CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 20090316263652265

Job options:

ID        	=	 20090316263652265
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 10
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   ASN A  28      53.375  71.856   1.496  1.00225.35      A    N  
ANISOU    1  N   ASN A  28    36251  25242  24129  -8381  -5314   8582  A    N  
ATOM      2  CA  ASN A  28      52.631  72.160   2.712  1.00226.20      A    C  
ANISOU    2  CA  ASN A  28    36421  24725  24799  -7820  -5578   8388  A    C  
ATOM      3  C   ASN A  28      53.283  71.468   3.906  1.00222.60      A    C  
ANISOU    3  C   ASN A  28    35799  24328  24450  -7671  -5261   8007  A    C  
ATOM      4  O   ASN A  28      53.539  70.266   3.865  1.00228.85      A    O  
ANISOU    4  O   ASN A  28    36391  25632  24930  -7657  -4871   7787  A    O  
ATOM      5  CB  ASN A  28      51.163  71.734   2.559  1.00227.27      A    C  
ANISOU    5  CB  ASN A  28    36572  24759  25021  -7316  -5767   8322  A    C  
ATOM      6  CG  ASN A  28      50.298  72.128   3.753  1.00224.16      A    C  
ANISOU    6  CG  ASN A  28    36239  23701  25230  -6727  -6041   8119  A    C  
ATOM      7  ND2 ASN A  28      49.147  72.727   3.471  1.00221.98      A    N  
ANISOU    7  ND2 ASN A  28    36068  23041  25234  -6448  -6437   8285  A    N  
ATOM      8  OD1 ASN A  28      50.656  71.899   4.908  1.00226.50      A    O  
ANISOU    8  OD1 ASN A  28    36482  23835  25743  -6534  -5897   7810  A    O  
ATOM      9  N   PRO A  29      53.569  72.236   4.971  1.00203.63      A    N  
ANISOU    9  N   PRO A  29    33482  21396  22493  -7577  -5437   7924  A    N  
ATOM     10  CA  PRO A  29      54.205  71.726   6.195  1.00187.84      A    C  
ANISOU   10  CA  PRO A  29    31350  19379  20639  -7469  -5208   7583  A    C  
ATOM     11  C   PRO A  29      53.364  70.670   6.914  1.00175.44      A    C  
ANISOU   11  C   PRO A  29    29694  17823  19142  -6912  -5102   7223  A    C  
ATOM     12  O   PRO A  29      53.911  69.683   7.407  1.00172.02      A    O  
ANISOU   12  O   PRO A  29    29072  17727  18561  -6911  -4769   6982  A    O  
ATOM     13  CB  PRO A  29      54.351  72.980   7.064  1.00197.41      A    C  
ANISOU   13  CB  PRO A  29    32749  19910  22346  -7441  -5534   7589  A    C  
ATOM     14  CG  PRO A  29      54.311  74.122   6.099  1.00201.12      A    C  
ANISOU   14  CG  PRO A  29    33398  20203  22815  -7747  -5825   8005  A    C  
ATOM     15  CD  PRO A  29      53.363  73.693   5.026  1.00200.61      A    C  
ANISOU   15  CD  PRO A  29    33335  20397  22491  -7621  -5873   8165  A    C  
ATOM     16  N   GLU A  30      52.053  70.889   6.975  1.00185.75      A    N  
ANISOU   16  N   GLU A  30    31122  18764  20692  -6451  -5389   7197  A    N  
ATOM     17  CA  GLU A  30      51.128  69.985   7.659  1.00189.21      A    C  
ANISOU   17  CA  GLU A  30    31490  19168  21231  -5898  -5328   6864  A    C  
ATOM     18  C   GLU A  30      51.027  68.627   6.967  1.00192.50      A    C  
ANISOU   18  C   GLU A  30    31718  20257  21164  -5906  -4999   6799  A    C  
ATOM     19  O   GLU A  30      50.925  67.595   7.629  1.00199.69      A    O  
ANISOU   19  O   GLU A  30    32505  21343  22024  -5639  -4777   6490  A    O  
ATOM     20  CB  GLU A  30      49.742  70.625   7.769  1.00193.45      A    C  
ANISOU   20  CB  GLU A  30    32164  19171  22168  -5433  -5712   6880  A    C  
ATOM     21  CG  GLU A  30      49.754  71.992   8.431  1.00202.20      A    C  
ANISOU   21  CG  GLU A  30    33462  19581  23784  -5389  -6027   6908  A    C  
ATOM     22  CD  GLU A  30      48.381  72.632   8.479  1.00212.29      A    C  
ANISOU   22  CD  GLU A  30    34831  20337  25494  -4924  -6379   6925  A    C  
ATOM     23  OE1 GLU A  30      47.485  72.182   7.734  1.00216.26      A    O  
ANISOU   23  OE1 GLU A  30    35256  21049  25865  -4744  -6439   7035  A    O  
ATOM     24  OE2 GLU A  30      48.199  73.595   9.254  1.00219.76      A    O1-
ANISOU   24  OE2 GLU A  30    35910  20665  26923  -4747  -6591   6820  A    O1-
ATOM     25  N   THR A  31      51.038  68.631   5.638  1.00213.42      A    N  
ANISOU   25  N   THR A  31    34360  23276  23454  -6219  -4971   7076  A    N  
ATOM     26  CA  THR A  31      50.929  67.396   4.868  1.00212.02      A    C  
ANISOU   26  CA  THR A  31    34023  23741  22796  -6264  -4651   6996  A    C  
ATOM     27  C   THR A  31      52.213  66.583   5.016  1.00228.44      A    C  
ANISOU   27  C   THR A  31    35904  26315  24579  -6582  -4177   6840  A    C  
ATOM     28  O   THR A  31      52.198  65.357   4.919  1.00222.31      A    O  
ANISOU   28  O   THR A  31    34958  25991  23518  -6486  -3846   6615  A    O  
ATOM     29  CB  THR A  31      50.658  67.668   3.375  1.00207.91      A    C  
ANISOU   29  CB  THR A  31    33567  23486  21943  -6576  -4746   7321  A    C  
ATOM     30  CG2 THR A  31      49.371  68.463   3.199  1.00210.40      A    C  
ANISOU   30  CG2 THR A  31    34042  23316  22585  -6267  -5236   7507  A    C  
ATOM     31  OG1 THR A  31      51.753  68.400   2.812  1.00216.98      A    O  
ANISOU   31  OG1 THR A  31    34764  24742  22936  -7150  -4699   7585  A    O  
ATOM     32  N   ASN A  32      53.321  67.280   5.247  1.00262.65      A    N  
ANISOU   32  N   ASN A  32    40239  30554  29002  -6964  -4148   6959  A    N  
ATOM     33  CA  ASN A  32      54.596  66.635   5.537  1.00271.78      A    C  
ANISOU   33  CA  ASN A  32    41164  32111  29988  -7266  -3727   6824  A    C  
ATOM     34  C   ASN A  32      54.540  65.956   6.899  1.00259.25      A    C  
ANISOU   34  C   ASN A  32    39488  30364  28651  -6884  -3654   6487  A    C  
ATOM     35  O   ASN A  32      55.126  64.893   7.104  1.00260.70      A    O  
ANISOU   35  O   ASN A  32    39413  30978  28661  -6915  -3268   6268  A    O  
ATOM     36  CB  ASN A  32      55.747  67.647   5.505  1.00286.68      A    C  
ANISOU   36  CB  ASN A  32    43064  33894  31968  -7769  -3765   7047  A    C  
ATOM     37  CG  ASN A  32      56.079  68.114   4.101  1.00301.38      A    C  
ANISOU   37  CG  ASN A  32    44966  36066  33479  -8252  -3726   7365  A    C  
ATOM     38  ND2 ASN A  32      57.269  68.683   3.934  1.00306.96      A    N  
ANISOU   38  ND2 ASN A  32    45600  36884  34147  -8758  -3617   7524  A    N  
ATOM     39  OD1 ASN A  32      55.278  67.967   3.178  1.00306.76      A    O  
ANISOU   39  OD1 ASN A  32    45740  36892  33922  -8189  -3802   7466  A    O  
ATOM     40  N   LEU A  33      53.836  66.594   7.828  1.00219.63      A    N  
ANISOU   40  N   LEU A  33    34659  24724  24066  -6510  -4018   6411  A    N  
ATOM     41  CA  LEU A  33      53.659  66.064   9.174  1.00178.21      A    C  
ANISOU   41  CA  LEU A  33    29328  19286  19098  -6091  -3986   6023  A    C  
ATOM     42  C   LEU A  33      52.805  64.802   9.197  1.00162.70      A    C  
ANISOU   42  C   LEU A  33    27167  17643  17009  -5602  -3789   5677  A    C  
ATOM     43  O   LEU A  33      53.063  63.895   9.981  1.00175.05      A    O  
ANISOU   43  O   LEU A  33    28429  19430  18652  -5339  -3530   5253  A    O  
ATOM     44  CB  LEU A  33      53.030  67.135  10.072  1.00168.46      A    C  
ANISOU   44  CB  LEU A  33    28387  17283  18338  -5835  -4414   6017  A    C  
ATOM     45  CG  LEU A  33      52.556  66.789  11.485  1.00151.17      A    C  
ANISOU   45  CG  LEU A  33    26094  14850  16495  -5290  -4414   5500  A    C  
ATOM     46  CD1 LEU A  33      52.755  67.993  12.386  1.00149.02      A    C  
ANISOU   46  CD1 LEU A  33    26065  13924  16631  -5349  -4710   5496  A    C  
ATOM     47  CD2 LEU A  33      51.091  66.372  11.495  1.00127.87      A    C  
ANISOU   47  CD2 LEU A  33    23189  11786  13610  -4740  -4516   5346  A    C  
ATOM     48  N   LEU A  34      51.790  64.748   8.340  1.00152.96      A    N  
ANISOU   48  N   LEU A  34    26106  16424  15588  -5500  -3940   5880  A    N  
ATOM     49  CA  LEU A  34      50.936  63.568   8.240  1.00152.28      A    C  
ANISOU   49  CA  LEU A  34    25851  16651  15355  -5087  -3773   5587  A    C  
ATOM     50  C   LEU A  34      51.703  62.388   7.650  1.00155.03      A    C  
ANISOU   50  C   LEU A  34    25893  17708  15304  -5297  -3281   5423  A    C  
ATOM     51  O   LEU A  34      51.448  61.235   7.996  1.00156.53      A    O  
ANISOU   51  O   LEU A  34    25830  18172  15472  -4953  -3031   5028  A    O  
ATOM     52  CB  LEU A  34      49.689  63.865   7.401  1.00163.79      A    C  
ANISOU   52  CB  LEU A  34    27538  17967  16728  -4966  -4085   5860  A    C  
ATOM     53  CG  LEU A  34      48.597  62.788   7.401  1.00161.55      A    C  
ANISOU   53  CG  LEU A  34    27143  17887  16353  -4516  -4018   5600  A    C  
ATOM     54  CD1 LEU A  34      47.215  63.423   7.453  1.00165.62      A    C  
ANISOU   54  CD1 LEU A  34    27798  17934  17194  -4134  -4437   5689  A    C  
ATOM     55  CD2 LEU A  34      48.718  61.874   6.184  1.00160.67      A    C  
ANISOU   55  CD2 LEU A  34    26926  18422  15700  -4775  -3733   5643  A    C  
ATOM     56  N   PHE A  35      52.627  62.684   6.742  1.00156.69      A    N  
ANISOU   56  N   PHE A  35    26127  18201  15208  -5871  -3136   5722  A    N  
ATOM     57  CA  PHE A  35      53.515  61.670   6.186  1.00164.63      A    C  
ANISOU   57  CA  PHE A  35    26816  19860  15876  -6116  -2622   5543  A    C  
ATOM     58  C   PHE A  35      54.422  61.099   7.274  1.00187.00      A    C  
ANISOU   58  C   PHE A  35    29263  22783  19007  -5955  -2350   5142  A    C  
ATOM     59  O   PHE A  35      54.601  59.884   7.364  1.00192.04      A    O  
ANISOU   59  O   PHE A  35    29577  23807  19581  -5756  -1991   4778  A    O  
ATOM     60  CB  PHE A  35      54.338  62.262   5.040  1.00163.80      A    C  
ANISOU   60  CB  PHE A  35    26829  20008  15399  -6810  -2524   5962  A    C  
ATOM     61  CG  PHE A  35      55.580  61.483   4.707  1.00160.67      A    C  
ANISOU   61  CG  PHE A  35    26052  20203  14793  -7119  -1965   5757  A    C  
ATOM     62  CD1 PHE A  35      55.518  60.368   3.885  1.00155.54      A    C  
ANISOU   62  CD1 PHE A  35    25241  20110  13747  -7148  -1563   5550  A    C  
ATOM     63  CD2 PHE A  35      56.818  61.890   5.182  1.00171.06      A    C  
ANISOU   63  CD2 PHE A  35    27162  21512  16322  -7401  -1839   5770  A    C  
ATOM     64  CE1 PHE A  35      56.661  59.658   3.567  1.00162.72      A    C  
ANISOU   64  CE1 PHE A  35    25773  21540  14514  -7411  -1019   5328  A    C  
ATOM     65  CE2 PHE A  35      57.965  61.185   4.868  1.00175.78      A    C  
ANISOU   65  CE2 PHE A  35    27355  22647  16784  -7670  -1318   5580  A    C  
ATOM     66  CZ  PHE A  35      57.888  60.068   4.059  1.00172.88      A    C  
ANISOU   66  CZ  PHE A  35    26815  22815  16056  -7661   -893   5348  A    C  
ATOM     67  N   ASN A  36      54.987  61.980   8.098  1.00200.38      A    N  
ANISOU   67  N   ASN A  36    31000  24100  21037  -6051  -2548   5219  A    N  
ATOM     68  CA  ASN A  36      55.847  61.568   9.207  1.00181.22      A    C  
ANISOU   68  CA  ASN A  36    28232  21712  18910  -5933  -2381   4892  A    C  
ATOM     69  C   ASN A  36      55.094  60.814  10.308  1.00162.34      A    C  
ANISOU   69  C   ASN A  36    25736  19176  16768  -5320  -2426   4473  A    C  
ATOM     70  O   ASN A  36      55.617  59.855  10.874  1.00165.19      A    O  
ANISOU   70  O   ASN A  36    25738  19799  17227  -5160  -2166   4150  A    O  
ATOM     71  CB  ASN A  36      56.558  62.785   9.805  1.00178.15      A    C  
ANISOU   71  CB  ASN A  36    27971  20926  18793  -6229  -2636   5097  A    C  
ATOM     72  CG  ASN A  36      57.746  63.233   8.971  1.00180.32      A    C  
ANISOU   72  CG  ASN A  36    28164  21480  18869  -6879  -2457   5409  A    C  
ATOM     73  ND2 ASN A  36      58.101  64.509   9.080  1.00181.56      A    N  
ANISOU   73  ND2 ASN A  36    28575  21246  19164  -7230  -2754   5735  A    N  
ATOM     74  OD1 ASN A  36      58.342  62.438   8.244  1.00179.18      A    O  
ANISOU   74  OD1 ASN A  36    27727  21893  18461  -7072  -2040   5343  A    O  
ATOM     75  N   LEU A  37      53.876  61.256  10.619  1.00145.63      A    N  
ANISOU   75  N   LEU A  37    23921  16637  14776  -4989  -2759   4490  A    N  
ATOM     76  CA  LEU A  37      53.035  60.568  11.599  1.00138.29      A    C  
ANISOU   76  CA  LEU A  37    22917  15585  14043  -4431  -2791   4106  A    C  
ATOM     77  C   LEU A  37      52.674  59.171  11.126  1.00139.10      A    C  
ANISOU   77  C   LEU A  37    22785  16157  13911  -4213  -2480   3877  A    C  
ATOM     78  O   LEU A  37      52.711  58.216  11.901  1.00117.49      A    O  
ANISOU   78  O   LEU A  37    19795  13550  11294  -3914  -2317   3524  A    O  
ATOM     79  CB  LEU A  37      51.756  61.355  11.888  1.00112.63      A    C  
ANISOU   79  CB  LEU A  37    20011  11807  10978  -4137  -3177   4176  A    C  
ATOM     80  CG  LEU A  37      51.839  62.471  12.926  1.00119.67      A    C  
ANISOU   80  CG  LEU A  37    21103  12127  12237  -4119  -3471   4167  A    C  
ATOM     81  CD1 LEU A  37      50.451  62.787  13.462  1.00119.16      A    C  
ANISOU   81  CD1 LEU A  37    21245  11620  12410  -3654  -3727   4032  A    C  
ATOM     82  CD2 LEU A  37      52.784  62.085  14.055  1.00111.96      A    C  
ANISOU   82  CD2 LEU A  37    19885  11242  11412  -4132  -3323   3872  A    C  
ATOM     83  N   ASN A  38      52.309  59.062   9.851  1.00151.14      A    N  
ANISOU   83  N   ASN A  38    24415  17919  15092  -4385  -2420   4087  A    N  
ATOM     84  CA  ASN A  38      51.992  57.771   9.252  1.00143.60      A    C  
ANISOU   84  CA  ASN A  38    23273  17418  13871  -4246  -2115   3874  A    C  
ATOM     85  C   ASN A  38      53.241  56.915   9.093  1.00143.00      A    C  
ANISOU   85  C   ASN A  38    22818  17802  13714  -4449  -1667   3686  A    C  
ATOM     86  O   ASN A  38      53.177  55.692   9.192  1.00141.99      A    O  
ANISOU   86  O   ASN A  38    22436  17950  13564  -4207  -1396   3358  A    O  
ATOM     87  CB  ASN A  38      51.311  57.961   7.894  1.00132.45      A    C  
ANISOU   87  CB  ASN A  38    22108  16146  12069  -4449  -2194   4169  A    C  
ATOM     88  CG  ASN A  38      49.898  58.500   8.018  1.00122.03      A    C  
ANISOU   88  CG  ASN A  38    21075  14420  10872  -4141  -2619   4299  A    C  
ATOM     89  ND2 ASN A  38      49.170  58.501   6.909  1.00131.19      A    N  
ANISOU   89  ND2 ASN A  38    22419  15716  11709  -4258  -2728   4535  A    N  
ATOM     90  OD1 ASN A  38      49.466  58.915   9.093  1.00118.69      A    O  
ANISOU   90  OD1 ASN A  38    20698  13569  10831  -3813  -2845   4183  A    O  
ATOM     91  N   SER A  39      54.378  57.563   8.853  1.00145.91      A    N  
ANISOU   91  N   SER A  39    23134  18234  14072  -4893  -1591   3893  A    N  
ATOM     92  CA  SER A  39      55.657  56.864   8.774  1.00144.25      A    C  
ANISOU   92  CA  SER A  39    22507  18429  13871  -5091  -1171   3722  A    C  
ATOM     93  C   SER A  39      56.038  56.241  10.113  1.00140.31      A    C  
ANISOU   93  C   SER A  39    21695  17840  13775  -4749  -1144   3393  A    C  
ATOM     94  O   SER A  39      56.625  55.162  10.158  1.00144.76      A    O  
ANISOU   94  O   SER A  39    21875  18729  14400  -4662   -805   3125  A    O  
ATOM     95  CB  SER A  39      56.763  57.807   8.310  1.00154.38      A    C  
ANISOU   95  CB  SER A  39    23794  19770  15093  -5659  -1131   4040  A    C  
ATOM     96  OG  SER A  39      58.038  57.283   8.635  1.00162.63      A    O  
ANISOU   96  OG  SER A  39    24381  21088  16322  -5779   -807   3856  A    O  
ATOM     97  N   CYS A  40      55.732  56.943  11.200  1.00139.11      A    N  
ANISOU   97  N   CYS A  40    21715  17237  13904  -4577  -1509   3418  A    N  
ATOM     98  CA  CYS A  40      55.966  56.421  12.544  1.00126.04      A    C  
ANISOU   98  CA  CYS A  40    19834  15472  12585  -4275  -1550   3133  A    C  
ATOM     99  C   CYS A  40      55.024  55.266  12.870  1.00117.72      A    C  
ANISOU   99  C   CYS A  40    18712  14485  11530  -3792  -1478   2821  A    C  
ATOM    100  O   CYS A  40      55.446  54.248  13.417  1.00117.37      A    O  
ANISOU  100  O   CYS A  40    18337  14618  11642  -3611  -1301   2567  A    O  
ATOM    101  CB  CYS A  40      55.815  57.523  13.595  1.00127.51      A    C  
ANISOU  101  CB  CYS A  40    20276  15158  13013  -4257  -1948   3216  A    C  
ATOM    102  SG  CYS A  40      57.329  58.441  13.947  1.00123.52      A    S  
ANISOU  102  SG  CYS A  40    19649  14587  12695  -4751  -2016   3417  A    S  
ATOM    103  N   SER A  41      53.749  55.431  12.524  1.00118.48      A    N  
ANISOU  103  N   SER A  41    19113  14432  11472  -3596  -1635   2861  A    N  
ATOM    104  CA  SER A  41      52.720  54.435  12.823  1.00106.58      A    C  
ANISOU  104  CA  SER A  41    17577  12961   9959  -3158  -1601   2590  A    C  
ATOM    105  C   SER A  41      53.028  53.105  12.131  1.00 96.12      A    C  
ANISOU  105  C   SER A  41    15953  12091   8477  -3138  -1207   2396  A    C  
ATOM    106  O   SER A  41      52.647  52.041  12.616  1.00114.20      A    O  
ANISOU  106  O   SER A  41    18084  14451  10855  -2810  -1113   2118  A    O  
ATOM    107  CB  SER A  41      51.339  54.947  12.416  1.00100.05      A    C  
ANISOU  107  CB  SER A  41    17100  11912   9004  -3006  -1847   2715  A    C  
ATOM    108  OG  SER A  41      50.326  54.021  12.764  1.00 92.97      A    O  
ANISOU  108  OG  SER A  41    16160  11046   8120  -2599  -1825   2454  A    O  
ATOM    109  N   LYS A  42      53.681  53.177  10.976  1.00 99.51      A    N  
ANISOU  109  N   LYS A  42    16325  12819   8667  -3505   -970   2538  A    N  
ATOM    110  CA  LYS A  42      54.153  51.982  10.280  1.00102.73      A    C  
ANISOU  110  CA  LYS A  42    16430  13658   8944  -3538   -538   2318  A    C  
ATOM    111  C   LYS A  42      55.106  51.175  11.168  1.00102.73      A    C  
ANISOU  111  C   LYS A  42    15999  13731   9305  -3393   -364   2071  A    C  
ATOM    112  O   LYS A  42      54.936  49.970  11.340  1.00103.70      A    O  
ANISOU  112  O   LYS A  42    15909  13981   9511  -3114   -181   1783  A    O  
ATOM    113  CB  LYS A  42      54.858  52.360   8.970  1.00121.07      A    C  
ANISOU  113  CB  LYS A  42    18760  16293  10949  -4031   -289   2514  A    C  
ATOM    114  CG  LYS A  42      53.955  52.937   7.884  1.00135.48      A    C  
ANISOU  114  CG  LYS A  42    20989  18135  12353  -4220   -430   2771  A    C  
ATOM    115  CD  LYS A  42      53.026  51.888   7.288  1.00141.18      A    C  
ANISOU  115  CD  LYS A  42    21749  19068  12824  -4011   -289   2551  A    C  
ATOM    116  CE  LYS A  42      51.564  52.194   7.583  1.00133.60      A    C  
ANISOU  116  CE  LYS A  42    21102  17792  11866  -3707   -702   2641  A    C  
ATOM    117  NZ  LYS A  42      51.144  53.527   7.064  1.00139.97      A    N1+
ANISOU  117  NZ  LYS A  42    22283  18388  12513  -3962  -1052   3079  A    N1+
ATOM    118  N   SER A  43      56.112  51.851  11.720  1.00114.59      A    N  
ANISOU  118  N   SER A  43    17371  15136  11032  -3601   -447   2204  A    N  
ATOM    119  CA  SER A  43      57.117  51.217  12.577  1.00130.46      A    C  
ANISOU  119  CA  SER A  43    18952  17203  13415  -3514   -347   2038  A    C  
ATOM    120  C   SER A  43      56.789  51.335  14.066  1.00145.68      A    C  
ANISOU  120  C   SER A  43    20950  18786  15618  -3239   -709   1985  A    C  
ATOM    121  O   SER A  43      57.608  50.974  14.909  1.00151.86      A    O  
ANISOU  121  O   SER A  43    21422  19568  16710  -3203   -730   1911  A    O  
ATOM    122  CB  SER A  43      58.501  51.816  12.307  1.00130.38      A    C  
ANISOU  122  CB  SER A  43    18701  17337  13500  -3941   -218   2210  A    C  
ATOM    123  OG  SER A  43      58.519  53.203  12.579  1.00132.55      A    O  
ANISOU  123  OG  SER A  43    19279  17331  13752  -4189   -549   2504  A    O  
ATOM    124  N   LYS A  44      55.614  51.889  14.365  1.00149.94      A    N  
ANISOU  124  N   LYS A  44    21892  19037  16040  -3077   -995   2034  A    N  
ATOM    125  CA  LYS A  44      55.057  52.001  15.721  1.00152.66      A    C  
ANISOU  125  CA  LYS A  44    22372  19063  16570  -2809  -1303   1939  A    C  
ATOM    126  C   LYS A  44      56.006  52.664  16.733  1.00157.74      A    C  
ANISOU  126  C   LYS A  44    22937  19536  17462  -2995  -1509   2024  A    C  
ATOM    127  O   LYS A  44      56.046  52.289  17.904  1.00173.24      A    O  
ANISOU  127  O   LYS A  44    24820  21389  19612  -2823  -1655   1889  A    O  
ATOM    128  CB  LYS A  44      54.581  50.623  16.240  1.00159.83      A    C  
ANISOU  128  CB  LYS A  44    23100  20063  17565  -2429  -1206   1657  A    C  
ATOM    129  CG  LYS A  44      55.648  49.587  16.610  1.00175.69      A    C  
ANISOU  129  CG  LYS A  44    24646  22275  19833  -2400  -1028   1528  A    C  
ATOM    130  CD  LYS A  44      55.033  48.283  17.093  1.00184.38      A    C  
ANISOU  130  CD  LYS A  44    25636  23406  21013  -2029   -977   1284  A    C  
ATOM    131  CE  LYS A  44      56.114  47.277  17.469  1.00185.35      A    C  
ANISOU  131  CE  LYS A  44    25287  23678  21460  -1988   -841   1187  A    C  
ATOM    132  NZ  LYS A  44      55.541  45.988  17.946  1.00180.77      A    N1+
ANISOU  132  NZ  LYS A  44    24611  23092  20981  -1645   -815    978  A    N1+
ATOM    133  N   ASP A  45      56.746  53.673  16.284  1.00143.58      A    N  
ANISOU  133  N   ASP A  45    21189  17718  15647  -3379  -1541   2262  A    N  
ATOM    134  CA  ASP A  45      57.607  54.443  17.177  1.00131.15      A    C  
ANISOU  134  CA  ASP A  45    19585  15960  14287  -3611  -1769   2364  A    C  
ATOM    135  C   ASP A  45      56.803  55.615  17.737  1.00118.27      A    C  
ANISOU  135  C   ASP A  45    18429  13884  12624  -3596  -2115   2430  A    C  
ATOM    136  O   ASP A  45      56.883  56.731  17.229  1.00113.18      A    O  
ANISOU  136  O   ASP A  45    18021  13070  11911  -3872  -2222   2659  A    O  
ATOM    137  CB  ASP A  45      58.855  54.936  16.432  1.00133.63      A    C  
ANISOU  137  CB  ASP A  45    19685  16470  14620  -4063  -1621   2584  A    C  
ATOM    138  CG  ASP A  45      59.912  55.522  17.361  1.00142.13      A    C  
ANISOU  138  CG  ASP A  45    20625  17423  15953  -4323  -1836   2673  A    C  
ATOM    139  OD1 ASP A  45      59.556  56.227  18.329  1.00143.60      A    O  
ANISOU  139  OD1 ASP A  45    21107  17253  16200  -4299  -2172   2668  A    O  
ATOM    140  OD2 ASP A  45      61.113  55.282  17.112  1.00145.83      A    O1-
ANISOU  140  OD2 ASP A  45    20678  18160  16569  -4567  -1660   2738  A    O1-
ATOM    141  N   LEU A  46      56.040  55.357  18.795  1.00115.21      A    N  
ANISOU  141  N   LEU A  46    18176  13298  12301  -3284  -2280   2223  A    N  
ATOM    142  CA  LEU A  46      55.170  56.367  19.394  1.00123.07      A    C  
ANISOU  142  CA  LEU A  46    19601  13862  13298  -3208  -2561   2203  A    C  
ATOM    143  C   LEU A  46      55.966  57.500  20.054  1.00143.21      A    C  
ANISOU  143  C   LEU A  46    22278  16147  15989  -3545  -2803   2315  A    C  
ATOM    144  O   LEU A  46      55.508  58.645  20.107  1.00148.80      A    O  
ANISOU  144  O   LEU A  46    23350  16477  16709  -3619  -3004   2390  A    O  
ATOM    145  CB  LEU A  46      54.222  55.708  20.406  1.00108.56      A    C  
ANISOU  145  CB  LEU A  46    17833  11937  11479  -2819  -2619   1915  A    C  
ATOM    146  CG  LEU A  46      53.199  56.586  21.137  1.00107.75      A    C  
ANISOU  146  CG  LEU A  46    18133  11407  11400  -2672  -2847   1800  A    C  
ATOM    147  CD1 LEU A  46      52.211  57.209  20.161  1.00107.66      A    C  
ANISOU  147  CD1 LEU A  46    18370  11223  11312  -2571  -2864   1920  A    C  
ATOM    148  CD2 LEU A  46      52.456  55.783  22.185  1.00107.20      A    C  
ANISOU  148  CD2 LEU A  46    18061  11345  11326  -2350  -2846   1505  A    C  
ATOM    149  N   SER A  47      57.156  57.176  20.553  1.00151.51      A    N  
ANISOU  149  N   SER A  47    23018  17378  17171  -3752  -2800   2328  A    N  
ATOM    150  CA  SER A  47      58.017  58.165  21.199  1.00155.45      A    C  
ANISOU  150  CA  SER A  47    23596  17666  17801  -4117  -3039   2435  A    C  
ATOM    151  C   SER A  47      58.413  59.263  20.215  1.00157.33      A    C  
ANISOU  151  C   SER A  47    23972  17800  18004  -4482  -3050   2728  A    C  
ATOM    152  O   SER A  47      58.390  60.448  20.550  1.00157.58      A    O  
ANISOU  152  O   SER A  47    24332  17450  18092  -4684  -3297   2806  A    O  
ATOM    153  CB  SER A  47      59.263  57.501  21.787  1.00155.28      A    C  
ANISOU  153  CB  SER A  47    23137  17915  17946  -4279  -3035   2434  A    C  
ATOM    154  OG  SER A  47      60.012  56.839  20.784  1.00162.64      A    O  
ANISOU  154  OG  SER A  47    23648  19239  18910  -4369  -2740   2552  A    O  
ATOM    155  N   ALA A  48      58.788  58.859  19.005  1.00149.08      A    N  
ANISOU  155  N   ALA A  48    22687  17094  16862  -4589  -2776   2884  A    N  
ATOM    156  CA  ALA A  48      59.130  59.808  17.953  1.00136.42      A    C  
ANISOU  156  CA  ALA A  48    21215  15451  15168  -4967  -2757   3194  A    C  
ATOM    157  C   ALA A  48      57.885  60.568  17.502  1.00128.39      A    C  
ANISOU  157  C   ALA A  48    20675  14081  14026  -4827  -2904   3274  A    C  
ATOM    158  O   ALA A  48      57.935  61.775  17.270  1.00132.65      A    O  
ANISOU  158  O   ALA A  48    21513  14300  14590  -5102  -3105   3502  A    O  
ATOM    159  CB  ALA A  48      59.777  59.094  16.779  1.00135.16      A    C  
ANISOU  159  CB  ALA A  48    20683  15784  14887  -5117  -2382   3297  A    C  
ATOM    160  N   ALA A  49      56.771  59.851  17.374  1.00121.16      A    N  
ANISOU  160  N   ALA A  49    19816  13214  13005  -4402  -2820   3100  A    N  
ATOM    161  CA  ALA A  49      55.495  60.464  17.020  1.00130.21      A    C  
ANISOU  161  CA  ALA A  49    21358  14030  14085  -4205  -2979   3156  A    C  
ATOM    162  C   ALA A  49      55.084  61.487  18.074  1.00139.09      A    C  
ANISOU  162  C   ALA A  49    22823  14607  15419  -4146  -3303   3067  A    C  
ATOM    163  O   ALA A  49      54.478  62.508  17.756  1.00151.53      A    O  
ANISOU  163  O   ALA A  49    24742  15788  17044  -4171  -3507   3223  A    O  
ATOM    164  CB  ALA A  49      54.418  59.405  16.861  1.00103.35      A    C  
ANISOU  164  CB  ALA A  49    17896  10805  10567  -3756  -2834   2946  A    C  
ATOM    165  N   LEU A  50      55.418  61.198  19.328  1.00139.77      A    N  
ANISOU  165  N   LEU A  50    22814  14661  15632  -4076  -3354   2811  A    N  
ATOM    166  CA  LEU A  50      55.165  62.117  20.430  1.00142.52      A    C  
ANISOU  166  CA  LEU A  50    23475  14524  16150  -4072  -3624   2664  A    C  
ATOM    167  C   LEU A  50      55.964  63.406  20.281  1.00157.58      A    C  
ANISOU  167  C   LEU A  50    25568  16139  18165  -4534  -3823   2918  A    C  
ATOM    168  O   LEU A  50      55.434  64.496  20.487  1.00168.97      A    O  
ANISOU  168  O   LEU A  50    27389  17072  19738  -4537  -4046   2927  A    O  
ATOM    169  CB  LEU A  50      55.499  61.455  21.765  1.00136.18      A    C  
ANISOU  169  CB  LEU A  50    22519  13831  15393  -3987  -3634   2366  A    C  
ATOM    170  CG  LEU A  50      54.335  60.853  22.549  1.00132.77      A    C  
ANISOU  170  CG  LEU A  50    22178  13335  14932  -3535  -3606   2025  A    C  
ATOM    171  CD1 LEU A  50      54.715  60.703  24.013  1.00135.54      A    C  
ANISOU  171  CD1 LEU A  50    22536  13644  15320  -3593  -3723   1775  A    C  
ATOM    172  CD2 LEU A  50      53.085  61.707  22.398  1.00133.91      A    C  
ANISOU  172  CD2 LEU A  50    22698  13035  15145  -3306  -3713   1969  A    C  
ATOM    173  N   ALA A  51      57.242  63.270  19.938  1.00158.18      A    N  
ANISOU  173  N   ALA A  51    25360  16525  18215  -4923  -3735   3114  A    N  
ATOM    174  CA  ALA A  51      58.126  64.418  19.751  1.00148.76      A    C  
ANISOU  174  CA  ALA A  51    24293  15115  17114  -5426  -3905   3382  A    C  
ATOM    175  C   ALA A  51      57.639  65.320  18.617  1.00158.28      A    C  
ANISOU  175  C   ALA A  51    25799  16068  18273  -5547  -3981   3703  A    C  
ATOM    176  O   ALA A  51      57.705  66.545  18.719  1.00162.33      A    O  
ANISOU  176  O   ALA A  51    26640  16111  18926  -5790  -4237   3848  A    O  
ATOM    177  CB  ALA A  51      59.550  63.951  19.485  1.00132.91      A    C  
ANISOU  177  CB  ALA A  51    21841  13569  15091  -5799  -3742   3532  A    C  
ATOM    178  N   LEU A  52      57.168  64.710  17.532  1.00159.51      A    N  
ANISOU  178  N   LEU A  52    25851  16527  18230  -5401  -3776   3824  A    N  
ATOM    179  CA  LEU A  52      56.579  65.464  16.429  1.00157.28      A    C  
ANISOU  179  CA  LEU A  52    25861  16032  17866  -5494  -3881   4153  A    C  
ATOM    180  C   LEU A  52      55.306  66.176  16.872  1.00148.74      A    C  
ANISOU  180  C   LEU A  52    25180  14359  16974  -5145  -4157   4046  A    C  
ATOM    181  O   LEU A  52      55.071  67.326  16.508  1.00162.52      A    O  
ANISOU  181  O   LEU A  52    27261  15651  18840  -5311  -4411   4305  A    O  
ATOM    182  CB  LEU A  52      56.285  64.551  15.236  1.00159.29      A    C  
ANISOU  182  CB  LEU A  52    25924  16775  17825  -5408  -3604   4262  A    C  
ATOM    183  CG  LEU A  52      57.461  63.752  14.673  1.00164.31      A    C  
ANISOU  183  CG  LEU A  52    26129  18019  18281  -5710  -3257   4321  A    C  
ATOM    184  CD1 LEU A  52      57.076  63.066  13.373  1.00153.33      A    C  
ANISOU  184  CD1 LEU A  52    24656  17038  16566  -5684  -3003   4438  A    C  
ATOM    185  CD2 LEU A  52      58.669  64.653  14.469  1.00176.04      A    C  
ANISOU  185  CD2 LEU A  52    27606  19462  19817  -6300  -3319   4616  A    C  
ATOM    186  N   TYR A  53      54.484  65.477  17.648  1.00132.85      A    N  
ANISOU  186  N   TYR A  53    23118  12349  15010  -4663  -4101   3666  A    N  
ATOM    187  CA  TYR A  53      53.265  66.052  18.212  1.00130.44      A    C  
ANISOU  187  CA  TYR A  53    23127  11513  14920  -4289  -4307   3478  A    C  
ATOM    188  C   TYR A  53      53.532  67.215  19.169  1.00135.83      A    C  
ANISOU  188  C   TYR A  53    24101  11630  15877  -4451  -4558   3375  A    C  
ATOM    189  O   TYR A  53      52.862  68.243  19.095  1.00137.85      A    O  
ANISOU  189  O   TYR A  53    24692  11327  16359  -4376  -4792   3447  A    O  
ATOM    190  CB  TYR A  53      52.462  64.959  18.922  1.00121.84      A    C  
ANISOU  190  CB  TYR A  53    21877  10625  13794  -3798  -4141   3069  A    C  
ATOM    191  CG  TYR A  53      51.309  65.460  19.761  1.00124.70      A    C  
ANISOU  191  CG  TYR A  53    22499  10488  14395  -3416  -4289   2774  A    C  
ATOM    192  CD1 TYR A  53      50.198  66.055  19.177  1.00117.79      A    C  
ANISOU  192  CD1 TYR A  53    21833   9253  13668  -3179  -4442   2897  A    C  
ATOM    193  CD2 TYR A  53      51.317  65.299  21.142  1.00127.90      A    C  
ANISOU  193  CD2 TYR A  53    22920  10799  14875  -3296  -4267   2363  A    C  
ATOM    194  CE1 TYR A  53      49.140  66.504  19.950  1.00119.74      A    C  
ANISOU  194  CE1 TYR A  53    22270   9042  14186  -2807  -4541   2593  A    C  
ATOM    195  CE2 TYR A  53      50.265  65.741  21.921  1.00125.87      A    C  
ANISOU  195  CE2 TYR A  53    22889  10113  14824  -2961  -4344   2045  A    C  
ATOM    196  CZ  TYR A  53      49.178  66.340  21.322  1.00126.85      A    C  
ANISOU  196  CZ  TYR A  53    23184   9870  15142  -2700  -4464   2145  A    C  
ATOM    197  OH  TYR A  53      48.132  66.776  22.104  1.00126.93      A    O  
ANISOU  197  OH  TYR A  53    23372   9449  15406  -2347  -4508   1796  A    O  
ATOM    198  N   ASP A  54      54.498  67.048  20.067  1.00139.98      A    N  
ANISOU  198  N   ASP A  54    24500  12285  16402  -4672  -4524   3201  A    N  
ATOM    199  CA  ASP A  54      54.881  68.112  20.996  1.00157.54      A    C  
ANISOU  199  CA  ASP A  54    27001  14014  18842  -4900  -4759   3085  A    C  
ATOM    200  C   ASP A  54      55.449  69.317  20.244  1.00169.77      A    C  
ANISOU  200  C   ASP A  54    28768  15239  20498  -5355  -4965   3503  A    C  
ATOM    201  O   ASP A  54      55.161  70.466  20.579  1.00180.54      A    O  
ANISOU  201  O   ASP A  54    30505  15979  22115  -5409  -5214   3481  A    O  
ATOM    202  CB  ASP A  54      55.899  67.599  22.019  1.00159.95      A    C  
ANISOU  202  CB  ASP A  54    27087  14606  19081  -5109  -4706   2874  A    C  
ATOM    203  CG  ASP A  54      55.332  66.512  22.916  1.00152.34      A    C  
ANISOU  203  CG  ASP A  54    25971  13887  18024  -4700  -4554   2468  A    C  
ATOM    204  OD1 ASP A  54      54.183  66.663  23.385  1.00147.76      A    O  
ANISOU  204  OD1 ASP A  54    25616  12999  17527  -4322  -4576   2191  A    O  
ATOM    205  OD2 ASP A  54      56.040  65.512  23.160  1.00145.77      A    O1-
ANISOU  205  OD2 ASP A  54    24784  13545  17057  -4765  -4416   2432  A    O1-
ATOM    206  N   ALA A  55      56.269  69.035  19.236  1.00169.85      A    N  
ANISOU  206  N   ALA A  55    28544  15675  20318  -5695  -4845   3870  A    N  
ATOM    207  CA  ALA A  55      56.848  70.061  18.372  1.00168.79      A    C  
ANISOU  207  CA  ALA A  55    28582  15331  20218  -6182  -5005   4327  A    C  
ATOM    208  C   ALA A  55      55.778  70.762  17.537  1.00168.69      A    C  
ANISOU  208  C   ALA A  55    28900  14897  20297  -6013  -5189   4578  A    C  
ATOM    209  O   ALA A  55      55.876  71.958  17.269  1.00175.29      A    O  
ANISOU  209  O   ALA A  55    30036  15251  21313  -6279  -5451   4838  A    O  
ATOM    210  CB  ALA A  55      57.913  69.460  17.467  1.00160.99      A    C  
ANISOU  210  CB  ALA A  55    27224  14978  18967  -6568  -4763   4621  A    C  
ATOM    211  N   ALA A  56      54.762  70.005  17.132  1.00163.59      A    N  
ANISOU  211  N   ALA A  56    28166  14451  19541  -5563  -5065   4498  A    N  
ATOM    212  CA  ALA A  56      53.709  70.511  16.254  1.00176.39      A    C  
ANISOU  212  CA  ALA A  56    30033  15755  21232  -5382  -5251   4770  A    C  
ATOM    213  C   ALA A  56      52.876  71.603  16.914  1.00189.28      A    C  
ANISOU  213  C   ALA A  56    32030  16595  23294  -5128  -5557   4620  A    C  
ATOM    214  O   ALA A  56      52.497  72.580  16.267  1.00204.97      A    O  
ANISOU  214  O   ALA A  56    34132  18302  25447  -5123  -5757   4848  A    O  
ATOM    215  CB  ALA A  56      52.806  69.371  15.806  1.00176.01      A    C  
ANISOU  215  CB  ALA A  56    29772  16126  20978  -4948  -5049   4659  A    C  
ATOM    216  N   ILE A  57      52.572  71.427  18.195  1.00185.77      A    N  
ANISOU  216  N   ILE A  57    31598  15970  23016  -4824  -5509   4113  A    N  
ATOM    217  CA  ILE A  57      51.773  72.404  18.927  1.00190.68      A    C  
ANISOU  217  CA  ILE A  57    32524  15871  24054  -4547  -5724   3858  A    C  
ATOM    218  C   ILE A  57      52.525  73.733  19.040  1.00216.46      A    C  
ANISOU  218  C   ILE A  57    35932  18798  27515  -4913  -5908   3962  A    C  
ATOM    219  O   ILE A  57      51.913  74.791  19.154  1.00240.66      A    O  
ANISOU  219  O   ILE A  57    39173  21338  30929  -4719  -6085   3893  A    O  
ATOM    220  CB  ILE A  57      51.407  71.904  20.339  1.00174.06      A    C  
ANISOU  220  CB  ILE A  57    30388  13734  22011  -4212  -5575   3244  A    C  
ATOM    221  CG1 ILE A  57      51.083  70.410  20.317  1.00159.20      A    C  
ANISOU  221  CG1 ILE A  57    28135  12536  19818  -3905  -5268   3068  A    C  
ATOM    222  CG2 ILE A  57      50.233  72.686  20.898  1.00177.71      A    C  
ANISOU  222  CG2 ILE A  57    31119  13510  22894  -3794  -5717   2948  A    C  
ATOM    223  CD1 ILE A  57      51.039  69.773  21.689  1.00157.90      A    C  
ANISOU  223  CD1 ILE A  57    27875  12517  19601  -3708  -5091   2521  A    C  
ATOM    224  N   THR A  58      53.853  73.657  19.063  1.00215.05      A    N  
ANISOU  224  N   THR A  58    35658  18917  27135  -5433  -5858   4107  A    N  
ATOM    225  CA  THR A  58      54.734  74.826  19.116  1.00206.72      A    C  
ANISOU  225  CA  THR A  58    34707  17627  26211  -5854  -6021   4244  A    C  
ATOM    226  C   THR A  58      55.095  75.481  17.766  1.00223.95      A    C  
ANISOU  226  C   THR A  58    36866  19900  28327  -6174  -6124   4786  A    C  
ATOM    227  O   THR A  58      55.342  76.682  17.705  1.00222.12      A    O  
ANISOU  227  O   THR A  58    36798  19289  28309  -6363  -6323   4902  A    O  
ATOM    228  CB  THR A  58      56.055  74.461  19.828  1.00172.10      A    C  
ANISOU  228  CB  THR A  58    30189  13542  21660  -6296  -5934   4142  A    C  
ATOM    229  CG2 THR A  58      55.772  73.756  21.142  1.00157.26      A    C  
ANISOU  229  CG2 THR A  58    28329  11637  19785  -6043  -5845   3626  A    C  
ATOM    230  OG1 THR A  58      56.834  73.599  18.989  1.00160.77      A    O  
ANISOU  230  OG1 THR A  58    28458  12727  19898  -6612  -5754   4480  A    O  
ATOM    231  N   SER A  59      55.120  74.686  16.699  1.00247.09      A    N  
ANISOU  231  N   SER A  59    39601  23338  30943  -6246  -5979   5099  A    N  
ATOM    232  CA  SER A  59      55.822  75.036  15.452  1.00253.73      A    C  
ANISOU  232  CA  SER A  59    40356  24475  31575  -6702  -5986   5592  A    C  
ATOM    233  C   SER A  59      55.404  76.206  14.523  1.00247.05      A    C  
ANISOU  233  C   SER A  59    39688  23304  30877  -6753  -6243   5943  A    C  
ATOM    234  O   SER A  59      56.265  77.018  14.187  1.00259.01      A    O  
ANISOU  234  O   SER A  59    41244  24783  32387  -7206  -6337   6195  A    O  
ATOM    235  CB  SER A  59      55.866  73.775  14.581  1.00249.04      A    C  
ANISOU  235  CB  SER A  59    39507  24548  30570  -6736  -5712   5766  A    C  
ATOM    236  OG  SER A  59      54.697  73.661  13.793  1.00246.83      A    O  
ANISOU  236  OG  SER A  59    39283  24237  30262  -6387  -5778   5893  A    O  
ATOM    237  N   SER A  60      54.143  76.335  14.101  1.00246.79      A    N  
ANISOU  237  N   SER A  60    39747  23035  30987  -6325  -6374   5983  A    N  
ATOM    238  CA  SER A  60      53.877  77.322  13.026  1.00244.76      A    C  
ANISOU  238  CA  SER A  60    39609  22583  30806  -6460  -6620   6406  A    C  
ATOM    239  C   SER A  60      53.026  78.607  13.234  1.00208.87      A    C  
ANISOU  239  C   SER A  60    35306  17285  26772  -6176  -6956   6392  A    C  
ATOM    240  O   SER A  60      53.273  79.585  12.527  1.00196.15      A    O  
ANISOU  240  O   SER A  60    33810  15492  25228  -6464  -7170   6755  A    O  
ATOM    241  CB  SER A  60      53.252  76.576  11.836  1.00227.62      A    C  
ANISOU  241  CB  SER A  60    37308  20854  28322  -6364  -6548   6669  A    C  
ATOM    242  OG  SER A  60      54.126  75.582  11.333  1.00213.87      A    O  
ANISOU  242  OG  SER A  60    35347  19818  26095  -6719  -6237   6774  A    O  
ATOM    243  N   GLU A  61      52.048  78.660  14.141  1.00204.09      A    N  
ANISOU  243  N   GLU A  61    34772  16236  26535  -5638  -6999   5995  A    N  
ATOM    244  CA  GLU A  61      51.432  77.518  14.800  1.00196.70      A    C  
ANISOU  244  CA  GLU A  61    33715  15485  25536  -5217  -6786   5607  A    C  
ATOM    245  C   GLU A  61      50.597  76.697  13.821  1.00187.48      A    C  
ANISOU  245  C   GLU A  61    32394  14690  24149  -4987  -6745   5817  A    C  
ATOM    246  O   GLU A  61      49.941  77.249  12.937  1.00180.59      A    O  
ANISOU  246  O   GLU A  61    31557  13666  23394  -4909  -6963   6128  A    O  
ATOM    247  CB  GLU A  61      50.557  77.988  15.965  1.00200.17      A    C  
ANISOU  247  CB  GLU A  61    34285  15307  26463  -4722  -6849   5130  A    C  
ATOM    248  CG  GLU A  61      51.323  78.662  17.106  1.00204.62      A    C  
ANISOU  248  CG  GLU A  61    35006  15533  27206  -4922  -6848   4813  A    C  
ATOM    249  CD  GLU A  61      52.246  77.715  17.856  1.00192.26      A    C  
ANISOU  249  CD  GLU A  61    33343  14400  25307  -5156  -6608   4567  A    C  
ATOM    250  OE1 GLU A  61      52.464  76.582  17.383  1.00178.61      A    O  
ANISOU  250  OE1 GLU A  61    31418  13247  23200  -5232  -6433   4701  A    O  
ATOM    251  OE2 GLU A  61      52.761  78.106  18.924  1.00188.33      A    O1-
ANISOU  251  OE2 GLU A  61    32958  13670  24928  -5276  -6597   4237  A    O1-
ATOM    252  N   VAL A  62      50.631  75.379  13.977  1.00187.09      A    N  
ANISOU  252  N   VAL A  62    32177  15131  23780  -4896  -6479   5651  A    N  
ATOM    253  CA  VAL A  62      49.881  74.487  13.100  1.00191.75      A    C  
ANISOU  253  CA  VAL A  62    32615  16124  24118  -4694  -6409   5808  A    C  
ATOM    254  C   VAL A  62      48.464  74.232  13.602  1.00193.03      A    C  
ANISOU  254  C   VAL A  62    32762  15995  24586  -4048  -6461   5508  A    C  
ATOM    255  O   VAL A  62      48.240  74.117  14.809  1.00186.18      A    O  
ANISOU  255  O   VAL A  62    31938  14853  23948  -3763  -6382   5059  A    O  
ATOM    256  CB  VAL A  62      50.603  73.125  12.952  1.00177.85      A    C  
ANISOU  256  CB  VAL A  62    30661  15062  21852  -4909  -6071   5782  A    C  
ATOM    257  CG1 VAL A  62      49.825  72.187  12.046  1.00165.54      A    C  
ANISOU  257  CG1 VAL A  62    28956  13934  20009  -4710  -5984   5912  A    C  
ATOM    258  CG2 VAL A  62      51.995  73.318  12.408  1.00183.39      A    C  
ANISOU  258  CG2 VAL A  62    31315  16102  22263  -5544  -5976   6068  A    C  
ATOM    259  N   ARG A  63      47.510  74.156  12.674  1.00196.31      A    N  
ANISOU  259  N   ARG A  63    33104  16484  25000  -3840  -6593   5747  A    N  
ATOM    260  CA  ARG A  63      46.213  73.578  12.990  1.00196.29      A    C  
ANISOU  260  CA  ARG A  63    32999  16401  25180  -3262  -6581   5492  A    C  
ATOM    261  C   ARG A  63      46.276  72.139  12.516  1.00195.15      A    C  
ANISOU  261  C   ARG A  63    32681  16944  24524  -3302  -6334   5521  A    C  
ATOM    262  O   ARG A  63      46.676  71.864  11.383  1.00206.79      A    O  
ANISOU  262  O   ARG A  63    34092  18877  25602  -3650  -6303   5880  A    O  
ATOM    263  CB  ARG A  63      45.054  74.313  12.313  1.00205.11      A    C  
ANISOU  263  CB  ARG A  63    34102  17187  26645  -2983  -6887   5720  A    C  
ATOM    264  CG  ARG A  63      44.455  75.458  13.118  1.00209.64      A    C  
ANISOU  264  CG  ARG A  63    34781  17004  27868  -2649  -7070   5491  A    C  
ATOM    265  CD  ARG A  63      43.259  76.064  12.392  1.00219.08      A    C  
ANISOU  265  CD  ARG A  63    35905  17915  29422  -2351  -7369   5741  A    C  
ATOM    266  NE  ARG A  63      42.079  76.148  13.251  1.00215.83      A    N  
ANISOU  266  NE  ARG A  63    35398  17079  29530  -1734  -7360   5330  A    N  
ATOM    267  CZ  ARG A  63      40.875  76.541  12.842  1.00214.59      A    C  
ANISOU  267  CZ  ARG A  63    35111  16656  29769  -1363  -7581   5447  A    C  
ATOM    268  NH1 ARG A  63      40.676  76.888  11.577  1.00211.99      A    N1+
ANISOU  268  NH1 ARG A  63    34759  16433  29355  -1557  -7865   5979  A    N1+
ATOM    269  NH2 ARG A  63      39.864  76.586  13.700  1.00214.26      A    N  
