  
ATOM   2183  O   LEU A1078     -19.100 -11.861   6.489  1.00 71.77      A    O  
ANISOU 2183  O   LEU A1078     6410  15045   5814    696    419   -688  A    O  
ATOM   2184  CB  LEU A1078     -17.550 -14.148   4.884  1.00 65.46      A    C  
ANISOU 2184  CB  LEU A1078     5726  14168   4977    475    415   -371  A    C  
ATOM   2185  CG  LEU A1078     -17.134 -14.816   3.571  1.00 68.09      A    C  
ANISOU 2185  CG  LEU A1078     6108  14426   5336    434    388   -246  A    C  
ATOM   2186  CD1 LEU A1078     -17.610 -16.266   3.535  1.00 66.94      A    C  
ANISOU 2186  CD1 LEU A1078     5906  14397   5133    343    428   -196  A    C  
ATOM   2187  CD2 LEU A1078     -17.631 -14.043   2.354  1.00 70.55      A    C  
ANISOU 2187  CD2 LEU A1078     6430  14661   5716    539    334   -236  A    C  
ATOM   2188  N   ARG A1079     -17.098 -12.246   7.474  1.00 64.61      A    N  
ANISOU 2188  N   ARG A1079     5602  14098   4848    541    447   -635  A    N  
ATOM   2189  CA  ARG A1079     -17.521 -11.873   8.818  1.00 64.64      A    C  
ANISOU 2189  CA  ARG A1079     5532  14233   4796    563    483   -775  A    C  
ATOM   2190  C   ARG A1079     -17.256 -10.369   9.132  1.00 69.94      A    C  
ANISOU 2190  C   ARG A1079     6236  14789   5551    650    456   -911  A    C  
ATOM   2191  O   ARG A1079     -17.378  -9.956  10.282  1.00 71.01      A    O  
ANISOU 2191  O   ARG A1079     6316  15022   5644    665    483  -1046  A    O  
ATOM   2192  CB  ARG A1079     -16.923 -12.837   9.860  1.00 61.00      A    C  
ANISOU 2192  CB  ARG A1079     5056  13908   4212    451    530   -740  A    C  
ATOM   2193  CG  ARG A1079     -17.650 -14.183   9.851  1.00 64.96      A    C  
ANISOU 2193  CG  ARG A1079     5498  14551   4632    383    575   -655  A    C  
ATOM   2194  CD  ARG A1079     -16.904 -15.311  10.527  1.00 76.78      A    C  
ANISOU 2194  CD  ARG A1079     7023  16123   6027    273    611   -555  A    C  
ATOM   2195  NE  ARG A1079     -17.157 -16.588   9.849  1.00 88.65      A    N  
ANISOU 2195  NE  ARG A1079     8534  17630   7519    200    631   -420  A    N  
ATOM   2196  CZ  ARG A1079     -16.573 -17.745  10.157  1.00 96.66      A    C  
ANISOU 2196  CZ  ARG A1079     9588  18674   8466    110    659   -304  A    C  
ATOM   2197  NH1 ARG A1079     -16.865 -18.846   9.472  1.00 80.14      A    N1+
ANISOU 2197  NH1 ARG A1079     7503  16562   6384     47    678   -199  A    N1+
ATOM   2198  NH2 ARG A1079     -15.686 -17.810  11.147  1.00 74.32      A    N  
ANISOU 2198  NH2 ARG A1079     6788  15892   5557     88    666   -296  A    N  
ATOM   2199  N   ASN A1080     -16.982  -9.546   8.094  1.00 66.20      A    N  
ANISOU 2199  N   ASN A1080     5848  14108   5195    710    408   -878  A    N  
ATOM   2200  CA  ASN A1080     -16.797  -8.095   8.212  1.00 66.73      A    C  
ANISOU 2200  CA  ASN A1080     5965  14021   5369    795    384   -993  A    C  
ATOM   2201  C   ASN A1080     -17.950  -7.402   7.476  1.00 71.50      A    C  
ANISOU 2201  C   ASN A1080     6552  14562   6054    946    349  -1020  A    C  
ATOM   2202  O   ASN A1080     -18.141  -7.637   6.282  1.00 69.93      A    O  
ANISOU 2202  O   ASN A1080     6388  14298   5884    972    318   -895  A    O  
ATOM   2203  CB  ASN A1080     -15.449  -7.662   7.642  1.00 65.99      A    C  
ANISOU 2203  CB  ASN A1080     5997  13728   5348    736    363   -925  A    C  
ATOM   2204  CG  ASN A1080     -14.988  -6.323   8.161  1.00 80.78      A    C  
ANISOU 2204  CG  ASN A1080     7914  15473   7307    766    363  -1069  A    C  
ATOM   2206  ND2 ASN A1080     -14.045  -6.343   9.084  1.00 68.75      A    N  
ANISOU 2206  ND2 ASN A1080     6383  14007   5733    671    388  -1137  A    N  
ATOM   2205  OD1 ASN A1080     -15.466  -5.263   7.748  1.00 76.57      A    O  
ANISOU 2205  OD1 ASN A1080     7419  14788   6886    875    340  -1126  A    O  
ATOM   2207  N   ALA A1081     -18.739  -6.583   8.204  1.00 70.73      A    N  
ANISOU 2207  N   ALA A1081     6391  14501   5982   1054    354  -1190  A    N  
ATOM   2208  CA  ALA A1081     -19.934  -5.876   7.708  1.00 72.18      A    C  
ANISOU 2208  CA  ALA A1081     6537  14652   6234   1225    318  -1248  A    C  
ATOM   2209  C   ALA A1081     -19.706  -4.998   6.477  1.00 78.79      A    C  
ANISOU 2209  C   ALA A1081     7501  15232   7203   1317    262  -1162  A    C  
ATOM   2210  O   ALA A1081     -20.606  -4.905   5.628  1.00 79.56      A    O  
ANISOU 2210  O   ALA A1081     7577  15327   7324   1436    222  -1116  A    O  
ATOM   2211  CB  ALA A1081     -20.567  -5.057   8.821  1.00 74.19      A    C  
ANISOU 2211  CB  ALA A1081     6710  14978   6501   1318    335  -1466  A    C  
ATOM   2212  N   LYS A1082     -18.512  -4.361   6.384  1.00 75.57      A    N  
ANISOU 2212  N   LYS A1082     7221  14618   6874   1260    260  -1139  A    N  
ATOM   2213  CA  LYS A1082     -18.123  -3.466   5.287  1.00 75.88      A    C  
ANISOU 2213  CA  LYS A1082     7400  14391   7038   1323    219  -1046  A    C  
ATOM   2214  C   LYS A1082     -17.557  -4.208   4.087  1.00 78.50      A    C  
ANISOU 2214  C   LYS A1082     7799  14687   7340   1239    203   -836  A    C  
ATOM   2215  O   LYS A1082     -17.856  -3.843   2.948  1.00 79.69      A    O  
ANISOU 2215  O   LYS A1082     8016  14718   7545   1329    161   -728  A    O  
ATOM   2216  CB  LYS A1082     -17.092  -2.432   5.769  1.00 79.25      A    C  
ANISOU 2216  CB  LYS A1082     7929  14615   7567   1280    236  -1132  A    C  
ATOM   2217  CG  LYS A1082     -17.682  -1.211   6.452  1.00 94.16      A    C  
ANISOU 2217  CG  LYS A1082     9798  16430   9547   1414    233  -1332  A    C  
ATOM   2218  CD  LYS A1082     -16.573  -0.274   6.897  1.00103.47      A    C  
ANISOU 2218  CD  LYS A1082    11080  17401  10834   1345    256  -1420  A    C  
ATOM   2219  CE  LYS A1082     -17.102   1.022   7.451  1.00116.90      A    C  
ANISOU 2219  CE  LYS A1082    12785  18975  12656   1488    250  -1616  A    C  
ATOM   2220  NZ  LYS A1082     -16.041   1.780   8.163  1.00127.17      A    N1+
ANISOU 2220  NZ  LYS A1082    14151  20124  14043   1390    285  -1749  A    N1+
ATOM   2221  N   LEU A1083     -16.721  -5.227   4.339  1.00 72.35      A    N  
ANISOU 2221  N   LEU A1083     7004  14013   6473   1075    235   -780  A    N  
ATOM   2222  CA  LEU A1083     -16.043  -5.982   3.292  1.00 70.23      A    C  
ANISOU 2222  CA  LEU A1083     6792  13719   6173    983    225   -601  A    C  
ATOM   2223  C   LEU A1083     -16.928  -7.009   2.568  1.00 74.19      A    C  
ANISOU 2223  C   LEU A1083     7217  14370   6600   1010    207   -510  A    C  
ATOM   2224  O   LEU A1083     -16.704  -7.234   1.371  1.00 74.15      A    O  
ANISOU 2224  O   LEU A1083     7267  14304   6602   1004    180   -372  A    O  
ATOM   2225  CB  LEU A1083     -14.755  -6.639   3.827  1.00 68.64      A    C  
ANISOU 2225  CB  LEU A1083     6604  13560   5914    812    261   -586  A    C  
ATOM   2226  CG  LEU A1083     -13.665  -5.705   4.386  1.00 73.06      A    C  
ANISOU 2226  CG  LEU A1083     7241  13975   6543    751    279   -665  A    C  
ATOM   2227  CD1 LEU A1083     -12.463  -6.495   4.844  1.00 71.92      A    C  
ANISOU 2227  CD1 LEU A1083     7087  13920   6320    597    306   -647  A    C  
ATOM   2228  CD2 LEU A1083     -13.229  -4.657   3.368  1.00 75.08      A    C  
ANISOU 2228  CD2 LEU A1083     7630  13982   6916    774    259   -588  A    C  
ATOM   2229  N   LYS A1084     -17.926  -7.611   3.259  1.00 70.43      A    N  
ANISOU 2229  N   LYS A1084     6611  14097   6052   1032    227   -593  A    N  
ATOM   2230  CA  LYS A1084     -18.817  -8.617   2.666  1.00 70.20      A    C  
ANISOU 2230  CA  LYS A1084     6493  14227   5954   1039    219   -533  A    C  
ATOM   2231  C   LYS A1084     -19.536  -8.126   1.364  1.00 77.80      A    C  
ANISOU 2231  C   LYS A1084     7471  15128   6961   1178    160   -466  A    C  
ATOM   2232  O   LYS A1084     -19.337  -8.788   0.335  1.00 77.35      A    O  
ANISOU 2232  O   LYS A1084     7434  15080   6877   1132    143   -341  A    O  
ATOM   2233  CB  LYS A1084     -19.823  -9.196   3.689  1.00 71.77      A    C  
ANISOU 2233  CB  LYS A1084     6548  14648   6075   1038    259   -649  A    C  
ATOM   2234  CG  LYS A1084     -20.349 -10.590   3.319  1.00 71.88      A    C  
ANISOU 2234  CG  LYS A1084     6475  14831   6004    961    279   -584  A    C  
ATOM   2235  CD  LYS A1084     -21.673 -10.537   2.566  1.00 76.10      A    C  
ANISOU 2235  CD  LYS A1084     6910  15467   6537   1080    250   -620  A    C  
ATOM   2236  CE  LYS A1084     -22.167 -11.887   2.095  1.00 77.47      A    C  
ANISOU 2236  CE  LYS A1084     7012  15777   6648    996    263   -551  A    C  
ATOM   2237  NZ  LYS A1084     -23.599 -11.835   1.648  1.00 73.49      A    N1+
ANISOU 2237  NZ  LYS A1084     6376  15419   6126   1104    242   -623  A    N1+
ATOM   2238  N   PRO A1085     -20.326  -7.004   1.345  1.00 75.95      A    N  
ANISOU 2238  N   PRO A1085     7231  14835   6792   1351    125   -542  A    N  
ATOM   2239  CA  PRO A1085     -20.993  -6.591   0.084  1.00 75.81      A    C  
ANISOU 2239  CA  PRO A1085     7229  14776   6801   1495     62   -462  A    C  
ATOM   2240  C   PRO A1085     -20.070  -6.237  -1.093  1.00 78.58      A    C  
ANISOU 2240  C   PRO A1085     7728  14931   7197   1481     31   -297  A    C  
ATOM   2241  O   PRO A1085     -20.498  -6.351  -2.244  1.00 77.56      A    O  
ANISOU 2241  O   PRO A1085     7600  14823   7047   1557    -16   -198  A    O  
ATOM   2242  CB  PRO A1085     -21.848  -5.393   0.504  1.00 79.47      A    C  
ANISOU 2242  CB  PRO A1085     7666  15197   7332   1688     33   -588  A    C  
ATOM   2243  CG  PRO A1085     -21.216  -4.884   1.750  1.00 84.74      A    C  
ANISOU 2243  CG  PRO A1085     8368  15785   8045   1633     77   -707  A    C  
ATOM   2244  CD  PRO A1085     -20.685  -6.091   2.454  1.00 78.73      A    C  
ANISOU 2244  CD  PRO A1085     7555  15169   7191   1436    137   -709  A    C  
ATOM   2245  N   VAL A1086     -18.810  -5.830  -0.808  1.00 75.69      A    N  
ANISOU 2245  N   VAL A1086     7481  14395   6883   1380     59   -273  A    N  
ATOM   2246  CA  VAL A1086     -17.779  -5.480  -1.809  1.00 75.16      A    C  
ANISOU 2246  CA  VAL A1086     7558  14145   6856   1333     46   -123  A    C  
ATOM   2247  C   VAL A1086     -17.203  -6.754  -2.451  1.00 75.47      A    C  
ANISOU 2247  C   VAL A1086     7574  14295   6806   1194     56    -12  A    C  
ATOM   2248  O   VAL A1086     -17.051  -6.786  -3.671  1.00 74.89      A    O  
ANISOU 2248  O   VAL A1086     7550  14185   6719   1215     24    120  A    O  
ATOM   2249  CB  VAL A1086     -16.653  -4.549  -1.267  1.00 79.74      A    C  
ANISOU 2249  CB  VAL A1086     8257  14517   7526   1260     79   -157  A    C  
ATOM   2250  CG1 VAL A1086     -15.866  -3.917  -2.408  1.00 79.92      A    C  
ANISOU 2250  CG1 VAL A1086     8428  14339   7599   1233     67     -2  A    C  
ATOM   2251  CG2 VAL A1086     -17.208  -3.458  -0.360  1.00 81.48      A    C  
ANISOU 2251  CG2 VAL A1086     8480  14645   7836   1382     78   -307  A    C  
ATOM   2252  N   TYR A1087     -16.906  -7.802  -1.637  1.00 69.35      A    N  
ANISOU 2252  N   TYR A1087     6724  13657   5968   1061     99    -66  A    N  
ATOM   2253  CA  TYR A1087     -16.394  -9.102  -2.107  1.00 67.12      A    C  
ANISOU 2253  CA  TYR A1087     6413  13481   5609    932    112     15  A    C  
ATOM   2254  C   TYR A1087     -17.403  -9.777  -3.056  1.00 73.39      A    C  
ANISOU 2254  C   TYR A1087     7123  14414   6348    995     79     60  A    C  
ATOM   2255  O   TYR A1087     -16.996 -10.373  -4.056  1.00 72.52      A    O  
ANISOU 2255  O   TYR A1087     7030  14323   6202    941     66    162  A    O  
ATOM   2256  CB  TYR A1087     -16.073 -10.022  -0.909  1.00 66.16      A    C  
ANISOU 2256  CB  TYR A1087     6227  13475   5435    811    163    -61  A    C  
ATOM   2257  CG  TYR A1087     -15.377 -11.325  -1.261  1.00 64.17      A    C  
ANISOU 2257  CG  TYR A1087     5963  13299   5120    677    181     17  A    C  
ATOM   2258  CD1 TYR A1087     -14.009 -11.363  -1.522  1.00 64.70      A    C  
ANISOU 2258  CD1 TYR A1087     6114  13274   5196    579    188     81  A    C  
ATOM   2259  CD2 TYR A1087     -16.078 -12.527  -1.286  1.00 63.92      A    C  
ANISOU 2259  CD2 TYR A1087     5832  13429   5024    646    193     13  A    C  
ATOM   2260  CE1 TYR A1087     -13.363 -12.561  -1.833  1.00 62.77      A    C  
ANISOU 2260  CE1 TYR A1087     5855  13097   4898    472    201    140  A    C  
ATOM   2261  CE2 TYR A1087     -15.442 -13.732  -1.587  1.00 63.28      A    C  
ANISOU 2261  CE2 TYR A1087     5748  13397   4900    530    210     76  A    C  
ATOM   2262  CZ  TYR A1087     -14.085 -13.745  -1.861  1.00 68.85      A    C  
ANISOU 2262  CZ  TYR A1087     6537  14009   5614    452    210    139  A    C  
ATOM   2263  OH  TYR A1087     -13.471 -14.936  -2.173  1.00 69.15      A    O  
ANISOU 2263  OH  TYR A1087     6567  14095   5613    355    223    192  A    O  
ATOM   2264  N   ASP A1088     -18.718  -9.629  -2.757  1.00 71.80      A    N  
ANISOU 2264  N   ASP A1088     6822  14320   6138   1110     65    -29  A    N  
ATOM   2265  CA  ASP A1088     -19.846 -10.154  -3.526  1.00 72.60      A    C  
ANISOU 2265  CA  ASP A1088     6817  14580   6187   1183     33    -25  A    C  
ATOM   2266  C   ASP A1088     -19.976  -9.543  -4.926  1.00 80.20      A    C  
ANISOU 2266  C   ASP A1088     7836  15477   7159   1300    -31     85  A    C  
ATOM   2267  O   ASP A1088     -20.401 -10.243  -5.852  1.00 80.85      A    O  
ANISOU 2267  O   ASP A1088     7852  15688   7181   1305    -56    128  A    O  
ATOM   2268  CB  ASP A1088     -21.155  -9.922  -2.756  1.00 75.68      A    C  
ANISOU 2268  CB  ASP A1088     7088  15094   6575   1290     35   -165  A    C  
ATOM   2269  CG  ASP A1088     -21.442 -10.902  -1.636  1.00 86.43      A    C  
ANISOU 2269  CG  ASP A1088     8342  16616   7883   1175     98   -263  A    C  
ATOM   2270  OD1 ASP A1088     -20.559 -11.737  -1.325  1.00 86.37      A    O  
ANISOU 2270  OD1 ASP A1088     8370  16594   7852   1019    142   -226  A    O  
ATOM   2271  OD2 ASP A1088     -22.548 -10.843  -1.077  1.00 92.51      A    O1-
ANISOU 2271  OD2 ASP A1088     8989  17530   8630   1243    105   -374  A    O1-
ATOM   2272  N   SER A1089     -19.658  -8.239  -5.076  1.00 78.18      A    N  
ANISOU 2272  N   SER A1089     7702  15026   6977   1396    -56    128  A    N  
ATOM   2273  CA  SER A1089     -19.759  -7.513  -6.348  1.00 78.93      A    C  
ANISOU 2273  CA  SER A1089     7874  15034   7080   1520   -115    253  A    C  
ATOM   2274  C   SER A1089     -18.547  -7.702  -7.265  1.00 82.78      A    C  
ANISOU 2274  C   SER A1089     8471  15430   7551   1406   -107    402  A    C  
ATOM   2275  O   SER A1089     -18.709  -7.716  -8.487  1.00 83.13      A    O  
ANISOU 2275  O   SER A1089     8531  15505   7549   1467   -151    513  A    O  
ATOM   2276  CB  SER A1089     -20.004  -6.028  -6.098  1.00 84.00      A    C  
ANISOU 2276  CB  SER A1089     8606  15493   7819   1680   -140    236  A    C  
ATOM   2277  OG  SER A1089     -18.875  -5.412  -5.502  1.00 93.70      A    O  
ANISOU 2277  OG  SER A1089     9961  16513   9127   1585    -97    240  A    O  
ATOM   2278  N   LEU A1090     -17.338  -7.817  -6.680  1.00 78.90      A    N  
ANISOU 2278  N   LEU A1090     8048  14841   7090   1247    -54    400  A    N  
ATOM   2279  CA  LEU A1090     -16.072  -7.978  -7.406  1.00 78.04      A    C  
ANISOU 2279  CA  LEU A1090     8034  14651   6968   1124    -39    521  A    C  
ATOM   2280  C   LEU A1090     -15.954  -9.332  -8.110  1.00 80.54      A    C  
ANISOU 2280  C   LEU A1090     8270  15142   7189   1033    -40    560  A    C  
ATOM   2281  O   LEU A1090     -16.462 -10.338  -7.605  1.00 79.72      A    O  
ANISOU 2281  O   LEU A1090     8050  15192   7047    992    -26    473  A    O  
ATOM   2282  CB  LEU A1090     -14.866  -7.791  -6.455  1.00 77.37      A    C  
ANISOU 2282  CB  LEU A1090     8017  14443   6936    983     17    477  A    C  
ATOM   2283  CG  LEU A1090     -14.622  -6.412  -5.826  1.00 83.38      A    C  
ANISOU 2283  CG  LEU A1090     8881  14996   7805   1030     30    436  A    C  
ATOM   2284  CD1 LEU A1090     -13.526  -6.488  -4.790  1.00 83.26      A    C  
ANISOU 2284  CD1 LEU A1090     8887  14929   7818    879     84    358  A    C  
ATOM   2285  CD2 LEU A1090     -14.244  -5.368  -6.858  1.00 87.04      A    C  
ANISOU 2285  CD2 LEU A1090     9484  15272   8314   1081     12    574  A    C  
ATOM   2286  N   ASP A1091     -15.257  -9.352  -9.264  1.00 76.46      A    N  
ANISOU 2286  N   ASP A1091     7817  14598   6637    994    -52    687  A    N  
ATOM   2287  CA  ASP A1091     -14.978 -10.563 -10.057  1.00 74.85      A    C  
ANISOU 2287  CA  ASP A1091     7547  14545   6349    904    -53    720  A    C  
ATOM   2288  C   ASP A1091     -13.781 -11.333  -9.461  1.00 76.37      A    C  
ANISOU 2288  C   ASP A1091     7747  14724   6545    726      0    688  A    C  
ATOM   2289  O   ASP A1091     -13.162 -10.833  -8.515  1.00 76.10      A    O  
ANISOU 2289  O   ASP A1091     7773  14571   6571    677     33    650  A    O  
ATOM   2290  CB  ASP A1091     -14.765 -10.232 -11.547  1.00 77.11      A    C  
ANISOU 2290  CB  ASP A1091     7880  14840   6576    950    -90    861  A    C  
ATOM   2291  CG  ASP A1091     -13.755  -9.135 -11.803  1.00 87.58      A    C  
ANISOU 2291  CG  ASP A1091     9360  15981   7937    920    -74    981  A    C  
ATOM   2292  OD1 ASP A1091     -14.134  -7.952 -11.744  1.00 87.03      A    O  
ANISOU 2292  OD1 ASP A1091     9367  15752   7950    870    -38    949  A    O  
ATOM   2293  OD2 ASP A1091     -12.585  -9.456 -12.060  1.00 97.03      A    O1-
ANISOU 2293  OD2 ASP A1091    10596  17199   9072    938    -96   1105  A    O1-
ATOM   2294  N   ALA A1092     -13.466 -12.543  -9.990  1.00 69.99      A    N  
ANISOU 2294  N   ALA A1092     6876  14044   5676    638      5    692  A    N  
ATOM   2295  CA  ALA A1092     -12.401 -13.400  -9.455  1.00 67.86      A    C  
ANISOU 2295  CA  ALA A1092     6601  13777   5404    492     47    659  A    C  
ATOM   2296  C   ALA A1092     -11.004 -12.742  -9.398  1.00 71.83      A    C  
ANISOU 2296  C   ALA A1092     7211  14145   5937    409     73    708  A    C  
ATOM   2297  O   ALA A1092     -10.337 -12.881  -8.372  1.00 70.42      A    O  
ANISOU 2297  O   ALA A1092     7041  13931   5786    331    106    648  A    O  
ATOM   2298  CB  ALA A1092     -12.347 -14.720 -10.196  1.00 67.57      A    C  
ANISOU 2298  CB  ALA A1092     6488  13882   5305    433     42    659  A    C  
ATOM   2299  N   VAL A1093     -10.585 -11.999 -10.462  1.00 69.22      A    N  
ANISOU 2299  N   VAL A1093     6958  13746   5596    425     60    815  A    N  
ATOM   2300  CA  VAL A1093      -9.286 -11.289 -10.528  1.00 68.29      A    C  
ANISOU 2300  CA  VAL A1093     6941  13501   5507    334     92    865  A    C  
ATOM   2301  C   VAL A1093      -9.234 -10.167  -9.477  1.00 73.10      A    C  
ANISOU 2301  C   VAL A1093     7622  13947   6208    351    113    818  A    C  
ATOM   2302  O   VAL A1093      -8.289 -10.113  -8.686  1.00 72.45      A    O  
ANISOU 2302  O   VAL A1093     7559  13814   6156    249    150    762  A    O  
ATOM   2303  CB  VAL A1093      -8.950 -10.789 -11.965  1.00 71.67      A    C  
ANISOU 2303  CB  VAL A1093     7432  13911   5889    339     80   1004  A    C  
ATOM   2304  CG1 VAL A1093      -7.901  -9.677 -11.960  1.00 71.95      A    C  
ANISOU 2304  CG1 VAL A1093     7588  13776   5972    261    120   1062  A    C  
ATOM   2305  CG2 VAL A1093      -8.498 -11.942 -12.846  1.00 70.42      A    C  
ANISOU 2305  CG2 VAL A1093     7202  13914   5641    273     75   1020  A    C  
ATOM   2306  N   ARG A1094     -10.270  -9.302  -9.455  1.00 70.58      A    N  
ANISOU 2306  N   ARG A1094     7331  13555   5929    487     88    827  A    N  
ATOM   2307  CA  ARG A1094     -10.396  -8.186  -8.516  1.00 70.99      A    C  
ANISOU 2307  CA  ARG A1094     7447  13447   6077    523    104    767  A    C  
ATOM   2308  C   ARG A1094     -10.468  -8.632  -7.054  1.00 73.75      A    C  
ANISOU 2308  C   ARG A1094     7724  13853   6445    491    125    618  A    C  
ATOM   2309  O   ARG A1094     -10.017  -7.885  -6.180  1.00 74.53      A    O  
ANISOU 2309  O   ARG A1094     7869  13838   6612    458    153    547  A    O  
ATOM   2310  CB  ARG A1094     -11.593  -7.299  -8.873  1.00 72.41      A    C  
ANISOU 2310  CB  ARG A1094     7666  13551   6294    699     64    806  A    C  
ATOM   2311  CG  ARG A1094     -11.332  -6.385 -10.055  1.00 79.88      A    C  
ANISOU 2311  CG  ARG A1094     8740  14357   7254    729     57    960  A    C  
ATOM   2312  CD  ARG A1094     -12.416  -5.337 -10.185  1.00 84.14      A    C  
ANISOU 2312  CD  ARG A1094     9322  14813   7836    926     12    996  A    C  
ATOM   2313  NE  ARG A1094     -12.103  -4.358 -11.225  1.00 90.11      A    N  
ANISOU 2313  NE  ARG A1094    10219  15410   8607    962      8   1163  A    N  
ATOM   2314  CZ  ARG A1094     -12.451  -4.480 -12.503  1.00 99.10      A    C  
ANISOU 2314  CZ  ARG A1094    11365  16631   9658   1035    -31   1305  A    C  
ATOM   2315  NH1 ARG A1094     -13.132  -5.543 -12.915  1.00 83.16      A    N1+
ANISOU 2315  NH1 ARG A1094     9212  14850   7535   1077    -72   1282  A    N1+
ATOM   2316  NH2 ARG A1094     -12.120  -3.541 -13.379  1.00 82.69      A    N  
ANISOU 2316  NH2 ARG A1094     9429  14400   7591   1062    -28   1469  A    N  
ATOM   2317  N   ARG A1095     -11.015  -9.845  -6.783  1.00 67.86      A    N  
ANISOU 2317  N   ARG A1095     6865  13282   5638    493    116    569  A    N  
ATOM   2318  CA  ARG A1095     -11.106 -10.376  -5.412  1.00 65.82      A    C  
ANISOU 2318  CA  ARG A1095     6536  13094   5377    457    140    448  A    C  
ATOM   2319  C   ARG A1095      -9.724 -10.723  -4.887  1.00 65.56      A    C  
ANISOU 2319  C   ARG A1095     6523  13051   5337    317    175    425  A    C  
ATOM   2320  O   ARG A1095      -9.414 -10.407  -3.739  1.00 64.79      A    O  
ANISOU 2320  O   ARG A1095     6426  12924   5266    289    199    334  A    O  
ATOM   2321  CB  ARG A1095     -12.100 -11.546  -5.294  1.00 64.43      A    C  
ANISOU 2321  CB  ARG A1095     6245  13093   5142    485    129    416  A    C  
ATOM   2322  CG  ARG A1095     -13.540 -11.110  -5.535  1.00 68.68      A    C  
ANISOU 2322  CG  ARG A1095     6740  13666   5689    631     97    396  A    C  
ATOM   2323  CD  ARG A1095     -14.581 -12.103  -5.088  1.00 77.50      A    C  
ANISOU 2323  CD  ARG A1095     7733  14954   6760    642    102    326  A    C  
ATOM   2324  NE  ARG A1095     -14.477 -13.412  -5.729  1.00 90.74      A    N  
ANISOU 2324  NE  ARG A1095     9356  16743   8378    569    102    365  A    N  
ATOM   2325  CZ  ARG A1095     -15.513 -14.219  -5.941  1.00113.26      A    C  
ANISOU 2325  CZ  ARG A1095    12104  19738  11192    589     98    330  A    C  
ATOM   2326  NH1 ARG A1095     -15.333 -15.397  -6.522  1.00110.03      A    N1+
ANISOU 2326  NH1 ARG A1095    11652  19411  10742    514    101    355  A    N1+
ATOM   2327  NH2 ARG A1095     -16.741 -13.846  -5.588  1.00 93.39      A    N  
ANISOU 2327  NH2 ARG A1095     9518  17286   8681    682     91    257  A    N  
ATOM   2328  N   ALA A1096      -8.865 -11.272  -5.763  1.00 60.47      A    N  
ANISOU 2328  N   ALA A1096     5890  12433   4652    238    175    501  A    N  
ATOM   2329  CA  ALA A1096      -7.462 -11.582  -5.471  1.00 59.55      A    C  
ANISOU 2329  CA  ALA A1096     5787  12317   4522    112    202    485  A    C  
ATOM   2330  C   ALA A1096      -6.689 -10.300  -5.089  1.00 64.54      A    C  
ANISOU 2330  C   ALA A1096     6501  12800   5221     68    228    457  A    C  
ATOM   2331  O   ALA A1096      -5.820 -10.367  -4.224  1.00 63.14      A    O  
ANISOU 2331  O   ALA A1096     6311  12635   5044    -12    251    381  A    O  
ATOM   2332  CB  ALA A1096      -6.813 -12.256  -6.670  1.00 59.62      A    C  
ANISOU 2332  CB  ALA A1096     5793  12381   4480     55    195    570  A    C  
