CNRS Nantes University UFIP UFIP
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***  ahw2  ***

elNémo ID: 200203201450142342

Job options:

ID        	=	 200203201450142342
JOBID     	=	 ahw2
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 ahw2

ATOM      1  N   ASP A 449     -16.130   8.418 -11.336  1.00 70.53      A    N  
ANISOU    1  N   ASP A 449     8482   9430   8885   1228    819  -1701  A    N  
ATOM      2  CA  ASP A 449     -15.729   8.054 -12.689  1.00 68.64      A    C  
ANISOU    2  CA  ASP A 449     8217   9220   8642   1303    514  -1572  A    C  
ATOM      3  C   ASP A 449     -14.210   8.112 -12.823  1.00 59.67      A    C  
ANISOU    3  C   ASP A 449     7475   7953   7245   1150    419  -1247  A    C  
ATOM      4  O   ASP A 449     -13.531   8.780 -12.043  1.00 56.49      A    O  
ANISOU    4  O   ASP A 449     7364   7416   6683   1078    493  -1147  A    O  
ATOM      5  CB  ASP A 449     -16.404   8.969 -13.716  1.00 73.37      A    C  
ANISOU    5  CB  ASP A 449     8730   9801   9347   1706    211  -1703  A    C  
ATOM      6  CG  ASP A 449     -16.532   8.320 -15.087  1.00 75.20      A    C  
ANISOU    6  CG  ASP A 449     8804  10126   9641   1807    -64  -1699  A    C  
ATOM      7  OD1 ASP A 449     -16.318   7.090 -15.191  1.00 72.34      A    O  
ANISOU    7  OD1 ASP A 449     8302   9874   9311   1558     20  -1655  A    O  
ATOM      8  OD2 ASP A 449     -16.858   9.038 -16.057  1.00 77.30      A    O1-
ANISOU    8  OD2 ASP A 449     9121  10342   9908   2149   -373  -1746  A    O1-
ATOM      9  N   TRP A 450     -13.679   7.407 -13.813  1.00 53.33      A    N  
ANISOU    9  N   TRP A 450     6658   7188   6416   1098    257  -1112  A    N  
ATOM     10  CA  TRP A 450     -12.237   7.287 -13.956  1.00 47.24      A    C  
ANISOU   10  CA  TRP A 450     6180   6317   5454    925    203   -847  A    C  
ATOM     11  C   TRP A 450     -11.725   7.980 -15.208  1.00 44.20      A    C  
ANISOU   11  C   TRP A 450     5987   5823   4983   1096    -38   -727  A    C  
ATOM     12  O   TRP A 450     -10.638   7.675 -15.696  1.00 42.61      A    O  
ANISOU   12  O   TRP A 450     5939   5570   4679    959    -85   -545  A    O  
ATOM     13  CB  TRP A 450     -11.828   5.813 -13.936  1.00 45.35      A    C  
ANISOU   13  CB  TRP A 450     5829   6177   5226    675    278   -771  A    C  
ATOM     14  CG  TRP A 450     -12.264   5.111 -12.683  1.00 46.26      A    C  
ANISOU   14  CG  TRP A 450     5858   6346   5373    486    550   -860  A    C  
ATOM     15  CD1 TRP A 450     -13.414   4.401 -12.500  1.00 47.85      A    C  
ANISOU   15  CD1 TRP A 450     5758   6669   5755    452    716  -1063  A    C  
ATOM     16  CD2 TRP A 450     -11.565   5.069 -11.434  1.00 43.42      A    C  
ANISOU   16  CD2 TRP A 450     5750   5900   4848    301    700   -764  A    C  
ATOM     17  CE2 TRP A 450     -12.347   4.311 -10.542  1.00 44.48      A    C  
ANISOU   17  CE2 TRP A 450     5783   6090   5029    164    977   -888  A    C  
ATOM     18  CE3 TRP A 450     -10.349   5.592 -10.984  1.00 39.42      A    C  
ANISOU   18  CE3 TRP A 450     5552   5267   4160    235    622   -605  A    C  
ATOM     19  NE1 TRP A 450     -13.471   3.913 -11.219  1.00 47.71      A    N  
ANISOU   19  NE1 TRP A 450     5830   6625   5672    239   1007  -1077  A    N  
ATOM     20  CZ2 TRP A 450     -11.954   4.063  -9.230  1.00 41.91      A    C  
ANISOU   20  CZ2 TRP A 450     5721   5682   4519    -11   1165   -830  A    C  
ATOM     21  CZ3 TRP A 450      -9.962   5.347  -9.683  1.00 37.42      A    C  
ANISOU   21  CZ3 TRP A 450     5506   4957   3755     78    759   -575  A    C  
ATOM     22  CH2 TRP A 450     -10.760   4.589  -8.821  1.00 38.92      A    C  
ANISOU   22  CH2 TRP A 450     5656   5189   3941    -32   1022   -672  A    C  
ATOM     23  N   GLU A 451     -12.508   8.921 -15.724  1.00 45.82      A    N  
ANISOU   23  N   GLU A 451     6207   5977   5227   1403   -179   -839  A    N  
ATOM     24  CA  GLU A 451     -12.071   9.698 -16.874  1.00 46.23      A    C  
ANISOU   24  CA  GLU A 451     6549   5872   5146   1586   -387   -715  A    C  
ATOM     25  C   GLU A 451     -11.044  10.749 -16.469  1.00 42.69      A    C  
ANISOU   25  C   GLU A 451     6486   5192   4541   1498   -315   -561  A    C  
ATOM     26  O   GLU A 451     -11.259  11.524 -15.536  1.00 44.83      A    O  
ANISOU   26  O   GLU A 451     6827   5385   4822   1530   -222   -635  A    O  
ATOM     27  CB  GLU A 451     -13.247  10.355 -17.593  1.00 53.40      A    C  
ANISOU   27  CB  GLU A 451     7400   6770   6121   1990   -611   -887  A    C  
ATOM     28  CG  GLU A 451     -12.816  11.152 -18.816  1.00 62.12      A    C  
ANISOU   28  CG  GLU A 451     8908   7668   7027   2198   -824   -738  A    C  
ATOM     29  CD  GLU A 451     -13.983  11.605 -19.662  1.00 72.10      A    C  
ANISOU   29  CD  GLU A 451    10131   8931   8332   2642  -1126   -912  A    C  
ATOM     30  OE1 GLU A 451     -15.138  11.303 -19.292  1.00 75.71      A    O  
ANISOU   30  OE1 GLU A 451    10170   9571   9026   2780  -1168  -1181  A    O  
ATOM     31  OE2 GLU A 451     -13.745  12.262 -20.699  1.00 75.84      A    O1-
ANISOU   31  OE2 GLU A 451    11002   9210   8603   2858  -1320   -794  A    O1-
ATOM     32  N   ILE A 452      -9.921  10.755 -17.175  1.00 39.01      A    N  
ANISOU   32  N   ILE A 452     6259   4614   3947   1370   -337   -369  A    N  
ATOM     33  CA  ILE A 452      -8.875  11.734 -16.947  1.00 39.02      A    C  
ANISOU   33  CA  ILE A 452     6609   4383   3835   1252   -259   -247  A    C  
ATOM     34  C   ILE A 452      -8.979  12.836 -17.992  1.00 43.46      A    C  
ANISOU   34  C   ILE A 452     7532   4711   4271   1498   -375   -187  A    C  
ATOM     35  O   ILE A 452      -8.779  12.591 -19.182  1.00 45.60      A    O  
ANISOU   35  O   ILE A 452     7928   4949   4449   1555   -461    -95  A    O  
ATOM     36  CB  ILE A 452      -7.487  11.087 -17.022  1.00 38.82      A    C  
ANISOU   36  CB  ILE A 452     6609   4360   3782    928   -166   -106  A    C  
ATOM     37  CG1 ILE A 452      -7.385   9.947 -16.005  1.00 38.57      A    C  
ANISOU   37  CG1 ILE A 452     6286   4529   3841    725    -88   -152  A    C  
ATOM     38  CG2 ILE A 452      -6.403  12.125 -16.790  1.00 38.75      A    C  
ANISOU   38  CG2 ILE A 452     6910   4109   3706    780    -75    -29  A    C  
ATOM     39  CD1 ILE A 452      -6.121   9.123 -16.123  1.00 36.97      A    C  
ANISOU   39  CD1 ILE A 452     6046   4357   3642    463    -50    -46  A    C  
ATOM     40  N   PRO A 453      -9.299  14.059 -17.545  1.00 45.32      A    N  
ANISOU   40  N   PRO A 453     7982   4759   4478   1654   -374   -239  A    N  
ATOM     41  CA  PRO A 453      -9.528  15.216 -18.418  1.00 47.55      A    C  
ANISOU   41  CA  PRO A 453     8676   4768   4623   1937   -493   -190  A    C  
ATOM     42  C   PRO A 453      -8.357  15.488 -19.350  1.00 47.38      A    C  
ANISOU   42  C   PRO A 453     9047   4524   4432   1770   -414     14  A    C  
ATOM     43  O   PRO A 453      -7.217  15.152 -19.037  1.00 45.34      A    O  
ANISOU   43  O   PRO A 453     8755   4271   4200   1410   -235     90  A    O  
ATOM     44  CB  PRO A 453      -9.693  16.372 -17.429  1.00 47.09      A    C  
ANISOU   44  CB  PRO A 453     8775   4533   4584   1997   -419   -271  A    C  
ATOM     45  CG  PRO A 453     -10.173  15.723 -16.182  1.00 45.29      A    C  
ANISOU   45  CG  PRO A 453     8128   4560   4519   1897   -330   -431  A    C  
ATOM     46  CD  PRO A 453      -9.462  14.408 -16.124  1.00 43.55      A    C  
ANISOU   46  CD  PRO A 453     7664   4551   4333   1576   -251   -353  A    C  
ATOM     47  N   ASP A 454      -8.657  16.088 -20.494  1.00 53.21      A    N  
ANISOU   47  N   ASP A 454    10163   5059   4997   2043   -549     85  A    N  
ATOM     48  CA  ASP A 454      -7.655  16.374 -21.511  1.00 55.70      A    C  
ANISOU   48  CA  ASP A 454    10920   5129   5116   1902   -433    275  A    C  
ATOM     49  C   ASP A 454      -6.562  17.287 -20.970  1.00 56.76      A    C  
ANISOU   49  C   ASP A 454    11332   4989   5245   1603   -170    343  A    C  
ATOM     50  O   ASP A 454      -6.843  18.329 -20.373  1.00 59.92      A    O  
ANISOU   50  O   ASP A 454    11921   5197   5648   1712   -168    292  A    O  
ATOM     51  CB  ASP A 454      -8.323  17.009 -22.734  1.00 62.56      A    C  
ANISOU   51  CB  ASP A 454    12248   5776   5746   2311   -644    332  A    C  
ATOM     52  CG  ASP A 454      -7.343  17.292 -23.862  1.00 67.98      A    C  
ANISOU   52  CG  ASP A 454    13470   6178   6181   2165   -479    535  A    C  
ATOM     53  OD1 ASP A 454      -6.228  16.729 -23.853  1.00 69.91      A    O  
ANISOU   53  OD1 ASP A 454    13605   6477   6481   1759   -223    603  A    O  
ATOM     54  OD2 ASP A 454      -7.696  18.073 -24.770  1.00 70.41      A    O1-
ANISOU   54  OD2 ASP A 454    14127   6329   6296   2364   -559    521  A    O1-
ATOM     55  N   GLY A 455      -5.313  16.881 -21.177  1.00 53.54      A    N  
ANISOU   55  N   GLY A 455    10923   4565   4853   1222     51    430  A    N  
ATOM     56  CA  GLY A 455      -4.172  17.688 -20.786  1.00 53.03      A    C  
ANISOU   56  CA  GLY A 455    11085   4243   4821    896    310    459  A    C  
ATOM     57  C   GLY A 455      -3.432  17.237 -19.539  1.00 49.63      A    C  
ANISOU   57  C   GLY A 455    10239   3998   4620    561    402    352  A    C  
ATOM     58  O   GLY A 455      -2.339  17.720 -19.265  1.00 51.66      A    O  
ANISOU   58  O   GLY A 455    10595   4083   4948    246    602    340  A    O  
ATOM     59  N   GLN A 456      -4.012  16.317 -18.777  1.00 46.10      A    N  
ANISOU   59  N   GLN A 456     9345   3884   4288    625    257    260  A    N  
ATOM     60  CA  GLN A 456      -3.377  15.868 -17.539  1.00 43.99      A    C  
ANISOU   60  CA  GLN A 456     8751   3776   4185    357    303    162  A    C  
ATOM     61  C   GLN A 456      -2.259  14.851 -17.769  1.00 43.09      A    C  
ANISOU   61  C   GLN A 456     8398   3803   4173     61    385    188  A    C  
ATOM     62  O   GLN A 456      -1.350  14.721 -16.950  1.00 40.74      A    O  
ANISOU   62  O   GLN A 456     7936   3539   4005   -196    433    111  A    O  
ATOM     63  CB  GLN A 456      -4.419  15.311 -16.568  1.00 38.09      A    C  
ANISOU   63  CB  GLN A 456     7694   3286   3492    525    164     56  A    C  
ATOM     64  CG  GLN A 456      -5.359  16.364 -16.012  1.00 39.96      A    C  
ANISOU   64  CG  GLN A 456     8101   3393   3689    770    118    -30  A    C  
ATOM     65  CD  GLN A 456      -6.158  15.859 -14.831  1.00 44.54      A    C  
ANISOU   65  CD  GLN A 456     8374   4206   4342    838     75   -168  A    C  
ATOM     66  NE2 GLN A 456      -7.017  16.710 -14.287  1.00 40.83      A    N  
ANISOU   66  NE2 GLN A 456     8007   3646   3862   1057     58   -276  A    N  
ATOM     67  OE1 GLN A 456      -6.003  14.713 -14.409  1.00 41.89      A    O  
ANISOU   67  OE1 GLN A 456     7738   4110   4067    696     77   -181  A    O  
ATOM     68  N   ILE A 457      -2.325  14.143 -18.892  1.00 45.05      A    N  
ANISOU   68  N   ILE A 457     8631   4125   4362    119    380    277  A    N  
ATOM     69  CA  ILE A 457      -1.358  13.095 -19.202  1.00 45.57      A    C  
ANISOU   69  CA  ILE A 457     8454   4331   4528   -118    457    288  A    C  
ATOM     70  C   ILE A 457      -0.301  13.549 -20.200  1.00 47.31      A    C  
ANISOU   70  C   ILE A 457     8934   4318   4723   -322    692    349  A    C  
ATOM     71  O   ILE A 457      -0.626  14.009 -21.290  1.00 50.38      A    O  
ANISOU   71  O   ILE A 457     9688   4528   4925   -186    749    452  A    O  
ATOM     72  CB  ILE A 457      -2.053  11.871 -19.807  1.00 46.30      A    C  
ANISOU   72  CB  ILE A 457     8341   4666   4585     45    330    323  A    C  
ATOM     73  CG1 ILE A 457      -3.096  11.311 -18.840  1.00 45.19      A    C  
ANISOU   73  CG1 ILE A 457     7919   4753   4497    199    160    243  A    C  
ATOM     74  CG2 ILE A 457      -1.032  10.811 -20.175  1.00 45.04      A    C  
ANISOU   74  CG2 ILE A 457     7960   4625   4530   -181    417    330  A    C  
ATOM     75  CD1 ILE A 457      -4.042  10.332 -19.496  1.00 45.56      A    C  
ANISOU   75  CD1 ILE A 457     7801   4995   4515    392     32    245  A    C  
ATOM     76  N   THR A 458       0.967  13.409 -19.830  1.00 47.36      A    N  
ANISOU   76  N   THR A 458     8760   4317   4916   -645    831    269  A    N  
ATOM     77  CA  THR A 458       2.057  13.701 -20.751  1.00 47.74      A    C  
ANISOU   77  CA  THR A 458     8975   4167   4996   -894   1117    284  A    C  
ATOM     78  C   THR A 458       2.586  12.414 -21.367  1.00 49.33      A    C  
ANISOU   78  C   THR A 458     8895   4570   5278   -980   1158    281  A    C  
ATOM     79  O   THR A 458       3.134  11.564 -20.672  1.00 51.21      A    O  
ANISOU   79  O   THR A 458     8717   5019   5720  -1093   1069    176  A    O  
ATOM     80  CB  THR A 458       3.220  14.418 -20.062  1.00 49.27      A    C  
ANISOU   80  CB  THR A 458     9108   4206   5405  -1225   1278    139  A    C  
ATOM     81  CG2 THR A 458       4.250  14.855 -21.102  1.00 44.16      A    C  
ANISOU   81  CG2 THR A 458     8676   3308   4796  -1503   1651    139  A    C  
ATOM     82  OG1 THR A 458       2.736  15.566 -19.353  1.00 51.07      A    O  
ANISOU   82  OG1 THR A 458     9580   4254   5571  -1150   1224    120  A    O  
ATOM     83  N   VAL A 459       2.427  12.283 -22.679  1.00 48.31      A    N  
ANISOU   83  N   VAL A 459     9031   4358   4968   -906   1282    393  A    N  
ATOM     84  CA  VAL A 459       2.825  11.074 -23.388  1.00 45.24      A    C  
ANISOU   84  CA  VAL A 459     8426   4142   4621   -956   1330    391  A    C  
ATOM     85  C   VAL A 459       4.311  11.088 -23.734  1.00 44.81      A    C  
ANISOU   85  C   VAL A 459     8281   3982   4763  -1315   1664    292  A    C  
ATOM     86  O   VAL A 459       4.829  12.078 -24.237  1.00 46.31      A    O  
ANISOU   86  O   VAL A 459     8811   3879   4906  -1488   1962    303  A    O  
ATOM     87  CB  VAL A 459       1.989  10.890 -24.664  1.00 47.63      A    C  
ANISOU   87  CB  VAL A 459     9070   4404   4621   -708   1301    529  A    C  
ATOM     88  CG1 VAL A 459       2.338   9.578 -25.356  1.00 47.70      A    C  
ANISOU   88  CG1 VAL A 459     8853   4603   4668   -748   1336    511  A    C  
ATOM     89  CG2 VAL A 459       0.509  10.942 -24.325  1.00 45.70      A    C  
ANISOU   89  CG2 VAL A 459     8859   4265   4240   -350    966    571  A    C  
ATOM     90  N   GLY A 460       4.992   9.983 -23.453  1.00 45.71      A    N  
ANISOU   90  N   GLY A 460     7933   4323   5111  -1425   1625    178  A    N  
ATOM     91  CA  GLY A 460       6.409   9.864 -23.743  1.00 46.90      A    C  
ANISOU   91  CA  GLY A 460     7890   4417   5514  -1746   1921     30  A    C  
ATOM     92  C   GLY A 460       6.668   8.863 -24.849  1.00 49.12      A    C  
ANISOU   92  C   GLY A 460     8126   4783   5756  -1742   2065     49  A    C  
ATOM     93  O   GLY A 460       5.876   8.744 -25.782  1.00 49.33      A    O  
ANISOU   93  O   GLY A 460     8493   4771   5478  -1552   2066    204  A    O  
ATOM     94  N   GLN A 461       7.773   8.133 -24.736  1.00 51.40      A    N  
ANISOU   94  N   GLN A 461     7990   5186   6355  -1931   2161   -130  A    N  
ATOM     95  CA  GLN A 461       8.211   7.235 -25.798  1.00 57.93      A    C  
ANISOU   95  CA  GLN A 461     8758   6066   7185  -1968   2363   -154  A    C  
ATOM     96  C   GLN A 461       7.229   6.094 -26.051  1.00 56.68      A    C  
ANISOU   96  C   GLN A 461     8578   6121   6837  -1669   2077    -34  A    C  
ATOM     97  O   GLN A 461       6.526   5.641 -25.143  1.00 52.39      A    O  
ANISOU   97  O   GLN A 461     7850   5753   6304  -1486   1714     -3  A    O  
ATOM     98  CB  GLN A 461       9.605   6.679 -25.490  1.00 68.23      A    C  
ANISOU   98  CB  GLN A 461     9541   7462   8921  -2203   2486   -415  A    C  
ATOM     99  CG  GLN A 461       9.604   5.446 -24.600  1.00 73.95      A    C  
ANISOU   99  CG  GLN A 461     9792   8473   9834  -2040   2091   -494  A    C  
ATOM    100  CD  GLN A 461      10.692   5.487 -23.546  1.00 81.89      A    C  
ANISOU  100  CD  GLN A 461    10332   9535  11249  -2196   1991   -751  A    C  
ATOM    101  NE2 GLN A 461      10.692   6.542 -22.738  1.00 84.05      A    N  
ANISOU  101  NE2 GLN A 461    10674   9704  11558  -2285   1927   -786  A    N  
ATOM    102  OE1 GLN A 461      11.519   4.578 -23.454  1.00 84.62      A    O  
ANISOU  102  OE1 GLN A 461    10262  10012  11878  -2218   1947   -933  A    O  
ATOM    103  N   ARG A 462       7.183   5.647 -27.301  1.00 60.00      A    N  
ANISOU  103  N   ARG A 462     9212   6507   7078  -1638   2267     21  A    N  
ATOM    104  CA  ARG A 462       6.364   4.510 -27.684  1.00 58.23      A    C  
ANISOU  104  CA  ARG A 462     8956   6470   6701  -1392   2032     93  A    C  
ATOM    105  C   ARG A 462       7.028   3.232 -27.193  1.00 54.20      A    C  
ANISOU  105  C   ARG A 462     7918   6173   6502  -1428   1929    -56  A    C  
ATOM    106  O   ARG A 462       8.236   3.060 -27.335  1.00 53.37      A    O  
ANISOU  106  O   ARG A 462     7578   6043   6656  -1635   2173   -220  A    O  
ATOM    107  CB  ARG A 462       6.200   4.460 -29.204  1.00 63.36      A    C  
ANISOU  107  CB  ARG A 462    10036   6995   7043  -1352   2267    174  A    C  
ATOM    108  CG  ARG A 462       5.273   3.358 -29.700  1.00 66.87      A    C  
ANISOU  108  CG  ARG A 462    10486   7614   7306  -1095   2008    228  A    C  
ATOM    109  CD  ARG A 462       5.614   2.964 -31.130  1.00 73.63      A    C  
ANISOU  109  CD  ARG A 462    11626   8385   7966  -1127   2289    223  A    C  
ATOM    110  NE  ARG A 462       6.990   2.482 -31.229  1.00 80.85      A    N  
ANISOU  110  NE  ARG A 462    12228   9308   9182  -1384   2618     53  A    N  
ATOM    111  CZ  ARG A 462       7.335   1.201 -31.317  1.00 82.68      A    C  
ANISOU  111  CZ  ARG A 462    12112   9713   9588  -1365   2574    -61  A    C  
ATOM    112  NH1 ARG A 462       6.404   0.255 -31.339  1.00 79.24      A    N1+
ANISOU  112  NH1 ARG A 462    11622   9444   9042  -1130   2238    -14  A    N1+
ATOM    113  NH2 ARG A 462       8.617   0.865 -31.395  1.00 85.41      A    N  
ANISOU  113  NH2 ARG A 462    12157  10055  10240  -1582   2877   -245  A    N  
ATOM    114  N   ILE A 463       6.234   2.341 -26.613  1.00 50.83      A    N  
ANISOU  114  N   ILE A 463     7313   5938   6062  -1225   1576    -16  A    N  
ATOM    115  CA  ILE A 463       6.746   1.082 -26.098  1.00 51.92      A    C  
ANISOU  115  CA  ILE A 463     7026   6248   6454  -1214   1436   -132  A    C  
ATOM    116  C   ILE A 463       6.542  -0.038 -27.116  1.00 54.83      A    C  
ANISOU  116  C   ILE A 463     7425   6685   6723  -1120   1476   -126  A    C  
ATOM    117  O   ILE A 463       7.465  -0.794 -27.412  1.00 55.29      A    O  
ANISOU  117  O   ILE A 463     7249   6777   6981  -1197   1606   -259  A    O  
ATOM    118  CB  ILE A 463       6.077   0.713 -24.756  1.00 50.28      A    C  
ANISOU  118  CB  ILE A 463     6641   6173   6291  -1077   1063    -99  A    C  
ATOM    119  CG1 ILE A 463       6.321   1.813 -23.717  1.00 49.16      A    C  
ANISOU  119  CG1 ILE A 463     6483   5959   6235  -1167   1016   -127  A    C  
ATOM    120  CG2 ILE A 463       6.575  -0.634 -24.253  1.00 49.10      A    C  
ANISOU  120  CG2 ILE A 463     6141   6157   6357  -1036    905   -198  A    C  
ATOM    121  CD1 ILE A 463       7.782   2.178 -23.527  1.00 49.75      A    C  
ANISOU  121  CD1 ILE A 463     6325   5967   6611  -1390   1186   -314  A    C  
ATOM    122  N   GLY A 464       5.331  -0.130 -27.657  1.00 55.70      A    N  
ANISOU  122  N   GLY A 464     7811   6814   6539   -945   1353      2  A    N  
ATOM    123  CA  GLY A 464       5.019  -1.127 -28.663  1.00 57.03      A    C  
ANISOU  123  CA  GLY A 464     8053   7039   6579   -848   1363     -3  A    C  
ATOM    124  C   GLY A 464       3.533  -1.402 -28.786  1.00 59.56      A    C  
ANISOU  124  C   GLY A 464     8521   7439   6670   -629   1081     87  A    C  
ATOM    125  O   GLY A 464       2.716  -0.733 -28.159  1.00 60.21      A    O  
ANISOU  125  O   GLY A 464     8668   7525   6683   -543    908    158  A    O  
ATOM    126  N   SER A 465       3.183  -2.391 -29.601  1.00 62.79      A    N  
ANISOU  126  N   SER A 465     8963   7911   6983   -540   1039     55  A    N  
ATOM    127  CA  SER A 465       1.788  -2.775 -29.788  1.00 64.20      A    C  
ANISOU  127  CA  SER A 465     9222   8179   6994   -345    764     83  A    C  
ATOM    128  C   SER A 465       1.540  -4.190 -29.283  1.00 63.50      A    C  
ANISOU  128  C   SER A 465     8810   8230   7086   -324    600     10  A    C  
ATOM    129  O   SER A 465       2.355  -5.087 -29.494  1.00 63.89      A    O  
ANISOU  129  O   SER A 465     8716   8290   7271   -396    710    -64  A    O  
ATOM    130  CB  SER A 465       1.385  -2.664 -31.262  1.00 67.72      A    C  
ANISOU  130  CB  SER A 465    10056   8556   7119   -234    807     93  A    C  
ATOM    131  OG  SER A 465       1.321  -1.311 -31.677  1.00 71.88      A    O  
ANISOU  131  OG  SER A 465    10974   8921   7416   -204    905    187  A    O  
ATOM    132  N   GLY A 466       0.407  -4.383 -28.619  1.00 62.00      A    N  
ANISOU  132  N   GLY A 466     8519   8130   6906   -229    360     19  A    N  
ATOM    133  CA  GLY A 466       0.074  -5.679 -28.059  1.00 61.73      A    C  
ANISOU  133  CA  GLY A 466     8233   8191   7032   -234    235    -42  A    C  
ATOM    134  C   GLY A 466      -1.131  -6.327 -28.710  1.00 63.14      A    C  
ANISOU  134  C   GLY A 466     8443   8442   7108   -122     73   -114  A    C  
ATOM    135  O   GLY A 466      -1.358  -6.176 -29.914  1.00 65.06      A    O  
ANISOU  135  O   GLY A 466     8904   8664   7151    -35     68   -144  A    O  
ATOM    136  N   SER A 467      -1.900  -7.056 -27.904  1.00 60.36      A    N  
ANISOU  136  N   SER A 467     7887   8161   6887   -131    -54   -157  A    N  
ATOM    137  CA  SER A 467      -3.101  -7.748 -28.370  1.00 59.26      A    C  
ANISOU  137  CA  SER A 467     7697   8096   6723    -61   -208   -275  A    C  
ATOM    138  C   SER A 467      -4.124  -6.762 -28.914  1.00 62.65      A    C  
ANISOU  138  C   SER A 467     8257   8562   6985    101   -360   -307  A    C  
ATOM    139  O   SER A 467      -4.895  -7.082 -29.820  1.00 65.17      A    O  
ANISOU  139  O   SER A 467     8622   8929   7211    210   -511   -427  A    O  
ATOM    140  CB  SER A 467      -3.715  -8.576 -27.239  1.00 55.92      A    C  
ANISOU  140  CB  SER A 467     7042   7711   6494   -146   -247   -317  A    C  
ATOM    141  OG  SER A 467      -4.913  -9.201 -27.659  1.00 54.54      A    O  
ANISOU  141  OG  SER A 467     6772   7606   6344   -113   -372   -470  A    O  
ATOM    142  N   PHE A 468      -4.128  -5.563 -28.345  1.00 63.01      A    N  
ANISOU  142  N   PHE A 468     8371   8577   6994    135   -347   -216  A    N  
ATOM    143  CA  PHE A 468      -4.906  -4.462 -28.891  1.00 64.85      A    C  
ANISOU  143  CA  PHE A 468     8793   8800   7046    326   -490   -226  A    C  
ATOM    144  C   PHE A 468      -4.357  -3.138 -28.370  1.00 61.96      A    C  
ANISOU  144  C   PHE A 468     8584   8332   6625    316   -382    -88  A    C  
ATOM    145  O   PHE A 468      -3.978  -3.029 -27.206  1.00 60.47      A    O  
ANISOU  145  O   PHE A 468     8243   8142   6591    192   -291    -36  A    O  
ATOM    146  CB  PHE A 468      -6.394  -4.613 -28.556  1.00 67.49      A    C  
ANISOU  146  CB  PHE A 468     8909   9253   7481    433   -704   -377  A    C  
ATOM    147  CG  PHE A 468      -6.748  -4.216 -27.151  1.00 70.36      A    C  
ANISOU  147  CG  PHE A 468     9080   9644   8011    370   -656   -357  A    C  
ATOM    148  CD1 PHE A 468      -6.593  -5.109 -26.102  1.00 70.53      A    C  
ANISOU  148  CD1 PHE A 468     8879   9692   8226    180   -534   -359  A    C  
ATOM    149  CD2 PHE A 468      -7.249  -2.951 -26.881  1.00 71.80      A    C  
ANISOU  149  CD2 PHE A 468     9347   9802   8130    514   -729   -338  A    C  
ATOM    150  CE1 PHE A 468      -6.921  -4.743 -24.806  1.00 69.75      A    C  
ANISOU  150  CE1 PHE A 468     8664   9602   8234    123   -470   -341  A    C  
ATOM    151  CE2 PHE A 468      -7.580  -2.579 -25.590  1.00 71.17      A    C  
ANISOU  151  CE2 PHE A 468     9110   9742   8188    457   -665   -335  A    C  
ATOM    152  CZ  PHE A 468      -7.416  -3.477 -24.551  1.00 70.55      A    C  
ANISOU  152  CZ  PHE A 468     8828   9698   8281    255   -527   -337  A    C  
ATOM    153  N   GLY A 469      -4.300  -2.143 -29.248  1.00 60.32      A    N  
ANISOU  153  N   GLY A 469     8721   8017   6178    446   -393    -32  A    N  
ATOM    154  CA  GLY A 469      -3.821  -0.825 -28.882  1.00 58.02      A    C  
ANISOU  154  CA  GLY A 469     8632   7592   5821    432   -279     88  A    C  
ATOM    155  C   GLY A 469      -2.314  -0.679 -28.952  1.00 55.72      A    C  
ANISOU  155  C   GLY A 469     8440   7184   5548    223     16    177  A    C  
ATOM    156  O   GLY A 469      -1.593  -1.646 -29.195  1.00 53.92      A    O  
ANISOU  156  O   GLY A 469     8088   6992   5408     98    131    143  A    O  
ATOM    157  N   THR A 470      -1.845   0.548 -28.734  1.00 54.34      A    N  
ANISOU  157  N   THR A 470     8473   6860   5314    183    144    266  A    N  
ATOM    158  CA  THR A 470      -0.418   0.858 -28.726  1.00 51.79      A    C  
ANISOU  158  CA  THR A 470     8206   6416   5058    -42    445    309  A    C  
ATOM    159  C   THR A 470      -0.011   1.534 -27.420  1.00 49.54      A    C  
ANISOU  159  C   THR A 470     7759   6103   4959   -164    486    327  A    C  
ATOM    160  O   THR A 470      -0.666   2.471 -26.966  1.00 52.05      A    O  
ANISOU  160  O   THR A 470     8194   6370   5214    -62    387    364  A    O  
ATOM    161  CB  THR A 470      -0.039   1.770 -29.894  1.00 52.08      A    C  
ANISOU  161  CB  THR A 470     8731   6236   4820    -29    638    382  A    C  
ATOM    162  CG2 THR A 470       1.465   2.005 -29.916  1.00 48.93      A    C  
ANISOU  162  CG2 THR A 470     8328   5716   4548   -308   1007    378  A    C  
ATOM    163  OG1 THR A 470      -0.448   1.156 -31.122  1.00 56.33      A    O  
ANISOU  163  OG1 THR A 470     9474   6792   5135    109    572    359  A    O  
ATOM    164  N   VAL A 471       1.087   1.063 -26.835  1.00 43.74      A    N  
ANISOU  164  N   VAL A 471     6765   5397   4456   -363    614    281  A    N  
ATOM    165  CA  VAL A 471       1.488   1.480 -25.498  1.00 39.08      A    C  
ANISOU  165  CA  VAL A 471     5984   4810   4054   -467    591    264  A    C  
ATOM    166  C   VAL A 471       2.588   2.533 -25.517  1.00 38.36      A    C  
ANISOU  166  C   VAL A 471     6011   4546   4019   -650    830    256  A    C  
ATOM    167  O   VAL A 471       3.563   2.413 -26.259  1.00 36.22      A    O  
ANISOU  167  O   VAL A 471     5764   4203   3795   -791   1068    214  A    O  
ATOM    168  CB  VAL A 471       1.943   0.264 -24.662  1.00 38.15      A    C  
ANISOU  168  CB  VAL A 471     5498   4830   4165   -533    504    193  A    C  
ATOM    169  CG1 VAL A 471       2.297   0.678 -23.237  1.00 36.49      A    C  
ANISOU  169  CG1 VAL A 471     5142   4620   4102   -607    428    168  A    C  
ATOM    170  CG2 VAL A 471       0.857  -0.800 -24.652  1.00 35.66      A    C  
ANISOU  170  CG2 VAL A 471     5087   4652   3808   -396    321    190  A    C  
ATOM    171  N   TYR A 472       2.408   3.564 -24.693  1.00 40.54      A    N  
ANISOU  171  N   TYR A 472     6355   4746   4302   -660    787    277  A    N  
ATOM    172  CA  TYR A 472       3.418   4.593 -24.462  1.00 45.46      A    C  
ANISOU  172  CA  TYR A 472     7047   5200   5026   -862    992    238  A    C  
ATOM    173  C   TYR A 472       3.687   4.727 -22.965  1.00 44.10      A    C  
ANISOU  173  C   TYR A 472     6617   5089   5050   -926    843    163  A    C  
ATOM    174  O   TYR A 472       2.814   4.444 -22.145  1.00 39.76      A    O  
ANISOU  174  O   TYR A 472     5990   4653   4463   -785    616    188  A    O  
ATOM    175  CB  TYR A 472       2.931   5.951 -24.969  1.00 49.67      A    C  
ANISOU  175  CB  TYR A 472     8029   5515   5330   -805   1090    333  A    C  
ATOM    176  CG  TYR A 472       2.707   6.061 -26.458  1.00 54.65      A    C  
ANISOU  176  CG  TYR A 472     9046   6022   5696   -726   1235    417  A    C  
ATOM    177  CD1 TYR A 472       1.576   5.519 -27.053  1.00 54.42      A    C  
ANISOU  177  CD1 TYR A 472     9121   6093   5462   -464   1021    472  A    C  
ATOM    178  CD2 TYR A 472       3.607   6.745 -27.265  1.00 58.24      A    C  
ANISOU  178  CD2 TYR A 472     9792   6242   6094   -919   1592    425  A    C  
ATOM    179  CE1 TYR A 472       1.363   5.634 -28.413  1.00 56.62      A    C  
ANISOU  179  CE1 TYR A 472     9805   6250   5457   -362   1110    540  A    C  
ATOM    180  CE2 TYR A 472       3.401   6.865 -28.623  1.00 59.84      A    C  
ANISOU  180  CE2 TYR A 472    10439   6302   5995   -839   1737    514  A    C  
ATOM    181  CZ  TYR A 472       2.277   6.308 -29.192  1.00 61.10      A    C  
ANISOU  181  CZ  TYR A 472    10721   6572   5923   -543   1469    574  A    C  
ATOM    182  OH  TYR A 472       2.066   6.426 -30.547  1.00 66.77      A    O  
ANISOU  182  OH  TYR A 472    11922   7142   6305   -433   1567    651  A    O  
ATOM    183  N   LYS A 473       4.888   5.174 -22.612  1.00 46.64      A    N  
ANISOU  183  N   LYS A 473     6817   5327   5579  -1145    981     50  A    N  
ATOM    184  CA  LYS A 473       5.176   5.552 -21.236  1.00 47.20      A    C  
ANISOU  184  CA  LYS A 473     6723   5415   5797  -1203    827    -36  A    C  
ATOM    185  C   LYS A 473       4.708   6.985 -21.046  1.00 49.64      A    C  
ANISOU  185  C   LYS A 473     7346   5542   5972  -1204    884     15  A    C  
ATOM    186  O   LYS A 473       4.821   7.810 -21.948  1.00 49.27      A    O  
ANISOU  186  O   LYS A 473     7593   5301   5826  -1273   1122     63  A    O  
ATOM    187  CB  LYS A 473       6.670   5.442 -20.931  1.00 50.32      A    C  
ANISOU  187  CB  LYS A 473     6815   5799   6504  -1425    906   -230  A    C  
ATOM    188  CG  LYS A 473       7.041   5.719 -19.478  1.00 49.88      A    C  
ANISOU  188  CG  LYS A 473     6583   5775   6596  -1461    680   -351  A    C  
ATOM    189  CD  LYS A 473       8.528   5.511 -19.243  1.00 53.14      A    C  
ANISOU  189  CD  LYS A 473     6637   6198   7355  -1648    703   -590  A    C  
ATOM    190  CE  LYS A 473       8.901   5.768 -17.793  1.00 56.90      A    C  
ANISOU  190  CE  LYS A 473     6963   6704   7953  -1654    416   -733  A    C  
ATOM    191  NZ  LYS A 473      10.351   5.532 -17.540  1.00 61.06      A    N1+
ANISOU  191  NZ  LYS A 473     7088   7257   8853  -1800    370  -1014  A    N1+
ATOM    192  N   GLY A 474       4.168   7.288 -19.876  1.00 49.73      A    N  
ANISOU  192  N   GLY A 474     7341   5593   5960  -1120    680      8  A    N  
ATOM    193  CA  GLY A 474       3.585   8.597 -19.669  1.00 48.25      A    C  
ANISOU  193  CA  GLY A 474     7459   5235   5638  -1077    713     53  A    C  
ATOM    194  C   GLY A 474       3.733   9.118 -18.263  1.00 46.15      A    C  
ANISOU  194  C   GLY A 474     7120   4961   5453  -1125    574    -47  A    C  
ATOM    195  O   GLY A 474       4.199   8.411 -17.370  1.00 44.63      A    O  
ANISOU  195  O   GLY A 474     6659   4908   5391  -1162    409   -142  A    O  
ATOM    196  N   LYS A 475       3.335  10.371 -18.076  1.00 46.40      A    N  
ANISOU  196  N   LYS A 475     7433   4808   5388  -1106    628    -30  A    N  
ATOM    197  CA  LYS A 475       3.351  10.998 -16.766  1.00 44.25      A    C  
ANISOU  197  CA  LYS A 475     7157   4503   5151  -1134    504   -129  A    C  
ATOM    198  C   LYS A 475       1.920  11.327 -16.339  1.00 42.84      A    C  
ANISOU  198  C   LYS A 475     7162   4343   4771   -878    395    -49  A    C  
ATOM    199  O   LYS A 475       1.147  11.900 -17.103  1.00 42.27      A    O  
ANISOU  199  O   LYS A 475     7348   4158   4555   -730    468     48  A    O  
ATOM    200  CB  LYS A 475       4.202  12.261 -16.781  1.00 48.96      A    C  
ANISOU  200  CB  LYS A 475     7909   4842   5852  -1362    680   -228  A    C  
ATOM    201  CG  LYS A 475       5.671  12.006 -17.113  1.00 57.61      A    C  
ANISOU  201  CG  LYS A 475     8756   5918   7214  -1648    818   -373  A    C  
ATOM    202  CD  LYS A 475       6.347  11.186 -16.024  1.00 64.18      A    C  
ANISOU  202  CD  LYS A 475     9200   6951   8234  -1689    560   -538  A    C  
ATOM    203  CE  LYS A 475       6.342  11.934 -14.689  1.00 69.84      A    C  
ANISOU  203  CE  LYS A 475     9970   7613   8951  -1707    382   -663  A    C  
ATOM    204  NZ  LYS A 475       7.038  11.168 -13.614  1.00 72.49      A    N1+
ANISOU  204  NZ  LYS A 475     9993   8121   9430  -1718     87   -832  A    N1+
ATOM    205  N   TRP A 476       1.572  10.920 -15.121  1.00 41.29      A    N  
ANISOU  205  N   TRP A 476     6839   4287   4563   -813    219   -106  A    N  
ATOM    206  CA  TRP A 476       0.300  11.261 -14.481  1.00 38.10      A    C  
ANISOU  206  CA  TRP A 476     6563   3904   4011   -607    152    -87  A    C  
ATOM    207  C   TRP A 476       0.348  10.866 -13.011  1.00 41.23      A    C  
ANISOU  207  C   TRP A 476     6858   4408   4398   -628     10   -179  A    C  
ATOM    208  O   TRP A 476       0.040   9.722 -12.660  1.00 41.99      A    O  
ANISOU  208  O   TRP A 476     6801   4684   4469   -574    -71   -155  A    O  
ATOM    209  CB  TRP A 476      -0.896  10.594 -15.182  1.00 35.28      A    C  
ANISOU  209  CB  TRP A 476     6169   3675   3560   -387    137     11  A    C  
ATOM    210  CG  TRP A 476      -2.228  11.120 -14.695  1.00 36.89      A    C  
ANISOU  210  CG  TRP A 476     6478   3878   3661   -169    106    -12  A    C  
ATOM    211  CD1 TRP A 476      -2.756  12.355 -14.939  1.00 40.93      A    C  
ANISOU  211  CD1 TRP A 476     7244   4203   4102    -34    145    -14  A    C  
ATOM    212  CD2 TRP A 476      -3.182  10.437 -13.866  1.00 34.56      A    C  
ANISOU  212  CD2 TRP A 476     6038   3757   3337    -62     54    -57  A    C  
ATOM    213  CE2 TRP A 476      -4.260  11.318 -13.654  1.00 37.19      A    C  
ANISOU  213  CE2 TRP A 476     6497   4022   3611    135     72   -109  A    C  
ATOM    214  CE3 TRP A 476      -3.228   9.167 -13.282  1.00 31.72      A    C  
ANISOU  214  CE3 TRP A 476     5476   3581   2994   -117     16    -64  A    C  
ATOM    215  NE1 TRP A 476      -3.976  12.483 -14.320  1.00 40.66      A    N  
ANISOU  215  NE1 TRP A 476     7188   4239   4023    169    103    -77  A    N  
ATOM    216  CZ2 TRP A 476      -5.370  10.973 -12.889  1.00 34.46      A    C  
ANISOU  216  CZ2 TRP A 476     6038   3805   3251    254     86   -191  A    C  
ATOM    217  CZ3 TRP A 476      -4.336   8.825 -12.522  1.00 32.66      A    C  
ANISOU  217  CZ3 TRP A 476     5539   3803   3067    -16     44   -121  A    C  
ATOM    218  CH2 TRP A 476      -5.389   9.724 -12.335  1.00 30.64      A    C  
ANISOU  218  CH2 TRP A 476     5367   3495   2780    157     94   -195  A    C  
ATOM    219  N   HIS A 477       0.729  11.824 -12.167  1.00 41.29      A    N  
ANISOU  219  N   HIS A 477     6998   4283   4408   -709    -12   -286  A    N  
ATOM    220  CA  HIS A 477       0.950  11.582 -10.743  1.00 39.46      A    C  
ANISOU  220  CA  HIS A 477     6744   4116   4134   -739   -165   -392  A    C  
ATOM    221  C   HIS A 477       2.003  10.494 -10.581  1.00 39.07      A    C  
ANISOU  221  C   HIS A 477     6460   4189   4196   -850   -308   -432  A    C  
ATOM    222  O   HIS A 477       1.858   9.578  -9.773  1.00 39.20      A    O  
ANISOU  222  O   HIS A 477     6438   4332   4126   -788   -444   -432  A    O  
ATOM    223  CB  HIS A 477      -0.351  11.191 -10.037  1.00 37.93      A    C  
ANISOU  223  CB  HIS A 477     6615   4031   3767   -554   -168   -358  A    C  
ATOM    224  CG  HIS A 477      -1.436  12.214 -10.153  1.00 37.66      A    C  
ANISOU  224  CG  HIS A 477     6762   3892   3655   -402    -50   -357  A    C  
ATOM    225  CD2 HIS A 477      -2.638  12.173 -10.775  1.00 33.25      A    C  
ANISOU  225  CD2 HIS A 477     6192   3379   3062   -209     32   -296  A    C  
ATOM    226  ND1 HIS A 477      -1.351  13.461  -9.567  1.00 38.45      A    N  
ANISOU  226  ND1 HIS A 477     7078   3812   3720   -420    -32   -455  A    N  
ATOM    227  CE1 HIS A 477      -2.451  14.142  -9.827  1.00 36.09      A    C  
ANISOU  227  CE1 HIS A 477     6906   3444   3364   -229     63   -442  A    C  
ATOM    228  NE2 HIS A 477      -3.250  13.384 -10.557  1.00 39.03      A    N  
ANISOU  228  NE2 HIS A 477     7128   3958   3743    -91     90   -355  A    N  
ATOM    229  N   GLY A 478       3.060  10.606 -11.377  1.00 38.83      A    N  
ANISOU  229  N   GLY A 478     6294   4101   4359  -1009   -260   -474  A    N  
ATOM    230  CA  GLY A 478       4.084   9.589 -11.456  1.00 33.97      A    C  
ANISOU  230  CA  GLY A 478     5409   3595   3901  -1091   -379   -532  A    C  
ATOM    231  C   GLY A 478       4.066   8.945 -12.828  1.00 40.22      A    C  
ANISOU  231  C   GLY A 478     6078   4440   4764  -1088   -226   -418  A    C  
ATOM    232  O   GLY A 478       3.474   9.472 -13.765  1.00 40.48      A    O  
ANISOU  232  O   GLY A 478     6257   4392   4734  -1055    -37   -315  A    O  
ATOM    233  N   ASP A 479       4.712   7.793 -12.946  1.00 40.09      A    N  
ANISOU  233  N   ASP A 479     5823   4549   4862  -1100   -326   -443  A    N  
ATOM    234  CA  ASP A 479       4.793   7.090 -14.214  1.00 36.56      A    C  
ANISOU  234  CA  ASP A 479     5254   4155   4483  -1103   -186   -360  A    C  
ATOM    235  C   ASP A 479       3.537   6.273 -14.480  1.00 36.24      A    C  
ANISOU  235  C   ASP A 479     5282   4227   4260   -918   -184   -196  A    C  
ATOM    236  O   ASP A 479       3.003   5.615 -13.586  1.00 35.22      A    O  
ANISOU  236  O   ASP A 479     5169   4187   4026   -815   -326   -173  A    O  
ATOM    237  CB  ASP A 479       6.009   6.169 -14.224  1.00 39.28      A    C  
ANISOU  237  CB  ASP A 479     5294   4579   5051  -1175   -296   -483  A    C  
ATOM    238  CG  ASP A 479       7.278   6.882 -13.834  1.00 46.38      A    C  
ANISOU  238  CG  ASP A 479     6042   5392   6187  -1360   -339   -710  A    C  
ATOM    239  OD1 ASP A 479       7.594   7.921 -14.450  1.00 49.42      A    O  
ANISOU  239  OD1 ASP A 479     6488   5630   6661  -1530   -104   -756  A    O  
ATOM    240  OD2 ASP A 479       7.959   6.404 -12.904  1.00 50.35      A    O1-
ANISOU  240  OD2 ASP A 479     6382   5961   6789  -1332   -615   -855  A    O1-
ATOM    241  N   VAL A 480       3.066   6.321 -15.720  1.00 34.99      A    N  
ANISOU  241  N   VAL A 480     5185   4050   4060   -883    -15    -98  A    N  
ATOM    242  CA  VAL A 480       1.954   5.486 -16.139  1.00 34.60      A    C  
ANISOU  242  CA  VAL A 480     5143   4116   3889   -724    -23     12  A    C  
ATOM    243  C   VAL A 480       2.236   4.843 -17.488  1.00 36.36      A    C  
ANISOU  243  C   VAL A 480     5287   4367   4160   -740     82     54  A    C  
ATOM    244  O   VAL A 480       3.153   5.239 -18.205  1.00 39.99      A    O  
ANISOU  244  O   VAL A 480     5744   4735   4717   -870    221     16  A    O  
ATOM    245  CB  VAL A 480       0.633   6.277 -16.243  1.00 32.03      A    C  
ANISOU  245  CB  VAL A 480     5021   3747   3400   -579     21     74  A    C  
ATOM    246  CG1 VAL A 480       0.209   6.795 -14.881  1.00 33.37      A    C  
ANISOU  246  CG1 VAL A 480     5273   3902   3506   -547    -56     23  A    C  