ANISOU  269  NH2 ARG A  63    34948  16253  30207   -810  -7511   5022  A    N  
ATOM    270  N   LEU A  64      45.874  71.224  13.388  1.00181.79      A    N  
ANISOU  270  N   LEU A  64    30917  15323  22834  -2951  -6145   5121  A    N  
ATOM    271  CA  LEU A  64      46.022  69.799  13.127  1.00155.44      A    C  
ANISOU  271  CA  LEU A  64    27423  12613  19024  -2978  -5880   5087  A    C  
ATOM    272  C   LEU A  64      44.712  69.204  12.634  1.00166.90      A    C  
ANISOU  272  C   LEU A  64    28735  14204  20476  -2567  -5934   5094  A    C  
ATOM    273  O   LEU A  64      43.671  69.347  13.273  1.00176.88      A    O  
ANISOU  273  O   LEU A  64    29982  15094  22130  -2085  -6025   4834  A    O  
ATOM    274  CB  LEU A  64      46.520  69.070  14.378  1.00143.94      A    C  
ANISOU  274  CB  LEU A  64    25952  11225  17513  -2902  -5625   4653  A    C  
ATOM    275  CG  LEU A  64      47.972  69.318  14.820  1.00143.89      A    C  
ANISOU  275  CG  LEU A  64    25979  11298  17394  -3367  -5505   4628  A    C  
ATOM    276  CD1 LEU A  64      48.189  70.712  15.419  1.00157.44      A    C  
ANISOU  276  CD1 LEU A  64    27949  12340  19530  -3466  -5747   4600  A    C  
ATOM    277  CD2 LEU A  64      48.434  68.252  15.795  1.00126.38      A    C  
ANISOU  277  CD2 LEU A  64    23490   9523  15007  -3256  -5144   4140  A    C  
ATOM    278  N   SER A  65      44.772  68.533  11.490  1.00170.64      A    N  
ANISOU  278  N   SER A  65    29091  15233  20511  -2775  -5860   5371  A    N  
ATOM    279  CA  SER A  65      43.573  67.979  10.892  1.00167.87      A    C  
ANISOU  279  CA  SER A  65    28597  15064  20120  -2458  -5934   5416  A    C  
ATOM    280  C   SER A  65      43.203  66.764  11.725  1.00127.17      A    C  
ANISOU  280  C   SER A  65    23341  10102  14878  -2106  -5700   5017  A    C  
ATOM    281  O   SER A  65      44.040  66.229  12.446  1.00123.76      A    O  
ANISOU  281  O   SER A  65    22833   9897  14293  -2199  -5397   4718  A    O  
ATOM    282  CB  SER A  65      43.813  67.603   9.429  1.00167.33      A    C  
ANISOU  282  CB  SER A  65    28457  15558  19562  -2839  -5899   5785  A    C  
ATOM    283  OG  SER A  65      42.608  67.240   8.775  1.00171.19      A    O  
ANISOU  283  OG  SER A  65    28822  16177  20047  -2575  -6035   5865  A    O  
ATOM    284  N   GLN A  66      41.947  66.340  11.638  1.00126.21      A    N  
ANISOU  284  N   GLN A  66    23089   9985  14882  -1687  -5782   4926  A    N  
ATOM    285  CA  GLN A  66      41.457  65.234  12.453  1.00120.98      A    C  
ANISOU  285  CA  GLN A  66    22187   9590  14190  -1303  -5488   4425  A    C  
ATOM    286  C   GLN A  66      42.254  63.948  12.253  1.00116.51      A    C  
ANISOU  286  C   GLN A  66    21435   9746  13087  -1529  -5094   4282  A    C  
ATOM    287  O   GLN A  66      42.396  63.175  13.189  1.00128.99      A    O  
ANISOU  287  O   GLN A  66    22837  11526  14649  -1343  -4792   3832  A    O  
ATOM    288  CB  GLN A  66      39.972  64.990  12.177  1.00143.43      A    C  
ANISOU  288  CB  GLN A  66    24899  12370  17229   -879  -5666   4429  A    C  
ATOM    289  CG  GLN A  66      39.077  66.147  12.618  1.00165.21      A    C  
ANISOU  289  CG  GLN A  66    27753  14383  20637   -531  -5996   4438  A    C  
ATOM    290  CD  GLN A  66      39.022  67.284  11.606  1.00196.52      A    C  
ANISOU  290  CD  GLN A  66    31766  18144  24759   -755  -6309   4889  A    C  
ATOM    291  NE2 GLN A  66      38.350  68.373  11.971  1.00206.47      A    N  
ANISOU  291  NE2 GLN A  66    33026  18803  26619   -474  -6532   4846  A    N  
ATOM    292  OE1 GLN A  66      39.573  67.181  10.510  1.00212.05      A    O  
ANISOU  292  OE1 GLN A  66    33758  20500  26313  -1180  -6328   5247  A    O  
ATOM    293  N   GLN A  67      42.800  63.742  11.056  1.00117.83      A    N  
ANISOU  293  N   GLN A  67    21652  10287  12832  -1944  -5093   4660  A    N  
ATOM    294  CA  GLN A  67      43.657  62.583  10.780  1.00119.08      A    C  
ANISOU  294  CA  GLN A  67    21629  11101  12514  -2185  -4697   4524  A    C  
ATOM    295  C   GLN A  67      44.864  62.504  11.713  1.00130.39      A    C  
ANISOU  295  C   GLN A  67    22988  12579  13976  -2327  -4430   4252  A    C  
ATOM    296  O   GLN A  67      45.306  61.409  12.060  1.00128.81      A    O  
ANISOU  296  O   GLN A  67    22553  12805  13585  -2291  -4089   3944  A    O  
ATOM    297  CB  GLN A  67      44.136  62.577   9.324  1.00117.43      A    C  
ANISOU  297  CB  GLN A  67    21526  11242  11852  -2675  -4728   4978  A    C  
ATOM    298  CG  GLN A  67      43.124  62.024   8.324  1.00130.56      A    C  
ANISOU  298  CG  GLN A  67    23170  13168  13268  -2600  -4847   5148  A    C  
ATOM    299  CD  GLN A  67      42.210  63.083   7.745  1.00146.51      A    C  
ANISOU  299  CD  GLN A  67    25250  14823  15593  -2520  -5251   5444  A    C  
ATOM    300  NE2 GLN A  67      42.038  63.055   6.428  1.00149.91      A    N  
ANISOU  300  NE2 GLN A  67    25655  15579  15724  -2798  -5309   5717  A    N  
ATOM    301  OE1 GLN A  67      41.668  63.919   8.467  1.00156.34      A    O  
ANISOU  301  OE1 GLN A  67    26557  15499  17347  -2217  -5500   5409  A    O  
ATOM    302  N   HIS A  68      45.413  63.659  12.085  1.00139.24      A    N  
ANISOU  302  N   HIS A  68    24306  13255  15344  -2508  -4609   4388  A    N  
ATOM    303  CA  HIS A  68      46.592  63.717  12.952  1.00140.72      A    C  
ANISOU  303  CA  HIS A  68    24439  13455  15572  -2697  -4420   4179  A    C  
ATOM    304  C   HIS A  68      46.615  62.873  14.220  1.00138.47      A    C  
ANISOU  304  C   HIS A  68    23939  13302  15372  -2392  -4167   3652  A    C  
ATOM    305  O   HIS A  68      47.478  62.011  14.385  1.00152.87      A    O  
ANISOU  305  O   HIS A  68    25546  15558  16980  -2533  -3881   3501  A    O  
ATOM    306  CB  HIS A  68      47.003  65.165  13.223  1.00153.55      A    C  
ANISOU  306  CB  HIS A  68    26344  14501  17498  -2912  -4702   4386  A    C  
ATOM    307  CG  HIS A  68      47.288  65.962  11.988  1.00165.93      A    C  
ANISOU  307  CG  HIS A  68    28125  15991  18931  -3336  -4931   4953  A    C  
ATOM    308  CD2 HIS A  68      47.068  65.698  10.678  1.00175.51      A    C  
ANISOU  308  CD2 HIS A  68    29359  17524  19804  -3532  -4969   5317  A    C  
ATOM    309  ND1 HIS A  68      47.882  67.204  12.033  1.00171.58      A    N  
ANISOU  309  ND1 HIS A  68    29093  16254  19848  -3655  -5166   5217  A    N  
ATOM    310  CE1 HIS A  68      48.012  67.673  10.805  1.00184.89      A    C  
ANISOU  310  CE1 HIS A  68    30830  18068  21353  -3984  -5283   5640  A    C  
ATOM    311  NE2 HIS A  68      47.527  66.779   9.964  1.00185.31      A    N  
ANISOU  311  NE2 HIS A  68    30749  18593  21067  -3925  -5165   5704  A    N  
ATOM    312  N   PHE A  69      45.688  63.146  15.127  1.00133.38      A    N  
ANISOU  312  N   PHE A  69    23351  12272  15054  -1989  -4276   3378  A    N  
ATOM    313  CA  PHE A  69      45.575  62.323  16.333  1.00149.44      A    C  
ANISOU  313  CA  PHE A  69    25207  14445  17129  -1712  -4048   2891  A    C  
ATOM    314  C   PHE A  69      44.600  61.062  16.268  1.00152.71      A    C  
ANISOU  314  C   PHE A  69    25394  15219  17409  -1349  -3875   2671  A    C  
ATOM    315  O   PHE A  69      44.398  60.241  17.164  1.00154.52      A    O  
ANISOU  315  O   PHE A  69    25467  15610  17633  -1123  -3683   2301  A    O  
ATOM    316  CB  PHE A  69      44.899  63.112  17.434  1.00153.44      A    C  
ANISOU  316  CB  PHE A  69    25870  14401  18028  -1427  -4188   2618  A    C  
ATOM    317  CG  PHE A  69      43.535  63.582  17.064  1.00140.58      A    C  
ANISOU  317  CG  PHE A  69    24318  12438  16657  -1090  -4398   2692  A    C  
ATOM    318  CD1 PHE A  69      42.426  62.789  17.283  1.00138.01      A    C  
ANISOU  318  CD1 PHE A  69    23813  12270  16354   -688  -4291   2443  A    C  
ATOM    319  CD2 PHE A  69      43.364  64.825  16.476  1.00141.20      A    C  
ANISOU  319  CD2 PHE A  69    24634  12032  16982  -1187  -4723   3038  A    C  
ATOM    320  CE1 PHE A  69      41.163  63.231  16.929  1.00149.33      A    C  
ANISOU  320  CE1 PHE A  69    25269  13400  18071   -373  -4501   2524  A    C  
ATOM    321  CE2 PHE A  69      42.109  65.274  16.120  1.00158.46      A    C  
ANISOU  321  CE2 PHE A  69    26858  13884  19466   -861  -4956   3137  A    C  
ATOM    322  CZ  PHE A  69      41.005  64.477  16.345  1.00164.13      A    C  
ANISOU  322  CZ  PHE A  69    27360  14779  20222   -447  -4843   2876  A    C  
ATOM    323  N   GLN A  70      44.078  60.946  15.051  1.00138.35      A    N  
ANISOU  323  N   GLN A  70    23580  13545  15443  -1372  -3967   2968  A    N  
ATOM    324  CA  GLN A  70      43.347  59.746  14.681  1.00128.03      A    C  
ANISOU  324  CA  GLN A  70    22070  12641  13936  -1156  -3815   2847  A    C  
ATOM    325  C   GLN A  70      44.575  58.847  14.716  1.00111.16      A    C  
ANISOU  325  C   GLN A  70    19761  10962  11514  -1413  -3506   2750  A    C  
ATOM    326  O   GLN A  70      44.619  57.875  15.463  1.00117.85      A    O  
ANISOU  326  O   GLN A  70    20417  12029  12330  -1244  -3286   2418  A    O  
ATOM    327  CB  GLN A  70      42.649  59.638  13.319  1.00144.15      A    C  
ANISOU  327  CB  GLN A  70    24139  14840  15793  -1196  -3960   3176  A    C  
ATOM    328  CG  GLN A  70      41.347  60.422  13.175  1.00154.27      A    C  
ANISOU  328  CG  GLN A  70    25529  15693  17395   -911  -4301   3312  A    C  
ATOM    329  CD  GLN A  70      40.164  59.775  13.864  1.00169.11      A    C  
ANISOU  329  CD  GLN A  70    27223  17577  19455   -443  -4232   2955  A    C  
ATOM    330  NE2 GLN A  70      39.855  60.237  15.072  1.00177.10      A    N  
ANISOU  330  NE2 GLN A  70    28246  18211  20831   -174  -4225   2646  A    N  
ATOM    331  OE1 GLN A  70      39.526  58.879  13.312  1.00176.50      A    O  
ANISOU  331  OE1 GLN A  70    28012  18855  20194   -348  -4177   2948  A    O  
ATOM    332  N   THR A  71      45.592  59.222  13.944  1.00 99.41      A    N  
ANISOU  332  N   THR A  71    18332   9590   9848  -1833  -3499   3048  A    N  
ATOM    333  CA  THR A  71      46.840  58.467  13.855  1.00 98.07      A    C  
ANISOU  333  CA  THR A  71    17963   9844   9455  -2103  -3201   2986  A    C  
ATOM    334  C   THR A  71      47.463  58.288  15.228  1.00123.98      A    C  
ANISOU  334  C   THR A  71    21134  13049  12926  -2027  -3105   2677  A    C  
ATOM    335  O   THR A  71      48.005  57.232  15.553  1.00110.22      A    O  
ANISOU  335  O   THR A  71    19141  11647  11092  -2009  -2857   2469  A    O  
ATOM    336  CB  THR A  71      47.875  59.165  12.941  1.00101.89      A    C  
ANISOU  336  CB  THR A  71    18542  10392   9779  -2601  -3223   3361  A    C  
ATOM    337  CG2 THR A  71      49.197  58.402  12.929  1.00100.93      A    C  
ANISOU  337  CG2 THR A  71    18153  10697   9498  -2857  -2890   3260  A    C  
ATOM    338  OG1 THR A  71      47.365  59.263  11.607  1.00106.14      A    O  
ANISOU  338  OG1 THR A  71    19200  11064  10065  -2740  -3310   3675  A    O  
ATOM    339  N   LEU A  72      47.369  59.334  16.038  1.00126.02      A    N  
ANISOU  339  N   LEU A  72    21588  12837  13458  -1991  -3320   2649  A    N  
ATOM    340  CA  LEU A  72      47.964  59.320  17.359  1.00124.67      A    C  
ANISOU  340  CA  LEU A  72    21368  12564  13435  -1982  -3278   2378  A    C  
ATOM    341  C   LEU A  72      47.235  58.368  18.301  1.00120.85      A    C  
ANISOU  341  C   LEU A  72    20755  12181  12984  -1604  -3156   1994  A    C  
ATOM    342  O   LEU A  72      47.865  57.511  18.918  1.00135.82      A    O  
ANISOU  342  O   LEU A  72    22449  14340  14815  -1627  -2991   1813  A    O  
ATOM    343  CB  LEU A  72      47.979  60.737  17.934  1.00127.17      A    C  
ANISOU  343  CB  LEU A  72    21973  12326  14020  -2062  -3538   2422  A    C  
ATOM    344  CG  LEU A  72      49.364  61.232  18.346  1.00125.64      A    C  
ANISOU  344  CG  LEU A  72    21789  12094  13856  -2459  -3559   2491  A    C  
ATOM    345  CD1 LEU A  72      50.355  61.047  17.207  1.00120.50      A    C  
ANISOU  345  CD1 LEU A  72    20995  11801  12987  -2841  -3446   2818  A    C  
ATOM    346  CD2 LEU A  72      49.289  62.681  18.764  1.00136.29      A    C  
ANISOU  346  CD2 LEU A  72    23464  12853  15469  -2554  -3833   2549  A    C  
ATOM    347  N   LEU A  73      45.914  58.500  18.391  1.00109.60      A    N  
ANISOU  347  N   LEU A  73    19423  10550  11669  -1269  -3244   1889  A    N  
ATOM    348  CA  LEU A  73      45.121  57.621  19.253  1.00104.43      A    C  
ANISOU  348  CA  LEU A  73    18650   9997  11033   -929  -3118   1535  A    C  
ATOM    349  C   LEU A  73      45.191  56.167  18.806  1.00 99.59      A    C  
ANISOU  349  C   LEU A  73    17773   9886  10182   -883  -2890   1489  A    C  
ATOM    350  O   LEU A  73      45.210  55.250  19.628  1.00 92.63      A    O  
ANISOU  350  O   LEU A  73    16746   9182   9268   -762  -2747   1233  A    O  
ATOM    351  CB  LEU A  73      43.660  58.062  19.303  1.00102.15      A    C  
ANISOU  351  CB  LEU A  73    18466   9410  10935   -586  -3240   1449  A    C  
ATOM    352  CG  LEU A  73      43.252  59.094  20.350  1.00102.64      A    C  
ANISOU  352  CG  LEU A  73    18729   8975  11296   -456  -3362   1237  A    C  
ATOM    353  CD1 LEU A  73      44.024  60.392  20.213  1.00113.69      A    C  
ANISOU  353  CD1 LEU A  73    20359  10002  12835   -739  -3561   1451  A    C  
ATOM    354  CD2 LEU A  73      41.763  59.337  20.242  1.00101.07      A    C  
ANISOU  354  CD2 LEU A  73    18538   8549  11313    -80  -3440   1153  A    C  
ATOM    355  N   TYR A  74      45.216  55.963  17.495  1.00107.51      A    N  
ANISOU  355  N   TYR A  74    18732  11104  11011   -999  -2863   1739  A    N  
ATOM    356  CA  TYR A  74      45.322  54.623  16.949  1.00118.34      A    C  
ANISOU  356  CA  TYR A  74    19874  12932  12159   -984  -2632   1681  A    C  
ATOM    357  C   TYR A  74      46.664  54.027  17.358  1.00118.04      A    C  
ANISOU  357  C   TYR A  74    19644  13124  12084  -1182  -2451   1607  A    C  
ATOM    358  O   TYR A  74      46.750  52.857  17.727  1.00126.09      A    O  
ANISOU  358  O   TYR A  74    20456  14389  13063  -1062  -2275   1406  A    O  
ATOM    359  CB  TYR A  74      45.166  54.646  15.422  1.00120.16      A    C  
ANISOU  359  CB  TYR A  74    20140  13347  12170  -1141  -2639   1962  A    C  
ATOM    360  CG  TYR A  74      43.812  55.142  14.942  1.00128.08      A    C  
ANISOU  360  CG  TYR A  74    21292  14147  13224   -944  -2862   2079  A    C  
ATOM    361  CD1 TYR A  74      42.746  55.293  15.824  1.00130.84      A    C  
ANISOU  361  CD1 TYR A  74    21666  14231  13814   -592  -2965   1871  A    C  
ATOM    362  CD2 TYR A  74      43.619  55.518  13.617  1.00138.78      A    C  
ANISOU  362  CD2 TYR A  74    22760  15570  14400  -1133  -2982   2411  A    C  
ATOM    363  CE1 TYR A  74      41.518  55.760  15.393  1.00141.43      A    C  
ANISOU  363  CE1 TYR A  74    23090  15376  15270   -394  -3179   1981  A    C  
ATOM    364  CE2 TYR A  74      42.391  55.987  13.177  1.00150.71      A    C  
ANISOU  364  CE2 TYR A  74    24385  16883  15996   -956  -3240   2558  A    C  
ATOM    365  CZ  TYR A  74      41.346  56.105  14.072  1.00150.33      A    C  
ANISOU  365  CZ  TYR A  74    24311  16561  16245   -569  -3339   2340  A    C  
ATOM    366  OH  TYR A  74      40.124  56.567  13.640  1.00156.33      A    O  
ANISOU  366  OH  TYR A  74    25130  17117  17152   -372  -3600   2486  A    O  
ATOM    367  N   LEU A  75      47.704  54.851  17.322  1.00 85.83      A    N  
ANISOU  367  N   LEU A  75    15622   8939   8051  -1487  -2515   1782  A    N  
ATOM    368  CA  LEU A  75      49.034  54.420  17.728  1.00 85.63      A    C  
ANISOU  368  CA  LEU A  75    15382   9106   8047  -1693  -2382   1742  A    C  
ATOM    369  C   LEU A  75      49.115  54.149  19.228  1.00 87.43      A    C  
ANISOU  369  C   LEU A  75    15570   9222   8429  -1554  -2432   1489  A    C  
ATOM    370  O   LEU A  75      49.873  53.285  19.666  1.00 98.10      A    O  
ANISOU  370  O   LEU A  75    16675  10796   9801  -1590  -2314   1395  A    O  
ATOM    371  CB  LEU A  75      50.078  55.464  17.324  1.00 94.00      A    C  
ANISOU  371  CB  LEU A  75    16515  10070   9130  -2084  -2462   2010  A    C  
ATOM    372  CG  LEU A  75      51.532  54.988  17.295  1.00104.26      A    C  
ANISOU  372  CG  LEU A  75    17520  11659  10436  -2353  -2284   2040  A    C  
ATOM    373  CD1 LEU A  75      51.652  53.692  16.513  1.00105.03      A    C  
ANISOU  373  CD1 LEU A  75    17338  12184  10384  -2290  -1981   1962  A    C  
ATOM    374  CD2 LEU A  75      52.430  56.054  16.692  1.00 93.66      A    C  
ANISOU  374  CD2 LEU A  75    16255  10249   9082  -2771  -2347   2337  A    C  
ATOM    375  N   CYS A  76      48.339  54.893  20.012  1.00 88.25      A    N  
ANISOU  375  N   CYS A  76    15913   8974   8644  -1408  -2611   1380  A    N  
ATOM    376  CA  CYS A  76      48.330  54.722  21.464  1.00 93.34      A    C  
ANISOU  376  CA  CYS A  76    16576   9514   9376  -1319  -2659   1126  A    C  
ATOM    377  C   CYS A  76      47.799  53.354  21.887  1.00106.17      A    C  
ANISOU  377  C   CYS A  76    18019  11391  10929  -1067  -2510    913  A    C  
ATOM    378  O   CYS A  76      48.352  52.718  22.783  1.00 96.95      A    O  
ANISOU  378  O   CYS A  76    16726  10337   9773  -1106  -2492    799  A    O  
ATOM    379  CB  CYS A  76      47.503  55.825  22.126  1.00 84.51      A    C  
ANISOU  379  CB  CYS A  76    15762   7963   8383  -1208  -2830   1007  A    C  
ATOM    380  SG  CYS A  76      48.314  57.439  22.177  1.00 98.68      A    S  
ANISOU  380  SG  CYS A  76    17805   9368  10321  -1543  -3050   1186  A    S  
ATOM    381  N   SER A  77      46.721  52.911  21.246  1.00120.98      A    N  
ANISOU  381  N   SER A  77    19886  13344  12735   -829  -2431    879  A    N  
ATOM    382  CA  SER A  77      46.151  51.596  21.521  1.00111.47      A    C  
ANISOU  382  CA  SER A  77    18517  12374  11462   -607  -2289    695  A    C  
ATOM    383  C   SER A  77      47.037  50.484  20.993  1.00111.70      A    C  
ANISOU  383  C   SER A  77    18268  12742  11431   -703  -2121    753  A    C  
ATOM    384  O   SER A  77      47.183  49.441  21.627  1.00123.61      A    O  
ANISOU  384  O   SER A  77    19615  14398  12955   -623  -2047    619  A    O  
ATOM    385  CB  SER A  77      44.769  51.471  20.901  1.00107.06      A    C  
ANISOU  385  CB  SER A  77    18012  11807  10859   -358  -2269    659  A    C  
ATOM    386  OG  SER A  77      43.936  52.515  21.337  1.00109.01      A    O  
ANISOU  386  OG  SER A  77    18473  11717  11228   -237  -2413    597  A    O  
ATOM    387  N   ALA A  78      47.620  50.718  19.823  1.00 86.25      A    N  
ANISOU  387  N   ALA A  78    14991   9632   8149   -883  -2055    951  A    N  
ATOM    388  CA  ALA A  78      48.583  49.797  19.241  1.00 85.64      A    C  
ANISOU  388  CA  ALA A  78    14633   9861   8045  -1000  -1854    984  A    C  
ATOM    389  C   ALA A  78      49.761  49.615  20.188  1.00 99.02      A    C  
ANISOU  389  C   ALA A  78    16154  11566   9902  -1132  -1889    966  A    C  
ATOM    390  O   ALA A  78      50.393  48.561  20.216  1.00102.97      A    O  
ANISOU  390  O   ALA A  78    16374  12275  10477  -1116  -1751    908  A    O  
ATOM    391  CB  ALA A  78      49.051  50.304  17.890  1.00 96.00      A    C  
ANISOU  391  CB  ALA A  78    15955  11283   9239  -1235  -1772   1199  A    C  
ATOM    392  N   SER A  79      50.051  50.665  20.951  1.00110.30      A    N  
ANISOU  392  N   SER A  79    17752  12750  11407  -1268  -2092   1017  A    N  
ATOM    393  CA  SER A  79      51.130  50.655  21.934  1.00116.84      A    C  
ANISOU  393  CA  SER A  79    18454  13565  12375  -1436  -2195   1023  A    C  
ATOM    394  C   SER A  79      50.802  49.814  23.170  1.00103.02      A    C  
ANISOU  394  C   SER A  79    16666  11821  10655  -1267  -2257    839  A    C  
ATOM    395  O   SER A  79      51.704  49.268  23.811  1.00 92.01      A    O  
ANISOU  395  O   SER A  79    15060  10521   9378  -1363  -2310    858  A    O  
ATOM    396  CB  SER A  79      51.463  52.084  22.355  1.00114.92      A    C  
ANISOU  396  CB  SER A  79    18451  13040  12175  -1664  -2406   1119  A    C  
ATOM    397  OG  SER A  79      51.423  52.951  21.240  1.00101.85      A    O  
ANISOU  397  OG  SER A  79    16918  11315  10465  -1792  -2386   1301  A    O  
ATOM    398  N   ILE A  80      49.514  49.714  23.491  1.00 92.88      A    N  
ANISOU  398  N   ILE A  80    15576  10442   9273  -1034  -2262    679  A    N  
ATOM    399  CA  ILE A  80      49.055  49.052  24.711  1.00 86.29      A    C  
ANISOU  399  CA  ILE A  80    14768   9603   8417   -911  -2321    505  A    C  
ATOM    400  C   ILE A  80      49.588  47.634  24.823  1.00 88.04      A    C  
ANISOU  400  C   ILE A  80    14680  10059   8711   -864  -2243    510  A    C  
ATOM    401  O   ILE A  80      50.082  47.233  25.877  1.00 93.59      A    O  
ANISOU  401  O   ILE A  80    15322  10773   9467   -943  -2375    503  A    O  
ATOM    402  CB  ILE A  80      47.521  49.014  24.783  1.00 86.76      A    C  
ANISOU  402  CB  ILE A  80    15012   9583   8369   -653  -2266    331  A    C  
ATOM    403  CG1 ILE A  80      46.966  50.437  24.791  1.00106.81      A    C  
ANISOU  403  CG1 ILE A  80    17841  11831  10911   -665  -2363    307  A    C  
ATOM    404  CG2 ILE A  80      47.060  48.263  26.020  1.00 81.32      A    C  
ANISOU  404  CG2 ILE A  80    14345   8931   7623   -569  -2294    157  A    C  
ATOM    405  CD1 ILE A  80      45.486  50.514  25.056  1.00121.45      A    C  
ANISOU  405  CD1 ILE A  80    19846  13576  12723   -409  -2324    112  A    C  
ATOM    406  N   THR A  81      49.492  46.883  23.732  1.00 87.35      A    N  
ANISOU  406  N   THR A  81    14410  10146   8634   -748  -2043    526  A    N  
ATOM    407  CA  THR A  81      49.957  45.503  23.718  1.00100.72      A    C  
ANISOU  407  CA  THR A  81    15801  12021  10448   -671  -1944    506  A    C  
ATOM    408  C   THR A  81      51.466  45.436  23.987  1.00109.06      A    C  
ANISOU  408  C   THR A  81    16590  13127  11719   -870  -2017    644  A    C  
ATOM    409  O   THR A  81      51.950  44.494  24.619  1.00107.20      A    O  
ANISOU  409  O   THR A  81    16142  12945  11645   -838  -2079    651  A    O  
ATOM    410  CB  THR A  81      49.622  44.799  22.388  1.00112.28      A    C  
ANISOU  410  CB  THR A  81    17136  13651  11873   -542  -1687    462  A    C  
ATOM    411  CG2 THR A  81      50.127  45.599  21.198  1.00113.64      A    C  
ANISOU  411  CG2 THR A  81    17301  13879  11997   -707  -1579    582  A    C  
ATOM    412  OG1 THR A  81      50.227  43.502  22.369  1.00133.81      A    O  
ANISOU  412  OG1 THR A  81    19552  16509  14782   -475  -1581    425  A    O  
ATOM    413  N   ASP A  82      52.207  46.429  23.504  1.00120.26      A    N  
ANISOU  413  N   ASP A  82    18007  14524  13164  -1085  -2028    772  A    N  
ATOM    414  CA  ASP A  82      53.638  46.496  23.773  1.00126.20      A    C  
ANISOU  414  CA  ASP A  82    18487  15327  14136  -1302  -2113    912  A    C  
ATOM    415  C   ASP A  82      53.864  46.986  25.198  1.00129.45      A    C  
ANISOU  415  C   ASP A  82    19047  15585  14553  -1447  -2430    946  A    C  
ATOM    416  O   ASP A  82      53.000  47.637  25.780  1.00126.18      A    O  
ANISOU  416  O   ASP A  82    18988  15005  13950  -1430  -2541    855  A    O  
ATOM    417  CB  ASP A  82      54.349  47.411  22.777  1.00134.07      A    C  
ANISOU  417  CB  ASP A  82    19435  16366  15139  -1529  -2010   1047  A    C  
ATOM    418  CG  ASP A  82      55.862  47.303  22.867  1.00144.59      A    C  
ANISOU  418  CG  ASP A  82    20386  17808  16743  -1740  -2034   1182  A    C  
ATOM    419  OD1 ASP A  82      56.457  47.936  23.768  1.00142.51      A    O  
ANISOU  419  OD1 ASP A  82    20159  17435  16553  -1946  -2298   1282  A    O  
ATOM    420  OD2 ASP A  82      56.455  46.577  22.040  1.00152.51      A    O1-
ANISOU  420  OD2 ASP A  82    21041  19010  17897  -1707  -1783   1173  A    O1-
ATOM    421  N   ILE A  83      55.024  46.671  25.762  1.00142.21      A    N  
ANISOU  421  N   ILE A  83    20383  17259  16392  -1598  -2577   1067  A    N  
ATOM    422  CA  ILE A  83      55.340  47.111  27.115  1.00148.40      A    C  
ANISOU  422  CA  ILE A  83    21307  17926  17152  -1795  -2909   1116  A    C  
ATOM    423  C   ILE A  83      56.286  48.313  27.127  1.00142.07      A    C  
ANISOU  423  C   ILE A  83    20520  17054  16405  -2129  -3049   1254  A    C  
ATOM    424  O   ILE A  83      56.107  49.241  27.917  1.00146.53      A    O  
ANISOU  424  O   ILE A  83    21410  17445  16820  -2305  -3257   1224  A    O  
ATOM    425  CB  ILE A  83      55.960  45.962  27.953  1.00131.60      A    C  
ANISOU  425  CB  ILE A  83    18885  15886  15230  -1778  -3083   1199  A    C  
ATOM    426  CG1 ILE A  83      57.065  45.243  27.175  1.00135.14      A    C  
ANISOU  426  CG1 ILE A  83    18811  16492  16044  -1748  -2947   1314  A    C  
ATOM    427  CG2 ILE A  83      54.884  44.986  28.396  1.00127.86      A    C  
ANISOU  427  CG2 ILE A  83    18539  15412  14630  -1530  -3051   1067  A    C  
ATOM    428  CD1 ILE A  83      58.440  45.408  27.787  1.00140.02      A    C  
ANISOU  428  CD1 ILE A  83    19133  17137  16931  -2011  -3218   1522  A    C  
ATOM    429  N   SER A  84      57.270  48.320  26.234  1.00126.18      A    N  
ANISOU  429  N   SER A  84    18166  15174  14602  -2232  -2915   1387  A    N  
ATOM    430  CA  SER A  84      58.303  49.348  26.276  1.00123.98      A    C  
ANISOU  430  CA  SER A  84    17836  14856  14414  -2586  -3060   1548  A    C  
ATOM    431  C   SER A  84      57.769  50.736  25.907  1.00114.87      A    C  
ANISOU  431  C   SER A  84    17101  13503  13041  -2718  -3053   1529  A    C  
ATOM    432  O   SER A  84      58.463  51.741  26.076  1.00 98.33      A    O  
ANISOU  432  O   SER A  84    15069  11308  10982  -3037  -3213   1647  A    O  
ATOM    433  CB  SER A  84      59.455  48.968  25.340  1.00125.83      A    C  
ANISOU  433  CB  SER A  84    17564  15310  14935  -2664  -2862   1679  A    C  
ATOM    434  OG  SER A  84      60.538  49.875  25.456  1.00136.69      A    O  
ANISOU  434  OG  SER A  84    18831  16674  16432  -3034  -3017   1854  A    O  
ATOM    435  N   LEU A  85      56.529  50.791  25.430  1.00111.21      A    N  
ANISOU  435  N   LEU A  85    16918  12961  12377  -2478  -2895   1392  A    N  
ATOM    436  CA  LEU A  85      55.901  52.056  25.051  1.00110.41      A    C  
ANISOU  436  CA  LEU A  85    17207  12628  12116  -2550  -2908   1384  A    C  
ATOM    437  C   LEU A  85      54.551  52.325  25.721  1.00117.40      A    C  
ANISOU  437  C   LEU A  85    18497  13289  12818  -2346  -2981   1176  A    C  
ATOM    438  O   LEU A  85      54.002  53.418  25.604  1.00132.10      A    O  
ANISOU  438  O   LEU A  85    20689  14896  14605  -2385  -3034   1148  A    O  
ATOM    439  CB  LEU A  85      55.731  52.117  23.530  1.00115.49      A    C  
ANISOU  439  CB  LEU A  85    17784  13382  12715  -2501  -2638   1468  A    C  
ATOM    440  CG  LEU A  85      57.000  51.984  22.683  1.00117.84      A    C  
ANISOU  440  CG  LEU A  85    17697  13916  13161  -2729  -2486   1647  A    C  
ATOM    441  CD1 LEU A  85      56.620  52.022  21.222  1.00113.98      A    C  
ANISOU  441  CD1 LEU A  85    17227  13548  12533  -2691  -2210   1695  A    C  
ATOM    442  CD2 LEU A  85      58.020  53.071  23.000  1.00130.18      A    C  
ANISOU  442  CD2 LEU A  85    19272  15367  14825  -3126  -2685   1820  A    C  
ATOM    443  N   GLN A  86      54.010  51.324  26.405  1.00122.03      A    N  
ANISOU  443  N   GLN A  86    19045  13963  13358  -2131  -2973   1031  A    N  
ATOM    444  CA  GLN A  86      52.654  51.408  26.945  1.00125.08      A    C  
ANISOU  444  CA  GLN A  86    19754  14198  13573  -1913  -2970    810  A    C  
ATOM    445  C   GLN A  86      52.399  52.553  27.930  1.00111.69      A    C  
ANISOU  445  C   GLN A  86    18434  12211  11791  -2068  -3163    686  A    C  
ATOM    446  O   GLN A  86      51.385  53.245  27.824  1.00103.96      A    O  
ANISOU  446  O   GLN A  86    17739  11014  10746  -1931  -3116    547  A    O  
ATOM    447  CB  GLN A  86      52.287  50.095  27.644  1.00139.14      A    C  
ANISOU  447  CB  GLN A  86    21410  16143  15313  -1733  -2951    705  A    C  
ATOM    448  CG  GLN A  86      50.802  49.957  27.950  1.00134.64      A    C  
ANISOU  448  CG  GLN A  86    21089  15493  14574  -1476  -2862    479  A    C  
ATOM    449  CD  GLN A  86      50.488  48.705  28.744  1.00125.36      A    C  
ANISOU  449  CD  GLN A  86    19819  14472  13339  -1363  -2867    399  A    C  
ATOM    450  NE2 GLN A  86      50.130  47.633  28.051  1.00121.99      A    N  
ANISOU  450  NE2 GLN A  86    19183  14211  12957  -1138  -2693    406  A    N  
ATOM    451  OE1 GLN A  86      50.569  48.705  29.970  1.00122.82      A    O  
ANISOU  451  OE1 GLN A  86    19629  14118  12917  -1504  -3035    335  A    O  
ATOM    452  N   TYR A  87      53.312  52.754  28.876  1.00105.33      A    N  
ANISOU  452  N   TYR A  87    17624  11392  11005  -2356  -3384    728  A    N  
ATOM    453  CA  TYR A  87      53.066  53.680  29.977  1.00105.63      A    C  
ANISOU  453  CA  TYR A  87    18037  11178  10922  -2527  -3560    552  A    C  
ATOM    454  C   TYR A  87      52.840  55.126  29.554  1.00127.66      A    C  
ANISOU  454  C   TYR A  87    21118  13633  13755  -2609  -3577    522  A    C  
ATOM    455  O   TYR A  87      51.949  55.791  30.079  1.00138.35      A    O  
ANISOU  455  O   TYR A  87    22811  14728  15028  -2532  -3576    279  A    O  
ATOM    456  CB  TYR A  87      54.228  53.650  30.971  1.00105.51      A    C  
ANISOU  456  CB  TYR A  87    17948  11232  10910  -2884  -3832    645  A    C  
ATOM    457  CG  TYR A  87      55.565  54.072  30.406  1.00108.19      A    C  
ANISOU  457  CG  TYR A  87    18046  11612  11450  -3166  -3937    913  A    C  
ATOM    458  CD1 TYR A  87      56.303  53.218  29.601  1.00108.38      A    C  
ANISOU  458  CD1 TYR A  87    17612  11904  11664  -3111  -3836   1129  A    C  
ATOM    459  CD2 TYR A  87      56.076  55.340  30.659  1.00112.02      A    C  
ANISOU  459  CD2 TYR A  87    18755  11858  11948  -3496  -4115    931  A    C  
ATOM    460  CE1 TYR A  87      57.525  53.603  29.087  1.00113.90      A    C  
ANISOU  460  CE1 TYR A  87    18054  12666  12556  -3381  -3895   1359  A    C  
ATOM    461  CE2 TYR A  87      57.295  55.737  30.143  1.00114.44      A    C  
ANISOU  461  CE2 TYR A  87    18826  12216  12439  -3785  -4205   1186  A    C  
ATOM    462  CZ  TYR A  87      58.016  54.862  29.357  1.00110.01      A    C  
ANISOU  462  CZ  TYR A  87    17781  11956  12060  -3726  -4084   1401  A    C  
ATOM    463  OH  TYR A  87      59.233  55.241  28.838  1.00103.13      A    O  
ANISOU  463  OH  TYR A  87    16635  11166  11384  -4023  -4136   1642  A    O  
ATOM    464  N   LEU A  88      53.642  55.615  28.616  1.00137.09      A    N  
ANISOU  464  N   LEU A  88    22176  14820  15092  -2774  -3588    765  A    N  
ATOM    465  CA  LEU A  88      53.450  56.959  28.081  1.00135.85      A    C  
ANISOU  465  CA  LEU A  88    22288  14328  15001  -2863  -3623    799  A    C  
ATOM    466  C   LEU A  88      52.134  57.085  27.306  1.00122.21      A    C  
ANISOU  466  C   LEU A  88    20695  12473  13265  -2508  -3453    721  A    C  
ATOM    467  O   LEU A  88      51.474  58.126  27.355  1.00126.84      A    O  
ANISOU  467  O   LEU A  88    21599  12694  13903  -2465  -3506    614  A    O  
ATOM    468  CB  LEU A  88      54.644  57.361  27.212  1.00148.13      A    C  
ANISOU  468  CB  LEU A  88    23642  15954  16686  -3160  -3662   1113  A    C  
ATOM    469  CG  LEU A  88      55.004  56.540  25.980  1.00149.71      A    C  
ANISOU  469  CG  LEU A  88    23462  16489  16930  -3075  -3450   1325  A    C  
ATOM    470  CD1 LEU A  88      54.423  57.192  24.745  1.00166.36      A    C  
ANISOU  470  CD1 LEU A  88    25716  18462  19031  -2999  -3342   1444  A    C  
ATOM    471  CD2 LEU A  88      56.512  56.411  25.858  1.00138.46      A    C  
ANISOU  471  CD2 LEU A  88    21698  15278  15635  -3412  -3506   1547  A    C  
ATOM    472  N   ALA A  89      51.754  56.015  26.613  1.00111.06      A    N  
ANISOU  472  N   ALA A  89    19036  11349  11815  -2257  -3263    769  A    N  
ATOM    473  CA  ALA A  89      50.538  56.005  25.806  1.00109.50      A    C  
ANISOU  473  CA  ALA A  89    18915  11086  11602  -1939  -3124    730  A    C  
ATOM    474  C   ALA A  89      49.315  56.264  26.677  1.00113.20      A    C  
ANISOU  474  C   ALA A  89    19646  11322  12041  -1708  -3127    418  A    C  
ATOM    475  O   ALA A  89      48.371  56.921  26.241  1.00122.36      A    O  
ANISOU  475  O   ALA A  89    20979  12235  13278  -1521  -3112    372  A    O  
ATOM    476  CB  ALA A  89      50.388  54.679  25.071  1.00100.33      A    C  
ANISOU  476  CB  ALA A  89    17444  10299  10379  -1744  -2925    792  A    C  
ATOM    477  N   ILE A  90      49.333  55.729  27.897  1.00100.75      A    N  
ANISOU  477  N   ILE A  90    18083   9836  10360  -1731  -3146    212  A    N  
ATOM    478  CA  ILE A  90      48.247  55.921  28.856  1.00 98.45      A    C  
ANISOU  478  CA  ILE A  90    18030   9373  10005  -1562  -3106   -126  A    C  
ATOM    479  C   ILE A  90      48.228  57.396  29.242  1.00111.91      A    C  
ANISOU  479  C   ILE A  90    20070  10638  11812  -1703  -3231   -247  A    C  
ATOM    480  O   ILE A  90      47.176  58.023  29.215  1.00133.06      A    O  
ANISOU  480  O   ILE A  90    22931  13035  14590  -1480  -3171   -434  A    O  
ATOM    481  CB  ILE A  90      48.395  55.040  30.116  1.00104.08      A    C  
ANISOU  481  CB  ILE A  90    18711  10304  10529  -1644  -3116   -289  A    C  
ATOM    482  CG1 ILE A  90      48.331  53.556  29.761  1.00 98.98      A    C  
ANISOU  482  CG1 ILE A  90    17746  10034   9826  -1480  -3000   -181  A    C  
ATOM    483  CG2 ILE A  90      47.277  55.347  31.082  1.00 99.82      A    C  
ANISOU  483  CG2 ILE A  90    18436   9595   9895  -1515  -3033   -661  A    C  
ATOM    484  CD1 ILE A  90      49.445  52.755  30.428  1.00 91.52      A    C  
ANISOU  484  CD1 ILE A  90    16623   9331   8822  -1719  -3132    -58  A    C  
ATOM    485  N   ASP A  91      49.388  57.936  29.628  1.00115.23      A    N  
ANISOU  485  N   ASP A  91    20558  10987  12236  -2073  -3411   -151  A    N  
ATOM    486  CA  ASP A  91      49.493  59.336  30.061  1.00123.99      A    C  
ANISOU  486  CA  ASP A  91    22009  11657  13445  -2262  -3550   -278  A    C  
ATOM    487  C   ASP A  91      49.121  60.301  28.949  1.00126.27      A    C  
ANISOU  487  C   ASP A  91    22394  11618  13966  -2152  -3568   -123  A    C  
ATOM    488  O   ASP A  91      48.360  61.251  29.151  1.00124.69      A    O  
ANISOU  488  O   ASP A  91    22466  10998  13913  -2030  -3581   -328  A    O  
ATOM    489  CB  ASP A  91      50.911  59.661  30.524  1.00127.21      A    C  
ANISOU  489  CB  ASP A  91    22424  12090  13818  -2721  -3764   -140  A    C  
ATOM    490  CG  ASP A  91      51.007  59.827  32.025  1.00146.23      A    C  
ANISOU  490  CG  ASP A  91    25076  14432  16054  -2933  -3859   -449  A    C  
ATOM    491  OD1 ASP A  91      49.972  60.143  32.659  1.00155.45      A    O  
ANISOU  491  OD1 ASP A  91    26500  15391  17173  -2758  -3748   -812  A    O  
ATOM    492  OD2 ASP A  91      52.116  59.643  32.572  1.00155.56      A    O1-
ANISOU  492  OD2 ASP A  91    26183  15778  17144  -3288  -4043   -334  A    O1-
ATOM    493  N   ARG A  92      49.662  60.039  27.766  1.00121.42      A    N  
ANISOU  493  N   ARG A  92    21551  11195  13391  -2202  -3569    242  A    N  
ATOM    494  CA  ARG A  92      49.418  60.887  26.603  1.00116.83      A    C  
ANISOU  494  CA  ARG A  92    21053  10353  12984  -2162  -3619    474  A    C  
ATOM    495  C   ARG A  92      48.039  60.688  25.981  1.00112.63      A    C  
ANISOU  495  C   ARG A  92    20508   9770  12517  -1739  -3503    422  A    C  
ATOM    496  O   ARG A  92      47.408  61.650  25.555  1.00120.29      A    O  
ANISOU  496  O   ARG A  92    21670  10344  13689  -1627  -3590    456  A    O  
ATOM    497  CB  ARG A  92      50.518  60.676  25.567  1.00123.94      A    C  
ANISOU  497  CB  ARG A  92    21722  11518  13853  -2424  -3636    873  A    C  
ATOM    498  CG  ARG A  92      51.774  61.424  25.968  1.00132.50      A    C  
ANISOU  498  CG  ARG A  92    22885  12475  14983  -2872  -3816    978  A    C  
ATOM    499  CD  ARG A  92      51.594  62.905  25.611  1.00139.21      A    C  
ANISOU  499  CD  ARG A  92    24065  12798  16028  -2986  -3982   1070  A    C  
ATOM    500  NE  ARG A  92      52.053  63.783  26.681  1.00150.28      A    N  
ANISOU  500  NE  ARG A  92    25735  13866  17499  -3254  -4157    883  A    N  
ATOM    501  CZ  ARG A  92      53.301  64.230  26.792  1.00154.02      A    C  
ANISOU  501  CZ  ARG A  92    26196  14341  17985  -3703  -4308   1058  A    C  
ATOM    502  NH1 ARG A  92      54.228  63.821  25.942  1.00148.43      A    N1+
ANISOU  502  NH1 ARG A  92    25183  13980  17234  -3916  -4272   1407  A    N1+
ATOM    503  NH2 ARG A  92      53.633  65.056  27.774  1.00155.38      A    N  
ANISOU  503  NH2 ARG A  92    26646  14184  18207  -3955  -4481    863  A    N  
ATOM    504  N   GLY A  93      47.566  59.450  25.935  1.00108.80      A    N  
ANISOU  504  N   GLY A  93    19790   9663  11887  -1510  -3331    352  A    N  
ATOM    505  CA  GLY A  93      46.332  59.143  25.234  1.00102.88      A    C  
ANISOU  505  CA  GLY A  93    18976   8931  11183  -1144  -3234    347  A    C  
ATOM    506  C   GLY A  93      45.096  59.946  25.601  1.00 98.46      A    C  
ANISOU  506  C   GLY A  93    18627   7951  10833   -866  -3255    101  A    C  
ATOM    507  O   GLY A  93      44.334  60.353  24.726  1.00 94.85      A    O  
ANISOU  507  O   GLY A  93    18182   7318  10537   -669  -3309    241  A    O  
ATOM    508  N   PHE A  94      44.891  60.177  26.891  1.00119.08      A    N  
ANISOU  508  N   PHE A  94    21394  10402  13449   -858  -3215   -269  A    N  
ATOM    509  CA  PHE A  94      43.728  60.933  27.344  1.00135.46      A    C  
ANISOU  509  CA  PHE A  94    23644  12070  15754   -585  -3184   -576  A    C  
ATOM    510  C   PHE A  94      43.809  62.416  26.993  1.00142.68      A    C  
ANISOU  510  C   PHE A  94    24808  12425  16980   -651  -3381   -480  A    C  
ATOM    511  O   PHE A  94      42.848  62.989  26.482  1.00144.07      A    O  
ANISOU  511  O   PHE A  94    25015  12285  17442   -367  -3425   -467  A    O  
ATOM    512  CB  PHE A  94      43.546  60.758  28.851  1.00147.61      A    C  
ANISOU  512  CB  PHE A  94    25300  13622  17162   -611  -3049  -1031  A    C  
ATOM    513  CG  PHE A  94      43.274  59.343  29.257  1.00145.37      A    C  
ANISOU  513  CG  PHE A  94    24798  13831  16606   -523  -2868  -1131  A    C  
ATOM    514  CD1 PHE A  94      42.021  58.784  29.085  1.00146.95      A    C  
ANISOU  514  CD1 PHE A  94    24845  14139  16852   -163  -2701  -1262  A    C  
ATOM    515  CD2 PHE A  94      44.283  58.567  29.793  1.00145.14      A    C  
ANISOU  515  CD2 PHE A  94    24701  14145  16301   -809  -2889  -1068  A    C  
ATOM    516  CE1 PHE A  94      41.782  57.479  29.449  1.00151.94      A    C  
ANISOU  516  CE1 PHE A  94    25289  15203  17237   -111  -2547  -1335  A    C  
ATOM    517  CE2 PHE A  94      44.053  57.265  30.156  1.00151.13      A    C  
ANISOU  517  CE2 PHE A  94    25270  15314  16838   -737  -2753  -1126  A    C  
ATOM    518  CZ  PHE A  94      42.802  56.720  29.987  1.00151.72      A    C  
ANISOU  518  CZ  PHE A  94    25222  15485  16940   -397  -2577  -1263  A    C  
ATOM    519  N   GLU A  95      44.940  63.043  27.306  1.00151.94      A    N  
ANISOU  519  N   GLU A  95    26154  13453  18123  -1030  -3519   -409  A    N  
ATOM    520  CA  GLU A  95      45.137  64.461  27.011  1.00160.26      A    C  
ANISOU  520  CA  GLU A  95    27472  13949  19472  -1152  -3727   -300  A    C  
ATOM    521  C   GLU A  95      45.152  64.728  25.502  1.00148.19      A    C  
ANISOU  521  C   GLU A  95    25865  12377  18064  -1142  -3878    194  A    C  
ATOM    522  O   GLU A  95      44.551  65.694  25.033  1.00144.98      A    O  
ANISOU  522  O   GLU A  95    25608  11495  17983   -998  -4024    280  A    O  
ATOM    523  CB  GLU A  95      46.424  64.978  27.664  1.00180.64      A    C  
ANISOU  523  CB  GLU A  95    30236  16440  21959  -1617  -3851   -311  A    C  
ATOM    524  CG  GLU A  95      47.652  64.106  27.464  1.00193.07      A    C  
ANISOU  524  CG  GLU A  95    31583  18539  23236  -1939  -3857    -38  A    C  
ATOM    525  CD  GLU A  95      48.880  64.677  28.145  1.00210.15      A    C  
ANISOU  525  CD  GLU A  95    33906  20596  25346  -2405  -4012    -45  A    C  
ATOM    526  OE1 GLU A  95      48.723  65.543  29.029  1.00218.77      A    O  
ANISOU  526  OE1 GLU A  95    35305  21274  26544  -2477  -4073   -360  A    O  
ATOM    527  OE2 GLU A  95      50.003  64.262  27.801  1.00214.64      A    O1-
ANISOU  527  OE2 GLU A  95    34283  21494  25778  -2707  -4068    248  A    O1-
ATOM    528  N   ILE A  96      45.847  63.872  24.754  1.00144.64      A    N  
ANISOU  528  N   ILE A  96    25184  12418  17354  -1310  -3843    515  A    N  
ATOM    529  CA  ILE A  96      45.909  63.974  23.294  1.00136.06      A    C  
ANISOU  529  CA  ILE A  96    24020  11397  16280  -1358  -3948    981  A    C  
ATOM    530  C   ILE A  96      44.512  63.868  22.701  1.00130.55      A    C  
ANISOU  530  C   ILE A  96    23259  10610  15733   -938  -3946    991  A    C  
ATOM    531  O   ILE A  96      44.148  64.615  21.794  1.00132.84      A    O  
ANISOU  531  O   ILE A  96    23646  10607  16219   -905  -4142   1288  A    O  
ATOM    532  CB  ILE A  96      46.802  62.881  22.678  1.00130.39      A    C  
ANISOU  532  CB  ILE A  96    23026  11283  15233  -1572  -3826   1221  A    C  
ATOM    533  CG1 ILE A  96      48.271  63.136  23.016  1.00157.83      A    C  
ANISOU  533  CG1 ILE A  96    26521  14821  18624  -2025  -3879   1317  A    C  
ATOM    534  CG2 ILE A  96      46.624  62.827  21.171  1.00109.88      A    C  
ANISOU  534  CG2 ILE A  96    20350   8817  12581  -1586  -3876   1633  A    C  
ATOM    535  CD1 ILE A  96      49.214  62.125  22.405  1.00163.97      A    C  
ANISOU  535  CD1 ILE A  96    26990  16161  19150  -2230  -3741   1536  A    C  
ATOM    536  N   PHE A  97      43.738  62.928  23.231  1.00131.30      A    N  
ANISOU  536  N   PHE A  97    23183  10963  15740   -637  -3746    686  A    N  
ATOM    537  CA  PHE A  97      42.366  62.710  22.796  1.00127.45      A    C  
ANISOU  537  CA  PHE A  97    22585  10439  15400   -230  -3727    652  A    C  
ATOM    538  C   PHE A  97      41.561  63.983  22.989  1.00126.68      A    C  
ANISOU  538  C   PHE A  97    22688   9696  15750    -16  -3887    545  A    C  
ATOM    539  O   PHE A  97      40.910  64.465  22.072  1.00123.71      A    O  