ATOM   2333  N   ALA A1097      -7.047  -9.133  -5.695  1.00 63.10      A    N  
ANISOU 2333  N   ALA A1097     6401  12478   5097    124    223    512  A    N  
ATOM   2334  CA  ALA A1097      -6.453  -7.821  -5.399  1.00 64.16      A    C  
ANISOU 2334  CA  ALA A1097     6627  12436   5314     84    252    486  A    C  
ATOM   2335  C   ALA A1097      -6.882  -7.261  -4.028  1.00 68.98      A    C  
ANISOU 2335  C   ALA A1097     7222  13002   5983    129    261    348  A    C  
ATOM   2336  O   ALA A1097      -6.102  -6.552  -3.396  1.00 68.87      A    O  
ANISOU 2336  O   ALA A1097     7246  12899   6024     54    293    270  A    O  
ATOM   2337  CB  ALA A1097      -6.770  -6.827  -6.504  1.00 66.12      A    C  
ANISOU 2337  CB  ALA A1097     6979  12538   5606    140    244    607  A    C  
ATOM   2338  N   LEU A1098      -8.106  -7.581  -3.568  1.00 66.44      A    N  
ANISOU 2338  N   LEU A1098     6838  12758   5646    244    236    305  A    N  
ATOM   2339  CA  LEU A1098      -8.599  -7.146  -2.252  1.00 67.32      A    C  
ANISOU 2339  CA  LEU A1098     6917  12865   5796    293    245    165  A    C  
ATOM   2340  C   LEU A1098      -8.006  -8.024  -1.134  1.00 70.97      A    C  
ANISOU 2340  C   LEU A1098     7298  13473   6195    207    265     71  A    C  
ATOM   2341  O   LEU A1098      -7.681  -7.509  -0.061  1.00 70.90      A    O  
ANISOU 2341  O   LEU A1098     7282  13442   6213    182    287    -50  A    O  
ATOM   2342  CB  LEU A1098     -10.140  -7.140  -2.213  1.00 67.75      A    C  
ANISOU 2342  CB  LEU A1098     6924  12967   5850    446    214    151  A    C  
ATOM   2343  CG  LEU A1098     -10.839  -6.488  -1.001  1.00 72.84      A    C  
ANISOU 2343  CG  LEU A1098     7541  13592   6544    525    221      4  A    C  
ATOM   2344  CD1 LEU A1098     -10.714  -4.963  -1.022  1.00 74.27      A    C  
ANISOU 2344  CD1 LEU A1098     7830  13545   6846    571    225    -22  A    C  
ATOM   2345  CD2 LEU A1098     -12.309  -6.847  -0.993  1.00 75.47      A    C  
ANISOU 2345  CD2 LEU A1098     7789  14042   6843    655    193    -14  A    C  
ATOM   2346  N   ILE A1099      -7.840  -9.344  -1.402  1.00 66.94      A    N  
ANISOU 2346  N   ILE A1099     6729  13107   5598    164    258    127  A    N  
ATOM   2347  CA  ILE A1099      -7.216 -10.312  -0.481  1.00 65.65      A    C  
ANISOU 2347  CA  ILE A1099     6500  13080   5364     92    273     72  A    C  
ATOM   2348  C   ILE A1099      -5.764  -9.852  -0.250  1.00 70.96      A    C  
ANISOU 2348  C   ILE A1099     7209  13700   6054    -17    293     33  A    C  
ATOM   2349  O   ILE A1099      -5.299  -9.836   0.897  1.00 72.26      A    O  
ANISOU 2349  O   ILE A1099     7336  13924   6195    -53    308    -71  A    O  
ATOM   2350  CB  ILE A1099      -7.293 -11.776  -1.027  1.00 66.80      A    C  
ANISOU 2350  CB  ILE A1099     6595  13353   5434     75    260    153  A    C  
ATOM   2351  CG1 ILE A1099      -8.752 -12.260  -1.178  1.00 66.00      A    C  
ANISOU 2351  CG1 ILE A1099     6442  13318   5317    166    246    171  A    C  
ATOM   2352  CG2 ILE A1099      -6.484 -12.760  -0.164  1.00 66.16      A    C  
ANISOU 2352  CG2 ILE A1099     6464  13389   5285      8    272    117  A    C  
ATOM   2353  CD1 ILE A1099      -8.932 -13.328  -2.260  1.00 64.42      A    C  
ANISOU 2353  CD1 ILE A1099     6216  13185   5076    158    229    263  A    C  
ATOM   2354  N   ASN A1100      -5.085  -9.419  -1.338  1.00 66.70      A    N  
ANISOU 2354  N   ASN A1100     6736  13059   5549    -69    296    110  A    N  
ATOM   2355  CA  ASN A1100      -3.715  -8.879  -1.340  1.00 66.88      A    C  
ANISOU 2355  CA  ASN A1100     6793  13024   5596   -186    323     76  A    C  
ATOM   2356  C   ASN A1100      -3.568  -7.691  -0.348  1.00 72.52      A    C  
ANISOU 2356  C   ASN A1100     7532  13638   6383   -201    347    -56  A    C  
ATOM   2357  O   ASN A1100      -2.580  -7.636   0.392  1.00 72.14      A    O  
ANISOU 2357  O   ASN A1100     7451  13639   6319   -286    366   -156  A    O  
ATOM   2358  CB  ASN A1100      -3.328  -8.456  -2.761  1.00 65.45      A    C  
ANISOU 2358  CB  ASN A1100     6687  12740   5443   -229    329    196  A    C  
ATOM   2359  CG  ASN A1100      -1.876  -8.120  -2.962  1.00 86.74      A    C  
ANISOU 2359  CG  ASN A1100     9405  15402   8149   -370    363    174  A    C  
ATOM   2361  ND2 ASN A1100      -1.226  -8.873  -3.825  1.00 82.09      A    N  
ANISOU 2361  ND2 ASN A1100     8788  14908   7496   -430    360    240  A    N  
ATOM   2360  OD1 ASN A1100      -1.331  -7.173  -2.383  1.00 80.74      A    O  
ANISOU 2360  OD1 ASN A1100     8684  14536   7457   -430    394     90  A    O  
ATOM   2362  N   MET A1101      -4.563  -6.764  -0.329  1.00 69.95      A    N  
ANISOU 2362  N   MET A1101     7259  13182   6138   -109    345    -68  A    N  
ATOM   2363  CA  MET A1101      -4.608  -5.607   0.575  1.00 70.78      A    C  
ANISOU 2363  CA  MET A1101     7390  13174   6328   -102    366   -206  A    C  
ATOM   2364  C   MET A1101      -4.756  -6.053   2.045  1.00 74.19      A    C  
ANISOU 2364  C   MET A1101     7723  13765   6701    -85    366   -352  A    C  
ATOM   2365  O   MET A1101      -4.212  -5.396   2.932  1.00 73.68      A    O  
ANISOU 2365  O   MET A1101     7650  13674   6670   -136    389   -495  A    O  
ATOM   2366  CB  MET A1101      -5.765  -4.670   0.203  1.00 73.96      A    C  
ANISOU 2366  CB  MET A1101     7862  13418   6821     26    353   -177  A    C  
ATOM   2367  CG  MET A1101      -5.489  -3.780  -0.990  1.00 77.86      A    C  
ANISOU 2367  CG  MET A1101     8482  13700   7401      4    366    -64  A    C  
ATOM   2368  SD  MET A1101      -6.823  -2.569  -1.224  1.00 82.80      A    S  
ANISOU 2368  SD  MET A1101     9194  14125   8141    180    345    -50  A    S  
ATOM   2369  CE  MET A1101      -6.304  -1.310  -0.094  1.00 81.00      A    C  
ANISOU 2369  CE  MET A1101     9004  13736   8036    127    388   -247  A    C  
ATOM   2370  N   VAL A1102      -5.492  -7.166   2.289  1.00 70.45      A    N  
ANISOU 2370  N   VAL A1102     7174  13458   6136    -20    343   -318  A    N  
ATOM   2371  CA  VAL A1102      -5.723  -7.749   3.620  1.00 70.40      A    C  
ANISOU 2371  CA  VAL A1102     7076  13625   6050     -1    346   -422  A    C  
ATOM   2372  C   VAL A1102      -4.405  -8.316   4.196  1.00 76.08      A    C  
ANISOU 2372  C   VAL A1102     7751  14462   6695   -107    354   -466  A    C  
ATOM   2373  O   VAL A1102      -4.098  -8.080   5.369  1.00 76.92      A    O  
ANISOU 2373  O   VAL A1102     7810  14645   6773   -125    366   -602  A    O  
ATOM   2374  CB  VAL A1102      -6.908  -8.766   3.600  1.00 72.76      A    C  
ANISOU 2374  CB  VAL A1102     7318  14049   6280     84    329   -355  A    C  
ATOM   2375  CG1 VAL A1102      -6.854  -9.758   4.756  1.00 71.64      A    C  
ANISOU 2375  CG1 VAL A1102     7088  14106   6025     69    338   -405  A    C  
ATOM   2376  CG2 VAL A1102      -8.254  -8.041   3.572  1.00 73.29      A    C  
ANISOU 2376  CG2 VAL A1102     7392  14046   6409    203    322   -384  A    C  
ATOM   2377  N   PHE A1103      -3.613  -9.019   3.358  1.00 72.24      A    N  
ANISOU 2377  N   PHE A1103     7275  13997   6174   -170    346   -361  A    N  
ATOM   2378  CA  PHE A1103      -2.311  -9.585   3.733  1.00 71.75      A    C  
ANISOU 2378  CA  PHE A1103     7169  14049   6042   -257    347   -393  A    C  
ATOM   2379  C   PHE A1103      -1.330  -8.478   4.178  1.00 77.35      A    C  
ANISOU 2379  C   PHE A1103     7889  14694   6805   -346    371   -527  A    C  
ATOM   2380  O   PHE A1103      -0.560  -8.690   5.122  1.00 77.64      A    O  
ANISOU 2380  O   PHE A1103     7860  14864   6777   -388    371   -629  A    O  
ATOM   2381  CB  PHE A1103      -1.719 -10.391   2.554  1.00 72.53      A    C  
ANISOU 2381  CB  PHE A1103     7284  14158   6117   -299    335   -261  A    C  
ATOM   2382  CG  PHE A1103      -2.088 -11.861   2.504  1.00 72.76      A    C  
ANISOU 2382  CG  PHE A1103     7268  14319   6059   -252    312   -174  A    C  
ATOM   2383  CD1 PHE A1103      -3.401 -12.262   2.266  1.00 74.92      A    C  
ANISOU 2383  CD1 PHE A1103     7543  14589   6333   -170    304   -108  A    C  
ATOM   2384  CD2 PHE A1103      -1.114 -12.845   2.647  1.00 74.02      A    C  
ANISOU 2384  CD2 PHE A1103     7383  14599   6140   -289    299   -162  A    C  
ATOM   2385  CE1 PHE A1103      -3.740 -13.622   2.219  1.00 74.64      A    C  
ANISOU 2385  CE1 PHE A1103     7471  14660   6230   -143    292    -35  A    C  
ATOM   2386  CE2 PHE A1103      -1.452 -14.206   2.592  1.00 75.77      A    C  
ANISOU 2386  CE2 PHE A1103     7577  14915   6297   -245    282    -80  A    C  
ATOM   2387  CZ  PHE A1103      -2.764 -14.584   2.379  1.00 73.35      A    C  
ANISOU 2387  CZ  PHE A1103     7278  14592   6000   -181    283    -18  A    C  
ATOM   2388  N   GLN A1104      -1.401  -7.288   3.520  1.00 73.76      A    N  
ANISOU 2388  N   GLN A1104     7518  14037   6470   -372    393   -529  A    N  
ATOM   2389  CA  GLN A1104      -0.559  -6.111   3.779  1.00 74.00      A    C  
ANISOU 2389  CA  GLN A1104     7577  13959   6581   -471    427   -652  A    C  
ATOM   2390  C   GLN A1104      -0.960  -5.260   5.009  1.00 77.09      A    C  
ANISOU 2390  C   GLN A1104     7945  14331   7015   -440    440   -833  A    C  
ATOM   2391  O   GLN A1104      -0.073  -4.779   5.714  1.00 75.84      A    O  
ANISOU 2391  O   GLN A1104     7748  14208   6860   -528    460   -983  A    O  
ATOM   2392  CB  GLN A1104      -0.495  -5.216   2.523  1.00 75.72      A    C  
ANISOU 2392  CB  GLN A1104     7909  13949   6912   -515    451   -558  A    C  
ATOM   2393  CG  GLN A1104       0.596  -4.123   2.545  1.00 87.56      A    C  
ANISOU 2393  CG  GLN A1104     9445  15326   8496   -660    498   -659  A    C  
ATOM   2394  CD  GLN A1104       0.426  -3.031   1.502  1.00106.91      A    C  
ANISOU 2394  CD  GLN A1104    12032  17512  11078   -687    531   -574  A    C  
ATOM   2396  NE2 GLN A1104       1.234  -1.985   1.609  1.00 99.45      A    N  
ANISOU 2396  NE2 GLN A1104    11130  16429  10229   -813    581   -676  A    N  
ATOM   2395  OE1 GLN A1104      -0.417  -3.099   0.594  1.00102.48      A    O  
ANISOU 2395  OE1 GLN A1104    11538  16866  10533   -598    513   -417  A    O  
ATOM   2397  N   MET A1105      -2.265  -5.012   5.227  1.00 75.00      A    N  
ANISOU 2397  N   MET A1105     7698  14013   6786   -319    430   -835  A    N  
ATOM   2398  CA  MET A1105      -2.680  -4.109   6.307  1.00 76.56      A    C  
ANISOU 2398  CA  MET A1105     7876  14180   7035   -283    444  -1019  A    C  
ATOM   2399  C   MET A1105      -3.876  -4.579   7.183  1.00 80.40      A    C  
ANISOU 2399  C   MET A1105     8289  14812   7449   -157    426  -1062  A    C  
ATOM   2400  O   MET A1105      -4.401  -3.766   7.952  1.00 81.84      A    O  
ANISOU 2400  O   MET A1105     8455  14961   7680   -109    437  -1214  A    O  
ATOM   2401  CB  MET A1105      -2.944  -2.689   5.743  1.00 80.47      A    C  
ANISOU 2401  CB  MET A1105     8483  14389   7701   -278    468  -1041  A    C  
ATOM   2402  CG  MET A1105      -4.008  -2.618   4.662  1.00 83.95      A    C  
ANISOU 2402  CG  MET A1105     9005  14698   8195   -165    448   -876  A    C  
ATOM   2403  SD  MET A1105      -3.772  -1.229   3.525  1.00 89.96      A    S  
ANISOU 2403  SD  MET A1105     9931  15118   9133   -202    477   -808  A    S  
ATOM   2404  CE  MET A1105      -4.494   0.082   4.475  1.00 88.71      A    C  
ANISOU 2404  CE  MET A1105     9791  14810   9103   -120    491  -1015  A    C  
ATOM   2405  N   GLY A1106      -4.250  -5.862   7.106  1.00 75.03      A    N  
ANISOU 2405  N   GLY A1106     7561  14293   6654   -114    403   -943  A    N  
ATOM   2406  CA  GLY A1106      -5.340  -6.434   7.903  1.00 74.50      A    C  
ANISOU 2406  CA  GLY A1106     7420  14381   6504    -17    395   -968  A    C  
ATOM   2407  C   GLY A1106      -6.735  -5.961   7.536  1.00 78.65      A    C  
ANISOU 2407  C   GLY A1106     7973  14808   7103    102    390   -953  A    C  
ATOM   2408  O   GLY A1106      -6.885  -4.973   6.815  1.00 79.52      A    O  
ANISOU 2408  O   GLY A1106     8167  14707   7342    125    390   -946  A    O  
ATOM   2409  N   GLU A1107      -7.771  -6.662   8.031  1.00 74.89      A    N  
ANISOU 2409  N   GLU A1107     7424  14486   6544    179    386   -946  A    N  
ATOM   2410  CA  GLU A1107      -9.187  -6.349   7.752  1.00 75.77      A    C  
ANISOU 2410  CA  GLU A1107     7532  14555   6703    301    378   -944  A    C  
ATOM   2411  C   GLU A1107      -9.666  -4.977   8.265  1.00 81.82      A    C  
ANISOU 2411  C   GLU A1107     8308  15207   7573    373    386  -1114  A    C  
ATOM   2412  O   GLU A1107     -10.473  -4.319   7.599  1.00 81.98      A    O  
ANISOU 2412  O   GLU A1107     8373  15088   7688    473    371  -1093  A    O  
ATOM   2413  CB  GLU A1107     -10.109  -7.454   8.277  1.00 76.55      A    C  
ANISOU 2413  CB  GLU A1107     7535  14871   6678    341    384   -917  A    C  
ATOM   2414  CG  GLU A1107     -10.240  -8.632   7.331  1.00 86.70      A    C  
ANISOU 2414  CG  GLU A1107     8830  16193   7920    326    371   -732  A    C  
ATOM   2415  CD  GLU A1107     -10.435  -9.969   8.018  1.00115.78      A    C  
ANISOU 2415  CD  GLU A1107    12438  20089  11464    291    388   -687  A    C  
ATOM   2416  OE1 GLU A1107      -9.788 -10.950   7.587  1.00118.68      A    O  
ANISOU 2416  OE1 GLU A1107    12826  20480  11788    228    381   -565  A    O  
ATOM   2417  OE2 GLU A1107     -11.226 -10.039   8.987  1.00113.32      A    O1-
ANISOU 2417  OE2 GLU A1107    12050  19918  11087    326    411   -773  A    O1-
ATOM   2418  N   THR A1108      -9.164  -4.557   9.439  1.00 79.11      A    N  
ANISOU 2418  N   THR A1108     7920  14927   7210    330    407  -1289  A    N  
ATOM   2419  CA  THR A1108      -9.506  -3.287  10.092  1.00 80.56      A    C  
ANISOU 2419  CA  THR A1108     8104  15013   7493    388    418  -1486  A    C  
ATOM   2420  C   THR A1108      -8.983  -2.070   9.307  1.00 84.86      A    C  
ANISOU 2420  C   THR A1108     8774  15257   8211    365    419  -1489  A    C  
ATOM   2421  O   THR A1108      -9.574  -0.991   9.388  1.00 86.08      A    O  
ANISOU 2421  O   THR A1108     8967  15253   8489    452    420  -1594  A    O  
ATOM   2422  CB  THR A1108      -9.020  -3.289  11.555  1.00 88.25      A    C  
ANISOU 2422  CB  THR A1108     8980  16176   8376    340    440  -1677  A    C  
ATOM   2424  CG2 THR A1108      -9.901  -2.450  12.464  1.00 86.89      A    C  
ANISOU 2424  CG2 THR A1108     8757  16004   8253    436    451  -1890  A    C  
ATOM   2423  OG1 THR A1108      -8.954  -4.630  12.046  1.00 87.65      A    O  
ANISOU 2423  OG1 THR A1108     8817  16365   8121    317    442  -1605  A    O  
ATOM   2425  N   GLY A1109      -7.884  -2.262   8.579  1.00 80.52      A    N  
ANISOU 2425  N   GLY A1109     8289  14635   7670    250    422  -1375  A    N  
ATOM   2426  CA  GLY A1109      -7.246  -1.234   7.765  1.00 81.35      A    C  
ANISOU 2426  CA  GLY A1109     8519  14467   7924    195    434  -1347  A    C  
ATOM   2427  C   GLY A1109      -7.927  -1.001   6.431  1.00 85.48      A    C  
ANISOU 2427  C   GLY A1109     9142  14809   8528    287    412  -1172  A    C  
ATOM   2428  O   GLY A1109      -8.088   0.153   6.024  1.00 86.38      A    O  
ANISOU 2428  O   GLY A1109     9355  14679   8789    333    418  -1197  A    O  
ATOM   2429  N   VAL A1110      -8.319  -2.106   5.736  1.00 80.70      A    N  
ANISOU 2429  N   VAL A1110     8513  14324   7827    315    386   -997  A    N  
ATOM   2430  CA  VAL A1110      -8.999  -2.106   4.422  1.00 80.30      A    C  
ANISOU 2430  CA  VAL A1110     8533  14163   7815    405    357   -819  A    C  
ATOM   2431  C   VAL A1110     -10.408  -1.489   4.550  1.00 84.68      A    C  
ANISOU 2431  C   VAL A1110     9077  14668   8428    586    335   -879  A    C  
ATOM   2432  O   VAL A1110     -10.865  -0.784   3.644  1.00 84.82      A    O  
ANISOU 2432  O   VAL A1110     9187  14501   8539    679    314   -793  A    O  
ATOM   2433  CB  VAL A1110      -9.021  -3.519   3.758  1.00 82.07      A    C  
ANISOU 2433  CB  VAL A1110     8711  14558   7913    379    338   -652  A    C  
ATOM   2434  CG1 VAL A1110      -9.637  -3.473   2.361  1.00 81.51      A    C  
ANISOU 2434  CG1 VAL A1110     8710  14385   7875    460    307   -478  A    C  
ATOM   2435  CG2 VAL A1110      -7.620  -4.125   3.692  1.00 80.94      A    C  
ANISOU 2435  CG2 VAL A1110     8566  14479   7710    218    356   -614  A    C  
ATOM   2436  N   ALA A1111     -11.057  -1.711   5.706  1.00 80.93      A    N  
ANISOU 2436  N   ALA A1111     8490  14364   7897    638    339  -1032  A    N  
ATOM   2437  CA  ALA A1111     -12.377  -1.173   6.019  1.00 81.78      A    C  
ANISOU 2437  CA  ALA A1111     8558  14467   8048    808    321  -1128  A    C  
ATOM   2438  C   ALA A1111     -12.368   0.360   6.283  1.00 87.32      A    C  
ANISOU 2438  C   ALA A1111     9343  14919   8916    870    329  -1265  A    C  
ATOM   2439  O   ALA A1111     -13.433   0.960   6.439  1.00 88.62      A    O  
ANISOU 2439  O   ALA A1111     9495  15035   9142   1032    308  -1339  A    O  
ATOM   2440  CB  ALA A1111     -12.970  -1.924   7.201  1.00 82.05      A    C  
ANISOU 2440  CB  ALA A1111     8441  14777   7957    821    334  -1253  A    C  
ATOM   2441  N   GLY A1112     -11.181   0.971   6.279  1.00 83.51      A    N  
ANISOU 2441  N   GLY A1112     8943  14278   8510    741    359  -1299  A    N  
ATOM   2442  CA  GLY A1112     -10.988   2.403   6.483  1.00 85.28      A    C  
ANISOU 2442  CA  GLY A1112     9261  14235   8906    763    377  -1427  A    C  
ATOM   2443  C   GLY A1112     -11.150   3.275   5.249  1.00 90.62      A    C  
ANISOU 2443  C   GLY A1112    10098  14610   9722    841    361  -1280  A    C  
ATOM   2444  O   GLY A1112     -11.199   4.501   5.384  1.00 92.77      A    O  
ANISOU 2444  O   GLY A1112    10456  14639  10152    902    371  -1379  A    O  
ATOM   2445  N   PHE A1113     -11.228   2.664   4.036  1.00 85.58      A    N  
ANISOU 2445  N   PHE A1113     9505  13984   9028    843    337  -1042  A    N  
ATOM   2446  CA  PHE A1113     -11.417   3.379   2.761  1.00 86.38      A    C  
ANISOU 2446  CA  PHE A1113     9758  13833   9231    925    317   -865  A    C  
ATOM   2447  C   PHE A1113     -12.916   3.420   2.382  1.00 89.14      A    C  
ANISOU 2447  C   PHE A1113    10075  14220   9572   1161    258   -823  A    C  
ATOM   2448  O   PHE A1113     -13.292   2.989   1.291  1.00 87.52      A    O  
ANISOU 2448  O   PHE A1113     9884  14064   9303   1218    222   -633  A    O  
ATOM   2449  CB  PHE A1113     -10.590   2.732   1.622  1.00 87.19      A    C  
ANISOU 2449  CB  PHE A1113     9920  13945   9266    797    323   -640  A    C  
ATOM   2450  CG  PHE A1113      -9.095   2.641   1.820  1.00 88.91      A    C  
ANISOU 2450  CG  PHE A1113    10157  14146   9478    568    378   -667  A    C  
ATOM   2451  CD1 PHE A1113      -8.281   3.751   1.621  1.00 94.01      A    C  
ANISOU 2451  CD1 PHE A1113    10939  14517  10264    473    422   -676  A    C  
ATOM   2452  CD2 PHE A1113      -8.491   1.431   2.143  1.00 89.36      A    C  
ANISOU 2452  CD2 PHE A1113    10100  14463   9391    447    384   -676  A    C  
ATOM   2453  CE1 PHE A1113      -6.892   3.659   1.784  1.00 94.58      A    C  
ANISOU 2453  CE1 PHE A1113    11013  14597  10326    254    475   -714  A    C  
ATOM   2454  CE2 PHE A1113      -7.103   1.341   2.300  1.00 91.71      A    C  
ANISOU 2454  CE2 PHE A1113    10404  14765   9676    248    428   -706  A    C  
ATOM   2455  CZ  PHE A1113      -6.314   2.455   2.120  1.00 91.39      A    C  
ANISOU 2455  CZ  PHE A1113    10481  14472   9770    150    473   -732  A    C  
ATOM   2456  N   THR A1114     -13.765   3.953   3.284  1.00 86.33      A    N  
ANISOU 2456  N   THR A1114     9667  13854   9279   1299    248  -1014  A    N  
ATOM   2457  CA  THR A1114     -15.231   4.019   3.121  1.00 86.40      A    C  
ANISOU 2457  CA  THR A1114     9619  13928   9281   1532    193  -1023  A    C  
ATOM   2458  C   THR A1114     -15.688   4.590   1.752  1.00 88.99      A    C  
ANISOU 2458  C   THR A1114    10080  14055   9677   1679    146   -818  A    C  
ATOM   2459  O   THR A1114     -16.553   3.989   1.121  1.00 86.86      A    O  
ANISOU 2459  O   THR A1114     9746  13940   9315   1793     98   -713  A    O  
ATOM   2460  CB  THR A1114     -15.896   4.752   4.306  1.00 95.80      A    C  
ANISOU 2460  CB  THR A1114    10746  15104  10551   1650    196  -1284  A    C  
ATOM   2462  CG2 THR A1114     -15.663   4.048   5.635  1.00 91.62      A    C  
ANISOU 2462  CG2 THR A1114    10052  14853   9905   1542    231  -1470  A    C  
ATOM   2461  OG1 THR A1114     -15.410   6.090   4.388  1.00100.50      A    O  
ANISOU 2461  OG1 THR A1114    11484  15371  11329   1641    222  -1359  A    O  
ATOM   2463  N   ASN A1115     -15.095   5.707   1.293  1.00 87.35      A    N  
ANISOU 2463  N   ASN A1115    10053  13514   9621   1667    164   -759  A    N  
ATOM   2464  CA  ASN A1115     -15.434   6.344   0.014  1.00 89.18      A    C  
ANISOU 2464  CA  ASN A1115    10435  13529   9920   1803    125   -549  A    C  
ATOM   2465  C   ASN A1115     -14.919   5.575  -1.211  1.00 92.70      A    C  
ANISOU 2465  C   ASN A1115    10919  14052  10251   1702    119   -294  A    C  
ATOM   2466  O   ASN A1115     -15.542   5.641  -2.271  1.00 92.52      A    O  
ANISOU 2466  O   ASN A1115    10941  14014  10200   1848     67   -119  A    O  
ATOM   2467  CB  ASN A1115     -14.961   7.799  -0.026  1.00 92.82      A    C  
ANISOU 2467  CB  ASN A1115    11089  13593  10586   1809    157   -566  A    C  
ATOM   2468  CG  ASN A1115     -15.741   8.721   0.876  1.00113.77      A    C  
ANISOU 2468  CG  ASN A1115    13729  16125  13374   1982    144   -793  A    C  
ATOM   2470  ND2 ASN A1115     -16.901   9.161   0.412  1.00107.71      A    N  
ANISOU 2470  ND2 ASN A1115    12978  15305  12642   2249     77   -748  A    N  
ATOM   2469  OD1 ASN A1115     -15.313   9.056   1.987  1.00103.97      A    O  
ANISOU 2469  OD1 ASN A1115    12455  14846  12203   1886    192  -1017  A    O  
ATOM   2471  N   SER A1116     -13.779   4.868  -1.072  1.00 88.35      A    N  
ANISOU 2471  N   SER A1116    10344  13593   9630   1460    171   -280  A    N  
ATOM   2472  CA  SER A1116     -13.187   4.062  -2.141  1.00 86.84      A    C  
ANISOU 2472  CA  SER A1116    10172  13496   9326   1344    172    -68  A    C  
ATOM   2473  C   SER A1116     -13.938   2.740  -2.299  1.00 90.22      A    C  
ANISOU 2473  C   SER A1116    10436  14255   9586   1396    128    -38  A    C  
ATOM   2474  O   SER A1116     -14.203   2.317  -3.427  1.00 90.21      A    O  
ANISOU 2474  O   SER A1116    10450  14316   9508   1438     93    146  A    O  
ATOM   2475  CB  SER A1116     -11.711   3.796  -1.861  1.00 88.91      A    C  
ANISOU 2475  CB  SER A1116    10454  13750   9580   1081    241    -90  A    C  
ATOM   2476  OG  SER A1116     -10.928   4.952  -2.107  1.00100.18      A    O  
ANISOU 2476  OG  SER A1116    12055  14862  11149   1006    286    -46  A    O  
ATOM   2477  N   LEU A1117     -14.286   2.100  -1.159  1.00 85.95      A    N  
ANISOU 2477  N   LEU A1117     9739  13929   8988   1387    133   -221  A    N  
ATOM   2478  CA  LEU A1117     -15.006   0.826  -1.044  1.00 83.96      A    C  
ANISOU 2478  CA  LEU A1117     9323  13990   8589   1414    105   -228  A    C  
ATOM   2479  C   LEU A1117     -16.351   0.860  -1.776  1.00 88.50      A    C  
ANISOU 2479  C   LEU A1117     9864  14620   9141   1635     39   -160  A    C  
ATOM   2480  O   LEU A1117     -16.709  -0.123  -2.429  1.00 86.20      A    O  
ANISOU 2480  O   LEU A1117     9494  14525   8733   1638     12    -66  A    O  
ATOM   2481  CB  LEU A1117     -15.187   0.463   0.450  1.00 83.32      A    C  
ANISOU 2481  CB  LEU A1117     9103  14081   8472   1375    133   -447  A    C  
ATOM   2482  CG  LEU A1117     -14.231  -0.578   1.088  1.00 85.64      A    C  