ATOM    247  CG2 VAL A 480       0.762   7.411 -17.263  1.00 28.15      A    C  
ANISOU  247  CG2 VAL A 480     4735   3084   2876   -597    169    106  A    C  
ATOM    248  N   ALA A 481       1.437   3.840 -17.819  1.00 33.18      A    N  
ANISOU  248  N   ALA A 481     4830   4084   3692   -624     40    115  A    N  
ATOM    249  CA  ALA A 481       1.423   3.298 -19.163  1.00 34.81      A    C  
ANISOU  249  CA  ALA A 481     5023   4314   3889   -601    130    155  A    C  
ATOM    250  C   ALA A 481       0.157   3.796 -19.836  1.00 33.12      A    C  
ANISOU  250  C   ALA A 481     4995   4085   3506   -442    144    220  A    C  
ATOM    251  O   ALA A 481      -0.926   3.728 -19.262  1.00 33.72      A    O  
ANISOU  251  O   ALA A 481     5060   4229   3524   -324     52    218  A    O  
ATOM    252  CB  ALA A 481       1.462   1.776 -19.132  1.00 34.60      A    C  
ANISOU  252  CB  ALA A 481     4803   4418   3926   -580     50    148  A    C  
ATOM    253  N   VAL A 482       0.301   4.322 -21.044  1.00 33.44      A    N  
ANISOU  253  N   VAL A 482     5219   4021   3464   -431    261    259  A    N  
ATOM    254  CA  VAL A 482      -0.845   4.824 -21.785  1.00 34.27      A    C  
ANISOU  254  CA  VAL A 482     5539   4092   3391   -232    220    308  A    C  
ATOM    255  C   VAL A 482      -1.068   3.985 -23.033  1.00 36.13      A    C  
ANISOU  255  C   VAL A 482     5790   4389   3550   -159    216    325  A    C  
ATOM    256  O   VAL A 482      -0.238   3.964 -23.939  1.00 36.85      A    O  
ANISOU  256  O   VAL A 482     5995   4396   3610   -252    368    347  A    O  
ATOM    257  CB  VAL A 482      -0.652   6.295 -22.190  1.00 34.52      A    C  
ANISOU  257  CB  VAL A 482     5910   3895   3310   -228    332    353  A    C  
ATOM    258  CG1 VAL A 482      -1.940   6.865 -22.779  1.00 32.53      A    C  
ANISOU  258  CG1 VAL A 482     5894   3598   2867     46    213    388  A    C  
ATOM    259  CG2 VAL A 482      -0.200   7.115 -20.994  1.00 34.70      A    C  
ANISOU  259  CG2 VAL A 482     5917   3839   3431   -347    357    310  A    C  
ATOM    260  N   LYS A 483      -2.186   3.278 -23.070  1.00 37.20      A    N  
ANISOU  260  N   LYS A 483     5803   4666   3664     -6     59    292  A    N  
ATOM    261  CA  LYS A 483      -2.521   2.495 -24.241  1.00 39.35      A    C  
ANISOU  261  CA  LYS A 483     6096   5000   3855     82     14    280  A    C  
ATOM    262  C   LYS A 483      -3.434   3.310 -25.127  1.00 41.31      A    C  
ANISOU  262  C   LYS A 483     6626   5170   3899    317    -92    293  A    C  
ATOM    263  O   LYS A 483      -4.593   3.544 -24.786  1.00 40.93      A    O  
ANISOU  263  O   LYS A 483     6511   5186   3854    496   -261    231  A    O  
ATOM    264  CB  LYS A 483      -3.194   1.176 -23.858  1.00 39.26      A    C  
ANISOU  264  CB  LYS A 483     5784   5175   3960     97   -100    203  A    C  
ATOM    265  CG  LYS A 483      -3.711   0.394 -25.065  1.00 41.40      A    C  
ANISOU  265  CG  LYS A 483     6068   5511   4150    203   -184    155  A    C  
ATOM    266  CD  LYS A 483      -4.185  -0.997 -24.687  1.00 40.74      A    C  
ANISOU  266  CD  LYS A 483     5690   5577   4213    156   -246     69  A    C  
ATOM    267  CE  LYS A 483      -3.018  -1.891 -24.315  1.00 41.73      A    C  
ANISOU  267  CE  LYS A 483     5700   5698   4458    -33   -126    101  A    C  
ATOM    268  NZ  LYS A 483      -3.427  -3.321 -24.280  1.00 42.61      A    N1+
ANISOU  268  NZ  LYS A 483     5617   5904   4667    -66   -173     28  A    N1+
ATOM    269  N   MET A 484      -2.896   3.759 -26.255  1.00 44.92      A    N  
ANISOU  269  N   MET A 484     7415   5476   4176    325     12    360  A    N  
ATOM    270  CA  MET A 484      -3.681   4.472 -27.249  1.00 50.24      A    C  
ANISOU  270  CA  MET A 484     8453   6041   4596    584   -117    385  A    C  
ATOM    271  C   MET A 484      -4.440   3.486 -28.115  1.00 54.04      A    C  
ANISOU  271  C   MET A 484     8864   6663   5005    745   -313    303  A    C  
ATOM    272  O   MET A 484      -3.841   2.597 -28.715  1.00 55.51      A    O  
ANISOU  272  O   MET A 484     9018   6891   5184    627   -214    298  A    O  
ATOM    273  CB  MET A 484      -2.766   5.276 -28.170  1.00 53.40      A    C  
ANISOU  273  CB  MET A 484     9319   6185   4784    511    112    497  A    C  
ATOM    274  CG  MET A 484      -1.973   6.350 -27.493  1.00 55.08      A    C  
ANISOU  274  CG  MET A 484     9648   6216   5063    332    326    556  A    C  
ATOM    275  SD  MET A 484      -3.043   7.503 -26.633  1.00 76.24      A    S  
ANISOU  275  SD  MET A 484    12401   8835   7732    557    122    548  A    S  
ATOM    276  CE  MET A 484      -1.868   8.789 -26.228  1.00 57.54      A    C  
ANISOU  276  CE  MET A 484    10299   6178   5384    304    433    620  A    C  
ATOM    277  N   LEU A 485      -5.755   3.664 -28.190  1.00 56.96      A    N  
ANISOU  277  N   LEU A 485     9201   7103   5339   1019   -596    211  A    N  
ATOM    278  CA  LEU A 485      -6.571   2.958 -29.167  1.00 62.91      A    C  
ANISOU  278  CA  LEU A 485     9949   7959   5993   1218   -837    100  A    C  
ATOM    279  C   LEU A 485      -6.629   3.738 -30.479  1.00 72.09      A    C  
ANISOU  279  C   LEU A 485    11677   8924   6791   1451   -931    169  A    C  
ATOM    280  O   LEU A 485      -6.960   4.927 -30.504  1.00 78.29      A    O  
ANISOU  280  O   LEU A 485    12770   9545   7434   1644  -1012    223  A    O  
ATOM    281  CB  LEU A 485      -7.986   2.715 -28.649  1.00 63.47      A    C  
ANISOU  281  CB  LEU A 485     9660   8212   6243   1404  -1112    -89  A    C  
ATOM    282  CG  LEU A 485      -8.177   1.871 -27.393  1.00 62.46      A    C  
ANISOU  282  CG  LEU A 485     9026   8266   6439   1197  -1022   -177  A    C  
ATOM    283  CD1 LEU A 485      -8.130   2.719 -26.121  1.00 61.01      A    C  
ANISOU  283  CD1 LEU A 485     8780   8034   6366   1138   -906   -131  A    C  
ATOM    284  CD2 LEU A 485      -9.492   1.132 -27.498  1.00 65.25      A    C  
ANISOU  284  CD2 LEU A 485     9043   8808   6942   1336  -1259   -411  A    C  
ATOM    285  N   ASN A 486      -6.312   3.060 -31.572  1.00 73.14      A    N  
ANISOU  285  N   ASN A 486    11990   9051   6748   1445   -918    168  A    N  
ATOM    286  CA  ASN A 486      -6.253   3.719 -32.869  1.00 77.74      A    C  
ANISOU  286  CA  ASN A 486    13083   9406   7050   1597   -926    228  A    C  
ATOM    287  C   ASN A 486      -7.607   4.246 -33.359  1.00 81.23      A    C  
ANISOU  287  C   ASN A 486    13593   9821   7451   1969  -1304    103  A    C  
ATOM    288  O   ASN A 486      -8.244   3.629 -34.199  1.00 83.18      A    O  
ANISOU  288  O   ASN A 486    13808  10141   7656   2124  -1530    -28  A    O  
ATOM    289  CB  ASN A 486      -5.642   2.771 -33.903  1.00 78.81      A    C  
ANISOU  289  CB  ASN A 486    13322   9550   7074   1481   -800    219  A    C  
ATOM    290  CG  ASN A 486      -5.348   3.448 -35.223  1.00 82.64      A    C  
ANISOU  290  CG  ASN A 486    14329   9759   7309   1560   -703    289  A    C  
ATOM    291  ND2 ASN A 486      -5.198   2.642 -36.260  1.00 84.27      A    N  
ANISOU  291  ND2 ASN A 486    14641   9981   7395   1559   -700    240  A    N  
ATOM    292  OD1 ASN A 486      -5.245   4.673 -35.313  1.00 84.06      A    O  
ANISOU  292  OD1 ASN A 486    14840   9701   7398   1618   -624    377  A    O  
ATOM    293  N   VAL A 487      -8.018   5.405 -32.852  1.00 82.72      A    N  
ANISOU  293  N   VAL A 487    13886   9890   7655   2115  -1369    126  A    N  
ATOM    294  CA  VAL A 487      -9.304   5.981 -33.208  1.00 86.38      A    C  
ANISOU  294  CA  VAL A 487    14394  10322   8105   2487  -1724    -22  A    C  
ATOM    295  C   VAL A 487      -9.425   7.403 -32.715  1.00 85.41      A    C  
ANISOU  295  C   VAL A 487    14510   9994   7946   2607  -1699     42  A    C  
ATOM    296  O   VAL A 487      -8.849   7.768 -31.722  1.00 82.06      A    O  
ANISOU  296  O   VAL A 487    14023   9551   7605   2421  -1489    149  A    O  
ATOM    297  CB  VAL A 487     -10.467   5.143 -32.619  1.00 65.37      A    C  
ANISOU  297  CB  VAL A 487    11151   7978   5710   2609  -2029   -263  A    C  
ATOM    298  CG1 VAL A 487     -10.217   4.936 -31.131  1.00 59.93      A    C  
ANISOU  298  CG1 VAL A 487    10088   7453   5231   2412  -1893   -235  A    C  
ATOM    299  CG2 VAL A 487     -11.823   5.837 -32.863  1.00 68.28      A    C  
ANISOU  299  CG2 VAL A 487    11504   8319   6120   2996  -2383   -463  A    C  
ATOM    300  N   PRO A 490     -14.318   9.231 -31.999  1.00 88.11      A    N  
ANISOU  300  N   PRO A 490    14228  10543   8708   3872  -2935   -779  A    N  
ATOM    301  CA  PRO A 490     -14.873   7.874 -32.021  1.00 86.39      A    C  
ANISOU  301  CA  PRO A 490    13471  10629   8726   3810  -3068   -982  A    C  
ATOM    302  C   PRO A 490     -16.273   7.812 -32.629  1.00 89.42      A    C  
ANISOU  302  C   PRO A 490    13663  11096   9214   4143  -3464  -1321  A    C  
ATOM    303  O   PRO A 490     -16.968   8.823 -32.697  1.00 90.58      A    O  
ANISOU  303  O   PRO A 490    13966  11129   9322   4438  -3659  -1434  A    O  
ATOM    304  CB  PRO A 490     -14.925   7.503 -30.541  1.00 82.87      A    C  
ANISOU  304  CB  PRO A 490    12491  10408   8589   3625  -2933  -1022  A    C  
ATOM    305  CG  PRO A 490     -13.792   8.268 -29.937  1.00 81.40      A    C  
ANISOU  305  CG  PRO A 490    12651  10029   8249   3453  -2632   -721  A    C  
ATOM    306  CD  PRO A 490     -13.707   9.563 -30.698  1.00 84.75      A    C  
ANISOU  306  CD  PRO A 490    13683  10125   8391   3662  -2673   -629  A    C  
ATOM    307  N   THR A 491     -16.663   6.624 -33.079  1.00 92.32      A    N  
ANISOU  307  N   THR A 491    13706  11655   9715   4088  -3580  -1493  A    N  
ATOM    308  CA  THR A 491     -18.015   6.360 -33.555  1.00 99.87      A    C  
ANISOU  308  CA  THR A 491    14371  12731  10845   4350  -3941  -1862  A    C  
ATOM    309  C   THR A 491     -18.890   6.151 -32.331  1.00101.96      A    C  
ANISOU  309  C   THR A 491    13964  13242  11533   4297  -3943  -2117  A    C  
ATOM    310  O   THR A 491     -18.382   5.761 -31.278  1.00 99.63      A    O  
ANISOU  310  O   THR A 491    13391  13068  11396   4011  -3666  -2009  A    O  
ATOM    311  CB  THR A 491     -18.037   5.087 -34.446  1.00103.90      A    C  
ANISOU  311  CB  THR A 491    14771  13345  11361   4260  -4022  -1954  A    C  
ATOM    312  CG2 THR A 491     -19.450   4.694 -34.867  1.00107.32      A    C  
ANISOU  312  CG2 THR A 491    14835  13916  12025   4493  -4383  -2373  A    C  
ATOM    313  OG1 THR A 491     -17.255   5.319 -35.622  1.00106.34      A    O  
ANISOU  313  OG1 THR A 491    15724  13411  11270   4319  -4003  -1732  A    O  
ATOM    314  N   PRO A 492     -20.198   6.441 -32.447  1.00106.75      A    N  
ANISOU  314  N   PRO A 492    14321  13913  12325   4572  -4242  -2467  A    N  
ATOM    315  CA  PRO A 492     -21.120   6.058 -31.377  1.00107.31      A    C  
ANISOU  315  CA  PRO A 492    13693  14232  12847   4475  -4204  -2766  A    C  
ATOM    316  C   PRO A 492     -20.926   4.618 -30.923  1.00104.16      A    C  
ANISOU  316  C   PRO A 492    12821  14053  12702   4094  -3975  -2809  A    C  
ATOM    317  O   PRO A 492     -20.931   4.351 -29.723  1.00102.18      A    O  
ANISOU  317  O   PRO A 492    12168  13941  12713   3858  -3720  -2835  A    O  
ATOM    318  CB  PRO A 492     -22.483   6.217 -32.040  1.00113.16      A    C  
ANISOU  318  CB  PRO A 492    14269  15005  13719   4802  -4595  -3168  A    C  
ATOM    319  CG  PRO A 492     -22.289   7.383 -32.951  1.00116.24      A    C  
ANISOU  319  CG  PRO A 492    15344  15116  13705   5157  -4827  -3030  A    C  
ATOM    320  CD  PRO A 492     -20.836   7.370 -33.398  1.00112.48      A    C  
ANISOU  320  CD  PRO A 492    15436  14453  12846   4990  -4595  -2592  A    C  
ATOM    321  N   GLN A 493     -20.732   3.709 -31.871  1.00103.44      A    N  
ANISOU  321  N   GLN A 493    12809  13974  12518   4033  -4053  -2814  A    N  
ATOM    322  CA  GLN A 493     -20.585   2.296 -31.544  1.00100.67      A    C  
ANISOU  322  CA  GLN A 493    12042  13810  12396   3677  -3854  -2873  A    C  
ATOM    323  C   GLN A 493     -19.191   1.932 -31.040  1.00 94.15      A    C  
ANISOU  323  C   GLN A 493    11381  12970  11422   3364  -3526  -2508  A    C  
ATOM    324  O   GLN A 493     -19.040   1.023 -30.223  1.00 91.27      A    O  
ANISOU  324  O   GLN A 493    10626  12760  11292   3045  -3288  -2539  A    O  
ATOM    325  CB  GLN A 493     -20.954   1.432 -32.745  1.00104.42      A    C  
ANISOU  325  CB  GLN A 493    12525  14305  12845   3739  -4074  -3043  A    C  
ATOM    326  CG  GLN A 493     -22.356   1.679 -33.246  1.00111.45      A    C  
ANISOU  326  CG  GLN A 493    13211  15223  13910   4047  -4426  -3450  A    C  
ATOM    327  CD  GLN A 493     -22.428   1.686 -34.751  1.00114.97      A    C  
ANISOU  327  CD  GLN A 493    14071  15536  14075   4330  -4758  -3480  A    C  
ATOM    328  NE2 GLN A 493     -22.408   2.878 -35.338  1.00117.64      A    N  
ANISOU  328  NE2 GLN A 493    14918  15670  14110   4682  -4975  -3390  A    N  
ATOM    329  OE1 GLN A 493     -22.492   0.634 -35.384  1.00114.84      A    O  
ANISOU  329  OE1 GLN A 493    13947  15585  14102   4234  -4812  -3582  A    O  
ATOM    330  N   GLN A 494     -18.175   2.631 -31.535  1.00 90.43      A    N  
ANISOU  330  N   GLN A 494    11500  12296  10562   3444  -3500  -2177  A    N  
ATOM    331  CA  GLN A 494     -16.814   2.421 -31.057  1.00 81.30      A    C  
ANISOU  331  CA  GLN A 494    10529  11108   9253   3164  -3198  -1843  A    C  
ATOM    332  C   GLN A 494     -16.704   2.833 -29.598  1.00 77.46      A    C  
ANISOU  332  C   GLN A 494     9794  10692   8947   3049  -2998  -1798  A    C  
ATOM    333  O   GLN A 494     -15.957   2.236 -28.824  1.00 71.51      A    O  
ANISOU  333  O   GLN A 494     8894  10026   8249   2761  -2757  -1670  A    O  
ATOM    334  CB  GLN A 494     -15.821   3.219 -31.898  1.00 77.91      A    C  
ANISOU  334  CB  GLN A 494    10799  10412   8393   3260  -3165  -1529  A    C  
ATOM    335  CG  GLN A 494     -15.606   2.648 -33.283  1.00 76.66      A    C  
ANISOU  335  CG  GLN A 494    10926  10180   8022   3298  -3268  -1515  A    C  
ATOM    336  CD  GLN A 494     -14.693   3.501 -34.128  1.00 73.77      A    C  
ANISOU  336  CD  GLN A 494    11259   9522   7248   3376  -3181  -1233  A    C  
ATOM    337  NE2 GLN A 494     -13.704   2.872 -34.747  1.00 71.36      A    N  
ANISOU  337  NE2 GLN A 494    11194   9165   6753   3177  -3002  -1060  A    N  
ATOM    338  OE1 GLN A 494     -14.869   4.714 -34.222  1.00 74.13      A    O  
ANISOU  338  OE1 GLN A 494    11629   9377   7158   3598  -3250  -1185  A    O  
ATOM    339  N   LEU A 495     -17.461   3.863 -29.238  1.00 80.71      A    N  
ANISOU  339  N   LEU A 495    10171  11057   9440   3291  -3109  -1918  A    N  
ATOM    340  CA  LEU A 495     -17.472   4.383 -27.881  1.00 81.02      A    C  
ANISOU  340  CA  LEU A 495     9990  11141   9652   3236  -2931  -1902  A    C  
ATOM    341  C   LEU A 495     -18.092   3.378 -26.918  1.00 79.01      A    C  
ANISOU  341  C   LEU A 495     9067  11138   9817   2991  -2764  -2155  A    C  
ATOM    342  O   LEU A 495     -17.643   3.237 -25.781  1.00 76.76      A    O  
ANISOU  342  O   LEU A 495     8613  10906   9647   2766  -2473  -2065  A    O  
ATOM    343  CB  LEU A 495     -18.228   5.710 -27.841  1.00 87.56      A    C  
ANISOU  343  CB  LEU A 495    10951  11848  10470   3570  -3102  -2007  A    C  
ATOM    344  CG  LEU A 495     -18.231   6.495 -26.529  1.00 90.46      A    C  
ANISOU  344  CG  LEU A 495    11194  12203  10973   3578  -2924  -1979  A    C  
ATOM    345  CD1 LEU A 495     -18.165   7.981 -26.825  1.00 93.19      A    C  
ANISOU  345  CD1 LEU A 495    12056  12289  11064   3872  -3050  -1855  A    C  
ATOM    346  CD2 LEU A 495     -19.470   6.178 -25.701  1.00 93.99      A    C  
ANISOU  346  CD2 LEU A 495    10993  12860  11858   3546  -2876  -2354  A    C  
ATOM    347  N   GLN A 496     -19.121   2.677 -27.382  1.00 79.94      A    N  
ANISOU  347  N   GLN A 496     8849  11369  10155   2995  -2893  -2469  A    N  
ATOM    348  CA  GLN A 496     -19.780   1.663 -26.570  1.00 79.62      A    C  
ANISOU  348  CA  GLN A 496     8217  11520  10515   2710  -2677  -2725  A    C  
ATOM    349  C   GLN A 496     -18.837   0.499 -26.309  1.00 75.53      A    C  
ANISOU  349  C   GLN A 496     7648  11067   9984   2346  -2433  -2559  A    C  
ATOM    350  O   GLN A 496     -18.729   0.011 -25.186  1.00 77.61      A    O  
ANISOU  350  O   GLN A 496     7612  11418  10457   2063  -2112  -2578  A    O  
ATOM    351  CB  GLN A 496     -21.039   1.155 -27.268  1.00 85.53      A    C  
ANISOU  351  CB  GLN A 496     8679  12339  11478   2791  -2881  -3097  A    C  
ATOM    352  CG  GLN A 496     -21.956   0.348 -26.367  1.00 89.27      A    C  
ANISOU  352  CG  GLN A 496     8566  12961  12390   2511  -2624  -3408  A    C  
ATOM    353  CD  GLN A 496     -22.777   1.226 -25.442  1.00 93.33      A    C  
ANISOU  353  CD  GLN A 496     8842  13498  13122   2606  -2540  -3590  A    C  
ATOM    354  NE2 GLN A 496     -24.063   1.357 -25.744  1.00 97.87      A    N  
ANISOU  354  NE2 GLN A 496     9145  14117  13925   2763  -2729  -3962  A    N  
ATOM    355  OE1 GLN A 496     -22.263   1.787 -24.473  1.00 91.65      A    O  
ANISOU  355  OE1 GLN A 496     8688  13260  12876   2548  -2311  -3413  A    O  
ATOM    356  N   ALA A 497     -18.154   0.059 -27.359  1.00 71.23      A    N  
ANISOU  356  N   ALA A 497     7424  10462   9179   2351  -2566  -2403  A    N  
ATOM    357  CA  ALA A 497     -17.201  -1.036 -27.250  1.00 66.12      A    C  
ANISOU  357  CA  ALA A 497     6778   9860   8484   2027  -2373  -2250  A    C  
ATOM    358  C   ALA A 497     -16.036  -0.640 -26.348  1.00 62.30      A    C  
ANISOU  358  C   ALA A 497     6584   9241   7846   1806  -2011  -1886  A    C  
ATOM    359  O   ALA A 497     -15.437  -1.481 -25.679  1.00 60.71      A    O  
ANISOU  359  O   ALA A 497     6320   9035   7712   1453  -1690  -1769  A    O  
ATOM    360  CB  ALA A 497     -16.699  -1.438 -28.628  1.00 65.22      A    C  
ANISOU  360  CB  ALA A 497     7025   9663   8091   2095  -2553  -2147  A    C  
ATOM    361  N   PHE A 498     -15.719   0.650 -26.344  1.00 60.99      A    N  
ANISOU  361  N   PHE A 498     6759   8941   7472   2023  -2075  -1718  A    N  
ATOM    362  CA  PHE A 498     -14.663   1.186 -25.501  1.00 55.77      A    C  
ANISOU  362  CA  PHE A 498     6370   8140   6682   1834  -1764  -1412  A    C  
ATOM    363  C   PHE A 498     -15.088   1.139 -24.038  1.00 55.91      A    C  
ANISOU  363  C   PHE A 498     6062   8221   6961   1646  -1487  -1502  A    C  
ATOM    364  O   PHE A 498     -14.304   0.770 -23.165  1.00 50.32      A    O  
ANISOU  364  O   PHE A 498     5407   7468   6244   1346  -1180  -1326  A    O  
ATOM    365  CB  PHE A 498     -14.343   2.625 -25.914  1.00 53.93      A    C  
ANISOU  365  CB  PHE A 498     6589   7724   6179   2117  -1908  -1252  A    C  
ATOM    366  CG  PHE A 498     -13.275   3.272 -25.080  1.00 50.25      A    C  
ANISOU  366  CG  PHE A 498     6387   7103   5601   1925  -1610   -979  A    C  
ATOM    367  CD1 PHE A 498     -11.984   2.775 -25.083  1.00 46.14      A    C  
ANISOU  367  CD1 PHE A 498     6054   6515   4961   1637  -1387   -747  A    C  
ATOM    368  CD2 PHE A 498     -13.558   4.386 -24.304  1.00 51.05      A    C  
ANISOU  368  CD2 PHE A 498     6535   7126   5735   2042  -1569   -984  A    C  
ATOM    369  CE1 PHE A 498     -10.998   3.364 -24.319  1.00 43.34      A    C  
ANISOU  369  CE1 PHE A 498     5900   6030   4539   1464  -1151   -543  A    C  
ATOM    370  CE2 PHE A 498     -12.576   4.983 -23.538  1.00 48.26      A    C  
ANISOU  370  CE2 PHE A 498     6421   6629   5287   1858  -1319   -763  A    C  
ATOM    371  CZ  PHE A 498     -11.293   4.471 -23.546  1.00 45.56      A    C  
ANISOU  371  CZ  PHE A 498     6237   6232   4841   1566  -1121   -550  A    C  
ATOM    372  N   LYS A 499     -16.336   1.513 -23.780  1.00 59.53      A    N  
ANISOU  372  N   LYS A 499     6193   8776   7648   1840  -1601  -1795  A    N  
ATOM    373  CA  LYS A 499     -16.880   1.480 -22.430  1.00 63.38      A    C  
ANISOU  373  CA  LYS A 499     6370   9324   8388   1671  -1306  -1926  A    C  
ATOM    374  C   LYS A 499     -17.006   0.055 -21.907  1.00 66.11      A    C  
ANISOU  374  C   LYS A 499     6414   9766   8937   1299  -1032  -2016  A    C  
ATOM    375  O   LYS A 499     -16.810  -0.196 -20.720  1.00 65.34      A    O  
ANISOU  375  O   LYS A 499     6291   9640   8895   1033   -680  -1950  A    O  
ATOM    376  CB  LYS A 499     -18.233   2.188 -22.384  1.00 69.61      A    C  
ANISOU  376  CB  LYS A 499     6835  10202   9413   1984  -1490  -2270  A    C  
ATOM    377  CG  LYS A 499     -18.124   3.696 -22.536  1.00 72.88      A    C  
ANISOU  377  CG  LYS A 499     7585  10471   9635   2334  -1680  -2166  A    C  
ATOM    378  CD  LYS A 499     -17.356   4.316 -21.375  1.00 70.66      A    C  
ANISOU  378  CD  LYS A 499     7557  10054   9237   2147  -1345  -1924  A    C  
ATOM    379  CE  LYS A 499     -16.816   5.691 -21.740  1.00 70.63      A    C  
ANISOU  379  CE  LYS A 499     8040   9841   8955   2415  -1511  -1719  A    C  
ATOM    380  NZ  LYS A 499     -17.853   6.570 -22.358  1.00 73.38      A    N1+
ANISOU  380  NZ  LYS A 499     8335  10182   9365   2893  -1878  -1951  A    N1+
ATOM    381  N   ASN A 500     -17.329  -0.878 -22.794  1.00 69.62      A    N  
ANISOU  381  N   ASN A 500     6678  10303   9471   1285  -1197  -2169  A    N  
ATOM    382  CA  ASN A 500     -17.439  -2.275 -22.402  1.00 72.46      A    C  
ANISOU  382  CA  ASN A 500     6795  10719  10020    927   -941  -2257  A    C  
ATOM    383  C   ASN A 500     -16.111  -2.864 -21.941  1.00 69.09      A    C  
ANISOU  383  C   ASN A 500     6702  10164   9383    638   -686  -1906  A    C  
ATOM    384  O   ASN A 500     -16.066  -3.610 -20.964  1.00 69.72      A    O  
ANISOU  384  O   ASN A 500     6710  10217   9564    338   -356  -1889  A    O  
ATOM    385  CB  ASN A 500     -18.018  -3.115 -23.538  1.00 76.42      A    C  
ANISOU  385  CB  ASN A 500     7057  11329  10651    984  -1205  -2508  A    C  
ATOM    386  CG  ASN A 500     -19.508  -2.915 -23.706  1.00 83.22      A    C  
ANISOU  386  CG  ASN A 500     7488  12308  11824   1156  -1363  -2929  A    C  
ATOM    387  ND2 ASN A 500     -20.203  -3.973 -24.106  1.00 86.02      A    N  
ANISOU  387  ND2 ASN A 500     7634  12681  12368    996  -1340  -3150  A    N  
ATOM    388  OD1 ASN A 500     -20.033  -1.826 -23.472  1.00 86.25      A    O  
ANISOU  388  OD1 ASN A 500     7847  12688  12236   1401  -1455  -3008  A    O  
ATOM    389  N   GLU A 501     -15.032  -2.534 -22.642  1.00 65.55      A    N  
ANISOU  389  N   GLU A 501     6633   9625   8648    735   -835  -1640  A    N  
ATOM    390  CA  GLU A 501     -13.719  -3.043 -22.264  1.00 62.98      A    C  
ANISOU  390  CA  GLU A 501     6584   9187   8158    500   -636  -1344  A    C  
ATOM    391  C   GLU A 501     -13.224  -2.374 -20.993  1.00 57.03      A    C  
ANISOU  391  C   GLU A 501     5989   8345   7335    409   -412  -1175  A    C  
ATOM    392  O   GLU A 501     -12.643  -3.023 -20.129  1.00 56.84      A    O  
ANISOU  392  O   GLU A 501     6040   8261   7298    166   -181  -1051  A    O  
ATOM    393  CB  GLU A 501     -12.706  -2.863 -23.395  1.00 66.32      A    C  
ANISOU  393  CB  GLU A 501     7331   9540   8329    611   -816  -1151  A    C  
ATOM    394  CG  GLU A 501     -12.087  -4.173 -23.866  1.00 72.31      A    C  
ANISOU  394  CG  GLU A 501     8110  10288   9077    425   -765  -1101  A    C  
ATOM    395  CD  GLU A 501     -11.162  -4.796 -22.833  1.00 75.83      A    C  
ANISOU  395  CD  GLU A 501     8644  10647   9522    157   -491   -915  A    C  
ATOM    396  OE1 GLU A 501     -10.513  -4.035 -22.086  1.00 76.45      A    O  
ANISOU  396  OE1 GLU A 501     8896  10650   9503    144   -396   -746  A    O  
ATOM    397  OE2 GLU A 501     -11.080  -6.043 -22.767  1.00 77.17      A    O1-
ANISOU  397  OE2 GLU A 501     8729  10809   9782    -28   -390   -948  A    O1-
ATOM    398  N   VAL A 502     -13.462  -1.072 -20.884  1.00 52.92      A    N  
ANISOU  398  N   VAL A 502     5549   7802   6757    624   -503  -1179  A    N  
ATOM    399  CA  VAL A 502     -13.114  -0.340 -19.676  1.00 49.50      A    C  
ANISOU  399  CA  VAL A 502     5258   7286   6263    558   -311  -1063  A    C  
ATOM    400  C   VAL A 502     -13.926  -0.897 -18.511  1.00 51.39      A    C  
ANISOU  400  C   VAL A 502     5251   7579   6697    371    -36  -1227  A    C  
ATOM    401  O   VAL A 502     -13.428  -1.009 -17.391  1.00 51.51      A    O  
ANISOU  401  O   VAL A 502     5418   7517   6637    185    196  -1102  A    O  
ATOM    402  CB  VAL A 502     -13.354   1.180 -19.840  1.00 45.42      A    C  
ANISOU  402  CB  VAL A 502     4871   6717   5667    843   -464  -1072  A    C  
ATOM    403  CG1 VAL A 502     -13.293   1.891 -18.497  1.00 42.45      A    C  
ANISOU  403  CG1 VAL A 502     4576   6275   5279    776   -254  -1035  A    C  
ATOM    404  CG2 VAL A 502     -12.338   1.772 -20.803  1.00 40.16      A    C  
ANISOU  404  CG2 VAL A 502     4564   5935   4761    957   -635   -858  A    C  
ATOM    405  N   GLY A 503     -15.170  -1.273 -18.793  1.00 52.01      A    N  
ANISOU  405  N   GLY A 503     4959   7781   7020    416    -58  -1525  A    N  
ATOM    406  CA  GLY A 503     -16.040  -1.863 -17.793  1.00 54.21      A    C  
ANISOU  406  CA  GLY A 503     4975   8103   7518    206    260  -1727  A    C  
ATOM    407  C   GLY A 503     -15.487  -3.157 -17.228  1.00 54.20      A    C  
ANISOU  407  C   GLY A 503     5091   8026   7477   -133    520  -1597  A    C  
ATOM    408  O   GLY A 503     -15.653  -3.445 -16.043  1.00 57.32      A    O  
ANISOU  408  O   GLY A 503     5535   8360   7885   -342    853  -1600  A    O  
ATOM    409  N   VAL A 504     -14.832  -3.940 -18.079  1.00 49.78      A    N  
ANISOU  409  N   VAL A 504     4614   7451   6850   -174    371  -1485  A    N  
ATOM    410  CA  VAL A 504     -14.191  -5.172 -17.640  1.00 50.37      A    C  
ANISOU  410  CA  VAL A 504     4845   7425   6869   -449    567  -1343  A    C  
ATOM    411  C   VAL A 504     -12.947  -4.869 -16.809  1.00 49.81      A    C  
ANISOU  411  C   VAL A 504     5170   7218   6538   -495    632  -1037  A    C  
ATOM    412  O   VAL A 504     -12.728  -5.472 -15.760  1.00 51.28      A    O  
ANISOU  412  O   VAL A 504     5523   7298   6665   -696    876   -956  A    O  
ATOM    413  CB  VAL A 504     -13.801  -6.072 -18.837  1.00 50.62      A    C  
ANISOU  413  CB  VAL A 504     4854   7472   6908   -452    376  -1327  A    C  
ATOM    414  CG1 VAL A 504     -13.130  -7.351 -18.351  1.00 49.07      A    C  
ANISOU  414  CG1 VAL A 504     4840   7143   6660   -709    571  -1185  A    C  
ATOM    415  CG2 VAL A 504     -15.025  -6.402 -19.671  1.00 51.49      A    C  
ANISOU  415  CG2 VAL A 504     4570   7719   7276   -401    264  -1663  A    C  
ATOM    416  N   LEU A 505     -12.137  -3.930 -17.285  1.00 47.39      A    N  
ANISOU  416  N   LEU A 505     5030   6902   6075   -308    408   -884  A    N  
ATOM    417  CA  LEU A 505     -10.890  -3.586 -16.617  1.00 44.58      A    C  
ANISOU  417  CA  LEU A 505     4996   6429   5511   -343    420   -638  A    C  
ATOM    418  C   LEU A 505     -11.152  -2.937 -15.260  1.00 48.73      A    C  
ANISOU  418  C   LEU A 505     5630   6905   5979   -384    607   -642  A    C  
ATOM    419  O   LEU A 505     -10.406  -3.147 -14.303  1.00 49.71      A    O  
ANISOU  419  O   LEU A 505     6008   6923   5957   -496    700   -496  A    O  
ATOM    420  CB  LEU A 505     -10.044  -2.674 -17.505  1.00 41.27      A    C  
ANISOU  420  CB  LEU A 505     4704   6001   4977   -165    183   -517  A    C  
ATOM    421  CG  LEU A 505      -9.724  -3.240 -18.892  1.00 42.49      A    C  
ANISOU  421  CG  LEU A 505     4812   6190   5141   -113     18   -509  A    C  
ATOM    422  CD1 LEU A 505      -9.013  -2.206 -19.759  1.00 44.10      A    C  
ANISOU  422  CD1 LEU A 505     5188   6358   5210     52   -150   -405  A    C  
ATOM    423  CD2 LEU A 505      -8.903  -4.524 -18.799  1.00 38.30      A    C  
ANISOU  423  CD2 LEU A 505     4349   5602   4602   -286     83   -410  A    C  
ATOM    424  N   ARG A 506     -12.230  -2.165 -15.182  1.00 50.91      A    N  
ANISOU  424  N   ARG A 506     5720   7256   6367   -275    649   -829  A    N  
ATOM    425  CA  ARG A 506     -12.615  -1.484 -13.952  1.00 52.81      A    C  
ANISOU  425  CA  ARG A 506     6044   7455   6565   -299    851   -875  A    C  
ATOM    426  C   ARG A 506     -13.002  -2.472 -12.850  1.00 53.60      A    C  
ANISOU  426  C   ARG A 506     6197   7496   6671   -555   1193   -916  A    C  
ATOM    427  O   ARG A 506     -13.156  -2.092 -11.692  1.00 53.10      A    O  
ANISOU  427  O   ARG A 506     6301   7366   6508   -616   1406   -921  A    O  
ATOM    428  CB  ARG A 506     -13.798  -0.556 -14.226  1.00 58.38      A    C  
ANISOU  428  CB  ARG A 506     6479   8260   7442   -104    823  -1117  A    C  
ATOM    429  CG  ARG A 506     -13.611   0.875 -13.763  1.00 63.48      A    C  
ANISOU  429  CG  ARG A 506     7298   8848   7971     63    774  -1076  A    C  
ATOM    430  CD  ARG A 506     -14.916   1.429 -13.218  1.00 71.23      A    C  
ANISOU  430  CD  ARG A 506     8046   9890   9128    143    949  -1349  A    C  
ATOM    431  NE  ARG A 506     -16.064   0.944 -13.976  1.00 76.39      A    N  
ANISOU  431  NE  ARG A 506     8268  10686  10070    204    913  -1622  A    N  
ATOM    432  CZ  ARG A 506     -16.766   1.682 -14.827  1.00 81.60      A    C  
ANISOU  432  CZ  ARG A 506     8700  11428  10878    500    663  -1805  A    C  
ATOM    433  NH1 ARG A 506     -16.448   2.954 -15.028  1.00 82.27      A    N1+
ANISOU  433  NH1 ARG A 506     8987  11441  10831    754    462  -1718  A    N1+
ATOM    434  NH2 ARG A 506     -17.793   1.146 -15.471  1.00 85.06      A    N  
ANISOU  434  NH2 ARG A 506     8720  12003  11595    548    602  -2089  A    N  
ATOM    435  N   LYS A 507     -13.165  -3.740 -13.214  1.00 55.01      A    N  
ANISOU  435  N   LYS A 507     6275   7676   6949   -708   1263   -949  A    N  
ATOM    436  CA  LYS A 507     -13.573  -4.763 -12.258  1.00 56.53      A    C  
ANISOU  436  CA  LYS A 507     6564   7771   7144   -973   1622   -987  A    C  
ATOM    437  C   LYS A 507     -12.403  -5.501 -11.611  1.00 52.18      A    C  
ANISOU  437  C   LYS A 507     6446   7045   6335  -1087   1632   -720  A    C  
ATOM    438  O   LYS A 507     -12.616  -6.406 -10.807  1.00 54.74      A    O  
ANISOU  438  O   LYS A 507     6963   7237   6599  -1296   1918   -707  A    O  
ATOM    439  CB  LYS A 507     -14.511  -5.774 -12.922  1.00 61.10      A    C  
ANISOU  439  CB  LYS A 507     6801   8414   7999  -1105   1733  -1208  A    C  
ATOM    440  CG  LYS A 507     -15.918  -5.254 -13.149  1.00 67.98      A    C  
ANISOU  440  CG  LYS A 507     7224   9437   9168  -1048   1825  -1553  A    C  
ATOM    441  CD  LYS A 507     -16.754  -6.238 -13.950  1.00 72.43      A    C  
ANISOU  441  CD  LYS A 507     7406  10078  10035  -1166   1858  -1805  A    C  
ATOM    442  CE  LYS A 507     -18.213  -5.811 -13.974  1.00 78.78      A    C  
ANISOU  442  CE  LYS A 507     7722  11028  11184  -1136   1989  -2208  A    C  
ATOM    443  NZ  LYS A 507     -18.379  -4.424 -14.499  1.00 80.18      A    N1+
ANISOU  443  NZ  LYS A 507     7749  11337  11379   -768   1654  -2275  A    N1+
ATOM    444  N   THR A 508     -11.177  -5.114 -11.951  1.00 45.16      A    N  
ANISOU  444  N   THR A 508     5720   6139   5299   -946   1326   -523  A    N  
ATOM    445  CA  THR A 508      -9.999  -5.790 -11.415  1.00 41.44      A    C  
ANISOU  445  CA  THR A 508     5609   5516   4618  -1002   1261   -306  A    C  
ATOM    446  C   THR A 508      -9.259  -4.973 -10.359  1.00 40.25      A    C  
ANISOU  446  C   THR A 508     5781   5284   4228   -939   1202   -185  A    C  
ATOM    447  O   THR A 508      -8.802  -3.864 -10.622  1.00 39.79      A    O  
ANISOU  447  O   THR A 508     5676   5287   4154   -794   1007   -165  A    O  
ATOM    448  CB  THR A 508      -9.004  -6.176 -12.526  1.00 39.80      A    C  
ANISOU  448  CB  THR A 508     5338   5334   4449   -914    968   -203  A    C  
ATOM    449  CG2 THR A 508      -9.670  -7.085 -13.551  1.00 38.65      A    C  
ANISOU  449  CG2 THR A 508     4922   5252   4510   -979   1005   -327  A    C  
ATOM    450  OG1 THR A 508      -8.515  -4.992 -13.174  1.00 40.42      A    O  
ANISOU  450  OG1 THR A 508     5319   5506   4533   -738    737   -182  A    O  
ATOM    451  N   ARG A 509      -9.146  -5.543  -9.164  1.00 41.63      A    N  
ANISOU  451  N   ARG A 509     6318   5299   4200  -1053   1374   -110  A    N  
ATOM    452  CA  ARG A 509      -8.342  -4.970  -8.091  1.00 39.59      A    C  
ANISOU  452  CA  ARG A 509     6430   4939   3674   -991   1274      1  A    C  
ATOM    453  C   ARG A 509      -7.535  -6.071  -7.421  1.00 38.86      A    C  
ANISOU  453  C   ARG A 509     6742   4657   3369  -1034   1218    158  A    C  
ATOM    454  O   ARG A 509      -7.965  -6.647  -6.425  1.00 43.42      A    O  
ANISOU  454  O   ARG A 509     7662   5077   3759  -1154   1477    180  A    O  
ATOM    455  CB  ARG A 509      -9.227  -4.269  -7.057  1.00 39.73      A    C  
ANISOU  455  CB  ARG A 509     6575   4933   3587  -1044   1563   -102  A    C  
ATOM    456  CG  ARG A 509      -9.697  -2.883  -7.476  1.00 38.36      A    C  
ANISOU  456  CG  ARG A 509     6107   4909   3557   -919   1517   -235  A    C  
ATOM    457  CD  ARG A 509     -10.642  -2.290  -6.436  1.00 43.05      A    C  
ANISOU  457  CD  ARG A 509     6811   5474   4071   -972   1844   -368  A    C  
ATOM    458  NE  ARG A 509     -10.976  -0.902  -6.738  1.00 45.90      A    N  
ANISOU  458  NE  ARG A 509     6952   5944   4545   -813   1763   -486  A    N  
ATOM    459  CZ  ARG A 509     -10.252   0.143  -6.351  1.00 43.70      A    C  
ANISOU  459  CZ  ARG A 509     6864   5627   4115   -697   1572   -428  A    C  
ATOM    460  NH1 ARG A 509      -9.145  -0.035  -5.643  1.00 42.07      A    N1+
ANISOU  460  NH1 ARG A 509     7031   5301   3654   -716   1414   -276  A    N1+
ATOM    461  NH2 ARG A 509     -10.634   1.370  -6.674  1.00 44.02      A    N  
ANISOU  461  NH2 ARG A 509     6724   5735   4266   -553   1521   -539  A    N  
ATOM    462  N   HIS A 510      -6.363  -6.361  -7.971  1.00 32.95      A    N  
ANISOU  462  N   HIS A 510     5971   3905   2644   -926    888    256  A    N  
ATOM    463  CA  HIS A 510      -5.526  -7.435  -7.459  1.00 34.04      A    C  
ANISOU  463  CA  HIS A 510     6462   3860   2612   -909    764    389  A    C  
ATOM    464  C   HIS A 510      -4.060  -7.126  -7.724  1.00 37.54      A    C  
ANISOU  464  C   HIS A 510     6868   4328   3066   -734    345    445  A    C  
ATOM    465  O   HIS A 510      -3.714  -6.576  -8.761  1.00 36.98      A    O  
ANISOU  465  O   HIS A 510     6437   4407   3206   -679    207    397  A    O  
ATOM    466  CB  HIS A 510      -5.914  -8.763  -8.113  1.00 34.32      A    C  
ANISOU  466  CB  HIS A 510     6420   3840   2781  -1014    901    394  A    C  
ATOM    467  CG  HIS A 510      -5.368  -9.966  -7.414  1.00 36.35      A    C  
ANISOU  467  CG  HIS A 510     7132   3849   2830  -1013    866    526  A    C  
ATOM    468  CD2 HIS A 510      -5.951 -10.848  -6.568  1.00 47.98      A    C  
ANISOU  468  CD2 HIS A 510     9019   5099   4113  -1154   1158    576  A    C  
ATOM    469  ND1 HIS A 510      -4.064 -10.390  -7.569  1.00 46.35      A    N  
ANISOU  469  ND1 HIS A 510     8489   5053   4069   -841    499    614  A    N  
ATOM    470  CE1 HIS A 510      -3.868 -11.474  -6.841  1.00 47.61      A    C  
ANISOU  470  CE1 HIS A 510     9113   4959   4018   -840    522    721  A    C  
ATOM    471  NE2 HIS A 510      -4.997 -11.775  -6.225  1.00 40.49      A    N  
ANISOU  471  NE2 HIS A 510     8448   3941   2995  -1041    934    715  A    N  
ATOM    472  N   VAL A 511      -3.204  -7.489  -6.776  1.00 40.06      A    N  
ANISOU  472  N   VAL A 511     7576   4489   3157   -645    148    529  A    N  
ATOM    473  CA  VAL A 511      -1.777  -7.181  -6.836  1.00 38.44      A    C  
ANISOU  473  CA  VAL A 511     7325   4301   2981   -476   -265    532  A    C  
ATOM    474  C   VAL A 511      -1.081  -7.822  -8.044  1.00 40.11      A    C  
ANISOU  474  C   VAL A 511     7217   4572   3452   -423   -421    526  A    C  
ATOM    475  O   VAL A 511      -0.099  -7.287  -8.557  1.00 40.75      A    O  
ANISOU  475  O   VAL A 511     7050   4745   3690   -335   -661    469  A    O  
ATOM    476  CB  VAL A 511      -1.070  -7.596  -5.516  1.00 46.36      A    C  
ANISOU  476  CB  VAL A 511     8842   5102   3669   -357   -487    600  A    C  
ATOM    477  CG1 VAL A 511      -1.264  -9.082  -5.239  1.00 44.79      A    C  
ANISOU  477  CG1 VAL A 511     8993   4694   3332   -368   -396    710  A    C  
ATOM    478  CG2 VAL A 511       0.408  -7.224  -5.535  1.00 47.19      A    C  
ANISOU  478  CG2 VAL A 511     8833   5243   3856   -174   -946    541  A    C  
ATOM    479  N   ASN A 512      -1.594  -8.958  -8.506  1.00 42.77      A    N  
ANISOU  479  N   ASN A 512     7561   4848   3844   -493   -255    565  A    N  
ATOM    480  CA  ASN A 512      -0.978  -9.663  -9.629  1.00 41.27      A    C  
ANISOU  480  CA  ASN A 512     7109   4694   3877   -440   -379    551  A    C  
ATOM    481  C   ASN A 512      -1.634  -9.351 -10.970  1.00 40.57      A    C  
ANISOU  481  C   ASN A 512     6605   4787   4023   -534   -210    475  A    C  
ATOM    482  O   ASN A 512      -1.318  -9.969 -11.984  1.00 40.13      A    O  
ANISOU  482  O   ASN A 512     6350   4762   4135   -514   -253    453  A    O  
ATOM    483  CB  ASN A 512      -0.957 -11.173  -9.383  1.00 41.99      A    C  
ANISOU  483  CB  ASN A 512     7492   4577   3886   -429   -358    630  A    C  
ATOM    484  CG  ASN A 512      -0.110 -11.557  -8.184  1.00 44.56      A    C  
ANISOU  484  CG  ASN A 512     8265   4700   3964   -266   -618    705  A    C  
ATOM    485  ND2 ASN A 512       1.168 -11.197  -8.221  1.00 35.82      A    N  
ANISOU  485  ND2 ASN A 512     7025   3644   2941    -79   -992    650  A    N  
ATOM    486  OD1 ASN A 512      -0.599 -12.170  -7.235  1.00 46.32      A    O  
ANISOU  486  OD1 ASN A 512     8961   4713   3924   -305   -484    797  A    O  
ATOM    487  N   ILE A 513      -2.553  -8.393 -10.968  1.00 39.12      A    N  
ANISOU  487  N   ILE A 513     6313   4711   3838   -612    -34    425  A    N  
ATOM    488  CA  ILE A 513      -3.154  -7.912 -12.204  1.00 34.80      A    C  
ANISOU  488  CA  ILE A 513     5409   4332   3482   -648     58    342  A    C  
ATOM    489  C   ILE A 513      -2.741  -6.469 -12.444  1.00 35.19      A    C  
ANISOU  489  C   ILE A 513     5318   4489   3563   -580    -52    309  A    C  
ATOM    490  O   ILE A 513      -2.791  -5.651 -11.529  1.00 36.64      A    O  
ANISOU  490  O   ILE A 513     5646   4650   3623   -571    -54    310  A    O  
ATOM    491  CB  ILE A 513      -4.683  -7.999 -12.162  1.00 32.56      A    C  
ANISOU  491  CB  ILE A 513     5072   4082   3219   -772    345    271  A    C  
ATOM    492  CG1 ILE A 513      -5.122  -9.444 -11.930  1.00 34.74      A    C  
ANISOU  492  CG1 ILE A 513     5502   4220   3480   -887    507    289  A    C  
ATOM    493  CG2 ILE A 513      -5.281  -7.466 -13.458  1.00 30.03      A    C  
ANISOU  493  CG2 ILE A 513     4397   3934   3082   -753    359    166  A    C  
ATOM    494  CD1 ILE A 513      -4.657 -10.394 -13.011  1.00 33.93      A    C  