ANISOU  539  O   PHE A  97    22311   9092  15601    138  -4074    814  A    O  
ATOM    540  CB  PHE A  97      41.741  61.558  23.588  1.00129.04      A    C  
ANISOU  540  CB  PHE A  97    22592  10992  15445      9  -3468    283  A    C  
ATOM    541  CG  PHE A  97      40.245  61.467  23.471  1.00120.73      A    C  
ANISOU  541  CG  PHE A  97    21427   9836  14609    438  -3430    138  A    C  
ATOM    542  CD1 PHE A  97      39.655  60.828  22.396  1.00103.37      A    C  
ANISOU  542  CD1 PHE A  97    19029   7904  12344    580  -3460    392  A    C  
ATOM    543  CD2 PHE A  97      39.427  62.011  24.450  1.00128.61      A    C  
ANISOU  543  CD2 PHE A  97    22506  10482  15879    685  -3353   -272  A    C  
ATOM    544  CE1 PHE A  97      38.283  60.735  22.293  1.00102.57      A    C  
ANISOU  544  CE1 PHE A  97    18789   7722  12462    960  -3449    275  A    C  
ATOM    545  CE2 PHE A  97      38.054  61.925  24.353  1.00128.23      A    C  
ANISOU  545  CE2 PHE A  97    22301  10349  16073   1085  -3304   -412  A    C  
ATOM    546  CZ  PHE A  97      37.480  61.282  23.272  1.00113.90      A    C  
ANISOU  546  CZ  PHE A  97    20264   8806  14207   1224  -3369   -122  A    C  
ATOM    547  N   ASP A  98      41.656  64.547  24.184  1.00141.37      A    N  
ANISOU  547  N   ASP A  98    24727  11245  17742    -30  -3827    157  A    N  
ATOM    548  CA  ASP A  98      40.879  65.721  24.549  1.00155.47      A    C  
ANISOU  548  CA  ASP A  98    26695  12383  19992    203  -3922    -57  A    C  
ATOM    549  C   ASP A  98      41.285  66.965  23.757  1.00161.17      A    C  
ANISOU  549  C   ASP A  98    27639  12603  20995     28  -4246    330  A    C  
ATOM    550  O   ASP A  98      40.496  67.902  23.613  1.00153.48      A    O  
ANISOU  550  O   ASP A  98    26762  11070  20483    279  -4399    310  A    O  
ATOM    551  CB  ASP A  98      41.003  65.977  26.051  1.00155.00      A    C  
ANISOU  551  CB  ASP A  98    26806  12153  19936    159  -3746   -604  A    C  
ATOM    552  CG  ASP A  98      40.015  65.156  26.857  1.00148.96      A    C  
ANISOU  552  CG  ASP A  98    25863  11637  19096    475  -3449  -1049  A    C  
ATOM    553  OD1 ASP A  98      38.981  64.748  26.284  1.00150.21      A    O  
ANISOU  553  OD1 ASP A  98    25790  11894  19388    818  -3415   -982  A    O  
ATOM    554  OD2 ASP A  98      40.271  64.905  28.054  1.00144.29      A    O1-
ANISOU  554  OD2 ASP A  98    25363  11163  18297    350  -3259  -1448  A    O1-
ATOM    555  N   ARG A  99      42.518  66.978  23.257  1.00170.27      A    N  
ANISOU  555  N   ARG A  99    28858  13942  21894   -408  -4352    684  A    N  
ATOM    556  CA  ARG A  99      42.987  68.076  22.418  1.00184.69      A    C  
ANISOU  556  CA  ARG A  99    30892  15358  23923   -647  -4660   1117  A    C  
ATOM    557  C   ARG A  99      42.251  68.487  21.139  1.00201.49      A    C  
ANISOU  557  C   ARG A  99    32998  17277  26282   -483  -4915   1561  A    C  
ATOM    558  O   ARG A  99      41.921  69.658  20.966  1.00225.17      A    O  
ANISOU  558  O   ARG A  99    36203  19638  29712   -419  -5168   1674  A    O  
ATOM    559  CB  ARG A  99      44.494  67.945  22.164  1.00180.45      A    C  
ANISOU  559  CB  ARG A  99    30391  15126  23045  -1181  -4683   1396  A    C  
ATOM    560  CG  ARG A  99      45.110  69.072  21.338  1.00181.82      A    C  
ANISOU  560  CG  ARG A  99    30793  14913  23378  -1517  -4986   1859  A    C  
ATOM    561  CD  ARG A  99      45.042  70.407  22.070  1.00181.31      A    C  
ANISOU  561  CD  ARG A  99    31057  14092  23740  -1527  -5153   1647  A    C  
ATOM    562  NE  ARG A  99      45.607  70.331  23.415  1.00184.47      A    N  
ANISOU  562  NE  ARG A  99    31539  14517  24035  -1665  -4987   1174  A    N  
ATOM    563  CZ  ARG A  99      46.890  70.531  23.704  1.00178.87      A    C  
ANISOU  563  CZ  ARG A  99    30928  13894  23141  -2148  -5029   1250  A    C  
ATOM    564  NH1 ARG A  99      47.754  70.821  22.740  1.00172.44      A    N1+
ANISOU  564  NH1 ARG A  99    30128  13156  22236  -2536  -5194   1764  A    N1+
ATOM    565  NH2 ARG A  99      47.311  70.441  24.958  1.00176.22      A    N  
ANISOU  565  NH2 ARG A  99    30670  13585  22699  -2268  -4911    818  A    N  
ATOM    566  N   MET A 100      42.010  67.533  20.241  1.00194.12      A    N  
ANISOU  566  N   MET A 100    31828  16862  25065   -437  -4868   1822  A    N  
ATOM    567  CA  MET A 100      41.096  67.803  19.099  1.00200.84      A    C  
ANISOU  567  CA  MET A 100    32636  17559  26117   -239  -5119   2207  A    C  
ATOM    568  C   MET A 100      39.494  67.493  19.169  1.00172.69      A    C  
ANISOU  568  C   MET A 100    28855  13915  22845    327  -5101   1997  A    C  
ATOM    569  O   MET A 100      38.609  67.830  18.382  1.00181.96      A    O  
ANISOU  569  O   MET A 100    29978  14871  24287    541  -5353   2276  A    O  
ATOM    570  CB  MET A 100      41.409  66.841  17.948  1.00200.00      A    C  
ANISOU  570  CB  MET A 100    32360  18091  25540   -446  -5085   2593  A    C  
ATOM    571  CG  MET A 100      40.624  67.011  16.668  1.00198.68      A    C  
ANISOU  571  CG  MET A 100    32304  18139  25047   -992  -5127   2975  A    C  
ATOM    572  SD  MET A 100      40.991  68.575  15.848  1.00406.58      A    S  
ANISOU  572  SD  MET A 100    58981  43801  51702  -1262  -5567   3484  A    S  
ATOM    573  CE  MET A 100      42.609  68.232  15.155  1.00173.35      A    C  
ANISOU  573  CE  MET A 100    29376  14248  22240  -1042  -5855   3925  A    C  
ATOM    574  N   VAL A 101      39.236  66.929  20.347  1.00155.27      A    N  
ANISOU  574  N   VAL A 101    26538  11850  20606    532  -4788   1444  A    N  
ATOM    575  CA  VAL A 101      37.861  66.712  20.785  1.00147.15      A    C  
ANISOU  575  CA  VAL A 101    25312  10720  19877   1031  -4686   1106  A    C  
ATOM    576  C   VAL A 101      37.494  68.182  20.988  1.00167.04      A    C  
ANISOU  576  C   VAL A 101    28041  12424  23004   1184  -4920   1070  A    C  
ATOM    577  O   VAL A 101      36.368  68.588  20.701  1.00178.58      A    O  
ANISOU  577  O   VAL A 101    29386  13544  24922   1564  -5072   1099  A    O  
ATOM    578  CB  VAL A 101      37.445  65.882  22.024  1.00136.73      A    C  
ANISOU  578  CB  VAL A 101    23833   9675  18441   1245  -4299    507  A    C  
ATOM    579  CG1 VAL A 101      35.964  66.033  22.300  1.00129.62      A    C  
ANISOU  579  CG1 VAL A 101    22745   8518  17987   1750  -4256    230  A    C  
ATOM    580  CG2 VAL A 101      37.762  64.420  21.803  1.00142.96      A    C  
ANISOU  580  CG2 VAL A 101    24414  11213  18691   1115  -4097    562  A    C  
ATOM    581  N   SER A 102      38.454  68.982  21.450  1.00178.48      A    N  
ANISOU  581  N   SER A 102    29786  13543  24486    882  -4967   1021  A    N  
ATOM    582  CA  SER A 102      38.236  70.411  21.680  1.00192.44      A    C  
ANISOU  582  CA  SER A 102    31796  14486  26836    981  -5188    967  A    C  
ATOM    583  C   SER A 102      37.815  71.119  20.390  1.00194.01      A    C  
ANISOU  583  C   SER A 102    31934  14447  27333   1024  -5561   1545  A    C  
ATOM    584  O   SER A 102      37.098  72.123  20.425  1.00184.36      A    O  
ANISOU  584  O   SER A 102    30629  12764  26657   1280  -5652   1484  A    O  
ATOM    585  CB  SER A 102      39.492  71.069  22.259  1.00196.88      A    C  
ANISOU  585  CB  SER A 102    32687  14824  27294    547  -5196    887  A    C  
ATOM    586  OG  SER A 102      39.316  72.461  22.446  1.00195.62      A    O  
ANISOU  586  OG  SER A 102    32636  14849  26844     86  -5409   1459  A    O  
ATOM    587  N   SER A 103      38.272  70.591  19.257  1.00198.68      A    N  
ANISOU  587  N   SER A 103    32515  15444  27530    744  -5726   2091  A    N  
ATOM    588  CA  SER A 103      37.929  71.130  17.940  1.00205.11      A    C  
ANISOU  588  CA  SER A 103    33226  16232  28475    695  -6045   2665  A    C  
ATOM    589  C   SER A 103      36.433  71.062  17.631  1.00208.56      A    C  
ANISOU  589  C   SER A 103    33356  16588  29297   1195  -6133   2651  A    C  
ATOM    590  O   SER A 103      35.947  71.741  16.725  1.00210.41      A    O  
ANISOU  590  O   SER A 103    33491  16666  29789   1226  -6417   3049  A    O  
ATOM    591  CB  SER A 103      38.699  70.381  16.852  1.00197.92      A    C  
ANISOU  591  CB  SER A 103    32345  15894  26961    272  -6115   3166  A    C  
ATOM    592  OG  SER A 103      40.092  70.421  17.091  1.00187.76      A    O  
ANISOU  592  OG  SER A 103    31286  14713  25341   -200  -6025   3202  A    O  
ATOM    593  N   GLY A 104      35.709  70.246  18.389  1.00206.10      A    N  
ANISOU  593  N   GLY A 104    32886  16396  29026   1566  -5892   2196  A    N  
ATOM    594  CA  GLY A 104      34.273  70.125  18.223  1.00199.91      A    C  
ANISOU  594  CA  GLY A 104    31766  15559  28633   2050  -5936   2124  A    C  
ATOM    595  C   GLY A 104      33.823  69.017  17.289  1.00183.41      A    C  
ANISOU  595  C   GLY A 104    29481  14013  26194   2070  -6034   2449  A    C  
ATOM    596  O   GLY A 104      32.628  68.874  17.034  1.00182.02      A    O  
ANISOU  596  O   GLY A 104    28996  13842  26321   2433  -6110   2450  A    O  
ATOM    597  N   ILE A 105      34.762  68.234  16.769  1.00173.96      A    N  
ANISOU  597  N   ILE A 105    28442  13290  24367   1670  -6019   2718  A    N  
ATOM    598  CA  ILE A 105      34.376  67.084  15.967  1.00182.35      A    C  
ANISOU  598  CA  ILE A 105    29272  14997  25017   1649  -5997   2921  A    C  
ATOM    599  C   ILE A 105      33.902  65.968  16.885  1.00181.84      A    C  
ANISOU  599  C   ILE A 105    28932  15355  24805   1907  -5563   2355  A    C  
ATOM    600  O   ILE A 105      34.591  65.615  17.846  1.00185.16      A    O  
ANISOU  600  O   ILE A 105    29413  15940  24998   1798  -5218   1955  A    O  
ATOM    601  CB  ILE A 105      35.528  66.563  15.063  1.00179.93      A    C  
ANISOU  601  CB  ILE A 105    29113  15213  24041   1103  -5996   3321  A    C  
ATOM    602  CG1 ILE A 105      35.156  65.190  14.482  1.00176.36      A    C  
ANISOU  602  CG1 ILE A 105    28411  15470  23127   1099  -5852   3354  A    C  
ATOM    603  CG2 ILE A 105      36.851  66.511  15.821  1.00158.98      A    C  
ANISOU  603  CG2 ILE A 105    26631  12669  21104    786  -5701   3072  A    C  
ATOM    604  CD1 ILE A 105      36.274  64.465  13.769  1.00157.27      A    C  
ANISOU  604  CD1 ILE A 105    26083  13633  20041    608  -5718   3585  A    C  
ATOM    605  N   SER A 106      32.716  65.431  16.605  1.00178.62      A    N  
ANISOU  605  N   SER A 106    28221  15112  24535   2231  -5605   2339  A    N  
ATOM    606  CA  SER A 106      32.217  64.313  17.388  1.00181.76      A    C  
ANISOU  606  CA  SER A 106    28351  15942  24769   2441  -5208   1850  A    C  
ATOM    607  C   SER A 106      33.226  63.214  17.140  1.00181.28      A    C  
ANISOU  607  C   SER A 106    28346  16534  23998   2047  -4989   1910  A    C  
ATOM    608  O   SER A 106      33.532  62.906  15.990  1.00181.45      A    O  
ANISOU  608  O   SER A 106    28408  16845  23688   1783  -5170   2354  A    O  
ATOM    609  CB  SER A 106      30.805  63.896  16.973  1.00182.31      A    C  
ANISOU  609  CB  SER A 106    28069  16115  25085   2799  -5326   1894  A    C  
ATOM    610  OG  SER A 106      30.303  62.871  17.817  1.00172.84      A    O  
ANISOU  610  OG  SER A 106    26617  15297  23757   2989  -4928   1403  A    O  
ATOM    611  N   PRO A 107      33.755  62.628  18.221  1.00174.18      A    N  
ANISOU  611  N   PRO A 107    27450  15859  22870   1996  -4600   1460  A    N  
ATOM    612  CA  PRO A 107      34.913  61.743  18.112  1.00164.84      A    C  
ANISOU  612  CA  PRO A 107    26337  15193  21102   1616  -4402   1504  A    C  
ATOM    613  C   PRO A 107      34.614  60.576  17.187  1.00165.98      A    C  
ANISOU  613  C   PRO A 107    26292  15899  20877   1558  -4386   1703  A    C  
ATOM    614  O   PRO A 107      33.450  60.223  16.995  1.00171.86      A    O  
ANISOU  614  O   PRO A 107    26812  16709  21778   1841  -4437   1665  A    O  
ATOM    615  CB  PRO A 107      35.134  61.289  19.560  1.00156.94      A    C  
ANISOU  615  CB  PRO A 107    25307  14287  20034   1683  -4031    954  A    C  
ATOM    616  CG  PRO A 107      33.773  61.394  20.183  1.00158.10      A    C  
ANISOU  616  CG  PRO A 107    25259  14227  20586   2125  -3959    617  A    C  
ATOM    617  CD  PRO A 107      33.203  62.637  19.587  1.00168.60      A    C  
ANISOU  617  CD  PRO A 107    26645  14989  22425   2297  -4315    880  A    C  
ATOM    618  N   ASN A 108      35.654  60.014  16.590  1.00159.59      A    N  
ANISOU  618  N   ASN A 108    25562  15476  19598   1184  -4318   1909  A    N  
ATOM    619  CA  ASN A 108      35.476  58.912  15.669  1.00141.34      A    C  
ANISOU  619  CA  ASN A 108    23107  13688  16906   1084  -4281   2071  A    C  
ATOM    620  C   ASN A 108      35.168  57.628  16.423  1.00134.22      A    C  
ANISOU  620  C   ASN A 108    21985  13167  15844   1240  -3945   1658  A    C  
ATOM    621  O   ASN A 108      35.611  57.451  17.554  1.00136.34      A    O  
ANISOU  621  O   ASN A 108    22263  13422  16118   1263  -3706   1315  A    O  
ATOM    622  CB  ASN A 108      36.730  58.753  14.807  1.00136.98      A    C  
ANISOU  622  CB  ASN A 108    22705  13414  15927    628  -4269   2378  A    C  
ATOM    623  CG  ASN A 108      36.589  57.672  13.767  1.00141.58      A    C  
ANISOU  623  CG  ASN A 108    23176  14520  16098    488  -4219   2529  A    C  
ATOM    624  ND2 ASN A 108      37.715  57.120  13.334  1.00138.13      A    N  
ANISOU  624  ND2 ASN A 108    22785  14442  15257    139  -4031   2596  A    N  
ATOM    625  OD1 ASN A 108      35.480  57.333  13.354  1.00150.39      A    O  
ANISOU  625  OD1 ASN A 108    24156  15717  17270    684  -4343   2571  A    O  
ATOM    626  N   GLU A 109      34.400  56.743  15.794  1.00137.19      A    N  
ANISOU  626  N   GLU A 109    22178  13879  16070   1319  -3952   1709  A    N  
ATOM    627  CA  GLU A 109      34.071  55.446  16.377  1.00127.92      A    C  
ANISOU  627  CA  GLU A 109    20798  13078  14727   1433  -3658   1366  A    C  
ATOM    628  C   GLU A 109      35.329  54.680  16.757  1.00113.70      A    C  
ANISOU  628  C   GLU A 109    19049  11572  12580   1179  -3378   1229  A    C  
ATOM    629  O   GLU A 109      35.419  54.098  17.837  1.00105.14      A    O  
ANISOU  629  O   GLU A 109    17889  10575  11485   1264  -3137    887  A    O  
ATOM    630  CB  GLU A 109      33.212  54.633  15.397  1.00142.25      A    C  
ANISOU  630  CB  GLU A 109    22447  15220  16381   1464  -3751   1515  A    C  
ATOM    631  CG  GLU A 109      32.795  53.237  15.872  1.00155.86      A    C  
ANISOU  631  CG  GLU A 109    23960  17326  17934   1559  -3475   1197  A    C  
ATOM    632  CD  GLU A 109      33.845  52.170  15.569  1.00157.12      A    C  
ANISOU  632  CD  GLU A 109    24160  17892  17647   1268  -3251   1176  A    C  
ATOM    633  OE1 GLU A 109      34.498  52.257  14.508  1.00169.19      A    O  
ANISOU  633  OE1 GLU A 109    25812  19548  18925    993  -3341   1463  A    O  
ATOM    634  OE2 GLU A 109      34.022  51.243  16.384  1.00140.68      A    O1-
ANISOU  634  OE2 GLU A 109    21982  15997  15473   1306  -2983    875  A    O1-
ATOM    635  N   ALA A 110      36.304  54.698  15.859  1.00107.25      A    N  
ANISOU  635  N   ALA A 110    18352  10909  11491    853  -3418   1510  A    N  
ATOM    636  CA  ALA A 110      37.581  54.046  16.099  1.00102.74      A    C  
ANISOU  636  CA  ALA A 110    17791  10599  10646    606  -3172   1418  A    C  
ATOM    637  C   ALA A 110      38.348  54.698  17.251  1.00108.22      A    C  
ANISOU  637  C   ALA A 110    18591  11020  11507    574  -3112   1252  A    C  
ATOM    638  O   ALA A 110      38.956  54.009  18.070  1.00102.36      A    O  
ANISOU  638  O   ALA A 110    17782  10442  10666    531  -2897   1018  A    O  
ATOM    639  CB  ALA A 110      38.415  54.057  14.830  1.00105.03      A    C  
ANISOU  639  CB  ALA A 110    18171  11098  10637    255  -3214   1751  A    C  
ATOM    640  N   SER A 111      38.310  56.027  17.316  1.00120.48      A    N  
ANISOU  640  N   SER A 111    20317  12139  13321    581  -3326   1383  A    N  
ATOM    641  CA  SER A 111      39.050  56.771  18.337  1.00123.50      A    C  
ANISOU  641  CA  SER A 111    20841  12227  13856    505  -3302   1236  A    C  
ATOM    642  C   SER A 111      38.482  56.525  19.732  1.00116.81      A    C  
ANISOU  642  C   SER A 111    19930  11291  13161    760  -3144    801  A    C  
ATOM    643  O   SER A 111      39.230  56.419  20.703  1.00124.97      A    O  
ANISOU  643  O   SER A 111    21012  12337  14135    646  -3014    597  A    O  
ATOM    644  CB  SER A 111      39.056  58.268  18.033  1.00135.12      A    C  
ANISOU  644  CB  SER A 111    22530  13206  15603    457  -3581   1473  A    C  
ATOM    645  OG  SER A 111      37.745  58.766  17.871  1.00153.17      A    O  
ANISOU  645  OG  SER A 111    24786  15208  18202    773  -3759   1486  A    O  
ATOM    646  N   VAL A 112      37.159  56.457  19.835  1.00102.43      A    N  
ANISOU  646  N   VAL A 112    17996   9390  11531   1082  -3162    667  A    N  
ATOM    647  CA  VAL A 112      36.512  56.215  21.118  1.00102.77      A    C  
ANISOU  647  CA  VAL A 112    17968   9380  11699   1309  -2978    241  A    C  
ATOM    648  C   VAL A 112      36.894  54.829  21.641  1.00114.54      A    C  
ANISOU  648  C   VAL A 112    19333  11320  12868   1220  -2730     62  A    C  
ATOM    649  O   VAL A 112      37.020  54.624  22.847  1.00126.78      A    O  
ANISOU  649  O   VAL A 112    20908  12873  14391   1223  -2570   -243  A    O  
ATOM    650  CB  VAL A 112      34.979  56.351  21.013  1.00 93.98      A    C  
ANISOU  650  CB  VAL A 112    16697   8135  10875   1669  -3029    149  A    C  
ATOM    651  CG1 VAL A 112      34.303  55.942  22.318  1.00 87.86      A    C  
ANISOU  651  CG1 VAL A 112    15818   7395  10169   1867  -2774   -312  A    C  
ATOM    652  CG2 VAL A 112      34.615  57.772  20.669  1.00 94.83      A    C  
ANISOU  652  CG2 VAL A 112    16923   7723  11385   1788  -3290    303  A    C  
ATOM    653  N   THR A 113      37.090  53.880  20.731  1.00110.87      A    N  
ANISOU  653  N   THR A 113    18747  11222  12158   1122  -2706    253  A    N  
ATOM    654  CA  THR A 113      37.587  52.566  21.122  1.00106.03      A    C  
ANISOU  654  CA  THR A 113    18017  10990  11281   1024  -2497    122  A    C  
ATOM    655  C   THR A 113      39.005  52.684  21.663  1.00107.37      A    C  
ANISOU  655  C   THR A 113    18289  11156  11349    759  -2457    128  A    C  
ATOM    656  O   THR A 113      39.368  52.023  22.635  1.00105.78      A    O  
ANISOU  656  O   THR A 113    18050  11088  11053    714  -2324    -70  A    O  
ATOM    657  CB  THR A 113      37.585  51.583  19.942  1.00 98.15      A    C  
ANISOU  657  CB  THR A 113    16884  10346  10062    957  -2472    310  A    C  
ATOM    658  CG2 THR A 113      37.900  50.172  20.410  1.00 81.71      A    C  
ANISOU  658  CG2 THR A 113    14662   8597   7786    917  -2259    139  A    C  
ATOM    659  OG1 THR A 113      36.299  51.598  19.315  1.00114.81      A    O  
ANISOU  659  OG1 THR A 113    18907  12448  12267   1161  -2572    362  A    O  
ATOM    660  N   SER A 114      39.796  53.541  21.026  1.00104.49      A    N  
ANISOU  660  N   SER A 114    18051  10641  11010    565  -2596    379  A    N  
ATOM    661  CA  SER A 114      41.192  53.735  21.394  1.00102.51      A    C  
ANISOU  661  CA  SER A 114    17869  10393  10689    283  -2586    430  A    C  
ATOM    662  C   SER A 114      41.390  54.268  22.816  1.00113.13      A    C  
ANISOU  662  C   SER A 114    19347  11498  12138    266  -2586    177  A    C  
ATOM    663  O   SER A 114      42.200  53.734  23.577  1.00121.11      A    O  
ANISOU  663  O   SER A 114    20321  12663  13034    115  -2513     82  A    O  
ATOM    664  CB  SER A 114      41.868  54.667  20.388  1.00 98.00      A    C  
ANISOU  664  CB  SER A 114    17415   9684  10136     61  -2741    763  A    C  
ATOM    665  OG  SER A 114      41.864  54.090  19.094  1.00 99.50      A    O  
ANISOU  665  OG  SER A 114    17499  10158  10147     -4  -2711    986  A    O  
ATOM    666  N   VAL A 115      40.656  55.319  23.170  1.00113.16      A    N  
ANISOU  666  N   VAL A 115    19505  11121  12368    414  -2678     65  A    N  
ATOM    667  CA  VAL A 115      40.726  55.872  24.520  1.00119.36      A    C  
ANISOU  667  CA  VAL A 115    20449  11667  13236    393  -2653   -234  A    C  
ATOM    668  C   VAL A 115      40.145  54.885  25.533  1.00130.36      A    C  
ANISOU  668  C   VAL A 115    21740  13289  14502    520  -2458   -551  A    C  
ATOM    669  O   VAL A 115      40.621  54.791  26.667  1.00137.97      A    O  
ANISOU  669  O   VAL A 115    22793  14270  15359    375  -2404   -751  A    O  
ATOM    670  CB  VAL A 115      39.996  57.236  24.615  1.00120.56      A    C  
ANISOU  670  CB  VAL A 115    20780  11317  13711    553  -2768   -322  A    C  
ATOM    671  CG1 VAL A 115      38.552  57.122  24.151  1.00118.09      A    C  
ANISOU  671  CG1 VAL A 115    20328  10967  13573    909  -2750   -365  A    C  
ATOM    672  CG2 VAL A 115      40.070  57.796  26.029  1.00135.21      A    C  
ANISOU  672  CG2 VAL A 115    22822  12929  15622    508  -2704   -691  A    C  
ATOM    673  N   ALA A 116      39.123  54.143  25.114  1.00127.37      A    N  
ANISOU  673  N   ALA A 116    21181  13097  14117    757  -2368   -578  A    N  
ATOM    674  CA  ALA A 116      38.523  53.118  25.961  1.00111.23      A    C  
ANISOU  674  CA  ALA A 116    19024  11298  11939    854  -2180   -838  A    C  
ATOM    675  C   ALA A 116      39.545  52.040  26.308  1.00 93.59      A    C  
ANISOU  675  C   ALA A 116    16724   9388   9450    628  -2131   -778  A    C  
ATOM    676  O   ALA A 116      39.639  51.618  27.460  1.00 90.26      A    O  
ANISOU  676  O   ALA A 116    16342   9053   8900    547  -2048   -982  A    O  
ATOM    677  CB  ALA A 116      37.309  52.502  25.282  1.00112.01      A    C  
ANISOU  677  CB  ALA A 116    18922  11549  12089   1114  -2121   -826  A    C  
ATOM    678  N   ARG A 117      40.312  51.605  25.311  1.00 90.37      A    N  
ANISOU  678  N   ARG A 117    16210   9152   8976    516  -2183   -496  A    N  
ATOM    679  CA  ARG A 117      41.370  50.626  25.541  1.00101.19      A    C  
ANISOU  679  CA  ARG A 117    17473  10788  10186    324  -2149   -421  A    C  
ATOM    680  C   ARG A 117      42.421  51.175  26.496  1.00106.83      A    C  
ANISOU  680  C   ARG A 117    18327  11379  10883     75  -2239   -453  A    C  
ATOM    681  O   ARG A 117      42.848  50.477  27.411  1.00112.46      A    O  
ANISOU  681  O   ARG A 117    19010  12240  11480    -38  -2222   -533  A    O  
ATOM    682  CB  ARG A 117      42.040  50.203  24.232  1.00113.22      A    C  
ANISOU  682  CB  ARG A 117    18851  12492  11676    244  -2153   -149  A    C  
ATOM    683  CG  ARG A 117      41.158  49.430  23.272  1.00110.42      A    C  
ANISOU  683  CG  ARG A 117    18354  12325  11276    425  -2069   -114  A    C  
ATOM    684  CD  ARG A 117      41.985  48.855  22.132  1.00117.57      A    C  
ANISOU  684  CD  ARG A 117    19123  13451  12095    292  -2023     93  A    C  
ATOM    685  NE  ARG A 117      41.160  48.127  21.174  1.00140.68      A    N  
ANISOU  685  NE  ARG A 117    21947  16562  14942    423  -1951    113  A    N  
ATOM    686  CZ  ARG A 117      40.869  46.834  21.272  1.00159.03      A    C  
ANISOU  686  CZ  ARG A 117    24123  19107  17195    501  -1826     -2  A    C  
ATOM    687  NH1 ARG A 117      41.337  46.122  22.289  1.00172.93      A    N1+
ANISOU  687  NH1 ARG A 117    25819  20924  18964    469  -1772   -116  A    N1+
ATOM    688  NH2 ARG A 117      40.109  46.253  20.353  1.00157.37      A    N  
ANISOU  688  NH2 ARG A 117    23841  19049  16904    590  -1779     13  A    N  
ATOM    689  N   LEU A 118      42.846  52.416  26.266  1.00109.73      A    N  
ANISOU  689  N   LEU A 118    18854  11473  11367    -33  -2363   -368  A    N  
ATOM    690  CA  LEU A 118      43.849  53.062  27.114  1.00111.95      A    C  
ANISOU  690  CA  LEU A 118    19286  11612  11639   -302  -2476   -393  A    C  
ATOM    691  C   LEU A 118      43.395  53.153  28.566  1.00105.93      A    C  
ANISOU  691  C   LEU A 118    18686  10766  10795   -310  -2439   -718  A    C  
ATOM    692  O   LEU A 118      44.165  52.880  29.490  1.00 79.57      A    O  
ANISOU  692  O   LEU A 118    15387   7521   7326   -541  -2498   -756  A    O  
ATOM    693  CB  LEU A 118      44.168  54.464  26.594  1.00104.73      A    C  
ANISOU  693  CB  LEU A 118    18546  10361  10887   -402  -2615   -267  A    C  
ATOM    694  CG  LEU A 118      44.937  54.572  25.278  1.00 96.53      A    C  
ANISOU  694  CG  LEU A 118    17397   9402   9877   -532  -2672     82  A    C  
ATOM    695  CD1 LEU A 118      44.856  55.988  24.749  1.00 96.47      A    C  
ANISOU  695  CD1 LEU A 118    17597   9014  10042   -579  -2817    204  A    C  
ATOM    696  CD2 LEU A 118      46.388  54.153  25.463  1.00 80.59      A    C  
ANISOU  696  CD2 LEU A 118    15248   7587   7786   -829  -2705    221  A    C  
ATOM    697  N   ALA A 119      42.133  53.523  28.751  1.00109.83      A    N  
ANISOU  697  N   ALA A 119    19262  11101  11367    -68  -2339   -950  A    N  
ATOM    698  CA  ALA A 119      41.541  53.610  30.075  1.00106.55      A    C  
ANISOU  698  CA  ALA A 119    18997  10629  10858    -65  -2237  -1308  A    C  
ATOM    699  C   ALA A 119      41.506  52.235  30.726  1.00111.94      A    C  
ANISOU  699  C   ALA A 119    19554  11681  11299   -115  -2145  -1353  A    C  
ATOM    700  O   ALA A 119      42.030  52.036  31.822  1.00105.32      A    O  
ANISOU  700  O   ALA A 119    18828  10920  10268   -355  -2182  -1451  A    O  
ATOM    701  CB  ALA A 119      40.146  54.208  29.987  1.00 82.26      A    C  
ANISOU  701  CB  ALA A 119    15956   7327   7972    244  -2115  -1543  A    C  
ATOM    702  N   ALA A 120      40.884  51.289  30.034  1.00114.82      A    N  
ANISOU  702  N   ALA A 120    19695  12262  11670     90  -2049  -1265  A    N  
ATOM    703  CA  ALA A 120      40.713  49.940  30.549  1.00105.93      A    C  
ANISOU  703  CA  ALA A 120    18443  11452  10353     68  -1963  -1292  A    C  
ATOM    704  C   ALA A 120      42.046  49.252  30.827  1.00104.26      A    C  
ANISOU  704  C   ALA A 120    18172  11412  10030   -194  -2103  -1083  A    C  
ATOM    705  O   ALA A 120      42.155  48.449  31.756  1.00102.78      A    O  
ANISOU  705  O   ALA A 120    17990  11398   9665   -324  -2105  -1130  A    O  
ATOM    706  CB  ALA A 120      39.895  49.114  29.569  1.00 98.71      A    C  
ANISOU  706  CB  ALA A 120    17301  10704   9501    317  -1862  -1209  A    C  
ATOM    707  N   ALA A 121      43.059  49.584  30.031  1.00105.85      A    N  
ANISOU  707  N   ALA A 121    18305  11562  10350   -283  -2226   -842  A    N  
ATOM    708  CA  ALA A 121      44.361  48.930  30.124  1.00112.79      A    C  
ANISOU  708  CA  ALA A 121    19048  12600  11206   -497  -2353   -624  A    C  
ATOM    709  C   ALA A 121      44.974  49.078  31.506  1.00122.24      A    C  
ANISOU  709  C   ALA A 121    20405  13784  12257   -779  -2494   -695  A    C  
ATOM    710  O   ALA A 121      45.586  48.149  32.028  1.00129.23      A    O  
ANISOU  710  O   ALA A 121    21179  14852  13072   -915  -2588   -581  A    O  
ATOM    711  CB  ALA A 121      45.312  49.482  29.071  1.00110.81      A    C  
ANISOU  711  CB  ALA A 121    18706  12283  11113   -573  -2430   -389  A    C  
ATOM    712  N   LYS A 122      44.807  50.253  32.096  1.00126.04      A    N  
ANISOU  712  N   LYS A 122    21156  14032  12700   -878  -2525   -883  A    N  
ATOM    713  CA  LYS A 122      45.329  50.498  33.431  1.00133.18      A    C  
ANISOU  713  CA  LYS A 122    22265  14921  13416  -1190  -2661   -986  A    C  
ATOM    714  C   LYS A 122      44.315  51.097  34.393  1.00121.72      A    C  
ANISOU  714  C   LYS A 122    21104  13341  11804  -1184  -2527  -1368  A    C  
ATOM    715  O   LYS A 122      44.251  52.312  34.576  1.00114.86      A    O  
ANISOU  715  O   LYS A 122    20460  12192  10989  -1238  -2533  -1546  A    O  
ATOM    716  CB  LYS A 122      46.573  51.385  33.361  1.00149.80      A    C  
ANISOU  716  CB  LYS A 122    24430  16874  15614  -1455  -2874   -836  A    C  
ATOM    717  CG  LYS A 122      47.746  50.726  32.657  1.00151.37      A    C  
ANISOU  717  CG  LYS A 122    24314  17243  15955  -1528  -2999   -483  A    C  
ATOM    718  CD  LYS A 122      48.397  49.669  33.532  1.00143.49      A    C  
ANISOU  718  CD  LYS A 122    23200  16478  14842  -1717  -3155   -365  A    C  
ATOM    719  CE  LYS A 122      49.208  48.677  32.718  1.00132.78      A    C  
ANISOU  719  CE  LYS A 122    21451  15308  13692  -1649  -3187    -69  A    C  
ATOM    720  NZ  LYS A 122      50.644  49.078  32.628  1.00114.49      A    N1+
ANISOU  720  NZ  LYS A 122    18996  12977  11528  -1912  -3399    156  A    N1+
ATOM    721  N   GLY A 123      43.495  50.222  34.966  1.00121.21      A    N  
ANISOU  721  N   GLY A 123    21021  13475  11560  -1116  -2386  -1502  A    N  
ATOM    722  CA  GLY A 123      42.580  50.592  36.028  1.00133.48      A    C  
ANISOU  722  CA  GLY A 123    22822  14984  12909  -1161  -2220  -1884  A    C  
ATOM    723  C   GLY A 123      41.262  51.226  35.660  1.00130.18      A    C  
ANISOU  723  C   GLY A 123    22426  14385  12650   -838  -1962  -2172  A    C  
ATOM    724  O   GLY A 123      40.198  50.669  35.928  1.00 99.55      A    O  
ANISOU  724  O   GLY A 123    18489  10648   8687   -695  -1748  -2350  A    O  
ATOM    725  N   ASN A 124      41.328  52.406  35.060  1.00152.98      A    N  
ANISOU  725  N   ASN A 124    25386  16946  15792   -733  -1995  -2207  A    N  
ATOM    726  CA  ASN A 124      40.129  53.202  34.841  1.00168.88      A    C  
ANISOU  726  CA  ASN A 124    27441  18712  18015   -438  -1792  -2498  A    C  
ATOM    727  C   ASN A 124      39.227  52.612  33.767  1.00169.55      A    C  
ANISOU  727  C   ASN A 124    27234  18897  18291    -75  -1687  -2372  A    C  
ATOM    728  O   ASN A 124      39.126  53.151  32.673  1.00171.30      A    O  
ANISOU  728  O   ASN A 124    27368  18927  18793    125  -1756  -2216  A    O  
ATOM    729  CB  ASN A 124      40.497  54.640  34.478  1.00170.75      A    C  
ANISOU  729  CB  ASN A 124    27848  18524  18507   -439  -1905  -2527  A    C  
ATOM    730  CG  ASN A 124      39.328  55.593  34.627  1.00168.61      A    C  
ANISOU  730  CG  ASN A 124    27673  17927  18463   -182  -1706  -2908  A    C  
ATOM    731  ND2 ASN A 124      39.625  56.885  34.695  1.00175.53      A    N  
ANISOU  731  ND2 ASN A 124    28775  18389  19528   -241  -1789  -3030  A    N  
ATOM    732  OD1 ASN A 124      38.171  55.175  34.679  1.00162.01      A    O  
ANISOU  732  OD1 ASN A 124    26694  17197  17664     67  -1482  -3093  A    O  
ATOM    733  N   GLY A 125      38.563  51.508  34.089  1.00163.18      A    N  
ANISOU  733  N   GLY A 125    26291  18393  17317    -21  -1537  -2429  A    N  
ATOM    734  CA  GLY A 125      37.558  50.961  33.200  1.00158.42      A    C  
ANISOU  734  CA  GLY A 125    25426  17888  16877    301  -1424  -2368  A    C  
ATOM    735  C   GLY A 125      36.357  51.862  33.004  1.00152.94      A    C  
ANISOU  735  C   GLY A 125    24711  16939  16458    600  -1268  -2634  A    C  
ATOM    736  O   GLY A 125      35.789  51.931  31.916  1.00176.61      A    O  
ANISOU  736  O   GLY A 125    27520  19874  19710    871  -1296  -2494  A    O  
ATOM    737  N   ASP A 126      35.979  52.557  34.070  1.00139.62      A    N  
ANISOU  737  N   ASP A 126    23218  15103  14728    540  -1109  -3025  A    N  
ATOM    738  CA  ASP A 126      34.785  53.395  34.066  1.00136.81      A    C  
ANISOU  738  CA  ASP A 126    22817  14488  14675    838   -918  -3348  A    C  
ATOM    739  C   ASP A 126      34.780  54.591  33.097  1.00156.97      A    C  
ANISOU  739  C   ASP A 126    25374  16608  17659   1064  -1079  -3239  A    C  
ATOM    740  O   ASP A 126      33.732  55.071  32.661  1.00166.68      A    O  
ANISOU  740  O   ASP A 126    26449  17641  19239   1395   -998  -3356  A    O  
ATOM    741  CB  ASP A 126      34.565  53.987  35.455  1.00141.49      A    C  
ANISOU  741  CB  ASP A 126    23660  14979  15122    680   -696  -3832  A    C  
ATOM    742  CG  ASP A 126      33.295  54.796  35.538  1.00168.68      A    C  
ANISOU  742  CG  ASP A 126    27017  18156  18920   1008   -447  -4225  A    C  
ATOM    743  OD1 ASP A 126      32.583  54.874  34.514  1.00181.38      A    O  
ANISOU  743  OD1 ASP A 126    28357  19663  20895   1358   -490  -4077  A    O  
ATOM    744  OD2 ASP A 126      33.002  55.344  36.620  1.00174.37      A    O1-
ANISOU  744  OD2 ASP A 126    27925  18769  19558    911   -209  -4686  A    O1-
ATOM    745  N   TYR A 127      35.981  55.038  32.748  1.00153.85      A    N  
ANISOU  745  N   TYR A 127    25138  16071  17246    867  -1330  -2982  A    N  
ATOM    746  CA  TYR A 127      36.145  56.112  31.777  1.00151.22      A    C  
ANISOU  746  CA  TYR A 127    24836  15344  17275   1006  -1527  -2794  A    C  
ATOM    747  C   TYR A 127      35.797  55.465  30.444  1.00150.51      A    C  
ANISOU  747  C   TYR A 127    24464  15431  17290   1209  -1628  -2426  A    C  
ATOM    748  O   TYR A 127      35.065  56.035  29.634  1.00156.50      A    O  
ANISOU  748  O   TYR A 127    25114  15958  18391   1485  -1693  -2352  A    O  
ATOM    749  CB  TYR A 127      37.556  56.701  31.705  1.00152.40      A    C  
ANISOU  749  CB  TYR A 127    25212  15335  17357    697  -1764  -2585  A    C  
ATOM    750  CG  TYR A 127      37.789  57.751  30.632  1.00157.74      A    C  
ANISOU  750  CG  TYR A 127    25930  15626  18377    789  -1988  -2326  A    C  
ATOM    751  CD1 TYR A 127      37.341  59.057  30.780  1.00164.60      A    C  
ANISOU  751  CD1 TYR A 127    26959  15986  19595    928  -2000  -2544  A    C  
ATOM    752  CD2 TYR A 127      38.461  57.422  29.462  1.00159.85      A    C  
ANISOU  752  CD2 TYR A 127    26082  16035  18619    720  -2183  -1861  A    C  
ATOM    753  CE1 TYR A 127      37.557  60.004  29.798  1.00172.94      A    C  
ANISOU  753  CE1 TYR A 127    28069  16670  20970    988  -2239  -2262  A    C  
ATOM    754  CE2 TYR A 127      38.684  58.361  28.475  1.00165.96      A    C  
ANISOU  754  CE2 TYR A 127    26914  16484  19659    751  -2393  -1591  A    C  
ATOM    755  CZ  TYR A 127      38.228  59.651  28.646  1.00172.77      A    C  
ANISOU  755  CZ  TYR A 127    27945  16828  20869    882  -2441  -1769  A    C  
ATOM    756  OH  TYR A 127      38.447  60.591  27.664  1.00181.79      A    O  
ANISOU  756  OH  TYR A 127    29163  17622  22286    892  -2685  -1458  A    O  
ATOM    757  N   ALA A 128      36.303  54.251  30.247  1.00139.75      A    N  
ANISOU  757  N   ALA A 128    22985  14476  15637   1063  -1647  -2205  A    N  
ATOM    758  CA  ALA A 128      36.087  53.509  29.013  1.00123.69      A    C  
ANISOU  758  CA  ALA A 128    20711  12653  13632   1194  -1724  -1882  A    C  
ATOM    759  C   ALA A 128      34.592  53.347  28.780  1.00121.05      A    C  
ANISOU  759  C   ALA A 128    20165  12336  13493   1522  -1596  -2027  A    C  
ATOM    760  O   ALA A 128      34.119  53.486  27.653  1.00130.97      A    O  
ANISOU  760  O   ALA A 128    21277  13534  14950   1708  -1720  -1806  A    O  
ATOM    761  CB  ALA A 128      36.770  52.149  29.035  1.00111.10      A    C  
ANISOU  761  CB  ALA A 128    19022  11472  11721   1002  -1713  -1716  A    C  
ATOM    762  N   PHE A 129      33.854  53.034  29.840  1.00109.09      A    N  
ANISOU  762  N   PHE A 129    18622  10922  11904   1565  -1355  -2385  A    N  
ATOM    763  CA  PHE A 129      32.404  52.917  29.742  1.00112.18      A    C  
ANISOU  763  CA  PHE A 129    18777  11336  12511   1867  -1203  -2563  A    C  
ATOM    764  C   PHE A 129      31.758  54.265  29.446  1.00120.93      A    C  
ANISOU  764  C   PHE A 129    19880  11988  14079   2139  -1257  -2670  A    C  
ATOM    765  O   PHE A 129      30.954  54.384  28.525  1.00130.79      A    O  
ANISOU  765  O   PHE A 129    20911  13169  15615   2399  -1357  -2520  A    O  
ATOM    766  CB  PHE A 129      31.817  52.344  31.035  1.00118.29      A    C  
ANISOU  766  CB  PHE A 129    19536  12327  13083   1804   -895  -2947  A    C  
ATOM    767  CG  PHE A 129      30.387  51.862  30.908  1.00131.35      A    C  
ANISOU  767  CG  PHE A 129    20879  14134  14893   2060   -717  -3087  A    C  
ATOM    768  CD1 PHE A 129      29.764  51.762  29.672  1.00131.04      A    C  
ANISOU  768  CD1 PHE A 129    20589  14088  15112   2302   -870  -2835  A    C  
ATOM    769  CD2 PHE A 129      29.660  51.532  32.041  1.00145.82      A    C  
ANISOU  769  CD2 PHE A 129    22671  16131  16602   2027   -397  -3472  A    C  
ATOM    770  CE1 PHE A 129      28.453  51.317  29.571  1.00133.60      A    C  
ANISOU  770  CE1 PHE A 129    20603  14565  15595   2517   -728  -2954  A    C  
ATOM    771  CE2 PHE A 129      28.351  51.096  31.946  1.00147.27      A    C  
ANISOU  771  CE2 PHE A 129    22540  16472  16946   2241   -220  -3604  A    C  
ATOM    772  CZ  PHE A 129      27.745  50.990  30.710  1.00141.03      A    C  
ANISOU  772  CZ  PHE A 129    21475  15666  16444   2495   -395  -3343  A    C  
ATOM    773  N   LYS A 130      32.137  55.285  30.209  1.00125.13      A    N  
ANISOU  773  N   LYS A 130    20659  12190  14694   2066  -1217  -2917  A    N  
ATOM    774  CA  LYS A 130      31.436  56.566  30.151  1.00138.29      A    C  
ANISOU  774  CA  LYS A 130    22324  13372  16847   2344  -1222  -3109  A    C  
ATOM    775  C   LYS A 130      31.571  57.258  28.796  1.00141.66      A    C  
ANISOU  775  C   LYS A 130    22721  13506  17598   2481  -1565  -2691  A    C  
ATOM    776  O   LYS A 130      30.605  57.826  28.290  1.00139.65      A    O  
ANISOU  776  O   LYS A 130    22285  12990  17784   2805  -1629  -2691  A    O  
ATOM    777  CB  LYS A 130      31.925  57.499  31.261  1.00129.82      A    C  
ANISOU  777  CB  LYS A 130    21570  11988  15767   2190  -1110  -3479  A    C  
ATOM    778  CG  LYS A 130      30.976  58.656  31.535  1.00126.36      A    C  
ANISOU  778  CG  LYS A 130    21098  11070  15842   2507   -988  -3847  A    C  
ATOM    779  CD  LYS A 130      31.573  59.661  32.501  1.00131.75      A    C  
ANISOU  779  CD  LYS A 130    22144  11392  16524   2326   -911  -4200  A    C  
ATOM    780  CE  LYS A 130      30.672  60.876  32.649  1.00139.14      A    C  
ANISOU  780  CE  LYS A 130    23041  11771  18054   2673   -807  -4560  A    C  
ATOM    781  NZ  LYS A 130      31.206  61.846  33.645  1.00141.20      A    N1+
ANISOU  781  NZ  LYS A 130    23679  11665  18307   2482   -698  -4973  A    N1+
ATOM    782  N   VAL A 131      32.755  57.187  28.197  1.00135.08      A    N  
ANISOU  782  N   VAL A 131    22045  12731  16548   2221  -1792  -2319  A    N  
ATOM    783  CA  VAL A 131      32.982  57.823  26.905  1.00132.08      A    C  
ANISOU  783  CA  VAL A 131    21674  12113  16396   2272  -2115  -1892  A    C  
ATOM    784  C   VAL A 131      32.153  57.162  25.793  1.00130.38      A    C  
ANISOU  784  C   VAL A 131    21162  12129  16248   2468  -2218  -1614  A    C  
ATOM    785  O   VAL A 131      31.667  57.846  24.889  1.00144.69      A    O  
ANISOU  785  O   VAL A 131    22907  13670  18400   2651  -2452  -1378  A    O  
ATOM    786  CB  VAL A 131      34.490  57.807  26.536  1.00171.81      A    C  
ANISOU  786  CB  VAL A 131    26919  17223  21137   1903  -2286  -1572  A    C  
ATOM    787  CG1 VAL A 131      35.035  56.386  26.488  1.00157.95      A    C  
ANISOU  787  CG1 VAL A 131    25061  16017  18937   1703  -2195  -1454  A    C  
ATOM    788  CG2 VAL A 131      34.742  58.534  25.218  1.00180.08      A    C  
ANISOU  788  CG2 VAL A 131    28007  18028  22385   1902  -2605  -1126  A    C  
ATOM    789  N   VAL A 132      31.983  55.843  25.865  1.00114.50      A    N  
ANISOU  789  N   VAL A 132    18983  10603  13917   2412  -2066  -1632  A    N  
ATOM    790  CA  VAL A 132      31.189  55.103  24.881  1.00114.12      A    C  
ANISOU  790  CA  VAL A 132    18663  10812  13885   2557  -2148  -1409  A    C  
ATOM    791  C   VAL A 132      29.694  55.420  24.999  1.00109.75      A    C  
ANISOU  791  C   VAL A 132    17851  10104  13745   2923  -2090  -1613  A    C  
ATOM    792  O   VAL A 132      28.997  55.561  23.991  1.00100.32      A    O  
ANISOU  792  O   VAL A 132    16474   8856  12787   3100  -2308  -1358  A    O  
ATOM    793  CB  VAL A 132      31.408  53.584  25.001  1.00113.08      A    C  
ANISOU  793  CB  VAL A 132    18433  11205  13328   2390  -1990  -1408  A    C  
ATOM    794  CG1 VAL A 132      30.537  52.858  24.011  1.00102.06      A    C  
ANISOU  794  CG1 VAL A 132    16774  10052  11953   2522  -2074  -1214  A    C  
ATOM    795  CG2 VAL A 132      32.857  53.246  24.729  1.00126.38      A    C  
ANISOU  795  CG2 VAL A 132    20302  13035  14680   2067  -2065  -1176  A    C  
ATOM    796  N   LYS A 133      29.200  55.519  26.231  1.00112.92      A    N  
ANISOU  796  N   LYS A 133    18224  10450  14231   3020  -1796  -2075  A    N  
ATOM    797  CA  LYS A 133      27.797  55.871  26.461  1.00123.51      A    C  
ANISOU  797  CA  LYS A 133    19284  11634  16011   3376  -1683  -2334  A    C  
ATOM    798  C   LYS A 133      27.464  57.259  25.912  1.00142.17      A    C  
ANISOU  798  C   LYS A 133    21647  13436  18936   3632  -1934  -2224  A    C  
ATOM    799  O   LYS A 133      26.430  57.458  25.281  1.00145.82      A    O  
ANISOU  799  O   LYS A 133    21819  13791  19796   3923  -2073  -2115  A    O  
ATOM    800  CB  LYS A 133      27.466  55.832  27.956  1.00126.27      A    C  
ANISOU  800  CB  LYS A 133    19651  12014  16312   3380  -1274  -2892  A    C  
ATOM    801  CG  LYS A 133      27.852  54.562  28.687  1.00121.33      A    C  
ANISOU  801  CG  LYS A 133    19077  11887  15136   3093  -1039  -3007  A    C  
ATOM    802  CD  LYS A 133      27.253  54.533  30.097  1.00126.42      A    C  
ANISOU  802  CD  LYS A 133    19699  12589  15746   3104   -629  -3554  A    C  
ATOM    803  CE  LYS A 133      25.772  54.889  30.098  1.00133.46      A    C  
ANISOU  803  CE  LYS A 133    20226  13353  17128   3484   -475  -3805  A    C  
ATOM    804  NZ  LYS A 133      25.293  55.239  31.469  1.00129.16      A    N1+
ANISOU  804  NZ  LYS A 133    19708  12747  16618   3500    -51  -4398  A    N1+
ATOM    805  N   GLU A 134      28.346  58.215  26.175  1.00158.81      A    N  
ANISOU  805  N   GLU A 134    24076  15171  21093   3511  -2011  -2244  A    N  
ATOM    806  CA  GLU A 134      28.233  59.570  25.652  1.00158.59      A    C  
ANISOU  806  CA  GLU A 134    24118  14555  21583   3697  -2287  -2095  A    C  
ATOM    807  C   GLU A 134      28.312  59.552  24.116  1.00144.39      A    C  
ANISOU  807  C   GLU A 134    22263  12784  19814   3675  -2711  -1482  A    C  
ATOM    808  O   GLU A 134      27.684  60.355  23.416  1.00132.77      A    O  
ANISOU  808  O   GLU A 134    20679  10937  18829   3919  -2993  -1269  A    O  