ANISOU 2482  CG  LEU A1117     9320  14559   8660   1170    175   -475  A    C  
ATOM   2483  CD1 LEU A1117     -12.773  -0.362   0.705  1.00 85.34      A    C  
ANISOU 2483  CD1 LEU A1117     9391  14374   8659    994    213   -407  A    C  
ATOM   2484  CD2 LEU A1117     -14.356  -0.574   2.606  1.00 87.62      A    C  
ANISOU 2484  CD2 LEU A1117     9460  14944   8888   1152    203   -691  A    C  
ATOM   2485  N   ARG A1118     -17.061   2.004  -1.702  1.00 88.52      A    N  
ANISOU 2485  N   ARG A1118     9928  14447   9259   1822     10   -212  A    N  
ATOM   2486  CA  ARG A1118     -18.344   2.220  -2.377  1.00 90.73      A    C  
ANISOU 2486  CA  ARG A1118    10182  14763   9529   2062    -61   -159  A    C  
ATOM   2487  C   ARG A1118     -18.150   2.402  -3.898  1.00 96.13      A    C  
ANISOU 2487  C   ARG A1118    10989  15340  10195   2102    -95     94  A    C  
ATOM   2488  O   ARG A1118     -18.941   1.864  -4.673  1.00 95.00      A    O  
ANISOU 2488  O   ARG A1118    10773  15368   9955   2213   -150    180  A    O  
ATOM   2489  CB  ARG A1118     -19.108   3.407  -1.752  1.00 94.90      A    C  
ANISOU 2489  CB  ARG A1118    10738  15127  10192   2259    -82   -305  A    C  
ATOM   2490  CG  ARG A1118     -20.565   3.534  -2.217  1.00111.58      A    C  
ANISOU 2490  CG  ARG A1118    12776  17340  12280   2528   -160   -303  A    C  
ATOM   2491  CD  ARG A1118     -21.484   4.144  -1.169  1.00132.93      A    C  
ANISOU 2491  CD  ARG A1118    15389  20065  15053   2685   -170   -542  A    C  
ATOM   2492  NE  ARG A1118     -21.258   5.580  -0.967  1.00150.15      A    N  
ANISOU 2492  NE  ARG A1118    17727  21904  17419   2785   -167   -593  A    N  
ATOM   2493  CZ  ARG A1118     -21.913   6.328  -0.081  1.00165.68      A    C  
ANISOU 2493  CZ  ARG A1118    19647  23823  19479   2932   -175   -808  A    C  
ATOM   2494  NH1 ARG A1118     -21.640   7.622   0.034  1.00155.39      A    N1+
ANISOU 2494  NH1 ARG A1118    18502  22181  18358   3013   -170   -849  A    N1+
ATOM   2495  NH2 ARG A1118     -22.845   5.790   0.697  1.00149.11      A    N  
ANISOU 2495  NH2 ARG A1118    17343  22016  17295   2994   -184   -989  A    N  
ATOM   2496  N   MET A1119     -17.094   3.144  -4.314  1.00 94.48      A    N  
ANISOU 2496  N   MET A1119    10960  14865  10072   2002    -60    206  A    N  
ATOM   2497  CA  MET A1119     -16.746   3.405  -5.718  1.00 95.40      A    C  
ANISOU 2497  CA  MET A1119    11214  14864  10171   2013    -78    456  A    C  
ATOM   2498  C   MET A1119     -16.433   2.107  -6.446  1.00 96.75      A    C  
ANISOU 2498  C   MET A1119    11299  15285  10178   1886    -80    567  A    C  
ATOM   2499  O   MET A1119     -16.803   1.954  -7.608  1.00 96.35      A    O  
ANISOU 2499  O   MET A1119    11267  15290  10050   1973   -126    737  A    O  
ATOM   2500  CB  MET A1119     -15.551   4.365  -5.817  1.00 99.33      A    C  
ANISOU 2500  CB  MET A1119    11906  15040  10793   1881    -17    524  A    C  
ATOM   2501  CG  MET A1119     -15.921   5.827  -5.653  1.00106.47      A    C  
ANISOU 2501  CG  MET A1119    12950  15629  11873   2042    -25    490  A    C  
ATOM   2502  SD  MET A1119     -14.477   6.862  -5.273  1.00112.49      A    S  
ANISOU 2502  SD  MET A1119    13901  16036  12804   1826     72    469  A    S  
ATOM   2503  CE  MET A1119     -15.266   8.455  -5.107  1.00112.65      A    C  
ANISOU 2503  CE  MET A1119    14045  15724  13032   2067     48    383  A    C  
ATOM   2504  N   LEU A1120     -15.774   1.167  -5.741  1.00 91.53      A    N  
ANISOU 2504  N   LEU A1120    10539  14777   9460   1689    -32    464  A    N  
ATOM   2505  CA  LEU A1120     -15.400  -0.167  -6.216  1.00 89.11      A    C  
ANISOU 2505  CA  LEU A1120    10141  14706   9013   1551    -25    529  A    C  
ATOM   2506  C   LEU A1120     -16.651  -1.038  -6.455  1.00 92.63      A    C  
ANISOU 2506  C   LEU A1120    10428  15418   9349   1681    -82    509  A    C  
ATOM   2507  O   LEU A1120     -16.737  -1.692  -7.497  1.00 91.85      A    O  
ANISOU 2507  O   LEU A1120    10300  15450   9149   1674   -109    635  A    O  
ATOM   2508  CB  LEU A1120     -14.462  -0.821  -5.183  1.00 87.32      A    C  
ANISOU 2508  CB  LEU A1120     9851  14552   8773   1342     37    399  A    C  
ATOM   2509  CG  LEU A1120     -13.079  -1.293  -5.649  1.00 90.37      A    C  
ANISOU 2509  CG  LEU A1120    10281  14942   9113   1128     81    492  A    C  
ATOM   2510  CD1 LEU A1120     -12.340  -0.225  -6.432  1.00 92.04      A    C  
ANISOU 2510  CD1 LEU A1120    10671  14891   9409   1081    107    618  A    C  
ATOM   2511  CD2 LEU A1120     -12.227  -1.689  -4.465  1.00 90.70      A    C  
ANISOU 2511  CD2 LEU A1120    10257  15053   9150    964    132    342  A    C  
ATOM   2512  N   GLN A1121     -17.628  -1.016  -5.510  1.00 88.78      A    N  
ANISOU 2512  N   GLN A1121     9833  15017   8883   1796    -98    340  A    N  
ATOM   2513  CA  GLN A1121     -18.900  -1.753  -5.601  1.00 88.12      A    C  
ANISOU 2513  CA  GLN A1121     9586  15188   8707   1917   -145    289  A    C  
ATOM   2514  C   GLN A1121     -19.770  -1.200  -6.759  1.00 94.75      A    C  
ANISOU 2514  C   GLN A1121    10461  16005   9535   2137   -221    412  A    C  
ATOM   2515  O   GLN A1121     -20.352  -1.975  -7.528  1.00 93.84      A    O  
ANISOU 2515  O   GLN A1121    10246  16098   9309   2179   -261    466  A    O  
ATOM   2516  CB  GLN A1121     -19.658  -1.673  -4.260  1.00 89.32      A    C  
ANISOU 2516  CB  GLN A1121     9625  15422   8893   1979   -133     71  A    C  
ATOM   2517  CG  GLN A1121     -20.847  -2.634  -4.128  1.00 94.64      A    C  
ANISOU 2517  CG  GLN A1121    10103  16394   9462   2043   -158    -13  A    C  
ATOM   2518  CD  GLN A1121     -21.665  -2.436  -2.861  1.00111.12      A    C  
ANISOU 2518  CD  GLN A1121    12076  18568  11576   2118   -144   -224  A    C  
ATOM   2520  NE2 GLN A1121     -22.655  -3.297  -2.654  1.00 98.19      A    N  
ANISOU 2520  NE2 GLN A1121    10263  17199   9846   2142   -151   -307  A    N  
ATOM   2519  OE1 GLN A1121     -21.434  -1.521  -2.057  1.00107.92      A    O  
ANISOU 2519  OE1 GLN A1121    11733  18001  11271   2149   -125   -324  A    O  
ATOM   2521  N   GLN A1122     -19.822   0.146  -6.888  1.00 93.55      A    N  
ANISOU 2521  N   GLN A1122    10453  15593   9497   2274   -241    458  A    N  
ATOM   2522  CA  GLN A1122     -20.567   0.867  -7.920  1.00 95.11      A    C  
ANISOU 2522  CA  GLN A1122    10715  15726   9697   2506   -315    590  A    C  
ATOM   2523  C   GLN A1122     -19.892   0.754  -9.289  1.00 99.62      A    C  
ANISOU 2523  C   GLN A1122    11395  16257  10200   2447   -324    829  A    C  
ATOM   2524  O   GLN A1122     -20.412   1.302 -10.266  1.00101.50      A    O  
ANISOU 2524  O   GLN A1122    11701  16444  10421   2631   -386    972  A    O  
ATOM   2525  CB  GLN A1122     -20.769   2.341  -7.526  1.00 98.80      A    C  
ANISOU 2525  CB  GLN A1122    11313  15902  10323   2671   -327    554  A    C  
ATOM   2526  CG  GLN A1122     -21.802   2.546  -6.422  1.00116.38      A    C  
ANISOU 2526  CG  GLN A1122    13409  18213  12595   2818   -347    325  A    C  
ATOM   2527  CD  GLN A1122     -22.073   4.007  -6.174  1.00141.74      A    C  
ANISOU 2527  CD  GLN A1122    16752  21138  15966   3016   -371    295  A    C  
ATOM   2529  NE2 GLN A1122     -23.106   4.539  -6.810  1.00134.12      A    N  
ANISOU 2529  NE2 GLN A1122    15884  19945  15133   2907   -308    200  A    N  
ATOM   2528  OE1 GLN A1122     -21.367   4.673  -5.412  1.00140.76      A    O  
ANISOU 2528  OE1 GLN A1122    16640  20991  15850   3272   -447    351  A    O  
ATOM   2530  N   LYS A1123     -18.748   0.029  -9.360  1.00 94.23      A    N  
ANISOU 2530  N   LYS A1123    10720  15613   9469   2200   -265    870  A    N  
ATOM   2531  CA  LYS A1123     -17.944  -0.239 -10.561  1.00 93.73      A    C  
ANISOU 2531  CA  LYS A1123    10738  15549   9327   2097   -258   1071  A    C  
ATOM   2532  C   LYS A1123     -17.403   1.051 -11.224  1.00100.05      A    C  
ANISOU 2532  C   LYS A1123    11760  16042  10210   2138   -249   1249  A    C  
ATOM   2533  O   LYS A1123     -17.353   1.159 -12.453  1.00100.15      A    O  
ANISOU 2533  O   LYS A1123    11843  16062  10147   2177   -276   1447  A    O  
ATOM   2534  CB  LYS A1123     -18.702  -1.143 -11.562  1.00 95.84      A    C  
ANISOU 2534  CB  LYS A1123    10879  16095   9439   2183   -321   1139  A    C  
ATOM   2535  CG  LYS A1123     -19.065  -2.515 -10.999  1.00108.84      A    C  
ANISOU 2535  CG  LYS A1123    12322  18028  11005   2091   -312    982  A    C  
ATOM   2536  CD  LYS A1123     -19.557  -3.469 -12.081  1.00119.50      A    C  
ANISOU 2536  CD  LYS A1123    13561  19639  12206   2117   -358   1050  A    C  
ATOM   2537  CE  LYS A1123     -19.450  -4.921 -11.669  1.00128.70      A    C  
ANISOU 2537  CE  LYS A1123    14562  21035  13303   1958   -326    925  A    C  
ATOM   2538  NZ  LYS A1123     -18.039  -5.400 -11.641  1.00134.11      A    N1+
ANISOU 2538  NZ  LYS A1123    15303  21663  13990   1719   -258    954  A    N1+
ATOM   2539  N   ARG A1124     -16.988   2.021 -10.386  1.00 98.19      A    N  
ANISOU 2539  N   ARG A1124    11636  15541  10131   2118   -206   1176  A    N  
ATOM   2540  CA  ARG A1124     -16.397   3.293 -10.806  1.00100.33      A    C  
ANISOU 2540  CA  ARG A1124    12129  15479  10513   2126   -180   1319  A    C  
ATOM   2541  C   ARG A1124     -14.884   3.178 -10.601  1.00102.80      A    C  
ANISOU 2541  C   ARG A1124    12509  15694  10855   1836    -87   1325  A    C  
ATOM   2542  O   ARG A1124     -14.314   3.833  -9.721  1.00102.56      A    O  
ANISOU 2542  O   ARG A1124    12543  15467  10957   1745    -31   1210  A    O  
ATOM   2543  CB  ARG A1124     -16.986   4.474 -10.012  1.00103.44      A    C  
ANISOU 2543  CB  ARG A1124    12596  15632  11074   2295   -192   1212  A    C  
ATOM   2544  CG  ARG A1124     -18.396   4.851 -10.425  1.00120.05      A    C  
ANISOU 2544  CG  ARG A1124    14681  17769  13163   2610   -288   1254  A    C  
ATOM   2545  CD  ARG A1124     -18.697   6.293 -10.079  1.00140.58      A    C  
ANISOU 2545  CD  ARG A1124    17434  20032  15947   2772   -294   1229  A    C  
ATOM   2546  NE  ARG A1124     -20.133   6.575 -10.114  1.00157.19      A    N  
ANISOU 2546  NE  ARG A1124    19472  22204  18049   3089   -388   1188  A    N  
ATOM   2547  CZ  ARG A1124     -20.921   6.587  -9.043  1.00173.86      A    C  
ANISOU 2547  CZ  ARG A1124    21447  24402  20208   3200   -410    949  A    C  
ATOM   2548  NH1 ARG A1124     -20.419   6.343  -7.838  1.00160.23      A    N1+
ANISOU 2548  NH1 ARG A1124    19643  22707  18532   3021   -343    738  A    N1+
ATOM   2549  NH2 ARG A1124     -22.215   6.851  -9.167  1.00162.66      A    N  
ANISOU 2549  NH2 ARG A1124    19964  23059  18782   3495   -498    918  A    N  
ATOM   2550  N   TRP A1125     -14.246   2.309 -11.414  1.00 98.03      A    N  
ANISOU 2550  N   TRP A1125    11876  15252  10121   1693    -72   1443  A    N  
ATOM   2551  CA  TRP A1125     -12.815   1.993 -11.363  1.00 96.84      A    C  
ANISOU 2551  CA  TRP A1125    11758  15074   9965   1421     10   1450  A    C  
ATOM   2552  C   TRP A1125     -11.900   3.211 -11.491  1.00103.25      A    C  
ANISOU 2552  C   TRP A1125    12775  15555  10903   1326     75   1542  A    C  
ATOM   2553  O   TRP A1125     -10.829   3.221 -10.887  1.00102.58      A    O  
ANISOU 2553  O   TRP A1125    12703  15399  10872   1117    148   1453  A    O  
ATOM   2554  CB  TRP A1125     -12.420   0.914 -12.397  1.00 94.09      A    C  
ANISOU 2554  CB  TRP A1125    11337  14966   9448   1321      4   1566  A    C  
ATOM   2555  CG  TRP A1125     -13.426  -0.179 -12.641  1.00 93.68      A    C  
ANISOU 2555  CG  TRP A1125    11110  15217   9269   1435    -65   1523  A    C  
ATOM   2556  CD1 TRP A1125     -13.987  -0.514 -13.836  1.00 97.06      A    C  
ANISOU 2556  CD1 TRP A1125    11508  15799   9571   1545   -122   1663  A    C  
ATOM   2557  CD2 TRP A1125     -13.966  -1.096 -11.675  1.00 91.66      A    C  
ANISOU 2557  CD2 TRP A1125    10680  15151   8995   1436    -79   1325  A    C  
ATOM   2559  CE2 TRP A1125     -14.864  -1.944 -12.359  1.00 95.13      A    C  
ANISOU 2559  CE2 TRP A1125    10993  15843   9308   1543   -141   1350  A    C  
ATOM   2560  CE3 TRP A1125     -13.780  -1.283 -10.296  1.00 91.75      A    C  
ANISOU 2560  CE3 TRP A1125    10629  15153   9078   1354    -41   1129  A    C  
ATOM   2558  NE1 TRP A1125     -14.852  -1.571 -13.676  1.00 95.18      A    N  
ANISOU 2558  NE1 TRP A1125    11086  15831   9249   1610   -170   1550  A    N  
ATOM   2561  CZ2 TRP A1125     -15.568  -2.968 -11.715  1.00 92.90      A    C  
ANISOU 2561  CZ2 TRP A1125    10532  15784   8980   1556   -159   1190  A    C  
ATOM   2562  CZ3 TRP A1125     -14.485  -2.292  -9.659  1.00 91.76      A    C  
ANISOU 2562  CZ3 TRP A1125    10459  15383   9023   1378    -62    985  A    C  
ATOM   2563  CH2 TRP A1125     -15.380  -3.109 -10.361  1.00 91.92      A    C  
ANISOU 2563  CH2 TRP A1125    10364  15633   8930   1474   -117   1017  A    C  
ATOM   2564  N   ASP A1126     -12.311   4.226 -12.267  1.00102.41      A    N  
ANISOU 2564  N   ASP A1126    12824  15247  10840   1478     51   1718  A    N  
ATOM   2565  CA  ASP A1126     -11.525   5.443 -12.476  1.00104.41      A    C  
ANISOU 2565  CA  ASP A1126    13293  15156  11221   1395    117   1829  A    C  
ATOM   2566  C   ASP A1126     -11.552   6.399 -11.279  1.00108.56      A    C  
ANISOU 2566  C   ASP A1126    13884  15418  11948   1413    149   1651  A    C  
ATOM   2567  O   ASP A1126     -10.513   6.960 -10.935  1.00108.64      A    O  
ANISOU 2567  O   ASP A1126    13995  15216  12065   1222    233   1621  A    O  
ATOM   2568  CB  ASP A1126     -11.964   6.159 -13.766  1.00108.98      A    C  
ANISOU 2568  CB  ASP A1126    14026  15613  11767   1560     80   2101  A    C  
ATOM   2569  CG  ASP A1126     -11.558   5.476 -15.065  1.00119.87      A    C  
ANISOU 2569  CG  ASP A1126    15386  17201  12957   1490     75   2302  A    C  
ATOM   2570  OD1 ASP A1126     -10.935   4.385 -15.002  1.00117.93      A    O  
ANISOU 2570  OD1 ASP A1126    14974  17242  12592   1365     77   2217  A    O  
ATOM   2571  OD2 ASP A1126     -11.858   6.033 -16.146  1.00128.16      A    O1-
ANISOU 2571  OD2 ASP A1126    16590  18129  13978   1565     69   2545  A    O1-
ATOM   2572  N   GLU A1127     -12.731   6.587 -10.655  1.00105.27      A    N  
ANISOU 2572  N   GLU A1127    13398  15021  11579   1637     83   1520  A    N  
ATOM   2573  CA  GLU A1127     -12.915   7.484  -9.513  1.00106.53      A    C  
ANISOU 2573  CA  GLU A1127    13599  14954  11922   1686    102   1327  A    C  
ATOM   2574  C   GLU A1127     -12.290   6.943  -8.216  1.00108.17      A    C  
ANISOU 2574  C   GLU A1127    13672  15279  12147   1490    155   1073  A    C  
ATOM   2575  O   GLU A1127     -11.920   7.732  -7.341  1.00108.92      A    O  
ANISOU 2575  O   GLU A1127    13828  15161  12395   1422    206    925  A    O  
ATOM   2576  CB  GLU A1127     -14.403   7.804  -9.318  1.00109.34      A    C  
ANISOU 2576  CB  GLU A1127    13910  15326  12307   2002     11   1269  A    C  
ATOM   2577  CG  GLU A1127     -14.650   9.233  -8.852  1.00125.93      A    C  
ANISOU 2577  CG  GLU A1127    16139  17085  14622   2114     24   1164  A    C  
ATOM   2578  CD  GLU A1127     -16.090   9.643  -8.606  1.00156.54      A    C  
ANISOU 2578  CD  GLU A1127    20039  20892  18548   2456    -66   1179  A    C  
ATOM   2579  OE1 GLU A1127     -17.001   9.088  -9.263  1.00155.00      A    O  
ANISOU 2579  OE1 GLU A1127    19726  20958  18209   2624   -148   1241  A    O  
ATOM   2580  OE2 GLU A1127     -16.306  10.541  -7.762  1.00155.49      A    O1-
ANISOU 2580  OE2 GLU A1127    20037  20440  18601   2558    -55   1117  A    O1-
ATOM   2581  N   ALA A1128     -12.174   5.603  -8.099  1.00101.32      A    N  
ANISOU 2581  N   ALA A1128    12624  14748  11124   1404    141   1022  A    N  
ATOM   2582  CA  ALA A1128     -11.585   4.906  -6.951  1.00 98.45      A    C  
ANISOU 2582  CA  ALA A1128    12125  14540  10743   1229    183    809  A    C  
ATOM   2583  C   ALA A1128     -10.049   4.893  -7.019  1.00100.68      A    C  
ANISOU 2583  C   ALA A1128    12469  14747  11037    953    268    834  A    C  
ATOM   2584  O   ALA A1128      -9.396   4.939  -5.973  1.00 99.82      A    O  
ANISOU 2584  O   ALA A1128    12317  14625  10985    814    316    649  A    O  
ATOM   2585  CB  ALA A1128     -12.113   3.485  -6.883  1.00 96.65      A    C  
ANISOU 2585  CB  ALA A1128    11701  14674  10347   1250    138    773  A    C  
ATOM   2586  N   ALA A1129      -9.482   4.822  -8.251  1.00 96.34      A    N  
ANISOU 2586  N   ALA A1129    12010  14170  10426    875    285   1057  A    N  
ATOM   2587  CA  ALA A1129      -8.042   4.812  -8.544  1.00 95.12      A    C  
ANISOU 2587  CA  ALA A1129    11913  13962  10267    615    366   1108  A    C  
ATOM   2588  C   ALA A1129      -7.374   6.097  -8.051  1.00 99.97      A    C  
ANISOU 2588  C   ALA A1129    12671  14245  11066    511    440   1039  A    C  
ATOM   2589  O   ALA A1129      -6.337   6.025  -7.392  1.00 98.93      A    O  
ANISOU 2589  O   ALA A1129    12502  14123  10964    301    504    902  A    O  
ATOM   2590  CB  ALA A1129      -7.812   4.634 -10.040  1.00 96.02      A    C  
ANISOU 2590  CB  ALA A1129    12102  14106  10276    595    364   1371  A    C  
ATOM   2591  N   VAL A1130      -7.991   7.262  -8.338  1.00 98.31      A    N  
ANISOU 2591  N   VAL A1130    12623  13746  10985    664    430   1121  A    N  
ATOM   2592  CA  VAL A1130      -7.518   8.585  -7.907  1.00100.24      A    C  
ANISOU 2592  CA  VAL A1130    13025  13629  11430    590    499   1057  A    C  
ATOM   2593  C   VAL A1130      -7.747   8.808  -6.405  1.00102.67      A    C  
ANISOU 2593  C   VAL A1130    13244  13921  11846    608    501    753  A    C  
ATOM   2594  O   VAL A1130      -6.956   9.502  -5.761  1.00103.16      A    O  
ANISOU 2594  O   VAL A1130    13359  13800  12038    444    575    617  A    O  
ATOM   2595  CB  VAL A1130      -8.079   9.754  -8.761  1.00107.39      A    C  
ANISOU 2595  CB  VAL A1130    14150  14208  12443    755    488   1262  A    C  
ATOM   2596  CG1 VAL A1130      -7.347   9.868 -10.095  1.00108.06      A    C  
ANISOU 2596  CG1 VAL A1130    14367  14234  12457    637    532   1547  A    C  
ATOM   2597  CG2 VAL A1130      -9.590   9.639  -8.970  1.00107.44      A    C  
ANISOU 2597  CG2 VAL A1130    14117  14290  12414   1082    379   1298  A    C  
ATOM   2598  N   ASN A1131      -8.830   8.218  -5.857  1.00 96.97      A    N  
ANISOU 2598  N   ASN A1131    12377  13404  11063    801    423    642  A    N  
ATOM   2599  CA  ASN A1131      -9.194   8.309  -4.442  1.00 95.96      A    C  
ANISOU 2599  CA  ASN A1131    12140  13318  11003    845    416    357  A    C  
ATOM   2600  C   ASN A1131      -8.225   7.514  -3.560  1.00 95.83      A    C  
ANISOU 2600  C   ASN A1131    11975  13523  10912    619    460    182  A    C  
ATOM   2601  O   ASN A1131      -7.863   7.987  -2.481  1.00 96.17      A    O  
ANISOU 2601  O   ASN A1131    11994  13494  11053    542    499    -41  A    O  
ATOM   2602  CB  ASN A1131     -10.634   7.842  -4.228  1.00 96.41      A    C  
ANISOU 2602  CB  ASN A1131    12079  13559  10994   1106    325    313  A    C  
ATOM   2603  CG  ASN A1131     -11.232   8.204  -2.892  1.00118.96      A    C  
ANISOU 2603  CG  ASN A1131    14850  16413  13937   1201    315     38  A    C  
ATOM   2605  ND2 ASN A1131     -10.708   9.256  -2.285  1.00111.73      A    N  
ANISOU 2605  ND2 ASN A1131    13775  15756  12921   1358    252    -39  A    N  
ATOM   2604  OD1 ASN A1131     -12.145   7.547  -2.380  1.00113.42      A    O  
ANISOU 2604  OD1 ASN A1131    14219  15487  13390   1134    365   -114  A    O  
ATOM   2606  N   LEU A1132      -7.805   6.319  -4.022  1.00 88.50      A    N  
ANISOU 2606  N   LEU A1132    10948  12867   9812    524    451    278  A    N  
ATOM   2607  CA  LEU A1132      -6.853   5.459  -3.308  1.00 85.85      A    C  
ANISOU 2607  CA  LEU A1132    10475  12757   9387    326    484    144  A    C  
ATOM   2608  C   LEU A1132      -5.389   5.942  -3.465  1.00 91.25      A    C  
ANISOU 2608  C   LEU A1132    11242  13297  10131     73    571    148  A    C  
ATOM   2609  O   LEU A1132      -4.532   5.568  -2.662  1.00 89.60      A    O  
ANISOU 2609  O   LEU A1132    10934  13215   9894    -89    606    -15  A    O  
ATOM   2610  CB  LEU A1132      -6.989   3.989  -3.755  1.00 82.75      A    C  
ANISOU 2610  CB  LEU A1132     9952  12690   8800    332    440    243  A    C  
ATOM   2611  CG  LEU A1132      -8.211   3.219  -3.263  1.00 84.77      A    C  
ANISOU 2611  CG  LEU A1132    10070  13168   8973    513    371    175  A    C  
ATOM   2612  CD1 LEU A1132      -8.559   2.102  -4.223  1.00 82.84      A    C  
ANISOU 2612  CD1 LEU A1132     9762  13140   8575    554    326    343  A    C  
ATOM   2613  CD2 LEU A1132      -7.991   2.659  -1.869  1.00 84.00      A    C  
ANISOU 2613  CD2 LEU A1132     9824  13253   8837    448    382    -53  A    C  
ATOM   2614  N   ALA A1133      -5.106   6.760  -4.500  1.00 90.25      A    N  
ANISOU 2614  N   ALA A1133    11293  12918  10080     38    606    334  A    N  
ATOM   2615  CA  ALA A1133      -3.770   7.309  -4.749  1.00 91.49      A    C  
ANISOU 2615  CA  ALA A1133    11541  12919  10304   -210    699    352  A    C  
ATOM   2616  C   ALA A1133      -3.442   8.443  -3.765  1.00 98.32      A    C  
ANISOU 2616  C   ALA A1133    12467  13530  11360   -283    756    140  A    C  
ATOM   2617  O   ALA A1133      -2.268   8.690  -3.480  1.00 98.76      A    O  
ANISOU 2617  O   ALA A1133    12525  13540  11459   -516    833     45  A    O  
ATOM   2618  CB  ALA A1133      -3.665   7.805  -6.181  1.00 93.71      A    C  
ANISOU 2618  CB  ALA A1133    11994  13017  10593   -217    722    636  A    C  
ATOM   2619  N   LYS A1134      -4.483   9.112  -3.234  1.00 96.69      A    N  
ANISOU 2619  N   LYS A1134    12299  13173  11266    -82    718     50  A    N  
ATOM   2620  CA  LYS A1134      -4.359  10.204  -2.262  1.00 99.19      A    C  
ANISOU 2620  CA  LYS A1134    12669  13245  11775   -114    763   -174  A    C  
ATOM   2621  C   LYS A1134      -4.217   9.686  -0.816  1.00103.08      A    C  
ANISOU 2621  C   LYS A1134    12966  13976  12224   -163    756   -477  A    C  
ATOM   2622  O   LYS A1134      -4.173  10.489   0.122  1.00104.50      A    O  
ANISOU 2622  O   LYS A1134    13156  14004  12544   -194    790   -703  A    O  
ATOM   2623  CB  LYS A1134      -5.545  11.178  -2.384  1.00103.85      A    C  
ANISOU 2623  CB  LYS A1134    13386  13566  12506    139    722   -142  A    C  
ATOM   2624  CG  LYS A1134      -5.529  12.003  -3.662  1.00120.95      A    C  
ANISOU 2624  CG  LYS A1134    15781  15417  14756    171    745    135  A    C  
ATOM   2625  CD  LYS A1134      -6.685  12.986  -3.703  1.00133.88      A    C  
ANISOU 2625  CD  LYS A1134    17548  16767  16553    429    705    141  A    C  
ATOM   2626  CE  LYS A1134      -6.919  13.532  -5.089  1.00147.78      A    C  
ANISOU 2626  CE  LYS A1134    19526  18268  18355    517    705    458  A    C  
ATOM   2627  NZ  LYS A1134      -7.585  12.536  -5.971  1.00155.56      A    N1+
ANISOU 2627  NZ  LYS A1134    20450  19512  19143    684    619    679  A    N1+
ATOM   2628  N   SER A1135      -4.129   8.347  -0.643  1.00 97.53      A    N  
ANISOU 2628  N   SER A1135    12088  13644  11324   -172    714   -480  A    N  
ATOM   2629  CA  SER A1135      -3.980   7.692   0.659  1.00 96.20      A    C  
ANISOU 2629  CA  SER A1135    11731  13744  11076   -210    702   -726  A    C  
ATOM   2630  C   SER A1135      -2.514   7.618   1.093  1.00100.94      A    C  
ANISOU 2630  C   SER A1135    12277  14414  11663   -476    769   -851  A    C  
ATOM   2631  O   SER A1135      -1.617   7.663   0.244  1.00100.39      A    O  
ANISOU 2631  O   SER A1135    12277  14279  11587   -637    816   -713  A    O  
ATOM   2632  CB  SER A1135      -4.598   6.293   0.635  1.00 96.34      A    C  