ANISOU  494  CD1 ILE A 513     5258   4114   3520   -864    403    286  A    C  
ATOM    495  N   LEU A 514      -2.320  -6.169 -13.670  1.00 36.80      A    N  
ANISOU  495  N   LEU A 514     5279   4786   3916   -540   -125    276  A    N  
ATOM    496  CA  LEU A 514      -1.892  -4.820 -14.034  1.00 34.51      A    C  
ANISOU  496  CA  LEU A 514     4891   4560   3660   -497   -192    249  A    C  
ATOM    497  C   LEU A 514      -2.947  -3.798 -13.635  1.00 32.58      A    C  
ANISOU  497  C   LEU A 514     4678   4354   3348   -503    -71    213  A    C  
ATOM    498  O   LEU A 514      -4.105  -3.899 -14.038  1.00 32.91      A    O  
ANISOU  498  O   LEU A 514     4621   4456   3427   -515     62    162  A    O  
ATOM    499  CB  LEU A 514      -1.615  -4.731 -15.535  1.00 31.07      A    C  
ANISOU  499  CB  LEU A 514     4252   4197   3357   -475   -200    221  A    C  
ATOM    500  CG  LEU A 514      -1.120  -3.380 -16.053  1.00 31.14      A    C  
ANISOU  500  CG  LEU A 514     4213   4228   3392   -452   -223    202  A    C  
ATOM    501  CD1 LEU A 514       0.285  -3.093 -15.552  1.00 30.52      A    C  
ANISOU  501  CD1 LEU A 514     4147   4091   3359   -466   -349    190  A    C  
ATOM    502  CD2 LEU A 514      -1.166  -3.330 -17.577  1.00 30.66      A    C  
ANISOU  502  CD2 LEU A 514     4040   4217   3392   -430   -176    185  A    C  
ATOM    503  N   LEU A 515      -2.542  -2.822 -12.830  1.00 30.80      A    N  
ANISOU  503  N   LEU A 515     4574   4089   3039   -486   -131    213  A    N  
ATOM    504  CA  LEU A 515      -3.480  -1.861 -12.257  1.00 30.61      A    C  
ANISOU  504  CA  LEU A 515     4616   4076   2938   -477    -14    168  A    C  
ATOM    505  C   LEU A 515      -4.067  -0.871 -13.265  1.00 30.92      A    C  
ANISOU  505  C   LEU A 515     4499   4185   3062   -412     25    118  A    C  
ATOM    506  O   LEU A 515      -3.367  -0.006 -13.788  1.00 29.93      A    O  
ANISOU  506  O   LEU A 515     4364   4041   2967   -381    -59    127  A    O  
ATOM    507  CB  LEU A 515      -2.821  -1.091 -11.115  1.00 31.28      A    C  
ANISOU  507  CB  LEU A 515     4904   4083   2898   -472   -108    169  A    C  
ATOM    508  CG  LEU A 515      -3.779  -0.177 -10.353  1.00 34.97      A    C  
ANISOU  508  CG  LEU A 515     5482   4541   3263   -461     34    112  A    C  
ATOM    509  CD1 LEU A 515      -4.921  -0.997  -9.771  1.00 35.85      A    C  
ANISOU  509  CD1 LEU A 515     5664   4651   3306   -516    254     95  A    C  
ATOM    510  CD2 LEU A 515      -3.053   0.604  -9.264  1.00 35.02      A    C  
ANISOU  510  CD2 LEU A 515     5711   4462   3132   -455    -83     96  A    C  
ATOM    511  N   PHE A 516      -5.362  -1.004 -13.524  1.00 30.84      A    N  
ANISOU  511  N   PHE A 516     4382   4243   3094   -389    153     48  A    N  
ATOM    512  CA  PHE A 516      -6.089  -0.002 -14.289  1.00 31.96      A    C  
ANISOU  512  CA  PHE A 516     4419   4435   3288   -274    152    -22  A    C  
ATOM    513  C   PHE A 516      -6.196   1.277 -13.455  1.00 35.95      A    C  
ANISOU  513  C   PHE A 516     5063   4882   3714   -227    178    -49  A    C  
ATOM    514  O   PHE A 516      -6.500   1.216 -12.263  1.00 35.38      A    O  
ANISOU  514  O   PHE A 516     5099   4780   3564   -281    283    -77  A    O  
ATOM    515  CB  PHE A 516      -7.481  -0.523 -14.642  1.00 28.73      A    C  
ANISOU  515  CB  PHE A 516     3814   4121   2981   -247    251   -144  A    C  
ATOM    516  CG  PHE A 516      -8.451   0.555 -15.038  1.00 32.78      A    C  
ANISOU  516  CG  PHE A 516     4233   4679   3544    -84    235   -259  A    C  
ATOM    517  CD1 PHE A 516      -8.503   1.009 -16.346  1.00 33.50      A    C  
ANISOU  517  CD1 PHE A 516     4272   4794   3661     64     83   -268  A    C  
ATOM    518  CD2 PHE A 516      -9.317   1.110 -14.103  1.00 33.42      A    C  
ANISOU  518  CD2 PHE A 516     4305   4761   3631    -60    371   -368  A    C  
ATOM    519  CE1 PHE A 516      -9.397   1.998 -16.719  1.00 33.79      A    C  
ANISOU  519  CE1 PHE A 516     4261   4849   3729    263     21   -377  A    C  
ATOM    520  CE2 PHE A 516     -10.212   2.100 -14.467  1.00 33.06      A    C  
ANISOU  520  CE2 PHE A 516     4159   4749   3654    128    332   -497  A    C  
ATOM    521  CZ  PHE A 516     -10.254   2.543 -15.777  1.00 34.17      A    C  
ANISOU  521  CZ  PHE A 516     4257   4906   3819    305    134   -499  A    C  
ATOM    522  N   MET A 517      -5.956   2.429 -14.079  1.00 34.23      A    N  
ANISOU  522  N   MET A 517     4884   4624   3498   -131    100    -43  A    N  
ATOM    523  CA  MET A 517      -5.971   3.701 -13.355  1.00 33.13      A    C  
ANISOU  523  CA  MET A 517     4899   4401   3290    -87    117    -74  A    C  
ATOM    524  C   MET A 517      -6.986   4.705 -13.896  1.00 35.96      A    C  
ANISOU  524  C   MET A 517     5226   4756   3680     96    123   -156  A    C  
ATOM    525  O   MET A 517      -7.487   5.549 -13.157  1.00 36.17      A    O  
ANISOU  525  O   MET A 517     5333   4737   3673    159    184   -230  A    O  
ATOM    526  CB  MET A 517      -4.570   4.319 -13.328  1.00 29.64      A    C  
ANISOU  526  CB  MET A 517     4598   3849   2813   -159     24     -6  A    C  
ATOM    527  CG  MET A 517      -3.603   3.567 -12.433  1.00 25.64      A    C  
ANISOU  527  CG  MET A 517     4142   3331   2271   -290    -33     26  A    C  
ATOM    528  SD  MET A 517      -1.949   4.268 -12.409  1.00 33.38      A    S  
ANISOU  528  SD  MET A 517     5189   4203   3289   -383   -161     30  A    S  
ATOM    529  CE  MET A 517      -2.275   5.913 -11.772  1.00 32.36      A    C  
ANISOU  529  CE  MET A 517     5252   3959   3086   -344   -122    -38  A    C  
ATOM    530  N   GLY A 518      -7.290   4.617 -15.186  1.00 38.29      A    N  
ANISOU  530  N   GLY A 518     5429   5090   4029    205     43   -155  A    N  
ATOM    531  CA  GLY A 518      -8.266   5.509 -15.777  1.00 37.37      A    C  
ANISOU  531  CA  GLY A 518     5303   4963   3934    432    -14   -243  A    C  
ATOM    532  C   GLY A 518      -8.310   5.439 -17.286  1.00 38.84      A    C  
ANISOU  532  C   GLY A 518     5490   5155   4113    559   -152   -213  A    C  
ATOM    533  O   GLY A 518      -7.578   4.675 -17.912  1.00 38.13      A    O  
ANISOU  533  O   GLY A 518     5392   5085   4009    451   -170   -127  A    O  
ATOM    534  N   TYR A 519      -9.179   6.249 -17.877  1.00 39.90      A    N  
ANISOU  534  N   TYR A 519     5657   5260   4242    813   -261   -294  A    N  
ATOM    535  CA  TYR A 519      -9.298   6.288 -19.325  1.00 40.81      A    C  
ANISOU  535  CA  TYR A 519     5855   5356   4295    981   -427   -271  A    C  
ATOM    536  C   TYR A 519      -9.397   7.711 -19.850  1.00 45.86      A    C  
ANISOU  536  C   TYR A 519     6809   5807   4808   1215   -527   -238  A    C  
ATOM    537  O   TYR A 519      -9.841   8.621 -19.151  1.00 45.69      A    O  
ANISOU  537  O   TYR A 519     6840   5715   4807   1322   -509   -304  A    O  
ATOM    538  CB  TYR A 519     -10.503   5.469 -19.791  1.00 38.71      A    C  
ANISOU  538  CB  TYR A 519     5281   5270   4157   1114   -542   -449  A    C  
ATOM    539  CG  TYR A 519     -11.840   6.028 -19.359  1.00 41.36      A    C  
ANISOU  539  CG  TYR A 519     5434   5659   4621   1335   -597   -663  A    C  
ATOM    540  CD1 TYR A 519     -12.392   5.688 -18.131  1.00 41.93      A    C  
ANISOU  540  CD1 TYR A 519     5258   5826   4846   1210   -407   -791  A    C  
ATOM    541  CD2 TYR A 519     -12.553   6.889 -20.183  1.00 44.89      A    C  
ANISOU  541  CD2 TYR A 519     5974   6050   5032   1682   -832   -750  A    C  
ATOM    542  CE1 TYR A 519     -13.615   6.192 -17.734  1.00 44.17      A    C  
ANISOU  542  CE1 TYR A 519     5337   6164   5281   1404   -415  -1023  A    C  
ATOM    543  CE2 TYR A 519     -13.776   7.400 -19.796  1.00 47.57      A    C  
ANISOU  543  CE2 TYR A 519     6102   6445   5529   1915   -899   -984  A    C  
ATOM    544  CZ  TYR A 519     -14.303   7.046 -18.571  1.00 47.86      A    C  
ANISOU  544  CZ  TYR A 519     5837   6594   5756   1763   -672  -1131  A    C  
ATOM    545  OH  TYR A 519     -15.521   7.547 -18.181  1.00 51.12      A    O  
ANISOU  545  OH  TYR A 519     6002   7066   6358   1985   -697  -1398  A    O  
ATOM    546  N   SER A 520      -8.980   7.888 -21.096  1.00 49.75      A    N  
ANISOU  546  N   SER A 520     7552   6196   5152   1296   -619   -137  A    N  
ATOM    547  CA  SER A 520      -9.036   9.183 -21.747  1.00 52.57      A    C  
ANISOU  547  CA  SER A 520     8307   6326   5342   1525   -710    -80  A    C  
ATOM    548  C   SER A 520      -9.977   9.114 -22.936  1.00 52.66      A    C  
ANISOU  548  C   SER A 520     8368   6367   5274   1858   -982   -161  A    C  
ATOM    549  O   SER A 520      -9.988   8.132 -23.679  1.00 51.85      A    O  
ANISOU  549  O   SER A 520     8151   6389   5160   1831  -1054   -176  A    O  
ATOM    550  CB  SER A 520      -7.643   9.607 -22.207  1.00 57.72      A    C  
ANISOU  550  CB  SER A 520     9324   6768   5840   1325   -549    114  A    C  
ATOM    551  OG  SER A 520      -7.318  10.893 -21.715  1.00 65.87      A    O  
ANISOU  551  OG  SER A 520    10639   7571   6819   1323   -460    161  A    O  
ATOM    552  N   THR A 521     -10.773  10.161 -23.105  1.00 54.33      A    N  
ANISOU  552  N   THR A 521     8759   6455   5428   2195  -1157   -231  A    N  
ATOM    553  CA  THR A 521     -11.688  10.247 -24.233  1.00 55.13      A    C  
ANISOU  553  CA  THR A 521     8957   6557   5433   2581  -1488   -328  A    C  
ATOM    554  C   THR A 521     -11.168  11.278 -25.229  1.00 55.60      A    C  
ANISOU  554  C   THR A 521     9675   6289   5160   2746  -1545   -141  A    C  
ATOM    555  O   THR A 521     -11.455  11.208 -26.420  1.00 59.22      A    O  
ANISOU  555  O   THR A 521    10384   6696   5421   2991  -1778   -135  A    O  
ATOM    556  CB  THR A 521     -13.123  10.579 -23.771  1.00 57.79      A    C  
ANISOU  556  CB  THR A 521     8982   7005   5972   2909  -1701   -597  A    C  
ATOM    557  CG2 THR A 521     -13.447  12.054 -23.966  1.00 60.75      A    C  
ANISOU  557  CG2 THR A 521     9775   7108   6200   3267  -1856   -579  A    C  
ATOM    558  OG1 THR A 521     -14.059   9.775 -24.499  1.00 61.46      A    O  
ANISOU  558  OG1 THR A 521     9153   7672   6528   3112  -1982   -801  A    O  
ATOM    559  N   LYS A 522     -10.383  12.224 -24.723  1.00 58.12      A    N  
ANISOU  559  N   LYS A 522    10302   6371   5408   2597  -1317      4  A    N  
ATOM    560  CA  LYS A 522      -9.753  13.251 -25.545  1.00 62.64      A    C  
ANISOU  560  CA  LYS A 522    11546   6580   5673   2669  -1269    197  A    C  
ATOM    561  C   LYS A 522      -8.344  13.501 -25.014  1.00 63.96      A    C  
ANISOU  561  C   LYS A 522    11843   6605   5852   2224   -876    353  A    C  
ATOM    562  O   LYS A 522      -8.127  13.465 -23.802  1.00 61.80      A    O  
ANISOU  562  O   LYS A 522    11256   6431   5796   2011   -733    296  A    O  
ATOM    563  CB  LYS A 522     -10.574  14.533 -25.522  1.00 63.76      A    C  
ANISOU  563  CB  LYS A 522    11975   6508   5743   3057  -1462    134  A    C  
ATOM    564  N   PRO A 523      -7.376  13.766 -25.909  1.00 66.09      A    N  
ANISOU  564  N   PRO A 523    12583   6635   5892   2079   -695    530  A    N  
ATOM    565  CA  PRO A 523      -7.463  13.956 -27.367  1.00 68.85      A    C  
ANISOU  565  CA  PRO A 523    13286   6853   6022   2214   -752    539  A    C  
ATOM    566  C   PRO A 523      -7.876  12.711 -28.158  1.00 67.31      A    C  
ANISOU  566  C   PRO A 523    12852   6906   5817   2301   -936    470  A    C  
ATOM    567  O   PRO A 523      -8.426  12.840 -29.250  1.00 68.56      A    O  
ANISOU  567  O   PRO A 523    13224   7001   5824   2537  -1114    405  A    O  
ATOM    568  CB  PRO A 523      -6.041  14.385 -27.750  1.00 69.30      A    C  
ANISOU  568  CB  PRO A 523    13675   6663   5993   1840   -349    673  A    C  
ATOM    569  CG  PRO A 523      -5.175  13.853 -26.659  1.00 66.12      A    C  
ANISOU  569  CG  PRO A 523    12960   6374   5788   1484   -131    725  A    C  
ATOM    570  CD  PRO A 523      -5.998  13.933 -25.415  1.00 64.00      A    C  
ANISOU  570  CD  PRO A 523    12353   6260   5706   1630   -317    623  A    C  
ATOM    571  N   GLN A 524      -7.619  11.527 -27.618  1.00 65.22      A    N  
ANISOU  571  N   GLN A 524    12175   6909   5696   2114   -900    469  A    N  
ATOM    572  CA  GLN A 524      -8.107  10.305 -28.247  1.00 66.02      A    C  
ANISOU  572  CA  GLN A 524    12004   7263   5816   2197  -1093    370  A    C  
ATOM    573  C   GLN A 524      -8.442   9.255 -27.201  1.00 57.98      A    C  
ANISOU  573  C   GLN A 524    10324   6582   5122   2055  -1114    231  A    C  
ATOM    574  O   GLN A 524      -8.192   9.456 -26.012  1.00 55.23      A    O  
ANISOU  574  O   GLN A 524     9744   6267   4972   1867   -952    221  A    O  
ATOM    575  CB  GLN A 524      -7.101   9.759 -29.265  1.00 71.59      A    C  
ANISOU  575  CB  GLN A 524    12901   7902   6396   1957   -868    464  A    C  
ATOM    576  CG  GLN A 524      -5.725   9.435 -28.711  1.00 73.70      A    C  
ANISOU  576  CG  GLN A 524    13106   8162   6735   1536   -497    586  A    C  
ATOM    577  CD  GLN A 524      -4.796   8.891 -29.780  1.00 81.61      A    C  
ANISOU  577  CD  GLN A 524    14262   9104   7641   1334   -272    638  A    C  
ATOM    578  NE2 GLN A 524      -3.555   9.365 -29.783  1.00 85.03      A    N  
ANISOU  578  NE2 GLN A 524    14882   9343   8083   1028     99    727  A    N  
ATOM    579  OE1 GLN A 524      -5.193   8.061 -30.600  1.00 83.52      A    O  
ANISOU  579  OE1 GLN A 524    14446   9469   7820   1449   -425    574  A    O  
ATOM    580  N   LEU A 525      -9.030   8.149 -27.642  1.00 55.79      A    N  
ANISOU  580  N   LEU A 525     9752   6537   4909   2129  -1298    103  A    N  
ATOM    581  CA  LEU A 525      -9.351   7.058 -26.736  1.00 51.67      A    C  
ANISOU  581  CA  LEU A 525     8624   6304   4704   1952  -1266    -39  A    C  
ATOM    582  C   LEU A 525      -8.068   6.464 -26.191  1.00 45.82      A    C  
ANISOU  582  C   LEU A 525     7773   5582   4052   1537   -938     81  A    C  
ATOM    583  O   LEU A 525      -7.170   6.101 -26.950  1.00 48.49      A    O  
ANISOU  583  O   LEU A 525     8307   5855   4263   1396   -811    186  A    O  
ATOM    584  CB  LEU A 525     -10.171   5.975 -27.433  1.00 53.13      A    C  
ANISOU  584  CB  LEU A 525     8551   6698   4938   2086  -1510   -211  A    C  
ATOM    585  CG  LEU A 525     -11.621   6.305 -27.780  1.00 58.89      A    C  
ANISOU  585  CG  LEU A 525     9186   7493   5695   2502  -1896   -430  A    C  
ATOM    586  CD1 LEU A 525     -12.390   5.017 -28.024  1.00 57.04      A    C  
ANISOU  586  CD1 LEU A 525     8495   7523   5653   2503  -2064   -661  A    C  
ATOM    587  CD2 LEU A 525     -12.288   7.151 -26.693  1.00 60.99      A    C  
ANISOU  587  CD2 LEU A 525     9274   7755   6146   2616  -1900   -526  A    C  
ATOM    588  N   ALA A 526      -7.982   6.376 -24.871  1.00 38.98      A    N  
ANISOU  588  N   ALA A 526     6608   4800   3402   1359   -808     48  A    N  
ATOM    589  CA  ALA A 526      -6.789   5.849 -24.235  1.00 38.96      A    C  
ANISOU  589  CA  ALA A 526     6493   4815   3497   1010   -560    135  A    C  
ATOM    590  C   ALA A 526      -7.132   5.199 -22.909  1.00 41.03      A    C  
ANISOU  590  C   ALA A 526     6354   5250   3986    883   -519     41  A    C  
ATOM    591  O   ALA A 526      -8.087   5.591 -22.241  1.00 40.80      A    O  
ANISOU  591  O   ALA A 526     6199   5268   4036   1015   -588    -66  A    O  
ATOM    592  CB  ALA A 526      -5.760   6.949 -24.035  1.00 38.94      A    C  
ANISOU  592  CB  ALA A 526     6805   4579   3411    883   -374    265  A    C  
ATOM    593  N   ILE A 527      -6.347   4.195 -22.541  1.00 39.40      A    N  
ANISOU  593  N   ILE A 527     5974   5122   3874    635   -396     75  A    N  
ATOM    594  CA  ILE A 527      -6.463   3.571 -21.235  1.00 36.60      A    C  
ANISOU  594  CA  ILE A 527     5350   4879   3679    490   -327     22  A    C  
ATOM    595  C   ILE A 527      -5.169   3.812 -20.474  1.00 35.79      A    C  
ANISOU  595  C   ILE A 527     5325   4684   3590    276   -191    116  A    C  
ATOM    596  O   ILE A 527      -4.079   3.714 -21.037  1.00 34.81      A    O  
ANISOU  596  O   ILE A 527     5294   4491   3440    162   -123    190  A    O  
ATOM    597  CB  ILE A 527      -6.757   2.066 -21.354  1.00 37.58      A    C  
ANISOU  597  CB  ILE A 527     5213   5160   3906    413   -341    -43  A    C  
ATOM    598  CG1 ILE A 527      -8.139   1.853 -21.978  1.00 39.65      A    C  
ANISOU  598  CG1 ILE A 527     5334   5529   4204    615   -497   -198  A    C  
ATOM    599  CG2 ILE A 527      -6.699   1.397 -19.993  1.00 38.90      A    C  
ANISOU  599  CG2 ILE A 527     5210   5385   4187    241   -234    -62  A    C  
ATOM    600  CD1 ILE A 527      -8.413   0.421 -22.396  1.00 39.94      A    C  
ANISOU  600  CD1 ILE A 527     5152   5690   4334    538   -520   -280  A    C  
ATOM    601  N   VAL A 528      -5.298   4.151 -19.197  1.00 35.61      A    N  
ANISOU  601  N   VAL A 528     5259   4659   3614    227   -151     87  A    N  
ATOM    602  CA  VAL A 528      -4.145   4.440 -18.358  1.00 34.05      A    C  
ANISOU  602  CA  VAL A 528     5126   4379   3434     49    -78    135  A    C  
ATOM    603  C   VAL A 528      -3.961   3.366 -17.298  1.00 32.47      A    C  
ANISOU  603  C   VAL A 528     4763   4274   3301    -77    -68    115  A    C  
ATOM    604  O   VAL A 528      -4.902   3.006 -16.590  1.00 30.47      A    O  
ANISOU  604  O   VAL A 528     4423   4095   3057    -42    -51     55  A    O  
ATOM    605  CB  VAL A 528      -4.307   5.789 -17.650  1.00 35.55      A    C  
ANISOU  605  CB  VAL A 528     5481   4449   3577     97    -59    115  A    C  
ATOM    606  CG1 VAL A 528      -3.087   6.093 -16.794  1.00 34.33      A    C  
ANISOU  606  CG1 VAL A 528     5379   4211   3452    -92    -18    128  A    C  
ATOM    607  CG2 VAL A 528      -4.551   6.885 -18.672  1.00 37.48      A    C  
ANISOU  607  CG2 VAL A 528     5958   4554   3727    250    -75    145  A    C  
ATOM    608  N   THR A 529      -2.742   2.857 -17.189  1.00 31.30      A    N  
ANISOU  608  N   THR A 529     4588   4105   3200   -219    -69    153  A    N  
ATOM    609  CA  THR A 529      -2.422   1.878 -16.163  1.00 33.01      A    C  
ANISOU  609  CA  THR A 529     4726   4368   3447   -307    -98    146  A    C  
ATOM    610  C   THR A 529      -1.156   2.293 -15.440  1.00 32.83      A    C  
ANISOU  610  C   THR A 529     4759   4265   3452   -409   -150    138  A    C  
ATOM    611  O   THR A 529      -0.509   3.265 -15.820  1.00 33.37      A    O  
ANISOU  611  O   THR A 529     4886   4246   3549   -448   -126    126  A    O  
ATOM    612  CB  THR A 529      -2.210   0.469 -16.766  1.00 30.92      A    C  
ANISOU  612  CB  THR A 529     4328   4175   3246   -338   -113    164  A    C  
ATOM    613  CG2 THR A 529      -3.335   0.117 -17.721  1.00 28.10      A    C  
ANISOU  613  CG2 THR A 529     3898   3894   2885   -245    -89    139  A    C  
ATOM    614  OG1 THR A 529      -0.957   0.428 -17.459  1.00 32.32      A    O  
ANISOU  614  OG1 THR A 529     4475   4311   3495   -401   -121    178  A    O  
ATOM    615  N   GLN A 530      -0.806   1.548 -14.401  1.00 31.46      A    N  
ANISOU  615  N   GLN A 530     4581   4105   3266   -450   -228    129  A    N  
ATOM    616  CA  GLN A 530       0.460   1.754 -13.720  1.00 33.58      A    C  
ANISOU  616  CA  GLN A 530     4864   4313   3581   -520   -348     83  A    C  
ATOM    617  C   GLN A 530       1.613   1.457 -14.663  1.00 36.77      A    C  
ANISOU  617  C   GLN A 530     5105   4715   4151   -580   -362     57  A    C  
ATOM    618  O   GLN A 530       1.449   0.774 -15.680  1.00 36.83      A    O  
ANISOU  618  O   GLN A 530     5023   4771   4201   -562   -294     94  A    O  
ATOM    619  CB  GLN A 530       0.567   0.830 -12.512  1.00 34.75      A    C  
ANISOU  619  CB  GLN A 530     5090   4465   3649   -504   -469     85  A    C  
ATOM    620  CG  GLN A 530       0.709  -0.636 -12.879  1.00 37.13      A    C  
ANISOU  620  CG  GLN A 530     5303   4806   3997   -486   -499    127  A    C  
ATOM    621  CD  GLN A 530       0.836  -1.533 -11.670  1.00 42.65      A    C  
ANISOU  621  CD  GLN A 530     6170   5458   4578   -453   -622    147  A    C  
ATOM    622  NE2 GLN A 530       1.830  -1.261 -10.834  1.00 45.59      A    N  
ANISOU  622  NE2 GLN A 530     6612   5775   4936   -434   -828     85  A    N  
ATOM    623  OE1 GLN A 530       0.056  -2.468 -11.492  1.00 42.07      A    O  
ANISOU  623  OE1 GLN A 530     6181   5382   4421   -445   -535    206  A    O  
ATOM    624  N   TRP A 531       2.788   1.958 -14.311  1.00 35.90      A    N  
ANISOU  624  N   TRP A 531     4943   4547   4149   -658   -445    -35  A    N  
ATOM    625  CA  TRP A 531       3.994   1.624 -15.046  1.00 35.38      A    C  
ANISOU  625  CA  TRP A 531     4675   4480   4286   -731   -442   -110  A    C  
ATOM    626  C   TRP A 531       4.790   0.540 -14.325  1.00 38.51      A    C  
ANISOU  626  C   TRP A 531     4955   4910   4767   -684   -664   -176  A    C  
ATOM    627  O   TRP A 531       5.062   0.641 -13.128  1.00 40.45      A    O  
ANISOU  627  O   TRP A 531     5276   5130   4964   -652   -861   -232  A    O  
ATOM    628  CB  TRP A 531       4.858   2.862 -15.249  1.00 33.80      A    C  
ANISOU  628  CB  TRP A 531     4439   4185   4216   -869   -364   -218  A    C  
ATOM    629  CG  TRP A 531       6.113   2.573 -15.984  1.00 36.36      A    C  
ANISOU  629  CG  TRP A 531     4523   4506   4787   -974   -304   -335  A    C  
ATOM    630  CD1 TRP A 531       7.359   2.457 -15.453  1.00 38.99      A    C  
ANISOU  630  CD1 TRP A 531     4632   4838   5345  -1035   -453   -521  A    C  
ATOM    631  CD2 TRP A 531       6.250   2.354 -17.392  1.00 39.50      A    C  
ANISOU  631  CD2 TRP A 531     4870   4899   5241  -1024    -74   -304  A    C  
ATOM    632  CE2 TRP A 531       7.614   2.117 -17.645  1.00 41.80      A    C  
ANISOU  632  CE2 TRP A 531     4887   5185   5809  -1135    -46   -480  A    C  
ATOM    633  CE3 TRP A 531       5.353   2.338 -18.465  1.00 41.01      A    C  
ANISOU  633  CE3 TRP A 531     5225   5088   5270   -973     99   -166  A    C  
ATOM    634  NE1 TRP A 531       8.271   2.186 -16.443  1.00 42.87      A    N  
ANISOU  634  NE1 TRP A 531     4894   5330   6066  -1132   -298   -623  A    N  
ATOM    635  CZ2 TRP A 531       8.105   1.864 -18.923  1.00 42.64      A    C  
ANISOU  635  CZ2 TRP A 531     4901   5277   6024  -1217    203   -511  A    C  
ATOM    636  CZ3 TRP A 531       5.841   2.089 -19.736  1.00 42.90      A    C  
ANISOU  636  CZ3 TRP A 531     5414   5306   5578  -1040    305   -183  A    C  
ATOM    637  CH2 TRP A 531       7.205   1.855 -19.953  1.00 44.04      A    C  
ANISOU  637  CH2 TRP A 531     5306   5438   5988  -1171    382   -348  A    C  
ATOM    638  N   CYS A 532       5.162  -0.499 -15.063  1.00 38.21      A    N  
ANISOU  638  N   CYS A 532     4765   4916   4838   -658   -648   -177  A    N  
ATOM    639  CA  CYS A 532       5.966  -1.573 -14.502  1.00 40.17      A    C  
ANISOU  639  CA  CYS A 532     4908   5173   5182   -576   -875   -248  A    C  
ATOM    640  C   CYS A 532       7.435  -1.332 -14.793  1.00 42.07      A    C  
ANISOU  640  C   CYS A 532     4863   5406   5715   -642   -928   -447  A    C  
ATOM    641  O   CYS A 532       7.813  -1.029 -15.924  1.00 39.70      A    O  
ANISOU  641  O   CYS A 532     4413   5108   5562   -751   -701   -494  A    O  
ATOM    642  CB  CYS A 532       5.540  -2.925 -15.071  1.00 41.17      A    C  
ANISOU  642  CB  CYS A 532     5029   5332   5281   -497   -836   -160  A    C  
ATOM    643  SG  CYS A 532       3.866  -3.414 -14.633  1.00 45.89      A    S  
ANISOU  643  SG  CYS A 532     5901   5934   5601   -447   -767     14  A    S  
ATOM    644  N   GLU A 533       8.256  -1.457 -13.758  1.00 46.77      A    N  
ANISOU  644  N   GLU A 533     5393   5985   6393   -575  -1223   -583  A    N  
ATOM    645  CA  GLU A 533       9.698  -1.350 -13.906  1.00 53.47      A    C  
ANISOU  645  CA  GLU A 533     5899   6839   7578   -619  -1323   -833  A    C  
ATOM    646  C   GLU A 533      10.256  -2.723 -14.243  1.00 55.13      A    C  
ANISOU  646  C   GLU A 533     5932   7080   7934   -478  -1437   -884  A    C  
ATOM    647  O   GLU A 533       9.851  -3.722 -13.655  1.00 58.03      A    O  
ANISOU  647  O   GLU A 533     6488   7429   8132   -300  -1633   -776  A    O  
ATOM    648  CB  GLU A 533      10.331  -0.840 -12.611  1.00 59.93      A    C  
ANISOU  648  CB  GLU A 533     6712   7629   8431   -579  -1656   -999  A    C  
ATOM    649  CG  GLU A 533       9.720   0.446 -12.075  1.00 63.61      A    C  
ANISOU  649  CG  GLU A 533     7406   8045   8717   -689  -1582   -951  A    C  
ATOM    650  CD  GLU A 533      10.131   1.673 -12.867  1.00 68.11      A    C  
ANISOU  650  CD  GLU A 533     7814   8576   9490   -928  -1297  -1061  A    C  
ATOM    651  OE1 GLU A 533       9.534   2.747 -12.640  1.00 69.35      A    O  
ANISOU  651  OE1 GLU A 533     8183   8668   9497  -1017  -1181  -1000  A    O  
ATOM    652  OE2 GLU A 533      11.050   1.570 -13.708  1.00 69.89      A    O1-
ANISOU  652  OE2 GLU A 533     7721   8814  10020  -1031  -1167  -1216  A    O1-
ATOM    653  N   GLY A 534      11.184  -2.772 -15.189  1.00 53.97      A    N  
ANISOU  653  N   GLY A 534     5447   6960   8101   -562  -1286  -1055  A    N  
ATOM    654  CA  GLY A 534      11.798  -4.030 -15.570  1.00 54.30      A    C  
ANISOU  654  CA  GLY A 534     5287   7025   8321   -419  -1378  -1141  A    C  
ATOM    655  C   GLY A 534      11.282  -4.565 -16.891  1.00 53.59      A    C  
ANISOU  655  C   GLY A 534     5228   6952   8183   -469  -1043  -1013  A    C  
ATOM    656  O   GLY A 534      10.945  -3.801 -17.794  1.00 53.47      A    O  
ANISOU  656  O   GLY A 534     5254   6936   8126   -649   -704   -958  A    O  
ATOM    657  N   SER A 535      11.215  -5.885 -17.006  1.00 52.17      A    N  
ANISOU  657  N   SER A 535     5067   6767   7989   -297  -1151   -971  A    N  
ATOM    658  CA  SER A 535      10.819  -6.507 -18.260  1.00 49.99      A    C  
ANISOU  658  CA  SER A 535     4805   6505   7684   -330   -868   -891  A    C  
ATOM    659  C   SER A 535       9.812  -7.632 -18.059  1.00 45.89      A    C  
ANISOU  659  C   SER A 535     4565   5951   6919   -191   -961   -691  A    C  
ATOM    660  O   SER A 535       9.485  -7.996 -16.929  1.00 48.21      A    O  
ANISOU  660  O   SER A 535     5058   6195   7065    -68  -1223   -610  A    O  
ATOM    661  CB  SER A 535      12.053  -7.011 -19.007  1.00 52.85      A    C  
ANISOU  661  CB  SER A 535     4795   6883   8400   -314   -791  -1134  A    C  
ATOM    662  OG  SER A 535      13.090  -7.339 -18.103  1.00 56.22      A    O  
ANISOU  662  OG  SER A 535     4986   7303   9071   -157  -1145  -1345  A    O  
ATOM    663  N   SER A 536       9.313  -8.169 -19.165  1.00 40.19      A    N  
ANISOU  663  N   SER A 536     3884   5242   6144   -225   -729   -622  A    N  
ATOM    664  CA  SER A 536       8.391  -9.293 -19.114  1.00 38.55      A    C  
ANISOU  664  CA  SER A 536     3903   4992   5753   -129   -777   -474  A    C  
ATOM    665  C   SER A 536       9.116 -10.553 -18.661  1.00 38.46      A    C  
ANISOU  665  C   SER A 536     3836   4901   5876     70  -1021   -557  A    C  
ATOM    666  O   SER A 536      10.341 -10.626 -18.706  1.00 38.71      A    O  
ANISOU  666  O   SER A 536     3588   4939   6182    144  -1120   -758  A    O  
ATOM    667  CB  SER A 536       7.766  -9.533 -20.485  1.00 35.92      A    C  
ANISOU  667  CB  SER A 536     3604   4693   5352   -211   -495   -427  A    C  
ATOM    668  OG  SER A 536       8.728 -10.036 -21.391  1.00 36.81      A    O  
ANISOU  668  OG  SER A 536     3494   4807   5685   -190   -388   -587  A    O  
ATOM    669  N   LEU A 537       8.350 -11.543 -18.220  1.00 39.27      A    N  
ANISOU  669  N   LEU A 537     4208   4913   5800    158  -1114   -418  A    N  
ATOM    670  CA  LEU A 537       8.906 -12.842 -17.858  1.00 44.17      A    C  
ANISOU  670  CA  LEU A 537     4869   5411   6504    367  -1335   -466  A    C  
ATOM    671  C   LEU A 537       9.556 -13.511 -19.071  1.00 48.53      A    C  
ANISOU  671  C   LEU A 537     5174   5978   7289    402  -1199   -613  A    C  
ATOM    672  O   LEU A 537      10.519 -14.266 -18.932  1.00 51.37      A    O  
ANISOU  672  O   LEU A 537     5399   6269   7850    595  -1389   -757  A    O  
ATOM    673  CB  LEU A 537       7.807 -13.741 -17.289  1.00 41.41      A    C  
ANISOU  673  CB  LEU A 537     4915   4927   5890    396  -1362   -273  A    C  
ATOM    674  CG  LEU A 537       8.152 -15.205 -17.022  1.00 41.84      A    C  
ANISOU  674  CG  LEU A 537     5125   4798   5973    600  -1541   -279  A    C  
ATOM    675  CD1 LEU A 537       9.202 -15.320 -15.928  1.00 42.49      A    C  
ANISOU  675  CD1 LEU A 537     5235   4791   6119    844  -1935   -363  A    C  
ATOM    676  CD2 LEU A 537       6.895 -15.978 -16.657  1.00 40.92      A    C  
ANISOU  676  CD2 LEU A 537     5411   4540   5596    535  -1440    -88  A    C  
ATOM    677  N   TYR A 538       9.019 -13.230 -20.256  1.00 46.93      A    N  
ANISOU  677  N   TYR A 538     4929   5857   7045    235   -881   -590  A    N  
ATOM    678  CA  TYR A 538       9.565 -13.767 -21.495  1.00 50.08      A    C  
ANISOU  678  CA  TYR A 538     5137   6272   7620    242   -695   -731  A    C  
ATOM    679  C   TYR A 538      11.007 -13.323 -21.669  1.00 52.42      A    C  
ANISOU  679  C   TYR A 538     5057   6618   8240    272   -694   -974  A    C  
ATOM    680  O   TYR A 538      11.887 -14.128 -21.967  1.00 55.87      A    O  
ANISOU  680  O   TYR A 538     5296   7015   8916    413   -739  -1151  A    O  
ATOM    681  CB  TYR A 538       8.733 -13.293 -22.687  1.00 51.82      A    C  
ANISOU  681  CB  TYR A 538     5432   6572   7685     57   -376   -665  A    C  
ATOM    682  CG  TYR A 538       9.205 -13.820 -24.025  1.00 56.28      A    C  
ANISOU  682  CG  TYR A 538     5873   7145   8367     51   -151   -804  A    C  
ATOM    683  CD1 TYR A 538      10.223 -13.185 -24.728  1.00 59.67      A    C  
ANISOU  683  CD1 TYR A 538     6054   7631   8989    -20     58   -978  A    C  
ATOM    684  CD2 TYR A 538       8.626 -14.949 -24.591  1.00 57.58      A    C  
ANISOU  684  CD2 TYR A 538     6183   7247   8447     98   -116   -778  A    C  
ATOM    685  CE1 TYR A 538      10.657 -13.664 -25.948  1.00 62.55      A    C  
ANISOU  685  CE1 TYR A 538     6338   7990   9436    -32    306  -1114  A    C  
ATOM    686  CE2 TYR A 538       9.053 -15.433 -25.814  1.00 60.15      A    C  
ANISOU  686  CE2 TYR A 538     6426   7572   8855     98     94   -917  A    C  
ATOM    687  CZ  TYR A 538      10.068 -14.787 -26.486  1.00 63.26      A    C  
ANISOU  687  CZ  TYR A 538     6593   8026   9418     39    311  -1081  A    C  
ATOM    688  OH  TYR A 538      10.498 -15.262 -27.704  1.00 65.87      A    O  
ANISOU  688  OH  TYR A 538     6872   8347   9809     31    563  -1228  A    O  
ATOM    689  N   HIS A 539      11.234 -12.028 -21.488  1.00 51.48      A    N  
ANISOU  689  N   HIS A 539     4829   6580   8151    132   -628  -1005  A    N  
ATOM    690  CA  HIS A 539      12.562 -11.453 -21.629  1.00 52.80      A    C  
ANISOU  690  CA  HIS A 539     4609   6796   8657    100   -583  -1266  A    C  
ATOM    691  C   HIS A 539      13.576 -12.076 -20.673  1.00 54.60      A    C  
ANISOU  691  C   HIS A 539     4626   6979   9142    345   -972  -1450  A    C  
ATOM    692  O   HIS A 539      14.729 -12.280 -21.042  1.00 58.78      A    O  
ANISOU  692  O   HIS A 539     4775   7529  10028    403   -948  -1728  A    O  
ATOM    693  CB  HIS A 539      12.507  -9.942 -21.412  1.00 53.34      A    C  
ANISOU  693  CB  HIS A 539     4662   6921   8684   -103   -474  -1248  A    C  
ATOM    694  CG  HIS A 539      13.821  -9.262 -21.610  1.00 56.42      A    C  
ANISOU  694  CG  HIS A 539     4646   7349   9442   -201   -363  -1539  A    C  
ATOM    695  CD2 HIS A 539      14.435  -8.817 -22.732  1.00 58.95      A    C  
ANISOU  695  CD2 HIS A 539     4765   7690   9944   -386     41  -1700  A    C  
ATOM    696  ND1 HIS A 539      14.679  -8.980 -20.568  1.00 58.95      A    N  
ANISOU  696  ND1 HIS A 539     4719   7679  10001   -120   -674  -1727  A    N  
ATOM    697  CE1 HIS A 539      15.761  -8.389 -21.039  1.00 63.12      A    C  
ANISOU  697  CE1 HIS A 539     4855   8242  10884   -264   -466  -2013  A    C  
ATOM    698  NE2 HIS A 539      15.638  -8.278 -22.351  1.00 63.06      A    N  
ANISOU  698  NE2 HIS A 539     4881   8234  10844   -439     -1  -1994  A    N  
ATOM    699  N   HIS A 540      13.151 -12.371 -19.448  1.00 53.02      A    N  
ANISOU  699  N   HIS A 540     4679   6708   8758    498  -1331  -1312  A    N  
ATOM    700  CA  HIS A 540      14.050 -12.971 -18.465  1.00 56.75      A    C  
ANISOU  700  CA  HIS A 540     5041   7111   9411    780  -1773  -1469  A    C  
ATOM    701  C   HIS A 540      14.404 -14.402 -18.830  1.00 58.53      A    C  
ANISOU  701  C   HIS A 540     5246   7236   9758   1014  -1860  -1542  A    C  
ATOM    702  O   HIS A 540      15.553 -14.820 -18.706  1.00 64.14      A    O  
ANISOU  702  O   HIS A 540     5637   7931  10802   1225  -2080  -1811  A    O  
ATOM    703  CB  HIS A 540      13.425 -12.953 -17.071  1.00 57.44      A    C  
ANISOU  703  CB  HIS A 540     5524   7112   9187    887  -2109  -1274  A    C  
ATOM    704  CG  HIS A 540      13.349 -11.591 -16.460  1.00 58.10      A    C  
ANISOU  704  CG  HIS A 540     5593   7276   9206    730  -2133  -1271  A    C  
ATOM    705  CD2 HIS A 540      12.286 -10.837 -16.091  1.00 55.33      A    C  
ANISOU  705  CD2 HIS A 540     5544   6939   8540    564  -2016  -1049  A    C  
ATOM    706  ND1 HIS A 540      14.470 -10.850 -16.154  1.00 61.43      A    N  
ANISOU  706  ND1 HIS A 540     5640   7768   9933    735  -2292  -1550  A    N  
ATOM    707  CE1 HIS A 540      14.101  -9.696 -15.628  1.00 61.27      A    C  
ANISOU  707  CE1 HIS A 540     5724   7789   9768    571  -2272  -1485  A    C  
ATOM    708  NE2 HIS A 540      12.781  -9.664 -15.577  1.00 57.62      A    N  
ANISOU  708  NE2 HIS A 540     5673   7293   8925    477  -2105  -1178  A    N  
ATOM    709  N   LEU A 541      13.400 -15.149 -19.272  1.00 54.92      A    N  
ANISOU  709  N   LEU A 541     5117   6702   9048    982  -1697  -1324  A    N  
ATOM    710  CA  LEU A 541      13.564 -16.565 -19.561  1.00 55.53      A    C  
ANISOU  710  CA  LEU A 541     5268   6643   9189   1196  -1775  -1357  A    C  
ATOM    711  C   LEU A 541      14.320 -16.823 -20.855  1.00 57.02      A    C  
ANISOU  711  C   LEU A 541     5080   6895   9688   1172  -1500  -1597  A    C  
ATOM    712  O   LEU A 541      15.179 -17.700 -20.910  1.00 59.82      A    O  
ANISOU  712  O   LEU A 541     5256   7173  10300   1420  -1663  -1796  A    O  
ATOM    713  CB  LEU A 541      12.203 -17.253 -19.625  1.00 52.66      A    C  
ANISOU  713  CB  LEU A 541     5371   6167   8472   1125  -1660  -1073  A    C  
ATOM    714  CG  LEU A 541      11.405 -17.344 -18.328  1.00 53.26      A    C  
ANISOU  714  CG  LEU A 541     5889   6119   8228   1169  -1888   -839  A    C  
ATOM    715  CD1 LEU A 541      10.081 -18.047 -18.579  1.00 52.64      A    C  
ANISOU  715  CD1 LEU A 541     6186   5936   7878   1045  -1685   -620  A    C  
ATOM    716  CD2 LEU A 541      12.201 -18.068 -17.253  1.00 55.27      A    C  
ANISOU  716  CD2 LEU A 541     6262   6202   8538   1511  -2343   -905  A    C  
ATOM    717  N   HIS A 542      14.007 -16.057 -21.894  1.00 56.08      A    N  
ANISOU  717  N   HIS A 542     4871   6902   9534    890  -1082  -1587  A    N  
ATOM    718  CA  HIS A 542      14.476 -16.397 -23.231  1.00 55.40      A    C  
ANISOU  718  CA  HIS A 542     4565   6850   9636    838   -744  -1766  A    C  
ATOM    719  C   HIS A 542      15.434 -15.387 -23.855  1.00 61.01      A    C  
ANISOU  719  C   HIS A 542     4858   7689  10634    667   -460  -2016  A    C  
ATOM    720  O   HIS A 542      16.076 -15.684 -24.860  1.00 63.22      A    O  
ANISOU  720  O   HIS A 542     4908   7986  11129    645   -177  -2226  A    O  
ATOM    721  CB  HIS A 542      13.282 -16.622 -24.159  1.00 49.50      A    C  
ANISOU  721  CB  HIS A 542     4144   6094   8570    672   -451  -1562  A    C  
ATOM    722  CG  HIS A 542      12.233 -17.516 -23.580  1.00 47.86      A    C  
ANISOU  722  CG  HIS A 542     4335   5756   8094    764   -656  -1332  A    C  
ATOM    723  CD2 HIS A 542      10.933 -17.288 -23.275  1.00 45.46      A    C  
ANISOU  723  CD2 HIS A 542     4364   5446   7462    633   -647  -1079  A    C  
ATOM    724  ND1 HIS A 542      12.478 -18.832 -23.243  1.00 49.53      A    N  
ANISOU  724  ND1 HIS A 542     4638   5799   8381   1011   -878  -1369  A    N  
ATOM    725  CE1 HIS A 542      11.377 -19.372 -22.755  1.00 48.53      A    C  
ANISOU  725  CE1 HIS A 542     4910   5556   7974    998   -967  -1138  A    C  
ATOM    726  NE2 HIS A 542      10.423 -18.457 -22.766  1.00 46.24      A    N  
ANISOU  726  NE2 HIS A 542     4742   5374   7453    765   -823   -974  A    N  
ATOM    727  N   ALA A 543      15.534 -14.198 -23.273  1.00 64.01      A    N  
ANISOU  727  N   ALA A 543     5157   8144  11020    528   -502  -2007  A    N  
ATOM    728  CA  ALA A 543      16.419 -13.179 -23.827  1.00 68.82      A    C  
ANISOU  728  CA  ALA A 543     5397   8846  11907    319   -192  -2248  A    C  
ATOM    729  C   ALA A 543      17.561 -12.854 -22.875  1.00 77.33      A    C  
ANISOU  729  C   ALA A 543     6166   9932  13283    418   -492  -2483  A    C  
ATOM    730  O   ALA A 543      18.734 -12.984 -23.225  1.00 82.59      A    O  
ANISOU  730  O   ALA A 543     6578  10584  14218    426   -390  -2748  A    O  
ATOM    731  CB  ALA A 543      15.636 -11.921 -24.172  1.00 64.71      A    C  
ANISOU  731  CB  ALA A 543     5117   8368  11101     16     99  -2047  A    C  
ATOM    732  N   SER A 544      17.203 -12.426 -21.670  1.00 79.36      A    N  
ANISOU  732  N   SER A 544     6553  10189  13412    479   -856  -2362  A    N  
ATOM    733  CA  SER A 544      18.177 -12.066 -20.650  1.00 84.29      A    C  
ANISOU  733  CA  SER A 544     7040  10796  14189    576  -1170  -2536  A    C  
ATOM    734  C   SER A 544      18.934 -13.277 -20.119  1.00 90.39      A    C  
ANISOU  734  C   SER A 544     7759  11479  15104    922  -1552  -2684  A    C  
ATOM    735  O   SER A 544      20.065 -13.146 -19.647  1.00 93.82      A    O  
ANISOU  735  O   SER A 544     7976  11902  15770   1004  -1727  -2939  A    O  
ATOM    736  CB  SER A 544      17.481 -11.353 -19.491  1.00 82.68      A    C  
ANISOU  736  CB  SER A 544     7073  10599  13742    565  -1458  -2347  A    C  
ATOM    737  OG  SER A 544      18.340 -11.252 -18.370  1.00 87.29      A    O  
ANISOU  737  OG  SER A 544     7596  11145  14424    733  -1841  -2504  A    O  
ATOM    738  N   GLU A 545      18.309 -14.448 -20.198  1.00 92.00      A    N  
ANISOU  738  N   GLU A 545     8176  11606  15174   1127  -1683  -2536  A    N  
ATOM    739  CA  GLU A 545      18.855 -15.656 -19.587  1.00 97.84      A    C  
ANISOU  739  CA  GLU A 545     8986  12217  15971   1479  -2083  -2618  A    C  
ATOM    740  C   GLU A 545      19.143 -15.425 -18.110  1.00101.58      A    C  
ANISOU  740  C   GLU A 545     9618  12635  16343   1647  -2560  -2616  A    C  
ATOM    741  O   GLU A 545      20.178 -15.846 -17.593  1.00106.45      A    O  
ANISOU  741  O   GLU A 545    10120  13193  17133   1858  -2846  -2840  A    O  
ATOM    742  CB  GLU A 545      20.117 -16.130 -20.314  1.00103.14      A    C  