ATOM    809  CB  GLU A 134      29.336  60.427  26.275  1.00157.55      A    C  
ANISOU  809  CB  GLU A 134    24387  14087  21387   3473  -2277  -2225  A    C  
ATOM    810  CG  GLU A 134      29.012  60.897  27.689  1.00156.73      A    C  
ANISOU  810  CG  GLU A 134    24353  13763  21433   3565  -1918  -2856  A    C  
ATOM    811  CD  GLU A 134      30.020  61.892  28.228  1.00156.87      A    C  
ANISOU  811  CD  GLU A 134    24777  13374  21452   3350  -1959  -2982  A    C  
ATOM    812  OE1 GLU A 134      31.204  61.811  27.837  1.00152.07      A    O  
ANISOU  812  OE1 GLU A 134    24404  12863  20513   3015  -2158  -2643  A    O  
ATOM    813  OE2 GLU A 134      29.623  62.770  29.023  1.00167.97      A    O1-
ANISOU  813  OE2 GLU A 134    26257  14355  23208   3510  -1786  -3432  A    O1-
ATOM    814  N   PHE A 135      29.084  58.601  23.605  1.00147.86      A    N  
ANISOU  814  N   PHE A 135    22778  13678  19724   3368  -2753  -1204  A    N  
ATOM    815  CA  PHE A 135      29.250  58.424  22.170  1.00150.08      A    C  
ANISOU  815  CA  PHE A 135    23038  14085  19901   3267  -3097   -658  A    C  
ATOM    816  C   PHE A 135      28.017  57.894  21.457  1.00156.52      A    C  
ANISOU  816  C   PHE A 135    23498  15095  20876   3497  -3211   -519  A    C  
ATOM    817  O   PHE A 135      27.612  58.432  20.429  1.00165.11      A    O  
ANISOU  817  O   PHE A 135    24524  15985  22227   3593  -3570   -143  A    O  
ATOM    818  CB  PHE A 135      30.420  57.485  21.898  1.00150.14      A    C  
ANISOU  818  CB  PHE A 135    23200  14540  19306   2880  -3041   -481  A    C  
ATOM    819  CG  PHE A 135      30.773  57.376  20.451  1.00159.69      A    C  
ANISOU  819  CG  PHE A 135    24449  15882  20345   2706  -3347     43  A    C  
ATOM    820  CD1 PHE A 135      31.399  58.418  19.795  1.00171.47      A    C  
ANISOU  820  CD1 PHE A 135    26166  17033  21953   2574  -3632    379  A    C  
ATOM    821  CD2 PHE A 135      30.473  56.226  19.741  1.00159.14      A    C  
ANISOU  821  CD2 PHE A 135    24205  16281  19979   2644  -3345    193  A    C  
ATOM    822  CE1 PHE A 135      31.721  58.311  18.460  1.00171.09      A    C  
ANISOU  822  CE1 PHE A 135    26171  17143  21694   2367  -3895    861  A    C  
ATOM    823  CE2 PHE A 135      30.794  56.116  18.407  1.00158.21      A    C  
ANISOU  823  CE2 PHE A 135    24147  16312  19655   2447  -3601    642  A    C  
ATOM    824  CZ  PHE A 135      31.417  57.160  17.765  1.00163.98      A    C  
ANISOU  824  CZ  PHE A 135    25103  16731  20469   2300  -3870    979  A    C  
ATOM    825  N   VAL A 136      27.430  56.832  21.998  1.00157.69      A    N  
ANISOU  825  N   VAL A 136    23421  15636  20857   3555  -2928   -799  A    N  
ATOM    826  CA  VAL A 136      26.262  56.211  21.384  1.00164.33      A    C  
ANISOU  826  CA  VAL A 136    23906  16713  21818   3736  -3018   -691  A    C  
ATOM    827  C   VAL A 136      25.077  57.178  21.433  1.00168.47      A    C  
ANISOU  827  C   VAL A 136    24173  16807  23030   4143  -3139   -776  A    C  
ATOM    828  O   VAL A 136      24.124  57.052  20.662  1.00166.44      A    O  
ANISOU  828  O   VAL A 136    23623  16603  23012   4314  -3370   -555  A    O  
ATOM    829  CB  VAL A 136      25.900  54.874  22.071  1.00155.58      A    C  
ANISOU  829  CB  VAL A 136    22620  16096  20397   3687  -2665   -998  A    C  
ATOM    830  CG1 VAL A 136      25.348  55.115  23.471  1.00157.29      A    C  
ANISOU  830  CG1 VAL A 136    22735  16182  20844   3876  -2299  -1535  A    C  
ATOM    831  CG2 VAL A 136      24.912  54.086  21.229  1.00152.65      A    C  
ANISOU  831  CG2 VAL A 136    21927  16034  20040   3767  -2806   -803  A    C  
ATOM    832  N   SER A 137      25.156  58.152  22.336  1.00166.87      A    N  
ANISOU  832  N   SER A 137    24076  16164  23162   4291  -2991  -1103  A    N  
ATOM    833  CA  SER A 137      24.131  59.179  22.472  1.00173.50      A    C  
ANISOU  833  CA  SER A 137    24682  16510  24730   4702  -3074  -1240  A    C  
ATOM    834  C   SER A 137      24.010  60.022  21.205  1.00179.94      A    C  
ANISOU  834  C   SER A 137    25503  16963  25902   4789  -3616   -693  A    C  
ATOM    835  O   SER A 137      22.908  60.405  20.816  1.00189.21      A    O  
ANISOU  835  O   SER A 137    26339  17923  27627   5121  -3821   -601  A    O  
ATOM    836  CB  SER A 137      24.434  60.075  23.674  1.00185.03      A    C  
ANISOU  836  CB  SER A 137    26336  17547  26421   4783  -2795  -1720  A    C  
ATOM    837  OG  SER A 137      24.878  59.307  24.778  1.00179.76      A    O  
ANISOU  837  OG  SER A 137    25789  17242  25271   4569  -2356  -2131  A    O  
ATOM    838  N   VAL A 138      25.144  60.316  20.573  1.00188.25      A    N  
ANISOU  838  N   VAL A 138    26927  17950  26648   4476  -3856   -316  A    N  
ATOM    839  CA  VAL A 138      25.160  61.140  19.366  1.00202.68      A    C  
ANISOU  839  CA  VAL A 138    28831  19444  28736   4476  -4384    249  A    C  
ATOM    840  C   VAL A 138      24.348  60.500  18.240  1.00217.09      A    C  
ANISOU  840  C   VAL A 138    30370  21594  30520   4506  -4688    648  A    C  
ATOM    841  O   VAL A 138      23.370  61.077  17.763  1.00242.20      A    O  
ANISOU  841  O   VAL A 138    33289  24472  34262   4801  -5008    844  A    O  
ATOM    842  CB  VAL A 138      26.600  61.392  18.873  1.00195.56      A    C  
ANISOU  842  CB  VAL A 138    28378  18533  27393   4050  -4532    582  A    C  
ATOM    843  CG1 VAL A 138      26.583  62.162  17.561  1.00203.00      A    C  
ANISOU  843  CG1 VAL A 138    29409  19189  28532   3990  -5086   1213  A    C  
ATOM    844  CG2 VAL A 138      27.398  62.141  19.926  1.00187.93      A    C  
ANISOU  844  CG2 VAL A 138    27700  17198  26506   3998  -4304    230  A    C  
ATOM    845  N   GLY A 139      24.759  59.308  17.817  1.00210.03      A    N  
ANISOU  845  N   GLY A 139    29522  21301  28978   4195  -4601    766  A    N  
ATOM    846  CA  GLY A 139      23.974  58.520  16.885  1.00199.49      A    C  
ANISOU  846  CA  GLY A 139    27923  20347  27526   4185  -4819   1048  A    C  
ATOM    847  C   GLY A 139      23.977  58.972  15.436  1.00196.00      A    C  
ANISOU  847  C   GLY A 139    27574  19814  27083   4039  -5379   1696  A    C  
ATOM    848  O   GLY A 139      23.493  58.249  14.563  1.00183.81      A    O  
ANISOU  848  O   GLY A 139    25882  18646  25311   3930  -5578   1963  A    O  
ATOM    849  N   GLY A 140      24.521  60.155  15.168  1.00200.93      A    N  
ANISOU  849  N   GLY A 140    28461  19946  27938   4001  -5645   1961  A    N  
ATOM    850  CA  GLY A 140      24.538  60.672  13.812  1.00201.48      A    C  
ANISOU  850  CA  GLY A 140    28651  19900  28002   3827  -6202   2615  A    C  
ATOM    851  C   GLY A 140      25.438  59.828  12.936  1.00194.32      A    C  
ANISOU  851  C   GLY A 140    28005  19540  26290   3321  -6203   2893  A    C  
ATOM    852  O   GLY A 140      25.015  59.319  11.900  1.00197.47      A    O  
ANISOU  852  O   GLY A 140    28325  20261  26446   3167  -6480   3243  A    O  
ATOM    853  N   VAL A 141      26.686  59.670  13.359  1.00186.91      A    N  
ANISOU  853  N   VAL A 141    27367  18711  24940   3053  -5886   2721  A    N  
ATOM    854  CA  VAL A 141      27.597  58.739  12.706  1.00180.31      A    C  
ANISOU  854  CA  VAL A 141    26730  18421  23360   2604  -5764   2860  A    C  
ATOM    855  C   VAL A 141      28.300  57.959  13.812  1.00168.00      A    C  
ANISOU  855  C   VAL A 141    25199  17111  21524   2564  -5220   2340  A    C  
ATOM    856  O   VAL A 141      29.520  57.794  13.805  1.00160.27      A    O  
ANISOU  856  O   VAL A 141    24473  16279  20142   2247  -5049   2348  A    O  
ATOM    857  CB  VAL A 141      28.631  59.450  11.798  1.00179.38      A    C  
ANISOU  857  CB  VAL A 141    26986  18184  22985   2209  -6026   3340  A    C  
ATOM    858  CG1 VAL A 141      29.289  58.447  10.857  1.00172.66      A    C  
ANISOU  858  CG1 VAL A 141    26266  17936  21398   1762  -5948   3524  A    C  
ATOM    859  CG2 VAL A 141      27.973  60.554  10.981  1.00178.61      A    C  
ANISOU  859  CG2 VAL A 141    26902  17651  23313   2292  -6602   3852  A    C  
ATOM    860  N   SER A 142      27.513  57.495  14.776  1.00167.33      A    N  
ANISOU  860  N   SER A 142    24835  17069  21672   2880  -4959   1901  A    N  
ATOM    861  CA  SER A 142      28.046  56.760  15.913  1.00177.44      A    C  
ANISOU  861  CA  SER A 142    26130  18567  22721   2853  -4476   1419  A    C  
ATOM    862  C   SER A 142      28.637  55.432  15.455  1.00181.23      A    C  
ANISOU  862  C   SER A 142    26655  19629  22575   2536  -4303   1447  A    C  
ATOM    863  O   SER A 142      29.805  55.136  15.723  1.00171.79      A    O  
ANISOU  863  O   SER A 142    25661  18573  21040   2289  -4085   1363  A    O  
ATOM    864  CB  SER A 142      26.954  56.532  16.963  1.00176.82      A    C  
ANISOU  864  CB  SER A 142    25736  18441  23007   3228  -4246    974  A    C  
ATOM    865  OG  SER A 142      25.870  55.796  16.422  1.00169.98      A    O  
ANISOU  865  OG  SER A 142    24561  17865  22159   3334  -4351   1054  A    O  
ATOM    866  N   ILE A 143      27.820  54.654  14.749  1.00193.24      A    N  
ANISOU  866  N   ILE A 143    27974  21469  23978   2546  -4414   1563  A    N  
ATOM    867  CA  ILE A 143      28.204  53.334  14.257  1.00187.00      A    C  
ANISOU  867  CA  ILE A 143    27200  21210  22640   2272  -4255   1556  A    C  
ATOM    868  C   ILE A 143      28.794  52.491  15.396  1.00176.25      A    C  
ANISOU  868  C   ILE A 143    25840  20036  21090   2253  -3803   1122  A    C  
ATOM    869  O   ILE A 143      29.914  51.990  15.285  1.00176.50      A    O  
ANISOU  869  O   ILE A 143    26048  20275  20740   1981  -3637   1121  A    O  
ATOM    870  CB  ILE A 143      29.224  53.442  13.089  1.00180.50      A    C  
ANISOU  870  CB  ILE A 143    26660  20522  21399   1875  -4409   1940  A    C  
ATOM    871  CG1 ILE A 143      28.868  54.607  12.159  1.00189.88      A    C  
ANISOU  871  CG1 ILE A 143    27934  21401  22811   1862  -4885   2410  A    C  
ATOM    872  CG2 ILE A 143      29.331  52.124  12.317  1.00175.28      A    C  
ANISOU  872  CG2 ILE A 143    25980  20390  20229   1619  -4308   1958  A    C  
ATOM    873  CD1 ILE A 143      27.624  54.376  11.317  1.00193.67      A    C  
ANISOU  873  CD1 ILE A 143    28206  22008  23372   1942  -5217   2643  A    C  
ATOM    874  N   PRO A 144      28.057  52.365  16.514  1.00166.09      A    N  
ANISOU  874  N   PRO A 144    24351  18670  20087   2531  -3606    759  A    N  
ATOM    875  CA  PRO A 144      28.647  51.752  17.707  1.00147.93      A    C  
ANISOU  875  CA  PRO A 144    22093  16486  17628   2493  -3219    380  A    C  
ATOM    876  C   PRO A 144      29.033  50.289  17.510  1.00132.20      A    C  
ANISOU  876  C   PRO A 144    20082  14959  15189   2277  -3030    320  A    C  
ATOM    877  O   PRO A 144      28.164  49.435  17.345  1.00134.72      A    O  
ANISOU  877  O   PRO A 144    20193  15525  15470   2336  -3003    254  A    O  
ATOM    878  CB  PRO A 144      27.530  51.883  18.741  1.00145.93      A    C  
ANISOU  878  CB  PRO A 144    21597  16101  17749   2814  -3075     41  A    C  
ATOM    879  CG  PRO A 144      26.279  51.844  17.927  1.00155.20      A    C  
ANISOU  879  CG  PRO A 144    22503  17322  19143   2978  -3325    222  A    C  
ATOM    880  CD  PRO A 144      26.624  52.659  16.714  1.00162.84      A    C  
ANISOU  880  CD  PRO A 144    23636  18111  20127   2868  -3714    679  A    C  
ATOM    881  N   ARG A 145      30.330  50.005  17.526  1.00124.83      A    N  
ANISOU  881  N   ARG A 145    19351  14125  13953   2029  -2904    340  A    N  
ATOM    882  CA  ARG A 145      30.801  48.645  17.304  1.00121.33      A    C  
ANISOU  882  CA  ARG A 145    18892  14071  13138   1835  -2725    280  A    C  
ATOM    883  C   ARG A 145      31.033  47.976  18.656  1.00124.23      A    C  
ANISOU  883  C   ARG A 145    19220  14502  13480   1871  -2429    -61  A    C  
ATOM    884  O   ARG A 145      31.308  48.647  19.649  1.00119.24      A    O  
ANISOU  884  O   ARG A 145    18664  13638  13003   1939  -2354   -211  A    O  
ATOM    885  CB  ARG A 145      32.076  48.615  16.458  1.00114.30      A    C  
ANISOU  885  CB  ARG A 145    18195  13282  11951   1539  -2746    499  A    C  
ATOM    886  CG  ARG A 145      32.423  47.221  15.958  1.00106.70      A    C  
ANISOU  886  CG  ARG A 145    17191  12702  10650   1359  -2584    448  A    C  
ATOM    887  CD  ARG A 145      33.719  47.174  15.171  1.00110.05      A    C  
ANISOU  887  CD  ARG A 145    17771  13240  10803   1070  -2540    610  A    C  
ATOM    888  NE  ARG A 145      33.620  47.829  13.870  1.00132.97      A    N  
ANISOU  888  NE  ARG A 145    20781  16146  13594    924  -2781    938  A    N  
ATOM    889  CZ  ARG A 145      34.624  47.914  13.001  1.00139.85      A    C  
ANISOU  889  CZ  ARG A 145    21795  17140  14203    635  -2755   1115  A    C  
ATOM    890  NH1 ARG A 145      35.804  47.383  13.296  1.00131.46      A    N1+
ANISOU  890  NH1 ARG A 145    20743  16190  13016    498  -2494    980  A    N1+
ATOM    891  NH2 ARG A 145      34.448  48.527  11.837  1.00144.47      A    N  
ANISOU  891  NH2 ARG A 145    22499  17739  14655    471  -2995   1436  A    N  
ATOM    892  N   LEU A 146      30.878  46.658  18.701  1.00131.09      A    N  
ANISOU  892  N   LEU A 146    19982  15675  14151   1808  -2277   -179  A    N  
ATOM    893  CA  LEU A 146      31.138  45.890  19.914  1.00124.74      A    C  
ANISOU  893  CA  LEU A 146    19154  14957  13283   1793  -2029   -446  A    C  
ATOM    894  C   LEU A 146      32.539  46.118  20.481  1.00118.82      A    C  
ANISOU  894  C   LEU A 146    18585  14117  12443   1642  -1947   -458  A    C  
ATOM    895  O   LEU A 146      32.716  46.183  21.695  1.00121.19      A    O  
ANISOU  895  O   LEU A 146    18923  14338  12785   1659  -1824   -653  A    O  
ATOM    896  CB  LEU A 146      30.932  44.399  19.644  1.00130.99      A    C  
ANISOU  896  CB  LEU A 146    19836  16065  13869   1703  -1921   -503  A    C  
ATOM    897  CG  LEU A 146      31.163  43.456  20.826  1.00121.89      A    C  
ANISOU  897  CG  LEU A 146    18660  15011  12640   1659  -1701   -726  A    C  
ATOM    898  CD1 LEU A 146      29.982  42.514  21.000  1.00123.32      A    C  
ANISOU  898  CD1 LEU A 146    18653  15377  12826   1720  -1630   -856  A    C  
ATOM    899  CD2 LEU A 146      32.456  42.671  20.648  1.00103.11      A    C  
ANISOU  899  CD2 LEU A 146    16372  12739  10067   1463  -1625   -676  A    C  
ATOM    900  N   ARG A 147      33.529  46.247  19.603  1.00118.50      A    N  
ANISOU  900  N   ARG A 147    18652  14105  12268   1469  -2017   -249  A    N  
ATOM    901  CA  ARG A 147      34.913  46.435  20.032  1.00114.30      A    C  
ANISOU  901  CA  ARG A 147    18247  13511  11669   1305  -1955   -233  A    C  
ATOM    902  C   ARG A 147      35.096  47.709  20.862  1.00114.28      A    C  
ANISOU  902  C   ARG A 147    18376  13191  11856   1354  -2016   -280  A    C  
ATOM    903  O   ARG A 147      36.028  47.794  21.657  1.00105.75      A    O  
ANISOU  903  O   ARG A 147    17383  12056  10744   1238  -1953   -348  A    O  
ATOM    904  CB  ARG A 147      35.854  46.450  18.831  1.00118.22      A    C  
ANISOU  904  CB  ARG A 147    18806  14105  12008   1103  -2001      0  A    C  
ATOM    905  CG  ARG A 147      35.795  47.716  18.009  1.00132.25      A    C  
ANISOU  905  CG  ARG A 147    20700  15695  13854   1076  -2210    244  A    C  
ATOM    906  CD  ARG A 147      36.796  47.667  16.876  1.00139.58      A    C  
ANISOU  906  CD  ARG A 147    21697  16768  14569    818  -2210    461  A    C  
ATOM    907  NE  ARG A 147      36.569  48.762  15.941  1.00140.23      A    N  
ANISOU  907  NE  ARG A 147    21900  16706  14673    759  -2441    743  A    N  
ATOM    908  CZ  ARG A 147      37.188  49.935  16.002  1.00133.18      A    C  
ANISOU  908  CZ  ARG A 147    21157  15559  13887    669  -2558    900  A    C  
ATOM    909  NH1 ARG A 147      38.086  50.161  16.949  1.00150.64      A    N1+
ANISOU  909  NH1 ARG A 147    23408  17653  16177    618  -2459    784  A    N1+
ATOM    910  NH2 ARG A 147      36.913  50.878  15.112  1.00114.53      A    N  
ANISOU  910  NH2 ARG A 147    18912  13054  11551    606  -2799   1192  A    N  
ATOM    911  N   THR A 148      34.245  48.711  20.641  1.00117.36      A    N  
ANISOU  911  N   THR A 148    18779  13355  12458   1516  -2158   -238  A    N  
ATOM    912  CA  THR A 148      34.242  49.917  21.472  1.00122.51      A    C  
ANISOU  912  CA  THR A 148    19552  13659  13336   1598  -2197   -344  A    C  
ATOM    913  C   THR A 148      33.765  49.590  22.887  1.00125.53      A    C  
ANISOU  913  C   THR A 148    19890  14049  13755   1695  -2003   -691  A    C  
ATOM    914  O   THR A 148      34.386  49.985  23.872  1.00134.52      A    O  
ANISOU  914  O   THR A 148    21170  15058  14885   1606  -1938   -836  A    O  
ATOM    915  CB  THR A 148      33.342  51.031  20.892  1.00126.57      A    C  
ANISOU  915  CB  THR A 148    20059  13888  14143   1788  -2402   -226  A    C  
ATOM    916  CG2 THR A 148      33.303  50.964  19.380  1.00132.54      A    C  
ANISOU  916  CG2 THR A 148    20796  14760  14802   1707  -2598    120  A    C  
ATOM    917  OG1 THR A 148      32.013  50.902  21.413  1.00129.23      A    O  
ANISOU  917  OG1 THR A 148    20216  14206  14679   2048  -2330   -451  A    O  
ATOM    918  N   TYR A 149      32.629  48.900  22.968  1.00111.42      A    N  
ANISOU  918  N   TYR A 149    17914  12425  11996   1849  -1917   -819  A    N  
ATOM    919  CA  TYR A 149      32.058  48.426  24.229  1.00 99.89      A    C  
ANISOU  919  CA  TYR A 149    16389  11044  10521   1907  -1703  -1137  A    C  
ATOM    920  C   TYR A 149      32.976  47.455  24.973  1.00106.33      A    C  
ANISOU  920  C   TYR A 149    17276  12067  11057   1684  -1576  -1197  A    C  
ATOM    921  O   TYR A 149      32.873  47.295  26.190  1.00 98.93      A    O  
ANISOU  921  O   TYR A 149    16383  11149  10055   1642  -1427  -1432  A    O  
ATOM    922  CB  TYR A 149      30.720  47.735  23.969  1.00102.42      A    C  
ANISOU  922  CB  TYR A 149    16460  11550  10906   2071  -1648  -1204  A    C  
ATOM    923  CG  TYR A 149      29.515  48.643  23.891  1.00109.09      A    C  
ANISOU  923  CG  TYR A 149    17166  12180  12105   2342  -1699  -1289  A    C  
ATOM    924  CD1 TYR A 149      29.353  49.705  24.766  1.00108.61      A    C  
ANISOU  924  CD1 TYR A 149    17180  11816  12269   2457  -1624  -1517  A    C  
ATOM    925  CD2 TYR A 149      28.529  48.427  22.935  1.00108.25      A    C  
ANISOU  925  CD2 TYR A 149    16839  12163  12128   2482  -1831  -1148  A    C  
ATOM    926  CE1 TYR A 149      28.233  50.528  24.687  1.00102.17      A    C  
ANISOU  926  CE1 TYR A 149    16197  10771  11852   2741  -1661  -1613  A    C  
ATOM    927  CE2 TYR A 149      27.417  49.241  22.849  1.00100.74      A    C  
ANISOU  927  CE2 TYR A 149    15710  11004  11562   2750  -1906  -1203  A    C  
ATOM    928  CZ  TYR A 149      27.275  50.291  23.724  1.00 98.63      A    C  
ANISOU  928  CZ  TYR A 149    15495  10414  11566   2896  -1812  -1439  A    C  
ATOM    929  OH  TYR A 149      26.166  51.098  23.633  1.00107.66      A    O  
ANISOU  929  OH  TYR A 149    16427  11317  13163   3195  -1878  -1511  A    O  
ATOM    930  N   ALA A 150      33.856  46.792  24.228  1.00119.16      A    N  
ANISOU  930  N   ALA A 150    18905  13848  12521   1533  -1637   -983  A    N  
ATOM    931  CA  ALA A 150      34.643  45.674  24.752  1.00114.76      A    C  
ANISOU  931  CA  ALA A 150    18351  13494  11760   1356  -1546  -1000  A    C  
ATOM    932  C   ALA A 150      35.575  46.026  25.919  1.00112.49      A    C  
ANISOU  932  C   ALA A 150    18226  13104  11413   1197  -1531  -1084  A    C  
ATOM    933  O   ALA A 150      35.480  45.391  26.968  1.00114.23      A    O  
ANISOU  933  O   ALA A 150    18455  13429  11518   1124  -1432  -1230  A    O  
ATOM    934  CB  ALA A 150      35.449  45.021  23.621  1.00122.27      A    C  
ANISOU  934  CB  ALA A 150    19253  14591  12613   1248  -1599   -777  A    C  
ATOM    935  N   PRO A 151      36.468  47.030  25.760  1.00114.11      A    N  
ANISOU  935  N   PRO A 151    18568  13110  11677   1109  -1644   -979  A    N  
ATOM    936  CA  PRO A 151      37.423  47.268  26.850  1.00103.44      A    C  
ANISOU  936  CA  PRO A 151    17364  11690  10246    914  -1659  -1043  A    C  
ATOM    937  C   PRO A 151      36.732  47.686  28.138  1.00 99.86      A    C  
ANISOU  937  C   PRO A 151    17022  11141   9779    940  -1559  -1337  A    C  
ATOM    938  O   PRO A 151      37.222  47.380  29.223  1.00116.60      A    O  
ANISOU  938  O   PRO A 151    19238  13325  11739    756  -1535  -1428  A    O  
ATOM    939  CB  PRO A 151      38.305  48.403  26.313  1.00106.49      A    C  
ANISOU  939  CB  PRO A 151    17870  11858  10734    826  -1803   -881  A    C  
ATOM    940  CG  PRO A 151      38.058  48.438  24.845  1.00115.01      A    C  
ANISOU  940  CG  PRO A 151    18849  12969  11880    924  -1857   -675  A    C  
ATOM    941  CD  PRO A 151      36.640  48.020  24.683  1.00117.14      A    C  
ANISOU  941  CD  PRO A 151    18998  13318  12192   1147  -1782   -792  A    C  
ATOM    942  N   ALA A 152      35.600  48.368  28.009  1.00 88.18      A    N  
ANISOU  942  N   ALA A 152    15520   9517   8469   1156  -1503  -1485  A    N  
ATOM    943  CA  ALA A 152      34.826  48.783  29.172  1.00105.15      A    C  
ANISOU  943  CA  ALA A 152    17743  11580  10628   1202  -1347  -1820  A    C  
ATOM    944  C   ALA A 152      34.383  47.572  29.986  1.00113.61      A    C  
ANISOU  944  C   ALA A 152    18738  12949  11478   1123  -1185  -1950  A    C  
ATOM    945  O   ALA A 152      34.562  47.531  31.204  1.00112.61      A    O  
ANISOU  945  O   ALA A 152    18757  12861  11169    946  -1097  -2136  A    O  
ATOM    946  CB  ALA A 152      33.620  49.606  28.745  1.00104.94      A    C  
ANISOU  946  CB  ALA A 152    17623  11352  10898   1494  -1309  -1942  A    C  
ATOM    947  N   LEU A 153      33.814  46.583  29.307  1.00115.97      A    N  
ANISOU  947  N   LEU A 153    18829  13459  11774   1221  -1159  -1842  A    N  
ATOM    948  CA  LEU A 153      33.361  45.371  29.976  1.00111.27      A    C  
ANISOU  948  CA  LEU A 153    18155  13134  10987   1134  -1023  -1926  A    C  
ATOM    949  C   LEU A 153      34.507  44.522  30.531  1.00109.35      A    C  
ANISOU  949  C   LEU A 153    18010  13023  10516    864  -1101  -1787  A    C  
ATOM    950  O   LEU A 153      34.432  44.057  31.666  1.00116.94      A    O  
ANISOU  950  O   LEU A 153    19054  14103  11277    691  -1018  -1905  A    O  
ATOM    951  CB  LEU A 153      32.495  44.542  29.022  1.00105.81      A    C  
ANISOU  951  CB  LEU A 153    17223  12608  10373   1290  -1003  -1833  A    C  
ATOM    952  CG  LEU A 153      31.959  43.207  29.543  1.00 91.45      A    C  
ANISOU  952  CG  LEU A 153    15304  11058   8385   1196   -880  -1885  A    C  
ATOM    953  CD1 LEU A 153      30.519  42.998  29.117  1.00 69.80      A    C  
ANISOU  953  CD1 LEU A 153    12334   8412   5775   1386   -774  -1984  A    C  
ATOM    954  CD2 LEU A 153      32.827  42.074  29.020  1.00 95.18      A    C  
ANISOU  954  CD2 LEU A 153    15752  11653   8761   1073   -995  -1640  A    C  
ATOM    955  N   LEU A 154      35.566  44.328  29.749  1.00 98.44      A    N  
ANISOU  955  N   LEU A 154    16608  11622   9171    815  -1262  -1532  A    N  
ATOM    956  CA  LEU A 154      36.676  43.473  30.177  1.00 98.21      A    C  
ANISOU  956  CA  LEU A 154    16607  11699   9009    595  -1358  -1376  A    C  
ATOM    957  C   LEU A 154      37.355  43.986  31.440  1.00107.73      A    C  
ANISOU  957  C   LEU A 154    18024  12836  10071    364  -1415  -1451  A    C  
ATOM    958  O   LEU A 154      37.690  43.209  32.336  1.00114.51      A    O  
ANISOU  958  O   LEU A 154    18931  13823  10755    164  -1452  -1417  A    O  
ATOM    959  CB  LEU A 154      37.723  43.327  29.070  1.00 92.86      A    C  
ANISOU  959  CB  LEU A 154    15839  10999   8444    597  -1485  -1126  A    C  
ATOM    960  CG  LEU A 154      37.544  42.158  28.099  1.00 96.20      A    C  
ANISOU  960  CG  LEU A 154    16068  11576   8908    685  -1451  -1012  A    C  
ATOM    961  CD1 LEU A 154      36.245  42.270  27.323  1.00103.36      A    C  
ANISOU  961  CD1 LEU A 154    16886  12513   9872    889  -1363  -1095  A    C  
ATOM    962  CD2 LEU A 154      38.742  42.048  27.160  1.00 85.19      A    C  
ANISOU  962  CD2 LEU A 154    14596  10171   7603    641  -1534   -811  A    C  
ATOM    963  N   CYS A 155      37.562  45.294  31.504  1.00102.75      A    N  
ANISOU  963  N   CYS A 155    17535  11993   9512    370  -1446  -1541  A    N  
ATOM    964  CA  CYS A 155      38.191  45.897  32.663  1.00103.46      A    C  
ANISOU  964  CA  CYS A 155    17855  12002   9454    127  -1508  -1642  A    C  
ATOM    965  C   CYS A 155      37.289  45.742  33.887  1.00100.84      A    C  
ANISOU  965  C   CYS A 155    17638  11771   8907     41  -1331  -1926  A    C  
ATOM    966  O   CYS A 155      37.764  45.401  34.966  1.00100.07      A    O  
ANISOU  966  O   CYS A 155    17687  11777   8560   -240  -1387  -1935  A    O  
ATOM    967  CB  CYS A 155      38.509  47.366  32.394  1.00115.24      A    C  
ANISOU  967  CB  CYS A 155    19482  13205  11097    159  -1568  -1701  A    C  
ATOM    968  SG  CYS A 155      39.523  48.150  33.656  1.00 98.80      A    S  
ANISOU  968  SG  CYS A 155    17696  11003   8841   -190  -1695  -1794  A    S  
ATOM    969  N   PHE A 156      35.993  45.995  33.719  1.00101.25      A    N  
ANISOU  969  N   PHE A 156    17614  11806   9052    264  -1121  -2150  A    N  
ATOM    970  CA  PHE A 156      35.024  45.798  34.800  1.00117.81      A    C  
ANISOU  970  CA  PHE A 156    19772  14035  10955    191   -890  -2445  A    C  
ATOM    971  C   PHE A 156      34.953  44.345  35.260  1.00109.47      A    C  
ANISOU  971  C   PHE A 156    18654  13275   9666     18   -884  -2316  A    C  
ATOM    972  O   PHE A 156      34.676  44.057  36.424  1.00105.33      A    O  
ANISOU  972  O   PHE A 156    18266  12899   8857   -214   -773  -2470  A    O  
ATOM    973  CB  PHE A 156      33.634  46.262  34.366  1.00126.56      A    C  
ANISOU  973  CB  PHE A 156    20721  15076  12290    502   -671  -2679  A    C  
ATOM    974  CG  PHE A 156      33.477  47.749  34.345  1.00140.28      A    C  
ANISOU  974  CG  PHE A 156    22564  16493  14244    642   -629  -2902  A    C  
ATOM    975  CD1 PHE A 156      34.384  48.559  35.010  1.00157.05      A    C  
ANISOU  975  CD1 PHE A 156    24964  18444  16262    429   -717  -2980  A    C  
ATOM    976  CD2 PHE A 156      32.424  48.341  33.666  1.00148.62      A    C  
ANISOU  976  CD2 PHE A 156    23439  17398  15631    978   -527  -3026  A    C  
ATOM    977  CE1 PHE A 156      34.249  49.933  34.996  1.00176.30      A    C  
ANISOU  977  CE1 PHE A 156    27519  20542  18926    550   -684  -3196  A    C  
ATOM    978  CE2 PHE A 156      32.282  49.715  33.649  1.00164.35      A    C  
ANISOU  978  CE2 PHE A 156    25526  19041  17879   1122   -509  -3222  A    C  
ATOM    979  CZ  PHE A 156      33.194  50.511  34.315  1.00172.30      A    C  
ANISOU  979  CZ  PHE A 156    26830  19855  18781    909   -577  -3317  A    C  
ATOM    980  N   CYS A 157      35.189  43.434  34.326  1.00105.21      A    N  
ANISOU  980  N   CYS A 157    17919  12811   9244    117   -999  -2039  A    N  
ATOM    981  CA  CYS A 157      35.192  42.011  34.621  1.00107.63      A    C  
ANISOU  981  CA  CYS A 157    18157  13339   9400    -25  -1029  -1880  A    C  
ATOM    982  C   CYS A 157      36.415  41.599  35.439  1.00105.03      A    C  
ANISOU  982  C   CYS A 157    17981  13043   8881   -341  -1247  -1688  A    C  
ATOM    983  O   CYS A 157      36.315  40.823  36.394  1.00 88.87      A    O  
ANISOU  983  O   CYS A 157    16020  11158   6589   -582  -1254  -1658  A    O  
ATOM    984  CB  CYS A 157      35.122  41.205  33.327  1.00106.53      A    C  
ANISOU  984  CB  CYS A 157    17774  13231   9471    178  -1083  -1676  A    C  
ATOM    985  SG  CYS A 157      33.428  40.934  32.761  1.00138.50      A    S  
ANISOU  985  SG  CYS A 157    21614  17387  13622    418   -853  -1847  A    S  
ATOM    986  N   GLU A 158      37.577  42.099  35.034  1.00114.96      A    N  
ANISOU  986  N   GLU A 158    19260  14154  10267   -353  -1446  -1529  A    N  
ATOM    987  CA  GLU A 158      38.823  41.794  35.720  1.00121.25      A    C  
ANISOU  987  CA  GLU A 158    20154  14965  10949   -637  -1696  -1318  A    C  
ATOM    988  C   GLU A 158      38.829  42.352  37.152  1.00139.22      A    C  
ANISOU  988  C   GLU A 158    22724  17275  12897   -949  -1696  -1495  A    C  
ATOM    989  O   GLU A 158      39.407  41.751  38.059  1.00153.48      A    O  
ANISOU  989  O   GLU A 158    24609  19191  14515  -1245  -1865  -1332  A    O  
ATOM    990  CB  GLU A 158      40.002  42.342  34.911  1.00116.54      A    C  
ANISOU  990  CB  GLU A 158    19482  14210  10588   -579  -1874  -1139  A    C  
ATOM    991  CG  GLU A 158      41.376  42.033  35.481  1.00135.36      A    C  
ANISOU  991  CG  GLU A 158    21891  16602  12938   -845  -2162   -890  A    C  
ATOM    992  CD  GLU A 158      41.834  40.611  35.199  1.00151.56      A    C  
ANISOU  992  CD  GLU A 158    23724  18743  15120   -830  -2286   -614  A    C  
ATOM    993  OE1 GLU A 158      40.979  39.711  35.051  1.00149.64      A    O  
ANISOU  993  OE1 GLU A 158    23403  18595  14858   -726  -2159   -641  A    O  
ATOM    994  OE2 GLU A 158      43.061  40.393  35.123  1.00167.18      A    O1-
ANISOU  994  OE2 GLU A 158    25592  20680  17248   -921  -2514   -376  A    O1-
ATOM    995  N   LYS A 159      38.190  43.504  37.344  1.00132.13      A    N  
ANISOU  995  N   LYS A 159    21962  16276  11966   -884  -1503  -1820  A    N  
ATOM    996  CA  LYS A 159      38.084  44.144  38.659  1.00110.10      A    C  
ANISOU  996  CA  LYS A 159    19371  13520   8941  -1153  -1411  -2044  A    C  
ATOM    997  C   LYS A 159      36.933  43.575  39.495  1.00 99.45      A    C  
ANISOU  997  C   LYS A 159    17963  12406   7416  -1231  -1139  -2215  A    C  
ATOM    998  O   LYS A 159      36.700  44.017  40.622  1.00118.36      A    O  
ANISOU  998  O   LYS A 159    20469  14880   9622  -1447  -1004  -2419  A    O  
ATOM    999  CB  LYS A 159      37.928  45.662  38.502  1.00106.74      A    C  
ANISOU  999  CB  LYS A 159    19108  12839   8611  -1040  -1309  -2349  A    C  
ATOM   1000  CG  LYS A 159      39.244  46.405  38.292  1.00100.70      A    C  
ANISOU 1000  CG  LYS A 159    18482  11870   7909  -1159  -1593  -2204  A    C  
ATOM   1001  CD  LYS A 159      39.025  47.813  37.748  1.00 97.50      A    C  
ANISOU 1001  CD  LYS A 159    18145  11156   7743   -954  -1504  -2426  A    C  
ATOM   1002  CE  LYS A 159      38.088  48.625  38.628  1.00 98.16      A    C  
ANISOU 1002  CE  LYS A 159    18419  11169   7710   -982  -1223  -2888  A    C  
ATOM   1003  NZ  LYS A 159      37.852  49.990  38.073  1.00 97.98      A    N1+
ANISOU 1003  NZ  LYS A 159    18466  10780   7983   -753  -1159  -3101  A    N1+
ATOM   1004  N   LEU A 160      36.203  42.624  38.915  1.00 87.88      A    N  
ANISOU 1004  N   LEU A 160    16327  11055   6009  -1062  -1053  -2147  A    N  
ATOM   1005  CA  LEU A 160      35.123  41.898  39.591  1.00 85.73      A    C  
ANISOU 1005  CA  LEU A 160    15974  11026   5574  -1152   -819  -2257  A    C  
ATOM   1006  C   LEU A 160      33.902  42.764  39.901  1.00 86.52      A    C  
ANISOU 1006  C   LEU A 160    16081  11133   5658  -1037   -453  -2704  A    C  
ATOM   1007  O   LEU A 160      33.113  42.434  40.787  1.00 88.83      A    O  
ANISOU 1007  O   LEU A 160    16345  11642   5764  -1191   -232  -2856  A    O  
ATOM   1008  CB  LEU A 160      35.628  41.233  40.880  1.00 81.87      A    C  
ANISOU 1008  CB  LEU A 160    15562  10719   4826  -1552   -936  -2073  A    C  
ATOM   1009  CG  LEU A 160      36.379  39.898  40.778  1.00 83.54      A    C  
ANISOU 1009  CG  LEU A 160    15708  10987   5048  -1677  -1233  -1640  A    C  
ATOM   1010  CD1 LEU A 160      37.699  40.040  40.047  1.00 78.17      A    C  
ANISOU 1010  CD1 LEU A 160    15029  10113   4560  -1607  -1556  -1391  A    C  
ATOM   1011  CD2 LEU A 160      36.596  39.294  42.157  1.00 97.69      A    C  
ANISOU 1011  CD2 LEU A 160    17597  12950   6571  -2075  -1313  -1490  A    C  
ATOM   1012  N   GLU A 161      33.740  43.862  39.171  1.00 93.33      A    N  
ANISOU 1012  N   GLU A 161    16982  11745   6735   -762   -392  -2913  A    N  
ATOM   1013  CA  GLU A 161      32.528  44.667  39.300  1.00111.87      A    C  
ANISOU 1013  CA  GLU A 161    19302  14041   9163   -577    -47  -3349  A    C  
ATOM   1014  C   GLU A 161      31.422  44.026  38.470  1.00123.89      A    C  
ANISOU 1014  C   GLU A 161    20599  15644  10831   -300     97  -3367  A    C  
ATOM   1015  O   GLU A 161      31.307  44.282  37.271  1.00127.18      A    O  
ANISOU 1015  O   GLU A 161    20810  15899  11615     34      9  -3252  A    O  
ATOM   1016  CB  GLU A 161      32.775  46.109  38.847  1.00124.97      A    C  
ANISOU 1016  CB  GLU A 161    21099  15334  11048   -372    -67  -3550  A    C  
ATOM   1017  CG  GLU A 161      34.189  46.621  39.114  1.00137.10      A    C  
ANISOU 1017  CG  GLU A 161    22835  16734  12525   -596   -350  -3376  A    C  
ATOM   1018  CD  GLU A 161      34.209  47.825  40.040  1.00154.75      A    C  
ANISOU 1018  CD  GLU A 161    25242  18836  14721   -730   -209  -3723  A    C  
ATOM   1019  OE1 GLU A 161      33.119  48.287  40.441  1.00154.21      A    O  
ANISOU 1019  OE1 GLU A 161    25121  18768  14705   -617    123  -4119  A    O  
ATOM   1020  OE2 GLU A 161      35.314  48.306  40.373  1.00165.75      A    O1-
ANISOU 1020  OE2 GLU A 161    26810  20124  16045   -949   -427  -3613  A    O1-
ATOM   1021  N   ALA A 162      30.607  43.195  39.116  1.00132.74      A    N  
ANISOU 1021  N   ALA A 162    21624  17054  11757   -454    303  -3439  A    N  
ATOM   1022  CA  ALA A 162      29.634  42.363  38.411  1.00130.18      A    C  
ANISOU 1022  CA  ALA A 162    21023  16864  11574   -264    401  -3377  A    C  
ATOM   1023  C   ALA A 162      28.478  43.164  37.821  1.00123.30      A    C  
ANISOU 1023  C   ALA A 162    19894  15882  11073    115    636  -3663  A    C  
ATOM   1024  O   ALA A 162      28.190  43.060  36.632  1.00101.32      A    O  
ANISOU 1024  O   ALA A 162    16861  13016   8618    414    524  -3500  A    O  
ATOM   1025  CB  ALA A 162      29.101  41.286  39.347  1.00130.98      A    C  
ANISOU 1025  CB  ALA A 162    21124  17300  11342   -583    554  -3374  A    C  
ATOM   1026  N   GLU A 163      27.821  43.958  38.661  1.00124.72      A    N  
ANISOU 1026  N   GLU A 163    20130  16057  11202     90    956  -4091  A    N  
ATOM   1027  CA  GLU A 163      26.660  44.751  38.255  1.00135.36      A    C  
ANISOU 1027  CA  GLU A 163    21202  17283  12947    456   1203  -4402  A    C  
ATOM   1028  C   GLU A 163      27.026  45.776  37.189  1.00129.05      A    C  
ANISOU 1028  C   GLU A 163    20352  16102  12581    810    980  -4312  A    C  
ATOM   1029  O   GLU A 163      26.189  46.164  36.374  1.00120.02      A    O  
ANISOU 1029  O   GLU A 163    18911  14839  11854   1167   1015  -4359  A    O  
ATOM   1030  CB  GLU A 163      26.028  45.445  39.467  1.00152.11      A    C  
ANISOU 1030  CB  GLU A 163    23421  19447  14926    337   1618  -4927  A    C  
ATOM   1031  CG  GLU A 163      24.946  44.626  40.168  1.00156.15      A    C  
ANISOU 1031  CG  GLU A 163    23770  20339  15221    157   1974  -5113  A    C  
ATOM   1032  CD  GLU A 163      25.464  43.311  40.725  1.00156.75      A    C  
ANISOU 1032  CD  GLU A 163    23980  20731  14845   -261   1813  -4759  A    C  
ATOM   1033  OE1 GLU A 163      26.650  43.252  41.115  1.00151.58      A    O  
ANISOU 1033  OE1 GLU A 163    23567  20035  13990   -487   1522  -4504  A    O  
ATOM   1034  OE2 GLU A 163      24.681  42.337  40.780  1.00160.88      A    O1-
ANISOU 1034  OE2 GLU A 163    24315  21534  15277   -356   1952  -4704  A    O1-
ATOM   1035  N   LYS A 164      28.266  46.251  37.239  1.00142.84      A    N  
ANISOU 1035  N   LYS A 164    22388  17658  14228    687    743  -4178  A    N  
ATOM   1036  CA  LYS A 164      28.782  47.165  36.228  1.00145.71      A    C  
ANISOU 1036  CA  LYS A 164    22746  17669  14947    949    497  -4030  A    C  
ATOM   1037  C   LYS A 164      28.852  46.472  34.866  1.00142.57      A    C  
ANISOU 1037  C   LYS A 164    22120  17317  14734   1126    244  -3617  A    C  
ATOM   1038  O   LYS A 164      28.456  47.035  33.846  1.00150.90      A    O  
ANISOU 1038  O   LYS A 164    22993  18179  16164   1439    151  -3548  A    O  
ATOM   1039  CB  LYS A 164      30.167  47.679  36.636  1.00144.33      A    C  
ANISOU 1039  CB  LYS A 164    22926  17333  14579    706    294  -3948  A    C  
ATOM   1040  CG  LYS A 164      30.137  48.693  37.762  1.00140.96      A    C  
ANISOU 1040  CG  LYS A 164    22755  16759  14046    573    508  -4385  A    C  
ATOM   1041  CD  LYS A 164      29.195  49.836  37.439  1.00141.69      A    C  
ANISOU 1041  CD  LYS A 164    22693  16545  14598    948    694  -4710  A    C  
ATOM   1042  CE  LYS A 164      29.033  50.769  38.620  1.00147.88      A    C  
ANISOU 1042  CE  LYS A 164    23719  17188  15283    819    980  -5229  A    C  
ATOM   1043  NZ  LYS A 164      28.485  50.054  39.804  1.00151.80      A    N1+
ANISOU 1043  NZ  LYS A 164    24262  18065  15352    529   1316  -5505  A    N1+
ATOM   1044  N   GLY A 165      29.370  45.246  34.874  1.00126.55      A    N  
ANISOU 1044  N   GLY A 165    20116  15534  12433    906    124  -3346  A    N  
ATOM   1045  CA  GLY A 165      29.480  44.424  33.682  1.00114.98      A    C  
ANISOU 1045  CA  GLY A 165    18464  14144  11081   1017    -78  -2998  A    C  
ATOM   1046  C   GLY A 165      28.130  44.056  33.085  1.00105.39      A    C  
ANISOU 1046  C   GLY A 165    16920  13046  10076   1243     45  -3052  A    C  
ATOM   1047  O   GLY A 165      27.972  43.983  31.868  1.00109.23      A    O  
ANISOU 1047  O   GLY A 165    17235  13483  10786   1444   -118  -2849  A    O  
ATOM   1048  N   TYR A 166      27.163  43.783  33.950  1.00 97.41      A    N  
ANISOU 1048  N   TYR A 166    15820  12221   8970   1176    331  -3321  A    N  
ATOM   1049  CA  TYR A 166      25.827  43.436  33.510  1.00106.88      A    C  
ANISOU 1049  CA  TYR A 166    16674  13556  10378   1363    467  -3396  A    C  
ATOM   1050  C   TYR A 166      25.193  44.656  32.846  1.00117.61      A    C  
ANISOU 1050  C   TYR A 166    17849  14650  12188   1735    461  -3522  A    C  
ATOM   1051  O   TYR A 166      24.471  44.537  31.855  1.00120.69      A    O  
ANISOU 1051  O   TYR A 166    17955  15049  12853   1959    364  -3400  A    O  
ATOM   1052  CB  TYR A 166      24.978  42.940  34.689  1.00114.02      A    C  
ANISOU 1052  CB  TYR A 166    17523  14730  11067   1169    813  -3677  A    C  
ATOM   1053  CG  TYR A 166      25.457  41.632  35.294  1.00128.48      A    C  
ANISOU 1053  CG  TYR A 166    19513  16823  12479    792    783  -3498  A    C  
ATOM   1054  CD1 TYR A 166      26.628  41.019  34.855  1.00127.02      A    C  
ANISOU 1054  CD1 TYR A 166    19495  16595  12174    676    473  -3144  A    C  
ATOM   1055  CD2 TYR A 166      24.761  41.034  36.336  1.00140.50      A    C  
ANISOU 1055  CD2 TYR A 166    21018  18624  13741    541   1067  -3683  A    C  
ATOM   1056  CE1 TYR A 166      27.075  39.837  35.416  1.00125.95      A    C  
ANISOU 1056  CE1 TYR A 166    19490  16648  11719    353    414  -2963  A    C  
ATOM   1057  CE2 TYR A 166      25.203  39.851  36.905  1.00146.55      A    C  
ANISOU 1057  CE2 TYR A 166    21947  19599  14137    178   1000  -3479  A    C  
ATOM   1058  CZ  TYR A 166      26.364  39.260  36.440  1.00136.55      A    C  
ANISOU 1058  CZ  TYR A 166    20835  18243  12805    101    657  -3112  A    C  
ATOM   1059  OH  TYR A 166      26.816  38.085  36.993  1.00135.90      A    O  
ANISOU 1059  OH  TYR A 166    20898  18318  12420   -235    557  -2887  A    O  
ATOM   1060  N   GLU A 167      25.473  45.830  33.407  1.00127.63      A    N  
ANISOU 1060  N   GLU A 167    19289  15666  13539   1784    544  -3760  A    N  
ATOM   1061  CA  GLU A 167      24.952  47.101  32.902  1.00126.44      A    C  
ANISOU 1061  CA  GLU A 167    18998  15185  13857   2136    527  -3893  A    C  
ATOM   1062  C   GLU A 167      25.474  47.450  31.508  1.00132.64      A    C  
ANISOU 1062  C   GLU A 167    19774  15756  14868   2309    145  -3513  A    C  
ATOM   1063  O   GLU A 167      24.709  47.925  30.669  1.00148.30      A    O  
ANISOU 1063  O   GLU A 167    21502  17599  17246   2605     48  -3458  A    O  
ATOM   1064  CB  GLU A 167      25.279  48.234  33.879  1.00125.47      A    C  
ANISOU 1064  CB  GLU A 167    19123  14809  13739   2100    697  -4246  A    C  
ATOM   1065  CG  GLU A 167      24.760  49.595  33.445  1.00130.46      A    C  
ANISOU 1065  CG  GLU A 167    19629  15033  14909   2472    682  -4406  A    C  
ATOM   1066  CD  GLU A 167      24.956  50.661  34.504  1.00135.04      A    C  
ANISOU 1066  CD  GLU A 167    20449  15356  15503   2428    909  -4837  A    C  
ATOM   1067  OE1 GLU A 167      24.847  50.338  35.707  1.00135.88      A    O  
ANISOU 1067  OE1 GLU A 167    20677  15683  15268   2175   1228  -5159  A    O  
ATOM   1068  OE2 GLU A 167      25.213  51.826  34.134  1.00132.50      A    O1-
ANISOU 1068  OE2 GLU A 167    20212  14607  15524   2624    766  -4857  A    O1-
ATOM   1069  N   VAL A 168      26.769  47.254  31.262  1.00119.86      A    N  
ANISOU 1069  N   VAL A 168    18421  14110  13010   2114    -74  -3248  A    N  
ATOM   1070  CA  VAL A 168      27.304  47.519  29.928  1.00123.08      A    C  
ANISOU 1070  CA  VAL A 168    18827  14362  13573   2224   -402  -2888  A    C  
ATOM   1071  C   VAL A 168      26.707  46.528  28.924  1.00124.35      A    C  
ANISOU 1071  C   VAL A 168    18729  14763  13755   2287   -507  -2654  A    C  
ATOM   1072  O   VAL A 168      26.359  46.917  27.815  1.00129.05      A    O  
ANISOU 1072  O   VAL A 168    19183  15243  14606   2482   -706  -2466  A    O  
ATOM   1073  CB  VAL A 168      28.864  47.488  29.885  1.00102.80      A    C  
ANISOU 1073  CB  VAL A 168    16565  11742  10754   1983   -582  -2669  A    C  
ATOM   1074  CG1 VAL A 168      29.414  46.167  30.350  1.00104.86      A    C  
ANISOU 1074  CG1 VAL A 168    16891  12314  10638   1706   -543  -2581  A    C  
ATOM   1075  CG2 VAL A 168      29.373  47.811  28.487  1.00 76.60      A    C  
ANISOU 1075  CG2 VAL A 168    13238   8285   7580   2072   -877  -2319  A    C  
ATOM   1076  N   GLU A 169      26.545  45.269  29.332  1.00122.72      A    N  
ANISOU 1076  N   GLU A 169    18470  14878  13281   2105   -384  -2666  A    N  
ATOM   1077  CA  GLU A 169      25.945  44.241  28.475  1.00127.95      A    C  
ANISOU 1077  CA  GLU A 169    18902  15771  13941   2126   -463  -2486  A    C  
ATOM   1078  C   GLU A 169      24.538  44.665  28.057  1.00129.08      A    C  
ANISOU 1078  C   GLU A 169    18710  15890  14443   2399   -434  -2582  A    C  