ANISOU 2632  CB  SER A1135    11602  14107  10897    -98    630   -657  A    C  
ATOM   2633  OG  SER A1135      -3.799   5.346  -0.055  1.00101.29      A    O  
ANISOU 2633  OG  SER A1135    12188  14909  11387   -228    637   -513  A    O  
ATOM   2634  N   ARG A1136      -2.279   7.487   2.420  1.00 98.08      A    N  
ANISOU 2634  N   ARG A1136    11776  14208  11280   -520    772  -1118  A    N  
ATOM   2635  CA  ARG A1136      -0.935   7.355   2.990  1.00 97.80      A    C  
ANISOU 2635  CA  ARG A1136    11654  14291  11212   -753    825  -1273  A    C  
ATOM   2636  C   ARG A1136      -0.306   5.992   2.643  1.00 99.04      A    C  
ANISOU 2636  C   ARG A1136    11698  14764  11168   -828    802  -1159  A    C  
ATOM   2637  O   ARG A1136       0.917   5.875   2.629  1.00 98.23      A    O  
ANISOU 2637  O   ARG A1136    11553  14734  11034  -1028    847  -1208  A    O  
ATOM   2638  CB  ARG A1136      -0.913   7.658   4.500  1.00 99.06      A    C  
ANISOU 2638  CB  ARG A1136    11698  14539  11401   -760    829  -1594  A    C  
ATOM   2639  CG  ARG A1136      -1.716   6.702   5.379  1.00110.67      A    C  
ANISOU 2639  CG  ARG A1136    13006  16329  12715   -605    760  -1673  A    C  
ATOM   2640  CD  ARG A1136      -1.013   6.449   6.703  1.00125.98      A    C  
ANISOU 2640  CD  ARG A1136    14784  18500  14583   -708    772  -1943  A    C  
ATOM   2641  NE  ARG A1136      -0.985   7.639   7.559  1.00142.22      A    N  
ANISOU 2641  NE  ARG A1136    16859  20380  16798   -727    809  -2205  A    N  
ATOM   2642  CZ  ARG A1136      -0.332   7.721   8.715  1.00161.11      A    C  
ANISOU 2642  CZ  ARG A1136    19125  22927  19161   -826    829  -2476  A    C  
ATOM   2643  NH1 ARG A1136       0.360   6.684   9.172  1.00147.45      A    N1+
ANISOU 2643  NH1 ARG A1136    17246  21534  17246   -907    812  -2511  A    N1+
ATOM   2644  NH2 ARG A1136      -0.364   8.843   9.422  1.00152.82      A    N  
ANISOU 2644  NH2 ARG A1136    18097  21700  18267   -839    864  -2720  A    N  
ATOM   2645  N   TRP A1137      -1.155   4.981   2.329  1.00 94.34      A    N  
ANISOU 2645  N   TRP A1137    11053  14348  10443   -666    733  -1012  A    N  
ATOM   2646  CA  TRP A1137      -0.782   3.630   1.887  1.00 92.29      A    C  
ANISOU 2646  CA  TRP A1137    10700  14362  10003   -698    704   -882  A    C  
ATOM   2647  C   TRP A1137       0.053   3.757   0.596  1.00 98.64      A    C  
ANISOU 2647  C   TRP A1137    11604  15055  10820   -836    746   -692  A    C  
ATOM   2648  O   TRP A1137       1.109   3.124   0.478  1.00 97.40      A    O  
ANISOU 2648  O   TRP A1137    11372  15069  10567   -979    763   -688  A    O  
ATOM   2649  CB  TRP A1137      -2.062   2.786   1.674  1.00 89.12      A    C  
ANISOU 2649  CB  TRP A1137    10258  14099   9505   -488    630   -763  A    C  
ATOM   2650  CG  TRP A1137      -1.939   1.563   0.801  1.00 87.79      A    C  
ANISOU 2650  CG  TRP A1137    10045  14122   9189   -490    599   -574  A    C  
ATOM   2651  CD1 TRP A1137      -1.130   0.484   1.006  1.00 89.10      A    C  
ANISOU 2651  CD1 TRP A1137    10097  14536   9223   -587    595   -593  A    C  
ATOM   2652  CD2 TRP A1137      -2.758   1.239  -0.335  1.00 86.71      A    C  
ANISOU 2652  CD2 TRP A1137     9966  13962   9019   -369    562   -357  A    C  
ATOM   2654  CE2 TRP A1137      -2.349  -0.031  -0.797  1.00 88.65      A    C  
ANISOU 2654  CE2 TRP A1137    10129  14437   9118   -415    541   -261  A    C  
ATOM   2655  CE3 TRP A1137      -3.771   1.919  -1.033  1.00 88.72      A    C  
ANISOU 2655  CE3 TRP A1137    10332  14026   9352   -221    541   -237  A    C  
ATOM   2653  NE1 TRP A1137      -1.353  -0.468   0.038  1.00 86.93      A    N  
ANISOU 2653  NE1 TRP A1137     9811  14372   8846   -543    562   -404  A    N  
ATOM   2656  CZ2 TRP A1137      -2.919  -0.638  -1.922  1.00 86.86      A    C  
ANISOU 2656  CZ2 TRP A1137     9922  14258   8822   -331    505    -63  A    C  
ATOM   2657  CZ3 TRP A1137      -4.333   1.317  -2.147  1.00 89.21      A    C  
ANISOU 2657  CZ3 TRP A1137    10410  14151   9333   -131    501    -33  A    C  
ATOM   2658  CH2 TRP A1137      -3.906   0.056  -2.583  1.00 87.90      A    C  
ANISOU 2658  CH2 TRP A1137    10156  14220   9024   -193    485     46  A    C  
ATOM   2659  N   TYR A1138      -0.402   4.638  -0.328  1.00 97.46      A    N  
ANISOU 2659  N   TYR A1138    11624  14618  10790   -791    766   -545  A    N  
ATOM   2660  CA  TYR A1138       0.262   4.978  -1.581  1.00 98.45      A    C  
ANISOU 2660  CA  TYR A1138    11869  14597  10939   -916    815   -353  A    C  
ATOM   2661  C   TYR A1138       1.571   5.739  -1.294  1.00104.76      A    C  
ANISOU 2661  C   TYR A1138    12691  15281  11831  -1163    906   -487  A    C  
ATOM   2662  O   TYR A1138       2.566   5.509  -1.979  1.00104.58      A    O  
ANISOU 2662  O   TYR A1138    12676  15301  11761  -1333    952   -397  A    O  
ATOM   2663  CB  TYR A1138      -0.673   5.834  -2.452  1.00101.39      A    C  
ANISOU 2663  CB  TYR A1138    12421  14684  11418   -776    809   -171  A    C  
ATOM   2664  CG  TYR A1138      -0.134   6.133  -3.835  1.00104.46      A    C  
ANISOU 2664  CG  TYR A1138    12940  14945  11805   -878    854     69  A    C  
ATOM   2665  CD1 TYR A1138      -0.402   5.288  -4.907  1.00105.08      A    C  
ANISOU 2665  CD1 TYR A1138    13002  15184  11740   -809    811    284  A    C  
ATOM   2666  CD2 TYR A1138       0.623   7.277  -4.078  1.00107.93      A    C  
ANISOU 2666  CD2 TYR A1138    13521  15104  12386  -1047    944     80  A    C  
ATOM   2667  CE1 TYR A1138       0.088   5.560  -6.183  1.00107.39      A    C  
ANISOU 2667  CE1 TYR A1138    13408  15383  12013   -902    854    505  A    C  
ATOM   2668  CE2 TYR A1138       1.127   7.554  -5.347  1.00110.09      A    C  
ANISOU 2668  CE2 TYR A1138    13916  15270  12645  -1150    994    311  A    C  
ATOM   2669  CZ  TYR A1138       0.850   6.697  -6.400  1.00117.03      A    C  
ANISOU 2669  CZ  TYR A1138    14770  16331  13365  -1072    947    526  A    C  
ATOM   2670  OH  TYR A1138       1.323   6.978  -7.660  1.00119.07      A    O  
ANISOU 2670  OH  TYR A1138    15143  16504  13594  -1170    997    756  A    O  
ATOM   2671  N   ASN A1139       1.558   6.654  -0.303  1.00103.08      A    N  
ANISOU 2671  N   ASN A1139    12485  14929  11751  -1188    934   -712  A    N  
ATOM   2672  CA  ASN A1139       2.722   7.459   0.084  1.00104.92      A    C  
ANISOU 2672  CA  ASN A1139    12730  15047  12087  -1426   1022   -880  A    C  
ATOM   2673  C   ASN A1139       3.845   6.611   0.697  1.00107.33      A    C  
ANISOU 2673  C   ASN A1139    12846  15681  12255  -1577   1026  -1030  A    C  
ATOM   2674  O   ASN A1139       5.024   6.855   0.412  1.00107.95      A    O  
ANISOU 2674  O   ASN A1139    12921  15751  12344  -1800   1096  -1054  A    O  
ATOM   2675  CB  ASN A1139       2.309   8.588   1.038  1.00108.71      A    C  
ANISOU 2675  CB  ASN A1139    13257  15303  12746  -1390   1044  -1101  A    C  
ATOM   2676  CG  ASN A1139       1.598   9.748   0.375  1.00136.09      A    C  
ANISOU 2676  CG  ASN A1139    16941  18372  16397  -1299   1067   -975  A    C  
ATOM   2678  ND2 ASN A1139       2.073  10.955   0.644  1.00129.90      A    N  
ANISOU 2678  ND2 ASN A1139    16256  17297  15805  -1432   1146  -1110  A    N  
ATOM   2677  OD1 ASN A1139       0.618   9.586  -0.365  1.00131.87      A    O  
ANISOU 2677  OD1 ASN A1139    16484  17783  15837  -1105   1013   -763  A    O  
ATOM   2679  N   GLN A1140       3.473   5.613   1.526  1.00101.20      A    N  
ANISOU 2679  N   GLN A1140    11913  15196  11344  -1453    953  -1124  A    N  
ATOM   2680  CA  GLN A1140       4.400   4.702   2.208  1.00 98.93      A    C  
ANISOU 2680  CA  GLN A1140    11440  15239  10908  -1547    938  -1259  A    C  
ATOM   2681  C   GLN A1140       4.981   3.646   1.250  1.00 99.02      A    C  
ANISOU 2681  C   GLN A1140    11412  15436  10775  -1597    925  -1070  A    C  
ATOM   2682  O   GLN A1140       6.204   3.545   1.116  1.00 98.40      A    O  
ANISOU 2682  O   GLN A1140    11275  15452  10662  -1784    970  -1123  A    O  
ATOM   2683  CB  GLN A1140       3.716   4.033   3.417  1.00 98.79      A    C  
ANISOU 2683  CB  GLN A1140    11289  15451  10795  -1384    866  -1397  A    C  
ATOM   2684  CG  GLN A1140       3.462   4.969   4.603  1.00114.32      A    C  
ANISOU 2684  CG  GLN A1140    13240  17323  12874  -1374    884  -1657  A    C  
ATOM   2685  CD  GLN A1140       2.344   4.508   5.525  1.00130.85      A    C  
ANISOU 2685  CD  GLN A1140    15256  19562  14901  -1166    816  -1730  A    C  
ATOM   2687  NE2 GLN A1140       2.247   5.144   6.683  1.00122.17      A    N  
ANISOU 2687  NE2 GLN A1140    14100  18460  13857  -1164    827  -1986  A    N  
ATOM   2686  OE1 GLN A1140       1.551   3.602   5.217  1.00123.62      A    O  
ANISOU 2686  OE1 GLN A1140    14324  18764  13882  -1013    759  -1568  A    O  
ATOM   2688  N   THR A1141       4.100   2.876   0.583  1.00 92.84      A    N  
ANISOU 2688  N   THR A1141    10655  14709   9913  -1430    866   -865  A    N  
ATOM   2689  CA  THR A1141       4.473   1.805  -0.345  1.00 90.34      A    C  
ANISOU 2689  CA  THR A1141    10299  14568   9459  -1447    845   -688  A    C  
ATOM   2690  C   THR A1141       3.978   2.109  -1.786  1.00 92.10      A    C  
ANISOU 2690  C   THR A1141    10675  14597   9720  -1407    858   -430  A    C  
ATOM   2691  O   THR A1141       2.957   1.556  -2.195  1.00 90.25      A    O  
ANISOU 2691  O   THR A1141    10458  14397   9436  -1229    798   -294  A    O  
ATOM   2692  CB  THR A1141       4.011   0.443   0.217  1.00 95.90      A    C  
ANISOU 2692  CB  THR A1141    10865  15565  10008  -1303    764   -698  A    C  
ATOM   2694  CG2 THR A1141       5.034  -0.168   1.162  1.00 92.88      A    C  
ANISOU 2694  CG2 THR A1141    10323  15438   9529  -1396    760   -879  A    C  
ATOM   2693  OG1 THR A1141       2.756   0.597   0.893  1.00 95.67      A    O  
ANISOU 2693  OG1 THR A1141    10846  15493  10011  -1125    721   -742  A    O  
ATOM   2695  N   PRO A1142       4.680   2.974  -2.571  1.00 88.76      A    N  
ANISOU 2695  N   PRO A1142    10362  13982   9381  -1572    936   -358  A    N  
ATOM   2696  CA  PRO A1142       4.182   3.318  -3.917  1.00 88.51      A    C  
ANISOU 2696  CA  PRO A1142    10485  13770   9376  -1524    948   -101  A    C  
ATOM   2697  C   PRO A1142       4.019   2.160  -4.896  1.00 89.33      A    C  
ANISOU 2697  C   PRO A1142    10542  14079   9321  -1460    902     87  A    C  
ATOM   2698  O   PRO A1142       2.947   2.043  -5.479  1.00 88.50      A    O  
ANISOU 2698  O   PRO A1142    10507  13918   9201  -1293    856    251  A    O  
ATOM   2699  CB  PRO A1142       5.196   4.349  -4.427  1.00 92.62      A    C  
ANISOU 2699  CB  PRO A1142    11113  14076  10003  -1752   1054    -85  A    C  
ATOM   2700  CG  PRO A1142       5.843   4.887  -3.214  1.00 98.15      A    C  
ANISOU 2700  CG  PRO A1142    11742  14767  10784  -1882   1094   -361  A    C  
ATOM   2701  CD  PRO A1142       5.898   3.747  -2.249  1.00 91.68      A    C  
ANISOU 2701  CD  PRO A1142    10726  14282   9828  -1810   1023   -508  A    C  
ATOM   2702  N   ASN A1143       5.057   1.308  -5.062  1.00 84.11      A    N  
ANISOU 2702  N   ASN A1143     9757  13659   8541  -1582    911     52  A    N  
ATOM   2703  CA  ASN A1143       5.076   0.172  -5.998  1.00 81.65      A    C  
ANISOU 2703  CA  ASN A1143     9388  13555   8080  -1541    873    202  A    C  
ATOM   2704  C   ASN A1143       3.989  -0.878  -5.752  1.00 81.58      A    C  
ANISOU 2704  C   ASN A1143     9309  13698   7988  -1323    778    230  A    C  
ATOM   2705  O   ASN A1143       3.320  -1.268  -6.707  1.00 80.40      A    O  
ANISOU 2705  O   ASN A1143     9197  13569   7781  -1221    744    404  A    O  
ATOM   2706  CB  ASN A1143       6.455  -0.491  -6.041  1.00 82.15      A    C  
ANISOU 2706  CB  ASN A1143     9322  13844   8047  -1710    901    120  A    C  
ATOM   2707  CG  ASN A1143       7.579   0.429  -6.440  1.00102.29      A    C  
ANISOU 2707  CG  ASN A1143    11925  16283  10657  -1947   1003    110  A    C  
ATOM   2709  ND2 ASN A1143       7.582   0.883  -7.686  1.00 94.37      A    N  
ANISOU 2709  ND2 ASN A1143    11036  15169   9651  -1999   1047    313  A    N  
ATOM   2708  OD1 ASN A1143       8.458   0.737  -5.637  1.00 96.98      A    O  
ANISOU 2708  OD1 ASN A1143    11186  15636  10024  -2090   1045    -80  A    O  
ATOM   2710  N   ARG A1144       3.808  -1.335  -4.494  1.00 75.96      A    N  
ANISOU 2710  N   ARG A1144     8494  13103   7264  -1257    738     58  A    N  
ATOM   2711  CA  ARG A1144       2.782  -2.332  -4.171  1.00 73.50      A    C  
ANISOU 2711  CA  ARG A1144     8114  12934   6876  -1070    659     75  A    C  
ATOM   2712  C   ARG A1144       1.366  -1.796  -4.444  1.00 75.98      A    C  
ANISOU 2712  C   ARG A1144     8530  13080   7258   -901    629    173  A    C  
ATOM   2713  O   ARG A1144       0.576  -2.483  -5.091  1.00 74.28      A    O  
ANISOU 2713  O   ARG A1144     8303  12947   6974   -775    579    293  A    O  
ATOM   2714  CB  ARG A1144       2.921  -2.856  -2.732  1.00 72.37      A    C  
ANISOU 2714  CB  ARG A1144     7846  12955   6698  -1047    631   -120  A    C  
ATOM   2715  CG  ARG A1144       2.514  -4.322  -2.621  1.00 77.94      A    C  
ANISOU 2715  CG  ARG A1144     8450  13886   7277   -930    566    -83  A    C  
ATOM   2716  CD  ARG A1144       2.009  -4.713  -1.248  1.00 77.56      A    C  
ANISOU 2716  CD  ARG A1144     8315  13952   7201   -846    532   -227  A    C  
ATOM   2717  NE  ARG A1144       1.478  -6.077  -1.258  1.00 78.08      A    N  
ANISOU 2717  NE  ARG A1144     8307  14198   7160   -737    478   -164  A    N  
ATOM   2718  CZ  ARG A1144       1.585  -6.935  -0.249  1.00 89.69      A    C  
ANISOU 2718  CZ  ARG A1144     9677  15850   8551   -704    451   -253  A    C  
ATOM   2719  NH1 ARG A1144       1.067  -8.152  -0.349  1.00 73.88      A    N1+
ANISOU 2719  NH1 ARG A1144     7627  13980   6466   -614    410   -180  A    N1+
ATOM   2720  NH2 ARG A1144       2.205  -6.584   0.868  1.00 79.56      A    N  
ANISOU 2720  NH2 ARG A1144     8340  14620   7268   -762    465   -416  A    N  
ATOM   2721  N   ALA A1145       1.088  -0.547  -4.004  1.00 72.97      A    N  
ANISOU 2721  N   ALA A1145     8248  12464   7015   -900    661    115  A    N  
ATOM   2722  CA  ALA A1145      -0.175   0.167  -4.201  1.00 73.21      A    C  
ANISOU 2722  CA  ALA A1145     8381  12306   7128   -734    636    189  A    C  
ATOM   2723  C   ALA A1145      -0.479   0.431  -5.694  1.00 77.09      A    C  
ANISOU 2723  C   ALA A1145     8989  12691   7609   -698    637    430  A    C  
ATOM   2724  O   ALA A1145      -1.617   0.223  -6.117  1.00 76.25      A    O  
ANISOU 2724  O   ALA A1145     8900  12592   7478   -521    581    531  A    O  
ATOM   2725  CB  ALA A1145      -0.169   1.473  -3.419  1.00 75.75      A    C  
ANISOU 2725  CB  ALA A1145     8781  12390   7608   -760    676     54  A    C  
ATOM   2726  N   LYS A1146       0.533   0.856  -6.485  1.00 73.98      A    N  
ANISOU 2726  N   LYS A1146     8665  12222   7224   -867    700    517  A    N  
ATOM   2727  CA  LYS A1146       0.394   1.109  -7.924  1.00 74.81      A    C  
ANISOU 2727  CA  LYS A1146     8879  12246   7299   -856    711    754  A    C  
ATOM   2728  C   LYS A1146      -0.022  -0.155  -8.690  1.00 75.89      A    C  
ANISOU 2728  C   LYS A1146     8926  12629   7278   -761    648    864  A    C  
ATOM   2729  O   LYS A1146      -0.848  -0.064  -9.602  1.00 75.56      A    O  
ANISOU 2729  O   LYS A1146     8951  12550   7208   -632    614   1032  A    O  
ATOM   2730  CB  LYS A1146       1.701   1.650  -8.522  1.00 79.62      A    C  
ANISOU 2730  CB  LYS A1146     9549  12780   7924  -1088    801    803  A    C  
ATOM   2731  CG  LYS A1146       1.939   3.148  -8.345  1.00104.62      A    C  
ANISOU 2731  CG  LYS A1146    12878  15614  11258  -1171    874    806  A    C  
ATOM   2732  CD  LYS A1146       3.313   3.524  -8.931  1.00118.73      A    C  
ANISOU 2732  CD  LYS A1146    14705  17364  13042  -1429    972    852  A    C  
ATOM   2733  CE  LYS A1146       3.649   4.997  -8.876  1.00131.42      A    C  
ANISOU 2733  CE  LYS A1146    16486  18627  14820  -1545   1061    870  A    C  
ATOM   2734  NZ  LYS A1146       4.059   5.427  -7.513  1.00140.62      A    N1+
ANISOU 2734  NZ  LYS A1146    17612  19704  16114  -1621   1089    607  A    N1+
ATOM   2735  N   ARG A1147       0.549  -1.325  -8.321  1.00 70.32      A    N  
ANISOU 2735  N   ARG A1147     8071  12175   6473   -820    633    766  A    N  
ATOM   2736  CA  ARG A1147       0.243  -2.618  -8.950  1.00 68.40      A    C  
ANISOU 2736  CA  ARG A1147     7731  12167   6091   -746    578    838  A    C  
ATOM   2737  C   ARG A1147      -1.162  -3.105  -8.593  1.00 72.05      A    C  
ANISOU 2737  C   ARG A1147     8152  12684   6541   -540    504    826  A    C  
ATOM   2738  O   ARG A1147      -1.837  -3.692  -9.442  1.00 71.21      A    O  
ANISOU 2738  O   ARG A1147     8028  12674   6355   -440    460    941  A    O  
ATOM   2739  CB  ARG A1147       1.300  -3.684  -8.606  1.00 66.72      A    C  
ANISOU 2739  CB  ARG A1147     7379  12179   5791   -862    585    728  A    C  
ATOM   2740  CG  ARG A1147       2.672  -3.431  -9.258  1.00 72.60      A    C  
ANISOU 2740  CG  ARG A1147     8137  12935   6513  -1063    654    757  A    C  
ATOM   2741  CD  ARG A1147       3.673  -4.568  -9.086  1.00 73.36      A    C  
ANISOU 2741  CD  ARG A1147     8087  13277   6508  -1148    648    664  A    C  
ATOM   2742  NE  ARG A1147       3.912  -4.910  -7.683  1.00 80.65      A    N  
ANISOU 2742  NE  ARG A1147     8918  14276   7450  -1147    631    473  A    N  
ATOM   2743  CZ  ARG A1147       4.920  -4.451  -6.946  1.00 93.26      A    C  
ANISOU 2743  CZ  ARG A1147    10485  15860   9088  -1286    677    332  A    C  
ATOM   2744  NH1 ARG A1147       5.036  -4.815  -5.675  1.00 79.90      A    N1+
ANISOU 2744  NH1 ARG A1147     8703  14261   7394  -1262    652    167  A    N1+
ATOM   2745  NH2 ARG A1147       5.817  -3.625  -7.472  1.00 76.73      A    N  
ANISOU 2745  NH2 ARG A1147     8449  13672   7033  -1454    751    356  A    N  
ATOM   2746  N   VAL A1148      -1.610  -2.826  -7.347  1.00 68.77      A    N  
ANISOU 2746  N   VAL A1148     7715  12213   6200   -481    493    679  A    N  
ATOM   2747  CA  VAL A1148      -2.933  -3.185  -6.821  1.00 67.15      A    C  
ANISOU 2747  CA  VAL A1148     7462  12059   5991   -298    433    639  A    C  
ATOM   2748  C   VAL A1148      -4.031  -2.341  -7.480  1.00 72.73      A    C  
ANISOU 2748  C   VAL A1148     8278  12601   6755   -148    409    760  A    C  
ATOM   2749  O   VAL A1148      -5.013  -2.901  -7.973  1.00 71.68      A    O  
ANISOU 2749  O   VAL A1148     8107  12569   6558    -11    355    832  A    O  
ATOM   2750  CB  VAL A1148      -2.956  -3.136  -5.264  1.00 69.94      A    C  
ANISOU 2750  CB  VAL A1148     7750  12433   6392   -297    436    436  A    C  
ATOM   2751  CG1 VAL A1148      -4.380  -3.036  -4.704  1.00 69.81      A    C  
ANISOU 2751  CG1 VAL A1148     7713  12410   6402   -113    390    392  A    C  
ATOM   2752  CG2 VAL A1148      -2.234  -4.344  -4.680  1.00 67.80      A    C  
ANISOU 2752  CG2 VAL A1148     7348  12388   6024   -380    433    346  A    C  
ATOM   2753  N   ILE A1149      -3.847  -1.002  -7.502  1.00 71.87      A    N  
ANISOU 2753  N   ILE A1149     8303  12239   6767   -175    449    778  A    N  
ATOM   2754  CA  ILE A1149      -4.787  -0.030  -8.078  1.00 73.45      A    C  
ANISOU 2754  CA  ILE A1149     8628  12241   7037    -25    429    897  A    C  
ATOM   2755  C   ILE A1149      -5.045  -0.305  -9.569  1.00 77.36      A    C  
ANISOU 2755  C   ILE A1149     9163  12796   7436     27    403   1116  A    C  
ATOM   2756  O   ILE A1149      -6.206  -0.305  -9.971  1.00 76.82      A    O  
ANISOU 2756  O   ILE A1149     9100  12742   7345    214    344   1190  A    O  
ATOM   2757  CB  ILE A1149      -4.339   1.435  -7.779  1.00 78.70      A    C  
ANISOU 2757  CB  ILE A1149     9440  12600   7863    -93    489    869  A    C  
ATOM   2758  CG1 ILE A1149      -4.627   1.796  -6.302  1.00 79.16      A    C  
ANISOU 2758  CG1 ILE A1149     9453  12604   8020    -55    489    641  A    C  
ATOM   2759  CG2 ILE A1149      -4.981   2.460  -8.729  1.00 81.33      A    C  
ANISOU 2759  CG2 ILE A1149     9940  12703   8259     29    480   1057  A    C  
ATOM   2760  CD1 ILE A1149      -3.726   2.879  -5.692  1.00 89.12      A    C  
ANISOU 2760  CD1 ILE A1149    10799  13640   9424   -204    563    528  A    C  
ATOM   2761  N   THR A1150      -3.989  -0.593 -10.361  1.00 75.14      A    N  
ANISOU 2761  N   THR A1150     8890  12577   7083   -134    445   1206  A    N  
ATOM   2762  CA  THR A1150      -4.111  -0.883 -11.805  1.00 75.97      A    C  
ANISOU 2762  CA  THR A1150     9021  12768   7076   -105    427   1407  A    C  
ATOM   2763  C   THR A1150      -4.941  -2.180 -12.049  1.00 78.55      A    C  
ANISOU 2763  C   THR A1150     9206  13359   7280     19    352   1397  A    C  
ATOM   2764  O   THR A1150      -5.695  -2.232 -13.030  1.00 78.91      A    O  
ANISOU 2764  O   THR A1150     9271  13452   7258    146    307   1535  A    O  
ATOM   2765  CB  THR A1150      -2.727  -0.862 -12.503  1.00 85.32      A    C  
ANISOU 2765  CB  THR A1150    10234  13972   8213   -322    498   1477  A    C  
ATOM   2767  CG2 THR A1150      -2.817  -1.084 -14.006  1.00 83.95      A    C  
ANISOU 2767  CG2 THR A1150    10090  13894   7914   -299    485   1684  A    C  
ATOM   2766  OG1 THR A1150      -2.106   0.406 -12.277  1.00 86.35      A    O  
ANISOU 2766  OG1 THR A1150    10501  13839   8469   -435    571   1484  A    O  
ATOM   2768  N   THR A1151      -4.845  -3.187 -11.134  1.00 72.25      A    N  
ANISOU 2768  N   THR A1151     8269  12727   6456    -13    339   1232  A    N  
ATOM   2769  CA  THR A1151      -5.635  -4.427 -11.209  1.00 69.71      A    C  
ANISOU 2769  CA  THR A1151     7814  12635   6039     85    279   1201  A    C  
ATOM   2770  C   THR A1151      -7.122  -4.087 -11.000  1.00 73.32      A    C  
ANISOU 2770  C   THR A1151     8273  13056   6531    293    222   1196  A    C  
ATOM   2771  O   THR A1151      -7.962  -4.590 -11.748  1.00 72.71      A    O  
ANISOU 2771  O   THR A1151     8147  13108   6373    405    171   1266  A    O  
ATOM   2772  CB  THR A1151      -5.132  -5.492 -10.212  1.00 72.41      A    C  
ANISOU 2772  CB  THR A1151     8029  13129   6355     -3    287   1041  A    C  
ATOM   2774  CG2 THR A1151      -5.745  -6.872 -10.463  1.00 65.98      A    C  
ANISOU 2774  CG2 THR A1151     7089  12543   5439     56    240   1029  A    C  
ATOM   2773  OG1 THR A1151      -3.709  -5.575 -10.269  1.00 71.99      A    O  
ANISOU 2773  OG1 THR A1151     7982  13082   6289   -185    341   1026  A    O  
ATOM   2775  N   PHE A1152      -7.435  -3.207 -10.011  1.00 70.16      A    N  
ANISOU 2775  N   PHE A1152     7922  12487   6248    345    232   1105  A    N  
ATOM   2776  CA  PHE A1152      -8.809  -2.753  -9.727  1.00 70.45      A    C  
ANISOU 2776  CA  PHE A1152     7959  12479   6329    548    181   1082  A    C  
ATOM   2777  C   PHE A1152      -9.378  -1.932 -10.892  1.00 77.95      A    C  
ANISOU 2777  C   PHE A1152     9023  13315   7281    678    151   1265  A    C  
ATOM   2778  O   PHE A1152     -10.594  -1.858 -11.046  1.00 78.39      A    O  
ANISOU 2778  O   PHE A1152     9052  13409   7325    868     92   1278  A    O  
ATOM   2779  CB  PHE A1152      -8.878  -1.916  -8.428  1.00 72.30      A    C  
ANISOU 2779  CB  PHE A1152     8223  12553   6693    565    203    929  A    C  
ATOM   2780  CG  PHE A1152      -8.962  -2.655  -7.107  1.00 71.48      A    C  
ANISOU 2780  CG  PHE A1152     7988  12594   6579    532    207    738  A    C  
ATOM   2781  CD1 PHE A1152      -9.916  -3.645  -6.903  1.00 72.47      A    C  
ANISOU 2781  CD1 PHE A1152     7982  12928   6624    623    164    693  A    C  