ANISOU  742  CB  GLU A 545     9295  12892  17003   1527  -1944  -2951  A    C  
ATOM    743  CG  GLU A 545      19.861 -16.748 -21.677  1.00103.84      A    C  
ANISOU  743  CG  GLU A 545     9328  12984  17142   1452  -1540  -2953  A    C  
ATOM    744  CD  GLU A 545      19.126 -18.073 -21.595  1.00104.26      A    C  
ANISOU  744  CD  GLU A 545     9698  12896  17018   1713  -1734  -2770  A    C  
ATOM    745  OE1 GLU A 545      19.735 -19.112 -21.927  1.00107.12      A    O  
ANISOU  745  OE1 GLU A 545     9988  13176  17536   1905  -1784  -2922  A    O  
ATOM    746  OE2 GLU A 545      17.938 -18.080 -21.207  1.00100.98      A    O1-
ANISOU  746  OE2 GLU A 545     9618  12437  16313   1722  -1827  -2481  A    O1-
ATOM    747  N   THR A 546      18.224 -14.729 -17.447  1.00 98.61      A    N  
ANISOU  747  N   THR A 546     9513  12276  15679   1550  -2638  -2376  A    N  
ATOM    748  CA  THR A 546      18.321 -14.487 -16.015  1.00 98.35      A    C  
ANISOU  748  CA  THR A 546     9726  12176  15466   1697  -3061  -2335  A    C  
ATOM    749  C   THR A 546      18.235 -15.814 -15.273  1.00 98.31      A    C  
ANISOU  749  C   THR A 546    10105  11976  15273   2044  -3447  -2236  A    C  
ATOM    750  O   THR A 546      17.290 -16.578 -15.466  1.00 96.67      A    O  
ANISOU  750  O   THR A 546    10217  11670  14843   2100  -3410  -1992  A    O  
ATOM    751  CB  THR A 546      17.182 -13.574 -15.527  1.00 93.63      A    C  
ANISOU  751  CB  THR A 546     9406  11620  14547   1514  -3025  -2067  A    C  
ATOM    752  CG2 THR A 546      17.299 -13.325 -14.033  1.00 94.64      A    C  
ANISOU  752  CG2 THR A 546     9832  11667  14461   1664  -3430  -2032  A    C  
ATOM    753  OG1 THR A 546      17.229 -12.322 -16.223  1.00 92.46      A    O  
ANISOU  753  OG1 THR A 546     8954  11627  14548   1183  -2655  -2146  A    O  
ATOM    754  N   LYS A 547      19.222 -16.093 -14.430  1.00 99.90      A    N  
ANISOU  754  N   LYS A 547    10299  12099  15558   2276  -3811  -2434  A    N  
ATOM    755  CA  LYS A 547      19.240 -17.353 -13.697  1.00100.35      A    C  
ANISOU  755  CA  LYS A 547    10764  11946  15419   2611  -4178  -2357  A    C  
ATOM    756  C   LYS A 547      18.413 -17.268 -12.421  1.00 97.98      A    C  
ANISOU  756  C   LYS A 547    11056  11516  14656   2677  -4422  -2081  A    C  
ATOM    757  O   LYS A 547      18.818 -16.629 -11.450  1.00101.93      A    O  
ANISOU  757  O   LYS A 547    11612  12019  15098   2720  -4660  -2170  A    O  
ATOM    758  CB  LYS A 547      20.675 -17.767 -13.371  1.00105.53      A    C  
ANISOU  758  CB  LYS A 547    11173  12562  16362   2858  -4483  -2714  A    C  
ATOM    759  CG  LYS A 547      21.527 -18.057 -14.595  1.00106.38      A    C  
ANISOU  759  CG  LYS A 547    10749  12762  16909   2817  -4237  -2998  A    C  
ATOM    760  CD  LYS A 547      22.939 -18.462 -14.203  1.00111.85      A    C  
ANISOU  760  CD  LYS A 547    11191  13410  17895   3075  -4573  -3375  A    C  
ATOM    761  CE  LYS A 547      23.789 -18.765 -15.427  1.00112.79      A    C  
ANISOU  761  CE  LYS A 547    10790  13614  18450   3021  -4294  -3670  A    C  
ATOM    762  NZ  LYS A 547      25.188 -19.123 -15.062  1.00118.67      A    N1+
ANISOU  762  NZ  LYS A 547    11244  14324  19520   3271  -4627  -4077  A    N1+
ATOM    763  N   PHE A 548      17.250 -17.911 -12.428  1.00 91.14      A    N  
ANISOU  763  N   PHE A 548    10646  10522  13460   2674  -4336  -1757  A    N  
ATOM    764  CA  PHE A 548      16.389 -17.933 -11.254  1.00 88.14      A    C  
ANISOU  764  CA  PHE A 548    10892   9989  12608   2707  -4487  -1482  A    C  
ATOM    765  C   PHE A 548      16.591 -19.211 -10.462  1.00 90.14      A    C  
ANISOU  765  C   PHE A 548    11634   9976  12641   3013  -4790  -1434  A    C  
ATOM    766  O   PHE A 548      16.639 -20.302 -11.026  1.00 90.08      A    O  
ANISOU  766  O   PHE A 548    11672   9857  12699   3136  -4757  -1423  A    O  
ATOM    767  CB  PHE A 548      14.914 -17.826 -11.647  1.00 84.02      A    C  
ANISOU  767  CB  PHE A 548    10638   9459  11826   2487  -4176  -1152  A    C  
ATOM    768  CG  PHE A 548      14.529 -16.499 -12.226  1.00 80.93      A    C  
ANISOU  768  CG  PHE A 548     9893   9309  11548   2187  -3913  -1157  A    C  
ATOM    769  CD1 PHE A 548      14.668 -15.338 -11.485  1.00 80.66      A    C  
ANISOU  769  CD1 PHE A 548     9827   9373  11447   2083  -3991  -1205  A    C  
ATOM    770  CD2 PHE A 548      14.001 -16.415 -13.503  1.00 77.09      A    C  
ANISOU  770  CD2 PHE A 548     9136   8934  11222   2011  -3585  -1117  A    C  
ATOM    771  CE1 PHE A 548      14.306 -14.116 -12.013  1.00 77.08      A    C  
ANISOU  771  CE1 PHE A 548     9084   9121  11083   1797  -3740  -1209  A    C  
ATOM    772  CE2 PHE A 548      13.635 -15.197 -14.037  1.00 73.97      A    C  
ANISOU  772  CE2 PHE A 548     8489   8745  10870   1678  -3251  -1114  A    C  
ATOM    773  CZ  PHE A 548      13.788 -14.044 -13.291  1.00 74.44      A    C  
ANISOU  773  CZ  PHE A 548     8501   8896  10885   1603  -3391  -1165  A    C  
ATOM    774  N   GLU A 549      16.707 -19.077  -9.148  1.00 92.62      A    N  
ANISOU  774  N   GLU A 549    12338  10173  12680   3137  -5075  -1412  A    N  
ATOM    775  CA  GLU A 549      16.705 -20.247  -8.295  1.00 95.36      A    C  
ANISOU  775  CA  GLU A 549    13273  10236  12723   3399  -5327  -1321  A    C  
ATOM    776  C   GLU A 549      15.291 -20.798  -8.359  1.00 89.94      A    C  
ANISOU  776  C   GLU A 549    13113   9396  11665   3248  -5030   -948  A    C  
ATOM    777  O   GLU A 549      14.355 -20.061  -8.664  1.00 85.34      A    O  
ANISOU  777  O   GLU A 549    12505   8923  10998   2973  -4729   -776  A    O  
ATOM    778  CB  GLU A 549      17.087 -19.873  -6.865  1.00100.19      A    C  
ANISOU  778  CB  GLU A 549    14210  10754  13102   3548  -5671  -1388  A    C  
ATOM    779  CG  GLU A 549      18.144 -18.777  -6.769  1.00102.51      A    C  
ANISOU  779  CG  GLU A 549    13955  11250  13743   3555  -5851  -1717  A    C  
ATOM    780  CD  GLU A 549      19.565 -19.276  -6.987  1.00107.70      A    C  
ANISOU  780  CD  GLU A 549    14218  11915  14789   3824  -6158  -2087  A    C  
ATOM    781  OE1 GLU A 549      19.762 -20.270  -7.718  1.00108.34      A    O  
ANISOU  781  OE1 GLU A 549    14208  11943  15013   3930  -6117  -2116  A    O  
ATOM    782  OE2 GLU A 549      20.493 -18.664  -6.418  1.00110.82      A    O1-
ANISOU  782  OE2 GLU A 549    14386  12363  15356   3933  -6441  -2366  A    O1-
ATOM    783  N   MET A 550      15.139 -22.089  -8.088  1.00 91.43      A    N  
ANISOU  783  N   MET A 550    13776   9321  11643   3420  -5101   -838  A    N  
ATOM    784  CA  MET A 550      13.846 -22.757  -8.212  1.00 86.42      A    C  
ANISOU  784  CA  MET A 550    13637   8504  10696   3260  -4776   -513  A    C  
ATOM    785  C   MET A 550      12.761 -22.054  -7.401  1.00 83.18      A    C  
ANISOU  785  C   MET A 550    13638   8068   9898   3026  -4580   -282  A    C  
ATOM    786  O   MET A 550      11.590 -22.044  -7.787  1.00 79.72      A    O  
ANISOU  786  O   MET A 550    13364   7605   9322   2769  -4205    -55  A    O  
ATOM    787  CB  MET A 550      13.959 -24.225  -7.789  1.00 88.22      A    C  
ANISOU  787  CB  MET A 550    14387   8417  10716   3489  -4910   -451  A    C  
ATOM    788  CG  MET A 550      12.702 -25.039  -8.045  1.00 85.45      A    C  
ANISOU  788  CG  MET A 550    14503   7855  10110   3299  -4526   -154  A    C  
ATOM    789  SD  MET A 550      12.172 -24.955  -9.764  1.00 77.50      A    S  
ANISOU  789  SD  MET A 550    12985   6999   9464   3076  -4145   -128  A    S  
ATOM    790  CE  MET A 550      13.644 -25.529 -10.601  1.00 96.28      A    C  
ANISOU  790  CE  MET A 550    14811   9455  12316   3389  -4420   -455  A    C  
ATOM    791  N   LYS A 551      13.164 -21.454  -6.285  1.00 84.14      A    N  
ANISOU  791  N   LYS A 551    13915   8191   9864   3115  -4828   -364  A    N  
ATOM    792  CA  LYS A 551      12.237 -20.752  -5.407  1.00 83.15      A    C  
ANISOU  792  CA  LYS A 551    14182   8037   9374   2916  -4654   -183  A    C  
ATOM    793  C   LYS A 551      11.566 -19.568  -6.102  1.00 76.79      A    C  
ANISOU  793  C   LYS A 551    12984   7492   8700   2607  -4354   -120  A    C  
ATOM    794  O   LYS A 551      10.373 -19.333  -5.922  1.00 75.41      A    O  
ANISOU  794  O   LYS A 551    13110   7281   8261   2362  -4023    101  A    O  
ATOM    795  CB  LYS A 551      12.950 -20.291  -4.132  1.00 89.56      A    C  
ANISOU  795  CB  LYS A 551    15185   8799  10043   3106  -5018   -330  A    C  
ATOM    796  CG  LYS A 551      12.075 -19.474  -3.191  1.00 89.73      A    C  
ANISOU  796  CG  LYS A 551    15584   8799   9711   2913  -4840   -179  A    C  
ATOM    797  CD  LYS A 551      12.695 -19.364  -1.808  1.00 94.50      A    C  
ANISOU  797  CD  LYS A 551    16567   9250  10089   3149  -5206   -297  A    C  
ATOM    798  CE  LYS A 551      11.717 -18.757  -0.816  1.00 94.39      A    C  
ANISOU  798  CE  LYS A 551    17034   9156   9674   2963  -4980   -128  A    C  
ATOM    799  NZ  LYS A 551      12.187 -18.911   0.590  1.00100.79      A    N1+
ANISOU  799  NZ  LYS A 551    18377   9736  10182   3215  -5312   -208  A    N1+
ATOM    800  N   LYS A 552      12.334 -18.829  -6.898  1.00 74.90      A    N  
ANISOU  800  N   LYS A 552    12075   7509   8875   2611  -4450   -332  A    N  
ATOM    801  CA  LYS A 552      11.797 -17.688  -7.636  1.00 70.91      A    C  
ANISOU  801  CA  LYS A 552    11178   7253   8510   2336  -4192   -297  A    C  
ATOM    802  C   LYS A 552      10.817 -18.138  -8.718  1.00 64.42      A    C  
ANISOU  802  C   LYS A 552    10348   6422   7708   2161  -3845   -111  A    C  
ATOM    803  O   LYS A 552       9.752 -17.549  -8.887  1.00 61.06      A    O  
ANISOU  803  O   LYS A 552    10008   6059   7132   1911  -3563     61  A    O  
ATOM    804  CB  LYS A 552      12.929 -16.887  -8.280  1.00 74.21      A    C  
ANISOU  804  CB  LYS A 552    10884   7924   9389   2366  -4336   -599  A    C  
ATOM    805  CG  LYS A 552      12.897 -15.394  -7.982  1.00 76.05      A    C  
ANISOU  805  CG  LYS A 552    10901   8351   9642   2186  -4302   -660  A    C  
ATOM    806  CD  LYS A 552      11.482 -14.830  -8.007  1.00 75.48      A    C  
ANISOU  806  CD  LYS A 552    11083   8314   9281   1915  -3981   -394  A    C  
ATOM    807  CE  LYS A 552      11.500 -13.316  -7.843  1.00 77.20      A    C  
ANISOU  807  CE  LYS A 552    11045   8734   9554   1735  -3941   -479  A    C  
ATOM    808  NZ  LYS A 552      10.362 -12.809  -7.024  1.00 77.25      A    N1+
ANISOU  808  NZ  LYS A 552    11520   8684   9147   1581  -3774   -264  A    N1+
ATOM    809  N   LEU A 553      11.194 -19.181  -9.449  1.00 63.37      A    N  
ANISOU  809  N   LEU A 553    10110   6198   7769   2301  -3872   -164  A    N  
ATOM    810  CA  LEU A 553      10.378 -19.708 -10.535  1.00 60.54      A    C  
ANISOU  810  CA  LEU A 553     9734   5792   7475   2169  -3569    -24  A    C  
ATOM    811  C   LEU A 553       9.015 -20.170 -10.043  1.00 58.21      A    C  
ANISOU  811  C   LEU A 553    10066   5276   6775   1981  -3278    269  A    C  
ATOM    812  O   LEU A 553       8.008 -20.015 -10.731  1.00 53.64      A    O  
ANISOU  812  O   LEU A 553     9394   4786   6201   1662  -2845    357  A    O  
ATOM    813  CB  LEU A 553      11.097 -20.869 -11.219  1.00 64.83      A    C  
ANISOU  813  CB  LEU A 553    10133   6227   8271   2384  -3663   -153  A    C  
ATOM    814  CG  LEU A 553      12.385 -20.532 -11.970  1.00 65.70      A    C  
ANISOU  814  CG  LEU A 553     9551   6561   8853   2515  -3823   -478  A    C  
ATOM    815  CD1 LEU A 553      13.063 -21.806 -12.444  1.00 67.06      A    C  
ANISOU  815  CD1 LEU A 553     9681   6588   9210   2745  -3912   -602  A    C  
ATOM    816  CD2 LEU A 553      12.091 -19.613 -13.144  1.00 60.95      A    C  
ANISOU  816  CD2 LEU A 553     8426   6234   8498   2235  -3487   -538  A    C  
ATOM    817  N   ILE A 554       8.988 -20.738  -8.844  1.00 62.67      A    N  
ANISOU  817  N   ILE A 554    11161   5633   7017   2068  -3363    338  A    N  
ATOM    818  CA  ILE A 554       7.743 -21.241  -8.283  1.00 63.29      A    C  
ANISOU  818  CA  ILE A 554    11826   5495   6726   1859  -3025    571  A    C  
ATOM    819  C   ILE A 554       6.911 -20.106  -7.685  1.00 60.56      A    C  
ANISOU  819  C   ILE A 554    11576   5270   6163   1615  -2822    664  A    C  
ATOM    820  O   ILE A 554       5.684 -20.112  -7.777  1.00 58.87      A    O  
ANISOU  820  O   ILE A 554    11564   5005   5800   1330  -2415    819  A    O  
ATOM    821  CB  ILE A 554       8.003 -22.375  -7.266  1.00 69.29      A    C  
ANISOU  821  CB  ILE A 554    13148   5963   7216   2042  -3157    597  A    C  
ATOM    822  CG1 ILE A 554       8.598 -23.587  -7.986  1.00 72.94      A    C  
ANISOU  822  CG1 ILE A 554    13544   6288   7882   2240  -3274    531  A    C  
ATOM    823  CG2 ILE A 554       6.725 -22.775  -6.544  1.00 68.41      A    C  
ANISOU  823  CG2 ILE A 554    13627   5644   6722   1790  -2761    799  A    C  
ATOM    824  CD1 ILE A 554       8.801 -24.784  -7.094  1.00 79.96      A    C  
ANISOU  824  CD1 ILE A 554    15018   6870   8495   2419  -3393    569  A    C  
ATOM    825  N   ASP A 555       7.579 -19.119  -7.097  1.00 61.38      A    N  
ANISOU  825  N   ASP A 555    11506   5536   6281   1713  -3084    539  A    N  
ATOM    826  CA  ASP A 555       6.877 -17.934  -6.626  1.00 62.78      A    C  
ANISOU  826  CA  ASP A 555    11708   5850   6296   1497  -2906    597  A    C  
ATOM    827  C   ASP A 555       6.214 -17.198  -7.789  1.00 58.15      A    C  
ANISOU  827  C   ASP A 555    10729   5477   5890   1261  -2656    646  A    C  
ATOM    828  O   ASP A 555       5.074 -16.747  -7.679  1.00 57.72      A    O  
ANISOU  828  O   ASP A 555    10782   5466   5682    982  -2279    749  A    O  
ATOM    829  CB  ASP A 555       7.816 -16.987  -5.885  1.00 68.27      A    C  
ANISOU  829  CB  ASP A 555    12241   6672   7026   1648  -3249    423  A    C  
ATOM    830  CG  ASP A 555       7.092 -15.769  -5.344  1.00 73.38      A    C  
ANISOU  830  CG  ASP A 555    12947   7438   7496   1436  -3061    475  A    C  
ATOM    831  OD1 ASP A 555       6.030 -15.951  -4.709  1.00 77.44      A    O  
ANISOU  831  OD1 ASP A 555    13905   7815   7702   1272  -2749    627  A    O  
ATOM    832  OD2 ASP A 555       7.566 -14.633  -5.568  1.00 72.66      A    O1-
ANISOU  832  OD2 ASP A 555    12444   7574   7591   1418  -3194    345  A    O1-
ATOM    833  N   ILE A 556       6.938 -17.076  -8.899  1.00 54.21      A    N  
ANISOU  833  N   ILE A 556     9637   5171   5788   1305  -2733    477  A    N  
ATOM    834  CA  ILE A 556       6.397 -16.450 -10.100  1.00 51.34      A    C  
ANISOU  834  CA  ILE A 556     8768   5071   5667   1021  -2363    423  A    C  
ATOM    835  C   ILE A 556       5.189 -17.233 -10.599  1.00 51.48      A    C  
ANISOU  835  C   ILE A 556     8957   4991   5611    800  -1953    550  A    C  
ATOM    836  O   ILE A 556       4.154 -16.653 -10.935  1.00 48.93      A    O  
ANISOU  836  O   ILE A 556     8519   4805   5269    530  -1611    585  A    O  
ATOM    837  CB  ILE A 556       7.450 -16.366 -11.221  1.00 50.58      A    C  
ANISOU  837  CB  ILE A 556     8085   5149   5983   1113  -2480    215  A    C  
ATOM    838  CG1 ILE A 556       8.563 -15.394 -10.828  1.00 53.40      A    C  
ANISOU  838  CG1 ILE A 556     8159   5644   6485   1252  -2817     35  A    C  
ATOM    839  CG2 ILE A 556       6.809 -15.917 -12.521  1.00 45.37      A    C  
ANISOU  839  CG2 ILE A 556     7037   4701   5501    838  -2083    189  A    C  
ATOM    840  CD1 ILE A 556       9.677 -15.290 -11.849  1.00 54.18      A    C  
ANISOU  840  CD1 ILE A 556     7672   5899   7014   1325  -2895   -206  A    C  
ATOM    841  N   ALA A 557       5.327 -18.555 -10.632  1.00 53.82      A    N  
ANISOU  841  N   ALA A 557     9527   5039   5883    926  -2005    598  A    N  
ATOM    842  CA  ALA A 557       4.233 -19.440 -11.014  1.00 51.74      A    C  
ANISOU  842  CA  ALA A 557     9469   4631   5558    714  -1633    696  A    C  
ATOM    843  C   ALA A 557       3.057 -19.277 -10.060  1.00 49.53      A    C  
ANISOU  843  C   ALA A 557     9634   4232   4954    501  -1357    847  A    C  
ATOM    844  O   ALA A 557       1.897 -19.284 -10.470  1.00 47.17      A    O  
ANISOU  844  O   ALA A 557     9264   3983   4675    208   -960    862  A    O  
ATOM    845  CB  ALA A 557       4.706 -20.892 -11.028  1.00 53.48      A    C  
ANISOU  845  CB  ALA A 557     9996   4544   5778    919  -1777    723  A    C  
ATOM    846  N   ARG A 558       3.370 -19.129  -8.780  1.00 50.81      A    N  
ANISOU  846  N   ARG A 558    10252   4234   4820    656  -1572    934  A    N  
ATOM    847  CA  ARG A 558       2.350 -18.971  -7.757  1.00 54.97      A    C  
ANISOU  847  CA  ARG A 558    11267   4618   5001    470  -1296   1071  A    C  
ATOM    848  C   ARG A 558       1.620 -17.638  -7.901  1.00 53.09      A    C  
ANISOU  848  C   ARG A 558    10666   4686   4822    233  -1057   1012  A    C  
ATOM    849  O   ARG A 558       0.397 -17.570  -7.770  1.00 52.66      A    O  
ANISOU  849  O   ARG A 558    10711   4616   4682    -45   -639   1051  A    O  
ATOM    850  CB  ARG A 558       2.989 -19.076  -6.376  1.00 64.24      A    C  
ANISOU  850  CB  ARG A 558    12812   5673   5924    689  -1554   1044  A    C  
ATOM    851  CG  ARG A 558       2.006 -19.223  -5.237  1.00 71.94      A    C  
ANISOU  851  CG  ARG A 558    14257   6496   6582    505  -1212   1103  A    C  
ATOM    852  CD  ARG A 558       2.233 -18.138  -4.213  1.00 76.39      A    C  
ANISOU  852  CD  ARG A 558    14894   7154   6978    572  -1360   1053  A    C  
ATOM    853  NE  ARG A 558       3.653 -17.932  -3.943  1.00 78.64      A    N  
ANISOU  853  NE  ARG A 558    15087   7473   7319    907  -1901    951  A    N  
ATOM    854  CZ  ARG A 558       4.259 -18.257  -2.805  1.00 81.71      A    C  
ANISOU  854  CZ  ARG A 558    15874   7680   7491   1122  -2154    908  A    C  
ATOM    855  NH1 ARG A 558       3.570 -18.804  -1.814  1.00 85.59      A    N1+
ANISOU  855  NH1 ARG A 558    16932   7929   7660   1040  -1911    978  A    N1+
ATOM    856  NH2 ARG A 558       5.556 -18.026  -2.658  1.00 81.72      A    N  
ANISOU  856  NH2 ARG A 558    15702   7738   7610   1414  -2646    771  A    N  
ATOM    857  N   GLN A 559       2.374 -16.580  -8.177  1.00 51.43      A    N  
ANISOU  857  N   GLN A 559    10028   4737   4776    342  -1314    898  A    N  
ATOM    858  CA  GLN A 559       1.793 -15.252  -8.326  1.00 49.46      A    C  
ANISOU  858  CA  GLN A 559     9460   4753   4582    159  -1132    840  A    C  
ATOM    859  C   GLN A 559       0.902 -15.178  -9.557  1.00 45.73      A    C  
ANISOU  859  C   GLN A 559     8559   4459   4356    -76   -789    780  A    C  
ATOM    860  O   GLN A 559      -0.179 -14.589  -9.521  1.00 44.45      A    O  
ANISOU  860  O   GLN A 559     8334   4395   4161   -285   -487    773  A    O  
ATOM    861  CB  GLN A 559       2.889 -14.193  -8.414  1.00 51.97      A    C  
ANISOU  861  CB  GLN A 559     9430   5272   5043    319  -1478    719  A    C  
ATOM    862  CG  GLN A 559       3.633 -13.955  -7.117  1.00 57.26      A    C  
ANISOU  862  CG  GLN A 559    10478   5816   5462    535  -1839    733  A    C  
ATOM    863  CD  GLN A 559       4.539 -12.749  -7.194  1.00 59.70      A    C  
ANISOU  863  CD  GLN A 559    10396   6341   5946    617  -2115    575  A    C  
ATOM    864  NE2 GLN A 559       5.835 -12.970  -7.011  1.00 62.45      A    N  
ANISOU  864  NE2 GLN A 559    10676   6654   6399    884  -2563    464  A    N  
ATOM    865  OE1 GLN A 559       4.081 -11.629  -7.427  1.00 58.59      A    O  
ANISOU  865  OE1 GLN A 559    10007   6388   5867    445  -1928    533  A    O  
ATOM    866  N   THR A 560       1.367 -15.776 -10.648  1.00 42.57      A    N  
ANISOU  866  N   THR A 560     7869   4102   4205    -22   -856    715  A    N  
ATOM    867  CA  THR A 560       0.597 -15.816 -11.880  1.00 38.62      A    C  
ANISOU  867  CA  THR A 560     7004   3755   3917   -210   -588    643  A    C  
ATOM    868  C   THR A 560      -0.692 -16.595 -11.666  1.00 37.84      A    C  
ANISOU  868  C   THR A 560     7155   3500   3721   -430   -236    691  A    C  
ATOM    869  O   THR A 560      -1.748 -16.214 -12.164  1.00 38.41      A    O  
ANISOU  869  O   THR A 560     6994   3716   3884   -631     28    622  A    O  
ATOM    870  CB  THR A 560       1.404 -16.454 -13.022  1.00 41.57      A    C  
ANISOU  870  CB  THR A 560     7101   4158   4534    -96   -723    560  A    C  
ATOM    871  CG2 THR A 560       0.609 -16.428 -14.322  1.00 40.86      A    C  
ANISOU  871  CG2 THR A 560     6670   4231   4622   -274   -479    473  A    C  
ATOM    872  OG1 THR A 560       2.630 -15.732 -13.201  1.00 41.32      A    O  
ANISOU  872  OG1 THR A 560     6808   4263   4629     80  -1004    481  A    O  
ATOM    873  N   ALA A 561      -0.600 -17.682 -10.910  1.00 38.99      A    N  
ANISOU  873  N   ALA A 561     7788   3337   3689   -387   -236    793  A    N  
ATOM    874  CA  ALA A 561      -1.775 -18.464 -10.550  1.00 45.31      A    C  
ANISOU  874  CA  ALA A 561     8899   3934   4384   -629    145    836  A    C  
ATOM    875  C   ALA A 561      -2.767 -17.649  -9.718  1.00 45.77      A    C  
ANISOU  875  C   ALA A 561     9070   4041   4281   -817    422    848  A    C  
ATOM    876  O   ALA A 561      -3.976 -17.755  -9.905  1.00 49.22      A    O  
ANISOU  876  O   ALA A 561     9405   4498   4796  -1083    799    774  A    O  
ATOM    877  CB  ALA A 561      -1.363 -19.725  -9.802  1.00 44.40      A    C  
ANISOU  877  CB  ALA A 561     9388   3425   4057   -522     81    968  A    C  
ATOM    878  N   ARG A 562      -2.248 -16.845  -8.794  1.00 43.79      A    N  
ANISOU  878  N   ARG A 562     9013   3804   3819   -674    232    911  A    N  
ATOM    879  CA  ARG A 562      -3.084 -15.970  -7.977  1.00 42.16      A    C  
ANISOU  879  CA  ARG A 562     8918   3651   3449   -821    477    909  A    C  
ATOM    880  C   ARG A 562      -3.887 -14.976  -8.818  1.00 40.93      A    C  
ANISOU  880  C   ARG A 562     8183   3818   3551   -965    646    758  A    C  
ATOM    881  O   ARG A 562      -5.077 -14.771  -8.580  1.00 41.61      A    O  
ANISOU  881  O   ARG A 562     8245   3926   3640  -1184   1014    692  A    O  
ATOM    882  CB  ARG A 562      -2.228 -15.225  -6.952  1.00 43.01      A    C  
ANISOU  882  CB  ARG A 562     9304   3737   3302   -607    168    977  A    C  
ATOM    883  CG  ARG A 562      -1.745 -16.089  -5.802  1.00 48.30      A    C  
ANISOU  883  CG  ARG A 562    10551   4107   3694   -456     41   1057  A    C  
ATOM    884  CD  ARG A 562      -0.717 -15.363  -4.954  1.00 49.72      A    C  
ANISOU  884  CD  ARG A 562    10849   4319   3724   -197   -367   1041  A    C  
ATOM    885  NE  ARG A 562      -0.515 -16.029  -3.671  1.00 57.16      A    N  
ANISOU  885  NE  ARG A 562    12314   5002   4401    -83   -420   1055  A    N  
ATOM    886  CZ  ARG A 562       0.413 -15.686  -2.783  1.00 59.30      A    C  
ANISOU  886  CZ  ARG A 562    12778   5230   4525    157   -790   1021  A    C  
ATOM    887  NH1 ARG A 562       1.246 -14.686  -3.038  1.00 57.59      A    N1+
ANISOU  887  NH1 ARG A 562    12231   5219   4431    297  -1133    955  A    N1+
ATOM    888  NH2 ARG A 562       0.519 -16.354  -1.642  1.00 62.33      A    N  
ANISOU  888  NH2 ARG A 562    13690   5349   4642    254   -817   1033  A    N  
ATOM    889  N   GLY A 563      -3.231 -14.362  -9.798  1.00 36.98      A    N  
ANISOU  889  N   GLY A 563     7231   3553   3267   -833    383    690  A    N  
ATOM    890  CA  GLY A 563      -3.890 -13.423 -10.688  1.00 37.71      A    C  
ANISOU  890  CA  GLY A 563     6831   3923   3573   -917    483    559  A    C  
ATOM    891  C   GLY A 563      -4.950 -14.073 -11.559  1.00 40.73      A    C  
ANISOU  891  C   GLY A 563     6976   4341   4157  -1104    745    448  A    C  
ATOM    892  O   GLY A 563      -6.041 -13.533 -11.738  1.00 39.19      A    O  
ANISOU  892  O   GLY A 563     6550   4280   4060  -1239    964    330  A    O  
ATOM    893  N   MET A 564      -4.629 -15.243 -12.099  1.00 44.37      A    N  
ANISOU  893  N   MET A 564     7484   4678   4696  -1101    705    461  A    N  
ATOM    894  CA  MET A 564      -5.548 -15.954 -12.983  1.00 41.22      A    C  
ANISOU  894  CA  MET A 564     6860   4299   4502  -1279    915    330  A    C  
ATOM    895  C   MET A 564      -6.757 -16.502 -12.232  1.00 41.53      A    C  
ANISOU  895  C   MET A 564     7109   4174   4498  -1543   1320    287  A    C  
ATOM    896  O   MET A 564      -7.876 -16.490 -12.743  1.00 40.77      A    O  
ANISOU  896  O   MET A 564     6705   4186   4599  -1726   1544    107  A    O  
ATOM    897  CB  MET A 564      -4.821 -17.080 -13.713  1.00 38.06      A    C  
ANISOU  897  CB  MET A 564     6493   3781   4187  -1202    769    347  A    C  
ATOM    898  CG  MET A 564      -3.763 -16.588 -14.679  1.00 32.48      A    C  
ANISOU  898  CG  MET A 564     5499   3257   3586   -989    455    331  A    C  
ATOM    899  SD  MET A 564      -4.444 -15.472 -15.924  1.00 44.15      A    S  
ANISOU  899  SD  MET A 564     6460   5071   5242  -1022    466    169  A    S  
ATOM    900  CE  MET A 564      -5.618 -16.541 -16.755  1.00 39.69      A    C  
ANISOU  900  CE  MET A 564     5749   4476   4855  -1226    679      0  A    C  
ATOM    901  N   ASP A 565      -6.530 -16.978 -11.016  1.00 45.05      A    N  
ANISOU  901  N   ASP A 565     8087   4347   4684  -1562   1418    435  A    N  
ATOM    902  CA  ASP A 565      -7.625 -17.454 -10.186  1.00 49.07      A    C  
ANISOU  902  CA  ASP A 565     8871   4661   5113  -1839   1870    404  A    C  
ATOM    903  C   ASP A 565      -8.566 -16.298  -9.873  1.00 48.05      A    C  
ANISOU  903  C   ASP A 565     8487   4740   5031  -1943   2079    277  A    C  
ATOM    904  O   ASP A 565      -9.785 -16.450  -9.897  1.00 51.30      A    O  
ANISOU  904  O   ASP A 565     8708   5175   5609  -2181   2436     94  A    O  
ATOM    905  CB  ASP A 565      -7.094 -18.068  -8.895  1.00 53.88      A    C  
ANISOU  905  CB  ASP A 565    10156   4943   5374  -1766   1876    592  A    C  
ATOM    906  CG  ASP A 565      -8.191 -18.684  -8.052  1.00 60.50      A    C  
ANISOU  906  CG  ASP A 565    11188   5631   6169  -1960   2278    483  A    C  
ATOM    907  OD1 ASP A 565      -9.115 -19.298  -8.631  1.00 58.57      A    O  
ANISOU  907  OD1 ASP A 565    10693   5394   6168  -2179   2545    314  A    O  
ATOM    908  OD2 ASP A 565      -8.134 -18.543  -6.812  1.00 65.18      A    O1-
ANISOU  908  OD2 ASP A 565    12182   6093   6489  -1896   2323    543  A    O1-
ATOM    909  N   TYR A 566      -7.985 -15.140  -9.588  1.00 46.85      A    N  
ANISOU  909  N   TYR A 566     8295   4743   4762  -1740   1830    339  A    N  
ATOM    910  CA  TYR A 566      -8.760 -13.932  -9.350  1.00 47.11      A    C  
ANISOU  910  CA  TYR A 566     8080   4977   4842  -1783   1973    218  A    C  
ATOM    911  C   TYR A 566      -9.584 -13.549 -10.578  1.00 44.44      A    C  
ANISOU  911  C   TYR A 566     7119   4908   4857  -1830   1989     -9  A    C  
ATOM    912  O   TYR A 566     -10.787 -13.311 -10.473  1.00 43.80      A    O  
ANISOU  912  O   TYR A 566     6818   4899   4924  -2000   2297   -198  A    O  
ATOM    913  CB  TYR A 566      -7.838 -12.777  -8.950  1.00 44.30      A    C  
ANISOU  913  CB  TYR A 566     7796   4724   4313  -1542   1651    322  A    C  
ATOM    914  CG  TYR A 566      -8.544 -11.443  -8.828  1.00 44.60      A    C  
ANISOU  914  CG  TYR A 566     7565   4969   4413  -1544   1749    195  A    C  
ATOM    915  CD1 TYR A 566      -9.215 -11.093  -7.660  1.00 48.09      A    C  
ANISOU  915  CD1 TYR A 566     8268   5322   4680  -1660   2064    171  A    C  
ATOM    916  CD2 TYR A 566      -8.536 -10.530  -9.877  1.00 40.62      A    C  
ANISOU  916  CD2 TYR A 566     6586   4725   4124  -1420   1538     98  A    C  
ATOM    917  CE1 TYR A 566      -9.860  -9.873  -7.543  1.00 47.32      A    C  
ANISOU  917  CE1 TYR A 566     7921   5403   4654  -1640   2153     37  A    C  
ATOM    918  CE2 TYR A 566      -9.178  -9.310  -9.769  1.00 41.36      A    C  
ANISOU  918  CE2 TYR A 566     6466   4977   4271  -1389   1607    -19  A    C  
ATOM    919  CZ  TYR A 566      -9.837  -8.987  -8.601  1.00 46.04      A    C  
ANISOU  919  CZ  TYR A 566     7282   5491   4721  -1494   1908    -56  A    C  
ATOM    920  OH  TYR A 566     -10.476  -7.775  -8.493  1.00 47.20      A    O  
ANISOU  920  OH  TYR A 566     7210   5786   4935  -1443   1976   -189  A    O  
ATOM    921  N   LEU A 567      -8.932 -13.487 -11.737  1.00 43.00      A    N  
ANISOU  921  N   LEU A 567     6663   4867   4807  -1667   1654     -7  A    N  
ATOM    922  CA  LEU A 567      -9.621 -13.167 -12.987  1.00 43.52      A    C  
ANISOU  922  CA  LEU A 567     6210   5169   5158  -1666   1602   -211  A    C  
ATOM    923  C   LEU A 567     -10.801 -14.097 -13.246  1.00 45.31      A    C  
ANISOU  923  C   LEU A 567     6269   5344   5600  -1921   1909   -415  A    C  
ATOM    924  O   LEU A 567     -11.862 -13.658 -13.688  1.00 46.50      A    O  
ANISOU  924  O   LEU A 567     6022   5670   5974  -1980   2002   -651  A    O  
ATOM    925  CB  LEU A 567      -8.661 -13.236 -14.176  1.00 41.39      A    C  
ANISOU  925  CB  LEU A 567     5791   4991   4946  -1481   1249   -162  A    C  
ATOM    926  CG  LEU A 567      -7.624 -12.129 -14.326  1.00 40.40      A    C  
ANISOU  926  CG  LEU A 567     5654   4980   4718  -1250    950    -47  A    C  
ATOM    927  CD1 LEU A 567      -6.768 -12.377 -15.557  1.00 39.00      A    C  
ANISOU  927  CD1 LEU A 567     5333   4866   4619  -1121    699    -32  A    C  
ATOM    928  CD2 LEU A 567      -8.311 -10.780 -14.413  1.00 40.87      A    C  
ANISOU  928  CD2 LEU A 567     5475   5229   4826  -1195    959   -151  A    C  
ATOM    929  N   HIS A 568     -10.611 -15.382 -12.966  1.00 44.98      A    N  
ANISOU  929  N   HIS A 568     6533   5051   5506  -2065   2054   -343  A    N  
ATOM    930  CA  HIS A 568     -11.646 -16.373 -13.243  1.00 48.07      A    C  
ANISOU  930  CA  HIS A 568     6786   5356   6122  -2343   2360   -547  A    C  
ATOM    931  C   HIS A 568     -12.772 -16.345 -12.218  1.00 52.28      A    C  
ANISOU  931  C   HIS A 568     7379   5814   6673  -2540   2769   -675  A    C  
ATOM    932  O   HIS A 568     -13.912 -16.681 -12.534  1.00 55.50      A    O  
ANISOU  932  O   HIS A 568     7468   6279   7340  -2668   2933   -946  A    O  
ATOM    933  CB  HIS A 568     -11.038 -17.773 -13.368  1.00 47.51      A    C  
ANISOU  933  CB  HIS A 568     7044   5014   5993  -2405   2359   -432  A    C  
ATOM    934  CG  HIS A 568     -10.203 -17.951 -14.595  1.00 48.27      A    C  
ANISOU  934  CG  HIS A 568     6959   5220   6161  -2196   1969   -410  A    C  
ATOM    935  CD2 HIS A 568      -9.813 -17.057 -15.539  1.00 45.47      A    C  
ANISOU  935  CD2 HIS A 568     6273   5140   5865  -1968   1636   -441  A    C  
ATOM    936  ND1 HIS A 568      -9.678 -19.164 -14.980  1.00 51.76      A    N  
ANISOU  936  ND1 HIS A 568     7597   5459   6610  -2214   1922   -357  A    N  
ATOM    937  CE1 HIS A 568      -8.996 -19.013 -16.102  1.00 50.60      A    C  
ANISOU  937  CE1 HIS A 568     7223   5474   6530  -2009   1588   -369  A    C  
ATOM    938  NE2 HIS A 568      -9.062 -17.742 -16.460  1.00 47.42      A    N  
ANISOU  938  NE2 HIS A 568     6515   5354   6148  -1867   1422   -413  A    N  
ATOM    939  N   ALA A 569     -12.455 -15.939 -10.995  1.00 53.76      A    N  
ANISOU  939  N   ALA A 569     7969   5881   6575  -2489   2856   -506  A    N  
ATOM    940  CA  ALA A 569     -13.480 -15.774  -9.972  1.00 56.56      A    C  
ANISOU  940  CA  ALA A 569     8392   6177   6923  -2600   3185   -640  A    C  
ATOM    941  C   ALA A 569     -14.386 -14.617 -10.372  1.00 56.95      A    C  
ANISOU  941  C   ALA A 569     7899   6520   7222  -2577   3202   -883  A    C  
ATOM    942  O   ALA A 569     -15.586 -14.625 -10.100  1.00 57.12      A    O  
ANISOU  942  O   ALA A 569     7713   6557   7434  -2701   3460  -1132  A    O  
ATOM    943  CB  ALA A 569     -12.845 -15.518  -8.621  1.00 55.76      A    C  
ANISOU  943  CB  ALA A 569     8858   5890   6438  -2515   3211   -413  A    C  
ATOM    944  N   LYS A 570     -13.794 -13.627 -11.033  1.00 55.95      A    N  
ANISOU  944  N   LYS A 570     7549   6614   7095  -2408   2921   -823  A    N  
ATOM    945  CA  LYS A 570     -14.536 -12.509 -11.600  1.00 59.50      A    C  
ANISOU  945  CA  LYS A 570     7474   7353   7780  -2323   2858  -1053  A    C  
ATOM    946  C   LYS A 570     -15.148 -12.896 -12.943  1.00 62.63      A    C  
ANISOU  946  C   LYS A 570     7367   7910   8520  -2332   2713  -1304  A    C  
ATOM    947  O   LYS A 570     -15.759 -12.064 -13.617  1.00 61.40      A    O  
ANISOU  947  O   LYS A 570     6756   7997   8575  -2207   2568  -1519  A    O  
ATOM    948  CB  LYS A 570     -13.611 -11.308 -11.788  1.00 57.48      A    C  
ANISOU  948  CB  LYS A 570     7249   7240   7351  -2026   2486   -882  A    C  
ATOM    949  CG  LYS A 570     -13.176 -10.644 -10.491  1.00 59.23      A    C  
ANISOU  949  CG  LYS A 570     7882   7356   7266  -1985   2585   -709  A    C  
ATOM    950  CD  LYS A 570     -14.330  -9.894  -9.860  1.00 61.69      A    C  
ANISOU  950  CD  LYS A 570     8010   7745   7684  -2068   2911   -929  A    C  
ATOM    951  CE  LYS A 570     -13.831  -8.786  -8.955  1.00 62.85      A    C  
ANISOU  951  CE  LYS A 570     8443   7880   7556  -1917   2851   -791  A    C  
ATOM    952  NZ  LYS A 570     -14.869  -7.735  -8.747  1.00 65.06      A    N1+
ANISOU  952  NZ  LYS A 570     8406   8312   8002  -1884   3026  -1036  A    N1+
ATOM    953  N   SER A 571     -14.979 -14.164 -13.315  1.00 65.20      A    N  
ANISOU  953  N   SER A 571     7807   8085   8882  -2449   2725  -1283  A    N  
ATOM    954  CA  SER A 571     -15.449 -14.697 -14.593  1.00 66.39      A    C  
ANISOU  954  CA  SER A 571     7561   8352   9314  -2455   2559  -1509  A    C  
ATOM    955  C   SER A 571     -14.900 -13.895 -15.772  1.00 62.52      A    C  
ANISOU  955  C   SER A 571     6799   8104   8850  -2208   2134  -1501  A    C  
ATOM    956  O   SER A 571     -15.627 -13.548 -16.702  1.00 63.01      A    O  
ANISOU  956  O   SER A 571     6417   8375   9149  -2121   1960  -1765  A    O  
ATOM    957  CB  SER A 571     -16.976 -14.773 -14.642  1.00 70.66      A    C  
ANISOU  957  CB  SER A 571     7735   8964  10149  -2534   2719  -1869  A    C  
ATOM    958  OG  SER A 571     -17.552 -13.484 -14.615  1.00 73.23      A    O  
ANISOU  958  OG  SER A 571     7750   9502  10573  -2383   2645  -2015  A    O  
ATOM    959  N   ILE A 572     -13.607 -13.598 -15.707  1.00 56.39      A    N  
ANISOU  959  N   ILE A 572     6357   7279   7789  -2011   1896  -1188  A    N  
ATOM    960  CA  ILE A 572     -12.907 -12.945 -16.798  1.00 49.84      A    C  
ANISOU  960  CA  ILE A 572     5417   6614   6907  -1725   1473  -1120  A    C  
ATOM    961  C   ILE A 572     -11.932 -13.926 -17.428  1.00 48.31      A    C  
ANISOU  961  C   ILE A 572     5410   6307   6640  -1708   1322   -982  A    C  
ATOM    962  O   ILE A 572     -11.158 -14.581 -16.734  1.00 47.71      A    O  
ANISOU  962  O   ILE A 572     5701   6022   6405  -1769   1410   -779  A    O  
ATOM    963  CB  ILE A 572     -12.124 -11.712 -16.312  1.00 47.23      A    C  
ANISOU  963  CB  ILE A 572     5268   6326   6350  -1516   1326   -909  A    C  
ATOM    964  CG1 ILE A 572     -13.080 -10.656 -15.752  1.00 47.15      A    C  
ANISOU  964  CG1 ILE A 572     5072   6430   6413  -1496   1456  -1057  A    C  
ATOM    965  CG2 ILE A 572     -11.289 -11.126 -17.446  1.00 42.39      A    C  
ANISOU  965  CG2 ILE A 572     4604   5833   5670  -1264    952   -824  A    C  
ATOM    966  CD1 ILE A 572     -12.383  -9.415 -15.232  1.00 42.16      A    C  
ANISOU  966  CD1 ILE A 572     4630   5821   5568  -1309   1330   -875  A    C  
ATOM    967  N   ILE A 573     -11.983 -14.028 -18.750  1.00 48.31      A    N  
ANISOU  967  N   ILE A 573     5175   6434   6746  -1604   1082  -1108  A    N  
ATOM    968  CA  ILE A 573     -11.053 -14.862 -19.493  1.00 44.51      A    C  
ANISOU  968  CA  ILE A 573     4840   5868   6204  -1559    930  -1008  A    C  
ATOM    969  C   ILE A 573     -10.018 -13.966 -20.154  1.00 42.16      A    C  
ANISOU  969  C   ILE A 573     4595   5680   5746  -1291    637   -855  A    C  
ATOM    970  O   ILE A 573     -10.368 -12.983 -20.800  1.00 44.25      A    O  
ANISOU  970  O   ILE A 573     4671   6122   6021  -1139    472   -941  A    O  
ATOM    971  CB  ILE A 573     -11.785 -15.673 -20.569  1.00 46.75      A    C  
ANISOU  971  CB  ILE A 573     4868   6199   6697  -1645    885  -1273  A    C  
ATOM    972  CG1 ILE A 573     -12.941 -16.452 -19.941  1.00 49.89      A    C  
ANISOU  972  CG1 ILE A 573     5148   6497   7310  -1952   1218  -1483  A    C  
ATOM    973  CG2 ILE A 573     -10.822 -16.609 -21.283  1.00 47.40      A    C  
ANISOU  973  CG2 ILE A 573     5130   6168   6711  -1607    767  -1179  A    C  
ATOM    974  CD1 ILE A 573     -13.892 -17.053 -20.956  1.00 52.39      A    C  
ANISOU  974  CD1 ILE A 573     5111   6900   7895  -2049   1159  -1829  A    C  
ATOM    975  N   HIS A 574      -8.745 -14.304 -19.984  1.00 40.33      A    N  
ANISOU  975  N   HIS A 574     4627   5324   5374  -1232    580   -642  A    N  
ATOM    976  CA  HIS A 574      -7.660 -13.475 -20.490  1.00 38.77      A    C  
ANISOU  976  CA  HIS A 574     4479   5201   5049  -1023    369   -508  A    C  
ATOM    977  C   HIS A 574      -7.555 -13.545 -22.011  1.00 42.99      A    C  
ANISOU  977  C   HIS A 574     4885   5840   5611   -919    198   -611  A    C  
ATOM    978  O   HIS A 574      -7.381 -12.517 -22.673  1.00 44.11      A    O  
ANISOU  978  O   HIS A 574     4980   6104   5677   -764     58   -603  A    O  
ATOM    979  CB  HIS A 574      -6.337 -13.903 -19.861  1.00 35.98      A    C  
ANISOU  979  CB  HIS A 574     4391   4689   4591   -990    351   -307  A    C  
ATOM    980  CG  HIS A 574      -5.196 -12.985 -20.170  1.00 36.80      A    C  
ANISOU  980  CG  HIS A 574     4516   4860   4606   -819    187   -197  A    C  
ATOM    981  CD2 HIS A 574      -4.441 -12.201 -19.366  1.00 36.99      A    C  
ANISOU  981  CD2 HIS A 574     4652   4866   4537   -752    139    -68  A    C  
ATOM    982  ND1 HIS A 574      -4.707 -12.804 -21.447  1.00 37.65      A    N  
ANISOU  982  ND1 HIS A 574     4532   5052   4722   -717     73   -238  A    N  
ATOM    983  CE1 HIS A 574      -3.705 -11.945 -21.417  1.00 35.46      A    C  
ANISOU  983  CE1 HIS A 574     4296   4798   4378   -617     -1   -139  A    C  
ATOM    984  NE2 HIS A 574      -3.523 -11.563 -20.166  1.00 37.05      A    N  
ANISOU  984  NE2 HIS A 574     4600   4944   4532   -635     19    -45  A    N  
ATOM    985  N   ARG A 575      -7.627 -14.767 -22.536  1.00 40.42      A    N  
ANISOU  985  N   ARG A 575     4554   5435   5369  -1004    223   -703  A    N  
ATOM    986  CA  ARG A 575      -7.601 -15.060 -23.974  1.00 40.59      A    C  
ANISOU  986  CA  ARG A 575     4492   5529   5402   -926     79   -831  A    C  
ATOM    987  C   ARG A 575      -6.241 -14.927 -24.652  1.00 38.69      A    C  
ANISOU  987  C   ARG A 575     4389   5272   5038   -781    -15   -705  A    C  
ATOM    988  O   ARG A 575      -6.093 -15.304 -25.812  1.00 42.46      A    O  
ANISOU  988  O   ARG A 575     4861   5775   5495   -726    -94   -800  A    O  
ATOM    989  CB  ARG A 575      -8.651 -14.249 -24.740  1.00 40.97      A    C  
ANISOU  989  CB  ARG A 575     4331   5765   5471   -839    -61  -1015  A    C  