ATOM   1079  O   GLU A 169      24.153  44.527  26.894  1.00129.16      A    O  
ANISOU 1079  O   GLU A 169    18554  15924  14598   2511   -644  -2362  A    O  
ATOM   1080  CB  GLU A 169      25.894  42.879  29.186  1.00130.84      A    C  
ANISOU 1080  CB  GLU A 169    19273  16445  13996   1876   -308  -2526  A    C  
ATOM   1081  CG  GLU A 169      24.859  41.905  28.599  1.00133.70      A    C  
ANISOU 1081  CG  GLU A 169    19349  17043  14407   1906   -304  -2463  A    C  
ATOM   1082  CD  GLU A 169      24.665  40.631  29.423  1.00129.41      A    C  
ANISOU 1082  CD  GLU A 169    18808  16772  13590   1648   -133  -2523  A    C  
ATOM   1083  OE1 GLU A 169      25.656  39.921  29.684  1.00118.55      A    O  
ANISOU 1083  OE1 GLU A 169    17649  15435  11961   1430   -195  -2390  A    O  
ATOM   1084  OE2 GLU A 169      23.513  40.336  29.807  1.00129.78      A    O1-
ANISOU 1084  OE2 GLU A 169    18625  16989  13698   1658     55  -2688  A    O1-
ATOM   1085  N   GLU A 170      23.779  45.175  29.024  1.00131.91      A    N  
ANISOU 1085  N   GLU A 170    18964  16212  14944   2489   -169  -2921  A    N  
ATOM   1086  CA  GLU A 170      22.418  45.652  28.796  1.00154.71      A    C  
ANISOU 1086  CA  GLU A 170    21482  19057  18243   2772   -103  -3063  A    C  
ATOM   1087  C   GLU A 170      22.402  46.750  27.727  1.00165.70      A    C  
ANISOU 1087  C   GLU A 170    22819  20117  20022   3047   -403  -2872  A    C  
ATOM   1088  O   GLU A 170      21.503  46.795  26.886  1.00190.19      A    O  
ANISOU 1088  O   GLU A 170    25613  23229  23421   3241   -559  -2745  A    O  
ATOM   1089  CB  GLU A 170      21.807  46.152  30.113  1.00171.38      A    C  
ANISOU 1089  CB  GLU A 170    23532  21145  20441   2811    283  -3516  A    C  
ATOM   1090  CG  GLU A 170      20.298  46.383  30.079  1.00183.92      A    C  
ANISOU 1090  CG  GLU A 170    24660  22772  22451   3074    441  -3720  A    C  
ATOM   1091  CD  GLU A 170      19.621  45.998  31.385  1.00191.21      A    C  
ANISOU 1091  CD  GLU A 170    25476  23941  23232   2937    899  -4124  A    C  
ATOM   1092  OE1 GLU A 170      20.148  45.111  32.090  1.00186.81      A    O  
ANISOU 1092  OE1 GLU A 170    25154  23636  22191   2589   1025  -4128  A    O  
ATOM   1093  OE2 GLU A 170      18.558  46.572  31.703  1.00198.35      A    O1-
ANISOU 1093  OE2 GLU A 170    26053  24791  24518   3167   1134  -4431  A    O1-
ATOM   1094  N   HIS A 171      23.382  47.648  27.779  1.00149.75      A    N  
ANISOU 1094  N   HIS A 171    21095  17799  18002   3043   -503  -2836  A    N  
ATOM   1095  CA  HIS A 171      23.513  48.694  26.766  1.00136.93      A    C  
ANISOU 1095  CA  HIS A 171    19480  15840  16708   3249   -817  -2604  A    C  
ATOM   1096  C   HIS A 171      23.973  48.113  25.431  1.00123.85      A    C  
ANISOU 1096  C   HIS A 171    17862  14314  14881   3142  -1143  -2168  A    C  
ATOM   1097  O   HIS A 171      23.539  48.550  24.367  1.00137.88      A    O  
ANISOU 1097  O   HIS A 171    19498  15974  16916   3301  -1419  -1926  A    O  
ATOM   1098  CB  HIS A 171      24.494  49.776  27.218  1.00136.55      A    C  
ANISOU 1098  CB  HIS A 171    19763  15440  16679   3221   -831  -2682  A    C  
ATOM   1099  CG  HIS A 171      23.833  51.037  27.681  1.00146.51      A    C  
ANISOU 1099  CG  HIS A 171    20927  16328  18411   3504   -730  -2970  A    C  
ATOM   1100  CD2 HIS A 171      23.540  52.182  27.022  1.00152.35      A    C  
ANISOU 1100  CD2 HIS A 171    21592  16665  19628   3776   -959  -2860  A    C  
ATOM   1101  ND1 HIS A 171      23.386  51.212  28.972  1.00154.45      A    N  
ANISOU 1101  ND1 HIS A 171    21904  17333  19445   3523   -346  -3443  A    N  
ATOM   1102  CE1 HIS A 171      22.847  52.413  29.090  1.00163.47      A    C  
ANISOU 1102  CE1 HIS A 171    22947  18078  21088   3817   -316  -3651  A    C  
ATOM   1103  NE2 HIS A 171      22.928  53.022  27.920  1.00163.51      A    N  
ANISOU 1103  NE2 HIS A 171    22918  17814  21395   3985   -704  -3287  A    N  
ATOM   1104  N   MET A 172      24.858  47.125  25.505  1.00118.32      A    N  
ANISOU 1104  N   MET A 172    17354  13853  13747   2860  -1108  -2074  A    N  
ATOM   1105  CA  MET A 172      25.354  46.427  24.325  1.00112.10      A    C  
ANISOU 1105  CA  MET A 172    16615  13225  12753   2723  -1341  -1731  A    C  
ATOM   1106  C   MET A 172      24.242  45.755  23.534  1.00141.67      A    C  
ANISOU 1106  C   MET A 172    20056  17187  16585   2795  -1439  -1628  A    C  
ATOM   1107  O   MET A 172      24.234  45.800  22.309  1.00141.98      A    O  
ANISOU 1107  O   MET A 172    20074  17232  16641   2798  -1712  -1341  A    O  
ATOM   1108  CB  MET A 172      26.396  45.391  24.726  1.00107.23      A    C  
ANISOU 1108  CB  MET A 172    16203  12815  11723   2438  -1233  -1719  A    C  
ATOM   1109  CG  MET A 172      27.656  45.995  25.309  1.00 98.53      A    C  
ANISOU 1109  CG  MET A 172    15401  11525  10510   2320  -1212  -1742  A    C  
ATOM   1110  SD  MET A 172      28.898  44.761  25.692  1.00135.03      A    S  
ANISOU 1110  SD  MET A 172    20207  16372  14725   2007  -1146  -1675  A    S  
ATOM   1111  CE  MET A 172      29.534  44.427  24.057  1.00 70.49      A    C  
ANISOU 1111  CE  MET A 172    12048   8258   6477   1948  -1381  -1326  A    C  
ATOM   1112  N   GLU A 173      23.339  45.081  24.234  1.00167.61      A    N  
ANISOU 1112  N   GLU A 173    23121  20676  19886   2807  -1217  -1853  A    N  
ATOM   1113  CA  GLU A 173      22.205  44.427  23.593  1.00169.65      A    C  
ANISOU 1113  CA  GLU A 173    23060  21153  20247   2856  -1300  -1780  A    C  
ATOM   1114  C   GLU A 173      21.259  45.468  22.984  1.00156.46      A    C  
ANISOU 1114  C   GLU A 173    21125  19278  19044   3151  -1505  -1702  A    C  
ATOM   1115  O   GLU A 173      20.722  45.278  21.894  1.00160.29      A    O  
ANISOU 1115  O   GLU A 173    21445  19850  19608   3176  -1777  -1458  A    O  
ATOM   1116  CB  GLU A 173      21.481  43.518  24.602  1.00181.95      A    C  
ANISOU 1116  CB  GLU A 173    24441  22970  21721   2772   -988  -2049  A    C  
ATOM   1117  CG  GLU A 173      20.204  44.082  25.220  1.00196.46      A    C  
ANISOU 1117  CG  GLU A 173    25931  24771  23943   3003   -809  -2311  A    C  
ATOM   1118  CD  GLU A 173      20.011  43.641  26.656  1.00203.07      A    C  
ANISOU 1118  CD  GLU A 173    26769  25765  24623   2875   -402  -2654  A    C  
ATOM   1119  OE1 GLU A 173      20.778  42.768  27.117  1.00202.80      A    O  
ANISOU 1119  OE1 GLU A 173    26986  25885  24183   2597   -311  -2638  A    O  
ATOM   1120  OE2 GLU A 173      19.091  44.164  27.321  1.00204.67      A    O1-
ANISOU 1120  OE2 GLU A 173    26715  25936  25113   3044   -175  -2937  A    O1-
ATOM   1121  N   ALA A 174      21.097  46.580  23.693  1.00137.63      A    N  
ANISOU 1121  N   ALA A 174    18716  16603  16975   3363  -1391  -1908  A    N  
ATOM   1122  CA  ALA A 174      20.190  47.660  23.311  1.00145.69      A    C  
ANISOU 1122  CA  ALA A 174    19462  17356  18538   3690  -1560  -1879  A    C  
ATOM   1123  C   ALA A 174      20.529  48.419  22.027  1.00159.62      A    C  
ANISOU 1123  C   ALA A 174    21328  18883  20437   3753  -2003  -1473  A    C  
ATOM   1124  O   ALA A 174      19.632  48.759  21.256  1.00162.38      A    O  
ANISOU 1124  O   ALA A 174    21393  19170  21134   3935  -2275  -1287  A    O  
ATOM   1125  CB  ALA A 174      20.084  48.650  24.460  1.00146.94      A    C  
ANISOU 1125  CB  ALA A 174    19623  17222  18984   3881  -1287  -2250  A    C  
ATOM   1126  N   ALA A 175      21.811  48.689  21.799  1.00166.57      A    N  
ANISOU 1126  N   ALA A 175    22602  19642  21046   3585  -2090  -1319  A    N  
ATOM   1127  CA  ALA A 175      22.231  49.511  20.654  1.00168.74      A    C  
ANISOU 1127  CA  ALA A 175    23018  19677  21416   3600  -2487   -933  A    C  
ATOM   1128  C   ALA A 175      21.981  48.941  19.234  1.00166.59      A    C  
ANISOU 1128  C   ALA A 175    22679  19639  20980   3468  -2828   -543  A    C  
ATOM   1129  O   ALA A 175      21.397  49.652  18.415  1.00176.37      A    O  
ANISOU 1129  O   ALA A 175    23780  20700  22532   3614  -3174   -278  A    O  
ATOM   1130  CB  ALA A 175      23.720  49.885  20.810  1.00164.31      A    C  
ANISOU 1130  CB  ALA A 175    22885  18968  20578   3407  -2456   -880  A    C  
ATOM   1131  N   GLY A 176      22.387  47.709  18.909  1.00140.66      A    N  
ANISOU 1131  N   GLY A 176    19492  16725  17229   3192  -2758   -500  A    N  
ATOM   1132  CA  GLY A 176      23.055  46.790  19.806  1.00133.24      A    C  
ANISOU 1132  CA  GLY A 176    18696  15983  15946   3015  -2405   -759  A    C  
ATOM   1133  C   GLY A 176      23.680  45.581  19.142  1.00134.73      A    C  
ANISOU 1133  C   GLY A 176    19031  16491  15671   2716  -2414   -630  A    C  
ATOM   1134  O   GLY A 176      23.011  44.833  18.435  1.00133.27      A    O  
ANISOU 1134  O   GLY A 176    18686  16544  15406   2647  -2531   -532  A    O  
ATOM   1135  N   ILE A 177      24.977  45.401  19.358  1.00135.61      A    N  
ANISOU 1135  N   ILE A 177    19436  16594  15495   2535  -2295   -640  A    N  
ATOM   1136  CA  ILE A 177      25.694  44.254  18.812  1.00148.82      A    C  
ANISOU 1136  CA  ILE A 177    21244  18530  16771   2270  -2255   -566  A    C  
ATOM   1137  C   ILE A 177      25.648  43.132  19.840  1.00140.86      A    C  
ANISOU 1137  C   ILE A 177    20183  17704  15633   2200  -1963   -832  A    C  
ATOM   1138  O   ILE A 177      25.833  43.365  21.036  1.00129.71      A    O  
ANISOU 1138  O   ILE A 177    18806  16190  14287   2254  -1764  -1038  A    O  
ATOM   1139  CB  ILE A 177      27.151  44.582  18.430  1.00166.52      A    C  
ANISOU 1139  CB  ILE A 177    23785  20682  18803   2104  -2283   -420  A    C  
ATOM   1140  CG1 ILE A 177      27.180  45.667  17.350  1.00180.36      A    C  
ANISOU 1140  CG1 ILE A 177    25611  22268  20648   2121  -2591   -114  A    C  
ATOM   1141  CG2 ILE A 177      27.867  43.331  17.926  1.00167.44      A    C  
ANISOU 1141  CG2 ILE A 177    23996  21062  18561   1857  -2191   -404  A    C  
ATOM   1142  CD1 ILE A 177      28.497  45.770  16.598  1.00183.52      A    C  
ANISOU 1142  CD1 ILE A 177    26274  22686  20768   1882  -2633     81  A    C  
ATOM   1143  N   ALA A 178      25.400  41.913  19.373  1.00146.67      A    N  
ANISOU 1143  N   ALA A 178    20855  18702  16172   2054  -1949   -823  A    N  
ATOM   1144  CA  ALA A 178      25.413  40.759  20.258  1.00142.00      A    C  
ANISOU 1144  CA  ALA A 178    20238  18267  15448   1950  -1707  -1025  A    C  
ATOM   1145  C   ALA A 178      26.847  40.332  20.523  1.00123.83      A    C  
ANISOU 1145  C   ALA A 178    18186  15941  12922   1787  -1597  -1027  A    C  
ATOM   1146  O   ALA A 178      27.757  40.651  19.757  1.00118.23      A    O  
ANISOU 1146  O   ALA A 178    17636  15174  12114   1717  -1695   -872  A    O  
ATOM   1147  CB  ALA A 178      24.612  39.608  19.655  1.00158.81      A    C  
ANISOU 1147  CB  ALA A 178    22212  20647  17483   1843  -1748  -1016  A    C  
ATOM   1148  N   LEU A 179      27.025  39.565  21.592  1.00114.76      A    N  
ANISOU 1148  N   LEU A 179    17053  14850  11699   1710  -1399  -1188  A    N  
ATOM   1149  CA  LEU A 179      28.342  39.302  22.152  1.00 98.43      A    C  
ANISOU 1149  CA  LEU A 179    15183  12719   9496   1589  -1308  -1195  A    C  
ATOM   1150  C   LEU A 179      29.101  38.184  21.456  1.00 97.88      A    C  
ANISOU 1150  C   LEU A 179    15180  12752   9256   1426  -1311  -1122  A    C  
ATOM   1151  O   LEU A 179      28.542  37.137  21.139  1.00120.24      A    O  
ANISOU 1151  O   LEU A 179    17923  15732  12031   1357  -1291  -1157  A    O  
ATOM   1152  CB  LEU A 179      28.198  38.946  23.630  1.00 98.21      A    C  
ANISOU 1152  CB  LEU A 179    15155  12708   9450   1546  -1129  -1371  A    C  
ATOM   1153  CG  LEU A 179      27.501  39.965  24.531  1.00108.90      A    C  
ANISOU 1153  CG  LEU A 179    16454  13967  10955   1683  -1044  -1528  A    C  
ATOM   1154  CD1 LEU A 179      27.109  39.313  25.844  1.00114.82      A    C  
ANISOU 1154  CD1 LEU A 179    17180  14832  11613   1576   -841  -1708  A    C  
ATOM   1155  CD2 LEU A 179      28.376  41.177  24.771  1.00113.67      A    C  
ANISOU 1155  CD2 LEU A 179    17236  14339  11613   1731  -1090  -1508  A    C  
ATOM   1156  N   GLU A 180      30.381  38.429  21.203  1.00 96.87      A    N  
ANISOU 1156  N   GLU A 180    15200  12536   9070   1363  -1327  -1033  A    N  
ATOM   1157  CA  GLU A 180      31.270  37.387  20.716  1.00111.71      A    C  
ANISOU 1157  CA  GLU A 180    17127  14480  10839   1226  -1278  -1009  A    C  
ATOM   1158  C   GLU A 180      31.736  36.580  21.928  1.00101.65      A    C  
ANISOU 1158  C   GLU A 180    15871  13178   9572   1158  -1173  -1088  A    C  
ATOM   1159  O   GLU A 180      31.415  36.934  23.058  1.00 94.66      A    O  
ANISOU 1159  O   GLU A 180    14995  12250   8722   1187  -1139  -1152  A    O  
ATOM   1160  CB  GLU A 180      32.441  37.981  19.930  1.00130.31      A    C  
ANISOU 1160  CB  GLU A 180    19589  16772  13150   1176  -1318   -884  A    C  
ATOM   1161  CG  GLU A 180      32.132  38.153  18.438  1.00140.42      A    C  
ANISOU 1161  CG  GLU A 180    20874  18154  14326   1136  -1410   -788  A    C  
ATOM   1162  CD  GLU A 180      33.258  38.817  17.663  1.00150.75      A    C  
ANISOU 1162  CD  GLU A 180    22295  19423  15561   1047  -1430   -654  A    C  
ATOM   1163  OE1 GLU A 180      34.437  38.630  18.039  1.00166.29      A    O  
ANISOU 1163  OE1 GLU A 180    24296  21336  17550    988  -1327   -670  A    O  
ATOM   1164  OE2 GLU A 180      32.961  39.510  16.664  1.00151.44      A    O1-
ANISOU 1164  OE2 GLU A 180    22428  19543  15571   1018  -1559   -517  A    O1-
ATOM   1165  N   GLU A 181      32.459  35.488  21.698  1.00108.18      A    N  
ANISOU 1165  N   GLU A 181    16706  14024  10372   1060  -1125  -1086  A    N  
ATOM   1166  CA  GLU A 181      32.808  34.544  22.768  1.00109.05      A    C  
ANISOU 1166  CA  GLU A 181    16822  14098  10513    982  -1074  -1118  A    C  
ATOM   1167  C   GLU A 181      33.580  35.180  23.922  1.00105.77      A    C  
ANISOU 1167  C   GLU A 181    16493  13575  10122    960  -1096  -1075  A    C  
ATOM   1168  O   GLU A 181      33.237  34.979  25.086  1.00116.16      A    O  
ANISOU 1168  O   GLU A 181    17834  14895  11406    905  -1078  -1112  A    O  
ATOM   1169  CB  GLU A 181      33.616  33.373  22.199  1.00119.55      A    C  
ANISOU 1169  CB  GLU A 181    18132  15407  11884    911  -1037  -1116  A    C  
ATOM   1170  CG  GLU A 181      34.131  32.402  23.253  1.00114.51      A    C  
ANISOU 1170  CG  GLU A 181    17498  14681  11331    834  -1036  -1094  A    C  
ATOM   1171  CD  GLU A 181      35.495  31.838  22.919  1.00115.16      A    C  
ANISOU 1171  CD  GLU A 181    17552  14653  11551    816  -1023  -1053  A    C  
ATOM   1172  OE1 GLU A 181      36.000  32.093  21.804  1.00107.40      A    O  
ANISOU 1172  OE1 GLU A 181    16546  13692  10568    845   -966  -1078  A    O  
ATOM   1173  OE2 GLU A 181      36.068  31.145  23.782  1.00127.12      A    O1-
ANISOU 1173  OE2 GLU A 181    19056  16061  13181    764  -1071   -990  A    O1-
ATOM   1174  N   ALA A 182      34.629  35.926  23.590  1.00101.24      A    N  
ANISOU 1174  N   ALA A 182    15970  12917   9579    968  -1135   -996  A    N  
ATOM   1175  CA  ALA A 182      35.491  36.565  24.585  1.00 98.51      A    C  
ANISOU 1175  CA  ALA A 182    15712  12465   9254    916  -1184   -946  A    C  
ATOM   1176  C   ALA A 182      34.719  37.357  25.637  1.00 81.00      A    C  
ANISOU 1176  C   ALA A 182    13570  10229   6979    932  -1178  -1033  A    C  
ATOM   1177  O   ALA A 182      35.044  37.312  26.823  1.00 73.10      A    O  
ANISOU 1177  O   ALA A 182    12648   9198   5930    827  -1194  -1040  A    O  
ATOM   1178  CB  ALA A 182      36.492  37.469  23.894  1.00 99.17      A    C  
ANISOU 1178  CB  ALA A 182    15826  12475   9378    920  -1225   -853  A    C  
ATOM   1179  N   GLU A 183      33.709  38.096  25.194  1.00 80.39      A    N  
ANISOU 1179  N   GLU A 183    13463  10167   6913   1054  -1157  -1101  A    N  
ATOM   1180  CA  GLU A 183      32.916  38.918  26.100  1.00 91.00      A    C  
ANISOU 1180  CA  GLU A 183    14847  11477   8253   1102  -1110  -1233  A    C  
ATOM   1181  C   GLU A 183      32.044  38.058  27.010  1.00100.36      A    C  
ANISOU 1181  C   GLU A 183    15983  12791   9358   1034  -1004  -1347  A    C  
ATOM   1182  O   GLU A 183      31.918  38.344  28.199  1.00111.64      A    O  
ANISOU 1182  O   GLU A 183    17496  14214  10707    956   -938  -1451  A    O  
ATOM   1183  CB  GLU A 183      32.058  39.913  25.315  1.00 94.24      A    C  
ANISOU 1183  CB  GLU A 183    15195  11839   8772   1279  -1137  -1260  A    C  
ATOM   1184  CG  GLU A 183      32.846  41.045  24.643  1.00113.64      A    C  
ANISOU 1184  CG  GLU A 183    17746  14134  11299   1316  -1250  -1140  A    C  
ATOM   1185  CD  GLU A 183      33.501  40.614  23.337  1.00129.93      A    C  
ANISOU 1185  CD  GLU A 183    19783  16258  13325   1269  -1315   -973  A    C  
ATOM   1186  OE1 GLU A 183      32.892  39.796  22.621  1.00153.77      A    O  
ANISOU 1186  OE1 GLU A 183    22698  19420  16308   1282  -1301   -971  A    O  
ATOM   1187  OE2 GLU A 183      34.609  41.102  23.013  1.00116.82      A    O1-
ANISOU 1187  OE2 GLU A 183    18207  14513  11664   1198  -1368   -859  A    O1-
ATOM   1188  N   ILE A 184      31.439  37.009  26.461  1.00 94.96      A    N  
ANISOU 1188  N   ILE A 184    15176  12231   8673   1031   -981  -1334  A    N  
ATOM   1189  CA  ILE A 184      30.596  36.138  27.278  1.00100.98      A    C  
ANISOU 1189  CA  ILE A 184    15887  13123   9359    932   -883  -1419  A    C  
ATOM   1190  C   ILE A 184      31.398  35.358  28.314  1.00107.12      A    C  
ANISOU 1190  C   ILE A 184    16784  13889  10028    730   -904  -1348  A    C  
ATOM   1191  O   ILE A 184      30.985  35.239  29.465  1.00119.86      A    O  
ANISOU 1191  O   ILE A 184    18452  15572  11517    600   -825  -1420  A    O  
ATOM   1192  CB  ILE A 184      29.813  35.130  26.416  1.00115.30      A    C  
ANISOU 1192  CB  ILE A 184    17551  15055  11203    942   -879  -1408  A    C  
ATOM   1193  CG1 ILE A 184      29.296  35.800  25.141  1.00119.22      A    C  
ANISOU 1193  CG1 ILE A 184    17945  15558  11796   1110   -938  -1401  A    C  
ATOM   1194  CG2 ILE A 184      28.675  34.506  27.221  1.00123.53      A    C  
ANISOU 1194  CG2 ILE A 184    18507  16242  12184    848   -761  -1511  A    C  
ATOM   1195  CD1 ILE A 184      28.254  34.985  24.395  1.00113.73      A    C  
ANISOU 1195  CD1 ILE A 184    17091  15007  11113   1102   -944  -1420  A    C  
ATOM   1196  N   SER A 185      32.555  34.847  27.906  1.00100.94      A    N  
ANISOU 1196  N   SER A 185    16034  13019   9300    693  -1012  -1203  A    N  
ATOM   1197  CA  SER A 185      33.405  34.064  28.799  1.00 97.86      A    C  
ANISOU 1197  CA  SER A 185    15727  12585   8870    516  -1091  -1086  A    C  
ATOM   1198  C   SER A 185      33.893  34.917  29.970  1.00102.86      A    C  
ANISOU 1198  C   SER A 185    16515  13183   9385    406  -1125  -1093  A    C  
ATOM   1199  O   SER A 185      33.933  34.453  31.111  1.00104.94      A    O  
ANISOU 1199  O   SER A 185    16874  13488   9510    209  -1152  -1053  A    O  
ATOM   1200  CB  SER A 185      34.582  33.455  28.025  1.00 94.16      A    C  
ANISOU 1200  CB  SER A 185    15209  12008   8560    543  -1189   -951  A    C  
ATOM   1201  OG  SER A 185      35.599  34.404  27.760  1.00105.33      A    O  
ANISOU 1201  OG  SER A 185    16656  13333  10030    591  -1247   -901  A    O  
ATOM   1202  N   ALA A 186      34.253  36.166  29.682  1.00 95.55      A    N  
ANISOU 1202  N   ALA A 186    15631  12176   8496    506  -1135  -1137  A    N  
ATOM   1203  CA  ALA A 186      34.676  37.107  30.712  1.00 81.94      A    C  
ANISOU 1203  CA  ALA A 186    14073  10400   6661    398  -1161  -1183  A    C  
ATOM   1204  C   ALA A 186      33.527  37.390  31.678  1.00 92.62      A    C  
ANISOU 1204  C   ALA A 186    15487  11858   7846    335   -999  -1388  A    C  
ATOM   1205  O   ALA A 186      33.727  37.502  32.888  1.00113.90      A    O  
ANISOU 1205  O   ALA A 186    18342  14586  10349    127  -1000  -1425  A    O  
ATOM   1206  CB  ALA A 186      35.178  38.402  30.080  1.00 70.10      A    C  
ANISOU 1206  CB  ALA A 186    12604   8765   5268    524  -1199  -1199  A    C  
ATOM   1207  N   LEU A 187      32.328  37.521  31.120  1.00 83.15      A    N  
ANISOU 1207  N   LEU A 187    14150  10723   6721    501   -858  -1526  A    N  
ATOM   1208  CA  LEU A 187      31.104  37.701  31.893  1.00 86.70      A    C  
ANISOU 1208  CA  LEU A 187    14579  11295   7067    471   -657  -1746  A    C  
ATOM   1209  C   LEU A 187      30.782  36.472  32.729  1.00 90.12      A    C  
ANISOU 1209  C   LEU A 187    15034  11898   7311    229   -611  -1702  A    C  
ATOM   1210  O   LEU A 187      30.254  36.582  33.836  1.00103.45      A    O  
ANISOU 1210  O   LEU A 187    16804  13702   8800     61   -462  -1850  A    O  
ATOM   1211  CB  LEU A 187      29.941  38.017  30.960  1.00101.65      A    C  
ANISOU 1211  CB  LEU A 187    16258  13216   9149    717   -562  -1856  A    C  
ATOM   1212  CG  LEU A 187      29.864  39.472  30.513  1.00109.76      A    C  
ANISOU 1212  CG  LEU A 187    17281  14073  10350    935   -564  -1958  A    C  
ATOM   1213  CD1 LEU A 187      28.736  39.666  29.517  1.00110.21      A    C  
ANISOU 1213  CD1 LEU A 187    17099  14155  10620   1169   -537  -2000  A    C  
ATOM   1214  CD2 LEU A 187      29.668  40.359  31.732  1.00118.11      A    C  
ANISOU 1214  CD2 LEU A 187    18470  15090  11318    869   -410  -2202  A    C  
ATOM   1215  N   LEU A 188      31.066  35.299  32.175  1.00 89.79      A    N  
ANISOU 1215  N   LEU A 188    14920  11866   7332    200   -727  -1508  A    N  
ATOM   1216  CA  LEU A 188      30.876  34.049  32.899  1.00102.72      A    C  
ANISOU 1216  CA  LEU A 188    16591  13612   8825    -43   -736  -1408  A    C  
ATOM   1217  C   LEU A 188      31.819  33.962  34.093  1.00115.67      A    C  
ANISOU 1217  C   LEU A 188    18452  15228  10268   -309   -860  -1285  A    C  
ATOM   1218  O   LEU A 188      31.411  33.571  35.186  1.00124.38      A    O  
ANISOU 1218  O   LEU A 188    19663  16468  11128   -570   -796  -1297  A    O  
ATOM   1219  CB  LEU A 188      31.091  32.852  31.971  1.00 93.23      A    C  
ANISOU 1219  CB  LEU A 188    15276  12358   7790      3   -852  -1237  A    C  
ATOM   1220  CG  LEU A 188      30.940  31.467  32.603  1.00 79.02      A    C  
ANISOU 1220  CG  LEU A 188    13512  10610   5903   -240   -902  -1096  A    C  
ATOM   1221  CD1 LEU A 188      29.489  31.036  32.551  1.00 78.84      A    C  
ANISOU 1221  CD1 LEU A 188    13361  10762   5832   -276   -723  -1223  A    C  
ATOM   1222  CD2 LEU A 188      31.833  30.448  31.915  1.00 62.80      A    C  
ANISOU 1222  CD2 LEU A 188    11420   8386   4055   -206  -1087   -898  A    C  
ATOM   1223  N   LYS A 189      33.072  34.355  33.876  1.00113.54      A    N  
ANISOU 1223  N   LYS A 189    18246  14801  10092   -266  -1043  -1159  A    N  
ATOM   1224  CA  LYS A 189      34.110  34.307  34.909  1.00103.48      A    C  
ANISOU 1224  CA  LYS A 189    17159  13489   8668   -517  -1227  -1001  A    C  
ATOM   1225  C   LYS A 189      33.709  35.072  36.168  1.00103.45      A    C  
ANISOU 1225  C   LYS A 189    17358  13605   8345   -734  -1106  -1182  A    C  
ATOM   1226  O   LYS A 189      33.860  34.572  37.281  1.00112.87      A    O  
ANISOU 1226  O   LYS A 189    18714  14892   9280  -1052  -1182  -1079  A    O  
ATOM   1227  CB  LYS A 189      35.425  34.871  34.361  1.00 85.95      A    C  
ANISOU 1227  CB  LYS A 189    14927  11094   6635   -407  -1408   -886  A    C  
ATOM   1228  CG  LYS A 189      36.506  35.073  35.397  1.00 75.56      A    C  
ANISOU 1228  CG  LYS A 189    13787   9741   5182   -660  -1621   -738  A    C  
ATOM   1229  CD  LYS A 189      37.727  35.764  34.803  1.00 92.05      A    C  
ANISOU 1229  CD  LYS A 189    15827  11672   7475   -550  -1769   -650  A    C  
ATOM   1230  CE  LYS A 189      38.769  34.762  34.326  1.00 97.14      A    C  
ANISOU 1230  CE  LYS A 189    16311  12213   8385   -519  -1979   -376  A    C  
ATOM   1231  NZ  LYS A 189      40.088  35.416  34.075  1.00 94.43      A    N1+
ANISOU 1231  NZ  LYS A 189    15924  11754   8202   -504  -2141   -266  A    N1+
ATOM   1232  N   VAL A 190      33.163  36.267  35.978  1.00100.89      A    N  
ANISOU 1232  N   VAL A 190    17026  13270   8038   -570   -915  -1455  A    N  
ATOM   1233  CA  VAL A 190      32.801  37.134  37.090  1.00101.00      A    C  
ANISOU 1233  CA  VAL A 190    17229  13364   7784   -743   -755  -1702  A    C  
ATOM   1234  C   VAL A 190      31.654  36.553  37.904  1.00109.59      A    C  
ANISOU 1234  C   VAL A 190    18328  14688   8623   -941   -527  -1834  A    C  
ATOM   1235  O   VAL A 190      31.697  36.546  39.136  1.00124.54      A    O  
ANISOU 1235  O   VAL A 190    20327  16709  10284  -1240   -480  -1849  A    O  
ATOM   1236  CB  VAL A 190      32.412  38.529  36.589  1.00 91.78      A    C  
ANISOU 1236  CB  VAL A 190    16015  12075   6783   -472   -596  -1978  A    C  
ATOM   1237  CG1 VAL A 190      31.940  39.404  37.747  1.00 84.65      A    C  
ANISOU 1237  CG1 VAL A 190    15299  11235   5628   -637   -376  -2303  A    C  
ATOM   1238  CG2 VAL A 190      33.591  39.156  35.895  1.00 92.86      A    C  
ANISOU 1238  CG2 VAL A 190    16175  11993   7115   -346   -819  -1833  A    C  
ATOM   1239  N   SER A 191      30.630  36.065  37.212  1.00102.50      A    N  
ANISOU 1239  N   SER A 191    17195  13863   7885   -764   -378  -1889  A    N  
ATOM   1240  CA  SER A 191      29.482  35.464  37.877  1.00105.93      A    C  
ANISOU 1240  CA  SER A 191    17591  14539   8120   -953   -144  -2006  A    C  
ATOM   1241  C   SER A 191      29.935  34.275  38.717  1.00101.71      A    C  
ANISOU 1241  C   SER A 191    17223  14101   7319  -1339   -314  -1725  A    C  
ATOM   1242  O   SER A 191      29.400  34.025  39.798  1.00 79.09      A    O  
ANISOU 1242  O   SER A 191    14393  11434   4224  -1620   -159  -1773  A    O  
ATOM   1243  CB  SER A 191      28.425  35.037  36.857  1.00 97.04      A    C  
ANISOU 1243  CB  SER A 191    16156  13458   7255   -705    -26  -2053  A    C  
ATOM   1244  OG  SER A 191      27.719  36.157  36.354  1.00 96.26      A    O  
ANISOU 1244  OG  SER A 191    15897  13316   7360   -405    163  -2334  A    O  
ATOM   1245  N   ALA A 192      30.938  33.559  38.215  1.00 93.55      A    N  
ANISOU 1245  N   ALA A 192    16188  12906   6450  -1310   -632  -1398  A    N  
ATOM   1246  CA  ALA A 192      31.532  32.438  38.932  1.00 89.79      A    C  
ANISOU 1246  CA  ALA A 192    15852  12446   5816  -1638   -871  -1072  A    C  
ATOM   1247  C   ALA A 192      32.267  32.892  40.180  1.00 91.60      A    C  
ANISOU 1247  C   ALA A 192    16226  12702   5877  -1904   -963   -995  A    C  
ATOM   1248  O   ALA A 192      32.097  32.308  41.249  1.00101.69      A    O  
ANISOU 1248  O   ALA A 192    17588  14112   6938  -2241   -971   -869  A    O  
ATOM   1249  CB  ALA A 192      32.480  31.674  38.019  1.00 89.88      A    C  
ANISOU 1249  CB  ALA A 192    15754  12230   6167  -1469  -1169   -778  A    C  
ATOM   1250  N   ALA A 193      33.086  33.930  40.034  1.00 91.75      A    N  
ANISOU 1250  N   ALA A 193    16284  12589   5986  -1776  -1043  -1060  A    N  
ATOM   1251  CA  ALA A 193      33.878  34.466  41.140  1.00 97.75      A    C  
ANISOU 1251  CA  ALA A 193    17191  13356   6596  -2029  -1156   -999  A    C  
ATOM   1252  C   ALA A 193      33.004  35.117  42.213  1.00 89.78      A    C  
ANISOU 1252  C   ALA A 193    16246  12543   5322  -2208   -839  -1294  A    C  
ATOM   1253  O   ALA A 193      33.260  34.965  43.409  1.00104.85      A    O  
ANISOU 1253  O   ALA A 193    18291  14548   6997  -2554   -895  -1192  A    O  
ATOM   1254  CB  ALA A 193      34.902  35.457  40.622  1.00 78.07      A    C  
ANISOU 1254  CB  ALA A 193    14722  10671   4272  -1852  -1304  -1019  A    C  
ATOM   1255  N   THR A 194      31.976  35.844  41.782  1.00 82.75      A    N  
ANISOU 1255  N   THR A 194    15259  11704   4479  -1976   -510  -1663  A    N  
ATOM   1256  CA  THR A 194      31.029  36.454  42.712  1.00 94.22      A    C  
ANISOU 1256  CA  THR A 194    16741  13337   5721  -2101   -162  -1997  A    C  
ATOM   1257  C   THR A 194      30.013  35.428  43.220  1.00 96.53      A    C  
ANISOU 1257  C   THR A 194    16979  13865   5832  -2318     13  -1963  A    C  
ATOM   1258  O   THR A 194      29.146  35.760  44.026  1.00116.35      A    O  
ANISOU 1258  O   THR A 194    19495  16558   8155  -2457    328  -2225  A    O  
ATOM   1259  CB  THR A 194      30.278  37.645  42.079  1.00102.21      A    C  
ANISOU 1259  CB  THR A 194    17652  14286   6897  -1758    125  -2421  A    C  
ATOM   1260  CG2 THR A 194      31.247  38.758  41.724  1.00 85.01      A    C  
ANISOU 1260  CG2 THR A 194    15568  11867   4865  -1606    -31  -2468  A    C  
ATOM   1261  OG1 THR A 194      29.595  37.213  40.898  1.00113.97      A    O  
ANISOU 1261  OG1 THR A 194    18960  15757   8585  -1483    185  -2438  A    O  
ATOM   1262  N   GLY A 195      30.129  34.188  42.747  1.00 86.33      A    N  
ANISOU 1262  N   GLY A 195    15640  12558   4603  -2359   -187  -1646  A    N  
ATOM   1263  CA  GLY A 195      29.248  33.113  43.170  1.00 99.53      A    C  
ANISOU 1263  CA  GLY A 195    17277  14427   6111  -2603    -68  -1560  A    C  
ATOM   1264  C   GLY A 195      27.778  33.313  42.842  1.00118.88      A    C  
ANISOU 1264  C   GLY A 195    19543  17053   8575  -2463    336  -1906  A    C  
ATOM   1265  O   GLY A 195      26.906  32.950  43.633  1.00133.84      A    O  
ANISOU 1265  O   GLY A 195    21422  19177  10255  -2727    575  -1986  A    O  
ATOM   1266  N   ARG A 196      27.495  33.875  41.669  1.00122.20      A    N  
ANISOU 1266  N   ARG A 196    19812  17368   9250  -2068    409  -2104  A    N  
ATOM   1267  CA  ARG A 196      26.113  34.006  41.212  1.00120.96      A    C  
ANISOU 1267  CA  ARG A 196    19438  17363   9159  -1915    757  -2412  A    C  
ATOM   1268  C   ARG A 196      25.676  32.765  40.438  1.00119.66      A    C  
ANISOU 1268  C   ARG A 196    19162  17249   9053  -1936    669  -2215  A    C  
ATOM   1269  O   ARG A 196      26.111  32.543  39.310  1.00119.40      A    O  
ANISOU 1269  O   ARG A 196    19030  17013   9323  -1660    439  -2056  A    O  
ATOM   1270  CB  ARG A 196      25.960  35.239  40.316  1.00113.32      A    C  
ANISOU 1270  CB  ARG A 196    18370  16241   8445  -1498    867  -2722  A    C  
ATOM   1271  CG  ARG A 196      26.278  36.568  40.988  1.00106.33      A    C  
ANISOU 1271  CG  ARG A 196    17591  15273   7538  -1451    980  -2976  A    C  
ATOM   1272  CD  ARG A 196      25.324  36.886  42.119  1.00126.00      A    C  
ANISOU 1272  CD  ARG A 196    20038  17988   9848  -1635   1368  -3279  A    C  
ATOM   1273  NE  ARG A 196      23.942  36.995  41.665  1.00133.48      A    N  
ANISOU 1273  NE  ARG A 196    20703  19068  10945  -1451   1723  -3592  A    N  
ATOM   1274  CZ  ARG A 196      23.420  38.086  41.110  1.00139.43      A    C  
ANISOU 1274  CZ  ARG A 196    21301  19704  11973  -1097   1931  -3960  A    C  
ATOM   1275  NH1 ARG A 196      24.164  39.172  40.937  1.00135.88      A    N1+
ANISOU 1275  NH1 ARG A 196    20996  18983  11651   -902   1817  -4056  A    N1+
ATOM   1276  NH2 ARG A 196      22.151  38.093  40.726  1.00145.94      A    N  
ANISOU 1276  NH2 ARG A 196    21785  20665  13002   -929   2231  -4210  A    N  
ATOM   1277  N   GLU A 197      24.824  31.951  41.056  1.00125.87      A    N  
ANISOU 1277  N   GLU A 197    19895  18275   9653  -2235    840  -2190  A    N  
ATOM   1278  CA  GLU A 197      24.443  30.666  40.474  1.00134.36      A    C  
ANISOU 1278  CA  GLU A 197    20868  19384  10800  -2314    726  -1958  A    C  
ATOM   1279  C   GLU A 197      23.616  30.850  39.195  1.00141.74      A    C  
ANISOU 1279  C   GLU A 197    21420  20272  12161  -1898    822  -2110  A    C  
ATOM   1280  O   GLU A 197      23.935  30.273  38.157  1.00146.59      A    O  
ANISOU 1280  O   GLU A 197    21940  20703  13054  -1705    573  -1905  A    O  
ATOM   1281  CB  GLU A 197      23.695  29.767  41.477  1.00145.75      A    C  
ANISOU 1281  CB  GLU A 197    22353  21102  11921  -2783    889  -1883  A    C  
ATOM   1282  CG  GLU A 197      22.415  30.350  42.094  1.00155.82      A    C  
ANISOU 1282  CG  GLU A 197    23441  22677  13087  -2858   1375  -2268  A    C  
ATOM   1283  CD  GLU A 197      22.672  31.349  43.216  1.00159.37      A    C  
ANISOU 1283  CD  GLU A 197    24014  23151  13388  -2936   1534  -2452  A    C  
ATOM   1284  OE1 GLU A 197      23.660  32.110  43.145  1.00156.29      A    O  
ANISOU 1284  OE1 GLU A 197    23763  22539  13080  -2749   1346  -2443  A    O  
ATOM   1285  OE2 GLU A 197      21.868  31.378  44.172  1.00165.18      A    O1-
ANISOU 1285  OE2 GLU A 197    24705  24136  13920  -3204   1859  -2619  A    O1-
ATOM   1286  N   ASN A 198      22.558  31.653  39.275  1.00137.12      A    N  
ANISOU 1286  N   ASN A 198    20612  19853  11633  -1769   1179  -2473  A    N  
ATOM   1287  CA  ASN A 198      21.634  31.829  38.160  1.00125.44      A    C  
ANISOU 1287  CA  ASN A 198    18744  18368  10551  -1416   1259  -2601  A    C  
ATOM   1288  C   ASN A 198      22.276  32.510  36.961  1.00130.29      A    C  
ANISOU 1288  C   ASN A 198    19302  18690  11512   -978   1020  -2561  A    C  
ATOM   1289  O   ASN A 198      21.956  32.204  35.814  1.00145.23      A    O  
ANISOU 1289  O   ASN A 198    20973  20514  13694   -755    892  -2477  A    O  
ATOM   1290  CB  ASN A 198      20.409  32.623  38.607  1.00134.06      A    C  
ANISOU 1290  CB  ASN A 198    19584  19681  11670  -1363   1693  -3006  A    C  
ATOM   1291  CG  ASN A 198      19.486  31.813  39.492  1.00160.55      A    C  
ANISOU 1291  CG  ASN A 198    22875  23376  14749  -1779   1969  -3049  A    C  
ATOM   1292  ND2 ASN A 198      18.354  32.400  39.859  1.00179.32      A    N  
ANISOU 1292  ND2 ASN A 198    24976  25975  17183  -1742   2385  -3417  A    N  
ATOM   1293  OD1 ASN A 198      19.788  30.672  39.845  1.00164.42      A    O  
ANISOU 1293  OD1 ASN A 198    23553  23921  14998  -2135   1812  -2752  A    O  
ATOM   1294  N   LYS A 199      23.175  33.447  37.233  1.00120.31      A    N  
ANISOU 1294  N   LYS A 199    18251  17266  10195   -889    961  -2622  A    N  
ATOM   1295  CA  LYS A 199      23.876  34.145  36.167  1.00113.26      A    C  
ANISOU 1295  CA  LYS A 199    17338  16100   9594   -523    739  -2565  A    C  
ATOM   1296  C   LYS A 199      24.836  33.239  35.395  1.00104.60      A    C  
ANISOU 1296  C   LYS A 199    16331  14842   8571   -520    390  -2215  A    C  
ATOM   1297  O   LYS A 199      24.945  33.354  34.177  1.00110.88      A    O  
ANISOU 1297  O   LYS A 199    16989  15501   9640   -242    245  -2150  A    O  
ATOM   1298  CB  LYS A 199      24.626  35.351  36.728  1.00114.52      A    C  
ANISOU 1298  CB  LYS A 199    17719  16126   9667   -479    763  -2714  A    C  
ATOM   1299  CG  LYS A 199      24.215  36.664  36.086  1.00111.74      A    C  
ANISOU 1299  CG  LYS A 199    17187  15631   9639    -89    856  -2956  A    C  
ATOM   1300  CD  LYS A 199      22.722  36.923  36.202  1.00113.72      A    C  
ANISOU 1300  CD  LYS A 199    17120  16057  10033     11   1185  -3250  A    C  
ATOM   1301  CE  LYS A 199      22.342  38.181  35.431  1.00111.19      A    C  
ANISOU 1301  CE  LYS A 199    16592  15537  10120    437   1204  -3429  A    C  
ATOM   1302  NZ  LYS A 199      20.920  38.578  35.628  1.00112.52      A    N1+
ANISOU 1302  NZ  LYS A 199    16413  15845  10496    569   1534  -3748  A    N1+
ATOM   1303  N   VAL A 200      25.526  32.341  36.092  1.00 94.35      A    N  
ANISOU 1303  N   VAL A 200    15258  13554   7038   -834    255  -1993  A    N  
ATOM   1304  CA  VAL A 200      26.394  31.379  35.416  1.00 93.21      A    C  
ANISOU 1304  CA  VAL A 200    15165  13236   7014   -827    -50  -1685  A    C  
ATOM   1305  C   VAL A 200      25.562  30.477  34.508  1.00 94.47      A    C  
ANISOU 1305  C   VAL A 200    15094  13441   7358   -762    -49  -1643  A    C  
ATOM   1306  O   VAL A 200      25.983  30.132  33.402  1.00 85.12      A    O  
ANISOU 1306  O   VAL A 200    13847  12099   6396   -580   -227  -1531  A    O  
ATOM   1307  CB  VAL A 200      27.194  30.511  36.419  1.00 87.03      A    C  
ANISOU 1307  CB  VAL A 200    14641  12438   5988  -1190   -219  -1429  A    C  
ATOM   1308  CG1 VAL A 200      27.984  29.436  35.696  1.00 81.13      A    C  
ANISOU 1308  CG1 VAL A 200    13895  11483   5449  -1151   -508  -1139  A    C  
ATOM   1309  CG2 VAL A 200      28.121  31.370  37.250  1.00 74.09      A    C  
ANISOU 1309  CG2 VAL A 200    13241  10750   4159  -1281   -278  -1443  A    C  
ATOM   1310  N   TYR A 201      24.366  30.128  34.970  1.00102.96      A    N  
ANISOU 1310  N   TYR A 201    16041  14747   8333   -930    167  -1753  A    N  
ATOM   1311  CA  TYR A 201      23.455  29.299  34.190  1.00106.99      A    C  
ANISOU 1311  CA  TYR A 201    16319  15328   9003   -912    174  -1730  A    C  
ATOM   1312  C   TYR A 201      23.077  30.025  32.905  1.00115.25      A    C  
ANISOU 1312  C   TYR A 201    17129  16320  10342   -534    158  -1856  A    C  
ATOM   1313  O   TYR A 201      23.190  29.462  31.817  1.00129.79      A    O  
ANISOU 1313  O   TYR A 201    18902  18060  12352   -430    -13  -1749  A    O  
ATOM   1314  CB  TYR A 201      22.207  28.954  35.008  1.00105.78      A    C  
ANISOU 1314  CB  TYR A 201    16041  15466   8686  -1179    442  -1847  A    C  
ATOM   1315  CG  TYR A 201      21.219  28.033  34.319  1.00111.38      A    C  
ANISOU 1315  CG  TYR A 201    16507  16269   9542  -1227    444  -1811  A    C  
ATOM   1316  CD1 TYR A 201      21.522  26.695  34.088  1.00100.48      A    C  
ANISOU 1316  CD1 TYR A 201    15231  14780   8167  -1423    239  -1563  A    C  
ATOM   1317  CD2 TYR A 201      19.969  28.498  33.924  1.00124.46      A    C  
ANISOU 1317  CD2 TYR A 201    17820  18111  11357  -1086    639  -2027  A    C  
ATOM   1318  CE1 TYR A 201      20.612  25.851  33.464  1.00103.20      A    C  
ANISOU 1318  CE1 TYR A 201    15372  15200   8638  -1498    233  -1545  A    C  
ATOM   1319  CE2 TYR A 201      19.055  27.662  33.301  1.00119.94      A    C  
ANISOU 1319  CE2 TYR A 201    17016  17642  10915  -1161    618  -1987  A    C  
ATOM   1320  CZ  TYR A 201      19.381  26.341  33.074  1.00112.19      A    C  
ANISOU 1320  CZ  TYR A 201    16173  16554   9901  -1381    418  -1753  A    C  
ATOM   1321  OH  TYR A 201      18.467  25.515  32.457  1.00111.47      A    O  
ANISOU 1321  OH  TYR A 201    15869  16554   9932  -1483    390  -1728  A    O  
ATOM   1322  N   ARG A 202      22.668  31.286  33.031  1.00105.06      A    N  
ANISOU 1322  N   ARG A 202    15730  15078   9108   -339    324  -2083  A    N  
ATOM   1323  CA  ARG A 202      22.268  32.086  31.874  1.00 96.66      A    C  
ANISOU 1323  CA  ARG A 202    14443  13950   8333     12    279  -2172  A    C  
ATOM   1324  C   ARG A 202      23.393  32.228  30.855  1.00 87.26      A    C  
ANISOU 1324  C   ARG A 202    13383  12522   7249    192     12  -2008  A    C  
ATOM   1325  O   ARG A 202      23.183  32.048  29.655  1.00103.42      A    O  
ANISOU 1325  O   ARG A 202    15296  14534   9462    335   -121  -1948  A    O  
ATOM   1326  CB  ARG A 202      21.816  33.478  32.318  1.00 97.24      A    C  
ANISOU 1326  CB  ARG A 202    14420  14043   8483    195    484  -2432  A    C  
ATOM   1327  CG  ARG A 202      21.524  34.433  31.173  1.00 99.57      A    C  
ANISOU 1327  CG  ARG A 202    14515  14218   9100    565    384  -2478  A    C  
ATOM   1328  CD  ARG A 202      21.082  35.795  31.683  1.00114.60      A    C  
ANISOU 1328  CD  ARG A 202    16323  16084  11136    756    587  -2747  A    C  
ATOM   1329  NE  ARG A 202      19.925  35.708  32.570  1.00142.06      A    N  
ANISOU 1329  NE  ARG A 202    19589  19799  14589    642    914  -2987  A    N  
ATOM   1330  CZ  ARG A 202      18.683  36.029  32.216  1.00151.34      A    C  
ANISOU 1330  CZ  ARG A 202    20372  21075  16057    823   1031  -3133  A    C  
ATOM   1331  NH1 ARG A 202      18.434  36.468  30.989  1.00154.40      A    N1+
ANISOU 1331  NH1 ARG A 202    20561  21336  16766   1118    805  -3035  A    N1+
ATOM   1332  NH2 ARG A 202      17.691  35.918  33.090  1.00144.63      A    N  
ANISOU 1332  NH2 ARG A 202    19317  20460  15175    693   1369  -3368  A    N  
ATOM   1333  N   TYR A 203      24.586  32.551  31.342  1.00 74.07      A    N  
ANISOU 1333  N   TYR A 203    11969  10707   5467    156    -61  -1940  A    N  
ATOM   1334  CA  TYR A 203      25.732  32.790  30.470  1.00 80.67      A    C  
ANISOU 1334  CA  TYR A 203    12915  11333   6405    310   -276  -1803  A    C  
ATOM   1335  C   TYR A 203      26.295  31.505  29.865  1.00 80.79      A    C  
ANISOU 1335  C   TYR A 203    12978  11278   6442    214   -442  -1609  A    C  
ATOM   1336  O   TYR A 203      26.921  31.543  28.806  1.00101.98      A    O  
ANISOU 1336  O   TYR A 203    15666  13837   9245    357   -577  -1535  A    O  
ATOM   1337  CB  TYR A 203      26.827  33.567  31.207  1.00 95.80      A    C  
ANISOU 1337  CB  TYR A 203    15060  13122   8218    287   -306  -1794  A    C  
ATOM   1338  CG  TYR A 203      26.423  34.999  31.490  1.00104.42      A    C  
ANISOU 1338  CG  TYR A 203    16118  14197   9359    448   -168  -2010  A    C  
ATOM   1339  CD1 TYR A 203      25.273  35.536  30.920  1.00116.00      A    C  
ANISOU 1339  CD1 TYR A 203    17334  15723  11018    655    -69  -2157  A    C  
ATOM   1340  CD2 TYR A 203      27.199  35.821  32.294  1.00 94.76      A    C  
ANISOU 1340  CD2 TYR A 203    15104  12877   8024    396   -157  -2065  A    C  
ATOM   1341  CE1 TYR A 203      24.891  36.836  31.168  1.00115.97      A    C  
ANISOU 1341  CE1 TYR A 203    17281  15655  11129    831     53  -2362  A    C  
ATOM   1342  CE2 TYR A 203      26.827  37.126  32.541  1.00107.04      A    C  
ANISOU 1342  CE2 TYR A 203    16641  14374   9656    548    -24  -2291  A    C  
ATOM   1343  CZ  TYR A 203      25.671  37.626  31.973  1.00120.93      A    C  
ANISOU 1343  CZ  TYR A 203    18140  16163  11645    780     87  -2443  A    C  
ATOM   1344  OH  TYR A 203      25.286  38.924  32.209  1.00145.00      A    O  
ANISOU 1344  OH  TYR A 203    21150  19105  14838    960    215  -2676  A    O  
ATOM   1345  N   LEU A 204      26.121  30.377  30.544  1.00 69.17      A    N  
ANISOU 1345  N   LEU A 204    11554   9869   4857    -41   -427  -1531  A    N  
ATOM   1346  CA  LEU A 204      26.486  29.104  29.927  1.00 82.97      A    C  
ANISOU 1346  CA  LEU A 204    13322  11517   6685   -116   -571  -1381  A    C  
ATOM   1347  C   LEU A 204      25.567  28.815  28.742  1.00 90.02      A    C  
ANISOU 1347  C   LEU A 204    14014  12483   7706    -17   -567  -1454  A    C  
ATOM   1348  O   LEU A 204      26.007  28.301  27.716  1.00 87.24      A    O  
ANISOU 1348  O   LEU A 204    13669  12018   7461     46   -684  -1403  A    O  