ATOM   2782  CD2 PHE A1152      -8.142  -2.302  -6.041  1.00 73.24      A    C  
ANISOU 2782  CD2 PHE A1152     8218  12742   6869    414    255    601  A    C  
ATOM   2783  CE1 PHE A1152     -10.004  -4.310  -5.682  1.00 72.18      A    C  
ANISOU 2783  CE1 PHE A1152     7835  13020   6570    589    173    535  A    C  
ATOM   2784  CE2 PHE A1152      -8.229  -2.970  -4.820  1.00 74.64      A    C  
ANISOU 2784  CE2 PHE A1152     8275  13065   7019    392    257    438  A    C  
ATOM   2785  CZ  PHE A1152      -9.167  -3.962  -4.644  1.00 71.63      A    C  
ANISOU 2785  CZ  PHE A1152     7777  12883   6555    481    218    415  A    C  
ATOM   2786  N   ARG A1153      -8.496  -1.321 -11.705  1.00 77.00      A    N  
ANISOU 2786  N   ARG A1153     9027  13064   7166    577    194   1407  A    N  
ATOM   2787  CA  ARG A1153      -8.869  -0.496 -12.849  1.00 79.56      A    C  
ANISOU 2787  CA  ARG A1153     9482  13267   7482    683    175   1610  A    C  
ATOM   2788  C   ARG A1153      -9.050  -1.304 -14.147  1.00 82.73      A    C  
ANISOU 2788  C   ARG A1153     9827  13887   7719    710    138   1751  A    C  
ATOM   2789  O   ARG A1153      -9.993  -1.030 -14.885  1.00 83.66      A    O  
ANISOU 2789  O   ARG A1153     9976  14018   7794    888     81   1870  A    O  
ATOM   2790  CB  ARG A1153      -7.847   0.640 -13.046  1.00 83.75      A    C  
ANISOU 2790  CB  ARG A1153    10185  13531   8105    549    251   1698  A    C  
ATOM   2791  CG  ARG A1153      -8.378   1.826 -13.858  1.00102.13      A    C  
ANISOU 2791  CG  ARG A1153    12688  15633  10484    692    236   1886  A    C  
ATOM   2792  CD  ARG A1153      -7.271   2.702 -14.427  1.00122.40      A    C  
ANISOU 2792  CD  ARG A1153    15424  17986  13097    526    320   2030  A    C  
ATOM   2793  NE  ARG A1153      -6.544   3.434 -13.387  1.00142.88      A    N  
ANISOU 2793  NE  ARG A1153    18078  20362  15850    378    394   1889  A    N  
ATOM   2794  CZ  ARG A1153      -5.277   3.205 -13.047  1.00162.84      A    C  
ANISOU 2794  CZ  ARG A1153    20570  22925  18377    133    468   1808  A    C  
ATOM   2795  NH1 ARG A1153      -4.702   3.919 -12.088  1.00152.50      A    N1+
ANISOU 2795  NH1 ARG A1153    19306  21424  17211     12    530   1665  A    N1+
ATOM   2796  NH2 ARG A1153      -4.573   2.266 -13.670  1.00150.80      A    N  
ANISOU 2796  NH2 ARG A1153    18955  21634  16707     12    479   1855  A    N  
ATOM   2797  N   THR A1154      -8.153  -2.273 -14.433  1.00 77.16      A    N  
ANISOU 2797  N   THR A1154     9037  13358   6922    544    167   1731  A    N  
ATOM   2798  CA  THR A1154      -8.196  -3.070 -15.670  1.00 76.10      A    C  
ANISOU 2798  CA  THR A1154     8843  13442   6631    549    138   1843  A    C  
ATOM   2799  C   THR A1154      -8.910  -4.421 -15.542  1.00 79.12      A    C  
ANISOU 2799  C   THR A1154     9044  14092   6928    606     85   1730  A    C  
ATOM   2800  O   THR A1154      -9.563  -4.847 -16.490  1.00 78.53      A    O  
ANISOU 2800  O   THR A1154     8915  14180   6741    698     35   1807  A    O  
ATOM   2801  CB  THR A1154      -6.787  -3.273 -16.263  1.00 78.73      A    C  
ANISOU 2801  CB  THR A1154     9203  13803   6909    336    206   1907  A    C  
ATOM   2803  CG2 THR A1154      -6.066  -1.961 -16.562  1.00 76.86      A    C  
ANISOU 2803  CG2 THR A1154     9149  13315   6738    262    268   2048  A    C  
ATOM   2802  OG1 THR A1154      -6.009  -4.078 -15.380  1.00 77.31      A    O  
ANISOU 2802  OG1 THR A1154     8928  13691   6753    186    241   1737  A    O  
ATOM   2804  N   GLY A1155      -8.760  -5.086 -14.398  1.00 75.53      A    N  
ANISOU 2804  N   GLY A1155     8496  13682   6520    544     98   1551  A    N  
ATOM   2805  CA  GLY A1155      -9.327  -6.412 -14.173  1.00 74.09      A    C  
ANISOU 2805  CA  GLY A1155     8151  13730   6271    569     62   1441  A    C  
ATOM   2806  C   GLY A1155      -8.497  -7.498 -14.839  1.00 78.33      A    C  
ANISOU 2806  C   GLY A1155     8616  14441   6706    437     78   1451  A    C  
ATOM   2807  O   GLY A1155      -9.032  -8.540 -15.232  1.00 76.98      A    O  
ANISOU 2807  O   GLY A1155     8328  14466   6453    473     42   1416  A    O  
ATOM   2808  N   THR A1156      -7.174  -7.251 -14.985  1.00 75.87      A    N  
ANISOU 2808  N   THR A1156     8367  14059   6400    279    136   1489  A    N  
ATOM   2809  CA  THR A1156      -6.207  -8.183 -15.581  1.00 75.17      A    C  
ANISOU 2809  CA  THR A1156     8213  14125   6222    145    158   1488  A    C  
ATOM   2810  C   THR A1156      -5.010  -8.436 -14.650  1.00 79.22      A    C  
ANISOU 2810  C   THR A1156     8710  14603   6787    -15    212   1376  A    C  
ATOM   2811  O   THR A1156      -4.840  -7.739 -13.647  1.00 79.90      A    O  
ANISOU 2811  O   THR A1156     8851  14534   6974    -37    237   1316  A    O  
ATOM   2812  CB  THR A1156      -5.741  -7.702 -16.971  1.00 83.44      A    C  
ANISOU 2812  CB  THR A1156     9335  15183   7187    113    174   1661  A    C  
ATOM   2814  CG2 THR A1156      -6.822  -7.819 -18.040  1.00 82.09      A    C  
ANISOU 2814  CG2 THR A1156     9142  15128   6921    269    111   1762  A    C  
ATOM   2813  OG1 THR A1156      -5.262  -6.361 -16.881  1.00 85.18      A    O  
ANISOU 2813  OG1 THR A1156     9705  15175   7485     66    221   1747  A    O  
ATOM   2815  N   TRP A1157      -4.169  -9.425 -15.002  1.00 74.50      A    N  
ANISOU 2815  N   TRP A1157     8031  14159   6117   -120    225   1339  A    N  
ATOM   2816  CA  TRP A1157      -2.960  -9.792 -14.261  1.00 72.82      A    C  
ANISOU 2816  CA  TRP A1157     7785  13954   5931   -261    268   1234  A    C  
ATOM   2817  C   TRP A1157      -1.725  -9.105 -14.851  1.00 77.94      A    C  
ANISOU 2817  C   TRP A1157     8500  14551   6563   -404    327   1306  A    C  
ATOM   2818  O   TRP A1157      -0.608  -9.393 -14.419  1.00 77.10      A    O  
ANISOU 2818  O   TRP A1157     8354  14480   6461   -529    363   1222  A    O  
ATOM   2819  CB  TRP A1157      -2.752 -11.309 -14.349  1.00 69.72      A    C  
ANISOU 2819  CB  TRP A1157     7262  13759   5471   -281    246   1149  A    C  
ATOM   2820  CG  TRP A1157      -3.844 -12.145 -13.751  1.00 69.64      A    C  
ANISOU 2820  CG  TRP A1157     7178  13808   5474   -175    202   1071  A    C  
ATOM   2821  CD1 TRP A1157      -4.786 -12.864 -14.425  1.00 72.33      A    C  
ANISOU 2821  CD1 TRP A1157     7456  14267   5760    -84    159   1086  A    C  
ATOM   2822  CD2 TRP A1157      -4.071 -12.392 -12.355  1.00 68.63      A    C  
ANISOU 2822  CD2 TRP A1157     7022  13641   5412   -161    202    958  A    C  
ATOM   2824  CE2 TRP A1157      -5.163 -13.283 -12.260  1.00 71.51      A    C  
ANISOU 2824  CE2 TRP A1157     7313  14098   5760    -69    165    919  A    C  
ATOM   2825  CE3 TRP A1157      -3.438 -11.970 -11.172  1.00 69.77      A    C  
ANISOU 2825  CE3 TRP A1157     7191  13699   5620   -224    233    881  A    C  
ATOM   2823  NE1 TRP A1157      -5.579 -13.555 -13.539  1.00 70.73      A    N  
ANISOU 2823  NE1 TRP A1157     7190  14091   5592    -26    139    991  A    N  
ATOM   2826  CZ2 TRP A1157      -5.649 -13.744 -11.032  1.00 69.84      A    C  
ANISOU 2826  CZ2 TRP A1157     7059  13886   5591    -41    162    822  A    C  
ATOM   2827  CZ3 TRP A1157      -3.924 -12.425  -9.955  1.00 70.47      A    C  
ANISOU 2827  CZ3 TRP A1157     7235  13798   5742   -183    223    782  A    C  
ATOM   2828  CH2 TRP A1157      -5.015 -13.301  -9.894  1.00 70.34      A    C  
ANISOU 2828  CH2 TRP A1157     7153  13868   5706    -95    190    761  A    C  
ATOM   2829  N   ASP A1158      -1.925  -8.205 -15.837  1.00 77.04      A    N  
ANISOU 2829  N   ASP A1158     8486  14362   6426   -385    338   1463  A    N  
ATOM   2830  CA  ASP A1158      -0.883  -7.521 -16.612  1.00 78.72      A    C  
ANISOU 2830  CA  ASP A1158     8771  14530   6607   -522    401   1564  A    C  
ATOM   2831  C   ASP A1158       0.159  -6.709 -15.798  1.00 83.82      A    C  
ANISOU 2831  C   ASP A1158     9476  15023   7350   -672    470   1500  A    C  
ATOM   2832  O   ASP A1158       1.270  -6.498 -16.298  1.00 84.56      A    O  
ANISOU 2832  O   ASP A1158     9579  15144   7407   -827    530   1529  A    O  
ATOM   2833  CB  ASP A1158      -1.515  -6.641 -17.701  1.00 82.51      A    C  
ANISOU 2833  CB  ASP A1158     9367  14930   7053   -443    395   1761  A    C  
ATOM   2834  CG  ASP A1158      -2.096  -7.428 -18.869  1.00 95.27      A    C  
ANISOU 2834  CG  ASP A1158    10914  16753   8529   -350    344   1838  A    C  
ATOM   2835  OD1 ASP A1158      -1.359  -8.243 -19.466  1.00 95.84      A    O  
ANISOU 2835  OD1 ASP A1158    10890  17018   8505   -434    354   1803  A    O  
ATOM   2836  OD2 ASP A1158      -3.278  -7.209 -19.202  1.00103.14      A    O1-
ANISOU 2836  OD2 ASP A1158    11949  17730   9512   -189    292   1925  A    O1-
ATOM   2837  N   ALA A1159      -0.175  -6.275 -14.568  1.00 79.75      A    N  
ANISOU 2837  N   ALA A1159     8986  14364   6951   -634    465   1402  A    N  
ATOM   2838  CA  ALA A1159       0.749  -5.513 -13.722  1.00 79.99      A    C  
ANISOU 2838  CA  ALA A1159     9059  14258   7077   -771    527   1315  A    C  
ATOM   2839  C   ALA A1159       1.747  -6.429 -13.003  1.00 82.08      A    C  
ANISOU 2839  C   ALA A1159     9194  14677   7315   -874    536   1149  A    C  
ATOM   2840  O   ALA A1159       2.819  -5.966 -12.593  1.00 81.83      A    O  
ANISOU 2840  O   ALA A1159     9168  14600   7324  -1023    594   1076  A    O  
ATOM   2841  CB  ALA A1159      -0.031  -4.690 -12.707  1.00 81.32      A    C  
ANISOU 2841  CB  ALA A1159     9299  14227   7373   -680    515   1262  A    C  
ATOM   2842  N   TYR A1160       1.385  -7.729 -12.856  1.00 76.70      A    N  
ANISOU 2842  N   TYR A1160     8395  14179   6568   -791    480   1087  A    N  
ATOM   2843  CA  TYR A1160       2.176  -8.763 -12.177  1.00 74.76      A    C  
ANISOU 2843  CA  TYR A1160     8027  14088   6291   -847    474    943  A    C  
ATOM   2844  C   TYR A1160       2.868  -9.684 -13.172  1.00 78.27      A    C  
ANISOU 2844  C   TYR A1160     8390  14724   6626   -900    474    966  A    C  
ATOM   2845  O   TYR A1160       2.215 -10.544 -13.774  1.00 77.02      A    O  
ANISOU 2845  O   TYR A1160     8183  14677   6405   -806    428   1001  A    O  
ATOM   2846  CB  TYR A1160       1.301  -9.555 -11.181  1.00 73.93      A    C  
ANISOU 2846  CB  TYR A1160     7859  14026   6204   -719    417    852  A    C  
ATOM   2847  CG  TYR A1160       0.888  -8.738  -9.980  1.00 75.03      A    C  
ANISOU 2847  CG  TYR A1160     8049  14015   6445   -686    423    781  A    C  
ATOM   2848  CD1 TYR A1160       1.709  -8.644  -8.862  1.00 76.87      A    C  
ANISOU 2848  CD1 TYR A1160     8244  14251   6712   -764    445    644  A    C  
ATOM   2849  CD2 TYR A1160      -0.314  -8.036  -9.969  1.00 75.91      A    C  
ANISOU 2849  CD2 TYR A1160     8238  13993   6612   -572    404    842  A    C  
ATOM   2850  CE1 TYR A1160       1.342  -7.880  -7.758  1.00 77.83      A    C  
ANISOU 2850  CE1 TYR A1160     8404  14248   6921   -737    452    562  A    C  
ATOM   2851  CE2 TYR A1160      -0.686  -7.257  -8.874  1.00 77.06      A    C  
ANISOU 2851  CE2 TYR A1160     8426  14002   6853   -538    411    762  A    C  
ATOM   2852  CZ  TYR A1160       0.144  -7.189  -7.768  1.00 84.17      A    C  
ANISOU 2852  CZ  TYR A1160     9286  14910   7785   -625    437    619  A    C  
ATOM   2853  OH  TYR A1160      -0.204  -6.428  -6.684  1.00 87.48      A    O  
ANISOU 2853  OH  TYR A1160     9736  15210   8291   -594    444    522  A    O  
CONECT    1    2
CONECT    2    1    3    5
CONECT    3    2    4    4    6
CONECT    4    3    3
CONECT    5    2
CONECT    6    3    7   12
CONECT    7    6    8   10
CONECT    8    7    9    9   13
CONECT    9    8    8
CONECT   10    7   11
CONECT   11   10   12
CONECT   12    6   11
CONECT   13    8   14   19
CONECT   14   13   15   17
CONECT   15   14   16   16   20
CONECT   16   15   15
CONECT   17   14   18
CONECT   18   17   19
CONECT   19   13   18
CONECT   20   15   21
CONECT   21   20   22   24
CONECT   22   21   23   23   28
CONECT   23   22   22
CONECT   24   21   25
CONECT   25   24   26
CONECT   26   25   27
CONECT   27   26
CONECT   28   22   29
CONECT   29   28   30   32
CONECT   30   29   31   31   37
CONECT   31   30   30
CONECT   32   29   33
CONECT   33   32   34
CONECT   34   33   35
CONECT   35   34   36
CONECT   36   35
CONECT   37   30   38
CONECT   38   37   39   41
CONECT   39   38   40   40   45
CONECT   40   39   39
CONECT   41   38   42
CONECT   42   41   43   43   44
CONECT   43   42   42
CONECT   44   42
CONECT   45   39   46
CONECT   46   45   47   49
CONECT   47   46   48   48   57
CONECT   48   47   47
CONECT   49   46   50
CONECT   50   49   51   51   52
CONECT   51   50   50   53
CONECT   52   50   54   54
CONECT   53   51   55   55
CONECT   54   52   52   55
CONECT   55   53   53   54   56
CONECT   56   55
CONECT   57   47   58
CONECT   58   57   59   61
CONECT   59   58   60   60   65
CONECT   60   59   59
CONECT   61   58   62
CONECT   62   61   63
CONECT   63   62   64
CONECT   64   63
CONECT   65   59   66
CONECT   66   65   67   69
CONECT   67   66   68   68   73
CONECT   68   67   67
CONECT   69   66   70   71
CONECT   70   69   72
CONECT   71   69
CONECT   72   70
CONECT   73   67   74
CONECT   74   73   75   77
CONECT   75   74   76   76   81
CONECT   76   75   75
CONECT   77   74   78
CONECT   78   77   79   80
CONECT   79   78
CONECT   80   78
CONECT   81   75   82
CONECT   82   81   83   85
CONECT   83   82   84   84   87
CONECT   84   83   83
CONECT   85   82   86
CONECT   86   85
CONECT   87   83   88
CONECT   88   87   89
CONECT   89   88   90   90   91
CONECT   90   89   89
CONECT   91   89   92   97
CONECT   92   91   93   95
CONECT   93   92   94   94   98
CONECT   94   93   93
CONECT   95   92   96
CONECT   96   95   97
CONECT   97   91   96
CONECT   98   93   99
CONECT   99   98  100  102
CONECT  100   99  101  101  107
CONECT  101  100  100
CONECT  102   99  103
CONECT  103  102  104
CONECT  104  103  106  105  105
CONECT  105  104  104
CONECT  106  104
CONECT  107  100  108
CONECT  108  107  109  111
CONECT  109  108  110  110  112
CONECT  110  109  109
CONECT  111  108
CONECT  112  109  113
CONECT  113  112  114  116
CONECT  114  113  115  115  119
CONECT  115  114  114
CONECT  116  113  118  117
CONECT  117  116
CONECT  118  116
CONECT  119  114  120
CONECT  120  119  121  123
CONECT  121  120  122  122  124
CONECT  122  121  121
CONECT  123  120
CONECT  124  121  125
CONECT  125  124  126  128
CONECT  126  125  127  127  131
CONECT  127  126  126
CONECT  128  125  129  130
CONECT  129  128
CONECT  130  128
CONECT  131  126  132
CONECT  132  131  133  135
CONECT  133  132  134  134  136
CONECT  134  133  133
CONECT  135  132
CONECT  136  133  137
CONECT  137  136  138  140
CONECT  138  137  139  139  143
CONECT  139  138  138
CONECT  140  137  141  142
CONECT  141  140
CONECT  142  140
CONECT  143  138  144
CONECT  144  143  145  147
CONECT  145  144  146  146  151
CONECT  146  145  145
CONECT  147  144  148
CONECT  148  147  149  150
CONECT  149  148
CONECT  150  148
CONECT  151  145  152
CONECT  152  151  153  155
CONECT  153  152  154  154  157
CONECT  154  153  153
CONECT  155  152  156
CONECT  156  155
CONECT  157  153  158
CONECT  158  157  159  161
CONECT  159  158  160  160  164
CONECT  160  159  159
CONECT  161  158  163  162
CONECT  162  161
CONECT  163  161
CONECT  164  159  165
CONECT  165  164  166  168
CONECT  166  165  167  167  172
CONECT  167  166  166
CONECT  168  165  169
CONECT  169  168  170  171
CONECT  170  169
CONECT  171  169
CONECT  172  166  173
CONECT  173  172  174  176
CONECT  174  173  175  175  180
CONECT  175  174  174
CONECT  176  173  177
CONECT  177  176  178  179
CONECT  178  177
CONECT  179  177
CONECT  180  174  181
CONECT  181  180  182
CONECT  182  181  183  183  184
CONECT  183  182  182
CONECT  184  182  185
CONECT  185  184  186  188
CONECT  186  185  187  187  192
CONECT  187  186  186
CONECT  188  185  189
CONECT  189  188  190  191
CONECT  190  189
CONECT  191  189
CONECT  192  186  193
CONECT  193  192  194  196
CONECT  194  193  195  195  200
CONECT  195  194  194
CONECT  196  193  197
CONECT  197  196  198  199
CONECT  198  197
CONECT  199  197
CONECT  200  194  201
CONECT  201  200  202  204
CONECT  202  201  203  203  206
CONECT  203  202  202
CONECT  204  201  205
CONECT  205  204
CONECT  206  202  207
CONECT  207  206  208  210
CONECT  208  207  209  209  211
CONECT  209  208  208
CONECT  210  207
CONECT  211  208  212
CONECT  212  211  213  215
CONECT  213  212  214  214  219
CONECT  214  213  213
CONECT  215  212  216
CONECT  216  215  217  218
CONECT  217  216
CONECT  218  216
CONECT  219  213  220
CONECT  220  219  221  223
CONECT  221  220  222  222  228
CONECT  222  221  221
CONECT  223  220  224
CONECT  224  223  225
CONECT  225  224  226  226  227
CONECT  226  225  225
CONECT  227  225
CONECT  228  221  229
CONECT  229  228  230  232
CONECT  230  229  231  231  236
CONECT  231  230  230
CONECT  232  229  233
CONECT  233  232  235  234  234
CONECT  234  233  233
CONECT  235  233
CONECT  236  230  237
CONECT  237  236  238  240
CONECT  238  237  239  239  243
CONECT  239  238  238
CONECT  240  237  241  242
CONECT  241  240
CONECT  242  240
CONECT  243  238  244
CONECT  244  243  245  247
CONECT  245  244  246  246  248
CONECT  246  245  245
CONECT  247  244
CONECT  248  245  249
CONECT  249  248  250  252
CONECT  250  249  251  251  255
CONECT  251  250  250
CONECT  252  249  253  254
CONECT  253  252
CONECT  254  252
CONECT  255  250  256
CONECT  256  255  257  259
CONECT  257  256  258  258  263
CONECT  258  257  257
CONECT  259  256  260
CONECT  260  259  261  262
CONECT  261  260
CONECT  262  260
CONECT  263  257  264
CONECT  264  263  265  267
CONECT  265  264  266  266  275
CONECT  266  265  265
CONECT  267  264  268
CONECT  268  267  269  269  270
CONECT  269  268  268  271
CONECT  270  268  272  272
CONECT  271  269  273  273
CONECT  272  270  270  273
CONECT  273  271  271  272  274
CONECT  274  273
CONECT  275  265  276
CONECT  276  275  277  279
CONECT  277  276  278  278  283
CONECT  278  277  277
CONECT  279  276  280
CONECT  280  279  281  282
CONECT  281  280
CONECT  282  280
CONECT  283  277  284
CONECT  284  283  285  287
CONECT  285  284  286  286  291
CONECT  286  285  285
CONECT  287  284  288  289
CONECT  288  287  290
CONECT  289  287
CONECT  290  288
CONECT  291  285  292
CONECT  292  291  293  295
CONECT  293  292  294  294  299
CONECT  294  293  293
CONECT  295  292  296
CONECT  296  295  297  298
CONECT  297  296
CONECT  298  296
CONECT  299  293  300
CONECT  300  299  301  303
CONECT  301  300  302  302  305
CONECT  302  301  301
CONECT  303  300  304
CONECT  304  303
CONECT  305  301  306
CONECT  306  305  307  309
CONECT  307  306  308  308  311
CONECT  308  307  307
CONECT  309  306  310
CONECT  310  309
CONECT  311  307  312
CONECT  312  311  313  315
CONECT  313  312  314  314  321
CONECT  314  313  313
CONECT  315  312  316
CONECT  316  315  318  318  317
CONECT  317  316  319  319
CONECT  318  316  316  320
CONECT  319  317  317  320
CONECT  320  318  319
CONECT  321  313  322
CONECT  322  321  323  325
CONECT  323  322  324  324  330
CONECT  324  323  323
CONECT  325  322  326
CONECT  326  325  327
CONECT  327  326  329  328  328
CONECT  328  327  327
CONECT  329  327
CONECT  330  323  331
CONECT  331  330  332  334
CONECT  332  331  333  333  338
CONECT  333  332  332
CONECT  334  331  335
CONECT  335  334  336  337
CONECT  336  335
CONECT  337  335
CONECT  338  332  339
CONECT  339  338  340  342
CONECT  340  339  341  341  349
CONECT  341  340  340
CONECT  342  339  343
CONECT  343  342  344
CONECT  344  343  345
CONECT  345  344  346
CONECT  346  345  347  347  348
CONECT  347  346  346
CONECT  348  346
CONECT  349  340  350
CONECT  350  349  351  353
CONECT  351  350  352  352  354
CONECT  352  351  351
CONECT  353  350
CONECT  354  351  355
CONECT  355  354  356  358
CONECT  356  355  357  357  363
CONECT  357  356  356
CONECT  358  355  359
CONECT  359  358  360
CONECT  360  359  361
CONECT  361  360  362
CONECT  362  361
CONECT  363  356  364  369
CONECT  364  363  365  367
CONECT  365  364  366  366  370
CONECT  366  365  365
CONECT  367  364  368
CONECT  368  367  369
CONECT  369  363  368
CONECT  370  365  371
CONECT  371  370  372  374
CONECT  372  371  373  373  376
CONECT  373  372  372
CONECT  374  371  375
CONECT  375  374
CONECT  376  372  377
CONECT  377  376  378  380
CONECT  378  377  379  379  388
CONECT  379  378  378
CONECT  380  377  381
CONECT  381  380  382  382  383
CONECT  382  381  381  384
CONECT  383  381  385  385
CONECT  384  382  386  386
CONECT  385  383  383  386
CONECT  386  384  384  385  387
CONECT  387  386
CONECT  388  378  389
CONECT  389  388  390  392
CONECT  390  389  391  391  396
CONECT  391  390  390
CONECT  392  389  393
CONECT  393  392  394  395
CONECT  394  393
CONECT  395  393
CONECT  396  390  397
CONECT  397  396  398  400
CONECT  398  397  399  399  407
CONECT  399  398  398
CONECT  400  397  401
CONECT  401  400  402  402  403
CONECT  402  401  401  404
CONECT  403  401  405  405
CONECT  404  402  406  406
CONECT  405  403  403  406
CONECT  406  404  404  405
CONECT  407  398  408
CONECT  408  407  409  411
CONECT  409  408  410  410  415
CONECT  410  409  409
CONECT  411  408  412  413
CONECT  412  411  414
CONECT  413  411
CONECT  414  412
CONECT  415  409  416
CONECT  416  415  417
CONECT  417  416  418  418  419
CONECT  418  417  417
CONECT  419  417  420
CONECT  420  419  421  423
CONECT  421  420  422  422  425
CONECT  422  421  421
CONECT  423  420  424
CONECT  424  423
CONECT  425  421  426
CONECT  426  425  427  429
CONECT  427  426  428  428  433
CONECT  428  427  427
CONECT  429  426  430
CONECT  430  429  431  432
CONECT  431  430
CONECT  432  430
CONECT  433  427  434
CONECT  434  433  435  437
CONECT  435  434  436  436  438
CONECT  436  435  435
CONECT  437  434
CONECT  438  435  439
CONECT  439  438  440  442
CONECT  440  439  441  441  446
CONECT  441  440  440
CONECT  442  439  443
CONECT  443  442  444  445
CONECT  444  443
CONECT  445  443
CONECT  446  440  447
CONECT  447  446  448  450
CONECT  448  447  449  449  451
CONECT  449  448  448
CONECT  450  447
CONECT  451  448  452
CONECT  452  451  453  455
CONECT  453  452  454  454  459
CONECT  454  453  453
CONECT  455  452  456
CONECT  456  455  457  457  458
CONECT  457  456  456
CONECT  458  456
CONECT  459  453  460
CONECT  460  459  461  463
CONECT  461  460  462  462  470
CONECT  462  461  461
CONECT  463  460  464
CONECT  464  463  465  465  466
CONECT  465  464  464  467
CONECT  466  464  468  468
CONECT  467  465  469  469
CONECT  468  466  466  469
CONECT  469  467  467  468
CONECT  470  461  471
CONECT  471  470  472  474
CONECT  472  471  473  473  478
CONECT  473  472  472
CONECT  474  471  475
CONECT  475  474  476  477
CONECT  476  475
CONECT  477  475
CONECT  478  472  479
CONECT  479  478  480  482
CONECT  480  479  481  481  483
CONECT  481  480  480
CONECT  482  479
CONECT  483  480  484
CONECT  484  483  485  487
CONECT  485  484  486  486  489
CONECT  486  485  485
CONECT  487  484  488
CONECT  488  487
CONECT  489  485  490
CONECT  490  489  491  493
CONECT  491  490  492  492  496
CONECT  492  491  491
CONECT  493  490  494  495
CONECT  494  493
CONECT  495  493
CONECT  496  491  497
CONECT  497  496  498  500
CONECT  498  497  499  499  503
CONECT  499  498  498
CONECT  500  497  501  502
CONECT  501  500
CONECT  502  500
CONECT  503  498  504
CONECT  504  503  505  507
CONECT  505  504  506  506  514
CONECT  506  505  505
CONECT  507  504  508
CONECT  508  507  509  509  510
CONECT  509  508  508  511
CONECT  510  508  512  512
CONECT  511  509  513  513
CONECT  512  510  510  513
CONECT  513  511  511  512
CONECT  514  505  515
CONECT  515  514  516  518
CONECT  516  515  517  517  519
CONECT  517  516  516
CONECT  518  515
CONECT  519  516  520
CONECT  520  519  521  523
CONECT  521  520  522  522  525
CONECT  522  521  521
CONECT  523  520  524
CONECT  524  523
CONECT  525  521  526