ATOM    990  CG  ARG A 575     -10.074 -14.549 -24.338  1.00 44.67      A    C  
ANISOU  990  CG  ARG A 575     4566   6271   6137   -988     26  -1238  A    C  
ATOM    991  CD  ARG A 575     -11.054 -13.789 -25.206  1.00 47.26      A    C  
ANISOU  991  CD  ARG A 575     4663   6789   6505   -842   -188  -1459  A    C  
ATOM    992  NE  ARG A 575     -12.433 -14.095 -24.840  1.00 54.60      A    N  
ANISOU  992  NE  ARG A 575     5288   7769   7688   -991   -102  -1734  A    N  
ATOM    993  CZ  ARG A 575     -13.134 -13.413 -23.941  1.00 55.93      A    C  
ANISOU  993  CZ  ARG A 575     5311   7988   7950  -1023     16  -1780  A    C  
ATOM    994  NH1 ARG A 575     -12.586 -12.378 -23.316  1.00 52.86      A    N1+
ANISOU  994  NH1 ARG A 575     5083   7602   7400   -908     35  -1556  A    N1+
ATOM    995  NH2 ARG A 575     -14.384 -13.763 -23.667  1.00 57.98      A    N  
ANISOU  995  NH2 ARG A 575     5254   8294   8483  -1180    132  -2075  A    N  
ATOM    996  N   ASP A 576      -5.249 -14.405 -23.943  1.00 34.31      A    N  
ANISOU  996  N   ASP A 576     3953   4671   4412   -726      5   -518  A    N  
ATOM    997  CA  ASP A 576      -3.940 -14.216 -24.552  1.00 35.74      A    C  
ANISOU  997  CA  ASP A 576     4210   4843   4528   -611    -47   -439  A    C  
ATOM    998  C   ASP A 576      -2.799 -14.233 -23.538  1.00 33.26      A    C  
ANISOU  998  C   ASP A 576     3996   4421   4219   -591    -28   -287  A    C  
ATOM    999  O   ASP A 576      -1.829 -13.496 -23.681  1.00 32.62      A    O  
ANISOU  999  O   ASP A 576     3919   4372   4105   -508    -60   -225  A    O  
ATOM   1000  CB  ASP A 576      -3.913 -12.911 -25.354  1.00 42.23      A    C  
ANISOU 1000  CB  ASP A 576     5016   5798   5234   -497   -117   -439  A    C  
ATOM   1001  CG  ASP A 576      -2.778 -12.868 -26.353  1.00 48.27      A    C  
ANISOU 1001  CG  ASP A 576     5855   6549   5936   -419   -108   -423  A    C  
ATOM   1002  OD1 ASP A 576      -2.446 -13.925 -26.929  1.00 48.37      A    O  
ANISOU 1002  OD1 ASP A 576     5882   6503   5994   -430    -87   -494  A    O  
ATOM   1003  OD2 ASP A 576      -2.210 -11.777 -26.552  1.00 54.44      A    O1-
ANISOU 1003  OD2 ASP A 576     6690   7364   6631   -359    -94   -352  A    O1-
ATOM   1004  N   LEU A 577      -2.910 -15.080 -22.521  1.00 33.40      A    N  
ANISOU 1004  N   LEU A 577     4113   4298   4280   -666     21   -244  A    N  
ATOM   1005  CA  LEU A 577      -1.856 -15.203 -21.524  1.00 32.43      A    C  
ANISOU 1005  CA  LEU A 577     4123   4056   4143   -607    -23   -118  A    C  
ATOM   1006  C   LEU A 577      -0.604 -15.818 -22.128  1.00 37.52      A    C  
ANISOU 1006  C   LEU A 577     4759   4638   4859   -498    -89   -137  A    C  
ATOM   1007  O   LEU A 577      -0.664 -16.852 -22.794  1.00 42.45      A    O  
ANISOU 1007  O   LEU A 577     5395   5193   5542   -510    -60   -216  A    O  
ATOM   1008  CB  LEU A 577      -2.325 -16.058 -20.349  1.00 33.10      A    C  
ANISOU 1008  CB  LEU A 577     4406   3961   4207   -698     49    -62  A    C  
ATOM   1009  CG  LEU A 577      -1.306 -16.266 -19.228  1.00 34.02      A    C  
ANISOU 1009  CG  LEU A 577     4734   3925   4266   -599    -50     66  A    C  
ATOM   1010  CD1 LEU A 577      -1.000 -14.944 -18.539  1.00 33.59      A    C  
ANISOU 1010  CD1 LEU A 577     4660   3972   4132   -548   -122    133  A    C  
ATOM   1011  CD2 LEU A 577      -1.816 -17.294 -18.221  1.00 35.38      A    C  
ANISOU 1011  CD2 LEU A 577     5205   3866   4372   -689     49    127  A    C  
ATOM   1012  N   LYS A 578       0.530 -15.172 -21.893  1.00 39.15      A    N  
ANISOU 1012  N   LYS A 578     4925   4869   5082   -397   -169    -93  A    N  
ATOM   1013  CA  LYS A 578       1.823 -15.701 -22.304  1.00 41.20      A    C  
ANISOU 1013  CA  LYS A 578     5129   5070   5456   -282   -225   -144  A    C  
ATOM   1014  C   LYS A 578       2.925 -15.016 -21.513  1.00 40.16      A    C  
ANISOU 1014  C   LYS A 578     4950   4940   5371   -191   -344   -109  A    C  
ATOM   1015  O   LYS A 578       2.667 -14.061 -20.785  1.00 42.16      A    O  
ANISOU 1015  O   LYS A 578     5231   5246   5543   -227   -372    -41  A    O  
ATOM   1016  CB  LYS A 578       2.039 -15.532 -23.808  1.00 43.73      A    C  
ANISOU 1016  CB  LYS A 578     5319   5492   5805   -280   -131   -251  A    C  
ATOM   1017  CG  LYS A 578       1.583 -14.204 -24.350  1.00 47.72      A    C  
ANISOU 1017  CG  LYS A 578     5775   6150   6205   -330    -70   -242  A    C  
ATOM   1018  CD  LYS A 578       1.592 -14.200 -25.864  1.00 51.16      A    C  
ANISOU 1018  CD  LYS A 578     6193   6647   6597   -324     26   -340  A    C  
ATOM   1019  CE  LYS A 578       0.796 -13.026 -26.398  1.00 53.62      A    C  
ANISOU 1019  CE  LYS A 578     6547   7075   6752   -348     48   -322  A    C  
ATOM   1020  NZ  LYS A 578       1.511 -12.344 -27.508  1.00 57.15      A    N1+
ANISOU 1020  NZ  LYS A 578     7030   7553   7131   -324    165   -357  A    N1+
ATOM   1021  N   SER A 579       4.150 -15.506 -21.656  1.00 39.64      A    N  
ANISOU 1021  N   SER A 579     4792   4815   5453    -68   -424   -185  A    N  
ATOM   1022  CA  SER A 579       5.258 -15.038 -20.830  1.00 41.98      A    C  
ANISOU 1022  CA  SER A 579     5010   5098   5841     39   -590   -204  A    C  
ATOM   1023  C   SER A 579       5.604 -13.558 -21.022  1.00 42.98      A    C  
ANISOU 1023  C   SER A 579     4967   5373   5990    -33   -529   -233  A    C  
ATOM   1024  O   SER A 579       6.180 -12.936 -20.132  1.00 42.87      A    O  
ANISOU 1024  O   SER A 579     4917   5360   6010      7   -671   -237  A    O  
ATOM   1025  CB  SER A 579       6.492 -15.915 -21.050  1.00 41.97      A    C  
ANISOU 1025  CB  SER A 579     4886   5011   6048    207   -695   -333  A    C  
ATOM   1026  OG  SER A 579       6.714 -16.140 -22.428  1.00 44.46      A    O  
ANISOU 1026  OG  SER A 579     5048   5385   6461    173   -506   -448  A    O  
ATOM   1027  N   ASN A 580       5.262 -12.995 -22.176  1.00 45.54      A    N  
ANISOU 1027  N   ASN A 580     5223   5799   6280   -135   -328   -260  A    N  
ATOM   1028  CA  ASN A 580       5.515 -11.577 -22.410  1.00 51.58      A    C  
ANISOU 1028  CA  ASN A 580     5901   6660   7038   -217   -235   -272  A    C  
ATOM   1029  C   ASN A 580       4.338 -10.701 -21.991  1.00 50.48      A    C  
ANISOU 1029  C   ASN A 580     5909   6568   6702   -292   -224   -151  A    C  
ATOM   1030  O   ASN A 580       4.416  -9.476 -22.034  1.00 50.44      A    O  
ANISOU 1030  O   ASN A 580     5888   6612   6663   -350   -164   -140  A    O  
ATOM   1031  CB  ASN A 580       5.923 -11.311 -23.861  1.00 55.88      A    C  
ANISOU 1031  CB  ASN A 580     6357   7253   7623   -270    -10   -365  A    C  
ATOM   1032  CG  ASN A 580       5.076 -12.069 -24.849  1.00 60.30      A    C  
ANISOU 1032  CG  ASN A 580     7033   7815   8062   -273     76   -359  A    C  
ATOM   1033  ND2 ASN A 580       5.604 -13.179 -25.354  1.00 61.72      A    N  
ANISOU 1033  ND2 ASN A 580     7153   7941   8356   -210    100   -457  A    N  
ATOM   1034  OD1 ASN A 580       3.957 -11.665 -25.158  1.00 62.68      A    O  
ANISOU 1034  OD1 ASN A 580     7468   8165   8183   -318    103   -289  A    O  
ATOM   1035  N   ASN A 581       3.251 -11.348 -21.583  1.00 50.39      A    N  
ANISOU 1035  N   ASN A 581     6039   6527   6580   -295   -263    -78  A    N  
ATOM   1036  CA  ASN A 581       2.105 -10.663 -21.001  1.00 48.75      A    C  
ANISOU 1036  CA  ASN A 581     5940   6357   6225   -352   -253      5  A    C  
ATOM   1037  C   ASN A 581       2.266 -10.567 -19.490  1.00 45.02      A    C  
ANISOU 1037  C   ASN A 581     5570   5816   5718   -328   -381     67  A    C  
ATOM   1038  O   ASN A 581       1.485  -9.905 -18.808  1.00 43.50      A    O  
ANISOU 1038  O   ASN A 581     5472   5646   5411   -372   -364    124  A    O  
ATOM   1039  CB  ASN A 581       0.815 -11.420 -21.326  1.00 53.06      A    C  
ANISOU 1039  CB  ASN A 581     6553   6906   6704   -395   -193      6  A    C  
ATOM   1040  CG  ASN A 581       0.327 -11.165 -22.731  1.00 62.15      A    C  
ANISOU 1040  CG  ASN A 581     7650   8147   7819   -406   -110    -58  A    C  
ATOM   1041  ND2 ASN A 581      -0.925 -11.514 -22.993  1.00 64.42      A    N  
ANISOU 1041  ND2 ASN A 581     7951   8467   8060   -443    -90    -95  A    N  
ATOM   1042  OD1 ASN A 581       1.063 -10.654 -23.573  1.00 68.99      A    O  
ANISOU 1042  OD1 ASN A 581     8475   9044   8695   -383    -60    -90  A    O  
ATOM   1043  N   ILE A 582       3.285 -11.248 -18.978  1.00 42.03      A    N  
ANISOU 1043  N   ILE A 582     5190   5349   5432   -238   -522     42  A    N  
ATOM   1044  CA  ILE A 582       3.539 -11.315 -17.546  1.00 41.83      A    C  
ANISOU 1044  CA  ILE A 582     5325   5230   5338   -174   -696     93  A    C  
ATOM   1045  C   ILE A 582       4.723 -10.433 -17.185  1.00 41.21      A    C  
ANISOU 1045  C   ILE A 582     5107   5187   5366   -123   -840     14  A    C  
ATOM   1046  O   ILE A 582       5.876 -10.780 -17.431  1.00 44.20      A    O  
ANISOU 1046  O   ILE A 582     5314   5548   5930    -33   -947    -97  A    O  
ATOM   1047  CB  ILE A 582       3.808 -12.766 -17.092  1.00 42.74      A    C  
ANISOU 1047  CB  ILE A 582     5601   5182   5457    -67   -815    113  A    C  
ATOM   1048  CG1 ILE A 582       2.613 -13.660 -17.436  1.00 42.21      A    C  
ANISOU 1048  CG1 ILE A 582     5669   5059   5311   -162   -640    166  A    C  
ATOM   1049  CG2 ILE A 582       4.112 -12.814 -15.603  1.00 43.33      A    C  
ANISOU 1049  CG2 ILE A 582     5923   5135   5406     31  -1025    172  A    C  
ATOM   1050  CD1 ILE A 582       2.845 -15.128 -17.168  1.00 43.94      A    C  
ANISOU 1050  CD1 ILE A 582     6079   5079   5536    -75   -713    185  A    C  
ATOM   1051  N   PHE A 583       4.424  -9.282 -16.602  1.00 40.89      A    N  
ANISOU 1051  N   PHE A 583     5116   5190   5229   -183   -836     45  A    N  
ATOM   1052  CA  PHE A 583       5.444  -8.296 -16.287  1.00 41.99      A    C  
ANISOU 1052  CA  PHE A 583     5113   5362   5479   -177   -948    -53  A    C  
ATOM   1053  C   PHE A 583       5.969  -8.488 -14.869  1.00 44.93      A    C  
ANISOU 1053  C   PHE A 583     5632   5646   5794    -56  -1237    -66  A    C  
ATOM   1054  O   PHE A 583       5.200  -8.519 -13.908  1.00 45.22      A    O  
ANISOU 1054  O   PHE A 583     5956   5622   5602    -50  -1268     42  A    O  
ATOM   1055  CB  PHE A 583       4.868  -6.890 -16.461  1.00 40.94      A    C  
ANISOU 1055  CB  PHE A 583     4986   5300   5269   -300   -795    -26  A    C  
ATOM   1056  CG  PHE A 583       4.203  -6.675 -17.793  1.00 41.84      A    C  
ANISOU 1056  CG  PHE A 583     5047   5479   5373   -377   -555      1  A    C  
ATOM   1057  CD1 PHE A 583       4.872  -6.969 -18.973  1.00 43.04      A    C  
ANISOU 1057  CD1 PHE A 583     5029   5652   5671   -391   -453    -77  A    C  
ATOM   1058  CD2 PHE A 583       2.904  -6.204 -17.867  1.00 42.18      A    C  
ANISOU 1058  CD2 PHE A 583     5218   5557   5253   -418   -442     85  A    C  
ATOM   1059  CE1 PHE A 583       4.262  -6.783 -20.205  1.00 39.77      A    C  
ANISOU 1059  CE1 PHE A 583     4633   5281   5195   -440   -259    -52  A    C  
ATOM   1060  CE2 PHE A 583       2.287  -6.017 -19.098  1.00 43.40      A    C  
ANISOU 1060  CE2 PHE A 583     5345   5764   5379   -445   -287     92  A    C  
ATOM   1061  CZ  PHE A 583       2.969  -6.310 -20.269  1.00 39.23      A    C  
ANISOU 1061  CZ  PHE A 583     4708   5246   4952   -454   -204     33  A    C  
ATOM   1062  N   LEU A 584       7.283  -8.639 -14.747  1.00 46.74      A    N  
ANISOU 1062  N   LEU A 584     5669   5861   6228     49  -1451   -218  A    N  
ATOM   1063  CA  LEU A 584       7.918  -8.710 -13.439  1.00 48.53      A    C  
ANISOU 1063  CA  LEU A 584     6023   6010   6407    200  -1798   -271  A    C  
ATOM   1064  C   LEU A 584       8.267  -7.313 -12.966  1.00 46.93      A    C  
ANISOU 1064  C   LEU A 584     5729   5866   6234    116  -1855   -366  A    C  
ATOM   1065  O   LEU A 584       9.380  -6.831 -13.175  1.00 47.51      A    O  
ANISOU 1065  O   LEU A 584     5487   5989   6577    110  -1953   -569  A    O  
ATOM   1066  CB  LEU A 584       9.177  -9.570 -13.481  1.00 54.81      A    C  
ANISOU 1066  CB  LEU A 584     6625   6760   7440    396  -2064   -435  A    C  
ATOM   1067  CG  LEU A 584       9.004 -11.063 -13.751  1.00 59.15      A    C  
ANISOU 1067  CG  LEU A 584     7315   7200   7961    529  -2080   -360  A    C  
ATOM   1068  CD1 LEU A 584      10.293 -11.786 -13.409  1.00 62.43      A    C  
ANISOU 1068  CD1 LEU A 584     7597   7542   8581    793  -2449   -539  A    C  
ATOM   1069  CD2 LEU A 584       7.836 -11.634 -12.960  1.00 60.47      A    C  
ANISOU 1069  CD2 LEU A 584     7972   7233   7772    533  -2048   -134  A    C  
ATOM   1070  N   HIS A 585       7.297  -6.667 -12.333  1.00 46.39      A    N  
ANISOU 1070  N   HIS A 585     5931   5788   5909     38  -1771   -240  A    N  
ATOM   1071  CA  HIS A 585       7.473  -5.318 -11.816  1.00 50.30      A    C  
ANISOU 1071  CA  HIS A 585     6404   6316   6392    -46  -1809   -317  A    C  
ATOM   1072  C   HIS A 585       8.508  -5.280 -10.696  1.00 55.96      A    C  
ANISOU 1072  C   HIS A 585     7141   6980   7141    100  -2217   -471  A    C  
ATOM   1073  O   HIS A 585       8.353  -5.954  -9.676  1.00 57.99      A    O  
ANISOU 1073  O   HIS A 585     7728   7136   7168    260  -2446   -401  A    O  
ATOM   1074  CB  HIS A 585       6.136  -4.784 -11.315  1.00 51.07      A    C  
ANISOU 1074  CB  HIS A 585     6811   6399   6196   -124  -1633   -157  A    C  
ATOM   1075  CG  HIS A 585       6.230  -3.449 -10.655  1.00 54.49      A    C  
ANISOU 1075  CG  HIS A 585     7289   6837   6578   -191  -1681   -229  A    C  
ATOM   1076  CD2 HIS A 585       5.820  -3.027  -9.436  1.00 58.01      A    C  
ANISOU 1076  CD2 HIS A 585     8043   7225   6775   -160  -1782   -200  A    C  
ATOM   1077  ND1 HIS A 585       6.811  -2.357 -11.264  1.00 54.94      A    N  
ANISOU 1077  ND1 HIS A 585     7083   6942   6849   -314  -1600   -356  A    N  
ATOM   1078  CE1 HIS A 585       6.754  -1.320 -10.448  1.00 57.52      A    C  
ANISOU 1078  CE1 HIS A 585     7539   7240   7078   -355  -1667   -406  A    C  
ATOM   1079  NE2 HIS A 585       6.157  -1.700  -9.332  1.00 60.05      A    N  
ANISOU 1079  NE2 HIS A 585     8200   7504   7113   -255  -1785   -317  A    N  
ATOM   1080  N   GLU A 586       9.563  -4.494 -10.900  1.00 59.06      A    N  
ANISOU 1080  N   GLU A 586     7195   7428   7816     43  -2305   -695  A    N  
ATOM   1081  CA  GLU A 586      10.680  -4.418  -9.960  1.00 64.56      A    C  
ANISOU 1081  CA  GLU A 586     7810   8098   8624    187  -2738   -916  A    C  
ATOM   1082  C   GLU A 586      11.276  -5.792  -9.688  1.00 68.62      A    C  
ANISOU 1082  C   GLU A 586     8345   8550   9178    455  -3060   -957  A    C  
ATOM   1083  O   GLU A 586      11.807  -6.041  -8.606  1.00 71.55      A    O  
ANISOU 1083  O   GLU A 586     8880   8846   9460    659  -3433  -1036  A    O  
ATOM   1084  CB  GLU A 586      10.250  -3.761  -8.644  1.00 67.64      A    C  
ANISOU 1084  CB  GLU A 586     8570   8428   8702    214  -2915   -876  A    C  
ATOM   1085  CG  GLU A 586       9.828  -2.307  -8.774  1.00 69.57      A    C  
ANISOU 1085  CG  GLU A 586     8787   8709   8935    -17  -2663   -885  A    C  
ATOM   1086  CD  GLU A 586      11.005  -1.348  -8.806  1.00 75.80      A    C  
ANISOU 1086  CD  GLU A 586     9209   9534  10058   -116  -2796  -1187  A    C  
ATOM   1087  OE1 GLU A 586      12.159  -1.810  -8.936  1.00 79.27      A    O  
ANISOU 1087  OE1 GLU A 586     9315  10001  10802    -25  -3035  -1412  A    O  
ATOM   1088  OE2 GLU A 586      10.776  -0.125  -8.694  1.00 76.93      A    O1-
ANISOU 1088  OE2 GLU A 586     9385   9666  10177   -286  -2654  -1220  A    O1-
ATOM   1089  N   ASP A 587      11.152  -6.681 -10.673  1.00 70.74      A    N  
ANISOU 1089  N   ASP A 587     8496   8828   9554    464  -2862   -886  A    N  
ATOM   1090  CA  ASP A 587      11.728  -8.025 -10.627  1.00 74.23      A    C  
ANISOU 1090  CA  ASP A 587     8931   9195  10077    719  -3120   -931  A    C  
ATOM   1091  C   ASP A 587      11.097  -8.974  -9.610  1.00 74.14      A    C  
ANISOU 1091  C   ASP A 587     9481   9014   9673    919  -3324   -725  A    C  
ATOM   1092  O   ASP A 587      11.498 -10.132  -9.521  1.00 77.91      A    O  
ANISOU 1092  O   ASP A 587    10045   9386  10173   1149  -3538   -734  A    O  
ATOM   1093  CB  ASP A 587      13.243  -7.954 -10.402  1.00 81.64      A    C  
ANISOU 1093  CB  ASP A 587     9501  10156  11361    860  -3410  -1248  A    C  
ATOM   1094  CG  ASP A 587      14.024  -7.953 -11.695  1.00 86.20      A    C  
ANISOU 1094  CG  ASP A 587     9535  10837  12379    758  -3189  -1451  A    C  
ATOM   1095  OD1 ASP A 587      14.057  -6.906 -12.376  1.00 85.58      A    O  
ANISOU 1095  OD1 ASP A 587     9184  10860  12473    492  -2911  -1535  A    O  
ATOM   1096  OD2 ASP A 587      14.609  -9.005 -12.026  1.00 90.43      A    O1-
ANISOU 1096  OD2 ASP A 587     9951  11331  13076    939  -3265  -1529  A    O1-
ATOM   1097  N   ASN A 588      10.112  -8.500  -8.854  1.00 71.21      A    N  
ANISOU 1097  N   ASN A 588     9518   8599   8941    829  -3226   -545  A    N  
ATOM   1098  CA  ASN A 588       9.530  -9.312  -7.788  1.00 70.49      A    C  
ANISOU 1098  CA  ASN A 588    10019   8317   8445    987  -3372   -360  A    C  
ATOM   1099  C   ASN A 588       8.046  -9.626  -7.955  1.00 64.84      A    C  
ANISOU 1099  C   ASN A 588     9625   7550   7460    810  -2941    -94  A    C  
ATOM   1100  O   ASN A 588       7.614 -10.746  -7.696  1.00 67.43      A    O  
ANISOU 1100  O   ASN A 588    10315   7711   7594    898  -2922     53  A    O  
ATOM   1101  CB  ASN A 588       9.770  -8.667  -6.420  1.00 74.27      A    C  
ANISOU 1101  CB  ASN A 588    10760   8732   8726   1052  -3553   -413  A    C  
ATOM   1102  CG  ASN A 588      11.239  -8.615  -6.049  1.00 81.12      A    C  
ANISOU 1102  CG  ASN A 588    11358   9600   9864   1239  -3889   -679  A    C  
ATOM   1103  ND2 ASN A 588      11.812  -7.417  -6.068  1.00 84.11      A    N  
ANISOU 1103  ND2 ASN A 588    11395  10109  10452   1131  -3928   -874  A    N  
ATOM   1104  OD1 ASN A 588      11.850  -9.638  -5.741  1.00 84.17      A    O  
ANISOU 1104  OD1 ASN A 588    11851   9858  10273   1473  -4105   -722  A    O  
ATOM   1105  N   THR A 589       7.267  -8.639  -8.381  1.00 58.47      A    N  
ANISOU 1105  N   THR A 589     8687   6871   6658    564  -2598    -53  A    N  
ATOM   1106  CA  THR A 589       5.820  -8.798  -8.453  1.00 53.95      A    C  
ANISOU 1106  CA  THR A 589     8366   6270   5864    400  -2212    143  A    C  
ATOM   1107  C   THR A 589       5.309  -9.064  -9.867  1.00 51.30      A    C  
ANISOU 1107  C   THR A 589     7723   6034   5733    256  -1885    173  A    C  
ATOM   1108  O   THR A 589       5.545  -8.281 -10.788  1.00 51.52      A    O  
ANISOU 1108  O   THR A 589     7375   6211   5988    155  -1774     82  A    O  
ATOM   1109  CB  THR A 589       5.096  -7.566  -7.895  1.00 53.25      A    C  
ANISOU 1109  CB  THR A 589     8394   6237   5603    259  -2057    165  A    C  
ATOM   1110  CG2 THR A 589       3.599  -7.813  -7.831  1.00 49.27      A    C  
ANISOU 1110  CG2 THR A 589     8137   5694   4891    113  -1675    325  A    C  
ATOM   1111  OG1 THR A 589       5.582  -7.284  -6.579  1.00 63.31      A    O  
ANISOU 1111  OG1 THR A 589     9980   7414   6659    394  -2373    120  A    O  
ATOM   1112  N   VAL A 590       4.596 -10.173 -10.024  1.00 46.07      A    N  
ANISOU 1112  N   VAL A 590     7263   5270   4972    242  -1726    295  A    N  
ATOM   1113  CA  VAL A 590       3.977 -10.520 -11.293  1.00 43.44      A    C  
ANISOU 1113  CA  VAL A 590     6695   5018   4794    111  -1436    314  A    C  
ATOM   1114  C   VAL A 590       2.824  -9.577 -11.612  1.00 41.17      A    C  
ANISOU 1114  C   VAL A 590     6330   4855   4460    -81  -1134    345  A    C  
ATOM   1115  O   VAL A 590       1.962  -9.329 -10.769  1.00 39.79      A    O  
ANISOU 1115  O   VAL A 590     6420   4631   4069   -146  -1017    415  A    O  
ATOM   1116  CB  VAL A 590       3.468 -11.977 -11.281  1.00 42.94      A    C  
ANISOU 1116  CB  VAL A 590     6891   4786   4639    129  -1348    413  A    C  
ATOM   1117  CG1 VAL A 590       2.444 -12.215 -12.384  1.00 39.01      A    C  
ANISOU 1117  CG1 VAL A 590     6216   4371   4235    -49  -1016    427  A    C  
ATOM   1118  CG2 VAL A 590       4.636 -12.939 -11.404  1.00 42.98      A    C  
ANISOU 1118  CG2 VAL A 590     6872   4686   4771    342  -1631    356  A    C  
ATOM   1119  N   LYS A 591       2.818  -9.051 -12.834  1.00 36.57      A    N  
ANISOU 1119  N   LYS A 591     5404   4419   4072   -157  -1008    282  A    N  
ATOM   1120  CA  LYS A 591       1.729  -8.204 -13.298  1.00 35.79      A    C  
ANISOU 1120  CA  LYS A 591     5223   4430   3945   -290   -764    297  A    C  
ATOM   1121  C   LYS A 591       1.165  -8.747 -14.607  1.00 35.74      A    C  
ANISOU 1121  C   LYS A 591     5040   4487   4052   -348   -591    286  A    C  
ATOM   1122  O   LYS A 591       1.808  -8.654 -15.651  1.00 34.02      A    O  
ANISOU 1122  O   LYS A 591     4601   4334   3991   -332   -604    225  A    O  
ATOM   1123  CB  LYS A 591       2.217  -6.764 -13.503  1.00 37.12      A    C  
ANISOU 1123  CB  LYS A 591     5221   4694   4188   -311   -798    228  A    C  
ATOM   1124  CG  LYS A 591       2.703  -6.068 -12.242  1.00 37.96      A    C  
ANISOU 1124  CG  LYS A 591     5487   4750   4187   -269   -975    205  A    C  
ATOM   1125  CD  LYS A 591       1.561  -5.826 -11.280  1.00 39.16      A    C  
ANISOU 1125  CD  LYS A 591     5919   4860   4100   -312   -852    278  A    C  
ATOM   1126  CE  LYS A 591       2.036  -5.128 -10.021  1.00 43.37      A    C  
ANISOU 1126  CE  LYS A 591     6657   5334   4488   -263  -1035    246  A    C  
ATOM   1127  NZ  LYS A 591       0.882  -4.735  -9.165  1.00 44.18      A    N1+
ANISOU 1127  NZ  LYS A 591     7024   5403   4359   -320   -852    297  A    N1+
ATOM   1128  N   ILE A 592      -0.034  -9.312 -14.556  1.00 34.53      A    N  
ANISOU 1128  N   ILE A 592     4988   4309   3822   -426   -418    323  A    N  
ATOM   1129  CA  ILE A 592      -0.654  -9.841 -15.763  1.00 35.63      A    C  
ANISOU 1129  CA  ILE A 592     4962   4510   4065   -479   -287    281  A    C  
ATOM   1130  C   ILE A 592      -1.428  -8.761 -16.506  1.00 38.84      A    C  
ANISOU 1130  C   ILE A 592     5202   5063   4494   -516   -186    231  A    C  
ATOM   1131  O   ILE A 592      -2.350  -8.157 -15.963  1.00 42.37      A    O  
ANISOU 1131  O   ILE A 592     5694   5538   4866   -558    -93    227  A    O  
ATOM   1132  CB  ILE A 592      -1.597 -11.023 -15.459  1.00 34.59      A    C  
ANISOU 1132  CB  ILE A 592     4979   4275   3889   -565   -145    298  A    C  
ATOM   1133  CG1 ILE A 592      -0.820 -12.177 -14.829  1.00 34.91      A    C  
ANISOU 1133  CG1 ILE A 592     5253   4126   3886   -497   -259    360  A    C  
ATOM   1134  CG2 ILE A 592      -2.296 -11.491 -16.729  1.00 32.31      A    C  
ANISOU 1134  CG2 ILE A 592     4491   4064   3723   -625    -38    213  A    C  
ATOM   1135  CD1 ILE A 592      -1.700 -13.318 -14.374  1.00 36.54      A    C  
ANISOU 1135  CD1 ILE A 592     5694   4169   4019   -607    -81    394  A    C  
ATOM   1136  N   GLY A 593      -1.041  -8.522 -17.752  1.00 39.26      A    N  
ANISOU 1136  N   GLY A 593     5087   5193   4638   -485   -201    186  A    N  
ATOM   1137  CA  GLY A 593      -1.725  -7.555 -18.584  1.00 38.54      A    C  
ANISOU 1137  CA  GLY A 593     4900   5208   4534   -479   -141    146  A    C  
ATOM   1138  C   GLY A 593      -1.998  -8.096 -19.971  1.00 37.80      A    C  
ANISOU 1138  C   GLY A 593     4705   5166   4490   -466   -114     83  A    C  
ATOM   1139  O   GLY A 593      -1.912  -9.306 -20.201  1.00 34.26      A    O  
ANISOU 1139  O   GLY A 593     4246   4674   4097   -489   -108     61  A    O  
ATOM   1140  N   ASP A 594      -2.348  -7.189 -20.880  1.00 38.32      A    N  
ANISOU 1140  N   ASP A 594     4739   5306   4516   -417   -108     53  A    N  
ATOM   1141  CA  ASP A 594      -2.501  -7.483 -22.301  1.00 38.52      A    C  
ANISOU 1141  CA  ASP A 594     4729   5374   4533   -375   -109     -9  A    C  
ATOM   1142  C   ASP A 594      -3.629  -8.469 -22.589  1.00 41.43      A    C  
ANISOU 1142  C   ASP A 594     5019   5781   4942   -397   -115   -106  A    C  
ATOM   1143  O   ASP A 594      -3.419  -9.466 -23.273  1.00 46.11      A    O  
ANISOU 1143  O   ASP A 594     5590   6355   5574   -413   -114   -154  A    O  
ATOM   1144  CB  ASP A 594      -1.180  -7.999 -22.875  1.00 41.01      A    C  
ANISOU 1144  CB  ASP A 594     5042   5639   4900   -384    -85     -1  A    C  
ATOM   1145  CG  ASP A 594      -1.057  -7.760 -24.360  1.00 49.25      A    C  
ANISOU 1145  CG  ASP A 594     6133   6709   5872   -337    -46    -44  A    C  
ATOM   1146  OD1 ASP A 594      -1.684  -6.805 -24.871  1.00 49.99      A    O  
ANISOU 1146  OD1 ASP A 594     6314   6836   5846   -275    -64    -42  A    O  
ATOM   1147  OD2 ASP A 594      -0.320  -8.524 -25.017  1.00 52.64      A    O1-
ANISOU 1147  OD2 ASP A 594     6543   7110   6349   -347      1    -82  A    O1-
ATOM   1148  N   PHE A 595      -4.823  -8.185 -22.077  1.00 42.38      A    N  
ANISOU 1148  N   PHE A 595     5079   5949   5073   -406   -107   -162  A    N  
ATOM   1149  CA  PHE A 595      -5.961  -9.082 -22.273  1.00 47.15      A    C  
ANISOU 1149  CA  PHE A 595     5558   6591   5767   -460    -90   -301  A    C  
ATOM   1150  C   PHE A 595      -6.327  -9.171 -23.751  1.00 51.31      A    C  
ANISOU 1150  C   PHE A 595     6032   7192   6272   -368   -203   -418  A    C  
ATOM   1151  O   PHE A 595      -5.995  -8.284 -24.535  1.00 50.70      A    O  
ANISOU 1151  O   PHE A 595     6049   7141   6075   -242   -281   -384  A    O  
ATOM   1152  CB  PHE A 595      -7.183  -8.635 -21.459  1.00 48.85      A    C  
ANISOU 1152  CB  PHE A 595     5672   6855   6034   -490    -31   -384  A    C  
ATOM   1153  CG  PHE A 595      -6.990  -8.703 -19.964  1.00 52.88      A    C  
ANISOU 1153  CG  PHE A 595     6286   7276   6531   -596    106   -289  A    C  
ATOM   1154  CD1 PHE A 595      -5.834  -9.231 -19.415  1.00 53.24      A    C  
ANISOU 1154  CD1 PHE A 595     6499   7204   6525   -637    115   -149  A    C  
ATOM   1155  CD2 PHE A 595      -7.976  -8.238 -19.108  1.00 55.40      A    C  
ANISOU 1155  CD2 PHE A 595     6547   7622   6881   -636    216   -358  A    C  
ATOM   1156  CE1 PHE A 595      -5.658  -9.287 -18.045  1.00 52.20      A    C  
ANISOU 1156  CE1 PHE A 595     6526   6975   6333   -703    199    -64  A    C  
ATOM   1157  CE2 PHE A 595      -7.807  -8.294 -17.737  1.00 55.02      A    C  
ANISOU 1157  CE2 PHE A 595     6659   7475   6770   -730    355   -271  A    C  
ATOM   1158  CZ  PHE A 595      -6.647  -8.820 -17.206  1.00 53.05      A    C  
ANISOU 1158  CZ  PHE A 595     6628   7101   6430   -758    330   -116  A    C  
ATOM   1159  N   GLY A 596      -7.008 -10.250 -24.124  1.00 55.08      A    N  
ANISOU 1159  N   GLY A 596     6396   7683   6849   -435   -206   -562  A    N  
ATOM   1160  CA  GLY A 596      -7.415 -10.464 -25.499  1.00 57.12      A    C  
ANISOU 1160  CA  GLY A 596     6618   8009   7077   -345   -345   -705  A    C  
ATOM   1161  C   GLY A 596      -8.440  -9.452 -25.974  1.00 61.95      A    C  
ANISOU 1161  C   GLY A 596     7153   8735   7650   -185   -507   -825  A    C  
ATOM   1162  O   GLY A 596      -9.542  -9.366 -25.433  1.00 65.35      A    O  
ANISOU 1162  O   GLY A 596     7382   9228   8219   -211   -507   -965  A    O  
ATOM   1163  N   GLY A 615      -0.202 -14.242 -33.888  1.00 82.08      A    N  
ANISOU 1163  N   GLY A 615    10891  10757   9538   -123    216   -892  A    N  
ATOM   1164  CA  GLY A 615       1.207 -14.573 -33.999  1.00 81.76      A    C  
ANISOU 1164  CA  GLY A 615    10820  10639   9608   -158    461   -897  A    C  
ATOM   1165  C   GLY A 615       1.708 -15.417 -32.842  1.00 80.03      A    C  
ANISOU 1165  C   GLY A 615    10340  10368   9698   -204    451   -882  A    C  
ATOM   1166  O   GLY A 615       2.736 -16.089 -32.951  1.00 82.35      A    O  
ANISOU 1166  O   GLY A 615    10563  10591  10136   -197    588   -948  A    O  
ATOM   1167  N   SER A 616       0.975 -15.383 -31.732  1.00 73.70      A    N  
ANISOU 1167  N   SER A 616     9420   9591   8992   -235    290   -804  A    N  
ATOM   1168  CA  SER A 616       1.359 -16.101 -30.519  1.00 66.70      A    C  
ANISOU 1168  CA  SER A 616     8375   8628   8341   -261    256   -761  A    C  
ATOM   1169  C   SER A 616       0.635 -17.440 -30.378  1.00 61.50      A    C  
ANISOU 1169  C   SER A 616     7714   7893   7760   -294    169   -843  A    C  
ATOM   1170  O   SER A 616      -0.254 -17.596 -29.539  1.00 60.27      A    O  
ANISOU 1170  O   SER A 616     7522   7729   7649   -359     77   -803  A    O  
ATOM   1171  CB  SER A 616       1.081 -15.236 -29.295  1.00 68.33      A    C  
ANISOU 1171  CB  SER A 616     8511   8872   8577   -292    180   -620  A    C  
ATOM   1172  OG  SER A 616      -0.274 -14.825 -29.274  1.00 69.29      A    O  
ANISOU 1172  OG  SER A 616     8666   9073   8589   -317     73   -616  A    O  
ATOM   1173  N   ILE A 617       1.043 -18.412 -31.187  1.00 55.75      A    N  
ANISOU 1173  N   ILE A 617     7034   7091   7058   -264    230   -970  A    N  
ATOM   1174  CA  ILE A 617       0.381 -19.709 -31.220  1.00 50.15      A    C  
ANISOU 1174  CA  ILE A 617     6353   6281   6419   -310    170  -1075  A    C  
ATOM   1175  C   ILE A 617       0.941 -20.731 -30.223  1.00 45.53      A    C  
ANISOU 1175  C   ILE A 617     5746   5516   6036   -300    172  -1032  A    C  
ATOM   1176  O   ILE A 617       0.329 -21.773 -29.992  1.00 43.80      A    O  
ANISOU 1176  O   ILE A 617     5585   5171   5885   -367    141  -1087  A    O  
ATOM   1177  CB  ILE A 617       0.451 -20.320 -32.623  1.00 52.41      A    C  
ANISOU 1177  CB  ILE A 617     6748   6552   6612   -275    220  -1254  A    C  
ATOM   1178  CG1 ILE A 617       1.909 -20.524 -33.032  1.00 53.54      A    C  
ANISOU 1178  CG1 ILE A 617     6891   6633   6818   -184    388  -1285  A    C  
ATOM   1179  CG2 ILE A 617      -0.269 -19.432 -33.623  1.00 52.99      A    C  
ANISOU 1179  CG2 ILE A 617     6926   6772   6437   -258    163  -1305  A    C  
ATOM   1180  CD1 ILE A 617       2.159 -21.844 -33.721  1.00 56.93      A    C  
ANISOU 1180  CD1 ILE A 617     7392   6933   7305   -152    440  -1457  A    C  
ATOM   1181  N   LEU A 618       2.099 -20.439 -29.639  1.00 42.42      A    N  
ANISOU 1181  N   LEU A 618     5284   5094   5738   -211    198   -950  A    N  
ATOM   1182  CA  LEU A 618       2.747 -21.377 -28.725  1.00 40.56      A    C  
ANISOU 1182  CA  LEU A 618     5064   4674   5674   -138    146   -918  A    C  
ATOM   1183  C   LEU A 618       1.945 -21.616 -27.445  1.00 39.61      A    C  
ANISOU 1183  C   LEU A 618     5039   4458   5552   -217     57   -791  A    C  
ATOM   1184  O   LEU A 618       2.115 -22.639 -26.782  1.00 40.04      A    O  
ANISOU 1184  O   LEU A 618     5221   4304   5690   -179     16   -768  A    O  
ATOM   1185  CB  LEU A 618       4.157 -20.903 -28.377  1.00 39.28      A    C  
ANISOU 1185  CB  LEU A 618     4765   4525   5634     -5    147   -899  A    C  
ATOM   1186  CG  LEU A 618       5.186 -20.946 -29.504  1.00 42.11      A    C  
ANISOU 1186  CG  LEU A 618     5022   4918   6061     73    297  -1057  A    C  
ATOM   1187  CD1 LEU A 618       6.529 -20.446 -29.003  1.00 41.29      A    C  
ANISOU 1187  CD1 LEU A 618     4714   4832   6143    180    295  -1076  A    C  
ATOM   1188  CD2 LEU A 618       5.312 -22.356 -30.063  1.00 44.37      A    C  
ANISOU 1188  CD2 LEU A 618     5391   5046   6423    140    323  -1195  A    C  
ATOM   1189  N   TRP A 619       1.075 -20.672 -27.106  1.00 37.62      A    N  
ANISOU 1189  N   TRP A 619     4757   4339   5197   -321     46   -716  A    N  
ATOM   1190  CA  TRP A 619       0.279 -20.758 -25.887  1.00 36.42      A    C  
ANISOU 1190  CA  TRP A 619     4697   4110   5032   -418     19   -609  A    C  
ATOM   1191  C   TRP A 619      -1.174 -21.092 -26.208  1.00 38.10      A    C  
ANISOU 1191  C   TRP A 619     4915   4340   5221   -592     73   -704  A    C  
ATOM   1192  O   TRP A 619      -2.027 -21.109 -25.321  1.00 36.65      A    O  
ANISOU 1192  O   TRP A 619     4780   4110   5037   -718    112   -655  A    O  
ATOM   1193  CB  TRP A 619       0.360 -19.441 -25.104  1.00 33.51      A    C  
ANISOU 1193  CB  TRP A 619     4266   3867   4597   -407    -21   -480  A    C  
ATOM   1194  CG  TRP A 619       1.738 -19.123 -24.590  1.00 33.36      A    C  
ANISOU 1194  CG  TRP A 619     4215   3823   4639   -258    -98   -416  A    C  
ATOM   1195  CD1 TRP A 619       2.215 -19.361 -23.336  1.00 33.99      A    C  
ANISOU 1195  CD1 TRP A 619     4407   3767   4740   -185   -203   -315  A    C  
ATOM   1196  CD2 TRP A 619       2.814 -18.516 -25.320  1.00 34.94      A    C  
ANISOU 1196  CD2 TRP A 619     4256   4125   4893   -165    -79   -479  A    C  
ATOM   1197  CE2 TRP A 619       3.911 -18.420 -24.442  1.00 34.26      A    C  
ANISOU 1197  CE2 TRP A 619     4128   3977   4911    -43   -190   -441  A    C  
ATOM   1198  CE3 TRP A 619       2.955 -18.043 -26.629  1.00 35.82      A    C  
ANISOU 1198  CE3 TRP A 619     4281   4362   4969   -178     34   -575  A    C  
ATOM   1199  NE1 TRP A 619       3.519 -18.945 -23.238  1.00 34.62      A    N  
ANISOU 1199  NE1 TRP A 619     4361   3878   4915    -37   -295   -335  A    N  
ATOM   1200  CZ2 TRP A 619       5.134 -17.872 -24.829  1.00 34.73      A    C  
ANISOU 1200  CZ2 TRP A 619     3992   4110   5095     40   -172   -526  A    C  
ATOM   1201  CZ3 TRP A 619       4.173 -17.499 -27.013  1.00 34.35      A    C  
ANISOU 1201  CZ3 TRP A 619     3963   4224   4866   -109     98   -628  A    C  
ATOM   1202  CH2 TRP A 619       5.244 -17.419 -26.116  1.00 34.51      A    C  
ANISOU 1202  CH2 TRP A 619     3874   4194   5044    -14      6   -618  A    C  
ATOM   1203  N   MET A 620      -1.450 -21.358 -27.481  1.00 40.28      A    N  
ANISOU 1203  N   MET A 620     5139   4682   5484   -602     79   -866  A    N  
ATOM   1204  CA  MET A 620      -2.812 -21.641 -27.917  1.00 42.62      A    C  
ANISOU 1204  CA  MET A 620     5388   5020   5788   -751     83  -1017  A    C  
ATOM   1205  C   MET A 620      -3.181 -23.104 -27.703  1.00 46.37      A    C  
ANISOU 1205  C   MET A 620     5977   5261   6382   -876    155  -1104  A    C  
ATOM   1206  O   MET A 620      -2.486 -24.003 -28.171  1.00 47.66      A    O  
ANISOU 1206  O   MET A 620     6240   5283   6585   -807    166  -1155  A    O  
ATOM   1207  CB  MET A 620      -3.001 -21.252 -29.385  1.00 44.53      A    C  
ANISOU 1207  CB  MET A 620     5566   5427   5927   -690     15  -1171  A    C  
ATOM   1208  CG  MET A 620      -3.141 -19.756 -29.603  1.00 46.80      A    C  
ANISOU 1208  CG  MET A 620     5782   5924   6075   -614    -49  -1109  A    C  
ATOM   1209  SD  MET A 620      -3.292 -19.311 -31.341  1.00 58.25      A    S  
ANISOU 1209  SD  MET A 620     7288   7517   7329   -506   -138  -1266  A    S  
ATOM   1210  CE  MET A 620      -4.656 -20.350 -31.827  1.00 60.97      A    C  
ANISOU 1210  CE  MET A 620     7565   7841   7758   -625   -242  -1532  A    C  
ATOM   1211  N   ALA A 621      -4.274 -23.332 -26.981  1.00 47.38      A    N  
ANISOU 1211  N   ALA A 621     6096   5329   6576  -1068    231  -1130  A    N  
ATOM   1212  CA  ALA A 621      -4.787 -24.678 -26.761  1.00 47.81      A    C  
ANISOU 1212  CA  ALA A 621     6279   5137   6752  -1243    348  -1229  A    C  
ATOM   1213  C   ALA A 621      -5.223 -25.269 -28.095  1.00 49.46      A    C  
ANISOU 1213  C   ALA A 621     6397   5382   7011  -1287    297  -1490  A    C  
ATOM   1214  O   ALA A 621      -5.598 -24.530 -29.000  1.00 49.13      A    O  
ANISOU 1214  O   ALA A 621     6180   5581   6906  -1231    172  -1611  A    O  
ATOM   1215  CB  ALA A 621      -5.950 -24.644 -25.787  1.00 47.30      A    C  
ANISOU 1215  CB  ALA A 621     6189   5024   6757  -1479    496  -1239  A    C  
ATOM   1216  N   PRO A 622      -5.167 -26.604 -28.222  1.00 51.82      A    N  
ANISOU 1216  N   PRO A 622     6858   5425   7406  -1371    377  -1581  A    N  
ATOM   1217  CA  PRO A 622      -5.586 -27.309 -29.437  1.00 51.16      A    C  
ANISOU 1217  CA  PRO A 622     6722   5339   7377  -1430    329  -1855  A    C  
ATOM   1218  C   PRO A 622      -6.962 -26.873 -29.932  1.00 52.92      A    C  
ANISOU 1218  C   PRO A 622     6679   5769   7657  -1582    257  -2097  A    C  
ATOM   1219  O   PRO A 622      -7.137 -26.681 -31.135  1.00 54.13      A    O  
ANISOU 1219  O   PRO A 622     6738   6087   7744  -1499     92  -2285  A    O  
ATOM   1220  CB  PRO A 622      -5.642 -28.767 -28.983  1.00 51.41      A    C  
ANISOU 1220  CB  PRO A 622     6986   5005   7542  -1586    488  -1892  A    C  
ATOM   1221  CG  PRO A 622      -4.617 -28.864 -27.932  1.00 51.24      A    C  
ANISOU 1221  CG  PRO A 622     7204   4798   7466  -1446    538  -1608  A    C  
ATOM   1222  CD  PRO A 622      -4.594 -27.528 -27.226  1.00 52.79      A    C  
ANISOU 1222  CD  PRO A 622     7274   5216   7566  -1382    496  -1424  A    C  
ATOM   1223  N   GLU A 623      -7.920 -26.716 -29.021  1.00 51.90      A    N  
ANISOU 1223  N   GLU A 623     6442   5629   7650  -1789    374  -2109  A    N  
ATOM   1224  CA  GLU A 623      -9.277 -26.345 -29.411  1.00 52.79      A    C  
ANISOU 1224  CA  GLU A 623     6240   5935   7881  -1930    300  -2388  A    C  
ATOM   1225  C   GLU A 623      -9.342 -24.914 -29.942  1.00 53.68      A    C  
ANISOU 1225  C   GLU A 623     6174   6380   7842  -1708     69  -2370  A    C  
ATOM   1226  O   GLU A 623     -10.203 -24.586 -30.759  1.00 58.34      A    O  
ANISOU 1226  O   GLU A 623     6543   7159   8465  -1693   -121  -2631  A    O  
ATOM   1227  CB  GLU A 623     -10.272 -26.554 -28.261  1.00 52.51      A    C  
ANISOU 1227  CB  GLU A 623     6116   5791   8045  -2226    544  -2432  A    C  
ATOM   1228  CG  GLU A 623     -10.147 -25.577 -27.099  1.00 52.90      A    C  
ANISOU 1228  CG  GLU A 623     6184   5905   8012  -2182    640  -2172  A    C  
ATOM   1229  CD  GLU A 623      -9.269 -26.096 -25.979  1.00 53.79      A    C  
ANISOU 1229  CD  GLU A 623     6676   5725   8037  -2191    835  -1868  A    C  
ATOM   1230  OE1 GLU A 623      -8.550 -27.091 -26.200  1.00 53.32      A    O  
ANISOU 1230  OE1 GLU A 623     6868   5434   7957  -2156    851  -1824  A    O  
ATOM   1231  OE2 GLU A 623      -9.301 -25.508 -24.875  1.00 54.15      A    O1-
ANISOU 1231  OE2 GLU A 623     6787   5764   8023  -2212    955  -1684  A    O1-
ATOM   1232  N   VAL A 624      -8.419 -24.071 -29.487  1.00 49.56      A    N  
ANISOU 1232  N   VAL A 624     5766   5912   7153  -1525     70  -2074  A    N  
ATOM   1233  CA  VAL A 624      -8.348 -22.686 -29.952  1.00 50.88      A    C  
ANISOU 1233  CA  VAL A 624     5837   6342   7152  -1314   -114  -2021  A    C  
ATOM   1234  C   VAL A 624      -7.783 -22.610 -31.371  1.00 53.93      A    C  
ANISOU 1234  C   VAL A 624     6322   6811   7357  -1120   -287  -2096  A    C  
ATOM   1235  O   VAL A 624      -8.229 -21.812 -32.192  1.00 55.77      A    O  
ANISOU 1235  O   VAL A 624     6485   7239   7467   -990   -488  -2206  A    O  
ATOM   1236  CB  VAL A 624      -7.494 -21.810 -28.998  1.00 43.25      A    C  
ANISOU 1236  CB  VAL A 624     4969   5385   6079  -1208    -38  -1699  A    C  
ATOM   1237  CG1 VAL A 624      -7.407 -20.380 -29.508  1.00 39.99      A    C  