ATOM   1349  CB  LEU A 204      26.435  27.953  30.929  1.00 87.03      A    C  
ANISOU 1349  CB  LEU A 204    13940  12052   7074   -428   -584  -1254  A    C  
ATOM   1350  CG  LEU A 204      27.617  27.832  31.890  1.00 94.16      A    C  
ANISOU 1350  CG  LEU A 204    15069  12828   7879   -570   -705  -1085  A    C  
ATOM   1351  CD1 LEU A 204      27.371  26.705  32.881  1.00 97.26      A    C  
ANISOU 1351  CD1 LEU A 204    15563  13260   8132   -913   -736   -929  A    C  
ATOM   1352  CD2 LEU A 204      28.924  27.626  31.128  1.00 85.33      A    C  
ANISOU 1352  CD2 LEU A 204    13999  11460   6963   -417   -897   -964  A    C  
ATOM   1353  N   HIS A 205      24.287  29.142  28.895  1.00 95.04      A    N  
ANISOU 1353  N   HIS A 205    14462  13319   8331    -19   -428  -1584  A    N  
ATOM   1354  CA  HIS A 205      23.326  29.018  27.803  1.00 91.53      A    C  
ANISOU 1354  CA  HIS A 205    13795  12969   8012     69   -455  -1643  A    C  
ATOM   1355  C   HIS A 205      23.605  30.039  26.719  1.00104.37      A    C  
ANISOU 1355  C   HIS A 205    15378  14523   9753    344   -551  -1665  A    C  
ATOM   1356  O   HIS A 205      23.419  29.769  25.534  1.00122.98      A    O  
ANISOU 1356  O   HIS A 205    17666  16883  12179    395   -668  -1641  A    O  
ATOM   1357  CB  HIS A 205      21.895  29.184  28.303  1.00 91.99      A    C  
ANISOU 1357  CB  HIS A 205    13612  13265   8076      7   -283  -1769  A    C  
ATOM   1358  CG  HIS A 205      21.308  27.932  28.868  1.00 99.73      A    C  
ANISOU 1358  CG  HIS A 205    14570  14356   8965   -302   -223  -1725  A    C  
ATOM   1359  CD2 HIS A 205      20.124  27.698  29.481  1.00114.76      A    C  
ANISOU 1359  CD2 HIS A 205    16280  16490  10834   -469    -49  -1807  A    C  
ATOM   1360  ND1 HIS A 205      21.957  26.717  28.812  1.00 91.42      A    N  
ANISOU 1360  ND1 HIS A 205    13704  13162   7871   -485   -350  -1575  A    N  
ATOM   1361  CE1 HIS A 205      21.203  25.792  29.379  1.00106.75      A    C  
ANISOU 1361  CE1 HIS A 205    15592  15224   9743   -766   -280  -1545  A    C  
ATOM   1362  NE2 HIS A 205      20.085  26.361  29.792  1.00120.17      A    N  
ANISOU 1362  NE2 HIS A 205    17061  17171  11429   -775    -87  -1684  A    N  
ATOM   1363  N   LYS A 206      24.051  31.217  27.138  1.00102.90      A    N  
ANISOU 1363  N   LYS A 206    15253  14273   9569    489   -508  -1706  A    N  
ATOM   1364  CA  LYS A 206      24.421  32.261  26.200  1.00 96.67      A    C  
ANISOU 1364  CA  LYS A 206    14459  13387   8885    725   -614  -1692  A    C  
ATOM   1365  C   LYS A 206      25.557  31.746  25.327  1.00 89.14      A    C  
ANISOU 1365  C   LYS A 206    13661  12299   7910    710   -756  -1569  A    C  
ATOM   1366  O   LYS A 206      25.562  31.942  24.115  1.00104.67      A    O  
ANISOU 1366  O   LYS A 206    15589  14257   9923    802   -864  -1535  A    O  
ATOM   1367  CB  LYS A 206      24.842  33.531  26.943  1.00101.49      A    C  
ANISOU 1367  CB  LYS A 206    15153  13907   9501    842   -543  -1758  A    C  
ATOM   1368  CG  LYS A 206      24.250  34.816  26.398  1.00109.71      A    C  
ANISOU 1368  CG  LYS A 206    16045  14921  10720   1089   -567  -1823  A    C  
ATOM   1369  CD  LYS A 206      22.761  34.897  26.686  1.00116.48      A    C  
ANISOU 1369  CD  LYS A 206    16617  15945  11694   1127   -439  -1965  A    C  
ATOM   1370  CE  LYS A 206      22.200  36.248  26.282  1.00127.89      A    C  
ANISOU 1370  CE  LYS A 206    17895  17311  13386   1402   -474  -2029  A    C  
ATOM   1371  NZ  LYS A 206      20.740  36.348  26.552  1.00133.75      A    N1+
ANISOU 1371  NZ  LYS A 206    18298  18211  14309   1467   -342  -2178  A    N1+
ATOM   1372  N   LEU A 207      26.495  31.043  25.951  1.00 72.49      A    N  
ANISOU 1372  N   LEU A 207    11718  10091   5732    577   -754  -1503  A    N  
ATOM   1373  CA  LEU A 207      27.612  30.439  25.239  1.00 76.87      A    C  
ANISOU 1373  CA  LEU A 207    12385  10505   6316    565   -850  -1416  A    C  
ATOM   1374  C   LEU A 207      27.163  29.384  24.244  1.00 91.40      A    C  
ANISOU 1374  C   LEU A 207    14161  12383   8184    496   -890  -1436  A    C  
ATOM   1375  O   LEU A 207      27.710  29.287  23.148  1.00105.78      A    O  
ANISOU 1375  O   LEU A 207    16017  14148  10028    546   -945  -1434  A    O  
ATOM   1376  CB  LEU A 207      28.604  29.812  26.220  1.00 87.27      A    C  
ANISOU 1376  CB  LEU A 207    13848  11697   7615    435   -864  -1324  A    C  
ATOM   1377  CG  LEU A 207      29.657  30.717  26.853  1.00 85.85      A    C  
ANISOU 1377  CG  LEU A 207    13787  11418   7414    484   -890  -1270  A    C  
ATOM   1378  CD1 LEU A 207      30.607  29.876  27.687  1.00 94.12      A    C  
ANISOU 1378  CD1 LEU A 207    14949  12343   8470    332   -965  -1137  A    C  
ATOM   1379  CD2 LEU A 207      30.414  31.482  25.783  1.00 84.50      A    C  
ANISOU 1379  CD2 LEU A 207    13622  11169   7316    648   -941  -1257  A    C  
ATOM   1380  N   ARG A 208      26.182  28.580  24.636  1.00101.07      A    N  
ANISOU 1380  N   ARG A 208    15302  13708   9391    352   -852  -1468  A    N  
ATOM   1381  CA  ARG A 208      25.684  27.517  23.772  1.00107.41      A    C  
ANISOU 1381  CA  ARG A 208    16056  14538  10216    246   -897  -1501  A    C  
ATOM   1382  C   ARG A 208      25.096  28.092  22.495  1.00125.06      A    C  
ANISOU 1382  C   ARG A 208    18182  16889  12444    347   -967  -1550  A    C  
ATOM   1383  O   ARG A 208      25.341  27.589  21.398  1.00157.22      A    O  
ANISOU 1383  O   ARG A 208    22304  20933  16499    311  -1028  -1578  A    O  
ATOM   1384  CB  ARG A 208      24.603  26.700  24.474  1.00 96.68      A    C  
ANISOU 1384  CB  ARG A 208    14605  13292   8839     50   -847  -1515  A    C  
ATOM   1385  CG  ARG A 208      24.061  25.578  23.615  1.00 93.68      A    C  
ANISOU 1385  CG  ARG A 208    14185  12924   8486    -91   -908  -1556  A    C  
ATOM   1386  CD  ARG A 208      22.694  25.088  24.065  1.00 99.22      A    C  
ANISOU 1386  CD  ARG A 208    14720  13806   9172   -272   -866  -1578  A    C  
ATOM   1387  NE  ARG A 208      21.646  26.063  23.768  1.00100.47      A    N  
ANISOU 1387  NE  ARG A 208    14642  14187   9343   -158   -854  -1635  A    N  
ATOM   1388  CZ  ARG A 208      21.155  26.944  24.630  1.00107.37      A    C  
ANISOU 1388  CZ  ARG A 208    15388  15183  10225    -80   -736  -1661  A    C  
ATOM   1389  NH1 ARG A 208      21.614  26.990  25.869  1.00118.16      A    N1+
ANISOU 1389  NH1 ARG A 208    16872  16503  11521   -141   -617  -1637  A    N1+
ATOM   1390  NH2 ARG A 208      20.198  27.780  24.248  1.00108.03      A    N  
ANISOU 1390  NH2 ARG A 208    15223  15429  10395     52   -744  -1717  A    N  
ATOM   1391  N   GLU A 209      24.330  29.167  22.659  1.00110.28      A    N  
ANISOU 1391  N   GLU A 209    16167  15142  10592    466   -960  -1561  A    N  
ATOM   1392  CA  GLU A 209      23.593  29.786  21.566  1.00 97.42      A    C  
ANISOU 1392  CA  GLU A 209    14399  13629   8986    556  -1073  -1560  A    C  
ATOM   1393  C   GLU A 209      24.496  30.435  20.515  1.00106.57      A    C  
ANISOU 1393  C   GLU A 209    15688  14705  10099    659  -1170  -1502  A    C  
ATOM   1394  O   GLU A 209      24.155  30.468  19.329  1.00118.96      A    O  
ANISOU 1394  O   GLU A 209    17226  16357  11615    634  -1297  -1479  A    O  
ATOM   1395  CB  GLU A 209      22.625  30.831  22.123  1.00 84.69      A    C  
ANISOU 1395  CB  GLU A 209    12578  12119   7482    694  -1039  -1585  A    C  
ATOM   1396  CG  GLU A 209      21.427  31.102  21.234  1.00111.26      A    C  
ANISOU 1396  CG  GLU A 209    15704  15640  10931    733  -1177  -1570  A    C  
ATOM   1397  CD  GLU A 209      20.289  31.753  21.987  1.00127.05      A    C  
ANISOU 1397  CD  GLU A 209    17422  17747  13103    839  -1093  -1637  A    C  
ATOM   1398  OE1 GLU A 209      20.459  32.015  23.196  1.00118.37      A    O  
ANISOU 1398  OE1 GLU A 209    16352  16610  12013    863   -900  -1719  A    O  
ATOM   1399  OE2 GLU A 209      19.226  31.995  21.374  1.00138.31      A    O1-
ANISOU 1399  OE2 GLU A 209    18591  19302  14659    886  -1217  -1614  A    O1-
ATOM   1400  N   TYR A 210      25.639  30.959  20.950  1.00107.15      A    N  
ANISOU 1400  N   TYR A 210    15907  14632  10173    741  -1117  -1467  A    N  
ATOM   1401  CA  TYR A 210      26.490  31.745  20.062  1.00105.94      A    C  
ANISOU 1401  CA  TYR A 210    15860  14413   9978    827  -1187  -1399  A    C  
ATOM   1402  C   TYR A 210      27.866  31.122  19.814  1.00102.30      A    C  
ANISOU 1402  C   TYR A 210    15566  13828   9474    760  -1128  -1405  A    C  
ATOM   1403  O   TYR A 210      28.653  31.655  19.035  1.00 97.06      A    O  
ANISOU 1403  O   TYR A 210    14987  13131   8759    791  -1152  -1359  A    O  
ATOM   1404  CB  TYR A 210      26.660  33.161  20.624  1.00107.34      A    C  
ANISOU 1404  CB  TYR A 210    16036  14516  10232    996  -1193  -1348  A    C  
ATOM   1405  CG  TYR A 210      25.355  33.923  20.748  1.00118.73      A    C  
ANISOU 1405  CG  TYR A 210    17282  16044  11786   1111  -1246  -1359  A    C  
ATOM   1406  CD1 TYR A 210      24.570  33.807  21.888  1.00123.12      A    C  
ANISOU 1406  CD1 TYR A 210    17708  16652  12419   1117  -1125  -1460  A    C  
ATOM   1407  CD2 TYR A 210      24.907  34.753  19.728  1.00125.95      A    C  
ANISOU 1407  CD2 TYR A 210    18127  16986  12743   1203  -1417  -1263  A    C  
ATOM   1408  CE1 TYR A 210      23.378  34.493  22.010  1.00123.16      A    C  
ANISOU 1408  CE1 TYR A 210    17484  16732  12579   1242  -1140  -1500  A    C  
ATOM   1409  CE2 TYR A 210      23.714  35.445  19.843  1.00132.73      A    C  
ANISOU 1409  CE2 TYR A 210    18761  17893  13778   1337  -1485  -1265  A    C  
ATOM   1410  CZ  TYR A 210      22.955  35.310  20.987  1.00131.50      A    C  
ANISOU 1410  CZ  TYR A 210    18443  17784  13737   1371  -1329  -1402  A    C  
ATOM   1411  OH  TYR A 210      21.767  35.994  21.113  1.00139.75      A    O  
ANISOU 1411  OH  TYR A 210    19217  18874  15007   1523  -1363  -1435  A    O  
ATOM   1412  N   VAL A 211      28.169  30.019  20.497  1.00110.73      A    N  
ANISOU 1412  N   VAL A 211    16666  14820  10585    665  -1050  -1451  A    N  
ATOM   1413  CA  VAL A 211      29.384  29.237  20.228  1.00112.18      A    C  
ANISOU 1413  CA  VAL A 211    16955  14863  10805    616   -996  -1475  A    C  
ATOM   1414  C   VAL A 211      29.099  27.738  20.333  1.00116.77      A    C  
ANISOU 1414  C   VAL A 211    17535  15394  11439    476   -968  -1552  A    C  
ATOM   1415  O   VAL A 211      28.261  27.314  21.132  1.00114.97      A    O  
ANISOU 1415  O   VAL A 211    17252  15206  11227    402   -977  -1541  A    O  
ATOM   1416  CB  VAL A 211      30.549  29.580  21.202  1.00135.21      A    C  
ANISOU 1416  CB  VAL A 211    19935  17629  13810    673   -967  -1396  A    C  
ATOM   1417  CG1 VAL A 211      31.867  29.004  20.687  1.00123.32      A    C  
ANISOU 1417  CG1 VAL A 211    18479  15985  12392    665   -916  -1417  A    C  
ATOM   1418  CG2 VAL A 211      30.679  31.085  21.424  1.00138.07      A    C  
ANISOU 1418  CG2 VAL A 211    20309  18014  14138    789  -1000  -1324  A    C  
ATOM   1419  N   GLY A 212      29.805  26.937  19.542  1.00121.31      A    N  
ANISOU 1419  N   GLY A 212    18171  15870  12051    429   -921  -1641  A    N  
ATOM   1420  CA  GLY A 212      29.660  25.495  19.616  1.00123.42      A    C  
ANISOU 1420  CA  GLY A 212    18457  16021  12417    306   -898  -1726  A    C  
ATOM   1421  C   GLY A 212      30.831  24.866  20.343  1.00119.76      A    C  
ANISOU 1421  C   GLY A 212    18030  15306  12167    337   -867  -1682  A    C  
ATOM   1422  O   GLY A 212      30.753  24.590  21.539  1.00108.07      A    O  
ANISOU 1422  O   GLY A 212    16548  13750  10764    299   -920  -1563  A    O  
ATOM   1423  N   CYS A 213      31.925  24.647  19.622  1.00130.67      A    N  
ANISOU 1423  N   CYS A 213    19435  16567  13649    392   -785  -1770  A    N  
ATOM   1424  CA  CYS A 213      33.160  24.201  20.249  1.00132.62      A    C  
ANISOU 1424  CA  CYS A 213    19666  16569  14156    459   -775  -1710  A    C  
ATOM   1425  C   CYS A 213      33.827  25.419  20.871  1.00139.95      A    C  
ANISOU 1425  C   CYS A 213    20574  17546  15054    558   -815  -1550  A    C  
ATOM   1426  O   CYS A 213      33.969  26.456  20.226  1.00146.71      A    O  
ANISOU 1426  O   CYS A 213    21433  18544  15765    612   -774  -1564  A    O  
ATOM   1427  CB  CYS A 213      34.083  23.513  19.240  1.00128.52      A    C  
ANISOU 1427  CB  CYS A 213    19132  15900  13798    492   -636  -1899  A    C  
ATOM   1428  SG  CYS A 213      34.354  24.438  17.712  1.00309.50      A    S  
ANISOU 1428  SG  CYS A 213    42076  39046  36474    505   -490  -2047  A    S  
ATOM   1429  N   VAL A 214      34.220  25.293  22.133  1.00137.20      A    N  
ANISOU 1429  N   VAL A 214    20224  17076  14830    552   -914  -1385  A    N  
ATOM   1430  CA  VAL A 214      34.721  26.432  22.891  1.00118.94      A    C  
ANISOU 1430  CA  VAL A 214    17919  14813  12460    601   -975  -1238  A    C  
ATOM   1431  C   VAL A 214      36.240  26.448  22.955  1.00116.82      A    C  
ANISOU 1431  C   VAL A 214    17588  14380  12418    676   -986  -1173  A    C  
ATOM   1432  O   VAL A 214      36.894  25.424  22.759  1.00115.09      A    O  
ANISOU 1432  O   VAL A 214    17304  13966  12461    697   -969  -1209  A    O  
ATOM   1433  CB  VAL A 214      34.165  26.435  24.324  1.00106.01      A    C  
ANISOU 1433  CB  VAL A 214    16336  13195  10749    500  -1084  -1095  A    C  
ATOM   1434  CG1 VAL A 214      34.046  27.854  24.835  1.00104.55      A    C  
ANISOU 1434  CG1 VAL A 214    16190  13152  10384    532  -1097  -1044  A    C  
ATOM   1435  CG2 VAL A 214      32.811  25.744  24.364  1.00113.71      A    C  
ANISOU 1435  CG2 VAL A 214    17323  14255  11626    387  -1067  -1156  A    C  
ATOM   1436  N   SER A 215      36.793  27.625  23.218  1.00122.38      A    N  
ANISOU 1436  N   SER A 215    18297  15151  13052    717  -1015  -1085  A    N  
ATOM   1437  CA  SER A 215      38.234  27.794  23.330  1.00121.16      A    C  
ANISOU 1437  CA  SER A 215    18054  14872  13109    769  -1041  -1002  A    C  
ATOM   1438  C   SER A 215      38.757  27.202  24.628  1.00117.16      A    C  
ANISOU 1438  C   SER A 215    17532  14196  12787    713  -1224   -813  A    C  
ATOM   1439  O   SER A 215      37.986  26.880  25.529  1.00121.06      A    O  
ANISOU 1439  O   SER A 215    18122  14702  13172    608  -1322   -733  A    O  
ATOM   1440  CB  SER A 215      38.610  29.272  23.251  1.00114.38      A    C  
ANISOU 1440  CB  SER A 215    17222  14131  12105    792  -1040   -951  A    C  
ATOM   1441  OG  SER A 215      38.084  29.986  24.354  1.00106.99      A    O  
ANISOU 1441  OG  SER A 215    16396  13254  11003    732  -1156   -849  A    O  
ATOM   1442  N   GLU A 216      40.076  27.057  24.703  1.00125.06      A    N  
ANISOU 1442  N   GLU A 216    18401  15050  14068    765  -1274   -730  A    N  
ATOM   1443  CA  GLU A 216      40.750  26.499  25.874  1.00145.99      A    C  
ANISOU 1443  CA  GLU A 216    21011  17521  16939    708  -1502   -505  A    C  
ATOM   1444  C   GLU A 216      40.649  27.399  27.104  1.00150.52      A    C  
ANISOU 1444  C   GLU A 216    21719  18199  17271    572  -1675   -324  A    C  
ATOM   1445  O   GLU A 216      40.481  26.917  28.223  1.00138.16      A    O  
ANISOU 1445  O   GLU A 216    20236  16574  15684    436  -1863   -150  A    O  
ATOM   1446  CB  GLU A 216      42.225  26.248  25.558  1.00157.35      A    C  
ANISOU 1446  CB  GLU A 216    22221  18791  18776    814  -1514   -465  A    C  
ATOM   1447  CG  GLU A 216      42.477  25.195  24.497  1.00169.41      A    C  
ANISOU 1447  CG  GLU A 216    23598  20162  20606    943  -1332   -667  A    C  
ATOM   1448  CD  GLU A 216      42.683  23.819  25.090  1.00180.83      A    C  
ANISOU 1448  CD  GLU A 216    24975  21308  22424    954  -1497   -555  A    C  
ATOM   1449  OE1 GLU A 216      42.108  23.543  26.165  1.00190.72      A    O  
ANISOU 1449  OE1 GLU A 216    26371  22531  23561    818  -1716   -355  A    O  
ATOM   1450  OE2 GLU A 216      43.430  23.018  24.489  1.00180.10      A    O1-
ANISOU 1450  OE2 GLU A 216    24683  21001  22748   1090  -1404   -668  A    O1-
ATOM   1451  N   GLU A 217      40.776  28.707  26.890  1.00156.60      A    N  
ANISOU 1451  N   GLU A 217    22529  19117  17856    587  -1613   -368  A    N  
ATOM   1452  CA  GLU A 217      40.716  29.676  27.979  1.00149.39      A    C  
ANISOU 1452  CA  GLU A 217    21760  18291  16711    458  -1746   -255  A    C  
ATOM   1453  C   GLU A 217      39.367  29.650  28.687  1.00136.70      A    C  
ANISOU 1453  C   GLU A 217    20331  16800  14808    347  -1732   -294  A    C  
ATOM   1454  O   GLU A 217      39.300  29.612  29.916  1.00140.76      A    O  
ANISOU 1454  O   GLU A 217    20962  17325  15195    175  -1881   -161  A    O  
ATOM   1455  CB  GLU A 217      40.997  31.090  27.456  1.00155.75      A    C  
ANISOU 1455  CB  GLU A 217    22582  19197  17398    507  -1659   -328  A    C  
ATOM   1456  CG  GLU A 217      42.376  31.283  26.832  1.00155.44      A    C  
ANISOU 1456  CG  GLU A 217    22359  19085  17617    571  -1655   -281  A    C  
ATOM   1457  CD  GLU A 217      42.426  30.891  25.366  1.00150.33      A    C  
ANISOU 1457  CD  GLU A 217    21580  18449  17090    707  -1430   -447  A    C  
ATOM   1458  OE1 GLU A 217      41.358  30.586  24.793  1.00153.12      A    O  
ANISOU 1458  OE1 GLU A 217    22007  18873  17299    745  -1305   -591  A    O  
ATOM   1459  OE2 GLU A 217      43.533  30.891  24.786  1.00145.03      A    O1-
ANISOU 1459  OE2 GLU A 217    20727  17731  16648    754  -1373   -442  A    O1-
ATOM   1460  N   THR A 218      38.296  29.654  27.901  1.00123.68      A    N  
ANISOU 1460  N   THR A 218    18694  15254  13046    424  -1552   -475  A    N  
ATOM   1461  CA  THR A 218      36.943  29.534  28.433  1.00116.90      A    C  
ANISOU 1461  CA  THR A 218    17943  14519  11956    333  -1503   -537  A    C  
ATOM   1462  C   THR A 218      36.731  28.194  29.128  1.00110.61      A    C  
ANISOU 1462  C   THR A 218    17167  13637  11224    194  -1604   -418  A    C  
ATOM   1463  O   THR A 218      36.057  28.113  30.154  1.00114.86      A    O  
ANISOU 1463  O   THR A 218    17821  14263  11558     20  -1639   -366  A    O  
ATOM   1464  CB  THR A 218      35.887  29.706  27.328  1.00123.12      A    C  
ANISOU 1464  CB  THR A 218    18688  15424  12667    447  -1326   -731  A    C  
ATOM   1465  CG2 THR A 218      34.499  29.856  27.935  1.00119.19      A    C  
ANISOU 1465  CG2 THR A 218    18256  15081  11949    364  -1261   -804  A    C  
ATOM   1466  OG1 THR A 218      36.187  30.882  26.566  1.00133.28      A    O  
ANISOU 1466  OG1 THR A 218    19959  16755  13925    567  -1266   -796  A    O  
ATOM   1467  N   LEU A 219      37.312  27.148  28.555  1.00106.02      A    N  
ANISOU 1467  N   LEU A 219    16473  12876  10933    261  -1641   -382  A    N  
ATOM   1468  CA  LEU A 219      37.153  25.794  29.067  1.00110.61      A    C  
ANISOU 1468  CA  LEU A 219    17068  13312  11646    145  -1757   -258  A    C  
ATOM   1469  C   LEU A 219      37.647  25.706  30.509  1.00120.95      A    C  
ANISOU 1469  C   LEU A 219    18476  14572  12907    -53  -1999     10  A    C  
ATOM   1470  O   LEU A 219      37.033  25.039  31.344  1.00120.02      A    O  
ANISOU 1470  O   LEU A 219    18468  14462  12672   -254  -2084    130  A    O  
ATOM   1471  CB  LEU A 219      37.908  24.804  28.184  1.00114.47      A    C  
ANISOU 1471  CB  LEU A 219    17406  13560  12529    285  -1755   -288  A    C  
ATOM   1472  CG  LEU A 219      37.640  23.323  28.435  1.00122.55      A    C  
ANISOU 1472  CG  LEU A 219    18437  14373  13753    200  -1854   -203  A    C  
ATOM   1473  CD1 LEU A 219      36.231  22.983  27.965  1.00113.79      A    C  
ANISOU 1473  CD1 LEU A 219    17394  13393  12448    140  -1698   -379  A    C  
ATOM   1474  CD2 LEU A 219      38.677  22.458  27.743  1.00130.60      A    C  
ANISOU 1474  CD2 LEU A 219    19286  15094  15241    362  -1871   -229  A    C  
ATOM   1475  N   LYS A 220      38.760  26.384  30.790  1.00124.83      A    N  
ANISOU 1475  N   LYS A 220    18933  15025  13470    -27  -2119    116  A    N  
ATOM   1476  CA  LYS A 220      39.326  26.440  32.139  1.00103.96      A    C  
ANISOU 1476  CA  LYS A 220    16394  12359  10748   -243  -2384    381  A    C  
ATOM   1477  C   LYS A 220      38.401  27.202  33.086  1.00 81.45      A    C  
ANISOU 1477  C   LYS A 220    13763   9752   7430   -455  -2326    335  A    C  
ATOM   1478  O   LYS A 220      38.237  26.818  34.239  1.00 81.99      A    O  
ANISOU 1478  O   LYS A 220    13981   9851   7320   -720  -2486    519  A    O  
ATOM   1479  CB  LYS A 220      40.717  27.087  32.127  1.00101.79      A    C  
ANISOU 1479  CB  LYS A 220    16008  12008  10659   -174  -2521    483  A    C  
ATOM   1480  CG  LYS A 220      41.777  26.296  31.365  1.00122.40      A    C  
ANISOU 1480  CG  LYS A 220    18360  14370  13777     18  -2580    540  A    C  
ATOM   1481  CD  LYS A 220      43.171  26.890  31.557  1.00135.65      A    C  
ANISOU 1481  CD  LYS A 220    19898  15991  15651     37  -2751    686  A    C  
ATOM   1482  CE  LYS A 220      44.232  26.120  30.770  1.00142.82      A    C  
ANISOU 1482  CE  LYS A 220    20495  16659  17111    248  -2763    706  A    C  
ATOM   1483  NZ  LYS A 220      44.032  26.211  29.295  1.00138.20      A    N1+
ANISOU 1483  NZ  LYS A 220    19796  16108  16604    470  -2410    388  A    N1+
ATOM   1484  N   ILE A 221      37.806  28.285  32.593  1.00 70.66      A    N  
ANISOU 1484  N   ILE A 221    12417   8554   5878   -347  -2096     86  A    N  
ATOM   1485  CA  ILE A 221      36.839  29.059  33.369  1.00 75.44      A    C  
ANISOU 1485  CA  ILE A 221    13194   9377   6094   -498  -1976    -33  A    C  
ATOM   1486  C   ILE A 221      35.620  28.223  33.761  1.00 86.66      A    C  
ANISOU 1486  C   ILE A 221    14671  10899   7358   -651  -1888    -52  A    C  
ATOM   1487  O   ILE A 221      35.173  28.256  34.910  1.00 82.07      A    O  
ANISOU 1487  O   ILE A 221    14253  10451   6481   -917  -1903     -2  A    O  
ATOM   1488  CB  ILE A 221      36.374  30.308  32.588  1.00 66.14      A    C  
ANISOU 1488  CB  ILE A 221    11979   8303   4847   -298  -1752   -298  A    C  
ATOM   1489  CG1 ILE A 221      37.514  31.325  32.501  1.00 63.61      A    C  
ANISOU 1489  CG1 ILE A 221    11662   7913   4595   -236  -1843   -265  A    C  
ATOM   1490  CG2 ILE A 221      35.175  30.955  33.264  1.00 63.77      A    C  
ANISOU 1490  CG2 ILE A 221    11799   8202   4228   -404  -1576   -475  A    C  
ATOM   1491  CD1 ILE A 221      37.293  32.420  31.475  1.00 61.29      A    C  
ANISOU 1491  CD1 ILE A 221    11309   7648   4329    -17  -1673   -462  A    C  
ATOM   1492  N   ILE A 222      35.090  27.476  32.797  1.00 97.55      A    N  
ANISOU 1492  N   ILE A 222    15920  12227   8918   -512  -1789   -132  A    N  
ATOM   1493  CA  ILE A 222      33.982  26.555  33.038  1.00 85.58      A    C  
ANISOU 1493  CA  ILE A 222    14427  10781   7307   -663  -1721   -134  A    C  
ATOM   1494  C   ILE A 222      34.361  25.469  34.041  1.00 73.05      A    C  
ANISOU 1494  C   ILE A 222    12948   9075   5731   -931  -1961    165  A    C  
ATOM   1495  O   ILE A 222      33.575  25.126  34.922  1.00 74.02      A    O  
ANISOU 1495  O   ILE A 222    13192   9335   5597  -1203  -1938    224  A    O  
ATOM   1496  CB  ILE A 222      33.509  25.898  31.725  1.00 96.10      A    C  
ANISOU 1496  CB  ILE A 222    15606  12043   8865   -478  -1614   -267  A    C  
ATOM   1497  CG1 ILE A 222      33.115  26.973  30.711  1.00102.74      A    C  
ANISOU 1497  CG1 ILE A 222    16351  13008   9676   -243  -1423   -514  A    C  
ATOM   1498  CG2 ILE A 222      32.329  24.976  31.982  1.00 95.68      A    C  
ANISOU 1498  CG2 ILE A 222    15571  12068   8715   -663  -1552   -268  A    C  
ATOM   1499  CD1 ILE A 222      33.261  26.535  29.270  1.00112.38      A    C  
ANISOU 1499  CD1 ILE A 222    17442  14124  11135    -46  -1377   -615  A    C  
ATOM   1500  N   GLU A 223      35.568  24.931  33.897  1.00 75.49      A    N  
ANISOU 1500  N   GLU A 223    13201   9128   6354   -862  -2193    362  A    N  
ATOM   1501  CA  GLU A 223      36.052  23.868  34.771  1.00 86.46      A    C  
ANISOU 1501  CA  GLU A 223    14670  10343   7839  -1088  -2486    697  A    C  
ATOM   1502  C   GLU A 223      36.164  24.329  36.229  1.00111.20      A    C  
ANISOU 1502  C   GLU A 223    18018  13635  10599  -1420  -2634    882  A    C  
ATOM   1503  O   GLU A 223      35.765  23.611  37.149  1.00107.93      A    O  
ANISOU 1503  O   GLU A 223    17754  13250  10006  -1736  -2758   1091  A    O  
ATOM   1504  CB  GLU A 223      37.406  23.361  34.265  1.00 79.04      A    C  
ANISOU 1504  CB  GLU A 223    13568   9083   7380   -892  -2699    846  A    C  
ATOM   1505  CG  GLU A 223      37.865  22.052  34.883  1.00109.17      A    C  
ANISOU 1505  CG  GLU A 223    17407  12626  11449  -1050  -3020   1192  A    C  
ATOM   1506  CD  GLU A 223      39.225  21.617  34.373  1.00129.16      A    C  
ANISOU 1506  CD  GLU A 223    19722  14828  14525   -816  -3209   1309  A    C  
ATOM   1507  OE1 GLU A 223      39.823  22.365  33.570  1.00129.55      A    O  
ANISOU 1507  OE1 GLU A 223    19615  14903  14705   -565  -3070   1118  A    O  
ATOM   1508  OE2 GLU A 223      39.692  20.527  34.767  1.00136.39      A    O1-
ANISOU 1508  OE2 GLU A 223    20612  15454  15758   -886  -3494   1594  A    O1-
ATOM   1509  N   GLU A 224      36.681  25.541  36.428  1.00130.62      A    N  
ANISOU 1509  N   GLU A 224    20510  16204  12913  -1378  -2616    798  A    N  
ATOM   1510  CA  GLU A 224      36.898  26.090  37.769  1.00127.57      A    C  
ANISOU 1510  CA  GLU A 224    20348  15971  12151  -1705  -2755    933  A    C  
ATOM   1511  C   GLU A 224      35.592  26.358  38.504  1.00113.64      A    C  
ANISOU 1511  C   GLU A 224    18763  14503   9911  -1963  -2513    773  A    C  
ATOM   1512  O   GLU A 224      35.539  26.248  39.727  1.00124.78      A    O  
ANISOU 1512  O   GLU A 224    20393  16038  10977  -2344  -2636    942  A    O  
ATOM   1513  CB  GLU A 224      37.725  27.376  37.711  1.00143.11      A    C  
ANISOU 1513  CB  GLU A 224    22310  17969  14095  -1595  -2769    834  A    C  
ATOM   1514  CG  GLU A 224      39.205  27.160  37.428  1.00162.57      A    C  
ANISOU 1514  CG  GLU A 224    24621  20187  16960  -1469  -3071   1069  A    C  
ATOM   1515  CD  GLU A 224      40.000  28.453  37.480  1.00180.56      A    C  
ANISOU 1515  CD  GLU A 224    26910  22517  19178  -1428  -3099    991  A    C  
ATOM   1516  OE1 GLU A 224      39.377  29.529  37.600  1.00185.88      A    O  
ANISOU 1516  OE1 GLU A 224    27711  23378  19537  -1449  -2865    725  A    O  
ATOM   1517  OE2 GLU A 224      41.245  28.394  37.399  1.00189.52      A    O1-
ANISOU 1517  OE2 GLU A 224    27911  23489  20608  -1374  -3356   1192  A    O1-
ATOM   1518  N   TRP A 225      34.558  26.760  37.771  1.00 87.57      A    N  
ANISOU 1518  N   TRP A 225    15358  11329   6584  -1770  -2169    445  A    N  
ATOM   1519  CA  TRP A 225      33.250  26.978  38.381  1.00 89.17      A    C  
ANISOU 1519  CA  TRP A 225    15661  11815   6406  -1980  -1898    261  A    C  
ATOM   1520  C   TRP A 225      32.610  25.697  38.925  1.00102.27      A    C  
ANISOU 1520  C   TRP A 225    17388  13507   7963  -2285  -1955    464  A    C  
ATOM   1521  O   TRP A 225      32.130  25.682  40.058  1.00118.48      A    O  
ANISOU 1521  O   TRP A 225    19632  15772   9611  -2662  -1908    511  A    O  
ATOM   1522  CB  TRP A 225      32.282  27.616  37.392  1.00 86.50      A    C  
ANISOU 1522  CB  TRP A 225    15141  11579   6148  -1680  -1560   -101  A    C  
ATOM   1523  CG  TRP A 225      30.852  27.392  37.796  1.00100.90      A    C  
ANISOU 1523  CG  TRP A 225    16962  13650   7726  -1863  -1296   -250  A    C  
ATOM   1524  CD1 TRP A 225      29.987  26.477  37.266  1.00104.14      A    C  
ANISOU 1524  CD1 TRP A 225    17236  14073   8257  -1855  -1213   -254  A    C  
ATOM   1525  CD2 TRP A 225      30.122  28.084  38.819  1.00115.46      A    C  
ANISOU 1525  CD2 TRP A 225    18930  15772   9169  -2101  -1061   -435  A    C  
ATOM   1526  CE2 TRP A 225      28.821  27.542  38.849  1.00110.34      A    C  
ANISOU 1526  CE2 TRP A 225    18180  15308   8435  -2218   -831   -537  A    C  
ATOM   1527  CE3 TRP A 225      30.439  29.117  39.711  1.00126.96      A    C  
ANISOU 1527  CE3 TRP A 225    20571  17337  10330  -2240  -1007   -551  A    C  
ATOM   1528  NE1 TRP A 225      28.768  26.557  37.893  1.00102.13      A    N  
ANISOU 1528  NE1 TRP A 225    16988  14099   7717  -2072   -950   -408  A    N  
ATOM   1529  CZ2 TRP A 225      27.838  27.989  39.732  1.00107.72      A    C  
ANISOU 1529  CZ2 TRP A 225    17898  15280   7752  -2453   -524   -754  A    C  
ATOM   1530  CZ3 TRP A 225      29.460  29.562  40.590  1.00131.14      A    C  
ANISOU 1530  CZ3 TRP A 225    21126  18137  10566  -2443   -690   -781  A    C  
ATOM   1531  CH2 TRP A 225      28.177  28.997  40.593  1.00118.93      A    C  
ANISOU 1531  CH2 TRP A 225    19486  16793   8911  -2562   -445   -889  A    C  
ATOM   1532  N   PHE A 226      32.584  24.634  38.121  1.00 92.86      A    N  
ANISOU 1532  N   PHE A 226    16055  12107   7120  -2148  -2041    571  A    N  
ATOM   1533  CA  PHE A 226      31.934  23.393  38.549  1.00109.50      A    C  
ANISOU 1533  CA  PHE A 226    18226  14209   9171  -2437  -2100    765  A    C  
ATOM   1534  C   PHE A 226      32.655  22.746  39.728  1.00119.28      A    C  
ANISOU 1534  C   PHE A 226    19684  15357  10281  -2809  -2457   1184  A    C  
ATOM   1535  O   PHE A 226      32.025  22.173  40.617  1.00127.00      A    O  
ANISOU 1535  O   PHE A 226    20824  16473  10957  -3209  -2468   1341  A    O  
ATOM   1536  CB  PHE A 226      31.830  22.393  37.390  1.00107.81      A    C  
ANISOU 1536  CB  PHE A 226    17830  13741   9392  -2207  -2134    770  A    C  
ATOM   1537  CG  PHE A 226      30.716  22.696  36.425  1.00110.03      A    C  
ANISOU 1537  CG  PHE A 226    17935  14175   9696  -2004  -1803    422  A    C  
ATOM   1538  CD1 PHE A 226      29.391  22.635  36.835  1.00109.54      A    C  
ANISOU 1538  CD1 PHE A 226    17878  14390   9353  -2229  -1570    306  A    C  
ATOM   1539  CD2 PHE A 226      30.989  23.033  35.111  1.00109.04      A    C  
ANISOU 1539  CD2 PHE A 226    17627  13932   9869  -1612  -1734    224  A    C  
ATOM   1540  CE1 PHE A 226      28.359  22.916  35.955  1.00 98.02      A    C  
ANISOU 1540  CE1 PHE A 226    16221  13073   7949  -2045  -1306     12  A    C  
ATOM   1541  CE2 PHE A 226      29.961  23.314  34.225  1.00105.00      A    C  
ANISOU 1541  CE2 PHE A 226    16960  13568   9368  -1453  -1483    -57  A    C  
ATOM   1542  CZ  PHE A 226      28.644  23.255  34.650  1.00100.71      A    C  
ANISOU 1542  CZ  PHE A 226    16399  13285   8581  -1659  -1285   -156  A    C  
ATOM   1543  N   CYS A 227      33.978  22.840  39.734  1.00116.12      A    N  
ANISOU 1543  N   CYS A 227    19280  14732  10109  -2698  -2763   1382  A    N  
ATOM   1544  CA  CYS A 227      34.764  22.377  40.870  1.00133.00      A    C  
ANISOU 1544  CA  CYS A 227    21614  16788  12133  -3046  -3160   1807  A    C  
ATOM   1545  C   CYS A 227      34.647  23.333  42.058  1.00139.75      A    C  
ANISOU 1545  C   CYS A 227    22718  17976  12406  -3394  -3103   1766  A    C  
ATOM   1546  O   CYS A 227      35.046  23.002  43.178  1.00148.75      A    O  
ANISOU 1546  O   CYS A 227    24014  19127  13377  -3765  -3355   2078  A    O  
ATOM   1547  CB  CYS A 227      36.226  22.198  40.464  1.00143.26      A    C  
ANISOU 1547  CB  CYS A 227    22773  17743  13915  -2800  -3508   2024  A    C  
ATOM   1548  SG  CYS A 227      36.458  20.946  39.192  1.00111.12      A    S  
ANISOU 1548  SG  CYS A 227    18437  13249  10536  -2439  -3577   2065  A    S  
ATOM   1549  N   GLY A 228      34.107  24.522  41.802  1.00133.91      A    N  
ANISOU 1549  N   GLY A 228    21945  17471  11466  -3241  -2729   1344  A    N  
ATOM   1550  CA  GLY A 228      33.930  25.503  42.851  1.00129.95      A    C  
ANISOU 1550  CA  GLY A 228    21533  17225  10617  -3461  -2532   1178  A    C  
ATOM   1551  C   GLY A 228      32.936  24.993  43.871  1.00137.79      A    C  
ANISOU 1551  C   GLY A 228    22622  18441  11290  -3874  -2362   1214  A    C  
ATOM   1552  O   GLY A 228      31.863  24.496  43.526  1.00140.79      A    O  
ANISOU 1552  O   GLY A 228    22965  18927  11599  -3899  -2149   1109  A    O  
ATOM   1553  N   GLU A 229      33.303  25.125  45.140  1.00145.65      A    N  
ANISOU 1553  N   GLU A 229    23744  19517  12080  -4226  -2460   1362  A    N  
ATOM   1554  CA  GLU A 229      32.476  24.650  46.234  1.00157.04      A    C  
ANISOU 1554  CA  GLU A 229    25304  21175  13190  -4679  -2324   1424  A    C  
ATOM   1555  C   GLU A 229      31.116  25.332  46.215  1.00149.87      A    C  
ANISOU 1555  C   GLU A 229    24322  20579  12043  -4643  -1779    963  A    C  
ATOM   1556  O   GLU A 229      30.100  24.692  46.480  1.00151.81      A    O  
ANISOU 1556  O   GLU A 229    24575  20988  12119  -4882  -1598    962  A    O  
ATOM   1557  CB  GLU A 229      33.181  24.874  47.577  1.00169.16      A    C  
ANISOU 1557  CB  GLU A 229    26998  22752  14523  -5055  -2514   1611  A    C  
ATOM   1558  CG  GLU A 229      34.382  23.950  47.802  1.00173.36      A    C  
ANISOU 1558  CG  GLU A 229    27583  22988  15298  -5187  -3087   2135  A    C  
ATOM   1559  CD  GLU A 229      35.060  24.177  49.142  1.00173.63      A    C  
ANISOU 1559  CD  GLU A 229    27772  23078  15120  -5593  -3295   2323  A    C  
ATOM   1560  OE1 GLU A 229      34.578  25.033  49.914  1.00172.50      A    O  
ANISOU 1560  OE1 GLU A 229    27726  23207  14610  -5791  -2980   2039  A    O  
ATOM   1561  OE2 GLU A 229      36.071  23.496  49.426  1.00171.56      A    O1-
ANISOU 1561  OE2 GLU A 229    27529  22582  15072  -5717  -3780   2751  A    O1-
ATOM   1562  N   LYS A 230      31.099  26.615  45.859  1.00140.69      A    N  
ANISOU 1562  N   LYS A 230    23070  19480  10904  -4337  -1531    581  A    N  
ATOM   1563  CA  LYS A 230      29.852  27.368  45.777  1.00145.80      A    C  
ANISOU 1563  CA  LYS A 230    23607  20385  11406  -4237  -1028    124  A    C  
ATOM   1564  C   LYS A 230      28.887  26.697  44.818  1.00143.99      A    C  
ANISOU 1564  C   LYS A 230    23227  20190  11291  -4090   -881     55  A    C  
ATOM   1565  O   LYS A 230      27.707  26.556  45.116  1.00136.31      A    O  
ANISOU 1565  O   LYS A 230    22192  19462  10136  -4255   -556   -119  A    O  
ATOM   1566  CB  LYS A 230      30.112  28.808  45.330  1.00146.96      A    C  
ANISOU 1566  CB  LYS A 230    23674  20503  11662  -3867   -866   -233  A    C  
ATOM   1567  CG  LYS A 230      28.859  29.679  45.269  1.00157.60      A    C  
ANISOU 1567  CG  LYS A 230    24890  22076  12916  -3731   -367   -715  A    C  
ATOM   1568  CD  LYS A 230      28.231  29.849  46.647  1.00174.83      A    C  
ANISOU 1568  CD  LYS A 230    27174  24517  14736  -4136   -110   -836  A    C  
ATOM   1569  CE  LYS A 230      27.122  30.895  46.636  1.00173.29      A    C  
ANISOU 1569  CE  LYS A 230    26835  24511  14498  -3962    385  -1352  A    C  
ATOM   1570  NZ  LYS A 230      26.065  30.584  45.633  1.00162.15      A    N1+
ANISOU 1570  NZ  LYS A 230    25183  23170  13257  -3722    601  -1511  A    N1+
ATOM   1571  N   ALA A 231      29.398  26.277  43.667  1.00144.01      A    N  
ANISOU 1571  N   ALA A 231    23171  19953  11594  -3797  -1121    186  A    N  
ATOM   1572  CA  ALA A 231      28.573  25.622  42.663  1.00143.00      A    C  
ANISOU 1572  CA  ALA A 231    22922  19832  11581  -3661  -1024    125  A    C  
ATOM   1573  C   ALA A 231      28.024  24.291  43.158  1.00147.57      A    C  
ANISOU 1573  C   ALA A 231    23585  20468  12016  -4068  -1102    408  A    C  
ATOM   1574  O   ALA A 231      26.853  23.979  42.958  1.00147.87      A    O  
ANISOU 1574  O   ALA A 231    23522  20700  11960  -4151   -834    256  A    O  
ATOM   1575  CB  ALA A 231      29.367  25.408  41.396  1.00141.82      A    C  
ANISOU 1575  CB  ALA A 231    22698  19371  11816  -3279  -1289    219  A    C  
ATOM   1576  N   GLY A 232      28.885  23.508  43.799  1.00148.69      A    N  
ANISOU 1576  N   GLY A 232    23902  20431  12161  -4331  -1488    837  A    N  
ATOM   1577  CA  GLY A 232      28.500  22.200  44.293  1.00140.66      A    C  
ANISOU 1577  CA  GLY A 232    22995  19405  11043  -4737  -1635   1175  A    C  
ATOM   1578  C   GLY A 232      27.471  22.206  45.405  1.00135.87      A    C  
ANISOU 1578  C   GLY A 232    22417  19142  10064  -5165  -1315   1077  A    C  
ATOM   1579  O   GLY A 232      26.496  21.456  45.361  1.00118.00      A    O  
ANISOU 1579  O   GLY A 232    20125  17006   7702  -5386  -1177   1107  A    O  
ATOM   1580  N   GLU A 233      27.694  23.043  46.413  1.00155.18      A    N  
ANISOU 1580  N   GLU A 233    24926  21738  12298  -5308  -1198    959  A    N  
ATOM   1581  CA  GLU A 233      26.804  23.086  47.565  1.00171.77      A    C  
ANISOU 1581  CA  GLU A 233    27076  24164  14026  -5744   -896    855  A    C  
ATOM   1582  C   GLU A 233      25.432  23.664  47.228  1.00176.59      A    C  
ANISOU 1582  C   GLU A 233    27470  25081  14546  -5619   -352    385  A    C  
ATOM   1583  O   GLU A 233      24.408  23.074  47.567  1.00176.71      A    O  
ANISOU 1583  O   GLU A 233    27446  25317  14379  -5936   -138    378  A    O  
ATOM   1584  CB  GLU A 233      27.448  23.908  48.687  1.00177.16      A    C  
ANISOU 1584  CB  GLU A 233    27898  24912  14501  -5918   -915    814  A    C  
ATOM   1585  CG  GLU A 233      28.824  23.410  49.111  1.00182.95      A    C  
ANISOU 1585  CG  GLU A 233    28814  25368  15332  -6066  -1461   1275  A    C  
ATOM   1586  CD  GLU A 233      29.580  24.413  49.962  1.00184.88      A    C  
ANISOU 1586  CD  GLU A 233    29169  25654  15422  -6146  -1492   1185  A    C  
ATOM   1587  OE1 GLU A 233      28.997  25.459  50.317  1.00194.85      A    O  
ANISOU 1587  OE1 GLU A 233    30401  27156  16476  -6122  -1080    766  A    O  
ATOM   1588  OE2 GLU A 233      30.761  24.154  50.277  1.00178.18      A    O1-
ANISOU 1588  OE2 GLU A 233    28433  24588  14678  -6237  -1936   1532  A    O1-
ATOM   1589  N   VAL A 234      25.414  24.817  46.562  1.00183.90      A    N  
ANISOU 1589  N   VAL A 234    28242  26013  15620  -5167   -141      1  A    N  
ATOM   1590  CA  VAL A 234      24.167  25.557  46.371  1.00191.85      A    C  
ANISOU 1590  CA  VAL A 234    29021  27300  16573  -5029    374   -474  A    C  
ATOM   1591  C   VAL A 234      23.466  25.050  45.113  1.00188.16      A    C  
ANISOU 1591  C   VAL A 234    28349  26826  16318  -4800    436   -536  A    C  
ATOM   1592  O   VAL A 234      22.270  25.278  44.927  1.00200.18      A    O  
ANISOU 1592  O   VAL A 234    29649  28605  17807  -4776    830   -846  A    O  
ATOM   1593  CB  VAL A 234      24.388  27.087  46.283  1.00197.24      A    C  
ANISOU 1593  CB  VAL A 234    29632  27978  17333  -4664    575   -870  A    C  
ATOM   1594  CG1 VAL A 234      24.826  27.491  44.889  1.00199.85      A    C  
ANISOU 1594  CG1 VAL A 234    29840  28078  18017  -4137    440   -953  A    C  
ATOM   1595  CG2 VAL A 234      23.108  27.818  46.646  1.00195.84      A    C  
ANISOU 1595  CG2 VAL A 234    29269  28113  17030  -4679   1116  -1329  A    C  
ATOM   1596  N   GLY A 235      24.237  24.390  44.247  1.00180.85      A    N  
ANISOU 1596  N   GLY A 235    27489  25604  15621  -4633     44   -253  A    N  
ATOM   1597  CA  GLY A 235      23.798  23.993  42.917  1.00169.70      A    C  
ANISOU 1597  CA  GLY A 235    25920  24129  14429  -4374     37   -319  A    C  
ATOM   1598  C   GLY A 235      22.431  23.351  42.866  1.00181.59      A    C  
ANISOU 1598  C   GLY A 235    27220  25870  15906  -4575    310   -398  A    C  
ATOM   1599  O   GLY A 235      21.669  23.570  41.931  1.00154.91      A    O  
ANISOU 1599  O   GLY A 235    23509  22518  12833  -4251    496   -647  A    O  
ATOM   1600  N   ASP A 236      22.135  22.536  43.873  1.00213.38      A    N  
ANISOU 1600  N   ASP A 236    31426  30055  19593  -5124    305   -156  A    N  
ATOM   1601  CA  ASP A 236      20.803  21.973  44.044  1.00232.67      A    C  
ANISOU 1601  CA  ASP A 236    33710  32801  21894  -5435    610   -231  A    C  
ATOM   1602  C   ASP A 236      19.744  23.068  44.045  1.00234.92      A    C  
ANISOU 1602  C   ASP A 236    33692  33432  22134  -5270   1144   -755  A    C  
ATOM   1603  O   ASP A 236      19.836  24.044  44.786  1.00243.72      A    O  
ANISOU 1603  O   ASP A 236    34810  34639  23155  -5224   1348   -981  A    O  
ATOM   1604  CB  ASP A 236      20.721  21.153  45.339  1.00238.82      A    C  
ANISOU 1604  CB  ASP A 236    34697  33676  22366  -6038    546     92  A    C  
ATOM   1605  CG  ASP A 236      20.774  22.016  46.588  1.00237.01      A    C  
ANISOU 1605  CG  ASP A 236    34523  33632  21896  -6197    770    -84  A    C  
ATOM   1606  OD1 ASP A 236      21.857  22.544  46.906  1.00236.28      A    O  
ANISOU 1606  OD1 ASP A 236    34599  33346  21833  -6064    544    -12  A    O  
ATOM   1607  OD2 ASP A 236      19.729  22.168  47.253  1.00234.36      A    O1-
ANISOU 1607  OD2 ASP A 236    34059  33644  21344  -6469   1176   -305  A    O1-
ATOM   1608  N   ASN A 237      18.743  22.909  43.191  1.00226.58      A    N  
ANISOU 1608  N   ASN A 237    32255  32443  21390  -5067   1321   -930  A    N  
ATOM   1609  CA  ASN A 237      17.626  23.837  43.164  1.00218.31      A    C  
ANISOU 1609  CA  ASN A 237    30857  31719  20372  -4913   1815  -1402  A    C  
ATOM   1610  C   ASN A 237      16.336  23.100  42.850  1.00213.21      A    C  
ANISOU 1610  C   ASN A 237    29873  31281  19857  -5077   2006  -1427  A    C  
ATOM   1611  O   ASN A 237      16.343  22.076  42.165  1.00199.11      A    O  
ANISOU 1611  O   ASN A 237    28056  29292  18305  -5094   1714  -1151  A    O  
ATOM   1612  CB  ASN A 237      17.873  24.953  42.147  1.00216.77      A    C  
ANISOU 1612  CB  ASN A 237    30446  31330  20588  -4261   1802  -1683  A    C  
ATOM   1613  CG  ASN A 237      17.005  26.169  42.399  1.00217.89      A    C  
ANISOU 1613  CG  ASN A 237    30311  31748  20728  -4093   2291  -2178  A    C  
ATOM   1614  ND2 ASN A 237      17.624  27.344  42.426  1.00211.33      A    N  
ANISOU 1614  ND2 ASN A 237    29572  30796  19926  -3786   2317  -2395  A    N  
ATOM   1615  OD1 ASN A 237      15.792  26.054  42.575  1.00221.98      A    O  
ANISOU 1615  OD1 ASN A 237    30523  32574  21244  -4241   2643  -2369  A    O  
ATOM   1616  N   GLY A 238      15.227  23.622  43.357  1.00220.64      A    N  
ANISOU 1616  N   GLY A 238    30549  32622  20660  -5206   2506  -1775  A    N  
ATOM   1617  CA  GLY A 238      13.951  22.960  43.193  1.00222.84      A    C  
ANISOU 1617  CA  GLY A 238    30477  33156  21035  -5421   2724  -1808  A    C  
ATOM   1618  C   GLY A 238      12.864  23.835  42.593  1.00235.52      A    C  
ANISOU 1618  C   GLY A 238    31532  34952  23002  -5031   3083  -2250  A    C  