CONECT  526  525  527  529
CONECT  527  526  528  528  531
CONECT  528  527  527
CONECT  529  526  530
CONECT  530  529
CONECT  531  527  532
CONECT  532  531  533  535
CONECT  533  532  534  534  542
CONECT  534  533  533
CONECT  535  532  536
CONECT  536  535  537  537  538
CONECT  537  536  536  539
CONECT  538  536  540  540
CONECT  539  537  541  541
CONECT  540  538  538  541
CONECT  541  539  539  540
CONECT  542  533  543
CONECT  543  542  544  546
CONECT  544  543  545  545  549
CONECT  545  544  544
CONECT  546  543  547  548
CONECT  547  546
CONECT  548  546
CONECT  549  544  550
CONECT  550  549  551  553
CONECT  551  550  552  552  557
CONECT  552  551  551
CONECT  553  550  554
CONECT  554  553  556  555  555
CONECT  555  554  554
CONECT  556  554
CONECT  557  551  558
CONECT  558  557  559  561
CONECT  559  558  560  560  568
CONECT  560  559  559
CONECT  561  558  562
CONECT  562  561  563  563  564
CONECT  563  562  562  565
CONECT  564  562  566  566
CONECT  565  563  567  567
CONECT  566  564  564  567
CONECT  567  565  565  566
CONECT  568  559  569
CONECT  569  568  570  572
CONECT  570  569  571  571  578
CONECT  571  570  570
CONECT  572  569  573
CONECT  573  572  575  575  574
CONECT  574  573  576  576
CONECT  575  573  573  577
CONECT  576  574  574  577
CONECT  577  575  576
CONECT  578  570  579
CONECT  579  578  580  582
CONECT  580  579  581  581  585
CONECT  581  580  580
CONECT  582  579  583  584
CONECT  583  582
CONECT  584  582
CONECT  585  580  586
CONECT  586  585  587  589
CONECT  587  586  588  588  596
CONECT  588  587  587
CONECT  589  586  590
CONECT  590  589  591  591  592
CONECT  591  590  590  593
CONECT  592  590  594  594
CONECT  593  591  595  595
CONECT  594  592  592  595
CONECT  595  593  593  594
CONECT  596  587  597
CONECT  597  596  598  600
CONECT  598  597  599  599  606
CONECT  599  598  598
CONECT  600  597  601
CONECT  601  600  603  603  602
CONECT  602  601  604  604
CONECT  603  601  601  605
CONECT  604  602  602  605
CONECT  605  603  604
CONECT  606  598  607
CONECT  607  606  608
CONECT  608  607  609  609  610
CONECT  609  608  608
CONECT  610  608  611
CONECT  611  610  612  614
CONECT  612  611  613  613  617
CONECT  613  612  612
CONECT  614  611  615  616
CONECT  615  614
CONECT  616  614
CONECT  617  612  618
CONECT  618  617  619  621
CONECT  619  618  620  620  625
CONECT  620  619  619
CONECT  621  618  622
CONECT  622  621  623  623  624
CONECT  623  622  622
CONECT  624  622
CONECT  625  619  626
CONECT  626  625  627  629
CONECT  627  626  628  628  631
CONECT  628  627  627
CONECT  629  626  630
CONECT  630  629
CONECT  631  627  632
CONECT  632  631  633  635
CONECT  633  632  634  634  640
CONECT  634  633  633
CONECT  635  632  636
CONECT  636  635  637
CONECT  637  636  638
CONECT  638  637  639
CONECT  639  638
CONECT  640  633  641
CONECT  641  640  642  644
CONECT  642  641  643  643  645
CONECT  643  642  642
CONECT  644  641
CONECT  645  642  646
CONECT  646  645  647  649
CONECT  647  646  648  648  652
CONECT  648  647  647
CONECT  649  646  650  651
CONECT  650  649
CONECT  651  649
CONECT  652  647  653
CONECT  653  652  654  656
CONECT  654  653  655  655  663
CONECT  655  654  654
CONECT  656  653  657
CONECT  657  656  658  658  659
CONECT  658  657  657  660
CONECT  659  657  661  661
CONECT  660  658  662  662
CONECT  661  659  659  662
CONECT  662  660  660  661
CONECT  663  654  664
CONECT  664  663  665  667
CONECT  665  664  666  666  671
CONECT  666  665  665
CONECT  667  664  668
CONECT  668  667  669  670
CONECT  669  668
CONECT  670  668
CONECT  671  665  672
CONECT  672  671  673  675
CONECT  673  672  674  674  679
CONECT  674  673  673
CONECT  675  672  676
CONECT  676  675  677  678
CONECT  677  676
CONECT  678  676
CONECT  679  673  680
CONECT  680  679  681  683
CONECT  681  680  682  682  688
CONECT  682  681  681
CONECT  683  680  684
CONECT  684  683  685
CONECT  685  684  686
CONECT  686  685  687
CONECT  687  686
CONECT  688  681  689
CONECT  689  688  690  692
CONECT  690  689  691  691  696
CONECT  691  690  690
CONECT  692  689  693  694
CONECT  693  692  695
CONECT  694  692
CONECT  695  693
CONECT  696  690  697
CONECT  697  696  698
CONECT  698  697  699  699  700
CONECT  699  698  698
CONECT  700  698  701
CONECT  701  700  702  704
CONECT  702  701  703  703  706
CONECT  703  702  702
CONECT  704  701  705
CONECT  705  704
CONECT  706  702  707
CONECT  707  706  708  710
CONECT  708  707  709  709  713
CONECT  709  708  708
CONECT  710  707  711  712
CONECT  711  710
CONECT  712  710
CONECT  713  708  714
CONECT  714  713  715  717
CONECT  715  714  716  716  720
CONECT  716  715  715
CONECT  717  714  719  718
CONECT  718  717
CONECT  719  717
CONECT  720  715  721
CONECT  721  720  722  724
CONECT  722  721  723  723  728
CONECT  723  722  722
CONECT  724  721  725
CONECT  725  724  726
CONECT  726  725  727
CONECT  727  726
CONECT  728  722  729
CONECT  729  728  730  732
CONECT  730  729  731  731  735
CONECT  731  730  730
CONECT  732  729  734  733
CONECT  733  732
CONECT  734  732
CONECT  735  730  736
CONECT  736  735  737  739
CONECT  737  736  738  738  746
CONECT  738  737  737
CONECT  739  736  740
CONECT  740  739  741  741  742
CONECT  741  740  740  743
CONECT  742  740  744  744
CONECT  743  741  745  745
CONECT  744  742  742  745
CONECT  745  743  743  744
CONECT  746  737  747
CONECT  747  746  748  750
CONECT  748  747  749  749  753
CONECT  749  748  748
CONECT  750  747  752  751
CONECT  751  750
CONECT  752  750
CONECT  753  748  754
CONECT  754  753  755  757
CONECT  755  754  756  756  758
CONECT  756  755  755
CONECT  757  754
CONECT  758  755  759
CONECT  759  758  760  762
CONECT  760  759  761  761  764
CONECT  761  760  760
CONECT  762  759  763
CONECT  763  762
CONECT  764  760  765
CONECT  765  764  766  768
CONECT  766  765  767  767  771
CONECT  767  766  766
CONECT  768  765  769  770
CONECT  769  768
CONECT  770  768
CONECT  771  766  772
CONECT  772  771  773
CONECT  773  772  774  774  775
CONECT  774  773  773
CONECT  775  773  776
CONECT  776  775  777  779
CONECT  777  776  778  778  781
CONECT  778  777  777
CONECT  779  776  780
CONECT  780  779
CONECT  781  777  782
CONECT  782  781  783  785
CONECT  783  782  784  784  789
CONECT  784  783  783
CONECT  785  782  786
CONECT  786  785  787  788
CONECT  787  786
CONECT  788  786
CONECT  789  783  790
CONECT  790  789  791  793
CONECT  791  790  792  792  797
CONECT  792  791  791
CONECT  793  790  794
CONECT  794  793  795  796
CONECT  795  794
CONECT  796  794
CONECT  797  791  798
CONECT  798  797  799  801
CONECT  799  798  800  800  805
CONECT  800  799  799
CONECT  801  798  802
CONECT  802  801  803  804
CONECT  803  802
CONECT  804  802
CONECT  805  799  806
CONECT  806  805  807  809
CONECT  807  806  808  808  810
CONECT  808  807  807
CONECT  809  806
CONECT  810  807  811
CONECT  811  810  812  814
CONECT  812  811  813  813  815
CONECT  813  812  812
CONECT  814  811
CONECT  815  812  816
CONECT  816  815  817  819
CONECT  817  816  818  818  823
CONECT  818  817  817
CONECT  819  816  820  821
CONECT  820  819  822
CONECT  821  819
CONECT  822  820
CONECT  823  817  824
CONECT  824  823  825  827
CONECT  825  824  826  826  831
CONECT  826  825  825
CONECT  827  824  828
CONECT  828  827  829  829  830
CONECT  829  828  828
CONECT  830  828
CONECT  831  825  832
CONECT  832  831  833  835
CONECT  833  832  834  834  842
CONECT  834  833  833
CONECT  835  832  836
CONECT  836  835  837
CONECT  837  836  838
CONECT  838  837  839
CONECT  839  838  840  840  841
CONECT  840  839  839
CONECT  841  839
CONECT  842  833  843
CONECT  843  842  844  846
CONECT  844  843  845  845  854
CONECT  845  844  844
CONECT  846  843  847
CONECT  847  846  848  848  849
CONECT  848  847  847  850
CONECT  849  847  851  851
CONECT  850  848  852  852
CONECT  851  849  849  852
CONECT  852  850  850  851  853
CONECT  853  852
CONECT  854  844  855
CONECT  855  854  856  858
CONECT  856  855  857  857  862
CONECT  857  856  856
CONECT  858  855  859
CONECT  859  858  860  861
CONECT  860  859
CONECT  861  859
CONECT  862  856  863
CONECT  863  862  864  866
CONECT  864  863  865  865  868
CONECT  865  864  864
CONECT  866  863  867
CONECT  867  866
CONECT  868  864  869
CONECT  869  868  870  872
CONECT  870  869  871  871  876
CONECT  871  870  870
CONECT  872  869  873
CONECT  873  872  874  875
CONECT  874  873
CONECT  875  873
CONECT  876  870  877
CONECT  877  876  878  880
CONECT  878  877  879  879  887
CONECT  879  878  878
CONECT  880  877  881
CONECT  881  880  882
CONECT  882  881  883
CONECT  883  882  884
CONECT  884  883  885  885  886
CONECT  885  884  884
CONECT  886  884
CONECT  887  878  888
CONECT  888  887  889  891
CONECT  889  888  890  890  899
CONECT  890  889  889
CONECT  891  888  892
CONECT  892  891  893  893  894
CONECT  893  892  892  895
CONECT  894  892  896  896
CONECT  895  893  897  897
CONECT  896  894  894  897
CONECT  897  895  895  896  898
CONECT  898  897
CONECT  899  889  900  905
CONECT  900  899  901  903
CONECT  901  900  902  902  906
CONECT  902  901  901
CONECT  903  900  904
CONECT  904  903  905
CONECT  905  899  904
CONECT  906  901  907  912
CONECT  907  906  908  910
CONECT  908  907  909  909  913
CONECT  909  908  908
CONECT  910  907  911
CONECT  911  910  912
CONECT  912  906  911
CONECT  913  908  914
CONECT  914  913  915  917
CONECT  915  914  916  916  919
CONECT  916  915  915
CONECT  917  914  918
CONECT  918  917
CONECT  919  915  920
CONECT  920  919  921  923
CONECT  921  920  922  922  931
CONECT  922  921  921
CONECT  923  920  924
CONECT  924  923  925  925  926
CONECT  925  924  924  927
CONECT  926  924  928  928
CONECT  927  925  929  929
CONECT  928  926  926  929
CONECT  929  927  927  928  930
CONECT  930  929
CONECT  931  921  932
CONECT  932  931  933  935
CONECT  933  932  934  934  940
CONECT  934  933  933
CONECT  935  932  936
CONECT  936  935  937
CONECT  937  936  938
CONECT  938  937  939
CONECT  939  938
CONECT  940  933  941
CONECT  941  940  942  944
CONECT  942  941  943  943  945
CONECT  943  942  942
CONECT  944  941
CONECT  945  942  946
CONECT  946  945  947  949
CONECT  947  946  948  948  950
CONECT  948  947  947
CONECT  949  946
CONECT  950  947  951
CONECT  951  950  952  954
CONECT  952  951  953  953  955
CONECT  953  952  952
CONECT  954  951
CONECT  955  952  956
CONECT  956  955  957  959
CONECT  957  956  958  958  962
CONECT  958  957  957
CONECT  959  956  961  960
CONECT  960  959
CONECT  961  959
CONECT  962  957  963
CONECT  963  962  964  966
CONECT  964  963  965  965  973
CONECT  965  964  964
CONECT  966  963  967
CONECT  967  966  968
CONECT  968  967  969
CONECT  969  968  970
CONECT  970  969  971  971  972
CONECT  971  970  970
CONECT  972  970
CONECT  973  964  974
CONECT  974  973  975
CONECT  975  974  976  976  977
CONECT  976  975  975
CONECT  977  975  978
CONECT  978  977  979  981
CONECT  979  978  980  980  988
CONECT  980  979  979
CONECT  981  978  982
CONECT  982  981  983
CONECT  983  982  984
CONECT  984  983  985
CONECT  985  984  986  986  987
CONECT  986  985  985
CONECT  987  985
CONECT  988  979  989
CONECT  989  988  990  992
CONECT  990  989  991  991  993
CONECT  991  990  990
CONECT  992  989
CONECT  993  990  994
CONECT  994  993  995  997
CONECT  995  994  996  996 1001
CONECT  996  995  995
CONECT  997  994  998
CONECT  998  997  999 1000
CONECT  999  998
CONECT 1000  998
CONECT 1001  995 1002
CONECT 1002 1001 1003 1005
CONECT 1003 1002 1004 1004 1008
CONECT 1004 1003 1003
CONECT 1005 1002 1006 1007
CONECT 1006 1005
CONECT 1007 1005
CONECT 1008 1003 1009
CONECT 1009 1008 1010 1012
CONECT 1010 1009 1011 1011 1016
CONECT 1011 1010 1010
CONECT 1012 1009 1013
CONECT 1013 1012 1014 1015
CONECT 1014 1013
CONECT 1015 1013
CONECT 1016 1010 1017
CONECT 1017 1016 1018 1020
CONECT 1018 1017 1019 1019 1024
CONECT 1019 1018 1018
CONECT 1020 1017 1021
CONECT 1021 1020 1022 1023
CONECT 1022 1021
CONECT 1023 1021
CONECT 1024 1018 1025
CONECT 1025 1024 1026
CONECT 1026 1025 1027 1027 1028
CONECT 1027 1026 1026
CONECT 1028 1026 1029
CONECT 1029 1028 1030 1032
CONECT 1030 1029 1031 1031 1036
CONECT 1031 1030 1030
CONECT 1032 1029 1033 1034
CONECT 1033 1032 1035
CONECT 1034 1032
CONECT 1035 1033
CONECT 1036 1030 1037
CONECT 1037 1036 1038 1040
CONECT 1038 1037 1039 1039 1044
CONECT 1039 1038 1038
CONECT 1040 1037 1041
CONECT 1041 1040 1042
CONECT 1042 1041 1043
CONECT 1043 1042
CONECT 1044 1038 1045
CONECT 1045 1044 1046 1048
CONECT 1046 1045 1047 1047 1058
CONECT 1047 1046 1046
CONECT 1048 1045 1049
CONECT 1049 1048 1050 1050 1051
CONECT 1050 1049 1049 1052
CONECT 1051 1049 1053 1053 1054
CONECT 1052 1050 1053
CONECT 1053 1051 1051 1055 1052
CONECT 1054 1051 1056 1056
CONECT 1055 1053 1057 1057
CONECT 1056 1054 1054 1057
CONECT 1057 1055 1055 1056
CONECT 1058 1046 1059
CONECT 1059 1058 1060 1062
CONECT 1060 1059 1061 1061 1065
CONECT 1061 1060 1060
CONECT 1062 1059 1063 1064
CONECT 1063 1062
CONECT 1064 1062
CONECT 1065 1060 1066
CONECT 1066 1065 1067 1069
CONECT 1067 1066 1068 1068 1073
CONECT 1068 1067 1067
CONECT 1069 1066 1070
CONECT 1070 1069 1071 1072
CONECT 1071 1070
CONECT 1072 1070
CONECT 1073 1067 1074
CONECT 1074 1073 1075 1077
CONECT 1075 1074 1076 1076 1079
CONECT 1076 1075 1075
CONECT 1077 1074 1078
CONECT 1078 1077
CONECT 1079 1075 1080
CONECT 1080 1079 1081 1083
CONECT 1081 1080 1082 1082 1084
CONECT 1082 1081 1081
CONECT 1083 1080
CONECT 1084 1081 1085
CONECT 1085 1084 1086 1088
CONECT 1086 1085 1087 1087 1092
CONECT 1087 1086 1086
CONECT 1088 1085 1089
CONECT 1089 1088 1090 1091
CONECT 1090 1089
CONECT 1091 1089
CONECT 1092 1086 1093
CONECT 1093 1092 1094 1096
CONECT 1094 1093 1095 1095 1099
CONECT 1095 1094 1094
CONECT 1096 1093 1097 1098
CONECT 1097 1096
CONECT 1098 1096
CONECT 1099 1094 1100
CONECT 1100 1099 1101 1103
CONECT 1101 1100 1102 1102 1105
CONECT 1102 1101 1101
CONECT 1103 1100 1104
CONECT 1104 1103
CONECT 1105 1101 1106
CONECT 1106 1105 1107 1109
CONECT 1107 1106 1108 1108 1117
CONECT 1108 1107 1107
CONECT 1109 1106 1110
CONECT 1110 1109 1111 1111 1112
CONECT 1111 1110 1110 1113
CONECT 1112 1110 1114 1114
CONECT 1113 1111 1115 1115
CONECT 1114 1112 1112 1115
CONECT 1115 1113 1113 1114 1116
CONECT 1116 1115
CONECT 1117 1107 1118
CONECT 1118 1117 1119 1121
CONECT 1119 1118 1120 1120 1125
CONECT 1120 1119 1119
CONECT 1121 1118 1122
CONECT 1122 1121 1123 1124
CONECT 1123 1122
CONECT 1124 1122
CONECT 1125 1119 1126 1131
CONECT 1126 1125 1127 1129
CONECT 1127 1126 1128 1128 1132
CONECT 1128 1127 1127
CONECT 1129 1126 1130
CONECT 1130 1129 1131
CONECT 1131 1125 1130
CONECT 1132 1127 1133
CONECT 1133 1132 1134 1136
CONECT 1134 1133 1135 1135 1140
CONECT 1135 1134 1134
CONECT 1136 1133 1137
CONECT 1137 1136 1138 1139
CONECT 1138 1137
CONECT 1139 1137
CONECT 1140 1134 1141
CONECT 1141 1140 1142 1144
CONECT 1142 1141 1143 1143 1148
CONECT 1143 1142 1142
CONECT 1144 1141 1145
CONECT 1145 1144 1146
CONECT 1146 1145 1147
CONECT 1147 1146
CONECT 1148 1142 1149
CONECT 1149 1148 1150
CONECT 1150 1149 1151 1151 1152
CONECT 1151 1150 1150
CONECT 1152 1150 1153
CONECT 1153 1152 1154 1156
CONECT 1154 1153 1155 1155 1166
CONECT 1155 1154 1154
CONECT 1156 1153 1157
CONECT 1157 1156 1158 1158 1159
CONECT 1158 1157 1157 1160
CONECT 1159 1157 1161 1161 1162
CONECT 1160 1158 1161
CONECT 1161 1159 1159 1163 1160
CONECT 1162 1159 1164 1164
CONECT 1163 1161 1165 1165
CONECT 1164 1162 1162 1165
CONECT 1165 1163 1163 1164
CONECT 1166 1154 1167
CONECT 1167 1166 1168 1170
CONECT 1168 1167 1169 1169 1173
CONECT 1169 1168 1168
CONECT 1170 1167 1172 1171
CONECT 1171 1170
CONECT 1172 1170
CONECT 1173 1168 1174
CONECT 1174 1173 1175 1177
CONECT 1175 1174 1176 1176 1179
CONECT 1176 1175 1175
CONECT 1177 1174 1178
CONECT 1178 1177 1215
CONECT 1179 1175 1180
CONECT 1180 1179 1181 1183
CONECT 1181 1180 1182 1182 1185
CONECT 1182 1181 1181
CONECT 1183 1180 1184
CONECT 1184 1183
CONECT 1185 1181 1186 1191
CONECT 1186 1185 1187 1189
CONECT 1187 1186 1188 1188 1192
CONECT 1188 1187 1187
CONECT 1189 1186 1190
CONECT 1190 1189 1191
CONECT 1191 1185 1190
CONECT 1192 1187 1193
CONECT 1193 1192 1194 1196
CONECT 1194 1193 1195 1195 1203
CONECT 1195 1194 1194
CONECT 1196 1193 1197
CONECT 1197 1196 1198
CONECT 1198 1197 1199
CONECT 1199 1198 1200
CONECT 1200 1199 1201 1201 1202
CONECT 1201 1200 1200
CONECT 1202 1200
CONECT 1203 1194 1204 1209
CONECT 1204 1203 1205 1207
CONECT 1205 1204 1206 1206 1210
CONECT 1206 1205 1205
CONECT 1207 1204 1208
CONECT 1208 1207 1209
CONECT 1209 1203 1208
CONECT 1210 1205 1211
CONECT 1211 1210 1212 1214
CONECT 1212 1211 1213 1213 1216
CONECT 1213 1212 1212
CONECT 1214 1211 1215
CONECT 1215 1178 1214
CONECT 1216 1212 1217
CONECT 1217 1216 1218 1220
CONECT 1218 1217 1219 1219 1222
CONECT 1219 1218 1218
CONECT 1220 1217 1221
CONECT 1221 1220
CONECT 1222 1218 1223
CONECT 1223 1222 1224 1226
CONECT 1224 1223 1225 1225 1231
CONECT 1225 1224 1224
CONECT 1226 1223 1227
CONECT 1227 1226 1228
CONECT 1228 1227 1229 1229 1230
CONECT 1229 1228 1228
CONECT 1230 1228
CONECT 1231 1224 1232
CONECT 1232 1231 1233 1235
CONECT 1233 1232 1234 1234 1239
CONECT 1234 1233 1233
CONECT 1235 1232 1236
CONECT 1236 1235 1237 1238
CONECT 1237 1236
CONECT 1238 1236
CONECT 1239 1233 1240
CONECT 1240 1239 1241 1243
CONECT 1241 1240 1242 1242 1250
CONECT 1242 1241 1241
CONECT 1243 1240 1244
CONECT 1244 1243 1245 1245 1246
CONECT 1245 1244 1244 1247
CONECT 1246 1244 1248 1248
CONECT 1247 1245 1249 1249
CONECT 1248 1246 1246 1249
CONECT 1249 1247 1247 1248
CONECT 1250 1241 1251 1256
CONECT 1251 1250 1252 1254
CONECT 1252 1251 1253 1253 1257
CONECT 1253 1252 1252
CONECT 1254 1251 1255
CONECT 1255 1254 1256
CONECT 1256 1250 1255
CONECT 1257 1252 1258
CONECT 1258 1257 1259 1261
CONECT 1259 1258 1260 1260 1265
CONECT 1260 1259 1259
CONECT 1261 1258 1262
CONECT 1262 1261 1263 1264
CONECT 1263 1262
CONECT 1264 1262
CONECT 1265 1259 1266
CONECT 1266 1265 1267 1269
CONECT 1267 1266 1268 1268 1273
CONECT 1268 1267 1267
CONECT 1269 1266 1270 1271
CONECT 1270 1269 1272
CONECT 1271 1269
CONECT 1272 1270
CONECT 1273 1267 1274 1279
CONECT 1274 1273 1275 1277
CONECT 1275 1274 1276 1276 1280
CONECT 1276 1275 1275
CONECT 1277 1274 1278
CONECT 1278 1277 1279
CONECT 1279 1273 1278
CONECT 1280 1275 1281
CONECT 1281 1280 1282 1284
CONECT 1282 1281 1283 1283 1288
CONECT 1283 1282 1282
CONECT 1284 1281 1285
CONECT 1285 1284 1287 1286 1286
CONECT 1286 1285 1285
CONECT 1287 1285
CONECT 1288 1282 1289
CONECT 1289 1288 1290 1292
CONECT 1290 1289 1291 1291 1296
CONECT 1291 1290 1290
CONECT 1292 1289 1293
CONECT 1293 1292 1294 1294 1295
CONECT 1294 1293 1293
CONECT 1295 1293
CONECT 1296 1290 1297
CONECT 1297 1296 1298 1300
CONECT 1298 1297 1299 1299 1308
CONECT 1299 1298 1298
CONECT 1300 1297 1301
CONECT 1301 1300 1302 1302 1303
CONECT 1302 1301 1301 1304
CONECT 1303 1301 1305 1305
CONECT 1304 1302 1306 1306
CONECT 1305 1303 1303 1306
CONECT 1306 1304 1304 1305 1307
CONECT 1307 1306
CONECT 1308 1298 1309
CONECT 1309 1308 1310 1312
CONECT 1310 1309 1311 1311 1316
CONECT 1311 1310 1310
CONECT 1312 1309 1313
CONECT 1313 1312 1314 1315
CONECT 1314 1313
CONECT 1315 1313
CONECT 1316 1310 1317
CONECT 1317 1316 1318 1320
CONECT 1318 1317 1319 1319 1324
CONECT 1319 1318 1318
CONECT 1320 1317 1321
CONECT 1321 1320 1322 1323
CONECT 1322 1321
CONECT 1323 1321
CONECT 1324 1318 1325
CONECT 1325 1324 1326 1328
CONECT 1326 1325 1327 1327 1330
CONECT 1327 1326 1326
CONECT 1328 1325 1329
CONECT 1329 1328
CONECT 1330 1326 1331
CONECT 1331 1330 1332 1334
CONECT 1332 1331 1333 1333 1344
CONECT 1333 1332 1332
CONECT 1334 1331 1335
CONECT 1335 1334 1336 1336 1337
CONECT 1336 1335 1335 1338
CONECT 1337 1335 1339 1339 1340
CONECT 1338 1336 1339
CONECT 1339 1337 1337 1341 1338
CONECT 1340 1337 1342 1342
CONECT 1341 1339 1343 1343
CONECT 1342 1340 1340 1343
CONECT 1343 1341 1341 1342
CONECT 1344 1332 1345
CONECT 1345 1344 1346 1348
CONECT 1346 1345 1347 1347 1352
CONECT 1347 1346 1346
CONECT 1348 1345 1349
CONECT 1349 1348 1350 1351
CONECT 1350 1349
CONECT 1351 1349
CONECT 1352 1346 1353
CONECT 1353 1352 1354 1356
CONECT 1354 1353 1355 1355 1360
CONECT 1355 1354 1354
CONECT 1356 1353 1357
CONECT 1357 1356 1358 1359
CONECT 1358 1357
CONECT 1359 1357
CONECT 1360 1354 1361
CONECT 1361 1360 1362 1364
CONECT 1362 1361 1363 1363 1371
CONECT 1363 1362 1362
CONECT 1364 1361 1365
CONECT 1365 1364 1366 1366 1367
CONECT 1366 1365 1365 1368
CONECT 1367 1365 1369 1369
CONECT 1368 1366 1370 1370
CONECT 1369 1367 1367 1370
CONECT 1370 1368 1368 1369
CONECT 1371 1362 1372
CONECT 1372 1371 1373 1375
CONECT 1373 1372 1374 1374 1379
CONECT 1374 1373 1373
CONECT 1375 1372 1376 1377
CONECT 1376 1375 1378
CONECT 1377 1375
CONECT 1378 1376
CONECT 1379 1373 1380
CONECT 1380 1379 1381 1383
CONECT 1381 1380 1382 1382 1384
CONECT 1382 1381 1381
CONECT 1383 1380
CONECT 1384 1381 1385 1386
CONECT 1385 1384 1387 1389
CONECT 1386 1384 1387 1390
CONECT 1387 1385 1386 1388 1388
CONECT 1387 1403
CONECT 1388 1387 1387
CONECT 1389 1385 1391
CONECT 1390 1386 1392
CONECT 1391 1389 1393 1393 1395
CONECT 1392 1390 1394 1394 1396
CONECT 1393 1391 1391 1397
CONECT 1394 1392 1392 1398
CONECT 1395 1391 1399 1399
CONECT 1396 1392 1400 1400
CONECT 1397 1393 1401 1401
CONECT 1398 1394 1402 1402
CONECT 1399 1395 1395 1401
CONECT 1400 1396 1396 1402
CONECT 1401 1397 1397 1399
CONECT 1402 1398 1398 1400
CONECT 1403 1387 1404
CONECT 1404 1403 1405 1407
CONECT 1405 1404 1406 1406 1411
CONECT 1406 1405 1405
CONECT 1407 1404 1408
CONECT 1408 1407 1409 1410
CONECT 1409 1408
CONECT 1410 1408
CONECT 1411 1405 1412
CONECT 1412 1411 1413 1415
CONECT 1413 1412 1414 1414 1422
CONECT 1414 1413 1413
CONECT 1415 1412 1416
CONECT 1416 1415 1417 1417 1418
CONECT 1417 1416 1416 1419
CONECT 1418 1416 1420 1420
CONECT 1419 1417 1421 1421
CONECT 1420 1418 1418 1421
CONECT 1421 1419 1419 1420
CONECT 1422 1413 1423
CONECT 1423 1422 1424 1426
CONECT 1424 1423 1425 1425 1428
CONECT 1425 1424 1424
CONECT 1426 1423 1427
CONECT 1427 1426
CONECT 1428 1424 1429
CONECT 1429 1428 1430
CONECT 1430 1429 1431 1431 1432
CONECT 1431 1430 1430
CONECT 1432 1430 1433
CONECT 1433 1432 1434 1436
CONECT 1434 1433 1435 1435 1440
CONECT 1435 1434 1434
CONECT 1436 1433 1437 1438
CONECT 1437 1436 1439
CONECT 1438 1436
CONECT 1439 1437
CONECT 1440 1434 1441
CONECT 1441 1440 1442 1444
CONECT 1442 1441 1443 1443 1448
CONECT 1443 1442 1442
CONECT 1444 1441 1445 1446
CONECT 1445 1444 1447
CONECT 1446 1444
CONECT 1447 1445
CONECT 1448 1442 1449
CONECT 1449 1448 1450 1452
CONECT 1450 1449 1451 1451 1460
CONECT 1451 1450 1450
CONECT 1452 1449 1453
CONECT 1453 1452 1454 1454 1455
CONECT 1454 1453 1453 1456
CONECT 1455 1453 1457 1457
CONECT 1456 1454 1458 1458
CONECT 1457 1455 1455 1458
CONECT 1458 1456 1456 1457 1459
CONECT 1459 1458
CONECT 1460 1450 1461
CONECT 1461 1460 1462 1464
CONECT 1462 1461 1463 1463 1467
CONECT 1463 1462 1462
CONECT 1464 1461 1466 1465
CONECT 1465 1464
CONECT 1466 1464
CONECT 1467 1462 1468
CONECT 1468 1467 1469 1471
CONECT 1469 1468 1470 1470 1479
CONECT 1470 1469 1469
CONECT 1471 1468 1472
CONECT 1472 1471 1473 1473 1474
CONECT 1473 1472 1472 1475
CONECT 1474 1472 1476 1476
CONECT 1475 1473 1477 1477
CONECT 1476 1474 1474 1477
CONECT 1477 1475 1475 1476 1478
CONECT 1478 1477
CONECT 1479 1469 1480
CONECT 1480 1479 1481
CONECT 1481 1480 1482 1482 1483
CONECT 1482 1481 1481
CONECT 1483 1481 1484
CONECT 1484 1483 1485 1487
CONECT 1485 1484 1486 1486 1493
CONECT 1486 1485 1485
CONECT 1487 1484 1488
CONECT 1488 1487 1490 1490 1489
CONECT 1489 1488 1491 1491
CONECT 1490 1488 1488 1492
CONECT 1491 1489 1489 1492
CONECT 1492 1490 1491
CONECT 1493 1485 1494
CONECT 1494 1493 1495 1497
CONECT 1495 1494 1496 1496 1500
CONECT 1496 1495 1495
CONECT 1497 1494 1498 1499
CONECT 1498 1497
CONECT 1499 1497
CONECT 1500 1495 1501
CONECT 1501 1500 1502 1504
CONECT 1502 1501 1503 1503 1508
CONECT 1503 1502 1502
CONECT 1504 1501 1505
CONECT 1505 1504 1506 1507
CONECT 1506 1505
CONECT 1507 1505
CONECT 1508 1502 1509
CONECT 1509 1508 1510 1512
CONECT 1510 1509 1511 1511 1522
CONECT 1511 1510 1510
CONECT 1512 1509 1513
CONECT 1513 1512 1514 1514 1515
CONECT 1514 1513 1513 1516
CONECT 1515 1513 1517 1517 1518
CONECT 1516 1514 1517
CONECT 1517 1515 1515 1519 1516