ANISOU 1237  CG1 VAL A 624     4497   5205   5493  -1009   -200  -1646  A    C  
ATOM   1238  CG2 VAL A 624      -8.079 -21.829 -27.590  1.00 42.51      A    C  
ANISOU 1238  CG2 VAL A 624     4835   5205   6112  -1390    141  -1625  A    C  
ATOM   1239  N   ILE A 625      -6.805 -23.462 -31.651  1.00 55.04      A    N  
ANISOU 1239  N   ILE A 625     6659   6785   7471  -1089   -202  -2045  A    N  
ATOM   1240  CA  ILE A 625      -6.177 -23.526 -32.967  1.00 55.85      A    C  
ANISOU 1240  CA  ILE A 625     6894   6929   7396   -926   -295  -2125  A    C  
ATOM   1241  C   ILE A 625      -7.161 -23.965 -34.067  1.00 61.31      A    C  
ANISOU 1241  C   ILE A 625     7527   7684   8083   -965   -475  -2458  A    C  
ATOM   1242  O   ILE A 625      -7.153 -23.397 -35.169  1.00 62.10      A    O  
ANISOU 1242  O   ILE A 625     7708   7926   7962   -799   -644  -2543  A    O  
ATOM   1243  CB  ILE A 625      -4.960 -24.467 -32.951  1.00 51.71      A    C  
ANISOU 1243  CB  ILE A 625     6556   6193   6899   -890   -145  -2041  A    C  
ATOM   1244  CG1 ILE A 625      -3.853 -23.872 -32.090  1.00 43.95      A    C  
ANISOU 1244  CG1 ILE A 625     5615   5189   5896   -786    -42  -1755  A    C  
ATOM   1245  CG2 ILE A 625      -4.456 -24.731 -34.357  1.00 52.18      A    C  
ANISOU 1245  CG2 ILE A 625     6754   6272   6799   -762   -192  -2186  A    C  
ATOM   1246  CD1 ILE A 625      -2.580 -24.688 -32.054  1.00 43.67      A    C  
ANISOU 1246  CD1 ILE A 625     5716   4964   5913   -696     66  -1695  A    C  
ATOM   1247  N   ARG A 626      -8.000 -24.961 -33.768  1.00 65.54      A    N  
ANISOU 1247  N   ARG A 626     7950   8102   8851  -1186   -437  -2654  A    N  
ATOM   1248  CA  ARG A 626      -8.928 -25.521 -34.747  1.00 70.48      A    C  
ANISOU 1248  CA  ARG A 626     8487   8767   9525  -1251   -618  -3019  A    C  
ATOM   1249  C   ARG A 626      -9.875 -24.488 -35.347  1.00 74.02      A    C  
ANISOU 1249  C   ARG A 626     8759   9483   9881  -1131   -912  -3189  A    C  
ATOM   1250  O   ARG A 626     -10.280 -23.541 -34.693  1.00 76.86      A    O  
ANISOU 1250  O   ARG A 626     8960   9970  10272  -1106   -933  -3088  A    O  
ATOM   1251  CB  ARG A 626      -9.726 -26.689 -34.143  1.00 72.54      A    C  
ANISOU 1251  CB  ARG A 626     8619   8838  10105  -1562   -478  -3210  A    C  
ATOM   1252  CG  ARG A 626      -8.890 -27.874 -33.653  1.00 71.43      A    C  
ANISOU 1252  CG  ARG A 626     8719   8377  10044  -1662   -224  -3080  A    C  
ATOM   1253  CD  ARG A 626      -9.695 -28.885 -32.883  1.00 72.37      A    C  
ANISOU 1253  CD  ARG A 626     8773   8269  10456  -1992    -29  -3215  A    C  
ATOM   1254  NE  ARG A 626      -8.892 -29.709 -31.969  1.00 71.78      A    N  
ANISOU 1254  NE  ARG A 626     8979   7868  10426  -2056    231  -2978  A    N  
ATOM   1255  CZ  ARG A 626      -9.265 -30.093 -30.752  1.00 71.74      A    C  
ANISOU 1255  CZ  ARG A 626     9024   7658  10574  -2283    476  -2883  A    C  
ATOM   1256  NH1 ARG A 626     -10.446 -29.766 -30.278  1.00 71.81      A    N1+
ANISOU 1256  NH1 ARG A 626     8783   7799  10701  -2434    533  -2937  A    N1+
ATOM   1257  NH2 ARG A 626      -8.443 -30.811 -30.015  1.00 71.89      A    N  
ANISOU 1257  NH2 ARG A 626     9373   7368  10574  -2272    653  -2655  A    N  
ATOM   1258  N   PRO A 632     -14.574 -21.431 -28.211  1.00 58.55      A    N  
ANISOU 1258  N   PRO A 632     5428   7787   9033  -1868     -1  -2946  A    N  
ATOM   1259  CA  PRO A 632     -13.170 -21.856 -28.234  1.00 56.91      A    C  
ANISOU 1259  CA  PRO A 632     5549   7418   8658  -1893     37  -2741  A    C  
ATOM   1260  C   PRO A 632     -12.379 -21.298 -27.049  1.00 55.00      A    C  
ANISOU 1260  C   PRO A 632     5522   7096   8279  -1872    227  -2382  A    C  
ATOM   1261  O   PRO A 632     -11.566 -22.015 -26.468  1.00 53.45      A    O  
ANISOU 1261  O   PRO A 632     5620   6669   8021  -1949    413  -2168  A    O  
ATOM   1262  CB  PRO A 632     -12.651 -21.275 -29.551  1.00 55.40      A    C  
ANISOU 1262  CB  PRO A 632     5418   7392   8240  -1593   -323  -2759  A    C  
ATOM   1263  CG  PRO A 632     -13.515 -20.088 -29.803  1.00 57.34      A    C  
ANISOU 1263  CG  PRO A 632     5412   7886   8488  -1412   -547  -2885  A    C  
ATOM   1264  CD  PRO A 632     -14.877 -20.450 -29.267  1.00 60.69      A    C  
ANISOU 1264  CD  PRO A 632     5558   8304   9197  -1565   -387  -3066  A    C  
ATOM   1265  N   TYR A 633     -12.613 -20.036 -26.701  1.00 53.61      A    N  
ANISOU 1265  N   TYR A 633     5226   7099   8044  -1735    156  -2313  A    N  
ATOM   1266  CA  TYR A 633     -11.937 -19.424 -25.562  1.00 52.09      A    C  
ANISOU 1266  CA  TYR A 633     5235   6845   7712  -1698    314  -1989  A    C  
ATOM   1267  C   TYR A 633     -12.710 -19.650 -24.273  1.00 54.74      A    C  
ANISOU 1267  C   TYR A 633     5511   7073   8214  -1964    642  -2027  A    C  
ATOM   1268  O   TYR A 633     -13.877 -19.279 -24.165  1.00 57.98      A    O  
ANISOU 1268  O   TYR A 633     5595   7613   8822  -2051    681  -2279  A    O  
ATOM   1269  CB  TYR A 633     -11.731 -17.928 -25.790  1.00 50.21      A    C  
ANISOU 1269  CB  TYR A 633     4951   6817   7308  -1426    102  -1884  A    C  
ATOM   1270  CG  TYR A 633     -10.680 -17.621 -26.825  1.00 49.03      A    C  
ANISOU 1270  CG  TYR A 633     4986   6714   6931  -1185   -119  -1755  A    C  
ATOM   1271  CD1 TYR A 633      -9.332 -17.726 -26.520  1.00 46.30      A    C  
ANISOU 1271  CD1 TYR A 633     4916   6244   6432  -1129    -47  -1475  A    C  
ATOM   1272  CD2 TYR A 633     -11.033 -17.227 -28.106  1.00 51.34      A    C  
ANISOU 1272  CD2 TYR A 633     5185   7164   7159  -1011   -396  -1932  A    C  
ATOM   1273  CE1 TYR A 633      -8.365 -17.447 -27.460  1.00 46.54      A    C  
ANISOU 1273  CE1 TYR A 633     5089   6310   6284   -941   -186  -1388  A    C  
ATOM   1274  CE2 TYR A 633     -10.073 -16.945 -29.057  1.00 50.84      A    C  
ANISOU 1274  CE2 TYR A 633     5341   7116   6859   -815   -536  -1815  A    C  
ATOM   1275  CZ  TYR A 633      -8.738 -17.056 -28.728  1.00 49.38      A    C  
ANISOU 1275  CZ  TYR A 633     5394   6810   6558   -798   -401  -1548  A    C  
ATOM   1276  OH  TYR A 633      -7.771 -16.779 -29.667  1.00 49.06      A    O  
ANISOU 1276  OH  TYR A 633     5547   6780   6313   -634   -479  -1461  A    O  
ATOM   1277  N   SER A 634     -12.049 -20.255 -23.295  1.00 51.92      A    N  
ANISOU 1277  N   SER A 634     5486   6470   7772  -2079    880  -1791  A    N  
ATOM   1278  CA  SER A 634     -12.692 -20.585 -22.032  1.00 51.66      A    C  
ANISOU 1278  CA  SER A 634     5516   6274   7837  -2351   1247  -1797  A    C  
ATOM   1279  C   SER A 634     -11.673 -20.500 -20.907  1.00 46.78      A    C  
ANISOU 1279  C   SER A 634     5329   5472   6973  -2292   1357  -1433  A    C  
ATOM   1280  O   SER A 634     -10.524 -20.133 -21.136  1.00 42.87      A    O  
ANISOU 1280  O   SER A 634     4996   5008   6287  -2045   1134  -1217  A    O  
ATOM   1281  CB  SER A 634     -13.282 -21.995 -22.099  1.00 56.52      A    C  
ANISOU 1281  CB  SER A 634     6168   6682   8626  -2604   1460  -1968  A    C  
ATOM   1282  OG  SER A 634     -12.256 -22.973 -22.182  1.00 57.35      A    O  
ANISOU 1282  OG  SER A 634     6633   6525   8634  -2634   1473  -1809  A    O  
ATOM   1283  N   PHE A 635     -12.092 -20.838 -19.693  1.00 47.68      A    N  
ANISOU 1283  N   PHE A 635     5637   5390   7090  -2520   1704  -1385  A    N  
ATOM   1284  CA  PHE A 635     -11.162 -20.886 -18.576  1.00 49.29      A    C  
ANISOU 1284  CA  PHE A 635     6314   5382   7032  -2457   1784  -1056  A    C  
ATOM   1285  C   PHE A 635     -10.129 -21.977 -18.807  1.00 48.30      A    C  
ANISOU 1285  C   PHE A 635     6528   5013   6812  -2386   1691   -906  A    C  
ATOM   1286  O   PHE A 635      -8.977 -21.849 -18.400  1.00 44.43      A    O  
ANISOU 1286  O   PHE A 635     6329   4441   6111  -2175   1536   -653  A    O  
ATOM   1287  CB  PHE A 635     -11.900 -21.138 -17.263  1.00 57.09      A    C  
ANISOU 1287  CB  PHE A 635     7516   6169   8005  -2727   2208  -1049  A    C  
ATOM   1288  CG  PHE A 635     -12.947 -20.115 -16.955  1.00 60.93      A    C  
ANISOU 1288  CG  PHE A 635     7667   6896   8588  -2739   2303  -1214  A    C  
ATOM   1289  CD1 PHE A 635     -12.591 -18.838 -16.563  1.00 58.92      A    C  
ANISOU 1289  CD1 PHE A 635     7389   6797   8201  -2588   2195  -1090  A    C  
ATOM   1290  CD2 PHE A 635     -14.289 -20.431 -17.057  1.00 66.99      A    C  
ANISOU 1290  CD2 PHE A 635     8148   7727   9579  -2868   2481  -1505  A    C  
ATOM   1291  CE1 PHE A 635     -13.552 -17.894 -16.277  1.00 62.56      A    C  
ANISOU 1291  CE1 PHE A 635     7549   7452   8769  -2602   2296  -1259  A    C  
ATOM   1292  CE2 PHE A 635     -15.258 -19.493 -16.772  1.00 69.50      A    C  
ANISOU 1292  CE2 PHE A 635     8157   8242  10009  -2854   2556  -1682  A    C  
ATOM   1293  CZ  PHE A 635     -14.889 -18.222 -16.381  1.00 67.06      A    C  
ANISOU 1293  CZ  PHE A 635     7833   8072   9574  -2712   2461  -1556  A    C  
ATOM   1294  N   GLN A 636     -10.555 -23.049 -19.466  1.00 52.04      A    N  
ANISOU 1294  N   GLN A 636     6942   5369   7462  -2556   1774  -1093  A    N  
ATOM   1295  CA  GLN A 636      -9.685 -24.184 -19.740  1.00 55.05      A    C  
ANISOU 1295  CA  GLN A 636     7638   5493   7786  -2498   1709   -992  A    C  
ATOM   1296  C   GLN A 636      -8.534 -23.823 -20.673  1.00 51.33      A    C  
ANISOU 1296  C   GLN A 636     7084   5187   7232  -2163   1331   -910  A    C  
ATOM   1297  O   GLN A 636      -7.411 -24.290 -20.484  1.00 50.88      A    O  
ANISOU 1297  O   GLN A 636     7330   4953   7048  -1992   1224   -723  A    O  
ATOM   1298  CB  GLN A 636     -10.485 -25.350 -20.323  1.00 63.34      A    C  
ANISOU 1298  CB  GLN A 636     8608   6391   9068  -2773   1887  -1253  A    C  
ATOM   1299  CG  GLN A 636     -11.493 -25.960 -19.357  1.00 72.64      A    C  
ANISOU 1299  CG  GLN A 636     9916   7426  10259  -2977   2244  -1283  A    C  
ATOM   1300  CD  GLN A 636     -12.770 -25.151 -19.248  1.00 79.12      A    C  
ANISOU 1300  CD  GLN A 636    10310   8526  11226  -3066   2353  -1500  A    C  
ATOM   1301  NE2 GLN A 636     -13.155 -24.816 -18.023  1.00 81.78      A    N  
ANISOU 1301  NE2 GLN A 636    10817   8805  11450  -3133   2606  -1405  A    N  
ATOM   1302  OE1 GLN A 636     -13.403 -24.828 -20.254  1.00 81.56      A    O  
ANISOU 1302  OE1 GLN A 636    10162   9092  11735  -3048   2193  -1762  A    O  
ATOM   1303  N   SER A 637      -8.806 -22.993 -21.678  1.00 48.64      A    N  
ANISOU 1303  N   SER A 637     6350   5170   6964  -2063   1136  -1063  A    N  
ATOM   1304  CA  SER A 637      -7.752 -22.564 -22.594  1.00 44.48      A    C  
ANISOU 1304  CA  SER A 637     5764   4793   6345  -1776    841   -996  A    C  
ATOM   1305  C   SER A 637      -6.762 -21.614 -21.915  1.00 42.58      A    C  
ANISOU 1305  C   SER A 637     5645   4611   5923  -1564    730   -742  A    C  
ATOM   1306  O   SER A 637      -5.578 -21.599 -22.254  1.00 42.31      A    O  
ANISOU 1306  O   SER A 637     5691   4570   5815  -1356    565   -636  A    O  
ATOM   1307  CB  SER A 637      -8.326 -21.962 -23.879  1.00 41.79      A    C  
ANISOU 1307  CB  SER A 637     5060   4739   6079  -1720    669  -1221  A    C  
ATOM   1308  OG  SER A 637      -9.245 -20.922 -23.622  1.00 43.50      A    O  
ANISOU 1308  OG  SER A 637     5035   5161   6334  -1756    680  -1302  A    O  
ATOM   1309  N   ASP A 638      -7.242 -20.837 -20.947  1.00 42.42      A    N  
ANISOU 1309  N   ASP A 638     5626   4642   5851  -1624    832   -673  A    N  
ATOM   1310  CA  ASP A 638      -6.348 -20.035 -20.115  1.00 42.64      A    C  
ANISOU 1310  CA  ASP A 638     5813   4681   5706  -1455    741   -447  A    C  
ATOM   1311  C   ASP A 638      -5.417 -20.943 -19.313  1.00 42.67      A    C  
ANISOU 1311  C   ASP A 638     6218   4387   5606  -1396    743   -269  A    C  
ATOM   1312  O   ASP A 638      -4.229 -20.661 -19.166  1.00 41.69      A    O  
ANISOU 1312  O   ASP A 638     6184   4262   5395  -1177    547   -137  A    O  
ATOM   1313  CB  ASP A 638      -7.142 -19.144 -19.159  1.00 45.54      A    C  
ANISOU 1313  CB  ASP A 638     6150   5125   6029  -1552    882   -429  A    C  
ATOM   1314  CG  ASP A 638      -7.510 -17.808 -19.769  1.00 46.25      A    C  
ANISOU 1314  CG  ASP A 638     5907   5519   6148  -1454    755   -517  A    C  
ATOM   1315  OD1 ASP A 638      -7.075 -17.523 -20.905  1.00 44.46      A    O  
ANISOU 1315  OD1 ASP A 638     5523   5432   5936  -1308    558   -564  A    O  
ATOM   1316  OD2 ASP A 638      -8.226 -17.035 -19.098  1.00 47.66      A    O1-
ANISOU 1316  OD2 ASP A 638     6016   5775   6317  -1515    864   -539  A    O1-
ATOM   1317  N   VAL A 639      -5.974 -22.032 -18.793  1.00 42.69      A    N  
ANISOU 1317  N   VAL A 639     6468   4124   5629  -1591    965   -284  A    N  
ATOM   1318  CA  VAL A 639      -5.208 -23.007 -18.024  1.00 43.37      A    C  
ANISOU 1318  CA  VAL A 639     7015   3871   5594  -1524    966   -118  A    C  
ATOM   1319  C   VAL A 639      -4.099 -23.633 -18.862  1.00 43.44      A    C  
ANISOU 1319  C   VAL A 639     7020   3828   5656  -1307    737   -122  A    C  
ATOM   1320  O   VAL A 639      -2.965 -23.778 -18.400  1.00 45.42      A    O  
ANISOU 1320  O   VAL A 639     7492   3956   5809  -1074    550     20  A    O  
ATOM   1321  CB  VAL A 639      -6.121 -24.114 -17.467  1.00 47.01      A    C  
ANISOU 1321  CB  VAL A 639     7769   4019   6072  -1813   1300   -155  A    C  
ATOM   1322  CG1 VAL A 639      -5.298 -25.286 -16.944  1.00 47.34      A    C  
ANISOU 1322  CG1 VAL A 639     8330   3668   5990  -1706   1264      3  A    C  
ATOM   1323  CG2 VAL A 639      -7.027 -23.550 -16.382  1.00 49.54      A    C  
ANISOU 1323  CG2 VAL A 639     8185   4332   6305  -2012   1571   -125  A    C  
ATOM   1324  N   TYR A 640      -4.431 -23.998 -20.095  1.00 40.72      A    N  
ANISOU 1324  N   TYR A 640     6417   3580   5476  -1370    742   -311  A    N  
ATOM   1325  CA  TYR A 640      -3.445 -24.537 -21.017  1.00 40.65      A    C  
ANISOU 1325  CA  TYR A 640     6371   3548   5528  -1176    565   -352  A    C  
ATOM   1326  C   TYR A 640      -2.313 -23.541 -21.259  1.00 40.16      A    C  
ANISOU 1326  C   TYR A 640     6134   3701   5423   -912    331   -283  A    C  
ATOM   1327  O   TYR A 640      -1.145 -23.920 -21.282  1.00 42.90      A    O  
ANISOU 1327  O   TYR A 640     6574   3947   5778   -695    179   -234  A    O  
ATOM   1328  CB  TYR A 640      -4.105 -24.905 -22.347  1.00 42.02      A    C  
ANISOU 1328  CB  TYR A 640     6288   3829   5850  -1298    608   -590  A    C  
ATOM   1329  CG  TYR A 640      -3.141 -25.499 -23.348  1.00 43.09      A    C  
ANISOU 1329  CG  TYR A 640     6406   3931   6037  -1113    470   -656  A    C  
ATOM   1330  CD1 TYR A 640      -2.369 -24.683 -24.171  1.00 36.67      A    C  
ANISOU 1330  CD1 TYR A 640     5361   3365   5207   -919    312   -678  A    C  
ATOM   1331  CD2 TYR A 640      -2.995 -26.879 -23.468  1.00 45.30      A    C  
ANISOU 1331  CD2 TYR A 640     6924   3909   6381  -1141    530   -706  A    C  
ATOM   1332  CE1 TYR A 640      -1.480 -25.221 -25.082  1.00 40.08      A    C  
ANISOU 1332  CE1 TYR A 640     5775   3763   5691   -762    236   -760  A    C  
ATOM   1333  CE2 TYR A 640      -2.108 -27.426 -24.382  1.00 43.57      A    C  
ANISOU 1333  CE2 TYR A 640     6683   3654   6218   -959    419   -787  A    C  
ATOM   1334  CZ  TYR A 640      -1.356 -26.592 -25.184  1.00 42.13      A    C  
ANISOU 1334  CZ  TYR A 640     6245   3740   6024   -773    283   -820  A    C  
ATOM   1335  OH  TYR A 640      -0.473 -27.125 -26.088  1.00 42.24      A    O  
ANISOU 1335  OH  TYR A 640     6234   3717   6098   -605    223   -922  A    O  
ATOM   1336  N   ALA A 641      -2.670 -22.276 -21.462  1.00 35.44      A    N  
ANISOU 1336  N   ALA A 641     5275   3390   4802   -932    310   -303  A    N  
ATOM   1337  CA  ALA A 641      -1.685 -21.226 -21.707  1.00 35.38      A    C  
ANISOU 1337  CA  ALA A 641     5102   3577   4764   -734    140   -253  A    C  
ATOM   1338  C   ALA A 641      -0.776 -21.064 -20.499  1.00 36.56      A    C  
ANISOU 1338  C   ALA A 641     5455   3606   4829   -587     23    -87  A    C  
ATOM   1339  O   ALA A 641       0.411 -20.757 -20.628  1.00 36.66      A    O  
ANISOU 1339  O   ALA A 641     5386   3666   4876   -391   -142    -73  A    O  
ATOM   1340  CB  ALA A 641      -2.379 -19.914 -22.023  1.00 33.28      A    C  
ANISOU 1340  CB  ALA A 641     4594   3584   4466   -796    158   -292  A    C  
ATOM   1341  N   PHE A 642      -1.355 -21.259 -19.322  1.00 37.42      A    N  
ANISOU 1341  N   PHE A 642     5831   3557   4829   -688    114     16  A    N  
ATOM   1342  CA  PHE A 642      -0.605 -21.232 -18.082  1.00 40.25      A    C  
ANISOU 1342  CA  PHE A 642     6477   3758   5057   -541    -19    170  A    C  
ATOM   1343  C   PHE A 642       0.318 -22.446 -17.995  1.00 42.42      A    C  
ANISOU 1343  C   PHE A 642     6996   3764   5358   -359   -156    195  A    C  
ATOM   1344  O   PHE A 642       1.405 -22.372 -17.425  1.00 43.73      A    O  
ANISOU 1344  O   PHE A 642     7263   3865   5488   -119   -396    256  A    O  
ATOM   1345  CB  PHE A 642      -1.565 -21.195 -16.894  1.00 43.90      A    C  
ANISOU 1345  CB  PHE A 642     7233   4091   5355   -716    166    267  A    C  
ATOM   1346  CG  PHE A 642      -0.880 -21.218 -15.565  1.00 45.38      A    C  
ANISOU 1346  CG  PHE A 642     7812   4085   5344   -560     20    430  A    C  
ATOM   1347  CD1 PHE A 642      -0.286 -20.077 -15.058  1.00 41.09      A    C  
ANISOU 1347  CD1 PHE A 642     7181   3702   4728   -425   -165    475  A    C  
ATOM   1348  CD2 PHE A 642      -0.829 -22.386 -14.820  1.00 48.52      A    C  
ANISOU 1348  CD2 PHE A 642     8702   4120   5612   -539     55    529  A    C  
ATOM   1349  CE1 PHE A 642       0.349 -20.097 -13.834  1.00 41.52      A    C  
ANISOU 1349  CE1 PHE A 642     7608   3582   4584   -261   -348    599  A    C  
ATOM   1350  CE2 PHE A 642      -0.199 -22.414 -13.597  1.00 48.93      A    C  
ANISOU 1350  CE2 PHE A 642     9176   3977   5438   -357   -124    676  A    C  
ATOM   1351  CZ  PHE A 642       0.391 -21.264 -13.100  1.00 45.76      A    C  
ANISOU 1351  CZ  PHE A 642     8659   3763   4965   -212   -343    703  A    C  
ATOM   1352  N   GLY A 643      -0.122 -23.563 -18.564  1.00 43.69      A    N  
ANISOU 1352  N   GLY A 643     7243   3764   5595   -459    -21    123  A    N  
ATOM   1353  CA  GLY A 643       0.698 -24.761 -18.623  1.00 44.90      A    C  
ANISOU 1353  CA  GLY A 643     7622   3646   5792   -275   -141    124  A    C  
ATOM   1354  C   GLY A 643       1.955 -24.547 -19.447  1.00 43.07      A    C  
ANISOU 1354  C   GLY A 643     7081   3565   5717    -23   -357     22  A    C  
ATOM   1355  O   GLY A 643       3.029 -25.030 -19.097  1.00 41.30      A    O  
ANISOU 1355  O   GLY A 643     6986   3184   5524    244   -576     39  A    O  
ATOM   1356  N   ILE A 644       1.816 -23.815 -20.547  1.00 39.31      A    N  
ANISOU 1356  N   ILE A 644     6209   3386   5343   -101   -290   -100  A    N  
ATOM   1357  CA  ILE A 644       2.951 -23.473 -21.398  1.00 39.73      A    C  
ANISOU 1357  CA  ILE A 644     5956   3599   5541     85   -409   -213  A    C  
ATOM   1358  C   ILE A 644       3.899 -22.517 -20.671  1.00 40.67      A    C  
ANISOU 1358  C   ILE A 644     5973   3822   5659    253   -606   -160  A    C  
ATOM   1359  O   ILE A 644       5.122 -22.616 -20.802  1.00 41.25      A    O  
ANISOU 1359  O   ILE A 644     5910   3889   5874    476   -770   -243  A    O  
ATOM   1360  CB  ILE A 644       2.488 -22.840 -22.725  1.00 39.03      A    C  
ANISOU 1360  CB  ILE A 644     5559   3776   5495    -54   -263   -338  A    C  
ATOM   1361  CG1 ILE A 644       1.635 -23.831 -23.524  1.00 40.48      A    C  
ANISOU 1361  CG1 ILE A 644     5815   3863   5703   -199   -118   -442  A    C  
ATOM   1362  CG2 ILE A 644       3.681 -22.388 -23.553  1.00 38.14      A    C  
ANISOU 1362  CG2 ILE A 644     5172   3812   5509    104   -317   -450  A    C  
ATOM   1363  CD1 ILE A 644       2.426 -24.967 -24.144  1.00 37.36      A    C  
ANISOU 1363  CD1 ILE A 644     5469   3296   5428    -49   -150   -552  A    C  
ATOM   1364  N   VAL A 645       3.330 -21.593 -19.903  1.00 39.44      A    N  
ANISOU 1364  N   VAL A 645     5862   3760   5363    142   -588    -51  A    N  
ATOM   1365  CA  VAL A 645       4.134 -20.693 -19.083  1.00 39.84      A    C  
ANISOU 1365  CA  VAL A 645     5859   3886   5394    280   -785     -7  A    C  
ATOM   1366  C   VAL A 645       4.899 -21.483 -18.025  1.00 45.26      A    C  
ANISOU 1366  C   VAL A 645     6846   4310   6041    519  -1039     51  A    C  
ATOM   1367  O   VAL A 645       6.082 -21.232 -17.794  1.00 48.44      A    O  
ANISOU 1367  O   VAL A 645     7105   4742   6557    745  -1286    -23  A    O  
ATOM   1368  CB  VAL A 645       3.276 -19.601 -18.409  1.00 39.10      A    C  
ANISOU 1368  CB  VAL A 645     5807   3915   5134    114   -703     96  A    C  
ATOM   1369  CG1 VAL A 645       4.089 -18.869 -17.346  1.00 39.90      A    C  
ANISOU 1369  CG1 VAL A 645     5950   4028   5184    264   -938    142  A    C  
ATOM   1370  CG2 VAL A 645       2.738 -18.630 -19.443  1.00 31.08      A    C  
ANISOU 1370  CG2 VAL A 645     4481   3165   4164    -43   -535     25  A    C  
ATOM   1371  N   LEU A 646       4.223 -22.440 -17.392  1.00 44.24      A    N  
ANISOU 1371  N   LEU A 646     7145   3909   5753    474   -979    166  A    N  
ATOM   1372  CA  LEU A 646       4.886 -23.355 -16.466  1.00 49.24      A    C  
ANISOU 1372  CA  LEU A 646     8173   4230   6307    728  -1224    234  A    C  
ATOM   1373  C   LEU A 646       6.040 -24.075 -17.152  1.00 50.78      A    C  
ANISOU 1373  C   LEU A 646     8188   4366   6740    995  -1410     81  A    C  
ATOM   1374  O   LEU A 646       7.116 -24.240 -16.576  1.00 50.90      A    O  
ANISOU 1374  O   LEU A 646     8254   4284   6803   1307  -1743     44  A    O  
ATOM   1375  CB  LEU A 646       3.902 -24.394 -15.925  1.00 53.04      A    C  
ANISOU 1375  CB  LEU A 646     9177   4385   6589    589  -1037    370  A    C  
ATOM   1376  CG  LEU A 646       2.784 -23.924 -14.995  1.00 53.10      A    C  
ANISOU 1376  CG  LEU A 646     9468   4362   6346    345   -829    516  A    C  
ATOM   1377  CD1 LEU A 646       1.882 -25.096 -14.619  1.00 55.85      A    C  
ANISOU 1377  CD1 LEU A 646    10313   4355   6552    174   -576    609  A    C  
ATOM   1378  CD2 LEU A 646       3.358 -23.256 -13.756  1.00 49.16      A    C  
ANISOU 1378  CD2 LEU A 646     9184   3841   5652    531  -1092    614  A    C  
ATOM   1379  N   TYR A 647       5.801 -24.508 -18.386  1.00 52.58      A    N  
ANISOU 1379  N   TYR A 647     8203   4653   7122    884  -1204    -32  A    N  
ATOM   1380  CA  TYR A 647       6.816 -25.199 -19.171  1.00 55.77      A    C  
ANISOU 1380  CA  TYR A 647     8413   5010   7765   1110  -1311   -204  A    C  
ATOM   1381  C   TYR A 647       8.019 -24.297 -19.388  1.00 55.07      A    C  
ANISOU 1381  C   TYR A 647     7875   5166   7885   1280  -1484   -357  A    C  
ATOM   1382  O   TYR A 647       9.157 -24.727 -19.231  1.00 56.80      A    O  
ANISOU 1382  O   TYR A 647     8012   5293   8277   1587  -1740   -479  A    O  
ATOM   1383  CB  TYR A 647       6.242 -25.641 -20.520  1.00 54.73      A    C  
ANISOU 1383  CB  TYR A 647     8131   4939   7726    919  -1025   -310  A    C  
ATOM   1384  CG  TYR A 647       7.228 -26.373 -21.405  1.00 55.90      A    C  
ANISOU 1384  CG  TYR A 647     8092   5035   8112   1134  -1079   -506  A    C  
ATOM   1385  CD1 TYR A 647       7.442 -27.738 -21.257  1.00 58.50      A    C  
ANISOU 1385  CD1 TYR A 647     8732   5025   8468   1311  -1165   -517  A    C  
ATOM   1386  CD2 TYR A 647       7.941 -25.704 -22.393  1.00 54.79      A    C  
ANISOU 1386  CD2 TYR A 647     7490   5163   8165   1156  -1013   -687  A    C  
ATOM   1387  CE1 TYR A 647       8.340 -28.415 -22.061  1.00 59.29      A    C  
ANISOU 1387  CE1 TYR A 647     8653   5072   8800   1526  -1207   -717  A    C  
ATOM   1388  CE2 TYR A 647       8.842 -26.376 -23.202  1.00 56.74      A    C  
ANISOU 1388  CE2 TYR A 647     7558   5361   8638   1345  -1017   -891  A    C  
ATOM   1389  CZ  TYR A 647       9.036 -27.730 -23.031  1.00 58.27      A    C  
ANISOU 1389  CZ  TYR A 647     8032   5235   8873   1539  -1124   -912  A    C  
ATOM   1390  OH  TYR A 647       9.930 -28.405 -23.831  1.00 59.30      A    O  
ANISOU 1390  OH  TYR A 647     7977   5311   9243   1744  -1122  -1136  A    O  
ATOM   1391  N   GLU A 648       7.757 -23.046 -19.750  1.00 52.59      A    N  
ANISOU 1391  N   GLU A 648     7265   5147   7570   1079  -1337   -370  A    N  
ATOM   1392  CA  GLU A 648       8.819 -22.067 -19.926  1.00 55.14      A    C  
ANISOU 1392  CA  GLU A 648     7169   5691   8090   1170  -1439   -518  A    C  
ATOM   1393  C   GLU A 648       9.652 -21.906 -18.666  1.00 57.40      A    C  
ANISOU 1393  C   GLU A 648     7530   5894   8387   1424  -1818   -517  A    C  
ATOM   1394  O   GLU A 648      10.878 -21.906 -18.725  1.00 58.32      A    O  
ANISOU 1394  O   GLU A 648     7355   6043   8762   1654  -2023   -715  A    O  
ATOM   1395  CB  GLU A 648       8.238 -20.714 -20.322  1.00 53.83      A    C  
ANISOU 1395  CB  GLU A 648     6805   5796   7853    900  -1221   -483  A    C  
ATOM   1396  CG  GLU A 648       7.649 -20.682 -21.710  1.00 54.54      A    C  
ANISOU 1396  CG  GLU A 648     6763   6007   7954    703   -907   -538  A    C  
ATOM   1397  CD  GLU A 648       7.120 -19.318 -22.066  1.00 54.94      A    C  
ANISOU 1397  CD  GLU A 648     6669   6292   7914    489   -738   -500  A    C  
ATOM   1398  OE1 GLU A 648       7.941 -18.424 -22.355  1.00 57.39      A    O  
ANISOU 1398  OE1 GLU A 648     6701   6747   8357    498   -717   -603  A    O  
ATOM   1399  OE2 GLU A 648       5.887 -19.134 -22.042  1.00 53.45      A    O1-
ANISOU 1399  OE2 GLU A 648     6644   6129   7537    314   -622   -382  A    O1-
ATOM   1400  N   LEU A 649       8.978 -21.766 -17.529  1.00 59.31      A    N  
ANISOU 1400  N   LEU A 649     8158   6027   8349   1384  -1909   -319  A    N  
ATOM   1401  CA  LEU A 649       9.656 -21.573 -16.253  1.00 63.44      A    C  
ANISOU 1401  CA  LEU A 649     8840   6458   8807   1627  -2295   -304  A    C  
ATOM   1402  C   LEU A 649      10.579 -22.738 -15.910  1.00 71.67      A    C  
ANISOU 1402  C   LEU A 649    10038   7243   9950   2011  -2637   -388  A    C  
ATOM   1403  O   LEU A 649      11.728 -22.529 -15.531  1.00 75.67      A    O  
ANISOU 1403  O   LEU A 649    10326   7783  10642   2287  -2989   -560  A    O  
ATOM   1404  CB  LEU A 649       8.642 -21.369 -15.125  1.00 61.79      A    C  
ANISOU 1404  CB  LEU A 649     9123   6132   8223   1502  -2272    -61  A    C  
ATOM   1405  CG  LEU A 649       7.830 -20.072 -15.110  1.00 58.81      A    C  
ANISOU 1405  CG  LEU A 649     8620   5992   7733   1199  -2037     10  A    C  
ATOM   1406  CD1 LEU A 649       6.684 -20.182 -14.117  1.00 59.93      A    C  
ANISOU 1406  CD1 LEU A 649     9279   5972   7519   1061  -1924    231  A    C  
ATOM   1407  CD2 LEU A 649       8.718 -18.887 -14.772  1.00 57.22      A    C  
ANISOU 1407  CD2 LEU A 649     8103   5988   7652   1279  -2255   -115  A    C  
ATOM   1408  N   MET A 650      10.080 -23.962 -16.048  1.00 73.42      A    N  
ANISOU 1408  N   MET A 650    10631   7197  10067   2037  -2545   -290  A    N  
ATOM   1409  CA  MET A 650      10.858 -25.136 -15.662  1.00 80.80      A    C  
ANISOU 1409  CA  MET A 650    11816   7829  11055   2428  -2877   -343  A    C  
ATOM   1410  C   MET A 650      11.868 -25.567 -16.725  1.00 84.04      A    C  
ANISOU 1410  C   MET A 650    11750   8311  11869   2615  -2910   -622  A    C  
ATOM   1411  O   MET A 650      12.956 -26.039 -16.401  1.00 89.17      A    O  
ANISOU 1411  O   MET A 650    12335   8858  12689   2992  -3277   -780  A    O  
ATOM   1412  CB  MET A 650       9.937 -26.302 -15.290  1.00 83.51      A    C  
ANISOU 1412  CB  MET A 650    12823   7797  11111   2380  -2754   -122  A    C  
ATOM   1413  CG  MET A 650       9.022 -26.000 -14.106  1.00 84.22      A    C  
ANISOU 1413  CG  MET A 650    13448   7760  10794   2225  -2709    136  A    C  
ATOM   1414  SD  MET A 650       9.919 -25.246 -12.733  1.00 83.69      A    S  
ANISOU 1414  SD  MET A 650    13445   7768  10585   2489  -3175    112  A    S  
ATOM   1415  CE  MET A 650       8.784 -25.531 -11.373  1.00116.50      A    C  
ANISOU 1415  CE  MET A 650    18387  11685  14193   2292  -2995    402  A    C  
ATOM   1416  N   THR A 651      11.508 -25.402 -17.991  1.00 81.73      A    N  
ANISOU 1416  N   THR A 651    11131   8208  11715   2347  -2518   -697  A    N  
ATOM   1417  CA  THR A 651      12.383 -25.804 -19.084  1.00 84.63      A    C  
ANISOU 1417  CA  THR A 651    11074   8642  12438   2481  -2462   -966  A    C  
ATOM   1418  C   THR A 651      13.408 -24.720 -19.415  1.00 82.70      A    C  
ANISOU 1418  C   THR A 651    10210   8710  12504   2505  -2502  -1214  A    C  
ATOM   1419  O   THR A 651      14.568 -25.014 -19.701  1.00 85.82      A    O  
ANISOU 1419  O   THR A 651    10255   9114  13238   2772  -2660  -1486  A    O  
ATOM   1420  CB  THR A 651      11.564 -26.169 -20.344  1.00 86.31      A    C  
ANISOU 1420  CB  THR A 651    11268   8894  12631   2194  -2023   -956  A    C  
ATOM   1421  CG2 THR A 651      12.479 -26.481 -21.521  1.00 90.79      A    C  
ANISOU 1421  CG2 THR A 651    11405   9547  13543   2310  -1914  -1248  A    C  
ATOM   1422  OG1 THR A 651      10.736 -27.308 -20.064  1.00 88.03      A    O  
ANISOU 1422  OG1 THR A 651    12027   8787  12632   2178  -1987   -784  A    O  
ATOM   1423  N   GLY A 652      12.978 -23.466 -19.357  1.00 78.76      A    N  
ANISOU 1423  N   GLY A 652     9572   8450  11903   2222  -2345  -1137  A    N  
ATOM   1424  CA  GLY A 652      13.843 -22.355 -19.706  1.00 76.94      A    C  
ANISOU 1424  CA  GLY A 652     8789   8494  11949   2171  -2308  -1361  A    C  
ATOM   1425  C   GLY A 652      13.725 -22.047 -21.182  1.00 74.68      A    C  
ANISOU 1425  C   GLY A 652     8200   8391  11786   1914  -1847  -1466  A    C  
ATOM   1426  O   GLY A 652      14.304 -21.082 -21.683  1.00 73.46      A    O  
ANISOU 1426  O   GLY A 652     7630   8451  11831   1789  -1685  -1634  A    O  
ATOM   1427  N   GLN A 653      12.952 -22.874 -21.878  1.00 73.66      A    N  
ANISOU 1427  N   GLN A 653     8318   8153  11517   1826  -1628  -1370  A    N  
ATOM   1428  CA  GLN A 653      12.830 -22.779 -23.323  1.00 72.22      A    C  
ANISOU 1428  CA  GLN A 653     7935   8102  11405   1630  -1224  -1479  A    C  
ATOM   1429  C   GLN A 653      11.383 -22.590 -23.740  1.00 65.75      A    C  
ANISOU 1429  C   GLN A 653     7407   7318  10258   1327   -973  -1257  A    C  
ATOM   1430  O   GLN A 653      10.471 -22.752 -22.934  1.00 62.91      A    O  
ANISOU 1430  O   GLN A 653     7395   6851   9656   1274  -1079  -1038  A    O  
ATOM   1431  CB  GLN A 653      13.353 -24.056 -23.971  1.00 76.84      A    C  
ANISOU 1431  CB  GLN A 653     8495   8525  12177   1839  -1207  -1655  A    C  
ATOM   1432  CG  GLN A 653      14.768 -24.430 -23.578  1.00 84.32      A    C  
ANISOU 1432  CG  GLN A 653     9140   9410  13487   2199  -1494  -1914  A    C  
ATOM   1433  CD  GLN A 653      15.217 -25.707 -24.255  1.00 91.58      A    C  
ANISOU 1433  CD  GLN A 653    10053  10156  14589   2418  -1458  -2094  A    C  
ATOM   1434  NE2 GLN A 653      15.685 -26.664 -23.463  1.00 94.84      A    N  
ANISOU 1434  NE2 GLN A 653    10628  10319  15087   2789  -1846  -2125  A    N  
ATOM   1435  OE1 GLN A 653      15.126 -25.840 -25.476  1.00 92.94      A    O  
ANISOU 1435  OE1 GLN A 653    10116  10396  14800   2268  -1093  -2202  A    O  
ATOM   1436  N   LEU A 654      11.180 -22.255 -25.009  1.00 63.46      A    N  
ANISOU 1436  N   LEU A 654     6979   7170   9962   1137   -637  -1335  A    N  
ATOM   1437  CA  LEU A 654       9.846 -22.243 -25.588  1.00 59.46      A    C  
ANISOU 1437  CA  LEU A 654     6720   6691   9181    900   -436  -1189  A    C  
ATOM   1438  C   LEU A 654       9.526 -23.647 -26.081  1.00 58.31      A    C  
ANISOU 1438  C   LEU A 654     6780   6350   9026    967   -403  -1232  A    C  
ATOM   1439  O   LEU A 654      10.433 -24.425 -26.379  1.00 60.10      A    O  
ANISOU 1439  O   LEU A 654     6896   6471   9466   1170   -435  -1409  A    O  
ATOM   1440  CB  LEU A 654       9.767 -21.240 -26.740  1.00 59.73      A    C  
ANISOU 1440  CB  LEU A 654     6586   6941   9168    698   -130  -1255  A    C  
ATOM   1441  CG  LEU A 654       9.773 -19.757 -26.364  1.00 59.53      A    C  
ANISOU 1441  CG  LEU A 654     6442   7088   9089    566   -107  -1178  A    C  
ATOM   1442  CD1 LEU A 654       9.939 -18.907 -27.613  1.00 59.17      A    C  
ANISOU 1442  CD1 LEU A 654     6276   7192   9013    407    220  -1271  A    C  
ATOM   1443  CD2 LEU A 654       8.498 -19.375 -25.614  1.00 55.68      A    C  
ANISOU 1443  CD2 LEU A 654     6209   6607   8340    445   -207   -942  A    C  
ATOM   1444  N   PRO A 655       8.233 -23.985 -26.150  1.00 55.59      A    N  
ANISOU 1444  N   PRO A 655     6719   5946   8458    796   -340  -1097  A    N  
ATOM   1445  CA  PRO A 655       7.850 -25.322 -26.612  1.00 55.20      A    C  
ANISOU 1445  CA  PRO A 655     6881   5691   8401    822   -297  -1151  A    C  
ATOM   1446  C   PRO A 655       8.217 -25.531 -28.071  1.00 54.75      A    C  
ANISOU 1446  C   PRO A 655     6674   5710   8420    813    -77  -1361  A    C  
ATOM   1447  O   PRO A 655       8.299 -24.562 -28.827  1.00 54.66      A    O  
ANISOU 1447  O   PRO A 655     6487   5918   8362    699     96  -1411  A    O  
ATOM   1448  CB  PRO A 655       6.327 -25.320 -26.467  1.00 53.63      A    C  
ANISOU 1448  CB  PRO A 655     6924   5481   7973    573   -232  -1004  A    C  
ATOM   1449  CG  PRO A 655       6.032 -24.245 -25.486  1.00 53.16      A    C  
ANISOU 1449  CG  PRO A 655     6850   5538   7811    501   -317   -836  A    C  
ATOM   1450  CD  PRO A 655       7.074 -23.200 -25.695  1.00 51.97      A    C  
ANISOU 1450  CD  PRO A 655     6387   5586   7774    581   -319   -911  A    C  
ATOM   1451  N   TYR A 656       8.432 -26.789 -28.445  1.00 55.59      A    N  
ANISOU 1451  N   TYR A 656     6894   5610   8618    935    -73  -1479  A    N  
ATOM   1452  CA  TYR A 656       8.675 -27.179 -29.832  1.00 56.03      A    C  
ANISOU 1452  CA  TYR A 656     6880   5696   8712    928    147  -1690  A    C  
ATOM   1453  C   TYR A 656       9.873 -26.452 -30.430  1.00 61.09      A    C  
ANISOU 1453  C   TYR A 656     7180   6513   9519   1008    297  -1861  A    C  
ATOM   1454  O   TYR A 656       9.814 -25.967 -31.559  1.00 59.64      A    O  
ANISOU 1454  O   TYR A 656     6944   6478   9239    879    551  -1956  A    O  
ATOM   1455  CB  TYR A 656       7.428 -26.945 -30.691  1.00 50.77      A    C  
ANISOU 1455  CB  TYR A 656     6357   5137   7795    667    299  -1666  A    C  
ATOM   1456  CG  TYR A 656       6.125 -27.139 -29.946  1.00 47.20      A    C  
ANISOU 1456  CG  TYR A 656     6135   4603   7195    506    187  -1491  A    C  
ATOM   1457  CD1 TYR A 656       5.754 -28.386 -29.460  1.00 48.69      A    C  
ANISOU 1457  CD1 TYR A 656     6573   4504   7421    530    107  -1473  A    C  
ATOM   1458  CD2 TYR A 656       5.265 -26.070 -29.728  1.00 44.17      A    C  
ANISOU 1458  CD2 TYR A 656     5726   4410   6646    322    188  -1359  A    C  
ATOM   1459  CE1 TYR A 656       4.561 -28.562 -28.780  1.00 46.55      A    C  
ANISOU 1459  CE1 TYR A 656     6507   4144   7035    341     72  -1337  A    C  
ATOM   1460  CE2 TYR A 656       4.072 -26.237 -29.046  1.00 41.37      A    C  
ANISOU 1460  CE2 TYR A 656     5539   3988   6193    162    127  -1237  A    C  
ATOM   1461  CZ  TYR A 656       3.726 -27.485 -28.577  1.00 44.83      A    C  
ANISOU 1461  CZ  TYR A 656     6210   4145   6680    155     90  -1232  A    C  
ATOM   1462  OH  TYR A 656       2.539 -27.654 -27.902  1.00 46.00      A    O  
ANISOU 1462  OH  TYR A 656     6519   4210   6748    -43     94  -1134  A    O  
ATOM   1463  N   SER A 657      10.958 -26.389 -29.665  1.00 68.94      A    N  
ANISOU 1463  N   SER A 657     7958   7476  10761   1220    140  -1915  A    N  
ATOM   1464  CA  SER A 657      12.159 -25.679 -30.087  1.00 76.37      A    C  
ANISOU 1464  CA  SER A 657     8512   8576  11929   1277    291  -2114  A    C  
ATOM   1465  C   SER A 657      12.810 -26.338 -31.298  1.00 80.38      A    C  
ANISOU 1465  C   SER A 657     8917   9046  12578   1353    552  -2387  A    C  
ATOM   1466  O   SER A 657      13.317 -25.655 -32.189  1.00 80.38      A    O  
ANISOU 1466  O   SER A 657     8722   9203  12616   1248    865  -2536  A    O  
ATOM   1467  CB  SER A 657      13.160 -25.596 -28.935  1.00 80.83      A    C  
ANISOU 1467  CB  SER A 657     8842   9102  12770   1517      2  -2161  A    C  
ATOM   1468  OG  SER A 657      13.580 -26.887 -28.534  1.00 86.96      A    O  
ANISOU 1468  OG  SER A 657     9707   9627  13708   1815   -225  -2243  A    O  
ATOM   1469  N   ASN A 658      12.792 -27.665 -31.335  1.00 84.78      A    N  
ANISOU 1469  N   ASN A 658     9641   9373  13199   1529    452  -2457  A    N  
ATOM   1470  CA  ASN A 658      13.395 -28.388 -32.450  1.00 91.80      A    C  
ANISOU 1470  CA  ASN A 658    10456  10201  14223   1623    694  -2733  A    C  
ATOM   1471  C   ASN A 658      12.555 -28.350 -33.724  1.00 90.48      A    C  
ANISOU 1471  C   ASN A 658    10524  10099  13754   1383    988  -2743  A    C  
ATOM   1472  O   ASN A 658      12.982 -28.829 -34.773  1.00 93.98      A    O  
ANISOU 1472  O   ASN A 658    10952  10512  14245   1424   1240  -2973  A    O  
ATOM   1473  CB  ASN A 658      13.728 -29.829 -32.051  1.00 98.87      A    C  
ANISOU 1473  CB  ASN A 658    11464  10800  15303   1924    473  -2823  A    C  
ATOM   1474  CG  ASN A 658      14.845 -29.903 -31.023  1.00105.41      A    C  
ANISOU 1474  CG  ASN A 658    12015  11564  16470   2244    180  -2910  A    C  
ATOM   1475  ND2 ASN A 658      14.474 -30.070 -29.759  1.00106.39      A    N  
ANISOU 1475  ND2 ASN A 658    12354  11553  16519   2340   -188  -2684  A    N  
ATOM   1476  OD1 ASN A 658      16.026 -29.803 -31.361  1.00109.27      A    O  
ANISOU 1476  OD1 ASN A 658    12112  12132  17273   2395    283  -3184  A    O  
ATOM   1477  N   ILE A 659      11.360 -27.775 -33.626  1.00 85.39      A    N  
ANISOU 1477  N   ILE A 659    10102   9543  12798   1151    942  -2513  A    N  
ATOM   1478  CA  ILE A 659      10.517 -27.565 -34.797  1.00 82.49      A    C  
ANISOU 1478  CA  ILE A 659     9954   9265  12122    942   1154  -2527  A    C  
ATOM   1479  C   ILE A 659      10.303 -26.084 -35.074  1.00 82.58      A    C  
ANISOU 1479  C   ILE A 659     9916   9518  11942    750   1296  -2422  A    C  
ATOM   1480  O   ILE A 659       9.499 -25.435 -34.403  1.00 80.77      A    O  
ANISOU 1480  O   ILE A 659     9753   9365  11572    636   1127  -2204  A    O  
ATOM   1481  CB  ILE A 659       9.139 -28.217 -34.638  1.00 78.26      A    C  
ANISOU 1481  CB  ILE A 659     9740   8617  11379    833    976  -2398  A    C  
ATOM   1482  CG1 ILE A 659       9.268 -29.689 -34.243  1.00 78.92      A    C  
ANISOU 1482  CG1 ILE A 659     9943   8407  11635   1002    834  -2468  A    C  
ATOM   1483  CG2 ILE A 659       8.340 -28.071 -35.928  1.00 76.96      A    C  
ANISOU 1483  CG2 ILE A 659     9780   8545  10916    663   1142  -2474  A    C  
ATOM   1484  CD1 ILE A 659       7.937 -30.382 -34.082  1.00 78.03      A    C  
ANISOU 1484  CD1 ILE A 659    10138   8153  11358    852    711  -2374  A    C  