ATOM   1619  O   GLY A 238      12.511  24.835  43.217  1.00231.82      A    O  
ANISOU 1619  O   GLY A 238    30956  34721  22405  -4985   3499  -2629  A    O  
ATOM   1620  N   ILE A 239      12.320  23.520  41.408  1.00251.61      A    N  
ANISOU 1620  N   ILE A 239    33214  36885  25501  -4750   2930  -2226  A    N  
ATOM   1621  CA  ILE A 239      12.678  22.414  40.492  1.00270.65      A    C  
ANISOU 1621  CA  ILE A 239    35716  38988  28132  -4741   2460  -1859  A    C  
ATOM   1622  C   ILE A 239      12.930  21.042  41.142  1.00290.06      A    C  
ANISOU 1622  C   ILE A 239    38517  41413  30278  -5330   2276  -1449  A    C  
ATOM   1623  O   ILE A 239      12.082  20.541  41.883  1.00297.59      A    O  
ANISOU 1623  O   ILE A 239    39387  42698  30986  -5815   2546  -1432  A    O  
ATOM   1624  CB  ILE A 239      13.908  22.794  39.628  1.00190.39      A    C  
ANISOU 1624  CB  ILE A 239    25759  28381  18199  -4259   2058  -1768  A    C  
ATOM   1625  CG1 ILE A 239      13.979  24.311  39.445  1.00188.24      A    C  
ANISOU 1625  CG1 ILE A 239    25325  28124  18074  -3781   2246  -2130  A    C  
ATOM   1626  CG2 ILE A 239      13.832  22.117  38.259  1.00182.45      A    C  
ANISOU 1626  CG2 ILE A 239    24601  27129  17592  -4040   1723  -1623  A    C  
ATOM   1627  CD1 ILE A 239      15.081  24.773  38.525  1.00182.47      A    C  
ANISOU 1627  CD1 ILE A 239    24746  27001  17584  -3315   1888  -2060  A    C  
ATOM   1628  N   GLY A 240      14.088  20.442  40.868  1.00299.02      A    N  
ANISOU 1628  N   GLY A 240    40024  42144  31444  -5293   1820  -1115  A    N  
ATOM   1629  CA  GLY A 240      14.387  19.095  41.331  1.00298.44      A    C  
ANISOU 1629  CA  GLY A 240    40267  41939  31186  -5789   1562   -686  A    C  
ATOM   1630  C   GLY A 240      13.589  18.055  40.563  1.00296.00      A    C  
ANISOU 1630  C   GLY A 240    39730  41582  31153  -5910   1457   -575  A    C  
ATOM   1631  O   GLY A 240      13.995  16.899  40.432  1.00298.73      A    O  
ANISOU 1631  O   GLY A 240    40313  41635  31556  -6135   1116   -225  A    O  
ATOM   1632  N   SER A 241      12.443  18.494  40.055  1.00258.83      A    N  
ANISOU 1632  N   SER A 241    34550  37151  26644  -5757   1743   -883  A    N  
ATOM   1633  CA  SER A 241      11.505  17.683  39.305  1.00228.46      A    C  
ANISOU 1633  CA  SER A 241    30407  33337  23061  -5872   1691   -845  A    C  
ATOM   1634  C   SER A 241      10.951  18.568  38.185  1.00192.10      A    C  
ANISOU 1634  C   SER A 241    25347  28792  18850  -5334   1767  -1180  A    C  
ATOM   1635  O   SER A 241      10.962  19.794  38.310  1.00180.58      A    O  
ANISOU 1635  O   SER A 241    23743  27467  17403  -5001   1994  -1464  A    O  
ATOM   1636  CB  SER A 241      10.394  17.152  40.225  1.00223.18      A    C  
ANISOU 1636  CB  SER A 241    29592  33088  22119  -6476   2024   -814  A    C  
ATOM   1637  OG  SER A 241       9.744  18.205  40.913  1.00207.96      A    O  
ANISOU 1637  OG  SER A 241    27398  31598  20018  -6460   2524  -1163  A    O  
ATOM   1638  N   ASP A 242      10.494  17.975  37.084  1.00161.93      A    N  
ANISOU 1638  N   ASP A 242    21318  24854  15355  -5254   1555  -1142  A    N  
ATOM   1639  CA  ASP A 242      10.469  16.531  36.882  1.00142.06      A    C  
ANISOU 1639  CA  ASP A 242    18977  22135  12862  -5638   1285   -839  A    C  
ATOM   1640  C   ASP A 242      11.002  16.173  35.502  1.00151.64      A    C  
ANISOU 1640  C   ASP A 242    20256  22942  14419  -5299    885   -797  A    C  
ATOM   1641  O   ASP A 242      10.843  16.939  34.553  1.00163.51      A    O  
ANISOU 1641  O   ASP A 242    21500  24460  16165  -4861    864  -1018  A    O  
ATOM   1642  CB  ASP A 242       9.049  15.998  37.074  1.00139.00      A    C  
ANISOU 1642  CB  ASP A 242    18223  22116  12473  -6060   1514   -868  A    C  
ATOM   1643  CG  ASP A 242       7.999  16.932  36.517  1.00128.94      A    C  
ANISOU 1643  CG  ASP A 242    16367  21172  11451  -5754   1763  -1212  A    C  
ATOM   1644  OD1 ASP A 242       8.253  18.153  36.479  1.00120.93      A    O  
ANISOU 1644  OD1 ASP A 242    15248  20207  10491  -5315   1901  -1451  A    O  
ATOM   1645  OD2 ASP A 242       6.903  16.456  36.162  1.00132.59      A    O1-
ANISOU 1645  OD2 ASP A 242    16463  21842  12073  -5969   1814  -1236  A    O1-
ATOM   1646  N   VAL A 243      11.641  15.011  35.402  1.00149.27      A    N  
ANISOU 1646  N   VAL A 243    20309  22270  14139  -5516    571   -514  A    N  
ATOM   1647  CA  VAL A 243      12.219  14.548  34.143  1.00143.59      A    C  
ANISOU 1647  CA  VAL A 243    19696  21138  13723  -5244    219   -496  A    C  
ATOM   1648  C   VAL A 243      11.195  14.467  33.010  1.00155.99      A    C  
ANISOU 1648  C   VAL A 243    20886  22842  15542  -5172    196   -676  A    C  
ATOM   1649  O   VAL A 243      11.546  14.669  31.852  1.00170.91      A    O  
ANISOU 1649  O   VAL A 243    22758  24534  17647  -4815      2   -791  A    O  
ATOM   1650  CB  VAL A 243      12.902  13.175  34.308  1.00134.57      A    C  
ANISOU 1650  CB  VAL A 243    18956  19566  12607  -5550    -83   -177  A    C  
ATOM   1651  CG1 VAL A 243      14.162  13.298  35.152  1.00141.30      A    C  
ANISOU 1651  CG1 VAL A 243    20195  20195  13299  -5511   -180     23  A    C  
ATOM   1652  CG2 VAL A 243      11.927  12.164  34.912  1.00134.68      A    C  
ANISOU 1652  CG2 VAL A 243    18924  19738  12510  -6157    -15      1  A    C  
ATOM   1653  N   GLY A 244       9.939  14.170  33.338  1.00149.52      A    N  
ANISOU 1653  N   GLY A 244    19759  22370  14680  -5538    387   -693  A    N  
ATOM   1654  CA  GLY A 244       8.876  14.127  32.344  1.00147.40      A    C  
ANISOU 1654  CA  GLY A 244    19081  22278  14647  -5510    356   -846  A    C  
ATOM   1655  C   GLY A 244       8.665  15.453  31.629  1.00145.17      A    C  
ANISOU 1655  C   GLY A 244    18459  22173  14525  -4990    426  -1113  A    C  
ATOM   1656  O   GLY A 244       8.612  15.505  30.398  1.00139.26      A    O  
ANISOU 1656  O   GLY A 244    17611  21312  13990  -4755    196  -1197  A    O  
ATOM   1657  N   MET A 245       8.534  16.524  32.407  1.00143.34      A    N  
ANISOU 1657  N   MET A 245    18063  22213  14187  -4833    740  -1247  A    N  
ATOM   1658  CA  MET A 245       8.400  17.875  31.866  1.00132.83      A    C  
ANISOU 1658  CA  MET A 245    16432  21007  13031  -4321    813  -1485  A    C  
ATOM   1659  C   MET A 245       9.672  18.287  31.139  1.00113.17      A    C  
ANISOU 1659  C   MET A 245    14270  18139  10589  -3897    551  -1476  A    C  
ATOM   1660  O   MET A 245       9.625  18.925  30.089  1.00114.00      A    O  
ANISOU 1660  O   MET A 245    14204  18212  10900  -3533    406  -1588  A    O  
ATOM   1661  CB  MET A 245       8.092  18.882  32.974  1.00141.26      A    C  
ANISOU 1661  CB  MET A 245    17314  22387  13970  -4266   1231  -1653  A    C  
ATOM   1662  CG  MET A 245       8.178  20.336  32.523  1.00141.41      A    C  
ANISOU 1662  CG  MET A 245    17109  22434  14186  -3704   1288  -1885  A    C  
ATOM   1663  SD  MET A 245       7.988  21.533  33.861  1.00272.19      A    S  
ANISOU 1663  SD  MET A 245    33536  39283  30601  -3621   1793  -2135  A    S  
ATOM   1664  CE  MET A 245       9.391  21.127  34.900  1.00126.82      A    C  
ANISOU 1664  CE  MET A 245    15803  20636  11746  -3851   1764  -1942  A    C  
ATOM   1665  N   LEU A 246      10.809  17.925  31.723  1.00100.23      A    N  
ANISOU 1665  N   LEU A 246    13094  16228   8760  -3967    485  -1324  A    N  
ATOM   1666  CA  LEU A 246      12.118  18.246  31.164  1.00103.27      A    C  
ANISOU 1666  CA  LEU A 246    13797  16255   9184  -3605    264  -1302  A    C  
ATOM   1667  C   LEU A 246      12.368  17.628  29.791  1.00 99.53      A    C  
ANISOU 1667  C   LEU A 246    13398  15513   8906  -3505    -58  -1283  A    C  
ATOM   1668  O   LEU A 246      12.860  18.306  28.896  1.00 91.62      A    O  
ANISOU 1668  O   LEU A 246    12400  14399   8012  -3123   -180  -1381  A    O  
ATOM   1669  CB  LEU A 246      13.227  17.825  32.128  1.00108.65      A    C  
ANISOU 1669  CB  LEU A 246    14924  16704   9654  -3761    231  -1107  A    C  
ATOM   1670  CG  LEU A 246      13.736  18.872  33.124  1.00106.13      A    C  
ANISOU 1670  CG  LEU A 246    14696  16495   9135  -3626    441  -1165  A    C  
ATOM   1671  CD1 LEU A 246      12.609  19.570  33.878  1.00 99.90      A    C  
ANISOU 1671  CD1 LEU A 246    13563  16152   8242  -3734    824  -1350  A    C  
ATOM   1672  CD2 LEU A 246      14.718  18.234  34.092  1.00116.93      A    C  
ANISOU 1672  CD2 LEU A 246    16496  17651  10282  -3887    346   -911  A    C  
ATOM   1673  N   ARG A 247      12.073  16.342  29.627  1.00116.37      A    N  
ANISOU 1673  N   ARG A 247    15618  17529  11066  -3868   -193  -1163  A    N  
ATOM   1674  CA  ARG A 247      12.290  15.694  28.334  1.00120.98      A    C  
ANISOU 1674  CA  ARG A 247    16299  17854  11816  -3814   -474  -1190  A    C  
ATOM   1675  C   ARG A 247      11.387  16.310  27.264  1.00114.48      A    C  
ANISOU 1675  C   ARG A 247    15094  17278  11127  -3640   -520  -1361  A    C  
ATOM   1676  O   ARG A 247      11.794  16.477  26.115  1.00105.46      A    O  
ANISOU 1676  O   ARG A 247    14019  15985  10068  -3405   -715  -1443  A    O  
ATOM   1677  CB  ARG A 247      12.045  14.182  28.422  1.00120.34      A    C  
ANISOU 1677  CB  ARG A 247    16379  17587  11759  -4272   -600  -1046  A    C  
ATOM   1678  CG  ARG A 247      13.141  13.408  29.141  1.00118.19      A    C  
ANISOU 1678  CG  ARG A 247    16540  16930  11438  -4401   -685   -840  A    C  
ATOM   1679  CD  ARG A 247      12.818  11.924  29.215  1.00122.77      A    C  
ANISOU 1679  CD  ARG A 247    17268  17294  12085  -4861   -827   -688  A    C  
ATOM   1680  NE  ARG A 247      12.762  11.306  27.893  1.00138.90      A    N  
ANISOU 1680  NE  ARG A 247    19342  19111  14322  -4830  -1037   -823  A    N  
ATOM   1681  CZ  ARG A 247      12.337  10.066  27.660  1.00153.93      A    C  
ANISOU 1681  CZ  ARG A 247    21335  20822  16327  -5209  -1177   -764  A    C  
ATOM   1682  NH1 ARG A 247      11.923   9.305  28.664  1.00156.03      A    N1+
ANISOU 1682  NH1 ARG A 247    21661  21094  16528  -5652  -1141   -536  A    N1+
ATOM   1683  NH2 ARG A 247      12.321   9.586  26.422  1.00159.45      A    N  
ANISOU 1683  NH2 ARG A 247    22082  21324  17176  -5174  -1354   -935  A    N  
ATOM   1684  N   GLU A 248      10.169  16.668  27.657  1.00114.56      A    N  
ANISOU 1684  N   GLU A 248    14691  17678  11159  -3765   -341  -1410  A    N  
ATOM   1685  CA  GLU A 248       9.251  17.359  26.762  1.00108.18      A    C  
ANISOU 1685  CA  GLU A 248    13457  17126  10520  -3586   -399  -1541  A    C  
ATOM   1686  C   GLU A 248       9.740  18.764  26.429  1.00115.21      A    C  
ANISOU 1686  C   GLU A 248    14289  18022  11464  -3078   -384  -1644  A    C  
ATOM   1687  O   GLU A 248       9.635  19.215  25.287  1.00129.96      A    O  
ANISOU 1687  O   GLU A 248    16041  19890  13449  -2854   -590  -1698  A    O  
ATOM   1688  CB  GLU A 248       7.852  17.419  27.383  1.00113.29      A    C  
ANISOU 1688  CB  GLU A 248    13629  18188  11229  -3830   -178  -1571  A    C  
ATOM   1689  CG  GLU A 248       6.860  18.290  26.624  1.00128.15      A    C  
ANISOU 1689  CG  GLU A 248    14990  20355  13347  -3603   -227  -1690  A    C  
ATOM   1690  CD  GLU A 248       6.558  19.595  27.336  1.00140.80      A    C  
ANISOU 1690  CD  GLU A 248    16276  22191  15030  -3303     73  -1817  A    C  
ATOM   1691  OE1 GLU A 248       6.264  19.556  28.548  1.00153.62      A    O  
ANISOU 1691  OE1 GLU A 248    17826  23993  16549  -3501    409  -1845  A    O  
ATOM   1692  OE2 GLU A 248       6.602  20.658  26.682  1.00140.28      A    O1-
ANISOU 1692  OE2 GLU A 248    16043  22125  15132  -2887    -24  -1896  A    O1-
ATOM   1693  N   ALA A 249      10.289  19.448  27.429  1.00112.17      A    N  
ANISOU 1693  N   ALA A 249    14008  17636  10977  -2928   -157  -1659  A    N  
ATOM   1694  CA  ALA A 249      10.810  20.796  27.236  1.00 93.21      A    C  
ANISOU 1694  CA  ALA A 249    11582  15204   8627  -2468   -130  -1754  A    C  
ATOM   1695  C   ALA A 249      12.153  20.805  26.510  1.00 95.38      A    C  
ANISOU 1695  C   ALA A 249    12260  15125   8853  -2249   -351  -1708  A    C  
ATOM   1696  O   ALA A 249      12.421  21.712  25.722  1.00107.12      A    O  
ANISOU 1696  O   ALA A 249    13698  16575  10427  -1910   -462  -1764  A    O  
ATOM   1697  CB  ALA A 249      10.932  21.511  28.574  1.00 93.68      A    C  
ANISOU 1697  CB  ALA A 249    11634  15382   8578  -2421    198  -1816  A    C  
ATOM   1698  N   VAL A 250      13.000  19.811  26.775  1.00102.97      A    N  
ANISOU 1698  N   VAL A 250    13605  15823   9697  -2445   -417  -1599  A    N  
ATOM   1699  CA  VAL A 250      14.284  19.726  26.079  1.00 94.24      A    C  
ANISOU 1699  CA  VAL A 250    12845  14379   8582  -2249   -599  -1576  A    C  
ATOM   1700  C   VAL A 250      14.050  19.459  24.599  1.00102.79      A    C  
ANISOU 1700  C   VAL A 250    13879  15422   9755  -2214   -832  -1638  A    C  
ATOM   1701  O   VAL A 250      14.754  20.000  23.759  1.00109.04      A    O  
ANISOU 1701  O   VAL A 250    14784  16092  10554  -1948   -944  -1683  A    O  
ATOM   1702  CB  VAL A 250      15.247  18.648  26.673  1.00120.68      A    C  
ANISOU 1702  CB  VAL A 250    16582  17414  11857  -2454   -639  -1441  A    C  
ATOM   1703  CG1 VAL A 250      14.769  17.238  26.398  1.00136.74      A    C  
ANISOU 1703  CG1 VAL A 250    18667  19350  13939  -2821   -756  -1387  A    C  
ATOM   1704  CG2 VAL A 250      16.650  18.826  26.105  1.00 97.22      A    C  
ANISOU 1704  CG2 VAL A 250    13901  14124   8915  -2181   -764  -1444  A    C  
ATOM   1705  N   LEU A 251      13.060  18.628  24.288  1.00108.00      A    N  
ANISOU 1705  N   LEU A 251    14377  16199  10458  -2516   -904  -1640  A    N  
ATOM   1706  CA  LEU A 251      12.747  18.279  22.910  1.00111.89      A    C  
ANISOU 1706  CA  LEU A 251    14839  16679  10996  -2562  -1140  -1705  A    C  
ATOM   1707  C   LEU A 251      12.303  19.490  22.102  1.00108.81      A    C  
ANISOU 1707  C   LEU A 251    14173  16506  10665  -2277  -1231  -1757  A    C  
ATOM   1708  O   LEU A 251      12.734  19.678  20.965  1.00104.69      A    O  
ANISOU 1708  O   LEU A 251    13777  15894  10106  -2153  -1416  -1798  A    O  
ATOM   1709  CB  LEU A 251      11.658  17.205  22.869  1.00124.69      A    C  
ANISOU 1709  CB  LEU A 251    16306  18416  12655  -2982  -1198  -1688  A    C  
ATOM   1710  CG  LEU A 251      11.295  16.637  21.496  1.00 93.57      A    C  
ANISOU 1710  CG  LEU A 251    12374  14452   8725  -3128  -1460  -1764  A    C  
ATOM   1711  CD1 LEU A 251      12.454  15.831  20.922  1.00 92.08      A    C  
ANISOU 1711  CD1 LEU A 251    12644  13861   8482  -3148  -1554  -1828  A    C  
ATOM   1712  CD2 LEU A 251      10.040  15.791  21.590  1.00 97.45      A    C  
ANISOU 1712  CD2 LEU A 251    12623  15128   9274  -3546  -1506  -1737  A    C  
ATOM   1713  N   ASN A 252      11.472  20.328  22.713  1.00101.05      A    N  
ANISOU 1713  N   ASN A 252    12818  15796   9779  -2177  -1092  -1755  A    N  
ATOM   1714  CA  ASN A 252      10.822  21.428  22.008  1.00102.34      A    C  
ANISOU 1714  CA  ASN A 252    12641  16164  10078  -1928  -1208  -1777  A    C  
ATOM   1715  C   ASN A 252      11.845  22.463  21.523  1.00107.94      A    C  
ANISOU 1715  C   ASN A 252    13549  16709  10752  -1549  -1273  -1778  A    C  
ATOM   1716  O   ASN A 252      11.625  23.151  20.529  1.00110.82      A    O  
ANISOU 1716  O   ASN A 252    13788  17141  11178  -1383  -1481  -1757  A    O  
ATOM   1717  CB  ASN A 252       9.784  22.080  22.927  1.00103.21      A    C  
ANISOU 1717  CB  ASN A 252    12300  16559  10356  -1880   -988  -1807  A    C  
ATOM   1718  CG  ASN A 252       8.825  23.003  22.193  1.00109.64      A    C  
ANISOU 1718  CG  ASN A 252    12660  17591  11406  -1678  -1146  -1808  A    C  
ATOM   1719  ND2 ASN A 252       7.711  23.319  22.843  1.00116.62      A    N  
ANISOU 1719  ND2 ASN A 252    13072  18743  12496  -1696   -971  -1855  A    N  
ATOM   1720  OD1 ASN A 252       9.076  23.432  21.071  1.00111.30      A    O  
ANISOU 1720  OD1 ASN A 252    12933  17734  11623  -1516  -1422  -1761  A    O  
ATOM   1721  N   ASN A 253      12.981  22.543  22.207  1.00127.85      A    N  
ANISOU 1721  N   ASN A 253    16391  19016  13172  -1444  -1119  -1780  A    N  
ATOM   1722  CA  ASN A 253      13.998  23.541  21.889  1.00139.58      A    C  
ANISOU 1722  CA  ASN A 253    18059  20347  14627  -1109  -1150  -1777  A    C  
ATOM   1723  C   ASN A 253      15.101  22.985  20.987  1.00133.39      A    C  
ANISOU 1723  C   ASN A 253    17655  19318  13709  -1134  -1295  -1776  A    C  
ATOM   1724  O   ASN A 253      16.190  23.558  20.892  1.00132.62      A    O  
ANISOU 1724  O   ASN A 253    17778  19053  13561   -918  -1277  -1769  A    O  
ATOM   1725  CB  ASN A 253      14.610  24.092  23.176  1.00143.57      A    C  
ANISOU 1725  CB  ASN A 253    18662  20780  15108   -973   -901  -1788  A    C  
ATOM   1726  CG  ASN A 253      13.617  24.884  23.997  1.00148.70      A    C  
ANISOU 1726  CG  ASN A 253    18941  21667  15893   -891   -711  -1848  A    C  
ATOM   1727  ND2 ASN A 253      13.780  24.854  25.314  1.00149.45      A    N  
ANISOU 1727  ND2 ASN A 253    19100  21777  15908   -971   -451  -1882  A    N  
ATOM   1728  OD1 ASN A 253      12.709  25.513  23.455  1.00150.33      A    O  
ANISOU 1728  OD1 ASN A 253    18800  22040  16278   -764   -798  -1868  A    O  
ATOM   1729  N   GLY A 254      14.808  21.885  20.301  1.00137.80      A    N  
ANISOU 1729  N   GLY A 254    18280  19858  14220  -1405  -1426  -1803  A    N  
ATOM   1730  CA  GLY A 254      15.832  21.183  19.552  1.00117.58      A    C  
ANISOU 1730  CA  GLY A 254    16079  17047  11550  -1463  -1502  -1857  A    C  
ATOM   1731  C   GLY A 254      16.382  20.084  20.434  1.00117.18      A    C  
ANISOU 1731  C   GLY A 254    16246  16764  11513  -1636  -1375  -1853  A    C  
ATOM   1732  O   GLY A 254      15.784  19.749  21.443  1.00115.21      A    O  
ANISOU 1732  O   GLY A 254    15872  16595  11308  -1792  -1270  -1795  A    O  
ATOM   1733  N   GLY A 255      17.488  19.477  20.030  1.00127.16      A    N  
ANISOU 1733  N   GLY A 255    17825  17740  12750  -1632  -1389  -1910  A    N  
ATOM   1734  CA  GLY A 255      18.119  18.455  20.844  1.00129.39      A    C  
ANISOU 1734  CA  GLY A 255    18317  17744  13101  -1764  -1311  -1874  A    C  
ATOM   1735  C   GLY A 255      18.768  19.003  22.103  1.00129.92      A    C  
ANISOU 1735  C   GLY A 255    18424  17755  13184  -1610  -1176  -1752  A    C  
ATOM   1736  O   GLY A 255      18.814  18.334  23.135  1.00132.85      A    O  
ANISOU 1736  O   GLY A 255    18865  18024  13589  -1780  -1121  -1649  A    O  
ATOM   1737  N   GLY A 256      19.256  20.235  22.008  1.00132.72      A    N  
ANISOU 1737  N   GLY A 256    18747  18179  13499  -1316  -1140  -1751  A    N  
ATOM   1738  CA  GLY A 256      20.231  20.789  22.937  1.00129.29      A    C  
ANISOU 1738  CA  GLY A 256    18429  17630  13067  -1147  -1044  -1667  A    C  
ATOM   1739  C   GLY A 256      19.929  21.108  24.393  1.00116.42      A    C  
ANISOU 1739  C   GLY A 256    16728  16111  11396  -1204   -914  -1566  A    C  
ATOM   1740  O   GLY A 256      20.766  20.838  25.252  1.00116.14      A    O  
ANISOU 1740  O   GLY A 256    16875  15898  11354  -1234   -886  -1466  A    O  
ATOM   1741  N   TRP A 257      18.779  21.702  24.692  1.00110.11      A    N  
ANISOU 1741  N   TRP A 257    15663  15604  10569  -1225   -832  -1596  A    N  
ATOM   1742  CA  TRP A 257      18.634  22.329  26.002  1.00104.73      A    C  
ANISOU 1742  CA  TRP A 257    14924  15050   9820  -1222   -657  -1560  A    C  
ATOM   1743  C   TRP A 257      17.204  22.496  26.511  1.00112.88      A    C  
ANISOU 1743  C   TRP A 257    15642  16399  10850  -1362   -516  -1611  A    C  
ATOM   1744  O   TRP A 257      16.249  22.493  25.735  1.00111.17      A    O  
ANISOU 1744  O   TRP A 257    15176  16341  10723  -1373   -579  -1672  A    O  
ATOM   1745  CB  TRP A 257      19.300  23.699  25.967  1.00112.28      A    C  
ANISOU 1745  CB  TRP A 257    15902  15988  10772   -892   -625  -1600  A    C  
ATOM   1746  CG  TRP A 257      18.701  24.591  24.928  1.00127.93      A    C  
ANISOU 1746  CG  TRP A 257    17661  18106  12842   -676   -691  -1685  A    C  
ATOM   1747  CD1 TRP A 257      18.961  24.580  23.588  1.00129.89      A    C  
ANISOU 1747  CD1 TRP A 257    17949  18282  13121   -581   -866  -1697  A    C  
ATOM   1748  CD2 TRP A 257      17.729  25.619  25.139  1.00136.68      A    C  
ANISOU 1748  CD2 TRP A 257    18468  19439  14027   -543   -597  -1760  A    C  
ATOM   1749  CE2 TRP A 257      17.450  26.195  23.885  1.00139.99      A    C  
ANISOU 1749  CE2 TRP A 257    18755  19893  14543   -362   -769  -1772  A    C  
ATOM   1750  CE3 TRP A 257      17.070  26.113  26.268  1.00144.52      A    C  
ANISOU 1750  CE3 TRP A 257    19286  20603  15023   -564   -374  -1829  A    C  
ATOM   1751  NE1 TRP A 257      18.216  25.541  22.954  1.00133.06      A    N  
ANISOU 1751  NE1 TRP A 257    18108  18851  13598   -412   -927  -1731  A    N  
ATOM   1752  CZ2 TRP A 257      16.543  27.237  23.727  1.00151.59      A    C  
ANISOU 1752  CZ2 TRP A 257    19905  21525  16165   -176   -764  -1819  A    C  
ATOM   1753  CZ3 TRP A 257      16.169  27.148  26.111  1.00147.54      A    C  
ANISOU 1753  CZ3 TRP A 257    19340  21152  15568   -365   -319  -1927  A    C  
ATOM   1754  CH2 TRP A 257      15.913  27.700  24.850  1.00149.50      A    C  
ANISOU 1754  CH2 TRP A 257    19444  21396  15965   -159   -532  -1907  A    C  
ATOM   1755  N   HIS A 258      17.082  22.666  27.828  1.00120.59      A    N  
ANISOU 1755  N   HIS A 258    16622  17479  11718  -1481   -322  -1590  A    N  
ATOM   1756  CA  HIS A 258      15.826  23.050  28.466  1.00123.97      A    C  
ANISOU 1756  CA  HIS A 258    16730  18229  12143  -1578   -107  -1682  A    C  
ATOM   1757  C   HIS A 258      16.040  24.339  29.261  1.00115.95      A    C  
ANISOU 1757  C   HIS A 258    15688  17292  11075  -1369     92  -1787  A    C  
ATOM   1758  O   HIS A 258      17.067  24.511  29.917  1.00107.72      A    O  
ANISOU 1758  O   HIS A 258    14934  16100   9894  -1356    108  -1730  A    O  
ATOM   1759  CB  HIS A 258      15.308  21.932  29.377  1.00132.01      A    C  
ANISOU 1759  CB  HIS A 258    17775  19344  13038  -2014     -4  -1590  A    C  
ATOM   1760  CG  HIS A 258      16.146  21.707  30.598  1.00134.81      A    C  
ANISOU 1760  CG  HIS A 258    18445  19595  13182  -2182     71  -1471  A    C  
ATOM   1761  CD2 HIS A 258      17.077  20.766  30.880  1.00126.79      A    C  
ANISOU 1761  CD2 HIS A 258    17769  18309  12098  -2357    -87  -1276  A    C  
ATOM   1762  ND1 HIS A 258      16.078  22.524  31.707  1.00135.00      A    N  
ANISOU 1762  ND1 HIS A 258    18453  19796  13045  -2190    317  -1549  A    N  
ATOM   1763  CE1 HIS A 258      16.924  22.090  32.623  1.00128.60      A    C  
ANISOU 1763  CE1 HIS A 258    17974  18856  12033  -2394    288  -1387  A    C  
ATOM   1764  NE2 HIS A 258      17.545  21.026  32.146  1.00123.15      A    N  
ANISOU 1764  NE2 HIS A 258    17489  17884  11419  -2485     31  -1203  A    N  
ATOM   1765  N   GLY A 259      15.068  25.240  29.197  1.00120.14      A    N  
ANISOU 1765  N   GLY A 259    15863  18044  11741  -1208    233  -1945  A    N  
ATOM   1766  CA  GLY A 259      15.213  26.562  29.776  1.00134.05      A    C  
ANISOU 1766  CA  GLY A 259    17578  19839  13516   -961    417  -2092  A    C  
ATOM   1767  C   GLY A 259      15.037  26.665  31.281  1.00145.53      A    C  
ANISOU 1767  C   GLY A 259    19075  21456  14765  -1179    738  -2183  A    C  
ATOM   1768  O   GLY A 259      15.556  27.589  31.905  1.00146.39      A    O  
ANISOU 1768  O   GLY A 259    19307  21517  14798  -1039    867  -2289  A    O  
ATOM   1769  N   HIS A 260      14.308  25.716  31.860  1.00153.71      A    N  
ANISOU 1769  N   HIS A 260    20026  22689  15687  -1554    866  -2145  A    N  
ATOM   1770  CA  HIS A 260      13.740  25.873  33.201  1.00154.64      A    C  
ANISOU 1770  CA  HIS A 260    20071  23070  15617  -1798   1234  -2278  A    C  
ATOM   1771  C   HIS A 260      14.733  26.142  34.339  1.00134.61      A    C  
ANISOU 1771  C   HIS A 260    17927  20458  12761  -1916   1336  -2262  A    C  
ATOM   1772  O   HIS A 260      14.416  26.897  35.256  1.00133.78      A    O  
ANISOU 1772  O   HIS A 260    17757  20533  12540  -1941   1657  -2478  A    O  
ATOM   1773  CB  HIS A 260      12.899  24.641  33.538  1.00163.37      A    C  
ANISOU 1773  CB  HIS A 260    21066  24381  16626  -2245   1308  -2177  A    C  
ATOM   1774  CG  HIS A 260      11.605  24.575  32.784  1.00170.68      A    C  
ANISOU 1774  CG  HIS A 260    21502  25507  17841  -2194   1328  -2266  A    C  
ATOM   1775  CD2 HIS A 260      10.738  25.549  32.418  1.00173.84      A    C  
ANISOU 1775  CD2 HIS A 260    21456  26064  18534  -1897   1456  -2481  A    C  
ATOM   1776  ND1 HIS A 260      11.071  23.393  32.319  1.00174.05      A    N  
ANISOU 1776  ND1 HIS A 260    21848  25976  18307  -2480   1177  -2114  A    N  
ATOM   1777  CE1 HIS A 260       9.932  23.641  31.697  1.00176.07      A    C  
ANISOU 1777  CE1 HIS A 260    21625  26433  18841  -2378   1205  -2226  A    C  
ATOM   1778  NE2 HIS A 260       9.706  24.941  31.743  1.00176.47      A    N  
ANISOU 1778  NE2 HIS A 260    21432  26554  19066  -2014   1367  -2439  A    N  
ATOM   1779  N   GLY A 261      15.916  25.537  34.304  1.00123.38      A    N  
ANISOU 1779  N   GLY A 261    16899  18774  11205  -1998   1070  -2023  A    N  
ATOM   1780  CA  GLY A 261      16.898  25.823  35.338  1.00119.55      A    C  
ANISOU 1780  CA  GLY A 261    16775  18214  10433  -2113   1107  -1978  A    C  
ATOM   1781  C   GLY A 261      17.847  24.699  35.709  1.00124.37      A    C  
ANISOU 1781  C   GLY A 261    17764  18634  10856  -2410    858  -1656  A    C  
ATOM   1782  O   GLY A 261      18.269  23.917  34.858  1.00122.12      A    O  
ANISOU 1782  O   GLY A 261    17543  18116  10742  -2356    575  -1476  A    O  
ATOM   1783  N   TRP A 262      18.211  24.656  36.989  1.00129.98      A    N  
ANISOU 1783  N   TRP A 262    18733  19432  11223  -2724    959  -1590  A    N  
ATOM   1784  CA  TRP A 262      19.106  23.638  37.535  1.00132.01      A    C  
ANISOU 1784  CA  TRP A 262    19351  19510  11297  -3041    704  -1248  A    C  
ATOM   1785  C   TRP A 262      18.363  22.357  37.896  1.00143.43      A    C  
ANISOU 1785  C   TRP A 262    20783  21074  12639  -3489    720  -1066  A    C  
ATOM   1786  O   TRP A 262      17.168  22.380  38.198  1.00148.56      A    O  
ANISOU 1786  O   TRP A 262    21189  22046  13210  -3670   1020  -1224  A    O  
ATOM   1787  CB  TRP A 262      19.821  24.155  38.781  1.00132.12      A    C  
ANISOU 1787  CB  TRP A 262    19670  19579  10949  -3236    761  -1220  A    C  
ATOM   1788  CG  TRP A 262      20.646  25.376  38.569  1.00127.24      A    C  
ANISOU 1788  CG  TRP A 262    19116  18826  10403  -2865    726  -1372  A    C  
ATOM   1789  CD1 TRP A 262      20.263  26.671  38.765  1.00132.29      A    C  
ANISOU 1789  CD1 TRP A 262    19627  19621  11016  -2668   1015  -1716  A    C  
ATOM   1790  CD2 TRP A 262      22.009  25.420  38.132  1.00118.07      A    C  
ANISOU 1790  CD2 TRP A 262    18156  17329   9376  -2655    386  -1188  A    C  
ATOM   1791  CE2 TRP A 262      22.388  26.777  38.081  1.00125.59      A    C  
ANISOU 1791  CE2 TRP A 262    19105  18263  10350  -2362    478  -1418  A    C  
ATOM   1792  CE3 TRP A 262      22.945  24.444  37.776  1.00107.83      A    C  
ANISOU 1792  CE3 TRP A 262    17023  15733   8216  -2684     22   -863  A    C  
ATOM   1793  NE1 TRP A 262      21.306  27.520  38.472  1.00129.07      A    N  
ANISOU 1793  NE1 TRP A 262    19355  18986  10700  -2368    856  -1740  A    N  
ATOM   1794  CZ2 TRP A 262      23.664  27.180  37.687  1.00115.22      A    C  
ANISOU 1794  CZ2 TRP A 262    17944  16674   9159  -2128    219  -1315  A    C  
ATOM   1795  CZ3 TRP A 262      24.210  24.847  37.385  1.00104.20      A    C  
ANISOU 1795  CZ3 TRP A 262    16686  15004   7903  -2425   -214   -783  A    C  
ATOM   1796  CH2 TRP A 262      24.558  26.203  37.343  1.00105.34      A    C  
ANISOU 1796  CH2 TRP A 262    16821  15169   8035  -2165   -115   -999  A    C  
ATOM   1797  N   VAL A 263      19.077  21.237  37.870  1.00150.30      A    N  
ANISOU 1797  N   VAL A 263    21901  21670  13537  -3670    395   -730  A    N  
ATOM   1798  CA  VAL A 263      18.469  19.952  38.184  1.00162.29      A    C  
ANISOU 1798  CA  VAL A 263    23448  23231  14984  -4112    356   -512  A    C  
ATOM   1799  C   VAL A 263      19.259  19.184  39.247  1.00162.73      A    C  
ANISOU 1799  C   VAL A 263    23897  23153  14781  -4522    140   -139  A    C  
ATOM   1800  O   VAL A 263      20.491  19.229  39.283  1.00151.25      A    O  
ANISOU 1800  O   VAL A 263    22679  21410  13381  -4383   -138     31  A    O  
ATOM   1801  CB  VAL A 263      18.328  19.084  36.915  1.00170.98      A    C  
ANISOU 1801  CB  VAL A 263    24423  24074  16465  -3962    133   -452  A    C  
ATOM   1802  CG1 VAL A 263      19.689  18.754  36.341  1.00172.78      A    C  
ANISOU 1802  CG1 VAL A 263    24877  23852  16919  -3718   -228   -279  A    C  
ATOM   1803  CG2 VAL A 263      17.543  17.813  37.213  1.00178.12      A    C  
ANISOU 1803  CG2 VAL A 263    25328  25034  17317  -4435    118   -261  A    C  
ATOM   1804  N   GLY A 264      18.532  18.505  40.129  1.00175.23      A    N  
ANISOU 1804  N   GLY A 264    25535  24961  16081  -5045    263      2  A    N  
ATOM   1805  CA  GLY A 264      19.124  17.548  41.042  1.00173.67      A    C  
ANISOU 1805  CA  GLY A 264    25702  24616  15667  -5500      0    429  A    C  
ATOM   1806  C   GLY A 264      19.774  18.159  42.261  1.00162.39      A    C  
ANISOU 1806  C   GLY A 264    24561  23330  13809  -5715     24    510  A    C  
ATOM   1807  O   GLY A 264      19.663  19.356  42.511  1.00145.98      A    O  
ANISOU 1807  O   GLY A 264    22403  21502  11560  -5550    309    189  A    O  
ATOM   1808  N   GLU A 265      20.452  17.313  43.027  1.00165.84      A    N  
ANISOU 1808  N   GLU A 265    25342  23591  14079  -6102   -301    951  A    N  
ATOM   1809  CA  GLU A 265      21.113  17.739  44.251  1.00170.58      A    C  
ANISOU 1809  CA  GLU A 265    26265  24323  14224  -6401   -354   1102  A    C  
ATOM   1810  C   GLU A 265      22.544  17.218  44.311  1.00158.30      A    C  
ANISOU 1810  C   GLU A 265    24987  22312  12846  -6350   -902   1525  A    C  
ATOM   1811  O   GLU A 265      22.889  16.238  43.646  1.00151.06      A    O  
ANISOU 1811  O   GLU A 265    24056  20990  12349  -6234  -1225   1767  A    O  
ATOM   1812  CB  GLU A 265      20.327  17.254  45.468  1.00179.03      A    C  
ANISOU 1812  CB  GLU A 265    27497  25763  14762  -7107   -167   1262  A    C  
ATOM   1813  CG  GLU A 265      18.893  17.750  45.510  1.00170.77      A    C  
ANISOU 1813  CG  GLU A 265    26138  25198  13549  -7193    410    837  A    C  
ATOM   1814  CD  GLU A 265      18.038  16.956  46.466  1.00168.56      A    C  
ANISOU 1814  CD  GLU A 265    25899  25176  12972  -7837    557   1017  A    C  
ATOM   1815  OE1 GLU A 265      18.575  16.034  47.113  1.00172.63      A    O  
ANISOU 1815  OE1 GLU A 265    26694  25468  13428  -8206    183   1477  A    O  
ATOM   1816  OE2 GLU A 265      16.827  17.244  46.555  1.00170.72      A    O1-
ANISOU 1816  OE2 GLU A 265    25888  25853  13126  -7957   1033    696  A    O1-
ATOM   1817  N   GLY A 266      23.367  17.867  45.125  1.00148.12      A    N  
ANISOU 1817  N   GLY A 266    23936  21085  11257  -6445  -1005   1601  A    N  
ATOM   1818  CA  GLY A 266      24.703  17.377  45.397  1.00142.85      A    C  
ANISOU 1818  CA  GLY A 266    23488  20016  10772  -6452  -1534   2032  A    C  
ATOM   1819  C   GLY A 266      25.801  18.077  44.630  1.00131.40      A    C  
ANISOU 1819  C   GLY A 266    21983  18303   9640  -5905  -1716   1925  A    C  
ATOM   1820  O   GLY A 266      25.566  19.078  43.958  1.00140.71      A    O  
ANISOU 1820  O   GLY A 266    22940  19600  10925  -5492  -1418   1488  A    O  
ATOM   1821  N   LYS A 267      27.008  17.532  44.730  1.00122.47      A    N  
ANISOU 1821  N   LYS A 267    21006  16787   8740  -5885  -2214   2330  A    N  
ATOM   1822  CA  LYS A 267      28.186  18.123  44.107  1.00113.65      A    C  
ANISOU 1822  CA  LYS A 267    19805  15397   7982  -5394  -2413   2269  A    C  
ATOM   1823  C   LYS A 267      28.420  17.610  42.691  1.00106.16      A    C  
ANISOU 1823  C   LYS A 267    18595  14051   7690  -4890  -2498   2188  A    C  
ATOM   1824  O   LYS A 267      27.898  16.563  42.309  1.00 99.57      A    O  
ANISOU 1824  O   LYS A 267    17707  13050   7074  -4967  -2540   2294  A    O  
ATOM   1825  CB  LYS A 267      29.417  17.853  44.970  1.00121.46      A    C  
ANISOU 1825  CB  LYS A 267    20989  16167   8993  -5589  -2882   2706  A    C  
ATOM   1826  CG  LYS A 267      29.327  18.470  46.363  1.00149.19      A    C  
ANISOU 1826  CG  LYS A 267    24565  19983  12136  -5946  -2725   2644  A    C  
ATOM   1827  CD  LYS A 267      30.462  18.021  47.278  1.00161.62      A    C  
ANISOU 1827  CD  LYS A 267    26272  21327  13811  -6183  -3208   3085  A    C  
ATOM   1828  CE  LYS A 267      31.813  18.558  46.827  1.00154.79      A    C  
ANISOU 1828  CE  LYS A 267    25337  20201  13274  -5787  -3489   3127  A    C  
ATOM   1829  NZ  LYS A 267      32.469  17.696  45.801  1.00156.92      A    N1+
ANISOU 1829  NZ  LYS A 267    25548  20021  14055  -5477  -3865   3397  A    N1+
ATOM   1830  N   TRP A 268      29.195  18.373  41.918  1.00117.93      A    N  
ANISOU 1830  N   TRP A 268    19936  15402   9469  -4403  -2507   1981  A    N  
ATOM   1831  CA  TRP A 268      29.503  18.044  40.524  1.00116.87      A    C  
ANISOU 1831  CA  TRP A 268    19562  14931   9913  -3916  -2544   1846  A    C  
ATOM   1832  C   TRP A 268      30.685  17.098  40.357  1.00115.54      A    C  
ANISOU 1832  C   TRP A 268    19421  14266  10213  -3821  -2998   2212  A    C  
ATOM   1833  O   TRP A 268      31.644  17.146  41.125  1.00125.81      A    O  
ANISOU 1833  O   TRP A 268    20864  15469  11469  -3955  -3317   2522  A    O  
ATOM   1834  CB  TRP A 268      29.806  19.312  39.727  1.00113.69      A    C  
ANISOU 1834  CB  TRP A 268    18982  14613   9602  -3456  -2333   1464  A    C  
ATOM   1835  CG  TRP A 268      28.655  20.244  39.571  1.00124.22      A    C  
ANISOU 1835  CG  TRP A 268    20206  16340  10651  -3412  -1891   1058  A    C  
ATOM   1836  CD1 TRP A 268      28.511  21.473  40.144  1.00131.59      A    C  
ANISOU 1836  CD1 TRP A 268    21192  17580  11227  -3446  -1676    848  A    C  
ATOM   1837  CD2 TRP A 268      27.462  20.010  38.809  1.00131.63      A    C  
ANISOU 1837  CD2 TRP A 268    20949  17394  11671  -3329  -1620    812  A    C  
ATOM   1838  CE2 TRP A 268      26.651  21.152  38.960  1.00137.33      A    C  
ANISOU 1838  CE2 TRP A 268    21581  18489  12111  -3290  -1255    472  A    C  
ATOM   1839  CE3 TRP A 268      27.011  18.951  38.021  1.00123.64      A    C  
ANISOU 1839  CE3 TRP A 268    19828  16194  10958  -3294  -1663    842  A    C  
ATOM   1840  NE1 TRP A 268      27.310  22.028  39.770  1.00132.96      A    N  
ANISOU 1840  NE1 TRP A 268    21188  18030  11299  -3354  -1282    483  A    N  
ATOM   1841  CZ2 TRP A 268      25.407  21.260  38.331  1.00134.08      A    C  
ANISOU 1841  CZ2 TRP A 268    20936  18274  11734  -3200   -956    191  A    C  
ATOM   1842  CZ3 TRP A 268      25.774  19.063  37.410  1.00119.32      A    C  
ANISOU 1842  CZ3 TRP A 268    19079  15864  10392  -3242  -1368    559  A    C  
ATOM   1843  CH2 TRP A 268      24.988  20.208  37.568  1.00122.78      A    C  
ANISOU 1843  CH2 TRP A 268    19397  16682  10571  -3191  -1029    252  A    C  
ATOM   1844  N   THR A 269      30.608  16.248  39.339  1.00119.13      A    N  
ANISOU 1844  N   THR A 269    19726  14404  11133  -3590  -3027   2159  A    N  
ATOM   1845  CA  THR A 269      31.732  15.412  38.931  1.00138.19      A    C  
ANISOU 1845  CA  THR A 269    22092  16302  14110  -3383  -3388   2395  A    C  
ATOM   1846  C   THR A 269      32.130  15.790  37.505  1.00137.48      A    C  
ANISOU 1846  C   THR A 269    21750  16067  14420  -2844  -3218   2026  A    C  
ATOM   1847  O   THR A 269      31.296  15.772  36.600  1.00137.69      A    O  
ANISOU 1847  O   THR A 269    21657  16179  14479  -2707  -2937   1704  A    O  
ATOM   1848  CB  THR A 269      31.399  13.906  39.013  1.00141.55      A    C  
ANISOU 1848  CB  THR A 269    22599  16399  14786  -3619  -3600   2675  A    C  
ATOM   1849  CG2 THR A 269      30.943  13.527  40.417  1.00136.21      A    C  
ANISOU 1849  CG2 THR A 269    22193  15899  13663  -4210  -3759   3064  A    C  
ATOM   1850  OG1 THR A 269      30.359  13.590  38.082  1.00146.94      A    O  
ANISOU 1850  OG1 THR A 269    23160  17126  15543  -3530  -3304   2352  A    O  
ATOM   1851  N   VAL A 270      33.402  16.122  37.302  1.00136.61      A    N  
ANISOU 1851  N   VAL A 270    21552  15752  14600  -2569  -3396   2083  A    N  
ATOM   1852  CA  VAL A 270      33.872  16.614  36.004  1.00142.30      A    C  
ANISOU 1852  CA  VAL A 270    22046  16386  15637  -2095  -3214   1736  A    C  
ATOM   1853  C   VAL A 270      34.750  15.594  35.271  1.00159.23      A    C  
ANISOU 1853  C   VAL A 270    24054  18018  18429  -1843  -3405   1804  A    C  
ATOM   1854  O   VAL A 270      35.721  15.081  35.823  1.00175.75      A    O  
ANISOU 1854  O   VAL A 270    26155  19808  20814  -1875  -3758   2146  A    O  
ATOM   1855  CB  VAL A 270      34.659  17.943  36.157  1.00102.23      A    C  
ANISOU 1855  CB  VAL A 270    16928  11501  10415  -1936  -3187   1663  A    C  
ATOM   1856  CG1 VAL A 270      35.648  17.861  37.316  1.00125.46      A    C  
ANISOU 1856  CG1 VAL A 270    19984  14332  13351  -2143  -3580   2085  A    C  
ATOM   1857  CG2 VAL A 270      35.368  18.308  34.861  1.00 92.02      A    C  
ANISOU 1857  CG2 VAL A 270    15403  10062   9497  -1484  -3060   1389  A    C  
ATOM   1858  N   LYS A 271      34.396  15.301  34.022  1.00160.81      A    N  
ANISOU 1858  N   LYS A 271    24122  18119  18859  -1600  -3173   1468  A    N  
ATOM   1859  CA  LYS A 271      35.174  14.377  33.200  1.00157.24      A    C  
ANISOU 1859  CA  LYS A 271    23532  17189  19024  -1339  -3271   1427  A    C  
ATOM   1860  C   LYS A 271      35.460  14.961  31.809  1.00158.86      A    C  
ANISOU 1860  C   LYS A 271    23544  17442  19374   -955  -2970    993  A    C  
ATOM   1861  O   LYS A 271      34.573  15.525  31.170  1.00161.79      A    O  
ANISOU 1861  O   LYS A 271    23912  18121  19439   -931  -2680    691  A    O  
ATOM   1862  CB  LYS A 271      34.426  13.044  33.063  1.00147.62      A    C  
ANISOU 1862  CB  LYS A 271    22399  15704  17985  -1514  -3323   1470  A    C  
ATOM   1863  CG  LYS A 271      34.424  12.178  34.321  1.00150.98      A    C  
ANISOU 1863  CG  LYS A 271    23005  15929  18432  -1878  -3694   1965  A    C  
ATOM   1864  CD  LYS A 271      33.409  11.039  34.210  1.00148.92      A    C  
ANISOU 1864  CD  LYS A 271    22859  15503  18220  -2123  -3690   1981  A    C  
ATOM   1865  CE  LYS A 271      33.335  10.209  35.487  1.00142.84      A    C  
ANISOU 1865  CE  LYS A 271    22298  14559  17417  -2542  -4064   2509  A    C  
ATOM   1866  NZ  LYS A 271      32.308   9.129  35.412  1.00129.32      A    N1+
ANISOU 1866  NZ  LYS A 271    20707  12698  15732  -2825  -4059   2542  A    N1+
ATOM   1867  N   LYS A 272      36.705  14.834  31.353  1.00156.98      A    N  
ANISOU 1867  N   LYS A 272    23134  16909  19603   -670  -3048    977  A    N  
ATOM   1868  CA  LYS A 272      37.095  15.258  30.005  1.00148.47      A    C  
ANISOU 1868  CA  LYS A 272    21878  15848  18688   -336  -2761    578  A    C  
ATOM   1869  C   LYS A 272      37.384  14.038  29.124  1.00154.75      A    C  
ANISOU 1869  C   LYS A 272    22578  16195  20023   -173  -2726    404  A    C  
ATOM   1870  O   LYS A 272      38.345  13.307  29.370  1.00153.80      A    O  
ANISOU 1870  O   LYS A 272    22353  15660  20423    -68  -2947    584  A    O  
ATOM   1871  CB  LYS A 272      38.318  16.185  30.053  1.00136.12      A    C  
ANISOU 1871  CB  LYS A 272    20157  14340  17223   -136  -2798    622  A    C  
ATOM   1872  CG  LYS A 272      38.154  17.395  30.971  1.00126.79      A    C  
ANISOU 1872  CG  LYS A 272    19085  13548  15542   -302  -2850    780  A    C  
ATOM   1873  CD  LYS A 272      39.446  18.207  31.096  1.00127.74      A    C  
ANISOU 1873  CD  LYS A 272    19055  13674  15805   -143  -2942    864  A    C  
ATOM   1874  CE  LYS A 272      40.625  17.360  31.585  1.00136.37      A    C  
ANISOU 1874  CE  LYS A 272    20013  14355  17447    -90  -3286   1177  A    C  
ATOM   1875  NZ  LYS A 272      40.473  16.834  32.976  1.00134.52      A    N1+
ANISOU 1875  NZ  LYS A 272    19958  14040  17114   -410  -3667   1621  A    N1+
ATOM   1876  N   GLY A 273      36.559  13.819  28.102  1.00160.43      A    N  
ANISOU 1876  N   GLY A 273    23329  16988  20638   -156  -2459     49  A    N  
ATOM   1877  CA  GLY A 273      36.645  12.603  27.310  1.00166.51      A    C  
ANISOU 1877  CA  GLY A 273    24065  17339  21861    -64  -2408   -155  A    C  
ATOM   1878  C   GLY A 273      36.252  12.745  25.850  1.00166.48      A    C  
ANISOU 1878  C   GLY A 273    24030  17468  21759     57  -2052   -646  A    C  
ATOM   1879  O   GLY A 273      35.568  13.691  25.472  1.00165.21      A    O  
ANISOU 1879  O   GLY A 273    23906  17746  21121     11  -1871   -794  A    O  
ATOM   1880  N   ASN A 274      36.699  11.802  25.026  1.00173.16      A    N  
ANISOU 1880  N   ASN A 274    24809  17919  23065    205  -1959   -900  A    N  
ATOM   1881  CA  ASN A 274      36.238  11.703  23.645  1.00170.57      A    C  
ANISOU 1881  CA  ASN A 274    24504  17679  22628    244  -1642  -1374  A    C  
ATOM   1882  C   ASN A 274      34.816  11.148  23.583  1.00174.96      A    C  
ANISOU 1882  C   ASN A 274    25254  18313  22911    -46  -1657  -1422  A    C  
ATOM   1883  O   ASN A 274      34.241  10.787  24.608  1.00173.40      A    O  
ANISOU 1883  O   ASN A 274    25161  18078  22646   -270  -1890  -1094  A    O  
ATOM   1884  CB  ASN A 274      37.180  10.819  22.823  1.00161.98      A    C  
ANISOU 1884  CB  ASN A 274    23291  16125  22128    474  -1510  -1673  A    C  
ATOM   1885  CG  ASN A 274      38.438  11.547  22.390  1.00160.04      A    C  
ANISOU 1885  CG  ASN A 274    22816  15939  22053    759  -1345  -1794  A    C  
ATOM   1886  ND2 ASN A 274      39.340  11.781  23.336  1.00163.46      A    N  
ANISOU 1886  ND2 ASN A 274    23104  16255  22747    865  -1578  -1439  A    N  
ATOM   1887  OD1 ASN A 274      38.593  11.906  21.220  1.00157.62      A    O  
ANISOU 1887  OD1 ASN A 274    22464  15800  21624    853  -1020  -2190  A    O  
ATOM   1888  N   VAL A 275      34.256  11.066  22.379  1.00173.49      A    N  