CONECT 1518 1515 1520 1520
CONECT 1519 1517 1521 1521
CONECT 1520 1518 1518 1521
CONECT 1521 1519 1519 1520
CONECT 1522 1510 1523
CONECT 1523 1522 1524 1526
CONECT 1524 1523 1525 1525 1531
CONECT 1525 1524 1524
CONECT 1526 1523 1527
CONECT 1527 1526 1528
CONECT 1528 1527 1529
CONECT 1529 1528 1530
CONECT 1530 1529
CONECT 1531 1524 1532
CONECT 1532 1531 1533 1535
CONECT 1533 1532 1534 1534 1536
CONECT 1534 1533 1533
CONECT 1535 1532
CONECT 1536 1533 1537
CONECT 1537 1536 1538 1540
CONECT 1538 1537 1539 1539 1546
CONECT 1539 1538 1538
CONECT 1540 1537 1541
CONECT 1541 1540 1543 1543 1542
CONECT 1542 1541 1544 1544
CONECT 1543 1541 1541 1545
CONECT 1544 1542 1542 1545
CONECT 1545 1543 1544
CONECT 1546 1538 1547
CONECT 1547 1546 1548 1550
CONECT 1548 1547 1549 1549 1555
CONECT 1549 1548 1548
CONECT 1550 1547 1551
CONECT 1551 1550 1552
CONECT 1552 1551 1554 1553 1553
CONECT 1553 1552 1552
CONECT 1554 1552
CONECT 1555 1548 1556
CONECT 1556 1555 1557 1559
CONECT 1557 1556 1558 1558 1565
CONECT 1558 1557 1557
CONECT 1559 1556 1560
CONECT 1560 1559 1562 1562 1561
CONECT 1561 1560 1563 1563
CONECT 1562 1560 1560 1564
CONECT 1563 1561 1561 1564
CONECT 1564 1562 1563
CONECT 1565 1557 1566
CONECT 1566 1565 1567 1569
CONECT 1567 1566 1568 1568 1572
CONECT 1568 1567 1567
CONECT 1569 1566 1570 1571
CONECT 1570 1569
CONECT 1571 1569
CONECT 1572 1567 1573
CONECT 1573 1572 1574 1576
CONECT 1574 1573 1575 1575 1577
CONECT 1575 1574 1574
CONECT 1576 1573
CONECT 1577 1574 1578
CONECT 1578 1577 1579 1581
CONECT 1579 1578 1580 1580 1583
CONECT 1580 1579 1579
CONECT 1581 1578 1582
CONECT 1582 1581
CONECT 1583 1579 1584
CONECT 1584 1583 1585 1587
CONECT 1585 1584 1586 1586 1591
CONECT 1586 1585 1585
CONECT 1587 1584 1588
CONECT 1588 1587 1590 1589 1589
CONECT 1589 1588 1588
CONECT 1590 1588
CONECT 1591 1585 1592
CONECT 1592 1591 1593 1595
CONECT 1593 1592 1594 1594 1599
CONECT 1594 1593 1593
CONECT 1595 1592 1596 1597
CONECT 1596 1595 1598
CONECT 1597 1595
CONECT 1598 1596
CONECT 1599 1593 1600
CONECT 1600 1599 1601 1603
CONECT 1601 1600 1602 1602 1610
CONECT 1602 1601 1601
CONECT 1603 1600 1604
CONECT 1604 1603 1605 1605 1606
CONECT 1605 1604 1604 1607
CONECT 1606 1604 1608 1608
CONECT 1607 1605 1609 1609
CONECT 1608 1606 1606 1609
CONECT 1609 1607 1607 1608
CONECT 1610 1601 1611
CONECT 1611 1610 1612 1614
CONECT 1612 1611 1613 1613 1619
CONECT 1613 1612 1612
CONECT 1614 1611 1615
CONECT 1615 1614 1616
CONECT 1616 1615 1617 1617 1618
CONECT 1617 1616 1616
CONECT 1618 1616
CONECT 1619 1612 1620
CONECT 1620 1619 1621 1623
CONECT 1621 1620 1622 1622 1627
CONECT 1622 1621 1621
CONECT 1623 1620 1624
CONECT 1624 1623 1625
CONECT 1625 1624 1626
CONECT 1626 1625
CONECT 1627 1621 1628
CONECT 1628 1627 1629 1631
CONECT 1629 1628 1630 1630 1635
CONECT 1630 1629 1629
CONECT 1631 1628 1632
CONECT 1632 1631 1633 1634
CONECT 1633 1632
CONECT 1634 1632
CONECT 1635 1629 1636
CONECT 1636 1635 1637 1639
CONECT 1637 1636 1638 1638 1646
CONECT 1638 1637 1637
CONECT 1639 1636 1640
CONECT 1640 1639 1641
CONECT 1641 1640 1642
CONECT 1642 1641 1643
CONECT 1643 1642 1644 1644 1645
CONECT 1644 1643 1643
CONECT 1645 1643
CONECT 1646 1637 1647
CONECT 1647 1646 1648 1650
CONECT 1648 1647 1649 1649 1654
CONECT 1649 1648 1648
CONECT 1650 1647 1651 1652
CONECT 1651 1650 1653
CONECT 1652 1650
CONECT 1653 1651
CONECT 1654 1648 1655
CONECT 1655 1654 1656 1658
CONECT 1656 1655 1657 1657 1662
CONECT 1657 1656 1656
CONECT 1658 1655 1659
CONECT 1659 1658 1660 1660 1661
CONECT 1660 1659 1659
CONECT 1661 1659
CONECT 1662 1656 1663
CONECT 1663 1662 1664 1666
CONECT 1664 1663 1665 1665 1671
CONECT 1665 1664 1664
CONECT 1666 1663 1667
CONECT 1667 1666 1668
CONECT 1668 1667 1669 1669 1670
CONECT 1669 1668 1668
CONECT 1670 1668
CONECT 1671 1664 1672
CONECT 1672 1671 1673
CONECT 1673 1672 1674 1674 1675
CONECT 1674 1673 1673
CONECT 1675 1673 1676
CONECT 1676 1675 1677 1679
CONECT 1677 1676 1678 1678 1683
CONECT 1678 1677 1677
CONECT 1679 1676 1680
CONECT 1680 1679 1681 1682
CONECT 1681 1680
CONECT 1682 1680
CONECT 1683 1677 1684
CONECT 1684 1683 1685 1687
CONECT 1685 1684 1686 1686 1694
CONECT 1686 1685 1685
CONECT 1687 1684 1688
CONECT 1688 1687 1689
CONECT 1689 1688 1690
CONECT 1690 1689 1691
CONECT 1691 1690 1692 1692 1693
CONECT 1692 1691 1691
CONECT 1693 1691
CONECT 1694 1685 1695
CONECT 1695 1694 1696 1698
CONECT 1696 1695 1697 1697 1702
CONECT 1697 1696 1696
CONECT 1698 1695 1699
CONECT 1699 1698 1700 1701
CONECT 1700 1699
CONECT 1701 1699
CONECT 1702 1696 1703
CONECT 1703 1702 1704 1706
CONECT 1704 1703 1705 1705 1711
CONECT 1705 1704 1704
CONECT 1706 1703 1707
CONECT 1707 1706 1708
CONECT 1708 1707 1709
CONECT 1709 1708 1710
CONECT 1710 1709
CONECT 1711 1704 1712
CONECT 1712 1711 1713 1715
CONECT 1713 1712 1714 1714 1719
CONECT 1714 1713 1713
CONECT 1715 1712 1716 1717
CONECT 1716 1715 1718
CONECT 1717 1715
CONECT 1718 1716
CONECT 1719 1713 1720
CONECT 1720 1719 1721 1723
CONECT 1721 1720 1722 1722 1731
CONECT 1722 1721 1721
CONECT 1723 1720 1724
CONECT 1724 1723 1725 1725 1726
CONECT 1725 1724 1724 1727
CONECT 1726 1724 1728 1728
CONECT 1727 1725 1729 1729
CONECT 1728 1726 1726 1729
CONECT 1729 1727 1727 1728 1730
CONECT 1730 1729
CONECT 1731 1721 1732
CONECT 1732 1731 1733 1735
CONECT 1733 1732 1734 1734 1740
CONECT 1734 1733 1733
CONECT 1735 1732 1736
CONECT 1736 1735 1737
CONECT 1737 1736 1738
CONECT 1738 1737 1739
CONECT 1739 1738
CONECT 1740 1733 1741
CONECT 1741 1740 1742 1744
CONECT 1742 1741 1743 1743 1748
CONECT 1743 1742 1742
CONECT 1744 1741 1745
CONECT 1745 1744 1746 1746 1747
CONECT 1746 1745 1745
CONECT 1747 1745
CONECT 1748 1742 1749
CONECT 1749 1748 1750 1752
CONECT 1750 1749 1751 1751 1755
CONECT 1751 1750 1750
CONECT 1752 1749 1754 1753
CONECT 1753 1752
CONECT 1754 1752
CONECT 1755 1750 1756
CONECT 1756 1755 1757 1759
CONECT 1757 1756 1758 1758 1764
CONECT 1758 1757 1757
CONECT 1759 1756 1760
CONECT 1760 1759 1761
CONECT 1761 1760 1762 1762 1763
CONECT 1762 1761 1761
CONECT 1763 1761
CONECT 1764 1757 1765
CONECT 1765 1764 1766
CONECT 1766 1765 1767 1767 1768
CONECT 1767 1766 1766
CONECT 1768 1766 1769
CONECT 1769 1768 1770 1772
CONECT 1770 1769 1771 1771 1780
CONECT 1771 1770 1770
CONECT 1772 1769 1773
CONECT 1773 1772 1774 1774 1775
CONECT 1774 1773 1773 1776
CONECT 1775 1773 1777 1777
CONECT 1776 1774 1778 1778
CONECT 1777 1775 1775 1778
CONECT 1778 1776 1776 1777 1779
CONECT 1779 1778
CONECT 1780 1770 1781
CONECT 1781 1780 1782 1784
CONECT 1782 1781 1783 1783 1792
CONECT 1783 1782 1782
CONECT 1784 1781 1785
CONECT 1785 1784 1786 1786 1787
CONECT 1786 1785 1785 1788
CONECT 1787 1785 1789 1789
CONECT 1788 1786 1790 1790
CONECT 1789 1787 1787 1790
CONECT 1790 1788 1788 1789 1791
CONECT 1791 1790
CONECT 1792 1782 1793
CONECT 1793 1792 1794 1796
CONECT 1794 1793 1795 1795 1799
CONECT 1795 1794 1794
CONECT 1796 1793 1798 1797
CONECT 1797 1796
CONECT 1798 1796
CONECT 1799 1794 1800
CONECT 1800 1799 1801 1803
CONECT 1801 1800 1802 1802 1807
CONECT 1802 1801 1801
CONECT 1803 1800 1804 1805
CONECT 1804 1803 1806
CONECT 1805 1803
CONECT 1806 1804
CONECT 1807 1801 1808
CONECT 1808 1807 1809
CONECT 1809 1808 1810 1810 1811
CONECT 1810 1809 1809
CONECT 1811 1809 1812
CONECT 1812 1811 1813 1815
CONECT 1813 1812 1814 1814 1819
CONECT 1814 1813 1813
CONECT 1815 1812 1816 1817
CONECT 1816 1815 1818
CONECT 1817 1815
CONECT 1818 1816
CONECT 1819 1813 1820
CONECT 1820 1819 1821
CONECT 1821 1820 1822 1822 1823
CONECT 1822 1821 1821
CONECT 1823 1821 1824
CONECT 1824 1823 1825 1827
CONECT 1825 1824 1826 1826 1833
CONECT 1826 1825 1825
CONECT 1827 1824 1828
CONECT 1828 1827 1830 1830 1829
CONECT 1829 1828 1831 1831
CONECT 1830 1828 1828 1832
CONECT 1831 1829 1829 1832
CONECT 1832 1830 1831
CONECT 1833 1825 1834
CONECT 1834 1833 1835 1837
CONECT 1835 1834 1836 1836 1841
CONECT 1836 1835 1835
CONECT 1837 1834 1838
CONECT 1838 1837 1839 1840
CONECT 1839 1838
CONECT 1840 1838
CONECT 1841 1835 1842
CONECT 1842 1841 1843 1845
CONECT 1843 1842 1844 1844 1849
CONECT 1844 1843 1843
CONECT 1845 1842 1846
CONECT 1846 1845 1847 1848
CONECT 1847 1846
CONECT 1848 1846
CONECT 1849 1843 1850
CONECT 1850 1849 1851 1853
CONECT 1851 1850 1852 1852 1856
CONECT 1852 1851 1851
CONECT 1853 1850 1855 1854
CONECT 1854 1853
CONECT 1855 1853
CONECT 1856 1851 1857
CONECT 1857 1856 1858 1860
CONECT 1858 1857 1859 1859 1865
CONECT 1859 1858 1858
CONECT 1860 1857 1861
CONECT 1861 1860 1862
CONECT 1862 1861 1863
CONECT 1863 1862 1864
CONECT 1864 1863
CONECT 1865 1858 1866
CONECT 1866 1865 1867 1869
CONECT 1867 1866 1868 1868 1871
CONECT 1868 1867 1867
CONECT 1869 1866 1870
CONECT 1870 1869
CONECT 1871 1867 1872 1877
CONECT 1872 1871 1873 1875
CONECT 1873 1872 1874 1874 1878
CONECT 1874 1873 1873
CONECT 1875 1872 1876
CONECT 1876 1875 1877
CONECT 1877 1871 1876
CONECT 1878 1873 1879
CONECT 1879 1878 1880 1882
CONECT 1880 1879 1881 1881 1884
CONECT 1881 1880 1880
CONECT 1882 1879 1883
CONECT 1883 1882
CONECT 1884 1880 1885
CONECT 1885 1884 1886 1888
CONECT 1886 1885 1887 1887 1892
CONECT 1887 1886 1886
CONECT 1888 1885 1889
CONECT 1889 1888 1890 1891
CONECT 1890 1889
CONECT 1891 1889
CONECT 1892 1886 1893
CONECT 1893 1892 1894 1896
CONECT 1894 1893 1895 1895 1900
CONECT 1895 1894 1894
CONECT 1896 1893 1897
CONECT 1897 1896 1899 1898 1898
CONECT 1898 1897 1897
CONECT 1899 1897
CONECT 1900 1894 1901
CONECT 1901 1900 1902 1904
CONECT 1902 1901 1903 1903 1905
CONECT 1903 1902 1902
CONECT 1904 1901
CONECT 1905 1902 1906
CONECT 1906 1905 1907 1909
CONECT 1907 1906 1908 1908 1910
CONECT 1908 1907 1907
CONECT 1909 1906
CONECT 1910 1907 1911
CONECT 1911 1910 1912 1914
CONECT 1912 1911 1913 1913 1919
CONECT 1913 1912 1912
CONECT 1914 1911 1915
CONECT 1915 1914 1916
CONECT 1916 1915 1917
CONECT 1917 1916 1918
CONECT 1918 1917
CONECT 1919 1912 1920
CONECT 1920 1919 1921 1923
CONECT 1921 1920 1922 1922 1925
CONECT 1922 1921 1921
CONECT 1923 1920 1924
CONECT 1924 1923
CONECT 1925 1921 1926
CONECT 1926 1925 1927 1929
CONECT 1927 1926 1928 1928 1934
CONECT 1928 1927 1927
CONECT 1929 1926 1930
CONECT 1930 1929 1931
CONECT 1931 1930 1932 1932 1933
CONECT 1932 1931 1931
CONECT 1933 1931
CONECT 1934 1927 1935
CONECT 1935 1934 1936 1938
CONECT 1936 1935 1937 1937 1942
CONECT 1937 1936 1936
CONECT 1938 1935 1939
CONECT 1939 1938 1940 1941
CONECT 1940 1939
CONECT 1941 1939
CONECT 1942 1936 1943
CONECT 1943 1942 1944 1946
CONECT 1944 1943 1945 1945 1950
CONECT 1945 1944 1944
CONECT 1946 1943 1947
CONECT 1947 1946 1948 1948 1949
CONECT 1948 1947 1947
CONECT 1949 1947
CONECT 1950 1944 1951
CONECT 1951 1950 1952 1954
CONECT 1952 1951 1953 1953 1955
CONECT 1953 1952 1952
CONECT 1954 1951
CONECT 1955 1952 1956
CONECT 1956 1955 1957 1959
CONECT 1957 1956 1958 1958 1960
CONECT 1958 1957 1957
CONECT 1959 1956
CONECT 1960 1957 1961
CONECT 1961 1960 1962 1964
CONECT 1962 1961 1963 1963 1968
CONECT 1963 1962 1962
CONECT 1964 1961 1965 1966
CONECT 1965 1964 1967
CONECT 1966 1964
CONECT 1967 1965
CONECT 1968 1962 1969
CONECT 1969 1968 1970
CONECT 1970 1969 1971 1971 1972
CONECT 1971 1970 1970
CONECT 1972 1970 1973
CONECT 1973 1972 1974 1976
CONECT 1974 1973 1975 1975 1983
CONECT 1975 1974 1974
CONECT 1976 1973 1977
CONECT 1977 1976 1978
CONECT 1978 1977 1979
CONECT 1979 1978 1980
CONECT 1980 1979 1981 1981 1982
CONECT 1981 1980 1980
CONECT 1982 1980
CONECT 1983 1974 1984
CONECT 1984 1983 1985 1987
CONECT 1985 1984 1986 1986 1991
CONECT 1986 1985 1985
CONECT 1987 1984 1988
CONECT 1988 1987 1990 1989 1989
CONECT 1989 1988 1988
CONECT 1990 1988
CONECT 1991 1985 1992
CONECT 1992 1991 1993 1995
CONECT 1993 1992 1994 1994 1998
CONECT 1994 1993 1993
CONECT 1995 1992 1997 1996
CONECT 1996 1995
CONECT 1997 1995
CONECT 1998 1993 1999
CONECT 1999 1998 2000 2002
CONECT 2000 1999 2001 2001 2006
CONECT 2001 2000 2000
CONECT 2002 1999 2003
CONECT 2003 2002 2005 2004 2004
CONECT 2004 2003 2003
CONECT 2005 2003
CONECT 2006 2000 2007
CONECT 2007 2006 2008
CONECT 2008 2007 2009 2009 2010
CONECT 2009 2008 2008
CONECT 2010 2008 2011
CONECT 2011 2010 2012 2014
CONECT 2012 2011 2013 2013 2017
CONECT 2013 2012 2012
CONECT 2014 2011 2015 2016
CONECT 2015 2014
CONECT 2016 2014
CONECT 2017 2012 2018
CONECT 2018 2017 2019 2021
CONECT 2019 2018 2020 2020 2025
CONECT 2020 2019 2019
CONECT 2021 2018 2022 2023
CONECT 2022 2021 2024
CONECT 2023 2021
CONECT 2024 2022
CONECT 2025 2019 2026
CONECT 2026 2025 2027 2029
CONECT 2027 2026 2028 2028 2032
CONECT 2028 2027 2027
CONECT 2029 2026 2031 2030
CONECT 2030 2029
CONECT 2031 2029
CONECT 2032 2027 2033
CONECT 2033 2032 2034 2036
CONECT 2034 2033 2035 2035 2041
CONECT 2035 2034 2034
CONECT 2036 2033 2037
CONECT 2037 2036 2038
CONECT 2038 2037 2039
CONECT 2039 2038 2040
CONECT 2040 2039
CONECT 2041 2034 2042
CONECT 2042 2041 2043 2045
CONECT 2043 2042 2044 2044 2049
CONECT 2044 2043 2043
CONECT 2045 2042 2046
CONECT 2046 2045 2047 2047 2048
CONECT 2047 2046 2046
CONECT 2048 2046
CONECT 2049 2043 2050
CONECT 2050 2049 2051 2053
CONECT 2051 2050 2052 2052 2058
CONECT 2052 2051 2051
CONECT 2053 2050 2054
CONECT 2054 2053 2055
CONECT 2055 2054 2056 2056 2057
CONECT 2056 2055 2055
CONECT 2057 2055
CONECT 2058 2051 2059
CONECT 2059 2058 2060 2062
CONECT 2060 2059 2061 2061 2063
CONECT 2061 2060 2060
CONECT 2062 2059
CONECT 2063 2060 2064
CONECT 2064 2063 2065 2067
CONECT 2065 2064 2066 2066 2072
CONECT 2066 2065 2065
CONECT 2067 2064 2068
CONECT 2068 2067 2069
CONECT 2069 2068 2070 2070 2071
CONECT 2070 2069 2069
CONECT 2071 2069
CONECT 2072 2065 2073
CONECT 2073 2072 2074 2076
CONECT 2074 2073 2075 2075 2081
CONECT 2075 2074 2074
CONECT 2076 2073 2077
CONECT 2077 2076 2078
CONECT 2078 2077 2079
CONECT 2079 2078 2080
CONECT 2080 2079
CONECT 2081 2074 2082
CONECT 2082 2081 2083 2085
CONECT 2083 2082 2084 2084 2089
CONECT 2084 2083 2083
CONECT 2085 2082 2086
CONECT 2086 2085 2087 2088
CONECT 2087 2086
CONECT 2088 2086
CONECT 2089 2083 2090
CONECT 2090 2089 2091 2093
CONECT 2091 2090 2092 2092 2100
CONECT 2092 2091 2091
CONECT 2093 2090 2094
CONECT 2094 2093 2095 2095 2096
CONECT 2095 2094 2094 2097
CONECT 2096 2094 2098 2098
CONECT 2097 2095 2099 2099
CONECT 2098 2096 2096 2099
CONECT 2099 2097 2097 2098
CONECT 2100 2091 2101
CONECT 2101 2100 2102 2104
CONECT 2102 2101 2103 2103 2108
CONECT 2103 2102 2102
CONECT 2104 2101 2105
CONECT 2105 2104 2107 2106 2106
CONECT 2106 2105 2105
CONECT 2107 2105
CONECT 2108 2102 2109
CONECT 2109 2108 2110 2112
CONECT 2110 2109 2111 2111 2117
CONECT 2111 2110 2110
CONECT 2112 2109 2113
CONECT 2113 2112 2114
CONECT 2114 2113 2116 2115 2115
CONECT 2115 2114 2114
CONECT 2116 2114
CONECT 2117 2110 2118
CONECT 2118 2117 2119 2121
CONECT 2119 2118 2120 2120 2125
CONECT 2120 2119 2119
CONECT 2121 2118 2122
CONECT 2122 2121 2123 2123 2124
CONECT 2123 2122 2122
CONECT 2124 2122
CONECT 2125 2119 2126
CONECT 2126 2125 2127 2129
CONECT 2127 2126 2128 2128 2132
CONECT 2128 2127 2127
CONECT 2129 2126 2130 2131
CONECT 2130 2129
CONECT 2131 2129
CONECT 2132 2127 2133
CONECT 2133 2132 2134 2136
CONECT 2134 2133 2135 2135 2140
CONECT 2135 2134 2134
CONECT 2136 2133 2137
CONECT 2137 2136 2138 2138 2139
CONECT 2138 2137 2137
CONECT 2139 2137
CONECT 2140 2134 2141
CONECT 2141 2140 2142 2144
CONECT 2142 2141 2143 2143 2145
CONECT 2143 2142 2142
CONECT 2144 2141
CONECT 2145 2142 2146
CONECT 2146 2145 2147 2149
CONECT 2147 2146 2148 2148 2150
CONECT 2148 2147 2147
CONECT 2149 2146
CONECT 2150 2147 2151
CONECT 2151 2150 2152 2154
CONECT 2152 2151 2153 2153 2157
CONECT 2153 2152 2152
CONECT 2154 2151 2155 2156
CONECT 2155 2154
CONECT 2156 2154
CONECT 2157 2152 2158
CONECT 2158 2157 2159 2161
CONECT 2159 2158 2160 2160 2168
CONECT 2160 2159 2159
CONECT 2161 2158 2162
CONECT 2162 2161 2163
CONECT 2163 2162 2164
CONECT 2164 2163 2165
CONECT 2165 2164 2166 2166 2167
CONECT 2166 2165 2165
CONECT 2167 2165
CONECT 2168 2159 2169
CONECT 2169 2168 2170
CONECT 2170 2169 2171 2171 2172
CONECT 2171 2170 2170
CONECT 2172 2170 2173
CONECT 2173 2172 2174 2176
CONECT 2174 2173 2175 2175 2180
CONECT 2175 2174 2174
CONECT 2176 2173 2177 2178
CONECT 2177 2176 2179
CONECT 2178 2176
CONECT 2179 2177
CONECT 2180 2174 2181
CONECT 2181 2180 2182 2184
CONECT 2182 2181 2183 2183 2188
CONECT 2183 2182 2182
CONECT 2184 2181 2185
CONECT 2185 2184 2186 2187
CONECT 2186 2185
CONECT 2187 2185
CONECT 2188 2182 2189
CONECT 2189 2188 2190 2192
CONECT 2190 2189 2191 2191 2199
CONECT 2191 2190 2190
CONECT 2192 2189 2193
CONECT 2193 2192 2194
CONECT 2194 2193 2195
CONECT 2195 2194 2196
CONECT 2196 2195 2197 2197 2198
CONECT 2197 2196 2196
CONECT 2198 2196
CONECT 2199 2190 2200
CONECT 2200 2199 2201 2203
CONECT 2201 2200 2202 2202 2207
CONECT 2202 2201 2201
CONECT 2203 2200 2204
CONECT 2204 2203 2206 2205 2205
CONECT 2205 2204 2204
CONECT 2206 2204
CONECT 2207 2201 2208
CONECT 2208 2207 2209 2211
CONECT 2209 2208 2210 2210 2212
CONECT 2210 2209 2209
CONECT 2211 2208
CONECT 2212 2209 2213
CONECT 2213 2212 2214 2216
CONECT 2214 2213 2215 2215 2221
CONECT 2215 2214 2214
CONECT 2216 2213 2217
CONECT 2217 2216 2218
CONECT 2218 2217 2219
CONECT 2219 2218 2220
CONECT 2220 2219
CONECT 2221 2214 2222
CONECT 2222 2221 2223 2225
CONECT 2223 2222 2224 2224 2229
CONECT 2224 2223 2223
CONECT 2225 2222 2226
CONECT 2226 2225 2227 2228
CONECT 2227 2226
CONECT 2228 2226
CONECT 2229 2223 2230
CONECT 2230 2229 2231 2233
CONECT 2231 2230 2232 2232 2238
CONECT 2232 2231 2231
CONECT 2233 2230 2234
CONECT 2234 2233 2235
CONECT 2235 2234 2236
CONECT 2236 2235 2237
CONECT 2237 2236
CONECT 2238 2231 2239 2244
CONECT 2239 2238 2240 2242
CONECT 2240 2239 2241 2241 2245
CONECT 2241 2240 2240
CONECT 2242 2239 2243
CONECT 2243 2242 2244
CONECT 2244 2238 2243
CONECT 2245 2240 2246
CONECT 2246 2245 2247 2249
CONECT 2247 2246 2248 2248 2252
CONECT 2248 2247 2247
CONECT 2249 2246 2250 2251
CONECT 2250 2249
CONECT 2251 2249
CONECT 2252 2247 2253
CONECT 2253 2252 2254 2256
CONECT 2254 2253 2255 2255 2264
CONECT 2255 2254 2254
CONECT 2256 2253 2257
CONECT 2257 2256 2258 2258 2259
CONECT 2258 2257 2257 2260
CONECT 2259 2257 2261 2261
CONECT 2260 2258 2262 2262
CONECT 2261 2259 2259 2262
CONECT 2262 2260 2260 2261 2263
CONECT 2263 2262
CONECT 2264 2254 2265
CONECT 2265 2264 2266 2268
CONECT 2266 2265 2267 2267 2272
CONECT 2267 2266 2266
CONECT 2268 2265 2269
CONECT 2269 2268 2270 2270 2271
CONECT 2270 2269 2269
CONECT 2271 2269
CONECT 2272 2266 2273
CONECT 2273 2272 2274 2276
CONECT 2274 2273 2275 2275 2278
CONECT 2275 2274 2274
CONECT 2276 2273 2277
CONECT 2277 2276
CONECT 2278 2274 2279
CONECT 2279 2278 2280 2282
CONECT 2280 2279 2281 2281 2286
CONECT 2281 2280 2280
CONECT 2282 2279 2283
CONECT 2283 2282 2284 2285
CONECT 2284 2283
CONECT 2285 2283
CONECT 2286 2280 2287
CONECT 2287 2286 2288 2290
CONECT 2288 2287 2289 2289 2294
CONECT 2289 2288 2288
CONECT 2290 2287 2291
CONECT 2291 2290 2292 2292 2293
CONECT 2292 2291 2291
CONECT 2293 2291
CONECT 2294 2288 2295
CONECT 2295 2294 2296 2298
CONECT 2296 2295 2297 2297 2299
CONECT 2297 2296 2296
CONECT 2298 2295
CONECT 2299 2296 2300
CONECT 2300 2299 2301 2303
CONECT 2301 2300 2302 2302 2306
CONECT 2302 2301 2301
CONECT 2303 2300 2304 2305
CONECT 2304 2303
CONECT 2305 2303
CONECT 2306 2301 2307
CONECT 2307 2306 2308 2310
CONECT 2308 2307 2309 2309 2317
CONECT 2309 2308 2308
CONECT 2310 2307 2311
CONECT 2311 2310 2312
CONECT 2312 2311 2313
CONECT 2313 2312 2314
CONECT 2314 2313 2315 2315 2316
CONECT 2315 2314 2314
CONECT 2316 2314
CONECT 2317 2308 2318
CONECT 2318 2317 2319 2321
CONECT 2319 2318 2320 2320 2328
CONECT 2320 2319 2319
CONECT 2321 2318 2322
CONECT 2322 2321 2323
CONECT 2323 2322 2324
CONECT 2324 2323 2325
CONECT 2325 2324 2326 2326 2327
CONECT 2326 2325 2325
CONECT 2327 2325
CONECT 2328 2319 2329
CONECT 2329 2328 2330 2332
CONECT 2330 2329 2331 2331 2333
CONECT 2331 2330 2330
CONECT 2332 2329
CONECT 2333 2330 2334
CONECT 2334 2333 2335 2337
CONECT 2335 2334 2336 2336 2338
CONECT 2336 2335 2335
CONECT 2337 2334
CONECT 2338 2335 2339
CONECT 2339 2338 2340 2342
CONECT 2340 2339 2341 2341 2346
CONECT 2341 2340 2340
CONECT 2342 2339 2343
CONECT 2343 2342 2344 2345
CONECT 2344 2343
CONECT 2345 2343
CONECT 2346 2340 2347
CONECT 2347 2346 2348 2350
CONECT 2348 2347 2349 2349 2354
CONECT 2349 2348 2348
CONECT 2350 2347 2351 2352
CONECT 2351 2350 2353
CONECT 2352 2350
CONECT 2353 2351
CONECT 2354 2348 2355
CONECT 2355 2354 2356 2358
CONECT 2356 2355 2357 2357 2362
CONECT 2357 2356 2356
CONECT 2358 2355 2359
CONECT 2359 2358 2361 2360 2360
CONECT 2360 2359 2359
CONECT 2361 2359
CONECT 2362 2356 2363
CONECT 2363 2362 2364 2366
CONECT 2364 2363 2365 2365 2370
CONECT 2365 2364 2364
CONECT 2366 2363 2367
CONECT 2367 2366 2368
CONECT 2368 2367 2369
CONECT 2369 2368
CONECT 2370 2364 2371
CONECT 2371 2370 2372 2374
CONECT 2372 2371 2373 2373 2377
CONECT 2373 2372 2372
CONECT 2374 2371 2375 2376
CONECT 2375 2374
CONECT 2376 2374
CONECT 2377 2372 2378
CONECT 2378 2377 2379 2381
CONECT 2379 2378 2380 2380 2388
CONECT 2380 2379 2379
CONECT 2381 2378 2382
CONECT 2382 2381 2383 2383 2384
CONECT 2383 2382 2382 2385
CONECT 2384 2382 2386 2386
CONECT 2385 2383 2387 2387
CONECT 2386 2384 2384 2387
CONECT 2387 2385 2385 2386
CONECT 2388 2379 2389
CONECT 2389 2388 2390 2392
CONECT 2390 2389 2391 2391 2397
CONECT 2391 2390 2390
CONECT 2392 2389 2393
CONECT 2393 2392 2394
CONECT 2394 2393 2396 2395 2395
CONECT 2395 2394 2394
CONECT 2396 2394
CONECT 2397 2390 2398
CONECT 2398 2397 2399 2401
CONECT 2399 2398 2400 2400 2405
CONECT 2400 2399 2399
CONECT 2401 2398 2402
CONECT 2402 2401 2403
CONECT 2403 2402 2404
CONECT 2404 2403
CONECT 2405 2399 2406
CONECT 2406 2405 2407
CONECT 2407 2406 2408 2408 2409
CONECT 2408 2407 2407
CONECT 2409 2407 2410
CONECT 2410 2409 2411 2413
CONECT 2411 2410 2412 2412 2418
CONECT 2412 2411 2411
CONECT 2413 2410 2414
CONECT 2414 2413 2415
CONECT 2415 2414 2416 2416 2417
CONECT 2416 2415 2415
CONECT 2417 2415
CONECT 2418 2411 2419
CONECT 2419 2418 2420 2422
CONECT 2420 2419 2421 2421 2425
CONECT 2421 2420 2420
CONECT 2422 2419 2424 2423
CONECT 2423 2422
CONECT 2424 2422
CONECT 2425 2420 2426
CONECT 2426 2425 2427
CONECT 2427 2426 2428 2428 2429
CONECT 2428 2427 2427
CONECT 2429 2427 2430
CONECT 2430 2429 2431 2433
CONECT 2431 2430 2432 2432 2436
CONECT 2432 2431 2431
CONECT 2433 2430 2434 2435
CONECT 2434 2433
CONECT 2435 2433
CONECT 2436 2431 2437
CONECT 2437 2436 2438 2440
CONECT 2438 2437 2439 2439 2441
CONECT 2439 2438 2438
CONECT 2440 2437
CONECT 2441 2438 2442
CONECT 2442 2441 2443
CONECT 2443 2442 2444 2444 2445
CONECT 2444 2443 2443
CONECT 2445 2443 2446
CONECT 2446 2445 2447 2449
CONECT 2447 2446 2448 2448 2456
CONECT 2448 2447 2447
CONECT 2449 2446 2450
CONECT 2450 2449 2451 2451 2452
CONECT 2451 2450 2450 2453
CONECT 2452 2450 2454 2454
CONECT 2453 2451 2455 2455
CONECT 2454 2452 2452 2455
CONECT 2455 2453 2453 2454
CONECT 2456 2447 2457
CONECT 2457 2456 2458 2460
CONECT 2458 2457 2459 2459 2463
CONECT 2459 2458 2458
CONECT 2460 2457 2462 2461
CONECT 2461 2460
CONECT 2462 2460
CONECT 2463 2458 2464
CONECT 2464 2463 2465 2467
CONECT 2465 2464 2466 2466 2471
CONECT 2466 2465 2465
CONECT 2467 2464 2468
CONECT 2468 2467 2470 2469 2469
CONECT 2469 2468 2468
CONECT 2470 2468
CONECT 2471 2465 2472
CONECT 2472 2471 2473 2475
CONECT 2473 2472 2474 2474 2477
CONECT 2474 2473 2473
CONECT 2475 2472 2476
CONECT 2476 2475
CONECT 2477 2473 2478
CONECT 2478 2477 2479 2481
CONECT 2479 2478 2480 2480 2485
CONECT 2480 2479 2479
CONECT 2481 2478 2482
CONECT 2482 2481 2483 2484
CONECT 2483 2482
CONECT 2484 2482
CONECT 2485 2479 2486
CONECT 2486 2485 2487 2489
CONECT 2487 2486 2488 2488 2496
CONECT 2488 2487 2487
CONECT 2489 2486 2490
CONECT 2490 2489 2491
CONECT 2491 2490 2492
CONECT 2492 2491 2493
CONECT 2493 2492 2494 2494 2495
CONECT 2494 2493 2493
CONECT 2495 2493
CONECT 2496 2487 2497
CONECT 2497 2496 2498 2500
CONECT 2498 2497 2499 2499 2504
CONECT 2499 2498 2498
CONECT 2500 2497 2501
CONECT 2501 2500 2502
CONECT 2502 2501 2503
CONECT 2503 2502
CONECT 2504 2498 2505
CONECT 2505 2504 2506 2508
CONECT 2506 2505 2507 2507 2512
CONECT 2507 2506 2506
CONECT 2508 2505 2509
CONECT 2509 2508 2510 2511
CONECT 2510 2509
CONECT 2511 2509
CONECT 2512 2506 2513
CONECT 2513 2512 2514 2516
CONECT 2514 2513 2515 2515 2521
CONECT 2515 2514 2514
CONECT 2516 2513 2517
CONECT 2517 2516 2518
CONECT 2518 2517 2520 2519 2519
CONECT 2519 2518 2518
CONECT 2520 2518
CONECT 2521 2514 2522
CONECT 2522 2521 2523 2525
CONECT 2523 2522 2524 2524 2530
CONECT 2524 2523 2523
CONECT 2525 2522 2526