ATOM   1485  N   ASN A 660      11.025 -25.545 -36.052  1.00 83.80      A    N  
ANISOU 1485  N   ASN A 660     9980   9773  12088    711   1629  -2583  A    N  
ATOM   1486  CA  ASN A 660      10.842 -24.141 -36.395  1.00 79.28      A    C  
ANISOU 1486  CA  ASN A 660     9436   9383  11304    528   1796  -2482  A    C  
ATOM   1487  C   ASN A 660       9.961 -23.960 -37.614  1.00 77.59      A    C  
ANISOU 1487  C   ASN A 660     9582   9213  10685    398   1937  -2480  A    C  
ATOM   1488  O   ASN A 660      10.400 -23.454 -38.632  1.00 77.93      A    O  
ANISOU 1488  O   ASN A 660     9713   9305  10590    333   2271  -2589  A    O  
ATOM   1489  CB  ASN A 660      12.173 -23.425 -36.609  1.00 79.47      A    C  
ANISOU 1489  CB  ASN A 660     9163   9480  11551    523   2105  -2638  A    C  
ATOM   1490  CG  ASN A 660      12.034 -21.915 -36.528  1.00 76.73      A    C  
ANISOU 1490  CG  ASN A 660     8825   9280  11050    339   2211  -2487  A    C  
ATOM   1491  ND2 ASN A 660      12.974 -21.201 -37.128  1.00 77.95      A    N  
ANISOU 1491  ND2 ASN A 660     8848   9483  11285    248   2602  -2635  A    N  
ATOM   1492  OD1 ASN A 660      11.093 -21.398 -35.929  1.00 73.74      A    O  
ANISOU 1492  OD1 ASN A 660     8575   8953  10490    271   1967  -2253  A    O  
ATOM   1493  N   ASN A 661       8.707 -24.367 -37.482  1.00 74.56      A    N  
ANISOU 1493  N   ASN A 661     9417   8801  10110    359   1678  -2369  A    N  
ATOM   1494  CA  ASN A 661       7.745 -24.278 -38.563  1.00 72.11      A    C  
ANISOU 1494  CA  ASN A 661     9441   8531   9425    269   1706  -2393  A    C  
ATOM   1495  C   ASN A 661       6.337 -24.037 -38.040  1.00 69.78      A    C  
ANISOU 1495  C   ASN A 661     9251   8291   8971    184   1391  -2219  A    C  
ATOM   1496  O   ASN A 661       5.696 -24.950 -37.524  1.00 69.45      A    O  
ANISOU 1496  O   ASN A 661     9215   8150   9024    187   1178  -2216  A    O  
ATOM   1497  CB  ASN A 661       7.801 -25.528 -39.435  1.00 72.95      A    C  
ANISOU 1497  CB  ASN A 661     9702   8504   9513    339   1784  -2619  A    C  
ATOM   1498  CG  ASN A 661       7.043 -25.354 -40.742  1.00 73.66      A    C  
ANISOU 1498  CG  ASN A 661    10157   8642   9188    271   1846  -2698  A    C  
ATOM   1499  ND2 ASN A 661       7.777 -25.188 -41.839  1.00 75.94      A    N  
ANISOU 1499  ND2 ASN A 661    10591   8928   9334    286   2191  -2853  A    N  
ATOM   1500  OD1 ASN A 661       5.812 -25.365 -40.764  1.00 72.39      A    O  
ANISOU 1500  OD1 ASN A 661    10151   8517   8838    210   1585  -2639  A    O  
ATOM   1501  N   ARG A 662       5.873 -22.798 -38.174  1.00 68.94      A    N  
ANISOU 1501  N   ARG A 662     9231   8327   8637    103   1386  -2088  A    N  
ATOM   1502  CA  ARG A 662       4.579 -22.386 -37.637  1.00 66.00      A    C  
ANISOU 1502  CA  ARG A 662     8902   8029   8146     34   1104  -1941  A    C  
ATOM   1503  C   ARG A 662       3.396 -23.218 -38.145  1.00 63.08      A    C  
ANISOU 1503  C   ARG A 662     8701   7623   7642      8    911  -2056  A    C  
ATOM   1504  O   ARG A 662       2.558 -23.658 -37.357  1.00 61.77      A    O  
ANISOU 1504  O   ARG A 662     8451   7427   7592    -48    698  -2011  A    O  
ATOM   1505  CB  ARG A 662       4.356 -20.902 -37.927  1.00 68.63      A    C  
ANISOU 1505  CB  ARG A 662     9348   8499   8230     -9   1150  -1819  A    C  
ATOM   1506  CG  ARG A 662       2.912 -20.450 -37.888  1.00 73.34      A    C  
ANISOU 1506  CG  ARG A 662    10059   9186   8622    -43    876  -1747  A    C  
ATOM   1507  CD  ARG A 662       2.792 -19.014 -38.358  1.00 77.58      A    C  
ANISOU 1507  CD  ARG A 662    10783   9817   8878    -40    933  -1643  A    C  
ATOM   1508  NE  ARG A 662       3.355 -18.078 -37.392  1.00 80.13      A    N  
ANISOU 1508  NE  ARG A 662    10921  10174   9352    -80   1008  -1472  A    N  
ATOM   1509  CZ  ARG A 662       2.634 -17.414 -36.495  1.00 82.45      A    C  
ANISOU 1509  CZ  ARG A 662    11116  10537   9674   -103    809  -1328  A    C  
ATOM   1510  NH1 ARG A 662       3.223 -16.578 -35.651  1.00 82.55      A    N1+
ANISOU 1510  NH1 ARG A 662    10980  10568   9815   -140    883  -1195  A    N1+
ATOM   1511  NH2 ARG A 662       1.319 -17.581 -36.445  1.00 83.43      A    N  
ANISOU 1511  NH2 ARG A 662    11275  10712   9711    -93    541  -1347  A    N  
ATOM   1512  N   ASP A 663       3.333 -23.429 -39.457  1.00 62.61      A    N  
ANISOU 1512  N   ASP A 663     8889   7560   7341     35   1001  -2222  A    N  
ATOM   1513  CA  ASP A 663       2.245 -24.190 -40.062  1.00 63.71      A    C  
ANISOU 1513  CA  ASP A 663     9188   7672   7349     13    800  -2381  A    C  
ATOM   1514  C   ASP A 663       2.174 -25.597 -39.491  1.00 62.66      A    C  
ANISOU 1514  C   ASP A 663     8933   7371   7505    -14    732  -2471  A    C  
ATOM   1515  O   ASP A 663       1.089 -26.135 -39.270  1.00 63.22      A    O  
ANISOU 1515  O   ASP A 663     8995   7412   7614    -99    520  -2532  A    O  
ATOM   1516  CB  ASP A 663       2.423 -24.258 -41.578  1.00 69.55      A    C  
ANISOU 1516  CB  ASP A 663    10253   8406   7766     72    930  -2563  A    C  
ATOM   1517  CG  ASP A 663       1.956 -22.999 -42.274  1.00 73.81      A    C  
ANISOU 1517  CG  ASP A 663    11048   9077   7919     99    882  -2496  A    C  
ATOM   1518  OD1 ASP A 663       1.508 -22.062 -41.579  1.00 71.76      A    O  
ANISOU 1518  OD1 ASP A 663    10677   8917   7671     75    748  -2316  A    O  
ATOM   1519  OD2 ASP A 663       2.046 -22.942 -43.518  1.00 79.62      A    O1-
ANISOU 1519  OD2 ASP A 663    12133   9798   8320    158    978  -2624  A    O1-
ATOM   1520  N   GLN A 664       3.343 -26.178 -39.251  1.00 61.44      A    N  
ANISOU 1520  N   GLN A 664     8687   7091   7567     62    922  -2494  A    N  
ATOM   1521  CA  GLN A 664       3.468 -27.534 -38.740  1.00 61.68      A    C  
ANISOU 1521  CA  GLN A 664     8665   6911   7860     81    880  -2572  A    C  
ATOM   1522  C   GLN A 664       2.895 -27.640 -37.328  1.00 57.23      A    C  
ANISOU 1522  C   GLN A 664     7963   6295   7488      6    696  -2396  A    C  
ATOM   1523  O   GLN A 664       2.049 -28.486 -37.050  1.00 56.66      A    O  
ANISOU 1523  O   GLN A 664     7946   6096   7485    -90    573  -2452  A    O  
ATOM   1524  CB  GLN A 664       4.941 -27.921 -38.736  1.00 66.03      A    C  
ANISOU 1524  CB  GLN A 664     9119   7358   8610    230   1100  -2632  A    C  
ATOM   1525  CG  GLN A 664       5.217 -29.399 -38.820  1.00 72.74      A    C  
ANISOU 1525  CG  GLN A 664    10030   7966   9641    308   1112  -2802  A    C  
ATOM   1526  CD  GLN A 664       6.700 -29.683 -38.891  1.00 79.35      A    C  
ANISOU 1526  CD  GLN A 664    10731   8724  10694    492   1323  -2900  A    C  
ATOM   1527  NE2 GLN A 664       7.366 -29.112 -39.891  1.00 81.53      A    N  
ANISOU 1527  NE2 GLN A 664    11025   9116  10839    517   1591  -3016  A    N  
ATOM   1528  OE1 GLN A 664       7.246 -30.396 -38.051  1.00 81.75      A    O  
ANISOU 1528  OE1 GLN A 664    10925   8857  11281    617   1251  -2884  A    O  
ATOM   1529  N   ILE A 665       3.362 -26.762 -36.448  1.00 52.69      A    N  
ANISOU 1529  N   ILE A 665     7226   5805   6990     34    701  -2197  A    N  
ATOM   1530  CA  ILE A 665       2.895 -26.711 -35.070  1.00 49.55      A    C  
ANISOU 1530  CA  ILE A 665     6736   5363   6727    -28    553  -2015  A    C  
ATOM   1531  C   ILE A 665       1.389 -26.488 -35.003  1.00 49.77      A    C  
ANISOU 1531  C   ILE A 665     6801   5470   6637   -199    407  -2006  A    C  
ATOM   1532  O   ILE A 665       0.696 -27.117 -34.206  1.00 49.65      A    O  
ANISOU 1532  O   ILE A 665     6796   5328   6740   -305    329  -1976  A    O  
ATOM   1533  CB  ILE A 665       3.624 -25.598 -34.300  1.00 48.81      A    C  
ANISOU 1533  CB  ILE A 665     6476   5385   6684     30    574  -1831  A    C  
ATOM   1534  CG1 ILE A 665       5.117 -25.921 -34.224  1.00 50.84      A    C  
ANISOU 1534  CG1 ILE A 665     6622   5555   7141    203    690  -1887  A    C  
ATOM   1535  CG2 ILE A 665       3.044 -25.421 -32.903  1.00 45.27      A    C  
ANISOU 1535  CG2 ILE A 665     5983   4907   6311    -39    424  -1641  A    C  
ATOM   1536  CD1 ILE A 665       5.984 -24.726 -33.924  1.00 51.06      A    C  
ANISOU 1536  CD1 ILE A 665     6460   5729   7211    245    767  -1802  A    C  
ATOM   1537  N   ILE A 666       0.886 -25.601 -35.853  1.00 51.59      A    N  
ANISOU 1537  N   ILE A 666     7064   5897   6639   -221    379  -2050  A    N  
ATOM   1538  CA  ILE A 666      -0.545 -25.336 -35.920  1.00 53.31      A    C  
ANISOU 1538  CA  ILE A 666     7275   6216   6765   -345    205  -2099  A    C  
ATOM   1539  C   ILE A 666      -1.318 -26.606 -36.267  1.00 55.13      A    C  
ANISOU 1539  C   ILE A 666     7570   6306   7072   -449    137  -2317  A    C  
ATOM   1540  O   ILE A 666      -2.311 -26.938 -35.619  1.00 54.96      A    O  
ANISOU 1540  O   ILE A 666     7466   6240   7177   -603     53  -2341  A    O  
ATOM   1541  CB  ILE A 666      -0.858 -24.232 -36.949  1.00 53.65      A    C  
ANISOU 1541  CB  ILE A 666     7406   6464   6514   -286    148  -2137  A    C  
ATOM   1542  CG1 ILE A 666      -0.389 -22.876 -36.417  1.00 51.42      A    C  
ANISOU 1542  CG1 ILE A 666     7055   6306   6178   -238    202  -1913  A    C  
ATOM   1543  CG2 ILE A 666      -2.345 -24.189 -37.268  1.00 42.94      A    C  
ANISOU 1543  CG2 ILE A 666     6034   5200   5082   -365    -87  -2284  A    C  
ATOM   1544  CD1 ILE A 666      -0.497 -21.750 -37.423  1.00 50.55      A    C  
ANISOU 1544  CD1 ILE A 666     7114   6341   5752   -160    189  -1917  A    C  
ATOM   1545  N   GLU A 667      -0.845 -27.318 -37.284  1.00 55.33      A    N  
ANISOU 1545  N   GLU A 667     7743   6248   7032   -381    204  -2494  A    N  
ATOM   1546  CA  GLU A 667      -1.490 -28.549 -37.721  1.00 59.26      A    C  
ANISOU 1546  CA  GLU A 667     8324   6593   7599   -479    147  -2733  A    C  
ATOM   1547  C   GLU A 667      -1.389 -29.649 -36.669  1.00 56.05      A    C  
ANISOU 1547  C   GLU A 667     7907   5916   7472   -564    214  -2682  A    C  
ATOM   1548  O   GLU A 667      -2.377 -30.314 -36.357  1.00 55.20      A    O  
ANISOU 1548  O   GLU A 667     7787   5700   7487   -750    157  -2787  A    O  
ATOM   1549  CB  GLU A 667      -0.880 -29.025 -39.042  1.00 66.60      A    C  
ANISOU 1549  CB  GLU A 667     9451   7482   8374   -366    227  -2931  A    C  
ATOM   1550  CG  GLU A 667      -1.376 -30.385 -39.515  1.00 76.67      A    C  
ANISOU 1550  CG  GLU A 667    10837   8564   9732   -456    184  -3197  A    C  
ATOM   1551  CD  GLU A 667      -2.819 -30.369 -39.989  1.00 82.99      A    C  
ANISOU 1551  CD  GLU A 667    11610   9466  10458   -598    -53  -3409  A    C  
ATOM   1552  OE1 GLU A 667      -3.350 -29.272 -40.276  1.00 84.40      A    O  
ANISOU 1552  OE1 GLU A 667    11741   9882  10447   -562   -203  -3381  A    O  
ATOM   1553  OE2 GLU A 667      -3.418 -31.463 -40.078  1.00 85.15      A    O1-
ANISOU 1553  OE2 GLU A 667    11907   9569  10876   -739    -99  -3624  A    O1-
ATOM   1554  N   MET A 668      -0.195 -29.831 -36.118  1.00 53.43      A    N  
ANISOU 1554  N   MET A 668     7592   5465   7246   -425    337  -2535  A    N  
ATOM   1555  CA  MET A 668       0.056 -30.947 -35.215  1.00 53.42      A    C  
ANISOU 1555  CA  MET A 668     7673   5159   7466   -441    381  -2486  A    C  
ATOM   1556  C   MET A 668      -0.504 -30.741 -33.808  1.00 47.83      A    C  
ANISOU 1556  C   MET A 668     6920   4397   6855   -566    346  -2281  A    C  
ATOM   1557  O   MET A 668      -1.042 -31.674 -33.216  1.00 52.59      A    O  
ANISOU 1557  O   MET A 668     7646   4752   7583   -708    374  -2300  A    O  
ATOM   1558  CB  MET A 668       1.547 -31.277 -35.175  1.00 49.70      A    C  
ANISOU 1558  CB  MET A 668     7232   4567   7083   -199    477  -2447  A    C  
ATOM   1559  CG  MET A 668       2.148 -31.413 -36.558  1.00 51.22      A    C  
ANISOU 1559  CG  MET A 668     7472   4818   7173    -85    577  -2658  A    C  
ATOM   1560  SD  MET A 668       3.704 -32.307 -36.602  1.00 60.06      A    S  
ANISOU 1560  SD  MET A 668     8623   5710   8489    178    708  -2734  A    S  
ATOM   1561  CE  MET A 668       4.621 -31.446 -35.345  1.00 64.08      A    C  
ANISOU 1561  CE  MET A 668     8920   6294   9134    319    670  -2475  A    C  
ATOM   1562  N   VAL A 669      -0.381 -29.531 -33.272  1.00 45.43      A    N  
ANISOU 1562  N   VAL A 669     6475   4302   6486   -528    312  -2093  A    N  
ATOM   1563  CA  VAL A 669      -0.976 -29.235 -31.972  1.00 44.34      A    C  
ANISOU 1563  CA  VAL A 669     6311   4132   6404   -652    293  -1912  A    C  
ATOM   1564  C   VAL A 669      -2.499 -29.235 -32.088  1.00 47.91      A    C  
ANISOU 1564  C   VAL A 669     6694   4649   6860   -906    267  -2046  A    C  
ATOM   1565  O   VAL A 669      -3.202 -29.718 -31.202  1.00 48.94      A    O  
ANISOU 1565  O   VAL A 669     6880   4616   7100  -1091    331  -2013  A    O  
ATOM   1566  CB  VAL A 669      -0.474 -27.886 -31.391  1.00 47.84      A    C  
ANISOU 1566  CB  VAL A 669     6618   4786   6775   -548    258  -1700  A    C  
ATOM   1567  CG1 VAL A 669      -1.212 -27.537 -30.105  1.00 40.88      A    C  
ANISOU 1567  CG1 VAL A 669     5730   3885   5919   -687    250  -1538  A    C  
ATOM   1568  CG2 VAL A 669       1.023 -27.941 -31.133  1.00 41.78      A    C  
ANISOU 1568  CG2 VAL A 669     5863   3943   6070   -313    273  -1609  A    C  
ATOM   1569  N   GLY A 670      -2.997 -28.712 -33.203  1.00 48.95      A    N  
ANISOU 1569  N   GLY A 670     6717   5009   6873   -910    177  -2217  A    N  
ATOM   1570  CA  GLY A 670      -4.426 -28.623 -33.443  1.00 50.19      A    C  
ANISOU 1570  CA  GLY A 670     6744   5269   7056  -1108     94  -2404  A    C  
ATOM   1571  C   GLY A 670      -5.128 -29.964 -33.542  1.00 57.33      A    C  
ANISOU 1571  C   GLY A 670     7716   5936   8130  -1318    145  -2629  A    C  
ATOM   1572  O   GLY A 670      -6.255 -30.116 -33.068  1.00 61.05      A    O  
ANISOU 1572  O   GLY A 670     8070   6386   8742  -1554    168  -2730  A    O  
ATOM   1573  N   ARG A 671      -4.469 -30.940 -34.161  1.00 59.06      A    N  
ANISOU 1573  N   ARG A 671     8118   5966   8354  -1245    186  -2729  A    N  
ATOM   1574  CA  ARG A 671      -5.042 -32.278 -34.302  1.00 62.63      A    C  
ANISOU 1574  CA  ARG A 671     8676   6151   8970  -1444    249  -2953  A    C  
ATOM   1575  C   ARG A 671      -4.691 -33.175 -33.116  1.00 64.80      A    C  
ANISOU 1575  C   ARG A 671     9165   6060   9395  -1517    432  -2780  A    C  
ATOM   1576  O   ARG A 671      -5.203 -34.289 -32.994  1.00 66.98      A    O  
ANISOU 1576  O   ARG A 671     9576   6051   9821  -1722    536  -2925  A    O  
ATOM   1577  CB  ARG A 671      -4.588 -32.933 -35.609  1.00 64.50      A    C  
ANISOU 1577  CB  ARG A 671     9043   6340   9126  -1331    200  -3180  A    C  
ATOM   1578  CG  ARG A 671      -3.129 -33.343 -35.627  1.00 54.88      A    C  
ANISOU 1578  CG  ARG A 671     8017   4958   7878  -1086    301  -3043  A    C  
ATOM   1579  CD  ARG A 671      -2.691 -33.762 -37.016  1.00 56.59      A    C  
ANISOU 1579  CD  ARG A 671     8341   5186   7976   -960    276  -3280  A    C  
ATOM   1580  NE  ARG A 671      -1.267 -34.071 -37.052  1.00 56.56      A    N  
ANISOU 1580  NE  ARG A 671     8460   5052   7977   -712    392  -3182  A    N  
ATOM   1581  CZ  ARG A 671      -0.614 -34.455 -38.141  1.00 58.15      A    C  
ANISOU 1581  CZ  ARG A 671     8774   5231   8088   -566    440  -3361  A    C  
ATOM   1582  NH1 ARG A 671      -1.259 -34.580 -39.290  1.00 72.10      A    N1+
ANISOU 1582  NH1 ARG A 671    10597   7088   9709   -638    360  -3631  A    N1+
ATOM   1583  NH2 ARG A 671       0.684 -34.716 -38.082  1.00 59.88      A    N  
ANISOU 1583  NH2 ARG A 671     9048   5337   8367   -337    561  -3295  A    N  
ATOM   1584  N   GLY A 672      -3.814 -32.684 -32.246  1.00 64.33      A    N  
ANISOU 1584  N   GLY A 672     9166   5991   9285  -1344    462  -2478  A    N  
ATOM   1585  CA  GLY A 672      -3.467 -33.399 -31.030  1.00 64.78      A    C  
ANISOU 1585  CA  GLY A 672     9480   5705   9429  -1363    587  -2284  A    C  
ATOM   1586  C   GLY A 672      -2.273 -34.336 -31.117  1.00 64.99      A    C  
ANISOU 1586  C   GLY A 672     9763   5447   9483  -1130    596  -2247  A    C  
ATOM   1587  O   GLY A 672      -1.993 -35.063 -30.166  1.00 68.94      A    O  
ANISOU 1587  O   GLY A 672    10547   5609  10038  -1114    667  -2102  A    O  
ATOM   1588  N   SER A 673      -1.557 -34.321 -32.237  1.00 60.06      A    N  
ANISOU 1588  N   SER A 673     9066   4942   8811   -934    529  -2383  A    N  
ATOM   1589  CA  SER A 673      -0.411 -35.213 -32.400  1.00 60.05      A    C  
ANISOU 1589  CA  SER A 673     9262   4683   8870   -690    544  -2398  A    C  
ATOM   1590  C   SER A 673       0.871 -34.686 -31.744  1.00 58.24      A    C  
ANISOU 1590  C   SER A 673     8999   4493   8637   -383    478  -2177  A    C  
ATOM   1591  O   SER A 673       1.840 -35.432 -31.573  1.00 56.31      A    O  
ANISOU 1591  O   SER A 673     8911   4002   8482   -148    461  -2167  A    O  
ATOM   1592  CB  SER A 673      -0.165 -35.523 -33.877  1.00 57.10      A    C  
ANISOU 1592  CB  SER A 673     8846   4391   8460   -617    543  -2673  A    C  
ATOM   1593  OG  SER A 673       0.193 -34.359 -34.594  1.00 54.99      A    O  
ANISOU 1593  OG  SER A 673     8348   4498   8047   -501    497  -2679  A    O  
ATOM   1594  N   LEU A 674       0.878 -33.410 -31.376  1.00 51.81      A    N  
ANISOU 1594  N   LEU A 674     7970   3977   7737   -373    426  -2024  A    N  
ATOM   1595  CA  LEU A 674       2.072 -32.798 -30.800  1.00 52.02      A    C  
ANISOU 1595  CA  LEU A 674     7910   4075   7779   -104    349  -1856  A    C  
ATOM   1596  C   LEU A 674       1.784 -32.096 -29.477  1.00 50.51      A    C  
ANISOU 1596  C   LEU A 674     7731   3919   7540   -162    293  -1605  A    C  
ATOM   1597  O   LEU A 674       0.782 -31.393 -29.333  1.00 48.62      A    O  
ANISOU 1597  O   LEU A 674     7395   3860   7220   -384    323  -1567  A    O  
ATOM   1598  CB  LEU A 674       2.706 -31.815 -31.791  1.00 49.14      A    C  
ANISOU 1598  CB  LEU A 674     7271   4048   7354     11    362  -1942  A    C  
ATOM   1599  CG  LEU A 674       4.019 -31.152 -31.373  1.00 48.42      A    C  
ANISOU 1599  CG  LEU A 674     7016   4051   7330    265    313  -1842  A    C  
ATOM   1600  CD1 LEU A 674       5.164 -32.157 -31.390  1.00 51.08      A    C  
ANISOU 1600  CD1 LEU A 674     7425   4140   7845    536    293  -1940  A    C  
ATOM   1601  CD2 LEU A 674       4.331 -29.950 -32.253  1.00 46.81      A    C  
ANISOU 1601  CD2 LEU A 674     6566   4189   7029    268    389  -1898  A    C  
ATOM   1602  N   SER A 675       2.678 -32.297 -28.516  1.00 50.73      A    N  
ANISOU 1602  N   SER A 675     7886   3770   7618     60    194  -1455  A    N  
ATOM   1603  CA  SER A 675       2.586 -31.650 -27.217  1.00 48.70      A    C  
ANISOU 1603  CA  SER A 675     7690   3526   7289     54    118  -1220  A    C  
ATOM   1604  C   SER A 675       4.002 -31.338 -26.733  1.00 48.92      A    C  
ANISOU 1604  C   SER A 675     7637   3566   7383    398    -61  -1151  A    C  
ATOM   1605  O   SER A 675       4.965 -31.914 -27.236  1.00 50.62      A    O  
ANISOU 1605  O   SER A 675     7812   3689   7730    634   -109  -1282  A    O  
ATOM   1606  CB  SER A 675       1.845 -32.549 -26.222  1.00 50.74      A    C  
ANISOU 1606  CB  SER A 675     8354   3419   7507    -94    179  -1105  A    C  
ATOM   1607  OG  SER A 675       2.739 -33.400 -25.531  1.00 79.06      A    O  
ANISOU 1607  OG  SER A 675    12252   6660  11127    177     55  -1021  A    O  
ATOM   1608  N   PRO A 676       4.138 -30.402 -25.779  1.00 47.46      A    N  
ANISOU 1608  N   PRO A 676     7400   3505   7127    429   -163   -978  A    N  
ATOM   1609  CA  PRO A 676       5.454 -30.013 -25.256  1.00 50.13      A    C  
ANISOU 1609  CA  PRO A 676     7619   3878   7551    744   -370   -945  A    C  
ATOM   1610  C   PRO A 676       6.251 -31.193 -24.695  1.00 54.80      A    C  
ANISOU 1610  C   PRO A 676     8495   4098   8231   1043   -544   -945  A    C  
ATOM   1611  O   PRO A 676       5.691 -32.064 -24.032  1.00 53.19      A    O  
ANISOU 1611  O   PRO A 676     8720   3562   7928    992   -539   -833  A    O  
ATOM   1612  CB  PRO A 676       5.101 -29.031 -24.133  1.00 48.96      A    C  
ANISOU 1612  CB  PRO A 676     7504   3838   7260    663   -444   -743  A    C  
ATOM   1613  CG  PRO A 676       3.819 -28.434 -24.561  1.00 43.97      A    C  
ANISOU 1613  CG  PRO A 676     6785   3403   6517    325   -243   -734  A    C  
ATOM   1614  CD  PRO A 676       3.067 -29.540 -25.247  1.00 45.36      A    C  
ANISOU 1614  CD  PRO A 676     7121   3396   6716    169    -91   -847  A    C  
ATOM   1615  N   ASP A 677       7.552 -31.210 -24.967  1.00 57.63      A    N  
ANISOU 1615  N   ASP A 677     8619   4498   8781   1356   -687  -1085  A    N  
ATOM   1616  CA  ASP A 677       8.436 -32.285 -24.523  1.00 60.61      A    C  
ANISOU 1616  CA  ASP A 677     9213   4538   9279   1714   -904  -1129  A    C  
ATOM   1617  C   ASP A 677       8.774 -32.131 -23.045  1.00 65.72      A    C  
ANISOU 1617  C   ASP A 677    10106   5036   9830   1918  -1204   -943  A    C  
ATOM   1618  O   ASP A 677       9.603 -31.304 -22.677  1.00 66.84      A    O  
ANISOU 1618  O   ASP A 677     9958   5377  10063   2094  -1398   -977  A    O  
ATOM   1619  CB  ASP A 677       9.726 -32.262 -25.344  1.00 60.70      A    C  
ANISOU 1619  CB  ASP A 677     8809   4683   9572   1984   -946  -1394  A    C  
ATOM   1620  CG  ASP A 677      10.569 -33.511 -25.160  1.00 67.41      A    C  
ANISOU 1620  CG  ASP A 677     9848   5177  10587   2370  -1146  -1504  A    C  
ATOM   1621  OD1 ASP A 677      10.236 -34.363 -24.306  1.00 70.43      A    O  
ANISOU 1621  OD1 ASP A 677    10736   5186  10839   2459  -1288  -1345  A    O  
ATOM   1622  OD2 ASP A 677      11.581 -33.634 -25.879  1.00 69.43      A    O1-
ANISOU 1622  OD2 ASP A 677     9760   5515  11106   2591  -1146  -1759  A    O1-
ATOM   1623  N   LEU A 678       8.145 -32.940 -22.201  1.00 70.07      A    N  
ANISOU 1623  N   LEU A 678    11217   5216  10190   1890  -1235   -759  A    N  
ATOM   1624  CA  LEU A 678       8.348 -32.847 -20.758  1.00 73.35      A    C  
ANISOU 1624  CA  LEU A 678    11991   5445  10433   2073  -1507   -559  A    C  
ATOM   1625  C   LEU A 678       9.702 -33.392 -20.302  1.00 77.80      A    C  
ANISOU 1625  C   LEU A 678    12617   5803  11139   2600  -1914   -648  A    C  
ATOM   1626  O   LEU A 678      10.084 -33.219 -19.147  1.00 79.81      A    O  
ANISOU 1626  O   LEU A 678    13058   6029  11237   2769  -2180   -513  A    O  
ATOM   1627  CB  LEU A 678       7.222 -33.564 -20.013  1.00 75.04      A    C  
ANISOU 1627  CB  LEU A 678    12851   5289  10371   1853  -1352   -336  A    C  
ATOM   1628  CG  LEU A 678       5.819 -32.992 -20.208  1.00 71.25      A    C  
ANISOU 1628  CG  LEU A 678    12315   4996   9761   1348   -986   -260  A    C  
ATOM   1629  CD1 LEU A 678       4.815 -33.767 -19.376  1.00 75.20      A    C  
ANISOU 1629  CD1 LEU A 678    13456   5091  10027   1134   -805    -72  A    C  
ATOM   1630  CD2 LEU A 678       5.792 -31.524 -19.844  1.00 66.30      A    C  
ANISOU 1630  CD2 LEU A 678    11358   4759   9072   1266  -1035   -200  A    C  
ATOM   1631  N   SER A 679      10.425 -34.047 -21.205  1.00 78.05      A    N  
ANISOU 1631  N   SER A 679    12415   5809  11433   2797  -1920   -879  A    N  
ATOM   1632  CA  SER A 679      11.737 -34.590 -20.872  1.00 80.07      A    C  
ANISOU 1632  CA  SER A 679    12550   6058  11814   3191  -2219   -979  A    C  
ATOM   1633  C   SER A 679      12.737 -33.461 -20.641  1.00 83.03      A    C  
ANISOU 1633  C   SER A 679    12400   6786  12363   3363  -2458  -1112  A    C  
ATOM   1634  O   SER A 679      13.791 -33.660 -20.036  1.00 86.41      A    O  
ANISOU 1634  O   SER A 679    12738   7243  12849   3661  -2776  -1180  A    O  
ATOM   1635  CB  SER A 679      12.236 -35.527 -21.979  1.00 77.77      A    C  
ANISOU 1635  CB  SER A 679    12086   5694  11768   3313  -2098  -1210  A    C  
ATOM   1636  OG  SER A 679      12.639 -34.811 -23.135  1.00 74.03      A    O  
ANISOU 1636  OG  SER A 679    11019   5529  11579   3273  -1941  -1477  A    O  
ATOM   1637  N   LYS A 680      12.387 -32.271 -21.117  1.00 81.82      A    N  
ANISOU 1637  N   LYS A 680    11902   6894  12294   3155  -2303  -1165  A    N  
ATOM   1638  CA  LYS A 680      13.284 -31.126 -21.069  1.00 84.92      A    C  
ANISOU 1638  CA  LYS A 680    11736   7639  12891   3245  -2444  -1323  A    C  
ATOM   1639  C   LYS A 680      13.203 -30.315 -19.775  1.00 82.79      A    C  
ANISOU 1639  C   LYS A 680    11616   7434  12406   3245  -2697  -1138  A    C  
ATOM   1640  O   LYS A 680      13.953 -29.354 -19.603  1.00 81.52      A    O  
ANISOU 1640  O   LYS A 680    11018   7554  12401   3299  -2837  -1270  A    O  
ATOM   1641  CB  LYS A 680      13.034 -30.216 -22.273  1.00 86.31      A    C  
ANISOU 1641  CB  LYS A 680    11427   8177  13188   2913  -2054  -1447  A    C  
ATOM   1642  CG  LYS A 680      13.474 -30.803 -23.605  1.00 90.83      A    C  
ANISOU 1642  CG  LYS A 680    11726   8773  14013   2952  -1821  -1709  A    C  
ATOM   1643  CD  LYS A 680      12.895 -29.990 -24.752  1.00 90.84      A    C  
ANISOU 1643  CD  LYS A 680    11456   9093  13967   2548  -1390  -1742  A    C  
ATOM   1644  CE  LYS A 680      13.742 -30.094 -26.007  1.00 94.08      A    C  
ANISOU 1644  CE  LYS A 680    11443   9633  14670   2616  -1171  -2063  A    C  
ATOM   1645  NZ  LYS A 680      15.072 -29.446 -25.813  1.00 97.23      A    N1+
ANISOU 1645  NZ  LYS A 680    11335  10205  15401   2836  -1315  -2294  A    N1+
ATOM   1646  N   VAL A 681      12.301 -30.690 -18.871  1.00 82.65      A    N  
ANISOU 1646  N   VAL A 681    12216   7162  12023   3151  -2720   -849  A    N  
ATOM   1647  CA  VAL A 681      12.238 -30.016 -17.578  1.00 83.53      A    C  
ANISOU 1647  CA  VAL A 681    12537   7320  11881   3156  -2945   -678  A    C  
ATOM   1648  C   VAL A 681      13.524 -30.289 -16.817  1.00 91.34      A    C  
ANISOU 1648  C   VAL A 681    13449   8340  12914   3497  -3352   -802  A    C  
ATOM   1649  O   VAL A 681      14.084 -31.383 -16.896  1.00 96.01      A    O  
ANISOU 1649  O   VAL A 681    14154   8762  13565   3718  -3464   -880  A    O  
ATOM   1650  CB  VAL A 681      11.028 -30.453 -16.719  1.00 82.76      A    C  
ANISOU 1650  CB  VAL A 681    13152   6938  11356   2957  -2818   -358  A    C  
ATOM   1651  CG1 VAL A 681       9.723 -30.071 -17.393  1.00 77.37      A    C  
ANISOU 1651  CG1 VAL A 681    12484   6295  10618   2538  -2393   -265  A    C  
ATOM   1652  CG2 VAL A 681      11.075 -31.946 -16.434  1.00 89.47      A    C  
ANISOU 1652  CG2 VAL A 681    14473   7452  12071   3087  -2845   -291  A    C  
ATOM   1653  N   ARG A 682      13.997 -29.283 -16.091  1.00 93.12      A    N  
ANISOU 1653  N   ARG A 682    13483   8778  13120   3535  -3583   -842  A    N  
ATOM   1654  CA  ARG A 682      15.231 -29.410 -15.332  1.00 99.36      A    C  
ANISOU 1654  CA  ARG A 682    14177   9610  13966   3836  -3998  -1011  A    C  
ATOM   1655  C   ARG A 682      15.062 -30.373 -14.163  1.00100.99      A    C  
ANISOU 1655  C   ARG A 682    15094   9495  13784   3997  -4216   -824  A    C  
ATOM   1656  O   ARG A 682      13.945 -30.626 -13.709  1.00 99.46      A    O  
ANISOU 1656  O   ARG A 682    15456   9098  13238   3813  -4029   -541  A    O  
ATOM   1657  CB  ARG A 682      15.707 -28.037 -14.857  1.00103.15      A    C  
ANISOU 1657  CB  ARG A 682    14288  10383  14521   3787  -4160  -1125  A    C  
ATOM   1658  CG  ARG A 682      16.102 -27.112 -16.000  1.00104.94      A    C  
ANISOU 1658  CG  ARG A 682    13780  10931  15161   3643  -3944  -1358  A    C  
ATOM   1659  CD  ARG A 682      16.616 -25.769 -15.508  1.00108.92      A    C  
ANISOU 1659  CD  ARG A 682    13931  11702  15751   3568  -4083  -1484  A    C  
ATOM   1660  NE  ARG A 682      16.908 -24.868 -16.621  1.00110.40      A    N  
ANISOU 1660  NE  ARG A 682    13465  12179  16303   3374  -3798  -1688  A    N  
ATOM   1661  CZ  ARG A 682      17.323 -23.613 -16.479  1.00112.15      A    C  
ANISOU 1661  CZ  ARG A 682    13305  12648  16661   3234  -3802  -1820  A    C  
ATOM   1662  NH1 ARG A 682      17.496 -23.105 -15.266  1.00113.97      A    N1+
ANISOU 1662  NH1 ARG A 682    13725  12873  16705   3286  -4103  -1784  A    N1+
ATOM   1663  NH2 ARG A 682      17.563 -22.866 -17.549  1.00110.59      A    N  
ANISOU 1663  NH2 ARG A 682    12567  12684  16768   3026  -3477  -1996  A    N  
ATOM   1664  N   SER A 683      16.180 -30.915 -13.692  1.00104.38      A    N  
ANISOU 1664  N   SER A 683    15504   9872  14284   4331  -4593  -1004  A    N  
ATOM   1665  CA  SER A 683      16.178 -31.902 -12.619  1.00107.24      A    C  
ANISOU 1665  CA  SER A 683    16544   9914  14287   4538  -4837   -869  A    C  
ATOM   1666  C   SER A 683      15.664 -31.335 -11.299  1.00105.00      A    C  
ANISOU 1666  C   SER A 683    16736   9581  13579   4453  -4943   -680  A    C  
ATOM   1667  O   SER A 683      14.935 -32.006 -10.568  1.00105.78      A    O  
ANISOU 1667  O   SER A 683    17530   9392  13271   4412  -4872   -439  A    O  
ATOM   1668  CB  SER A 683      17.585 -32.464 -12.423  1.00113.94      A    C  
ANISOU 1668  CB  SER A 683    17206  10747  15341   4943  -5268  -1155  A    C  
ATOM   1669  OG  SER A 683      18.499 -31.429 -12.105  1.00115.38      A    O  
ANISOU 1669  OG  SER A 683    16906  11207  15728   5021  -5543  -1410  A    O  
ATOM   1670  N   ASN A 684      16.046 -30.097 -11.001  1.00102.03      A    N  
ANISOU 1670  N   ASN A 684    15989   9478  13299   4408  -5081   -806  A    N  
ATOM   1671  CA  ASN A 684      15.654 -29.445  -9.754  1.00102.42      A    C  
ANISOU 1671  CA  ASN A 684    16439   9503  12972   4337  -5190   -672  A    C  
ATOM   1672  C   ASN A 684      14.164 -29.143  -9.663  1.00 96.69      A    C  
ANISOU 1672  C   ASN A 684    16083   8714  11940   3968  -4764   -351  A    C  
ATOM   1673  O   ASN A 684      13.656 -28.808  -8.592  1.00 97.10      A    O  
ANISOU 1673  O   ASN A 684    16591   8686  11618   3885  -4774   -203  A    O  
ATOM   1674  CB  ASN A 684      16.460 -28.161  -9.550  1.00103.90      A    C  
ANISOU 1674  CB  ASN A 684    16090   9998  13389   4362  -5418   -915  A    C  
ATOM   1675  CG  ASN A 684      16.829 -27.496 -10.859  1.00101.72      A    C  
ANISOU 1675  CG  ASN A 684    15013  10026  13609   4235  -5230  -1112  A    C  
ATOM   1676  ND2 ASN A 684      17.011 -26.181 -10.828  1.00100.29      A    N  
ANISOU 1676  ND2 ASN A 684    14422  10113  13571   4085  -5222  -1221  A    N  
ATOM   1677  OD1 ASN A 684      16.957 -28.160 -11.888  1.00101.27      A    O  
ANISOU 1677  OD1 ASN A 684    14726   9953  13798   4264  -5073  -1176  A    O  
ATOM   1678  N   CYS A 685      13.468 -29.253 -10.789  1.00 91.83      A    N  
ANISOU 1678  N   CYS A 685    15268   8128  11493   3743  -4382   -270  A    N  
ATOM   1679  CA  CYS A 685      12.033 -29.007 -10.817  1.00 89.02      A    C  
ANISOU 1679  CA  CYS A 685    15217   7707  10898   3377  -3960     -2  A    C  
ATOM   1680  C   CYS A 685      11.300 -30.046  -9.977  1.00 91.19      A    C  
ANISOU 1680  C   CYS A 685    16279   7626  10745   3329  -3833    224  A    C  
ATOM   1681  O   CYS A 685      11.429 -31.244 -10.225  1.00 91.98      A    O  
ANISOU 1681  O   CYS A 685    16604   7491  10854   3451  -3826    230  A    O  
ATOM   1682  CB  CYS A 685      11.504 -29.013 -12.255  1.00 85.96      A    C  
ANISOU 1682  CB  CYS A 685    14465   7390  10805   3174  -3608    -11  A    C  
ATOM   1683  SG  CYS A 685       9.699 -29.038 -12.379  1.00 88.95      A    S  
ANISOU 1683  SG  CYS A 685    15260   7615  10921   2717  -3070    278  A    S  
ATOM   1684  N   PRO A 686      10.541 -29.584  -8.965  1.00 92.28      A    N  
ANISOU 1684  N   PRO A 686    16838   7716  10508   3145  -3712    393  A    N  
ATOM   1685  CA  PRO A 686       9.733 -30.463  -8.113  1.00 95.40      A    C  
ANISOU 1685  CA  PRO A 686    17989   7781  10478   3037  -3507    596  A    C  
ATOM   1686  C   PRO A 686       8.801 -31.319  -8.954  1.00 95.74      A    C  
ANISOU 1686  C   PRO A 686    18146   7650  10582   2782  -3067    712  A    C  
ATOM   1687  O   PRO A 686       8.250 -30.832  -9.939  1.00 92.21      A    O  
ANISOU 1687  O   PRO A 686    17302   7358  10375   2538  -2796    709  A    O  
ATOM   1688  CB  PRO A 686       8.910 -29.480  -7.280  1.00 92.24      A    C  
ANISOU 1688  CB  PRO A 686    17787   7466   9794   2779  -3314    716  A    C  
ATOM   1689  CG  PRO A 686       9.755 -28.273  -7.201  1.00 90.83      A    C  
ANISOU 1689  CG  PRO A 686    17120   7592   9800   2928  -3652    549  A    C  
ATOM   1690  CD  PRO A 686      10.447 -28.177  -8.540  1.00 88.87      A    C  
ANISOU 1690  CD  PRO A 686    16186   7541  10041   3029  -3751    377  A    C  
ATOM   1691  N   LYS A 687       8.630 -32.576  -8.565  1.00101.64      A    N  
ANISOU 1691  N   LYS A 687    19444   8063  11113   2833  -3002    797  A    N  
ATOM   1692  CA  LYS A 687       7.848 -33.520  -9.353  1.00102.78      A    C  
ANISOU 1692  CA  LYS A 687    19699   8010  11341   2604  -2608    869  A    C  
ATOM   1693  C   LYS A 687       6.353 -33.215  -9.320  1.00100.29      A    C  
ANISOU 1693  C   LYS A 687    19532   7685  10890   2112  -2066   1012  A    C  
ATOM   1694  O   LYS A 687       5.622 -33.598 -10.234  1.00 98.23      A    O  
ANISOU 1694  O   LYS A 687    19135   7374  10813   1844  -1714   1013  A    O  
ATOM   1695  CB  LYS A 687       8.111 -34.950  -8.880  1.00109.82      A    C  
ANISOU 1695  CB  LYS A 687    21166   8531  12029   2799  -2696    913  A    C  
ATOM   1696  CG  LYS A 687       9.588 -35.330  -8.896  1.00114.59      A    C  
ANISOU 1696  CG  LYS A 687    21623   9135  12781   3299  -3240    743  A    C  
ATOM   1697  CD  LYS A 687       9.786 -36.813  -8.596  1.00121.76      A    C  
ANISOU 1697  CD  LYS A 687    23097   9652  13513   3488  -3302    788  A    C  
ATOM   1698  CE  LYS A 687      11.236 -37.122  -8.265  1.00126.89      A    C  
ANISOU 1698  CE  LYS A 687    23705  10287  14220   4011  -3893    615  A    C  
ATOM   1699  NZ  LYS A 687      11.412 -38.544  -7.874  1.00133.47      A    N1+
ANISOU 1699  NZ  LYS A 687    25163  10716  14834   4218  -3976    671  A    N1+
ATOM   1700  N   ARG A 688       5.900 -32.532  -8.272  1.00100.68      A    N  
ANISOU 1700  N   ARG A 688    19841   7781  10633   1990  -1994   1098  A    N  
ATOM   1701  CA  ARG A 688       4.489 -32.172  -8.158  1.00 99.08      A    C  
ANISOU 1701  CA  ARG A 688    19733   7597  10317   1527  -1471   1196  A    C  
ATOM   1702  C   ARG A 688       4.097 -31.136  -9.206  1.00 91.99      A    C  
ANISOU 1702  C   ARG A 688    18201   7007   9746   1309  -1321   1137  A    C  
ATOM   1703  O   ARG A 688       2.954 -31.105  -9.669  1.00 88.86      A    O  
ANISOU 1703  O   ARG A 688    17721   6622   9420    920   -875   1157  A    O  
ATOM   1704  CB  ARG A 688       4.174 -31.650  -6.755  1.00103.39      A    C  
ANISOU 1704  CB  ARG A 688    20700   8121  10462   1482  -1438   1271  A    C  
ATOM   1705  CG  ARG A 688       4.252 -32.703  -5.660  1.00112.37      A    C  
ANISOU 1705  CG  ARG A 688    22591   8898  11205   1612  -1465   1340  A    C  
ATOM   1706  CD  ARG A 688       3.879 -32.125  -4.300  1.00117.06      A    C  
ANISOU 1706  CD  ARG A 688    23616   9459  11404   1550  -1393   1387  A    C  
ATOM   1707  NE  ARG A 688       3.953 -33.122  -3.233  1.00127.22      A    N  
ANISOU 1707  NE  ARG A 688    25692  10367  12277   1683  -1414   1444  A    N  
ATOM   1708  CZ  ARG A 688       3.739 -32.858  -1.947  1.00131.48      A    C  
ANISOU 1708  CZ  ARG A 688    26757  10782  12415   1688  -1380   1472  A    C  
ATOM   1709  NH1 ARG A 688       3.441 -31.624  -1.564  1.00127.96      A    N1+
ANISOU 1709  NH1 ARG A 688    26101  10571  11948   1565  -1324   1447  A    N1+
ATOM   1710  NH2 ARG A 688       3.826 -33.825  -1.043  1.00138.24      A    N  
ANISOU 1710  NH2 ARG A 688    28379  11261  12886   1823  -1398   1519  A    N  
ATOM   1711  N   MET A 689       5.057 -30.294  -9.569  1.00 89.29      A    N  
ANISOU 1711  N   MET A 689    17406   6910   9609   1563  -1701   1038  A    N  
ATOM   1712  CA  MET A 689       4.852 -29.268 -10.577  1.00 84.24      A    C  
ANISOU 1712  CA  MET A 689    16190   6548   9268   1414  -1618    971  A    C  
ATOM   1713  C   MET A 689       4.856 -29.888 -11.971  1.00 81.71      A    C  
ANISOU 1713  C   MET A 689    15579   6179   9288   1378  -1511    870  A    C  
ATOM   1714  O   MET A 689       4.149 -29.423 -12.865  1.00 76.71      A    O  
ANISOU 1714  O   MET A 689    14649   5658   8839   1106  -1246    830  A    O  
ATOM   1715  CB  MET A 689       5.944 -28.201 -10.462  1.00 85.08      A    C  
ANISOU 1715  CB  MET A 689    15919   6920   9488   1703  -2056    870  A    C  
ATOM   1716  CG  MET A 689       5.689 -26.931 -11.266  1.00 81.04      A    C  
ANISOU 1716  CG  MET A 689    14887   6697   9207   1544  -1974    822  A    C  
ATOM   1717  SD  MET A 689       4.413 -25.870 -10.560  1.00 97.97      A    S  
ANISOU 1717  SD  MET A 689    17179   8956  11088   1161  -1626    961  A    S  
ATOM   1718  CE  MET A 689       5.398 -24.478 -10.010  1.00103.95      A    C  
ANISOU 1718  CE  MET A 689    17641  10003  11852   1401  -2054    886  A    C  
ATOM   1719  N   LYS A 690       5.659 -30.933 -12.154  1.00 86.13      A    N  
ANISOU 1719  N   LYS A 690    16234   6566   9925   1659  -1724    807  A    N  
ATOM   1720  CA  LYS A 690       5.695 -31.655 -13.424  1.00 86.99      A    C  
ANISOU 1720  CA  LYS A 690    16119   6595  10337   1643  -1616    689  A    C  
ATOM   1721  C   LYS A 690       4.340 -32.283 -13.718  1.00 83.97      A    C  
ANISOU 1721  C   LYS A 690    15965   6039   9902   1214  -1118    749  A    C  
ATOM   1722  O   LYS A 690       3.855 -32.237 -14.849  1.00 81.33      A    O  
ANISOU 1722  O   LYS A 690    15331   5761   9811   1004   -901    638  A    O  
ATOM   1723  CB  LYS A 690       6.781 -32.731 -13.416  1.00 93.99      A    C  
ANISOU 1723  CB  LYS A 690    17117   7309  11286   2028  -1922    612  A    C  
ATOM   1724  CG  LYS A 690       8.185 -32.183 -13.266  1.00 98.45      A    C  
ANISOU 1724  CG  LYS A 690    17336   8078  11993   2440  -2410    472  A    C  
ATOM   1725  CD  LYS A 690       9.231 -33.282 -13.344  1.00105.46      A    C  
ANISOU 1725  CD  LYS A 690    18284   8804  12981   2810  -2692    359  A    C  
ATOM   1726  CE  LYS A 690      10.616 -32.745 -13.011  1.00108.07      A    C  
ANISOU 1726  CE  LYS A 690    18268   9347  13444   3192  -3178    184  A    C  
ATOM   1727  NZ  LYS A 690      11.655 -33.810 -13.073  1.00112.75      A    N1+
ANISOU 1727  NZ  LYS A 690    18897   9791  14152   3561  -3464     48  A    N1+
ATOM   1728  N   ARG A 691       3.731 -32.864 -12.689  1.00 83.74      A    N  
ANISOU 1728  N   ARG A 691    16454   5807   9555   1077   -935    891  A    N  
ATOM   1729  CA  ARG A 691       2.393 -33.425 -12.814  1.00 82.69      A    C  
ANISOU 1729  CA  ARG A 691    16504   5536   9379    639   -436    919  A    C  
ATOM   1730  C   ARG A 691       1.371 -32.338 -13.110  1.00 76.09      A    C  
ANISOU 1730  C   ARG A 691    15342   4951   8619    263   -136    890  A    C  
ATOM   1731  O   ARG A 691       0.541 -32.488 -14.002  1.00 74.57      A    O  
ANISOU 1731  O   ARG A 691    14913   4789   8630    -51    168    780  A    O  
ATOM   1732  CB  ARG A 691       2.002 -34.177 -11.541  1.00 88.36      A    C  
ANISOU 1732  CB  ARG A 691    17857   5994   9722    586   -293   1058  A    C  