CONECT 2526 2525 2527
CONECT 2527 2526 2529 2528 2528
CONECT 2528 2527 2527
CONECT 2529 2527
CONECT 2530 2523 2531
CONECT 2531 2530 2532 2534
CONECT 2532 2531 2533 2533 2539
CONECT 2533 2532 2532
CONECT 2534 2531 2535
CONECT 2535 2534 2536
CONECT 2536 2535 2537
CONECT 2537 2536 2538
CONECT 2538 2537
CONECT 2539 2532 2540
CONECT 2540 2539 2541 2543
CONECT 2541 2540 2542 2542 2550
CONECT 2542 2541 2541
CONECT 2543 2540 2544
CONECT 2544 2543 2545
CONECT 2545 2544 2546
CONECT 2546 2545 2547
CONECT 2547 2546 2548 2548 2549
CONECT 2548 2547 2547
CONECT 2549 2547
CONECT 2550 2541 2551
CONECT 2551 2550 2552 2554
CONECT 2552 2551 2553 2553 2564
CONECT 2553 2552 2552
CONECT 2554 2551 2555
CONECT 2555 2554 2556 2556 2557
CONECT 2556 2555 2555 2558
CONECT 2557 2555 2559 2559 2560
CONECT 2558 2556 2559
CONECT 2559 2557 2557 2561 2558
CONECT 2560 2557 2562 2562
CONECT 2561 2559 2563 2563
CONECT 2562 2560 2560 2563
CONECT 2563 2561 2561 2562
CONECT 2564 2552 2565
CONECT 2565 2564 2566 2568
CONECT 2566 2565 2567 2567 2572
CONECT 2567 2566 2566
CONECT 2568 2565 2569
CONECT 2569 2568 2570 2570 2571
CONECT 2570 2569 2569
CONECT 2571 2569
CONECT 2572 2566 2573
CONECT 2573 2572 2574 2576
CONECT 2574 2573 2575 2575 2581
CONECT 2575 2574 2574
CONECT 2576 2573 2577
CONECT 2577 2576 2578
CONECT 2578 2577 2579 2579 2580
CONECT 2579 2578 2578
CONECT 2580 2578
CONECT 2581 2574 2582
CONECT 2582 2581 2583 2585
CONECT 2583 2582 2584 2584 2586
CONECT 2584 2583 2583
CONECT 2585 2582
CONECT 2586 2583 2587
CONECT 2587 2586 2588 2590
CONECT 2588 2587 2589 2589 2591
CONECT 2589 2588 2588
CONECT 2590 2587
CONECT 2591 2588 2592
CONECT 2592 2591 2593 2595
CONECT 2593 2592 2594 2594 2598
CONECT 2594 2593 2593
CONECT 2595 2592 2596 2597
CONECT 2596 2595
CONECT 2597 2595
CONECT 2598 2593 2599
CONECT 2599 2598 2600 2602
CONECT 2600 2599 2601 2601 2606
CONECT 2601 2600 2600
CONECT 2602 2599 2603
CONECT 2603 2602 2605 2604 2604
CONECT 2604 2603 2603
CONECT 2605 2603
CONECT 2606 2600 2607
CONECT 2607 2606 2608 2610
CONECT 2608 2607 2609 2609 2614
CONECT 2609 2608 2608
CONECT 2610 2607 2611
CONECT 2611 2610 2612 2613
CONECT 2612 2611
CONECT 2613 2611
CONECT 2614 2608 2615
CONECT 2615 2614 2616 2618
CONECT 2616 2615 2617 2617 2619
CONECT 2617 2616 2616
CONECT 2618 2615
CONECT 2619 2616 2620
CONECT 2620 2619 2621 2623
CONECT 2621 2620 2622 2622 2628
CONECT 2622 2621 2621
CONECT 2623 2620 2624
CONECT 2624 2623 2625
CONECT 2625 2624 2626
CONECT 2626 2625 2627
CONECT 2627 2626
CONECT 2628 2621 2629
CONECT 2629 2628 2630 2632
CONECT 2630 2629 2631 2631 2634
CONECT 2631 2630 2630
CONECT 2632 2629 2633
CONECT 2633 2632
CONECT 2634 2630 2635
CONECT 2635 2634 2636 2638
CONECT 2636 2635 2637 2637 2645
CONECT 2637 2636 2636
CONECT 2638 2635 2639
CONECT 2639 2638 2640
CONECT 2640 2639 2641
CONECT 2641 2640 2642
CONECT 2642 2641 2643 2643 2644
CONECT 2643 2642 2642
CONECT 2644 2642
CONECT 2645 2636 2646
CONECT 2646 2645 2647 2649
CONECT 2647 2646 2648 2648 2659
CONECT 2648 2647 2647
CONECT 2649 2646 2650
CONECT 2650 2649 2651 2651 2652
CONECT 2651 2650 2650 2653
CONECT 2652 2650 2654 2654 2655
CONECT 2653 2651 2654
CONECT 2654 2652 2652 2656 2653
CONECT 2655 2652 2657 2657
CONECT 2656 2654 2658 2658
CONECT 2657 2655 2655 2658
CONECT 2658 2656 2656 2657
CONECT 2659 2647 2660
CONECT 2660 2659 2661 2663
CONECT 2661 2660 2662 2662 2671
CONECT 2662 2661 2661
CONECT 2663 2660 2664
CONECT 2664 2663 2665 2665 2666
CONECT 2665 2664 2664 2667
CONECT 2666 2664 2668 2668
CONECT 2667 2665 2669 2669
CONECT 2668 2666 2666 2669
CONECT 2669 2667 2667 2668 2670
CONECT 2670 2669
CONECT 2671 2661 2672
CONECT 2672 2671 2673 2675
CONECT 2673 2672 2674 2674 2679
CONECT 2674 2673 2673
CONECT 2675 2672 2676
CONECT 2676 2675 2678 2677 2677
CONECT 2677 2676 2676
CONECT 2678 2676
CONECT 2679 2673 2680
CONECT 2680 2679 2681 2683
CONECT 2681 2680 2682 2682 2688
CONECT 2682 2681 2681
CONECT 2683 2680 2684
CONECT 2684 2683 2685
CONECT 2685 2684 2687 2686 2686
CONECT 2686 2685 2685
CONECT 2687 2685
CONECT 2688 2681 2689
CONECT 2689 2688 2690 2692
CONECT 2690 2689 2691 2691 2695
CONECT 2691 2690 2690
CONECT 2692 2689 2694 2693
CONECT 2693 2692
CONECT 2694 2692
CONECT 2695 2690 2696 2701
CONECT 2696 2695 2697 2699
CONECT 2697 2696 2698 2698 2702
CONECT 2698 2697 2697
CONECT 2699 2696 2700
CONECT 2700 2699 2701
CONECT 2701 2695 2700
CONECT 2702 2697 2703
CONECT 2703 2702 2704 2706
CONECT 2704 2703 2705 2705 2710
CONECT 2705 2704 2704
CONECT 2706 2703 2707
CONECT 2707 2706 2709 2708 2708
CONECT 2708 2707 2707
CONECT 2709 2707
CONECT 2710 2704 2711
CONECT 2711 2710 2712 2714
CONECT 2712 2711 2713 2713 2721
CONECT 2713 2712 2712
CONECT 2714 2711 2715
CONECT 2715 2714 2716
CONECT 2716 2715 2717
CONECT 2717 2716 2718
CONECT 2718 2717 2719 2719 2720
CONECT 2719 2718 2718
CONECT 2720 2718
CONECT 2721 2712 2722
CONECT 2722 2721 2723 2725
CONECT 2723 2722 2724 2724 2726
CONECT 2724 2723 2723
CONECT 2725 2722
CONECT 2726 2723 2727
CONECT 2727 2726 2728 2730
CONECT 2728 2727 2729 2729 2735
CONECT 2729 2728 2728
CONECT 2730 2727 2731
CONECT 2731 2730 2732
CONECT 2732 2731 2733
CONECT 2733 2732 2734
CONECT 2734 2733
CONECT 2735 2728 2736
CONECT 2736 2735 2737 2739
CONECT 2737 2736 2738 2738 2746
CONECT 2738 2737 2737
CONECT 2739 2736 2740
CONECT 2740 2739 2741
CONECT 2741 2740 2742
CONECT 2742 2741 2743
CONECT 2743 2742 2744 2744 2745
CONECT 2744 2743 2743
CONECT 2745 2743
CONECT 2746 2737 2747
CONECT 2747 2746 2748 2750
CONECT 2748 2747 2749 2749 2753
CONECT 2749 2748 2748
CONECT 2750 2747 2751 2752
CONECT 2751 2750
CONECT 2752 2750
CONECT 2753 2748 2754
CONECT 2754 2753 2755 2757
CONECT 2755 2754 2756 2756 2761
CONECT 2756 2755 2755
CONECT 2757 2754 2758 2759
CONECT 2758 2757 2760
CONECT 2759 2757
CONECT 2760 2758
CONECT 2761 2755 2762
CONECT 2762 2761 2763 2765
CONECT 2763 2762 2764 2764 2768
CONECT 2764 2763 2763
CONECT 2765 2762 2767 2766
CONECT 2766 2765
CONECT 2767 2765
CONECT 2768 2763 2769
CONECT 2769 2768 2770 2772
CONECT 2770 2769 2771 2771 2775
CONECT 2771 2770 2770
CONECT 2772 2769 2774 2773
CONECT 2773 2772
CONECT 2774 2772
CONECT 2775 2770 2776
CONECT 2776 2775 2777 2779
CONECT 2777 2776 2778 2778 2786
CONECT 2778 2777 2777
CONECT 2779 2776 2780
CONECT 2780 2779 2781 2781 2782
CONECT 2781 2780 2780 2783
CONECT 2782 2780 2784 2784
CONECT 2783 2781 2785 2785
CONECT 2784 2782 2782 2785
CONECT 2785 2783 2783 2784
CONECT 2786 2777 2787
CONECT 2787 2786 2788 2790
CONECT 2788 2787 2789 2789 2797
CONECT 2789 2788 2788
CONECT 2790 2787 2791
CONECT 2791 2790 2792
CONECT 2792 2791 2793
CONECT 2793 2792 2794
CONECT 2794 2793 2795 2795 2796
CONECT 2795 2794 2794
CONECT 2796 2794
CONECT 2797 2788 2798
CONECT 2798 2797 2799 2801
CONECT 2799 2798 2800 2800 2804
CONECT 2800 2799 2799
CONECT 2801 2798 2803 2802
CONECT 2802 2801
CONECT 2803 2801
CONECT 2804 2799 2805
CONECT 2805 2804 2806
CONECT 2806 2805 2807 2807 2808
CONECT 2807 2806 2806
CONECT 2808 2806 2809
CONECT 2809 2808 2810 2812
CONECT 2810 2809 2811 2811 2815
CONECT 2811 2810 2810
CONECT 2812 2809 2814 2813
CONECT 2813 2812
CONECT 2814 2812
CONECT 2815 2810 2816
CONECT 2816 2815 2817 2819
CONECT 2817 2816 2818 2818 2829
CONECT 2818 2817 2817
CONECT 2819 2816 2820
CONECT 2820 2819 2821 2821 2822
CONECT 2821 2820 2820 2823
CONECT 2822 2820 2824 2824 2825
CONECT 2823 2821 2824
CONECT 2824 2822 2822 2826 2823
CONECT 2825 2822 2827 2827
CONECT 2826 2824 2828 2828
CONECT 2827 2825 2825 2828
CONECT 2828 2826 2826 2827
CONECT 2829 2817 2830
CONECT 2830 2829 2831 2833
CONECT 2831 2830 2832 2832 2837
CONECT 2832 2831 2831
CONECT 2833 2830 2834
CONECT 2834 2833 2835 2835 2836
CONECT 2835 2834 2834
CONECT 2836 2834
CONECT 2837 2831 2838
CONECT 2838 2837 2839 2841
CONECT 2839 2838 2840 2840 2842
CONECT 2840 2839 2839
CONECT 2841 2838
CONECT 2842 2839 2843
CONECT 2843 2842 2844 2846
CONECT 2844 2843 2854 2845 2845
CONECT 2845 2844 2844
CONECT 2846 2843 2847
CONECT 2847 2846 2848 2848 2849
CONECT 2848 2847 2847 2850
CONECT 2849 2847 2851 2851
CONECT 2850 2848 2852 2852
CONECT 2851 2849 2849 2852
CONECT 2852 2850 2850 2851 2853
CONECT 2853 2852
CONECT 2854 2855 2844
CONECT 2855 2854 2856 2858
CONECT 2856 2855 2857 2857 2859
CONECT 2857 2856 2856
CONECT 2858 2855
CONECT 2859 2856 2860
CONECT 2860 2859 2861 2863
CONECT 2861 2860 2862 2862 2870
CONECT 2862 2861 2861
CONECT 2863 2860 2864
CONECT 2864 2863 2865
CONECT 2865 2864 2866
CONECT 2866 2865 2867
CONECT 2867 2866 2868 2868 2869
CONECT 2868 2867 2867
CONECT 2869 2867
CONECT 2870 2861 2871
CONECT 2871 2870 2872 2874
CONECT 2872 2871 2873 2873 2878
CONECT 2873 2872 2872
CONECT 2874 2871 2875
CONECT 2875 2874 2876
CONECT 2876 2875 2877
CONECT 2877 2876
CONECT 2878 2872 2879
CONECT 2879 2878 2880 2882
CONECT 2880 2879 2881 2881 2889
CONECT 2881 2880 2880
CONECT 2882 2879 2883
CONECT 2883 2882 2884
CONECT 2884 2883 2885
CONECT 2885 2884 2886
CONECT 2886 2885 2887 2887 2888
CONECT 2887 2886 2886
CONECT 2888 2886
CONECT 2889 2880 2890
CONECT 2890 2889 2891 2893
CONECT 2891 2890 2892 2892 2897
CONECT 2892 2891 2891
CONECT 2893 2890 2894
CONECT 2894 2893 2895 2896
CONECT 2895 2894
CONECT 2896 2894
CONECT 2897 2891 2898
CONECT 2898 2897 2899 2901
CONECT 2899 2898 2900 2900 2905
CONECT 2900 2899 2899
CONECT 2901 2898 2902
CONECT 2902 2901 2903 2903 2904
CONECT 2903 2902 2902
CONECT 2904 2902
CONECT 2905 2899 2906
CONECT 2906 2905 2907 2909
CONECT 2907 2906 2908 2908 2912
CONECT 2908 2907 2907
CONECT 2909 2906 2910 2911
CONECT 2910 2909
CONECT 2911 2909
CONECT 2912 2907 2913
CONECT 2913 2912 2914 2916
CONECT 2914 2913 2915 2915 2921
CONECT 2915 2914 2914
CONECT 2916 2913 2917
CONECT 2917 2916 2918
CONECT 2918 2917 2919 2919 2920
CONECT 2919 2918 2918
CONECT 2920 2918
CONECT 2921 2914 2922
CONECT 2922 2921 2923 2925
CONECT 2923 2922 2924 2924 2929
CONECT 2924 2923 2923
CONECT 2925 2922 2926
CONECT 2926 2925 2927 2928
CONECT 2927 2926
CONECT 2928 2926
CONECT 2929 2923 2930
CONECT 2930 2929 2931 2933
CONECT 2931 2930 2932 2932 2934
CONECT 2932 2931 2931
CONECT 2933 2930
CONECT 2934 2931 2935
CONECT 2935 2934 2936 2938
CONECT 2936 2935 2937 2937 2943
CONECT 2937 2936 2936
CONECT 2938 2935 2939
CONECT 2939 2938 2940
CONECT 2940 2939 2941
CONECT 2941 2940 2942
CONECT 2942 2941
CONECT 2943 2936 2944
CONECT 2944 2943 2945 2947
CONECT 2945 2944 2946 2946 2950
CONECT 2946 2945 2945
CONECT 2947 2944 2949 2948
CONECT 2948 2947
CONECT 2949 2947
CONECT 2950 2945 2951
CONECT 2951 2950 2952 2954
CONECT 2952 2951 2953 2953 2958
CONECT 2953 2952 2952
CONECT 2954 2951 2955
CONECT 2955 2954 2956 2957
CONECT 2956 2955
CONECT 2957 2955
CONECT 2958 2952 2959
CONECT 2959 2958 2960
CONECT 2960 2959 2961 2961 2962
CONECT 2961 2960 2960
CONECT 2962 2960 2963
CONECT 2963 2962 2964 2966
CONECT 2964 2963 2965 2965 2970
CONECT 2965 2964 2964
CONECT 2966 2963 2967
CONECT 2967 2966 2968 2969
CONECT 2968 2967
CONECT 2969 2967
CONECT 2970 2964 2971
CONECT 2971 2970 2972 2974
CONECT 2972 2971 2973 2973 2977
CONECT 2973 2972 2972
CONECT 2974 2971 2975 2976
CONECT 2975 2974
CONECT 2976 2974
CONECT 2977 2972 2978
CONECT 2978 2977 2979 2981
CONECT 2979 2978 2980 2980 2985
CONECT 2980 2979 2979
CONECT 2981 2978 2982
CONECT 2982 2981 2983 2984
CONECT 2983 2982
CONECT 2984 2982
CONECT 2985 2979 2986
CONECT 2986 2985 2987 2989
CONECT 2987 2986 2988 2988 2990
CONECT 2988 2987 2987
CONECT 2989 2986
CONECT 2990 2987 2991
CONECT 2991 2990 2992 2994
CONECT 2992 2991 2993 2993 2997
CONECT 2993 2992 2992
CONECT 2994 2991 2995 2996
CONECT 2995 2994
CONECT 2996 2994
CONECT 2997 2992 2998
CONECT 2998 2997 2999 3001
CONECT 2999 2998 3000 3000 3005
CONECT 3000 2999 2999
CONECT 3001 2998 3002
CONECT 3002 3001 3003 3004
CONECT 3003 3002
CONECT 3004 3002
CONECT 3005 2999 3006
CONECT 3006 3005 3007 3009
CONECT 3007 3006 3008 3008 3013
CONECT 3008 3007 3007
CONECT 3009 3006 3010
CONECT 3010 3009 3011 3012
CONECT 3011 3010
CONECT 3012 3010
CONECT 3013 3007 3014
CONECT 3014 3013 3015 3017
CONECT 3015 3014 3016 3016 3021
CONECT 3016 3015 3015
CONECT 3017 3014 3018 3019
CONECT 3018 3017 3020
CONECT 3019 3017
CONECT 3020 3018
CONECT 3021 3015 3022
CONECT 3022 3021 3023 3025
CONECT 3023 3022 3024 3024 3027
CONECT 3024 3023 3023
CONECT 3025 3022 3026
CONECT 3026 3025
CONECT 3027 3023 3028
CONECT 3028 3027 3029 3031
CONECT 3029 3028 3030 3030 3041
CONECT 3030 3029 3029
CONECT 3031 3028 3032
CONECT 3032 3031 3033 3033 3034
CONECT 3033 3032 3032 3035
CONECT 3034 3032 3036 3036 3037
CONECT 3035 3033 3036
CONECT 3036 3034 3034 3038 3035
CONECT 3037 3034 3039 3039
CONECT 3038 3036 3040 3040
CONECT 3039 3037 3037 3040
CONECT 3040 3038 3038 3039
CONECT 3041 3029 3042
CONECT 3042 3041 3043 3045
CONECT 3043 3042 3044 3044 3052
CONECT 3044 3043 3043
CONECT 3045 3042 3046
CONECT 3046 3045 3047 3047 3048
CONECT 3047 3046 3046 3049
CONECT 3048 3046 3050 3050
CONECT 3049 3047 3051 3051
CONECT 3050 3048 3048 3051
CONECT 3051 3049 3049 3050
CONECT 3052 3043 3053 3058
CONECT 3053 3052 3054 3056
CONECT 3054 3053 3055 3055 3059
CONECT 3055 3054 3054
CONECT 3056 3053 3057
CONECT 3057 3056 3058
CONECT 3058 3052 3057
CONECT 3059 3054 3060
CONECT 3060 3059 3061 3063
CONECT 3061 3060 3062 3062 3066
CONECT 3062 3061 3061
CONECT 3063 3060 3064 3065
CONECT 3064 3063
CONECT 3065 3063
CONECT 3066 3061 3067
CONECT 3067 3066 3068 3070
CONECT 3068 3067 3069 3069 3074
CONECT 3069 3068 3068
CONECT 3070 3067 3071
CONECT 3071 3070 3072 3073
CONECT 3072 3071
CONECT 3073 3071
CONECT 3074 3068 3075
CONECT 3075 3074 3076 3078
CONECT 3076 3075 3077 3077 3079
CONECT 3077 3076 3076
CONECT 3078 3075
CONECT 3079 3076 3080
CONECT 3080 3079 3081 3083
CONECT 3081 3080 3082 3082 3087
CONECT 3082 3081 3081
CONECT 3083 3080 3084
CONECT 3084 3083 3085 3086
CONECT 3085 3084
CONECT 3086 3084
CONECT 3087 3081 3088
CONECT 3088 3087 3089 3091
CONECT 3089 3088 3090 3090 3095
CONECT 3090 3089 3089
CONECT 3091 3088 3092
CONECT 3092 3091 3093
CONECT 3093 3092 3094
CONECT 3094 3093
CONECT 3095 3089 3096
CONECT 3096 3095 3097 3099
CONECT 3097 3096 3098 3098 3100
CONECT 3098 3097 3097
CONECT 3099 3096
CONECT 3100 3097 3101
CONECT 3101 3100 3102 3104
CONECT 3102 3101 3103 3103 3110
CONECT 3103 3102 3102
CONECT 3104 3101 3105
CONECT 3105 3104 3107 3107 3106
CONECT 3106 3105 3108 3108
CONECT 3107 3105 3105 3109
CONECT 3108 3106 3106 3109
CONECT 3109 3107 3108
CONECT 3110 3102 3111
CONECT 3111 3110 3112 3114
CONECT 3112 3111 3113 3113 3116
CONECT 3113 3112 3112
CONECT 3114 3111 3115
CONECT 3115 3114
CONECT 3116 3112 3117
CONECT 3117 3116 3118 3120
CONECT 3118 3117 3119 3119 3124
CONECT 3119 3118 3118
CONECT 3120 3117 3121
CONECT 3121 3120 3122 3123
CONECT 3122 3121
CONECT 3123 3121
CONECT 3124 3118 3125
CONECT 3125 3124 3126 3128
CONECT 3126 3125 3127 3127 3129
CONECT 3127 3126 3126
CONECT 3128 3125
CONECT 3129 3126 3130
CONECT 3130 3129 3131 3133
CONECT 3131 3130 3132 3132 3136
CONECT 3132 3131 3131
CONECT 3133 3130 3135 3134
CONECT 3134 3133
CONECT 3135 3133
CONECT 3136 3131 3137
CONECT 3137 3136 3138 3140
CONECT 3138 3137 3139 3139 3143
CONECT 3139 3138 3138
CONECT 3140 3137 3142 3141
CONECT 3141 3140
CONECT 3142 3140
CONECT 3143 3138 3144
CONECT 3144 3143 3145 3147
CONECT 3145 3144 3146 3146 3151
CONECT 3146 3145 3145
CONECT 3147 3144 3148
CONECT 3148 3147 3149 3150
CONECT 3149 3148
CONECT 3150 3148
CONECT 3151 3145 3152
CONECT 3152 3151 3153 3155
CONECT 3153 3152 3154 3154 3157
CONECT 3154 3153 3153
CONECT 3155 3152 3156
CONECT 3156 3155
CONECT 3157 3153 3158
CONECT 3158 3157 3159 3161
CONECT 3159 3158 3160 3160 3165
CONECT 3160 3159 3159
CONECT 3161 3158 3162
CONECT 3162 3161 3163 3163 3164
CONECT 3163 3162 3162
CONECT 3164 3162
CONECT 3165 3159 3166
CONECT 3166 3165 3167 3169
CONECT 3167 3166 3168 3168 3174
CONECT 3168 3167 3167
CONECT 3169 3166 3170
CONECT 3170 3169 3171
CONECT 3171 3170 3173 3172 3172
CONECT 3172 3171 3171
CONECT 3173 3171
CONECT 3174 3167 3175
CONECT 3175 3174 3176 3178
CONECT 3176 3175 3177 3177 3181
CONECT 3177 3176 3176
CONECT 3178 3175 3179 3180
CONECT 3179 3178
CONECT 3180 3178
CONECT 3181 3176 3182
CONECT 3182 3181 3183 3185
CONECT 3183 3182 3184 3184 3190
CONECT 3184 3183 3183
CONECT 3185 3182 3186
CONECT 3186 3185 3187
CONECT 3187 3186 3188
CONECT 3188 3187 3189
CONECT 3189 3188
CONECT 3190 3183 3191
CONECT 3191 3190 3192 3194
CONECT 3192 3191 3193 3193 3199
CONECT 3193 3192 3192
CONECT 3194 3191 3195
CONECT 3195 3194 3196
CONECT 3196 3195 3197
CONECT 3197 3196 3198
CONECT 3198 3197
CONECT 3199 3192 3200
CONECT 3200 3199 3201 3203
CONECT 3201 3200 3202 3202 3204
CONECT 3202 3201 3201
CONECT 3203 3200
CONECT 3204 3201 3205
CONECT 3205 3204 3206 3208
CONECT 3206 3205 3207 3207 3215
CONECT 3207 3206 3206
CONECT 3208 3205 3209
CONECT 3209 3208 3210 3210 3211
CONECT 3210 3209 3209 3212
CONECT 3211 3209 3213 3213
CONECT 3212 3210 3214 3214
CONECT 3213 3211 3211 3214
CONECT 3214 3212 3212 3213
CONECT 3215 3206 3216
CONECT 3216 3215 3217 3219
CONECT 3217 3216 3218 3218 3220
CONECT 3218 3217 3217
CONECT 3219 3216
CONECT 3220 3217 3221
CONECT 3221 3220 3222 3224
CONECT 3222 3221 3223 3223 3231
CONECT 3223 3222 3222
CONECT 3224 3221 3225
CONECT 3225 3224 3226 3226 3227
CONECT 3226 3225 3225 3228
CONECT 3227 3225 3229 3229
CONECT 3228 3226 3230 3230
CONECT 3229 3227 3227 3230
CONECT 3230 3228 3228 3229
CONECT 3231 3222 3232
CONECT 3232 3231 3233 3235
CONECT 3233 3232 3234 3234 3237
CONECT 3234 3233 3233
CONECT 3235 3232 3236
CONECT 3236 3235
CONECT 3237 3233 3238
CONECT 3238 3237 3239 3241
CONECT 3239 3238 3240 3240 3243
CONECT 3240 3239 3239
CONECT 3241 3238 3242
CONECT 3242 3241
CONECT 3243 3239 3244
CONECT 3244 3243 3245 3247
CONECT 3245 3244 3246 3246 3251
CONECT 3246 3245 3245
CONECT 3247 3244 3248
CONECT 3248 3247 3249
CONECT 3249 3248 3250
CONECT 3250 3249
CONECT 3251 3245 3252
CONECT 3252 3251 3253 3255
CONECT 3253 3252 3254 3254 3259
CONECT 3254 3253 3253
CONECT 3255 3252 3256
CONECT 3256 3255 3257 3258
CONECT 3257 3256
CONECT 3258 3256
CONECT 3259 3253 3260
CONECT 3260 3259 3261 3263
CONECT 3261 3260 3262 3262 3265
CONECT 3262 3261 3261
CONECT 3263 3260 3264
CONECT 3264 3263
CONECT 3265 3261 3266
CONECT 3266 3265 3267 3269
CONECT 3267 3266 3268 3268 3273
CONECT 3268 3267 3267
CONECT 3269 3266 3270
CONECT 3270 3269 3271 3272
CONECT 3271 3270
CONECT 3272 3270
CONECT 3273 3267 3274
CONECT 3274 3273 3275 3277
CONECT 3275 3274 3276 3276 3281
CONECT 3276 3275 3275
CONECT 3277 3274 3278 3279
CONECT 3278 3277 3280
CONECT 3279 3277
CONECT 3280 3278
CONECT 3281 3275 3282
CONECT 3282 3281 3283 3285
CONECT 3283 3282 3284 3284 3289
CONECT 3284 3283 3283
CONECT 3285 3282 3286
CONECT 3286 3285 3288 3287 3287
CONECT 3287 3286 3286
CONECT 3288 3286
CONECT 3289 3283 3290
CONECT 3290 3289 3291 3293
CONECT 3291 3290 3292 3292 3295
CONECT 3292 3291 3291
CONECT 3293 3290 3294
CONECT 3294 3293
CONECT 3295 3291 3296
CONECT 3296 3295 3297 3299
CONECT 3297 3296 3298 3298 3303
CONECT 3298 3297 3297
CONECT 3299 3296 3300
CONECT 3300 3299 3301
CONECT 3301 3300 3302
CONECT 3302 3301
CONECT 3303 3297 3304
CONECT 3304 3303 3305 3307
CONECT 3305 3304 3306 3306 3310
CONECT 3306 3305 3305
CONECT 3307 3304 3308 3309
CONECT 3308 3307
CONECT 3309 3307
CONECT 3310 3305 3311
CONECT 3311 3310 3312 3314
CONECT 3312 3311 3313 3313 3318
CONECT 3313 3312 3312
CONECT 3314 3311 3315
CONECT 3315 3314 3317 3316 3316
CONECT 3316 3315 3315
CONECT 3317 3315
CONECT 3318 3312 3319 3324
CONECT 3319 3318 3320 3322
CONECT 3320 3319 3321 3321 3325
CONECT 3321 3320 3320
CONECT 3322 3319 3323
CONECT 3323 3322 3324
CONECT 3324 3318 3323
CONECT 3325 3320 3326
CONECT 3326 3325 3327 3329
CONECT 3327 3326 3328 3328 3332
CONECT 3328 3327 3327
CONECT 3329 3326 3330 3331
CONECT 3330 3329
CONECT 3331 3329
CONECT 3332 3327 3333
CONECT 3333 3332 3334 3336
CONECT 3334 3333 3335 3335 3340
CONECT 3335 3334 3334
CONECT 3336 3333 3337 3338
CONECT 3337 3336 3339
CONECT 3338 3336
CONECT 3339 3337
CONECT 3340 3334 3341
CONECT 3341 3340 3342 3344
CONECT 3342 3341 3343 3343 3352
CONECT 3343 3342 3342
CONECT 3344 3341 3345
CONECT 3345 3344 3346 3346 3347
CONECT 3346 3345 3345 3348
CONECT 3347 3345 3349 3349
CONECT 3348 3346 3350 3350
CONECT 3349 3347 3347 3350
CONECT 3350 3348 3348 3349 3351
CONECT 3351 3350
CONECT 3352 3342 3353
CONECT 3353 3352 3354 3356
CONECT 3354 3353 3355 3355 3357
CONECT 3355 3354 3354
CONECT 3356 3353
CONECT 3357 3354 3358
CONECT 3358 3357 3359 3361
CONECT 3359 3358 3360 3360 3365
CONECT 3360 3359 3359
CONECT 3361 3358 3362
CONECT 3362 3361 3363 3364
CONECT 3363 3362
CONECT 3364 3362
CONECT 3365 3359 3366
CONECT 3366 3365 3367 3369
CONECT 3367 3366 3368 3368 3376
CONECT 3368 3367 3367
CONECT 3369 3366 3370
CONECT 3370 3369 3371
CONECT 3371 3370 3372
CONECT 3372 3371 3373
CONECT 3373 3372 3374 3374 3375
CONECT 3374 3373 3373
CONECT 3375 3373
CONECT 3376 3367 3377
CONECT 3377 3376 3378 3380
CONECT 3378 3377 3379 3379 3382
CONECT 3379 3378 3378
CONECT 3380 3377 3381
CONECT 3381 3380
CONECT 3382 3378 3383
CONECT 3383 3382 3384 3386
CONECT 3384 3383 3385 3385 3391
CONECT 3385 3384 3384
CONECT 3386 3383 3387
CONECT 3387 3386 3388
CONECT 3388 3387 3389 3389 3390
CONECT 3389 3388 3388
CONECT 3390 3388
CONECT 3391 3384 3392
CONECT 3392 3391 3393 3395
CONECT 3393 3392 3394 3394 3400
CONECT 3394 3393 3393
CONECT 3395 3392 3396
CONECT 3396 3395 3397
CONECT 3397 3396 3398 3398 3399
CONECT 3398 3397 3397
CONECT 3399 3397
CONECT 3400 3393 3401
CONECT 3401 3400 3402 3404
CONECT 3402 3401 3403 3403 3408
CONECT 3403 3402 3402
CONECT 3404 3401 3405 3406
CONECT 3405 3404 3407
CONECT 3406 3404
CONECT 3407 3405
CONECT 3408 3402 3409
CONECT 3409 3408 3410 3412
CONECT 3410 3409 3411 3411 3419
CONECT 3411 3410 3410
CONECT 3412 3409 3413
CONECT 3413 3412 3414
CONECT 3414 3413 3415
CONECT 3415 3414 3416
CONECT 3416 3415 3417 3417 3418
CONECT 3417 3416 3416
CONECT 3418 3416
CONECT 3419 3410 3420
CONECT 3420 3419 3421 3423
CONECT 3421 3420 3422 3422 3425
CONECT 3422 3421 3421
CONECT 3423 3420 3424
CONECT 3424 3423
CONECT 3425 3421 3426
CONECT 3426 3425 3427 3429
CONECT 3427 3426 3428 3428 3431
CONECT 3428 3427 3427
CONECT 3429 3426 3430
CONECT 3430 3429
CONECT 3431 3427 3432
CONECT 3432 3431 3433 3435
CONECT 3433 3432 3434 3434 3436
CONECT 3434 3433 3433
CONECT 3435 3432
CONECT 3436 3433 3437 3438
CONECT 3437 3436 3439 3441
CONECT 3438 3436 3439 3442
CONECT 3439 3437 3438 3440 3440
CONECT 3439 3453
CONECT 3440 3439 3439
CONECT 3441 3437 3443
CONECT 3442 3438 3444
CONECT 3443 3441 3447 3447 3445
CONECT 3444 3442 3448 3448 3446
CONECT 3445 3443 3449 3449
CONECT 3446 3444 3450 3450
CONECT 3447 3443 3443 3451
CONECT 3448 3444 3444 3452
CONECT 3449 3445 3445 3451
CONECT 3450 3446 3446 3452
CONECT 3451 3447 3449
CONECT 3452 3448 3450
CONECT 3453 3439 3454
CONECT 3454 3453 3455 3457
CONECT 3455 3454 3456 3456 3463
CONECT 3456 3455 3455
CONECT 3457 3454 3458
CONECT 3458 3457 3460 3460 3459
CONECT 3459 3458 3461 3461
CONECT 3460 3458 3458 3462
CONECT 3461 3459 3459 3462
CONECT 3462 3460 3461
CONECT 3463 3455 3464
CONECT 3464 3463 3465 3467
CONECT 3465 3464 3466 3466 3469
CONECT 3466 3465 3465
CONECT 3467 3464 3468
CONECT 3468 3467
CONECT 3469 3465 3470
CONECT 3470 3469 3471 3473
CONECT 3471 3470 3472 3472 3477
CONECT 3472 3471 3471
CONECT 3473 3470 3474
CONECT 3474 3473 3475 3476
CONECT 3475 3474
CONECT 3476 3474
CONECT 3477 3471 3478
CONECT 3478 3477 3479 3481
CONECT 3479 3478 3480 3480 3482
CONECT 3480 3479 3479
CONECT 3481 3478
CONECT 3482 3479 3483
CONECT 3483 3482 3484 3486
CONECT 3484 3483 3485 3485 3492
CONECT 3485 3484 3484
CONECT 3486 3483 3487
CONECT 3487 3486 3489 3489 3488
CONECT 3488 3487 3490 3490
CONECT 3489 3487 3487 3491
CONECT 3490 3488 3488 3491
CONECT 3491 3489 3490
CONECT 3492 3484 3493
CONECT 3493 3492 3494 3496
CONECT 3494 3493 3495 3495 3506
CONECT 3495 3494 3494
CONECT 3496 3493 3497
CONECT 3497 3496 3498 3498 3499
CONECT 3498 3497 3497 3500
CONECT 3499 3497 3501 3501 3502
CONECT 3500 3498 3501
CONECT 3501 3499 3499 3503 3500
CONECT 3502 3499 3504 3504
CONECT 3503 3501 3505 3505
CONECT 3504 3502 3502 3505
CONECT 3505 3503 3503 3504
CONECT 3506 3494 3507
CONECT 3507 3506 3508 3510
CONECT 3508 3507 3509 3509 3515
CONECT 3509 3508 3508
CONECT 3510 3507 3511
CONECT 3511 3510 3512
CONECT 3512 3511 3513
CONECT 3513 3512 3514
CONECT 3514 3513
CONECT 3515 3508 3516
CONECT 3516 3515 3517 3519
CONECT 3517 3516 3518 3518
CONECT 3518 3517 3517
CONECT 3519 3516 3520
CONECT 3520 3519 3521
CONECT 3521 3520 3522
CONECT 3522 3521 3523
CONECT 3523 3522
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.