ATOM   1733  CG  ARG A 691       2.678 -35.524 -11.396  1.00 95.50      A    C  
ANISOU 1733  CG  ARG A 691    19149   6580  10555    854   -468   1076  A    C  
ATOM   1734  CD  ARG A 691       2.398 -36.137 -10.039  1.00102.19      A    C  
ANISOU 1734  CD  ARG A 691    20689   7164  10975    845   -369   1212  A    C  
ATOM   1735  NE  ARG A 691       3.634 -36.477  -9.341  1.00107.48      A    N  
ANISOU 1735  NE  ARG A 691    21667   7711  11458   1324   -854   1244  A    N  
ATOM   1736  CZ  ARG A 691       3.880 -36.186  -8.068  1.00111.45      A    C  
ANISOU 1736  CZ  ARG A 691    22579   8172  11594   1474  -1022   1321  A    C  
ATOM   1737  NH1 ARG A 691       2.974 -35.546  -7.342  1.00110.32      A    N1+
ANISOU 1737  NH1 ARG A 691    22596   8092  11228   1182   -714   1384  A    N1+
ATOM   1738  NH2 ARG A 691       5.035 -36.536  -7.519  1.00115.78      A    N  
ANISOU 1738  NH2 ARG A 691    23373   8612  12005   1923  -1501   1307  A    N  
ATOM   1739  N   LEU A 692       1.442 -31.244 -12.357  1.00 72.46      A    N  
ANISOU 1739  N   LEU A 692    14858   4676   7998    303   -240    965  A    N  
ATOM   1740  CA  LEU A 692       0.507 -30.136 -12.519  1.00 68.77      A    C  
ANISOU 1740  CA  LEU A 692    14096   4454   7580    -24     24    942  A    C  
ATOM   1741  C   LEU A 692       0.625 -29.513 -13.901  1.00 63.12      A    C  
ANISOU 1741  C   LEU A 692    12843   3934   7203    -64    -26    799  A    C  
ATOM   1742  O   LEU A 692      -0.376 -29.157 -14.519  1.00 59.55      A    O  
ANISOU 1742  O   LEU A 692    12086   3650   6890   -414    285    697  A    O  
ATOM   1743  CB  LEU A 692       0.737 -29.070 -11.449  1.00 69.30      A    C  
ANISOU 1743  CB  LEU A 692    14248   4673   7409     84   -133   1039  A    C  
ATOM   1744  CG  LEU A 692      -0.179 -27.851 -11.538  1.00 65.29      A    C  
ANISOU 1744  CG  LEU A 692    13440   4426   6942   -222    121   1018  A    C  
ATOM   1745  CD1 LEU A 692      -1.633 -28.260 -11.375  1.00 65.31      A    C  
ANISOU 1745  CD1 LEU A 692    13525   4375   6914   -649    646    978  A    C  
ATOM   1746  CD2 LEU A 692       0.208 -26.819 -10.497  1.00 66.66      A    C  
ANISOU 1746  CD2 LEU A 692    13705   4738   6884    -67    -85   1100  A    C  
ATOM   1747  N   MET A 693       1.858 -29.387 -14.374  1.00 62.66      A    N  
ANISOU 1747  N   MET A 693    12559   3960   7289    304   -422    736  A    N  
ATOM   1748  CA  MET A 693       2.120 -28.875 -15.710  1.00 60.47      A    C  
ANISOU 1748  CA  MET A 693    11576   4079   7322    297   -462    532  A    C  
ATOM   1749  C   MET A 693       1.478 -29.771 -16.764  1.00 61.34      A    C  
ANISOU 1749  C   MET A 693    11595   4101   7609     74   -197    396  A    C  
ATOM   1750  O   MET A 693       0.883 -29.289 -17.724  1.00 59.30      A    O  
ANISOU 1750  O   MET A 693    10872   4147   7510   -150    -30    251  A    O  
ATOM   1751  CB  MET A 693       3.624 -28.796 -15.942  1.00 60.20      A    C  
ANISOU 1751  CB  MET A 693    11328   4123   7424    731   -886    456  A    C  
ATOM   1752  CG  MET A 693       4.020 -28.282 -17.304  1.00 55.03      A    C  
ANISOU 1752  CG  MET A 693    10004   3842   7064    733   -893    245  A    C  
ATOM   1753  SD  MET A 693       5.761 -28.599 -17.624  1.00 78.42      A    S  
ANISOU 1753  SD  MET A 693    12760   6789  10248   1220  -1302    102  A    S  
ATOM   1754  CE  MET A 693       6.519 -27.854 -16.185  1.00 70.02      A    C  
ANISOU 1754  CE  MET A 693    11870   5720   9015   1495  -1684    218  A    C  
ATOM   1755  N   ALA A 694       1.601 -31.079 -16.571  1.00 62.69      A    N  
ANISOU 1755  N   ALA A 694    12247   3836   7737    150   -180    438  A    N  
ATOM   1756  CA  ALA A 694       1.030 -32.048 -17.498  1.00 64.55      A    C  
ANISOU 1756  CA  ALA A 694    12463   3928   8136    -59     61    298  A    C  
ATOM   1757  C   ALA A 694      -0.495 -32.037 -17.451  1.00 67.59      A    C  
ANISOU 1757  C   ALA A 694    12876   4306   8501   -552    495    271  A    C  
ATOM   1758  O   ALA A 694      -1.155 -32.283 -18.458  1.00 66.02      A    O  
ANISOU 1758  O   ALA A 694    12373   4214   8495   -793    682     78  A    O  
ATOM   1759  CB  ALA A 694       1.560 -33.444 -17.204  1.00 64.87      A    C  
ANISOU 1759  CB  ALA A 694    12980   3545   8124    154    -29    351  A    C  
ATOM   1760  N   GLU A 695      -1.050 -31.765 -16.275  1.00 71.57      A    N  
ANISOU 1760  N   GLU A 695    13664   4756   8775   -685    643    430  A    N  
ATOM   1761  CA  GLU A 695      -2.498 -31.700 -16.121  1.00 74.89      A    C  
ANISOU 1761  CA  GLU A 695    13993   5262   9200  -1129   1062    367  A    C  
ATOM   1762  C   GLU A 695      -3.057 -30.466 -16.823  1.00 70.70      A    C  
ANISOU 1762  C   GLU A 695    12928   5097   8839  -1325   1127    226  A    C  
ATOM   1763  O   GLU A 695      -4.154 -30.499 -17.381  1.00 71.62      A    O  
ANISOU 1763  O   GLU A 695    12765   5327   9121  -1664   1400     44  A    O  
ATOM   1764  CB  GLU A 695      -2.884 -31.689 -14.641  1.00 80.36      A    C  
ANISOU 1764  CB  GLU A 695    15082   5868   9584  -1178   1208    542  A    C  
ATOM   1765  CG  GLU A 695      -2.509 -32.960 -13.903  1.00 88.42      A    C  
ANISOU 1765  CG  GLU A 695    16659   6538  10397  -1027   1187    659  A    C  
ATOM   1766  CD  GLU A 695      -3.250 -34.172 -14.426  1.00 96.81      A    C  
ANISOU 1766  CD  GLU A 695    17772   7415  11596  -1285   1483    536  A    C  
ATOM   1767  OE1 GLU A 695      -2.595 -35.194 -14.728  1.00 99.71      A    O  
ANISOU 1767  OE1 GLU A 695    18353   7543  11992  -1093   1336    545  A    O  
ATOM   1768  OE2 GLU A 695      -4.492 -34.103 -14.529  1.00 99.36      A    O1-
ANISOU 1768  OE2 GLU A 695    17901   7838  12012  -1671   1855    410  A    O1-
ATOM   1769  N   CYS A 696      -2.290 -29.382 -16.800  1.00 65.37      A    N  
ANISOU 1769  N   CYS A 696    11971   4743   8125  -1060    828    278  A    N  
ATOM   1770  CA  CYS A 696      -2.696 -28.143 -17.450  1.00 61.23      A    C  
ANISOU 1770  CA  CYS A 696    10846   4696   7721  -1149    819    153  A    C  
ATOM   1771  C   CYS A 696      -2.598 -28.255 -18.965  1.00 56.78      A    C  
ANISOU 1771  C   CYS A 696     9829   4350   7394  -1132    742    -61  A    C  
ATOM   1772  O   CYS A 696      -3.352 -27.610 -19.689  1.00 53.07      A    O  
ANISOU 1772  O   CYS A 696     8943   4181   7038  -1303    825   -216  A    O  
ATOM   1773  CB  CYS A 696      -1.835 -26.975 -16.966  1.00 60.02      A    C  
ANISOU 1773  CB  CYS A 696    10575   4776   7455   -881    538    270  A    C  
ATOM   1774  SG  CYS A 696      -2.036 -26.566 -15.217  1.00 67.29      A    S  
ANISOU 1774  SG  CYS A 696    11993   5517   8058   -902    609    496  A    S  
ATOM   1775  N   LEU A 697      -1.673 -29.086 -19.434  1.00 58.11      A    N  
ANISOU 1775  N   LEU A 697    10107   4351   7621   -907    575    -82  A    N  
ATOM   1776  CA  LEU A 697      -1.394 -29.193 -20.861  1.00 56.12      A    C  
ANISOU 1776  CA  LEU A 697     9478   4290   7554   -847    492   -281  A    C  
ATOM   1777  C   LEU A 697      -2.217 -30.267 -21.547  1.00 56.73      A    C  
ANISOU 1777  C   LEU A 697     9610   4187   7757  -1094    703   -455  A    C  
ATOM   1778  O   LEU A 697      -1.929 -30.640 -22.686  1.00 56.37      A    O  
ANISOU 1778  O   LEU A 697     9374   4208   7838  -1027    636   -623  A    O  
ATOM   1779  CB  LEU A 697       0.092 -29.455 -21.093  1.00 55.89      A    C  
ANISOU 1779  CB  LEU A 697     9467   4208   7560   -462    214   -260  A    C  
ATOM   1780  CG  LEU A 697       1.010 -28.272 -20.797  1.00 53.46      A    C  
ANISOU 1780  CG  LEU A 697     8932   4167   7214   -224    -18   -183  A    C  
ATOM   1781  CD1 LEU A 697       2.460 -28.685 -20.959  1.00 55.02      A    C  
ANISOU 1781  CD1 LEU A 697     9130   4274   7503    146   -275   -212  A    C  
ATOM   1782  CD2 LEU A 697       0.672 -27.100 -21.702  1.00 48.72      A    C  
ANISOU 1782  CD2 LEU A 697     7846   3989   6674   -334     24   -294  A    C  
ATOM   1783  N   LYS A 698      -3.238 -30.758 -20.852  1.00 60.61      A    N  
ANISOU 1783  N   LYS A 698    10371   4442   8216  -1395    977   -433  A    N  
ATOM   1784  CA  LYS A 698      -4.111 -31.791 -21.396  1.00 62.38      A    C  
ANISOU 1784  CA  LYS A 698    10649   4465   8587  -1687   1211   -626  A    C  
ATOM   1785  C   LYS A 698      -4.744 -31.317 -22.692  1.00 61.44      A    C  
ANISOU 1785  C   LYS A 698     9988   4716   8639  -1813   1187   -898  A    C  
ATOM   1786  O   LYS A 698      -5.297 -30.218 -22.760  1.00 57.80      A    O  
ANISOU 1786  O   LYS A 698     9183   4595   8182  -1886   1178   -939  A    O  
ATOM   1787  CB  LYS A 698      -5.203 -32.156 -20.394  1.00 63.07      A    C  
ANISOU 1787  CB  LYS A 698    11027   4306   8631  -2037   1563   -582  A    C  
ATOM   1788  CG  LYS A 698      -5.126 -33.576 -19.889  1.00 68.03      A    C  
ANISOU 1788  CG  LYS A 698    12102   4565   9182  -2021   1668   -490  A    C  
ATOM   1789  CD  LYS A 698      -3.868 -33.804 -19.080  1.00 69.41      A    C  
ANISOU 1789  CD  LYS A 698    12742   4487   9142  -1650   1444   -226  A    C  
ATOM   1790  CE  LYS A 698      -3.818 -35.222 -18.540  1.00 73.46      A    C  
ANISOU 1790  CE  LYS A 698    13725   4633   9553  -1625   1541   -136  A    C  
ATOM   1791  NZ  LYS A 698      -4.937 -35.504 -17.593  1.00 76.42      A    N1+
ANISOU 1791  NZ  LYS A 698    14292   4941   9802  -1931   1900    -89  A    N1+
ATOM   1792  N   LYS A 699      -4.654 -32.156 -23.717  1.00 63.67      A    N  
ANISOU 1792  N   LYS A 699    10231   4915   9047  -1816   1159  -1088  A    N  
ATOM   1793  CA  LYS A 699      -5.167 -31.822 -25.038  1.00 63.40      A    C  
ANISOU 1793  CA  LYS A 699     9756   5198   9135  -1891   1089  -1360  A    C  
ATOM   1794  C   LYS A 699      -6.684 -31.704 -25.009  1.00 62.67      A    C  
ANISOU 1794  C   LYS A 699     9451   5186   9174  -2274   1292  -1560  A    C  
ATOM   1795  O   LYS A 699      -7.266 -30.858 -25.688  1.00 59.92      A    O  
ANISOU 1795  O   LYS A 699     8693   5199   8876  -2306   1191  -1725  A    O  
ATOM   1796  CB  LYS A 699      -4.720 -32.875 -26.055  1.00 65.90      A    C  
ANISOU 1796  CB  LYS A 699    10153   5351   9535  -1813   1031  -1528  A    C  
ATOM   1797  CG  LYS A 699      -3.287 -33.343 -25.833  1.00 68.99      A    C  
ANISOU 1797  CG  LYS A 699    10830   5533   9852  -1463    896  -1355  A    C  
ATOM   1798  CD  LYS A 699      -2.698 -34.034 -27.052  1.00 73.99      A    C  
ANISOU 1798  CD  LYS A 699    11423   6129  10561  -1314    804  -1546  A    C  
ATOM   1799  CE  LYS A 699      -1.343 -34.644 -26.711  1.00 78.28      A    C  
ANISOU 1799  CE  LYS A 699    12252   6409  11082   -969    689  -1408  A    C  
ATOM   1800  NZ  LYS A 699      -0.661 -35.254 -27.890  1.00 79.60      A    N1+
ANISOU 1800  NZ  LYS A 699    12361   6553  11331   -791    619  -1605  A    N1+
ATOM   1801  N   LYS A 700      -7.319 -32.550 -24.207  1.00 65.26      A    N  
ANISOU 1801  N   LYS A 700    10044   5209   9543  -2520   1559  -1533  A    N  
ATOM   1802  CA  LYS A 700      -8.762 -32.497 -24.046  1.00 68.78      A    C  
ANISOU 1802  CA  LYS A 700    10215   5820  10101  -2801   1746  -1683  A    C  
ATOM   1803  C   LYS A 700      -9.119 -31.465 -22.988  1.00 69.10      A    C  
ANISOU 1803  C   LYS A 700    10207   5997  10052  -2846   1855  -1533  A    C  
ATOM   1804  O   LYS A 700      -8.705 -31.566 -21.834  1.00 69.66      A    O  
ANISOU 1804  O   LYS A 700    10668   5847   9952  -2801   1970  -1271  A    O  
ATOM   1805  CB  LYS A 700      -9.323 -33.879 -23.702  1.00 74.75      A    C  
ANISOU 1805  CB  LYS A 700    11214   6280  10907  -2991   1989  -1710  A    C  
ATOM   1806  CG  LYS A 700      -9.108 -34.898 -24.810  1.00 79.14      A    C  
ANISOU 1806  CG  LYS A 700    11782   6717  11570  -2969   1885  -1893  A    C  
ATOM   1807  CD  LYS A 700      -9.726 -36.246 -24.487  1.00 85.99      A    C  
ANISOU 1807  CD  LYS A 700    12879   7290  12501  -3184   2139  -1937  A    C  
ATOM   1808  CE  LYS A 700      -9.551 -37.214 -25.650  1.00 88.91      A    C  
ANISOU 1808  CE  LYS A 700    13239   7557  12984  -3165   2020  -2141  A    C  
ATOM   1809  NZ  LYS A 700     -10.105 -38.564 -25.349  1.00 94.45      A    N1+
ANISOU 1809  NZ  LYS A 700    14189   7945  13754  -3382   2272  -2185  A    N1+
ATOM   1810  N   ARG A 701      -9.887 -30.467 -23.409  1.00 70.92      A    N  
ANISOU 1810  N   ARG A 701     9971   6594  10381  -2904   1792  -1710  A    N  
ATOM   1811  CA  ARG A 701     -10.185 -29.289 -22.599  1.00 71.31      A    C  
ANISOU 1811  CA  ARG A 701     9904   6830  10361  -2908   1847  -1605  A    C  
ATOM   1812  C   ARG A 701     -10.781 -29.603 -21.224  1.00 74.32      A    C  
ANISOU 1812  C   ARG A 701    10539   7034  10665  -3068   2183  -1473  A    C  
ATOM   1813  O   ARG A 701     -10.418 -28.979 -20.229  1.00 74.36      A    O  
ANISOU 1813  O   ARG A 701    10756   7004  10493  -3000   2233  -1248  A    O  
ATOM   1814  CB  ARG A 701     -11.102 -28.347 -23.386  1.00 70.75      A    C  
ANISOU 1814  CB  ARG A 701     9272   7169  10439  -2927   1714  -1870  A    C  
ATOM   1815  CG  ARG A 701     -12.174 -27.675 -22.562  1.00 74.96      A    C  
ANISOU 1815  CG  ARG A 701     9609   7856  11018  -3047   1907  -1907  A    C  
ATOM   1816  CD  ARG A 701     -13.492 -27.636 -23.309  1.00 79.88      A    C  
ANISOU 1816  CD  ARG A 701     9758   8720  11872  -3136   1879  -2257  A    C  
ATOM   1817  NE  ARG A 701     -13.594 -26.487 -24.202  1.00 80.05      A    N  
ANISOU 1817  NE  ARG A 701     9397   9096  11922  -2949   1552  -2390  A    N  
ATOM   1818  CZ  ARG A 701     -14.744 -26.022 -24.678  1.00 83.41      A    C  
ANISOU 1818  CZ  ARG A 701     9401   9779  12513  -2941   1467  -2663  A    C  
ATOM   1819  NH1 ARG A 701     -15.884 -26.608 -24.343  1.00 87.53      A    N1+
ANISOU 1819  NH1 ARG A 701     9787  10249  13220  -3138   1711  -2857  A    N1+
ATOM   1820  NH2 ARG A 701     -14.759 -24.970 -25.483  1.00 82.52      A    N  
ANISOU 1820  NH2 ARG A 701     9019   9960  12374  -2723   1137  -2753  A    N  
ATOM   1821  N   ASP A 702     -11.680 -30.580 -21.165  1.00 77.97      A    N  
ANISOU 1821  N   ASP A 702    11005   7376  11243  -3280   2419  -1623  A    N  
ATOM   1822  CA  ASP A 702     -12.395 -30.862 -19.924  1.00 81.57      A    C  
ANISOU 1822  CA  ASP A 702    11678   7685  11631  -3460   2786  -1561  A    C  
ATOM   1823  C   ASP A 702     -11.599 -31.672 -18.910  1.00 76.99      A    C  
ANISOU 1823  C   ASP A 702    11755   6707  10793  -3404   2911  -1260  A    C  
ATOM   1824  O   ASP A 702     -12.063 -31.909 -17.796  1.00 77.68      A    O  
ANISOU 1824  O   ASP A 702    12121   6643  10753  -3527   3215  -1182  A    O  
ATOM   1825  CB  ASP A 702     -13.740 -31.527 -20.209  1.00 91.10      A    C  
ANISOU 1825  CB  ASP A 702    12616   8921  13076  -3726   3025  -1874  A    C  
ATOM   1826  CG  ASP A 702     -14.850 -30.518 -20.375  1.00 95.91      A    C  
ANISOU 1826  CG  ASP A 702    12684   9888  13868  -3788   3041  -2124  A    C  
ATOM   1827  OD1 ASP A 702     -15.272 -29.942 -19.351  1.00 97.79      A    O  
ANISOU 1827  OD1 ASP A 702    12972  10152  14031  -3841   3260  -2066  A    O  
ATOM   1828  OD2 ASP A 702     -15.291 -30.288 -21.521  1.00 97.48      A    O1-
ANISOU 1828  OD2 ASP A 702    12431  10336  14272  -3757   2816  -2385  A    O1-
ATOM   1829  N   GLU A 703     -10.399 -32.086 -19.290  1.00 71.54      A    N  
ANISOU 1829  N   GLU A 703    11326   5842  10014  -3193   2667  -1108  A    N  
ATOM   1830  CA  GLU A 703      -9.550 -32.838 -18.382  1.00 74.37      A    C  
ANISOU 1830  CA  GLU A 703    12312   5826  10119  -3059   2698   -826  A    C  
ATOM   1831  C   GLU A 703      -8.533 -31.937 -17.696  1.00 71.72      A    C  
ANISOU 1831  C   GLU A 703    12195   5505   9550  -2788   2489   -557  A    C  
ATOM   1832  O   GLU A 703      -7.650 -32.415 -16.986  1.00 73.83      A    O  
ANISOU 1832  O   GLU A 703    12967   5497   9590  -2585   2402   -320  A    O  
ATOM   1833  CB  GLU A 703      -8.854 -33.976 -19.122  1.00 79.29      A    C  
ANISOU 1833  CB  GLU A 703    13127   6204  10796  -2954   2556   -840  A    C  
ATOM   1834  CG  GLU A 703      -9.808 -35.060 -19.580  1.00 86.20      A    C  
ANISOU 1834  CG  GLU A 703    13915   6981  11854  -3226   2789  -1071  A    C  
ATOM   1835  CD  GLU A 703      -9.098 -36.202 -20.267  1.00 92.01      A    C  
ANISOU 1835  CD  GLU A 703    14875   7454  12631  -3111   2652  -1081  A    C  
ATOM   1836  OE1 GLU A 703      -9.788 -37.125 -20.750  1.00 96.16      A    O  
ANISOU 1836  OE1 GLU A 703    15335   7888  13315  -3323   2809  -1279  A    O  
ATOM   1837  OE2 GLU A 703      -7.851 -36.177 -20.324  1.00 91.90      A    O1-
ANISOU 1837  OE2 GLU A 703    15093   7322  12503  -2799   2385   -910  A    O1-
ATOM   1838  N   ARG A 704      -8.668 -30.631 -17.909  1.00 68.02      A    N  
ANISOU 1838  N   ARG A 704    11344   5363   9138  -2770   2386   -606  A    N  
ATOM   1839  CA  ARG A 704      -7.791 -29.652 -17.277  1.00 62.61      A    C  
ANISOU 1839  CA  ARG A 704    10818   4722   8251  -2540   2194   -377  A    C  
ATOM   1840  C   ARG A 704      -8.366 -29.181 -15.950  1.00 62.78      A    C  
ANISOU 1840  C   ARG A 704    11020   4755   8078  -2626   2423   -269  A    C  
ATOM   1841  O   ARG A 704      -9.575 -28.992 -15.825  1.00 64.84      A    O  
ANISOU 1841  O   ARG A 704    11021   5162   8453  -2870   2696   -447  A    O  
ATOM   1842  CB  ARG A 704      -7.573 -28.451 -18.196  1.00 59.62      A    C  
ANISOU 1842  CB  ARG A 704     9967   4673   8013  -2476   1970   -485  A    C  
ATOM   1843  CG  ARG A 704      -6.674 -28.730 -19.380  1.00 58.37      A    C  
ANISOU 1843  CG  ARG A 704     9659   4577   7943  -2244   1662   -547  A    C  
ATOM   1844  CD  ARG A 704      -6.663 -27.559 -20.344  1.00 54.37      A    C  
ANISOU 1844  CD  ARG A 704     8591   4547   7520  -2112   1427   -670  A    C  
ATOM   1845  NE  ARG A 704      -6.467 -28.012 -21.717  1.00 56.90      A    N  
ANISOU 1845  NE  ARG A 704     8683   4955   7983  -2048   1278   -861  A    N  
ATOM   1846  CZ  ARG A 704      -6.978 -27.413 -22.785  1.00 54.82      A    C  
ANISOU 1846  CZ  ARG A 704     7975   5019   7833  -2069   1175  -1075  A    C  
ATOM   1847  NH1 ARG A 704      -7.714 -26.320 -22.645  1.00 53.21      A    N1+
ANISOU 1847  NH1 ARG A 704     7482   5091   7645  -2135   1189  -1127  A    N1+
ATOM   1848  NH2 ARG A 704      -6.753 -27.908 -23.993  1.00 53.05      A    N  
ANISOU 1848  NH2 ARG A 704     7631   4834   7692  -2003   1047  -1242  A    N  
ATOM   1849  N   PRO A 705      -7.494 -28.984 -14.952  1.00 61.53      A    N  
ANISOU 1849  N   PRO A 705    11307   4445   7627  -2400   2295     -4  A    N  
ATOM   1850  CA  PRO A 705      -7.912 -28.525 -13.624  1.00 60.02      A    C  
ANISOU 1850  CA  PRO A 705    11362   4247   7197  -2443   2485     99  A    C  
ATOM   1851  C   PRO A 705      -8.300 -27.050 -13.622  1.00 59.26      A    C  
ANISOU 1851  C   PRO A 705    10866   4491   7161  -2482   2474     40  A    C  
ATOM   1852  O   PRO A 705      -7.879 -26.298 -14.501  1.00 54.94      A    O  
ANISOU 1852  O   PRO A 705     9965   4152   6759  -2396   2235      2  A    O  
ATOM   1853  CB  PRO A 705      -6.657 -28.739 -12.776  1.00 60.76      A    C  
ANISOU 1853  CB  PRO A 705    12011   4106   6969  -2115   2220    373  A    C  
ATOM   1854  CG  PRO A 705      -5.532 -28.629 -13.746  1.00 60.37      A    C  
ANISOU 1854  CG  PRO A 705    11809   4083   7045  -1867   1831    405  A    C  
ATOM   1855  CD  PRO A 705      -6.042 -29.227 -15.025  1.00 59.80      A    C  
ANISOU 1855  CD  PRO A 705    11384   4049   7288  -2057   1933    181  A    C  
ATOM   1856  N   SER A 706      -9.104 -26.647 -12.644  1.00 61.88      A    N  
ANISOU 1856  N   SER A 706    11270   4864   7379  -2611   2743     18  A    N  
ATOM   1857  CA  SER A 706      -9.469 -25.246 -12.492  1.00 60.30      A    C  
ANISOU 1857  CA  SER A 706    10741   4961   7210  -2623   2739    -30  A    C  
ATOM   1858  C   SER A 706      -8.387 -24.509 -11.714  1.00 59.01      A    C  
ANISOU 1858  C   SER A 706    10901   4768   6750  -2353   2475    225  A    C  
ATOM   1859  O   SER A 706      -7.624 -25.119 -10.966  1.00 60.86      A    O  
ANISOU 1859  O   SER A 706    11660   4744   6720  -2180   2365    409  A    O  
ATOM   1860  CB  SER A 706     -10.823 -25.109 -11.791  1.00 66.52      A    C  
ANISOU 1860  CB  SER A 706    11446   5796   8032  -2862   3144   -204  A    C  
ATOM   1861  OG  SER A 706     -10.789 -25.658 -10.483  1.00 73.29      A    O  
ANISOU 1861  OG  SER A 706    12897   6370   8582  -2862   3339    -76  A    O  
ATOM   1862  N   PHE A 707      -8.316 -23.196 -11.901  1.00 58.11      A    N  
ANISOU 1862  N   PHE A 707    10471   4926   6680  -2299   2347    217  A    N  
ATOM   1863  CA  PHE A 707      -7.317 -22.382 -11.207  1.00 54.99      A    C  
ANISOU 1863  CA  PHE A 707    10331   4538   6024  -2047   2077    430  A    C  
ATOM   1864  C   PHE A 707      -7.334 -22.429  -9.673  1.00 57.27      A    C  
ANISOU 1864  C   PHE A 707    11126   4660   5976  -1983   2177    541  A    C  
ATOM   1865  O   PHE A 707      -6.273 -22.349  -9.058  1.00 57.71      A    O  
ANISOU 1865  O   PHE A 707    11540   4605   5781  -1718   1879    719  A    O  
ATOM   1866  CB  PHE A 707      -7.311 -20.938 -11.725  1.00 49.39      A    C  
ANISOU 1866  CB  PHE A 707     9156   4180   5431  -2004   1934    375  A    C  
ATOM   1867  CG  PHE A 707      -6.314 -20.711 -12.818  1.00 46.91      A    C  
ANISOU 1867  CG  PHE A 707     8500   4074   5249  -1732   1505    362  A    C  
ATOM   1868  CD1 PHE A 707      -4.959 -20.724 -12.537  1.00 42.51      A    C  
ANISOU 1868  CD1 PHE A 707     8178   3440   4535  -1427   1147    525  A    C  
ATOM   1869  CD2 PHE A 707      -6.725 -20.516 -14.126  1.00 45.09      A    C  
ANISOU 1869  CD2 PHE A 707     7729   4103   5301  -1778   1463    166  A    C  
ATOM   1870  CE1 PHE A 707      -4.029 -20.539 -13.537  1.00 48.94      A    C  
ANISOU 1870  CE1 PHE A 707     8665   4433   5496  -1205    815    486  A    C  
ATOM   1871  CE2 PHE A 707      -5.799 -20.326 -15.138  1.00 43.93      A    C  
ANISOU 1871  CE2 PHE A 707     7324   4122   5246  -1546   1124    155  A    C  
ATOM   1872  CZ  PHE A 707      -4.449 -20.339 -14.845  1.00 44.73      A    C  
ANISOU 1872  CZ  PHE A 707     7636   4145   5215  -1276    830    311  A    C  
ATOM   1873  N   PRO A 708      -8.522 -22.551  -9.050  1.00 60.00      A    N  
ANISOU 1873  N   PRO A 708    11495   4981   6320  -2213   2577    406  A    N  
ATOM   1874  CA  PRO A 708      -8.506 -22.730  -7.594  1.00 64.22      A    C  
ANISOU 1874  CA  PRO A 708    12587   5301   6512  -2163   2691    496  A    C  
ATOM   1875  C   PRO A 708      -7.712 -23.962  -7.174  1.00 67.12      A    C  
ANISOU 1875  C   PRO A 708    13515   5336   6650  -2011   2558    644  A    C  
ATOM   1876  O   PRO A 708      -6.967 -23.903  -6.200  1.00 66.55      A    O  
ANISOU 1876  O   PRO A 708    13904   5124   6260  -1790   2358    785  A    O  
ATOM   1877  CB  PRO A 708      -9.983 -22.922  -7.255  1.00 65.67      A    C  
ANISOU 1877  CB  PRO A 708    12669   5470   6812  -2478   3193    281  A    C  
ATOM   1878  CG  PRO A 708     -10.696 -22.145  -8.291  1.00 63.78      A    C  
ANISOU 1878  CG  PRO A 708    11735   5560   6938  -2608   3238     87  A    C  
ATOM   1879  CD  PRO A 708      -9.888 -22.308  -9.550  1.00 59.87      A    C  
ANISOU 1879  CD  PRO A 708    10987   5155   6604  -2492   2904    145  A    C  
ATOM   1880  N   ARG A 709      -7.871 -25.057  -7.910  1.00 70.09      A    N  
ANISOU 1880  N   ARG A 709    13849   5591   7193  -2113   2648    591  A    N  
ATOM   1881  CA  ARG A 709      -7.118 -26.273  -7.637  1.00 75.58      A    C  
ANISOU 1881  CA  ARG A 709    15051   5968   7698  -1954   2512    720  A    C  
ATOM   1882  C   ARG A 709      -5.640 -26.064  -7.943  1.00 71.17      A    C  
ANISOU 1882  C   ARG A 709    14535   5425   7082  -1583   1972    879  A    C  
ATOM   1883  O   ARG A 709      -4.771 -26.506  -7.190  1.00 72.17      A    O  
ANISOU 1883  O   ARG A 709    15142   5347   6934  -1322   1725   1009  A    O  
ATOM   1884  CB  ARG A 709      -7.661 -27.433  -8.471  1.00 82.46      A    C  
ANISOU 1884  CB  ARG A 709    15807   6722   8803  -2160   2733    603  A    C  
ATOM   1885  CG  ARG A 709      -9.132 -27.753  -8.233  1.00 90.25      A    C  
ANISOU 1885  CG  ARG A 709    16713   7683   9894  -2529   3264    400  A    C  
ATOM   1886  CD  ARG A 709      -9.299 -29.079  -7.500  1.00 99.55      A    C  
ANISOU 1886  CD  ARG A 709    18493   8478  10852  -2603   3513    435  A    C  
ATOM   1887  NE  ARG A 709     -10.652 -29.617  -7.629  1.00105.65      A    N  
ANISOU 1887  NE  ARG A 709    19106   9211  11825  -2976   4013    200  A    N  
ATOM   1888  CZ  ARG A 709     -10.994 -30.597  -8.462  1.00109.41      A    C  
ANISOU 1888  CZ  ARG A 709    19435   9606  12532  -3136   4134     84  A    C  
ATOM   1889  NH1 ARG A 709     -10.082 -31.161  -9.243  1.00107.49      A    N1+
ANISOU 1889  NH1 ARG A 709    19203   9296  12342  -2952   3803    190  A    N1+
ATOM   1890  NH2 ARG A 709     -12.250 -31.021  -8.510  1.00114.19      A    N  
ANISOU 1890  NH2 ARG A 709    19874  10185  13327  -3475   4586   -160  A    N  
ATOM   1891  N   ILE A 710      -5.369 -25.393  -9.058  1.00 65.88      A    N  
ANISOU 1891  N   ILE A 710    13355   4996   6681  -1556   1786    839  A    N  
ATOM   1892  CA  ILE A 710      -4.006 -25.093  -9.481  1.00 62.00      A    C  
ANISOU 1892  CA  ILE A 710    12818   4541   6199  -1220   1294    946  A    C  
ATOM   1893  C   ILE A 710      -3.267 -24.298  -8.413  1.00 60.55      A    C  
ANISOU 1893  C   ILE A 710    12878   4394   5733   -963   1012   1057  A    C  
ATOM   1894  O   ILE A 710      -2.135 -24.620  -8.054  1.00 60.83      A    O  
ANISOU 1894  O   ILE A 710    13179   4305   5629   -637    629   1143  A    O  
ATOM   1895  CB  ILE A 710      -4.005 -24.283 -10.794  1.00 59.71      A    C  
ANISOU 1895  CB  ILE A 710    11947   4514   6226  -1286   1215    859  A    C  
ATOM   1896  CG1 ILE A 710      -4.634 -25.101 -11.925  1.00 59.09      A    C  
ANISOU 1896  CG1 ILE A 710    11609   4403   6439  -1514   1428    704  A    C  
ATOM   1897  CG2 ILE A 710      -2.592 -23.835 -11.156  1.00 49.95      A    C  
ANISOU 1897  CG2 ILE A 710    10618   3351   5009   -924    714    932  A    C  
ATOM   1898  CD1 ILE A 710      -4.736 -24.352 -13.237  1.00 55.73      A    C  
ANISOU 1898  CD1 ILE A 710    10519   4338   6317  -1548   1329    537  A    C  
ATOM   1899  N   LEU A 711      -3.925 -23.263  -7.905  1.00 60.87      A    N  
ANISOU 1899  N   LEU A 711    12802   4614   5713  -1103   1190   1021  A    N  
ATOM   1900  CA  LEU A 711      -3.335 -22.388  -6.901  1.00 61.08      A    C  
ANISOU 1900  CA  LEU A 711    13020   4698   5491   -894    945   1090  A    C  
ATOM   1901  C   LEU A 711      -2.978 -23.158  -5.634  1.00 68.71      A    C  
ANISOU 1901  C   LEU A 711    14616   5376   6116   -738    878   1154  A    C  
ATOM   1902  O   LEU A 711      -1.902 -22.973  -5.070  1.00 70.43      A    O  
ANISOU 1902  O   LEU A 711    15039   5556   6165   -424    462   1210  A    O  
ATOM   1903  CB  LEU A 711      -4.293 -21.243  -6.571  1.00 57.38      A    C  
ANISOU 1903  CB  LEU A 711    12333   4440   5028  -1107   1225   1015  A    C  
ATOM   1904  CG  LEU A 711      -3.824 -20.246  -5.511  1.00 58.76      A    C  
ANISOU 1904  CG  LEU A 711    12690   4678   4958   -930   1016   1057  A    C  
ATOM   1905  CD1 LEU A 711      -2.494 -19.634  -5.918  1.00 57.35      A    C  
ANISOU 1905  CD1 LEU A 711    12333   4635   4823   -627    492   1114  A    C  
ATOM   1906  CD2 LEU A 711      -4.871 -19.164  -5.297  1.00 56.81      A    C  
ANISOU 1906  CD2 LEU A 711    12196   4629   4758  -1152   1332    962  A    C  
ATOM   1907  N   ALA A 712      -3.883 -24.030  -5.201  1.00 71.58      A    N  
ANISOU 1907  N   ALA A 712    15279   5531   6388   -959   1283   1121  A    N  
ATOM   1908  CA  ALA A 712      -3.675 -24.815  -3.990  1.00 75.83      A    C  
ANISOU 1908  CA  ALA A 712    16487   5754   6569   -847   1284   1176  A    C  
ATOM   1909  C   ALA A 712      -2.434 -25.704  -4.067  1.00 80.44      A    C  
ANISOU 1909  C   ALA A 712    17342   6153   7070   -508    851   1259  A    C  
ATOM   1910  O   ALA A 712      -1.615 -25.703  -3.151  1.00 84.41      A    O  
ANISOU 1910  O   ALA A 712    18235   6535   7301   -227    528   1304  A    O  
ATOM   1911  CB  ALA A 712      -4.907 -25.649  -3.682  1.00 76.95      A    C  
ANISOU 1911  CB  ALA A 712    16872   5697   6669  -1175   1839   1106  A    C  
ATOM   1912  N   GLU A 713      -2.292 -26.452  -5.158  1.00 80.15      A    N  
ANISOU 1912  N   GLU A 713    17084   6090   7279   -523    830   1255  A    N  
ATOM   1913  CA  GLU A 713      -1.155 -27.358  -5.305  1.00 84.89      A    C  
ANISOU 1913  CA  GLU A 713    17903   6507   7842   -195    436   1309  A    C  
ATOM   1914  C   GLU A 713       0.179 -26.622  -5.376  1.00 82.27      A    C  
ANISOU 1914  C   GLU A 713    17361   6341   7556    184   -141   1313  A    C  
ATOM   1915  O   GLU A 713       1.184 -27.100  -4.856  1.00 83.45      A    O  
ANISOU 1915  O   GLU A 713    17814   6342   7552    518   -525   1329  A    O  
ATOM   1916  CB  GLU A 713      -1.332 -28.279  -6.514  1.00 87.68      A    C  
ANISOU 1916  CB  GLU A 713    18037   6795   8484   -305    560   1279  A    C  
ATOM   1917  CG  GLU A 713      -1.607 -29.733  -6.138  1.00 97.06      A    C  
ANISOU 1917  CG  GLU A 713    19749   7625   9505   -358    766   1307  A    C  
ATOM   1918  CD  GLU A 713      -0.338 -30.527  -5.864  1.00103.79      A    C  
ANISOU 1918  CD  GLU A 713    20959   8264  10212     60    309   1369  A    C  
ATOM   1919  OE1 GLU A 713      -0.051 -30.824  -4.683  1.00108.80      A    O  
ANISOU 1919  OE1 GLU A 713    22163   8693  10481    221    207   1421  A    O  
ATOM   1920  OE2 GLU A 713       0.368 -30.865  -6.838  1.00103.33      A    O1-
ANISOU 1920  OE2 GLU A 713    20614   8234  10413    235     50   1344  A    O1-
ATOM   1921  N   ILE A 714       0.187 -25.461  -6.020  1.00 79.70      A    N  
ANISOU 1921  N   ILE A 714    16505   6322   7453    132   -204   1276  A    N  
ATOM   1922  CA  ILE A 714       1.373 -24.616  -6.018  1.00 80.94      A    C  
ANISOU 1922  CA  ILE A 714    16426   6659   7667    452   -710   1248  A    C  
ATOM   1923  C   ILE A 714       1.583 -24.044  -4.621  1.00 88.06      A    C  
ANISOU 1923  C   ILE A 714    17672   7539   8250    567   -848   1250  A    C  
ATOM   1924  O   ILE A 714       2.711 -23.941  -4.138  1.00 89.34      A    O  
ANISOU 1924  O   ILE A 714    17917   7687   8340    901  -1311   1208  A    O  
ATOM   1925  CB  ILE A 714       1.249 -23.466  -7.020  1.00 74.08      A    C  
ANISOU 1925  CB  ILE A 714    14955   6106   7086    341   -702   1210  A    C  
ATOM   1926  CG1 ILE A 714       0.947 -24.011  -8.413  1.00 71.20      A    C  
ANISOU 1926  CG1 ILE A 714    14287   5735   7031    202   -536   1186  A    C  
ATOM   1927  CG2 ILE A 714       2.525 -22.650  -7.052  1.00 71.93      A    C  
ANISOU 1927  CG2 ILE A 714    14412   6015   6904    666  -1219   1152  A    C  
ATOM   1928  CD1 ILE A 714       0.758 -22.938  -9.454  1.00 65.14      A    C  
ANISOU 1928  CD1 ILE A 714    12990   5237   6523     77   -505   1142  A    C  
ATOM   1929  N   GLU A 715       0.482 -23.678  -3.975  1.00 92.60      A    N  
ANISOU 1929  N   GLU A 715    18428   8102   8654    288   -438   1267  A    N  
ATOM   1930  CA  GLU A 715       0.533 -23.133  -2.629  1.00 99.15      A    C  
ANISOU 1930  CA  GLU A 715    19625   8875   9173    362   -502   1258  A    C  
ATOM   1931  C   GLU A 715       1.024 -24.202  -1.656  1.00104.51      A    C  
ANISOU 1931  C   GLU A 715    20963   9211   9537    578   -662   1283  A    C  
ATOM   1932  O   GLU A 715       1.852 -23.928  -0.788  1.00107.32      A    O  
ANISOU 1932  O   GLU A 715    21566   9510   9701    852  -1040   1250  A    O  
ATOM   1933  CB  GLU A 715      -0.849 -22.627  -2.214  1.00103.68      A    C  
ANISOU 1933  CB  GLU A 715    20245   9483   9667      3     32   1248  A    C  
ATOM   1934  CG  GLU A 715      -0.838 -21.458  -1.247  1.00109.23      A    C  
ANISOU 1934  CG  GLU A 715    21026  10280  10196     41    -39   1215  A    C  
ATOM   1935  CD  GLU A 715      -0.415 -20.154  -1.899  1.00110.04      A    C  
ANISOU 1935  CD  GLU A 715    20547  10729  10534     95   -277   1178  A    C  
ATOM   1936  OE1 GLU A 715       0.805 -19.921  -2.024  1.00112.65      A    O  
ANISOU 1936  OE1 GLU A 715    20744  11131  10926    390   -774   1155  A    O  
ATOM   1937  OE2 GLU A 715      -1.302 -19.357  -2.280  1.00107.48      A    O1-
ANISOU 1937  OE2 GLU A 715    19894  10602  10343   -156     35   1152  A    O1-
ATOM   1938  N   GLU A 716       0.516 -25.421  -1.811  1.00106.98      A    N  
ANISOU 1938  N   GLU A 716    21565   9285   9797    455   -380   1327  A    N  
ATOM   1939  CA  GLU A 716       0.924 -26.536  -0.961  1.00113.65      A    C  
ANISOU 1939  CA  GLU A 716    23085   9772  10324    651   -502   1360  A    C  
ATOM   1940  C   GLU A 716       2.399 -26.869  -1.142  1.00112.26      A    C  
ANISOU 1940  C   GLU A 716    22866   9579  10208   1088  -1122   1329  A    C  
ATOM   1941  O   GLU A 716       3.117 -27.102  -0.172  1.00114.99      A    O  
ANISOU 1941  O   GLU A 716    23671   9741  10279   1374  -1452   1306  A    O  
ATOM   1942  CB  GLU A 716       0.078 -27.776  -1.253  1.00119.74      A    C  
ANISOU 1942  CB  GLU A 716    24116  10302  11076    408    -56   1404  A    C  
ATOM   1943  CG  GLU A 716      -1.376 -27.662  -0.823  1.00124.44      A    C  
ANISOU 1943  CG  GLU A 716    24865  10841  11575     -6    575   1387  A    C  
ATOM   1944  CD  GLU A 716      -2.193 -28.883  -1.202  1.00130.02      A    C  
ANISOU 1944  CD  GLU A 716    25752  11325  12322   -266   1017   1392  A    C  
ATOM   1945  OE1 GLU A 716      -3.437 -28.820  -1.111  1.00131.83      A    O  
ANISOU 1945  OE1 GLU A 716    25950  11550  12589   -641   1561   1332  A    O  
ATOM   1946  OE2 GLU A 716      -1.590 -29.908  -1.589  1.00131.95      A    O1-
ANISOU 1946  OE2 GLU A 716    26155  11399  12582    -95    821   1436  A    O1-
ATOM   1947  N   LEU A 717       2.841 -26.889  -2.395  1.00108.97      A    N  
ANISOU 1947  N   LEU A 717    21893   9346  10165   1142  -1277   1304  A    N  
ATOM   1948  CA  LEU A 717       4.220 -27.220  -2.734  1.00110.76      A    C  
ANISOU 1948  CA  LEU A 717    21965   9583  10537   1543  -1832   1233  A    C  
ATOM   1949  C   LEU A 717       5.174 -26.108  -2.307  1.00109.86      A    C  
ANISOU 1949  C   LEU A 717    21604   9678  10460   1792  -2292   1122  A    C  
ATOM   1950  O   LEU A 717       6.377 -26.326  -2.152  1.00111.73      A    O  
ANISOU 1950  O   LEU A 717    21821   9889  10743   2157  -2791   1015  A    O  
ATOM   1951  CB  LEU A 717       4.334 -27.467  -4.241  1.00108.29      A    C  
ANISOU 1951  CB  LEU A 717    21097   9407  10640   1499  -1806   1215  A    C  
ATOM   1952  CG  LEU A 717       5.683 -27.915  -4.801  1.00110.90      A    C  
ANISOU 1952  CG  LEU A 717    21182   9752  11202   1886  -2305   1111  A    C  
ATOM   1953  CD1 LEU A 717       6.125 -29.206  -4.126  1.00117.99      A    C  
ANISOU 1953  CD1 LEU A 717    22678  10304  11847   2127  -2474   1127  A    C  
ATOM   1954  CD2 LEU A 717       5.605 -28.084  -6.312  1.00107.10      A    C  
ANISOU 1954  CD2 LEU A 717    20174   9390  11127   1789  -2185   1087  A    C  
ATOM   1955  N   ALA A 718       4.620 -24.918  -2.103  1.00107.68      A    N  
ANISOU 1955  N   ALA A 718    21130   9606  10179   1587  -2116   1125  A    N  
ATOM   1956  CA  ALA A 718       5.410 -23.738  -1.766  1.00107.55      A    C  
ANISOU 1956  CA  ALA A 718    20826   9806  10231   1763  -2494   1012  A    C  
ATOM   1957  C   ALA A 718       5.958 -23.770  -0.344  1.00114.01      A    C  
ANISOU 1957  C   ALA A 718    22183  10427  10710   2007  -2791    956  A    C  
ATOM   1958  O   ALA A 718       6.910 -23.055  -0.029  1.00113.82      A    O  
ANISOU 1958  O   ALA A 718    21955  10527  10765   2239  -3220    820  A    O  
ATOM   1959  CB  ALA A 718       4.590 -22.476  -1.983  1.00102.83      A    C  
ANISOU 1959  CB  ALA A 718    19889   9465   9717   1464  -2192   1037  A    C  
ATOM   1960  N   ARG A 719       5.343 -24.585   0.508  1.00121.35      A    N  
ANISOU 1960  N   ARG A 719    23804  11035  11266   1945  -2551   1046  A    N  
ATOM   1961  CA  ARG A 719       5.732 -24.688   1.912  1.00131.18      A    C  
ANISOU 1961  CA  ARG A 719    25682  12033  12129   2166  -2789   1006  A    C  
ATOM   1962  C   ARG A 719       7.229 -24.921   2.079  1.00135.89      A    C  
ANISOU 1962  C   ARG A 719    26237  12600  12797   2620  -3453    854  A    C  
ATOM   1963  O   ARG A 719       7.872 -24.316   2.939  1.00138.73      A    O  
ANISOU 1963  O   ARG A 719    26722  12950  13040   2832  -3808    741  A    O  
ATOM   1964  CB  ARG A 719       4.977 -25.830   2.588  1.00138.79      A    C  
ANISOU 1964  CB  ARG A 719    27417  12609  12707   2066  -2446   1118  A    C  
ATOM   1965  CG  ARG A 719       3.481 -25.627   2.719  1.00139.64      A    C  
ANISOU 1965  CG  ARG A 719    27656  12694  12705   1623  -1774   1217  A    C  
ATOM   1966  CD  ARG A 719       2.867 -26.838   3.403  1.00147.12      A    C  
ANISOU 1966  CD  ARG A 719    29385  13230  13285   1544  -1451   1295  A    C  
ATOM   1967  NE  ARG A 719       1.415 -26.756   3.518  1.00147.81      A    N  
ANISOU 1967  NE  ARG A 719    29578  13276  13307   1105   -771   1349  A    N  
ATOM   1968  CZ  ARG A 719       0.656 -27.720   4.030  1.00152.91      A    C  
ANISOU 1968  CZ  ARG A 719    30838  13583  13678    936   -354   1400  A    C  
ATOM   1969  NH1 ARG A 719       1.212 -28.840   4.472  1.00158.02      A    N1+
ANISOU 1969  NH1 ARG A 719    32095  13890  14055   1181   -559   1430  A    N1+
ATOM   1970  NH2 ARG A 719      -0.660 -27.567   4.099  1.00152.93      A    N  
ANISOU 1970  NH2 ARG A 719    30844  13577  13685    526    271   1402  A    N  
ATOM   1971  N   GLU A 720       7.771 -25.805   1.249  1.00136.76      A    N  
ANISOU 1971  N   GLU A 720    26156  12688  13117   2770  -3615    832  A    N  
ATOM   1972  CA  GLU A 720       9.187 -26.145   1.287  1.00140.38      A    C  
ANISOU 1972  CA  GLU A 720    26514  13122  13702   3204  -4226    656  A    C  
ATOM   1973  C   GLU A 720      10.061 -24.922   1.035  1.00137.69      A    C  
ANISOU 1973  C   GLU A 720    25500  13114  13701   3320  -4585    463  A    C  
ATOM   1974  O   GLU A 720      11.003 -24.974   0.246  1.00136.68      A    O  
ANISOU 1974  O   GLU A 720    24835  13148  13950   3509  -4894    309  A    O  
ATOM   1975  CB  GLU A 720       9.487 -27.223   0.248  1.00140.62      A    C  
ANISOU 1975  CB  GLU A 720    26350  13112  13968   3291  -4251    664  A    C  
ATOM   1976  CG  GLU A 720       8.640 -28.472   0.399  1.00144.74      A    C  
ANISOU 1976  CG  GLU A 720    27501  13299  14193   3157  -3876    845  A    C  
ATOM   1977  CD  GLU A 720       8.810 -29.430  -0.759  1.00145.66      A    C  
ANISOU 1977  CD  GLU A 720    27357  13398  14588   3188  -3837    864  A    C  
ATOM   1978  OE1 GLU A 720       9.303 -28.996  -1.822  1.00142.54      A    O  
ANISOU 1978  OE1 GLU A 720    26240  13287  14633   3216  -3965    766  A    O  
ATOM   1979  OE2 GLU A 720       8.453 -30.618  -0.608  1.00149.39      A    O1-
ANISOU 1979  OE2 GLU A 720    28361  13559  14843   3181  -3665    968  A    O1-
TER   
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.