ANISOU 1888  N   VAL A 275    25115  18246  22558    -72  -1414  -1824  A    N  
ATOM   1889  CA  VAL A 275      32.919  10.508  22.202  1.00172.69      A    C  
ANISOU 1889  CA  VAL A 275    25171  18218  22225   -358  -1430  -1898  A    C  
ATOM   1890  C   VAL A 275      32.895   9.454  21.101  1.00189.05      A    C  
ANISOU 1890  C   VAL A 275    27307  19959  24566   -363  -1284  -2306  A    C  
ATOM   1891  O   VAL A 275      33.742   9.453  20.204  1.00199.71      A    O  
ANISOU 1891  O   VAL A 275    28580  21183  26119   -147  -1072  -2629  A    O  
ATOM   1892  CB  VAL A 275      31.881  11.599  21.865  1.00162.07      A    C  
ANISOU 1892  CB  VAL A 275    23844  17464  20271   -480  -1319  -1962  A    C  
ATOM   1893  CG1 VAL A 275      31.604  12.473  23.076  1.00155.23      A    C  
ANISOU 1893  CG1 VAL A 275    22954  16898  19130   -547  -1462  -1583  A    C  
ATOM   1894  CG2 VAL A 275      32.351  12.434  20.684  1.00162.93      A    C  
ANISOU 1894  CG2 VAL A 275    23881  17803  20223   -288  -1070  -2281  A    C  
ATOM   1895  N   SER A 276      31.908   8.567  21.174  1.00208.02      A    N  
ANISOU 1895  N   SER A 276    29854  22230  26952   -634  -1382  -2307  A    N  
ATOM   1896  CA  SER A 276      31.788   7.457  20.233  1.00216.36      A    C  
ANISOU 1896  CA  SER A 276    31011  22926  28268   -693  -1274  -2692  A    C  
ATOM   1897  C   SER A 276      31.360   7.910  18.844  1.00209.44      A    C  
ANISOU 1897  C   SER A 276    30173  22395  27012   -732  -1003  -3139  A    C  
ATOM   1898  O   SER A 276      30.975   9.062  18.638  1.00211.20      A    O  
ANISOU 1898  O   SER A 276    30346  23142  26757   -741   -938  -3105  A    O  
ATOM   1899  CB  SER A 276      30.795   6.415  20.753  1.00222.72      A    C  
ANISOU 1899  CB  SER A 276    31973  23510  29139  -1022  -1482  -2534  A    C  
ATOM   1900  OG  SER A 276      29.460   6.867  20.615  1.00223.29      A    O  
ANISOU 1900  OG  SER A 276    32099  24071  28670  -1303  -1474  -2526  A    O  
ATOM   1901  N   SER A 277      31.449   6.989  17.892  1.00200.87      A    N  
ANISOU 1901  N   SER A 277    29184  20989  26148   -764   -857  -3557  A    N  
ATOM   1902  CA  SER A 277      30.908   7.194  16.557  1.00187.40      A    C  
ANISOU 1902  CA  SER A 277    27573  19578  24053   -898   -639  -3987  A    C  
ATOM   1903  C   SER A 277      29.394   7.389  16.617  1.00179.12      A    C  
ANISOU 1903  C   SER A 277    26610  18921  22526  -1242   -786  -3858  A    C  
ATOM   1904  O   SER A 277      28.838   8.204  15.883  1.00170.75      A    O  
ANISOU 1904  O   SER A 277    25550  18343  20985  -1329   -702  -3980  A    O  
ATOM   1905  CB  SER A 277      31.265   6.014  15.653  1.00190.98      A    C  
ANISOU 1905  CB  SER A 277    28144  19553  24865   -910   -465  -4473  A    C  
ATOM   1906  OG  SER A 277      32.668   5.814  15.603  1.00194.02      A    O  
ANISOU 1906  OG  SER A 277    28398  19563  25756   -571   -309  -4611  A    O  
ATOM   1907  N   THR A 278      28.736   6.641  17.501  1.00179.07      A    N  
ANISOU 1907  N   THR A 278    26661  18707  22672  -1446  -1016  -3591  A    N  
ATOM   1908  CA  THR A 278      27.303   6.805  17.742  1.00167.73      A    C  
ANISOU 1908  CA  THR A 278    25250  17641  20839  -1776  -1159  -3420  A    C  
ATOM   1909  C   THR A 278      27.040   8.103  18.501  1.00163.61      A    C  
ANISOU 1909  C   THR A 278    24570  17617  19976  -1704  -1217  -3064  A    C  
ATOM   1910  O   THR A 278      25.901   8.552  18.619  1.00147.54      A    O  
ANISOU 1910  O   THR A 278    22489  15989  17580  -1913  -1285  -2948  A    O  
ATOM   1911  CB  THR A 278      26.722   5.621  18.549  1.00161.47      A    C  
ANISOU 1911  CB  THR A 278    24559  16478  20315  -2045  -1374  -3211  A    C  
ATOM   1912  CG2 THR A 278      25.206   5.540  18.394  1.00159.33      A    C  
ANISOU 1912  CG2 THR A 278    24318  16547  19673  -2437  -1462  -3194  A    C  
ATOM   1913  OG1 THR A 278      27.311   4.396  18.099  1.00170.82      A    O  
ANISOU 1913  OG1 THR A 278    25879  17046  21981  -2018  -1337  -3491  A    O  
ATOM   1914  N   GLY A 279      28.113   8.703  19.005  1.00186.38      A    N  
ANISOU 1914  N   GLY A 279    27358  20454  23004  -1406  -1187  -2908  A    N  
ATOM   1915  CA  GLY A 279      28.038   9.963  19.721  1.00198.42      A    C  
ANISOU 1915  CA  GLY A 279    28753  22397  24241  -1311  -1223  -2611  A    C  
ATOM   1916  C   GLY A 279      27.711   9.769  21.185  1.00197.57      A    C  
ANISOU 1916  C   GLY A 279    28639  22241  24190  -1447  -1425  -2184  A    C  
ATOM   1917  O   GLY A 279      27.227  10.681  21.852  1.00190.69      A    O  
ANISOU 1917  O   GLY A 279    27683  21756  23013  -1481  -1455  -1959  A    O  
ATOM   1918  N   ARG A 280      27.999   8.574  21.687  1.00189.53      A    N  
ANISOU 1918  N   ARG A 280    27716  20731  23568  -1532  -1561  -2076  A    N  
ATOM   1919  CA  ARG A 280      27.819   8.258  23.096  1.00176.84      A    C  
ANISOU 1919  CA  ARG A 280    26138  19024  22029  -1699  -1776  -1639  A    C  
ATOM   1920  C   ARG A 280      29.032   8.736  23.884  1.00162.72      A    C  
ANISOU 1920  C   ARG A 280    24284  17119  20421  -1447  -1853  -1387  A    C  
ATOM   1921  O   ARG A 280      30.166   8.404  23.540  1.00160.84      A    O  
ANISOU 1921  O   ARG A 280    24018  16508  20586  -1195  -1836  -1498  A    O  
ATOM   1922  CB  ARG A 280      27.613   6.749  23.283  1.00182.89      A    C  
ANISOU 1922  CB  ARG A 280    27051  19276  23163  -1926  -1934  -1589  A    C  
ATOM   1923  CG  ARG A 280      27.094   6.325  24.652  1.00178.16      A    C  
ANISOU 1923  CG  ARG A 280    26521  18638  22535  -2230  -2164  -1128  A    C  
ATOM   1924  CD  ARG A 280      27.285   4.825  24.867  1.00174.42      A    C  
ANISOU 1924  CD  ARG A 280    26201  17519  22552  -2381  -2361  -1031  A    C  
ATOM   1925  NE  ARG A 280      28.699   4.477  24.984  1.00175.05      A    N  
ANISOU 1925  NE  ARG A 280    26265  17092  23155  -2065  -2454   -980  A    N  
ATOM   1926  CZ  ARG A 280      29.251   3.933  26.063  1.00173.80      A    C  
ANISOU 1926  CZ  ARG A 280    26161  16566  23311  -2111  -2735   -553  A    C  
ATOM   1927  NH1 ARG A 280      28.505   3.652  27.121  1.00176.28      A    N1+
ANISOU 1927  NH1 ARG A 280    26584  16971  23424  -2493  -2933   -147  A    N1+
ATOM   1928  NH2 ARG A 280      30.548   3.657  26.081  1.00170.57      A    N  
ANISOU 1928  NH2 ARG A 280    25685  15701  23424  -1793  -2824   -524  A    N  
ATOM   1929  N   CYS A 281      28.805   9.529  24.927  1.00152.53      A    N  
ANISOU 1929  N   CYS A 281    22958  16157  18842  -1520  -1927  -1069  A    N  
ATOM   1930  CA  CYS A 281      29.917  10.004  25.741  1.00143.11      A    C  
ANISOU 1930  CA  CYS A 281    21718  14879  17779  -1331  -2034   -808  A    C  
ATOM   1931  C   CYS A 281      30.452   8.841  26.561  1.00136.76      A    C  
ANISOU 1931  C   CYS A 281    21004  13548  17409  -1426  -2306   -503  A    C  
ATOM   1932  O   CYS A 281      29.719   8.236  27.344  1.00132.43      A    O  
ANISOU 1932  O   CYS A 281    20574  12962  16783  -1755  -2463   -242  A    O  
ATOM   1933  CB  CYS A 281      29.496  11.157  26.652  1.00151.22      A    C  
ANISOU 1933  CB  CYS A 281    22713  16393  18353  -1420  -2032   -582  A    C  
ATOM   1934  SG  CYS A 281      30.822  11.784  27.725  1.00138.88      A    S  
ANISOU 1934  SG  CYS A 281    21120  14760  16889  -1255  -2198   -249  A    S  
ATOM   1935  N   LEU A 282      31.728   8.530  26.365  1.00146.88      A    N  
ANISOU 1935  N   LEU A 282    22219  14421  19167  -1145  -2365   -526  A    N  
ATOM   1936  CA  LEU A 282      32.351   7.371  26.992  1.00171.38      A    C  
ANISOU 1936  CA  LEU A 282    25377  16937  22801  -1176  -2649   -252  A    C  
ATOM   1937  C   LEU A 282      32.272   7.418  28.516  1.00189.99      A    C  
ANISOU 1937  C   LEU A 282    27824  19358  25005  -1431  -2952    297  A    C  
ATOM   1938  O   LEU A 282      32.120   6.383  29.170  1.00216.56      A    O  
ANISOU 1938  O   LEU A 282    31318  22360  28606  -1661  -3214    595  A    O  
ATOM   1939  CB  LEU A 282      33.810   7.261  26.552  1.00169.11      A    C  
ANISOU 1939  CB  LEU A 282    24926  16268  23059   -780  -2641   -372  A    C  
ATOM   1940  CG  LEU A 282      34.037   7.191  25.043  1.00161.67      A    C  
ANISOU 1940  CG  LEU A 282    23902  15253  22272   -540  -2310   -938  A    C  
ATOM   1941  CD1 LEU A 282      35.516   7.035  24.742  1.00161.83      A    C  
ANISOU 1941  CD1 LEU A 282    23726  14888  22875   -164  -2288  -1036  A    C  
ATOM   1942  CD2 LEU A 282      33.233   6.052  24.426  1.00166.58      A    C  
ANISOU 1942  CD2 LEU A 282    24674  15591  23029   -727  -2265  -1183  A    C  
ATOM   1943  N   SER A 283      32.370   8.622  29.070  1.00169.79      A    N  
ANISOU 1943  N   SER A 283    25218  17258  22038  -1413  -2916    426  A    N  
ATOM   1944  CA  SER A 283      32.384   8.808  30.516  1.00157.31      A    C  
ANISOU 1944  CA  SER A 283    23735  15793  20240  -1667  -3175    913  A    C  
ATOM   1945  C   SER A 283      31.054   8.481  31.204  1.00166.67      A    C  
ANISOU 1945  C   SER A 283    25092  17207  21029  -2127  -3204   1095  A    C  
ATOM   1946  O   SER A 283      31.038   7.760  32.200  1.00176.70      A    O  
ANISOU 1946  O   SER A 283    26506  18264  22367  -2417  -3493   1509  A    O  
ATOM   1947  CB  SER A 283      32.795  10.242  30.847  1.00131.91      A    C  
ANISOU 1947  CB  SER A 283    20435  13018  16666  -1537  -3085    927  A    C  
ATOM   1948  OG  SER A 283      31.822  11.162  30.395  1.00127.78      A    O  
ANISOU 1948  OG  SER A 283    19887  13012  15650  -1569  -2779    643  A    O  
ATOM   1949  N   CYS A 284      29.944   9.002  30.682  1.00150.96      A    N  
ANISOU 1949  N   CYS A 284    23073  15649  18634  -2211  -2918    805  A    N  
ATOM   1950  CA  CYS A 284      28.656   8.841  31.361  1.00137.61      A    C  
ANISOU 1950  CA  CYS A 284    21488  14255  16543  -2647  -2899    957  A    C  
ATOM   1951  C   CYS A 284      27.670   7.954  30.596  1.00151.02      A    C  
ANISOU 1951  C   CYS A 284    23210  15842  18331  -2814  -2813    744  A    C  
ATOM   1952  O   CYS A 284      26.533   7.771  31.031  1.00155.98      A    O  
ANISOU 1952  O   CYS A 284    23887  16722  18655  -3183  -2772    835  A    O  
ATOM   1953  CB  CYS A 284      28.011  10.205  31.633  1.00115.97      A    C  
ANISOU 1953  CB  CYS A 284    18669  12156  13240  -2677  -2659    852  A    C  
ATOM   1954  SG  CYS A 284      27.492  11.131  30.170  1.00136.32      A    S  
ANISOU 1954  SG  CYS A 284    21049  15072  15676  -2373  -2308    317  A    S  
ATOM   1955  N   SER A 285      28.104   7.425  29.454  1.00159.54      A    N  
ANISOU 1955  N   SER A 285    24247  16558  19813  -2559  -2770    442  A    N  
ATOM   1956  CA  SER A 285      27.317   6.469  28.673  1.00170.18      A    C  
ANISOU 1956  CA  SER A 285    25646  17713  21301  -2721  -2724    220  A    C  
ATOM   1957  C   SER A 285      26.012   7.038  28.121  1.00159.56      A    C  
ANISOU 1957  C   SER A 285    24215  16898  19511  -2866  -2480    -42  A    C  
ATOM   1958  O   SER A 285      25.066   6.293  27.864  1.00169.30      A    O  
ANISOU 1958  O   SER A 285    25500  18093  20732  -3154  -2483   -105  A    O  
ATOM   1959  CB  SER A 285      27.011   5.226  29.513  1.00193.10      A    C  
ANISOU 1959  CB  SER A 285    28729  20245  24395  -3104  -2996    590  A    C  
ATOM   1960  OG  SER A 285      28.205   4.597  29.943  1.00205.71      A    O  
ANISOU 1960  OG  SER A 285    30389  21283  26487  -2960  -3269    846  A    O  
ATOM   1961  N   GLU A 286      25.960   8.353  27.945  1.00137.47      A    N  
ANISOU 1961  N   GLU A 286    21277  14579  16378  -2672  -2290   -180  A    N  
ATOM   1962  CA  GLU A 286      24.800   8.988  27.333  1.00136.30      A    C  
ANISOU 1962  CA  GLU A 286    21003  14915  15870  -2747  -2081   -430  A    C  
ATOM   1963  C   GLU A 286      25.204   9.567  25.992  1.00137.11      A    C  
ANISOU 1963  C   GLU A 286    21013  15072  16011  -2400  -1923   -819  A    C  
ATOM   1964  O   GLU A 286      26.288  10.138  25.863  1.00135.94      A    O  
ANISOU 1964  O   GLU A 286    20837  14847  15967  -2082  -1897   -853  A    O  
ATOM   1965  CB  GLU A 286      24.216  10.081  28.227  1.00139.00      A    C  
ANISOU 1965  CB  GLU A 286    21248  15788  15777  -2842  -1983   -276  A    C  
ATOM   1966  CG  GLU A 286      23.096   9.607  29.138  1.00139.57      A    C  
ANISOU 1966  CG  GLU A 286    21348  16041  15642  -3300  -2010    -49  A    C  
ATOM   1967  CD  GLU A 286      23.596   9.195  30.506  1.00146.62      A    C  
ANISOU 1967  CD  GLU A 286    22409  16756  16546  -3512  -2197    373  A    C  
ATOM   1968  OE1 GLU A 286      24.592   9.786  30.974  1.00160.77      A    O  
ANISOU 1968  OE1 GLU A 286    24233  18509  18343  -3301  -2255    494  A    O  
ATOM   1969  OE2 GLU A 286      22.988   8.291  31.118  1.00139.34      A    O1-
ANISOU 1969  OE2 GLU A 286    21590  15743  15610  -3918  -2303    602  A    O1-
ATOM   1970  N   GLN A 287      24.361   9.391  24.981  1.00140.73      A    N  
ANISOU 1970  N   GLN A 287    21431  15660  16380  -2489  -1830  -1103  A    N  
ATOM   1971  CA  GLN A 287      24.691   9.942  23.676  1.00140.97      A    C  
ANISOU 1971  CA  GLN A 287    21401  15778  16382  -2219  -1687  -1460  A    C  
ATOM   1972  C   GLN A 287      24.140  11.344  23.434  1.00148.08      A    C  
ANISOU 1972  C   GLN A 287    22132  17233  16897  -2114  -1558  -1527  A    C  
ATOM   1973  O   GLN A 287      23.039  11.692  23.873  1.00 84.88      A    O  
ANISOU 1973  O   GLN A 287    14021   9583   8645  -2310  -1544  -1429  A    O  
ATOM   1974  CB  GLN A 287      24.232   9.016  22.548  1.00135.82      A    C  
ANISOU 1974  CB  GLN A 287    20824  14939  15840  -2362  -1675  -1765  A    C  
ATOM   1975  CG  GLN A 287      22.741   8.839  22.423  1.00144.42      A    C  
ANISOU 1975  CG  GLN A 287    21855  16332  16686  -2706  -1694  -1783  A    C  
ATOM   1976  CD  GLN A 287      22.379   8.069  21.176  1.00164.25      A    C  
ANISOU 1976  CD  GLN A 287    24453  18691  19264  -2838  -1685  -2126  A    C  
ATOM   1977  NE2 GLN A 287      21.164   8.276  20.684  1.00176.16      A    N  
ANISOU 1977  NE2 GLN A 287    25856  20574  20500  -3061  -1686  -2218  A    N  
ATOM   1978  OE1 GLN A 287      23.184   7.293  20.659  1.00169.53      A    O  
ANISOU 1978  OE1 GLN A 287    25273  18905  20237  -2747  -1679  -2317  A    O  
ATOM   1979  N   LEU A 288      24.945  12.152  22.756  1.00137.12      A    N  
ANISOU 1979  N   LEU A 288    20707  15900  15491  -1800  -1462  -1687  A    N  
ATOM   1980  CA  LEU A 288      24.585  13.533  22.481  1.00140.07      A    C  
ANISOU 1980  CA  LEU A 288    20937  16730  15554  -1662  -1364  -1735  A    C  
ATOM   1981  C   LEU A 288      23.446  13.652  21.481  1.00149.35      A    C  
ANISOU 1981  C   LEU A 288    22030  18192  16524  -1796  -1338  -1936  A    C  
ATOM   1982  O   LEU A 288      23.373  12.882  20.522  1.00171.42      A    O  
ANISOU 1982  O   LEU A 288    24912  20823  19396  -1890  -1346  -2159  A    O  
ATOM   1983  CB  LEU A 288      25.807  14.276  21.952  1.00140.39      A    C  
ANISOU 1983  CB  LEU A 288    20981  16716  15646  -1329  -1283  -1839  A    C  
ATOM   1984  CG  LEU A 288      26.922  14.351  22.997  1.00134.03      A    C  
ANISOU 1984  CG  LEU A 288    20211  15687  15028  -1191  -1338  -1607  A    C  
ATOM   1985  CD1 LEU A 288      28.197  14.960  22.433  1.00139.07      A    C  
ANISOU 1985  CD1 LEU A 288    20829  16241  15770   -882  -1256  -1718  A    C  
ATOM   1986  CD2 LEU A 288      26.438  15.133  24.189  1.00141.07      A    C  
ANISOU 1986  CD2 LEU A 288    21041  16866  15692  -1263  -1365  -1355  A    C  
ATOM   1987  N   ALA A 289      22.563  14.617  21.701  1.00130.12      A    N  
ANISOU 1987  N   ALA A 289    19421  16175  13844  -1810  -1313  -1866  A    N  
ATOM   1988  CA  ALA A 289      21.397  14.786  20.849  1.00114.29      A    C  
ANISOU 1988  CA  ALA A 289    17289  14468  11668  -1946  -1335  -2002  A    C  
ATOM   1989  C   ALA A 289      21.876  15.338  19.511  1.00116.60      A    C  
ANISOU 1989  C   ALA A 289    17618  14813  11871  -1761  -1309  -2218  A    C  
ATOM   1990  O   ALA A 289      22.975  15.882  19.407  1.00115.98      A    O  
ANISOU 1990  O   ALA A 289    17603  14636  11827  -1507  -1241  -2234  A    O  
ATOM   1991  CB  ALA A 289      20.328  15.687  21.444  1.00103.91      A    C  
ANISOU 1991  CB  ALA A 289    15733  13565  10183  -1981  -1313  -1873  A    C  
ATOM   1992  N   CYS A 290      21.057  15.156  18.482  1.00212.25      A    N  
ANISOU 1992  N   CYS A 290    38833  25913  15898   1614  -2728  -2695  A    N  
ATOM   1993  CA  CYS A 290      21.349  15.694  17.161  1.00152.37      A    C  
ANISOU 1993  CA  CYS A 290    30748  18245   8900   1382  -2922  -2836  A    C  
ATOM   1994  C   CYS A 290      21.150  17.205  17.182  1.00179.89      A    C  
ANISOU 1994  C   CYS A 290    33987  21777  12585   1390  -3063  -3219  A    C  
ATOM   1995  O   CYS A 290      20.214  17.699  17.810  1.00154.91      A    O  
ANISOU 1995  O   CYS A 290    30968  18736   9154   1486  -2747  -3334  A    O  
ATOM   1996  CB  CYS A 290      20.456  15.046  16.096  1.00148.06      A    C  
ANISOU 1996  CB  CYS A 290    30071  17667   8519   1083  -2419  -2638  A    C  
ATOM   1997  SG  CYS A 290      20.995  15.320  14.384  1.00180.38      A    S  
ANISOU 1997  SG  CYS A 290    33611  21629  13298    805  -2675  -2710  A    S  
ATOM   1998  N   VAL A 291      22.028  17.937  16.507  1.00175.33      A    N  
ANISOU 1998  N   VAL A 291    33054  21097  12468   1289  -3519  -3415  A    N  
ATOM   1999  CA  VAL A 291      21.849  19.377  16.366  1.00199.56      A    C  
ANISOU 1999  CA  VAL A 291    35921  24121  15780   1254  -3634  -3756  A    C  
ATOM   2000  C   VAL A 291      20.540  19.639  15.637  1.00217.70      A    C  
ANISOU 2000  C   VAL A 291    38089  26440  18188   1141  -3131  -3759  A    C  
ATOM   2001  O   VAL A 291      20.237  18.990  14.643  1.00241.93      A    O  
ANISOU 2001  O   VAL A 291    40977  29492  21453    943  -2905  -3570  A    O  
ATOM   2002  CB  VAL A 291      23.028  20.040  15.599  1.00198.79      A    C  
ANISOU 2002  CB  VAL A 291    35446  23882  16204   1072  -4156  -3926  A    C  
ATOM   2003  CG1 VAL A 291      23.343  19.288  14.310  1.00190.92      A    C  
ANISOU 2003  CG1 VAL A 291    34149  22822  15571    838  -4144  -3710  A    C  
ATOM   2004  CG2 VAL A 291      22.745  21.515  15.323  1.00196.44      A    C  
ANISOU 2004  CG2 VAL A 291    35004  23455  16181    996  -4206  -4240  A    C  
ATOM   2005  N   ASP A 292      19.745  20.565  16.156  1.00209.74      A    N  
ANISOU 2005  N   ASP A 292    37176  25494  17022   1292  -2953  -3987  A    N  
ATOM   2006  CA  ASP A 292      18.548  20.993  15.452  1.00200.73      A    C  
ANISOU 2006  CA  ASP A 292    35859  24410  15998   1251  -2535  -4055  A    C  
ATOM   2007  C   ASP A 292      18.694  22.470  15.151  1.00192.33      A    C  
ANISOU 2007  C   ASP A 292    34666  23159  15251   1296  -2800  -4376  A    C  
ATOM   2008  O   ASP A 292      18.818  23.301  16.051  1.00200.21      A    O  
ANISOU 2008  O   ASP A 292    35870  24121  16079   1488  -2972  -4611  A    O  
ATOM   2009  CB  ASP A 292      17.284  20.718  16.268  1.00206.43      A    C  
ANISOU 2009  CB  ASP A 292    36801  25414  16219   1423  -1990  -4032  A    C  
ATOM   2010  CG  ASP A 292      16.907  19.247  16.290  1.00202.79      A    C  
ANISOU 2010  CG  ASP A 292    36450  25102  15500   1280  -1593  -3682  A    C  
ATOM   2011  OD1 ASP A 292      17.382  18.494  15.413  1.00195.66      A    O  
ANISOU 2011  OD1 ASP A 292    35406  24077  14860   1050  -1670  -3474  A    O  
ATOM   2012  OD2 ASP A 292      16.130  18.842  17.181  1.00206.94      A    O1-
ANISOU 2012  OD2 ASP A 292    37218  25854  15557   1382  -1185  -3613  A    O1-
ATOM   2013  N   THR A 293      18.686  22.781  13.862  1.00177.97      A    N  
ANISOU 2013  N   THR A 293    32539  21196  13886   1110  -2827  -4376  A    N  
ATOM   2014  CA  THR A 293      18.983  24.119  13.390  1.00164.43      A    C  
ANISOU 2014  CA  THR A 293    30727  19216  12533   1094  -3103  -4624  A    C  
ATOM   2015  C   THR A 293      17.856  25.085  13.776  1.00160.34      A    C  
ANISOU 2015  C   THR A 293    30362  18738  11823   1393  -2837  -4861  A    C  
ATOM   2016  O   THR A 293      16.683  24.709  13.795  1.00155.18      A    O  
ANISOU 2016  O   THR A 293    29689  18352  10920   1535  -2368  -4813  A    O  
ATOM   2017  CB  THR A 293      19.219  24.080  11.860  1.00150.32      A    C  
ANISOU 2017  CB  THR A 293    28593  17274  11246    820  -3156  -4514  A    C  
ATOM   2018  CG2 THR A 293      19.457  25.446  11.306  1.00150.23      A    C  
ANISOU 2018  CG2 THR A 293    28536  16950  11596    785  -3386  -4729  A    C  
ATOM   2019  OG1 THR A 293      20.336  23.232  11.557  1.00135.52      A    O  
ANISOU 2019  OG1 THR A 293    26568  15380   9544    577  -3428  -4325  A    O  
ATOM   2020  N   ASN A 294      18.220  26.329  14.077  1.00162.97      A    N  
ANISOU 2020  N   ASN A 294    30839  18816  12266   1483  -3128  -5128  A    N  
ATOM   2021  CA  ASN A 294      17.271  27.299  14.620  1.00168.03      A    C  
ANISOU 2021  CA  ASN A 294    31695  19466  12684   1830  -2933  -5382  A    C  
ATOM   2022  C   ASN A 294      16.206  27.706  13.611  1.00169.64      A    C  
ANISOU 2022  C   ASN A 294    31731  19676  13048   1961  -2620  -5407  A    C  
ATOM   2023  O   ASN A 294      16.515  28.047  12.473  1.00170.40      A    O  
ANISOU 2023  O   ASN A 294    31658  19522  13566   1788  -2766  -5366  A    O  
ATOM   2024  CB  ASN A 294      18.014  28.535  15.132  1.00181.57      A    C  
ANISOU 2024  CB  ASN A 294    33649  20842  14500   1859  -3349  -5663  A    C  
ATOM   2025  CG  ASN A 294      17.129  29.448  15.966  1.00196.00      A    C  
ANISOU 2025  CG  ASN A 294    35778  22685  16008   2263  -3178  -5936  A    C  
ATOM   2026  ND2 ASN A 294      17.406  30.747  15.918  1.00199.38      A    N  
ANISOU 2026  ND2 ASN A 294    36400  22727  16627   2312  -3433  -6188  A    N  
ATOM   2027  OD1 ASN A 294      16.207  28.993  16.641  1.00201.76      A    O  
ANISOU 2027  OD1 ASN A 294    36574  23767  16318   2518  -2804  -5922  A    O  
ATOM   2028  N   GLU A 295      14.950  27.656  14.044  1.00176.42      A    N  
ANISOU 2028  N   GLU A 295    32623  20859  13549   2278  -2181  -5480  A    N  
ATOM   2029  CA  GLU A 295      13.806  27.950  13.182  1.00175.60      A    C  
ANISOU 2029  CA  GLU A 295    32315  20889  13518   2481  -1843  -5528  A    C  
ATOM   2030  C   GLU A 295      13.896  29.330  12.538  1.00167.21      A    C  
ANISOU 2030  C   GLU A 295    31353  19400  12780   2638  -2089  -5719  A    C  
ATOM   2031  O   GLU A 295      13.746  29.458  11.324  1.00164.99      A    O  
ANISOU 2031  O   GLU A 295    30873  19007  12807   2582  -2078  -5647  A    O  
ATOM   2032  CB  GLU A 295      12.501  27.823  13.968  1.00186.60      A    C  
ANISOU 2032  CB  GLU A 295    33718  22750  14434   2831  -1350  -5641  A    C  
ATOM   2033  CG  GLU A 295      12.245  26.423  14.502  1.00194.46      A    C  
ANISOU 2033  CG  GLU A 295    34632  24169  15084   2646  -1007  -5420  A    C  
ATOM   2034  CD  GLU A 295      12.260  25.369  13.410  1.00191.57      A    C  
ANISOU 2034  CD  GLU A 295    33950  23908  14931   2304   -866  -5150  A    C  
ATOM   2035  OE1 GLU A 295      11.753  25.647  12.303  1.00199.54      A    O  
ANISOU 2035  OE1 GLU A 295    34689  24938  16189   2346   -768  -5185  A    O  
ATOM   2036  OE2 GLU A 295      12.787  24.263  13.658  1.00185.30      A    O1-
ANISOU 2036  OE2 GLU A 295    33202  23163  14042   2014   -862  -4903  A    O1-
ATOM   2037  N   VAL A 296      14.127  30.359  13.349  1.00164.23      A    N  
ANISOU 2037  N   VAL A 296    31322  18769  12311   2837  -2302  -5959  A    N  
ATOM   2038  CA  VAL A 296      14.234  31.723  12.833  1.00163.60      A    C  
ANISOU 2038  CA  VAL A 296    31443  18211  12506   2982  -2531  -6137  A    C  
ATOM   2039  C   VAL A 296      15.387  31.799  11.838  1.00174.26      A    C  
ANISOU 2039  C   VAL A 296    32706  19159  14347   2528  -2894  -5991  A    C  
ATOM   2040  O   VAL A 296      15.342  32.563  10.876  1.00182.79      A    O  
ANISOU 2040  O   VAL A 296    33827  19901  15724   2557  -2973  -6006  A    O  
ATOM   2041  CB  VAL A 296      14.428  32.765  13.963  1.00170.34      A    C  
ANISOU 2041  CB  VAL A 296    32732  18825  13166   3205  -2727  -6425  A    C  
ATOM   2042  CG1 VAL A 296      15.726  32.525  14.721  1.00169.95      A    C  
ANISOU 2042  CG1 VAL A 296    32801  18653  13120   2841  -3102  -6423  A    C  
ATOM   2043  CG2 VAL A 296      14.392  34.178  13.401  1.00168.79      A    C  
ANISOU 2043  CG2 VAL A 296    32806  18107  13221   3386  -2904  -6596  A    C  
ATOM   2044  N   GLU A 297      16.421  31.000  12.079  1.00153.77      A    N  
ANISOU 2044  N   GLU A 297    29993  16615  11817   2127  -3105  -5846  A    N  
ATOM   2045  CA  GLU A 297      17.543  30.912  11.159  1.00162.72      A    C  
ANISOU 2045  CA  GLU A 297    30953  17473  13402   1671  -3414  -5699  A    C  
ATOM   2046  C   GLU A 297      17.142  30.194   9.865  1.00173.19      A    C  
ANISOU 2046  C   GLU A 297    31934  18938  14933   1560  -3200  -5459  A    C  
ATOM   2047  O   GLU A 297      17.575  30.585   8.782  1.00172.92      A    O  
ANISOU 2047  O   GLU A 297    31814  18603  15284   1346  -3349  -5387  A    O  
ATOM   2048  CB  GLU A 297      18.729  30.210  11.826  1.00153.17      A    C  
ANISOU 2048  CB  GLU A 297    29674  16358  12167   1350  -3698  -5632  A    C  
ATOM   2049  CG  GLU A 297      19.360  30.989  12.980  1.00155.91      A    C  
ANISOU 2049  CG  GLU A 297    30333  16538  12368   1382  -3999  -5895  A    C  
ATOM   2050  CD  GLU A 297      19.833  32.375  12.579  1.00160.12      A    C  
ANISOU 2050  CD  GLU A 297    31057  16563  13220   1258  -4257  -6089  A    C  
ATOM   2051  OE1 GLU A 297      19.029  33.331  12.651  1.00161.74      A    O  
ANISOU 2051  OE1 GLU A 297    31554  16565  13336   1586  -4127  -6259  A    O  
ATOM   2052  OE2 GLU A 297      21.015  32.512  12.201  1.00158.18      A    O1-
ANISOU 2052  OE2 GLU A 297    30677  16124  13301    832  -4580  -6075  A    O1-
ATOM   2053  N   THR A 298      16.306  29.160   9.976  1.00173.98      A    N  
ANISOU 2053  N   THR A 298    31850  19494  14760   1685  -2835  -5341  A    N  
ATOM   2054  CA  THR A 298      15.848  28.430   8.793  1.00169.15      A    C  
ANISOU 2054  CA  THR A 298    30908  19062  14298   1578  -2609  -5144  A    C  
ATOM   2055  C   THR A 298      15.145  29.337   7.800  1.00175.67      A    C  
ANISOU 2055  C   THR A 298    31735  19716  15298   1822  -2527  -5232  A    C  
ATOM   2056  O   THR A 298      15.487  29.360   6.619  1.00179.89      A    O  
ANISOU 2056  O   THR A 298    32120  20059  16171   1611  -2633  -5105  A    O  
ATOM   2057  CB  THR A 298      14.846  27.298   9.138  1.00176.69      A    C  
ANISOU 2057  CB  THR A 298    31698  20560  14876   1694  -2153  -5054  A    C  
ATOM   2058  CG2 THR A 298      15.471  26.242   9.995  1.00166.77      A    C  
ANISOU 2058  CG2 THR A 298    30483  19463  13420   1472  -2193  -4904  A    C  
ATOM   2059  OG1 THR A 298      13.712  27.848   9.820  1.00184.99      A    O  
ANISOU 2059  OG1 THR A 298    32873  21831  15584   2145  -1863  -5268  A    O  
ATOM   2060  N   GLN A 299      14.168  30.092   8.291  1.00172.39      A    N  
ANISOU 2060  N   GLN A 299    31499  19373  14629   2301  -2340  -5448  A    N  
ATOM   2061  CA  GLN A 299      13.388  30.980   7.441  1.00173.37      A    C  
ANISOU 2061  CA  GLN A 299    31657  19365  14849   2666  -2253  -5546  A    C  
ATOM   2062  C   GLN A 299      14.258  32.058   6.805  1.00182.63      A    C  
ANISOU 2062  C   GLN A 299    33104  19884  16403   2514  -2632  -5553  A    C  
ATOM   2063  O   GLN A 299      14.079  32.395   5.636  1.00188.49      A    O  
ANISOU 2063  O   GLN A 299    33807  20445  17366   2566  -2639  -5481  A    O  
ATOM   2064  CB  GLN A 299      12.242  31.621   8.226  1.00168.34      A    C  
ANISOU 2064  CB  GLN A 299    31168  18943  13851   3256  -2003  -5795  A    C  
ATOM   2065  CG  GLN A 299      11.302  32.475   7.374  1.00174.18      A    C  
ANISOU 2065  CG  GLN A 299    31911  19634  14638   3757  -1890  -5900  A    C  
ATOM   2066  CD  GLN A 299      10.458  31.660   6.401  1.00175.66      A    C  
ANISOU 2066  CD  GLN A 299    31609  20328  14806   3834  -1577  -5794  A    C  
ATOM   2067  NE2 GLN A 299       9.170  31.536   6.700  1.00180.63      A    N  
ANISOU 2067  NE2 GLN A 299    31982  21534  15114   4288  -1187  -5937  A    N  
ATOM   2068  OE1 GLN A 299      10.956  31.156   5.393  1.00175.90      A    O  
ANISOU 2068  OE1 GLN A 299    31465  20266  15103   3482  -1679  -5599  A    O  
ATOM   2069  N   LYS A 300      15.206  32.592   7.568  1.00177.44      A    N  
ANISOU 2069  N   LYS A 300    32727  18885  15805   2309  -2936  -5641  A    N  
ATOM   2070  CA  LYS A 300      16.070  33.649   7.053  1.00184.91      A    C  
ANISOU 2070  CA  LYS A 300    33945  19212  17098   2088  -3264  -5660  A    C  
ATOM   2071  C   LYS A 300      16.995  33.140   5.953  1.00190.32      A    C  
ANISOU 2071  C   LYS A 300    34360  19775  18179   1555  -3418  -5414  A    C  
ATOM   2072  O   LYS A 300      17.351  33.885   5.039  1.00201.04      A    O  
ANISOU 2072  O   LYS A 300    35859  20695  19833   1417  -3549  -5359  A    O  
ATOM   2073  CB  LYS A 300      16.894  34.273   8.181  1.00190.69      A    C  
ANISOU 2073  CB  LYS A 300    34983  19689  17784   1943  -3543  -5844  A    C  
ATOM   2074  CG  LYS A 300      17.621  35.543   7.769  1.00199.66      A    C  
ANISOU 2074  CG  LYS A 300    36463  20176  19223   1744  -3825  -5917  A    C  
ATOM   2075  CD  LYS A 300      16.666  36.521   7.096  1.00208.44      A    C  
ANISOU 2075  CD  LYS A 300    37883  20988  20327   2215  -3683  -5965  A    C  
ATOM   2076  CE  LYS A 300      15.594  37.004   8.063  1.00216.49      A    C  
ANISOU 2076  CE  LYS A 300    39161  22155  20942   2850  -3509  -6210  A    C  
ATOM   2077  NZ  LYS A 300      14.534  37.792   7.376  1.00215.42      A    N1+
ANISOU 2077  NZ  LYS A 300    39243  21851  20757   3424  -3344  -6245  A    N1+
ATOM   2078  N   PHE A 301      17.387  31.874   6.046  1.00194.58      A    N  
ANISOU 2078  N   PHE A 301    34535  20690  18708   1261  -3389  -5256  A    N  
ATOM   2079  CA  PHE A 301      18.175  31.254   4.991  1.00174.03      A    C  
ANISOU 2079  CA  PHE A 301    31619  18054  16451    800  -3496  -5020  A    C  
ATOM   2080  C   PHE A 301      17.304  31.044   3.751  1.00152.05      A    C  
ANISOU 2080  C   PHE A 301    28681  15368  13723    970  -3258  -4901  A    C  
ATOM   2081  O   PHE A 301      17.727  31.314   2.626  1.00138.25      A    O  
ANISOU 2081  O   PHE A 301    26893  13345  12290    741  -3359  -4774  A    O  
ATOM   2082  CB  PHE A 301      18.762  29.927   5.469  1.00168.28      A    C  
ANISOU 2082  CB  PHE A 301    30582  17703  15653    524  -3524  -4888  A    C  
ATOM   2083  CG  PHE A 301      19.812  29.362   4.558  1.00162.40      A    C  
ANISOU 2083  CG  PHE A 301    29518  16909  15276     38  -3698  -4678  A    C  
ATOM   2084  CD1 PHE A 301      19.468  28.634   3.429  1.00147.04      A    C  
ANISOU 2084  CD1 PHE A 301    27295  15120  13451    -47  -3524  -4480  A    C  
ATOM   2085  CD2 PHE A 301      21.155  29.556   4.840  1.00163.49      A    C  
ANISOU 2085  CD2 PHE A 301    29605  16887  15627   -330  -4034  -4701  A    C  
ATOM   2086  CE1 PHE A 301      20.444  28.120   2.597  1.00140.76      A    C  
ANISOU 2086  CE1 PHE A 301    26199  14295  12987   -477  -3676  -4294  A    C  
ATOM   2087  CE2 PHE A 301      22.135  29.042   4.011  1.00158.94      A    C  
ANISOU 2087  CE2 PHE A 301    28686  16324  15382   -753  -4177  -4525  A    C  
ATOM   2088  CZ  PHE A 301      21.778  28.324   2.889  1.00147.83      A    C  
ANISOU 2088  CZ  PHE A 301    27024  15048  14097   -819  -3994  -4312  A    C  
ATOM   2089  N   VAL A 302      16.085  30.559   3.976  1.00154.73      A    N  
ANISOU 2089  N   VAL A 302    28920  16137  13734   1368  -2930  -4953  A    N  
ATOM   2090  CA  VAL A 302      15.100  30.380   2.912  1.00160.77      A    C  
ANISOU 2090  CA  VAL A 302    29366  17153  14565   1598  -2644  -4824  A    C  
ATOM   2091  C   VAL A 302      14.779  31.695   2.212  1.00169.74      A    C  
ANISOU 2091  C   VAL A 302    30808  17868  15816   1919  -2719  -4903  A    C  
ATOM   2092  O   VAL A 302      14.812  31.776   0.987  1.00169.31      A    O  
ANISOU 2092  O   VAL A 302    30530  17736  16064   1826  -2699  -4681  A    O  
ATOM   2093  CB  VAL A 302      13.790  29.763   3.451  1.00159.73      A    C  
ANISOU 2093  CB  VAL A 302    28982  17637  14070   1974  -2236  -4889  A    C  
ATOM   2094  CG1 VAL A 302      12.710  29.762   2.375  1.00154.65      A    C  
ANISOU 2094  CG1 VAL A 302    27913  17314  13533   2256  -1956  -4782  A    C  
ATOM   2095  CG2 VAL A 302      14.039  28.356   3.973  1.00161.84      A    C  
ANISOU 2095  CG2 VAL A 302    28964  18294  14234   1629  -2103  -4739  A    C  
ATOM   2096  N   ASP A 303      14.482  32.724   2.997  1.00170.72      A    N  
ANISOU 2096  N   ASP A 303    31451  17714  15701   2307  -2796  -5193  A    N  
ATOM   2097  CA  ASP A 303      14.159  34.038   2.452  1.00177.94      A    C  
ANISOU 2097  CA  ASP A 303    32761  18160  16688   2675  -2868  -5270  A    C  
ATOM   2098  C   ASP A 303      15.307  34.591   1.615  1.00192.65      A    C  
ANISOU 2098  C   ASP A 303    34835  19408  18956   2194  -3151  -5109  A    C  
ATOM   2099  O   ASP A 303      15.081  35.214   0.576  1.00188.96      A    O  
ANISOU 2099  O   ASP A 303    34547  18632  18616   2362  -3154  -5022  A    O  
ATOM   2100  CB  ASP A 303      13.811  35.020   3.578  1.00191.19      A    C  
ANISOU 2100  CB  ASP A 303    34840  19663  18142   3076  -2890  -5517  A    C  
ATOM   2101  CG  ASP A 303      12.492  34.692   4.255  1.00182.77      A    C  
ANISOU 2101  CG  ASP A 303    33577  19202  16666   3649  -2556  -5686  A    C  
ATOM   2102  OD1 ASP A 303      12.021  33.542   4.123  1.00177.51      A    O  
ANISOU 2102  OD1 ASP A 303    32441  19130  15876   3596  -2311  -5612  A    O  
ATOM   2103  OD2 ASP A 303      11.928  35.584   4.923  1.00153.63      A    O1-
ANISOU 2103  OD2 ASP A 303    30193  15407  12772   4133  -2524  -5893  A    O1-
ATOM   2104  N   SER A 304      16.535  34.355   2.066  1.00203.30      A    N  
ANISOU 2104  N   SER A 304    36125  20622  20499   1604  -3370  -5055  A    N  
ATOM   2105  CA  SER A 304      17.713  34.867   1.375  1.00208.11      A    C  
ANISOU 2105  CA  SER A 304    36853  20724  21497   1070  -3610  -4916  A    C  
ATOM   2106  C   SER A 304      17.862  34.279  -0.029  1.00190.88      A    C  
ANISOU 2106  C   SER A 304    34391  18594  19543    825  -3556  -4666  A    C  
ATOM   2107  O   SER A 304      18.054  35.014  -0.997  1.00192.60      A    O  
ANISOU 2107  O   SER A 304    34828  18379  19973    750  -3593  -4537  A    O  
ATOM   2108  CB  SER A 304      18.973  34.583   2.196  1.00223.05      A    C  
ANISOU 2108  CB  SER A 304    38595  22636  23518    526  -3839  -4944  A    C  
ATOM   2109  OG  SER A 304      20.117  35.168   1.598  1.00235.84      A    O  
ANISOU 2109  OG  SER A 304    40285  23820  25504     -6  -4043  -4848  A    O  
ATOM   2110  N   LEU A 305      17.768  32.958  -0.140  1.00185.43      A    N  
ANISOU 2110  N   LEU A 305    33083  18504  18869    691  -3399  -4492  A    N  
ATOM   2111  CA  LEU A 305      17.896  32.300  -1.439  1.00153.84      A    C  
ANISOU 2111  CA  LEU A 305    28560  14725  15166    452  -3265  -4142  A    C  
ATOM   2112  C   LEU A 305      16.721  32.614  -2.368  1.00147.09      A    C  
ANISOU 2112  C   LEU A 305    27622  13994  14273    946  -3024  -4026  A    C  
ATOM   2113  O   LEU A 305      16.909  32.842  -3.563  1.00124.43      A    O  
ANISOU 2113  O   LEU A 305    24675  10965  11639    831  -3009  -3794  A    O  
ATOM   2114  CB  LEU A 305      18.065  30.784  -1.248  1.00148.56      A    C  
ANISOU 2114  CB  LEU A 305    27306  14637  14503    208  -3156  -4008  A    C  
ATOM   2115  CG  LEU A 305      17.024  29.923  -0.521  1.00134.77      A    C  
ANISOU 2115  CG  LEU A 305    25324  13453  12431    539  -2892  -4077  A    C  
ATOM   2116  CD1 LEU A 305      15.858  29.526  -1.411  1.00127.58      A    C  
ANISOU 2116  CD1 LEU A 305    23995  12962  11518    832  -2565  -3929  A    C  
ATOM   2117  CD2 LEU A 305      17.685  28.675   0.061  1.00127.28      A    C  
ANISOU 2117  CD2 LEU A 305    24102  12798  11459    184  -2924  -4006  A    C  
ATOM   2118  N   VAL A 306      15.519  32.662  -1.803  1.00159.99      A    N  
ANISOU 2118  N   VAL A 306    29275  15931  15581   1518  -2842  -4203  A    N  
ATOM   2119  CA  VAL A 306      14.311  32.976  -2.559  1.00166.04      A    C  
ANISOU 2119  CA  VAL A 306    29922  16910  16254   2081  -2637  -4156  A    C  
ATOM   2120  C   VAL A 306      14.367  34.360  -3.208  1.00185.37      A    C  
ANISOU 2120  C   VAL A 306    32954  18708  18770   2330  -2779  -4143  A    C  
ATOM   2121  O   VAL A 306      13.941  34.535  -4.349  1.00193.29      A    O  
ANISOU 2121  O   VAL A 306    33827  19756  19859   2540  -2696  -3944  A    O  
ATOM   2122  CB  VAL A 306      13.050  32.880  -1.657  1.00141.05      A    C  
ANISOU 2122  CB  VAL A 306    26689  14210  12694   2665  -2421  -4416  A    C  
ATOM   2123  CG1 VAL A 306      11.849  33.544  -2.312  1.00140.65      A    C  
ANISOU 2123  CG1 VAL A 306    26635  14296  12509   3362  -2286  -4455  A    C  
ATOM   2124  CG2 VAL A 306      12.744  31.430  -1.316  1.00126.83      A    C  
ANISOU 2124  CG2 VAL A 306    24258  13110  10821   2443  -2183  -4355  A    C  
ATOM   2125  N   ALA A 307      14.903  35.338  -2.484  1.00200.46      A    N  
ANISOU 2125  N   ALA A 307    35545  19996  20624   2300  -2997  -4357  A    N  
ATOM   2126  CA  ALA A 307      14.989  36.708  -2.990  1.00219.59      A    C  
ANISOU 2126  CA  ALA A 307    38660  21685  23087   2510  -3128  -4362  A    C  
ATOM   2127  C   ALA A 307      15.848  36.811  -4.248  1.00226.75      A    C  
ANISOU 2127  C   ALA A 307    39542  22262  24351   2004  -3188  -4019  A    C  
ATOM   2128  O   ALA A 307      15.512  37.541  -5.183  1.00230.93      A    O  
ANISOU 2128  O   ALA A 307    40368  22478  24898   2301  -3156  -3862  A    O  
ATOM   2129  CB  ALA A 307      15.529  37.627  -1.911  1.00229.93      A    C  
ANISOU 2129  CB  ALA A 307    40703  22373  24287   2439  -3360  -4685  A    C  
ATOM   2130  N   LEU A 308      16.961  36.085  -4.261  1.00230.14      A    N  
ANISOU 2130  N   LEU A 308    39631  22775  25036   1271  -3271  -3905  A    N  
ATOM   2131  CA  LEU A 308      17.856  36.068  -5.414  1.00228.45      A    C  
ANISOU 2131  CA  LEU A 308    39307  22338  25157    734  -3296  -3590  A    C  
ATOM   2132  C   LEU A 308      17.231  35.314  -6.583  1.00217.86      A    C  
ANISOU 2132  C   LEU A 308    37382  21529  23864    921  -3073  -3292  A    C  
ATOM   2133  O   LEU A 308      17.635  35.476  -7.735  1.00219.33      A    O  
ANISOU 2133  O   LEU A 308    37557  21536  24242    696  -3042  -3010  A    O  
ATOM   2134  CB  LEU A 308      19.201  35.441  -5.049  1.00230.07      A    C  
ANISOU 2134  CB  LEU A 308    39232  22586  25598    -43  -3450  -3592  A    C  
ATOM   2135  CG  LEU A 308      20.333  35.702  -6.046  1.00230.59      A    C  
ANISOU 2135  CG  LEU A 308    39310  22301  26003   -675  -3505  -3346  A    C  
ATOM   2136  CD1 LEU A 308      20.563  37.198  -6.190  1.00233.16      A    C  
ANISOU 2136  CD1 LEU A 308    40473  21776  26343   -709  -3607  -3403  A    C  
ATOM   2137  CD2 LEU A 308      21.611  34.997  -5.622  1.00230.10      A    C  
ANISOU 2137  CD2 LEU A 308    38862  22417  26150  -1366  -3664  -3392  A    C  
ATOM   2138  N   ALA A 309      16.242  34.484  -6.274  1.00194.59      A    N  
ANISOU 2138  N   ALA A 309    33957  19253  20726   1311  -2909  -3367  A    N  
ATOM   2139  CA  ALA A 309      15.587  33.658  -7.276  1.00170.64      A    C  
ANISOU 2139  CA  ALA A 309    30314  16804  17719   1463  -2707  -3149  A    C  
ATOM   2140  C   ALA A 309      14.627  34.446  -8.159  1.00160.99      A    C  
ANISOU 2140  C   ALA A 309    29309  15505  16356   2098  -2639  -3068  A    C  
ATOM   2141  O   ALA A 309      14.659  34.315  -9.379  1.00169.38      A    O  
ANISOU 2141  O   ALA A 309    30181  16643  17533   2048  -2584  -2799  A    O  
ATOM   2142  CB  ALA A 309      14.849  32.524  -6.598  1.00169.30      A    C  
ANISOU 2142  CB  ALA A 309    29582  17358  17386   1602  -2540  -3283  A    C  
ATOM   2143  N   MET A 310      13.786  35.272  -7.545  1.00151.16      A    N  
ANISOU 2143  N   MET A 310    28480  14117  14837   2734  -2653  -3306  A    N  
ATOM   2144  CA  MET A 310      12.840  36.102  -8.289  1.00177.74      A    C  
ANISOU 2144  CA  MET A 310    32114  17397  18021   3460  -2623  -3261  A    C  
ATOM   2145  C   MET A 310      13.517  37.072  -9.272  1.00186.67      A    C  
ANISOU 2145  C   MET A 310    33857  17775  19292   3323  -2736  -2997  A    C  
ATOM   2146  O   MET A 310      12.887  37.539 -10.228  1.00185.27      A    O  
ANISOU 2146  O   MET A 310    33815  17580  18998   3833  -2706  -2840  A    O  
ATOM   2147  CB  MET A 310      11.950  36.875  -7.311  1.00189.34      A    C  
ANISOU 2147  CB  MET A 310    33993  18783  19163   4173  -2635  -3604  A    C  
ATOM   2148  CG  MET A 310      11.068  35.981  -6.444  1.00187.84      A    C  
ANISOU 2148  CG  MET A 310    33192  19410  18771   4404  -2457  -3852  A    C  
ATOM   2149  SD  MET A 310       9.930  34.970  -7.421  1.00193.49      A    S  
ANISOU 2149  SD  MET A 310    32966  21122  19430   4697  -2227  -3735  A    S  
ATOM   2150  CE  MET A 310       9.040  34.104  -6.132  1.00136.02      A    C  
ANISOU 2150  CE  MET A 310    25146  14633  11902   4842  -1993  -4067  A    C  
ATOM   2151  N   ASP A 311      14.790  37.380  -9.035  1.00185.46      A    N  
ANISOU 2151  N   ASP A 311    34077  17022  19369   2638  -2863  -2952  A    N  
ATOM   2152  CA  ASP A 311      15.541  38.243  -9.945  1.00185.22      A    C  
ANISOU 2152  CA  ASP A 311    34616  16271  19489   2358  -2926  -2687  A    C  
ATOM   2153  C   ASP A 311      16.455  37.445 -10.874  1.00176.60      A    C  
ANISOU 2153  C   ASP A 311    33021  15388  18692   1651  -2860  -2372  A    C  
ATOM   2154  O   ASP A 311      16.891  36.343 -10.541  1.00173.97      A    O  
ANISOU 2154  O   ASP A 311    32047  15548  18506   1207  -2836  -2409  A    O  
ATOM   2155  CB  ASP A 311      16.365  39.264  -9.165  1.00195.08      A    C  
ANISOU 2155  CB  ASP A 311    36662  16663  20797   2025  -3098  -2862  A    C  
ATOM   2156  CG  ASP A 311      16.493  40.584  -9.899  1.00206.44      A    C  
ANISOU 2156  CG  ASP A 311    38994  17238  22204   2168  -3132  -2686  A    C  
ATOM   2157  OD1 ASP A 311      16.556  40.564 -11.148  1.00205.43      A    O  
ANISOU 2157  OD1 ASP A 311    38806  17110  22138   2128  -3032  -2328  A    O  
ATOM   2158  OD2 ASP A 311      16.522  41.640  -9.230  1.00211.94      A    O1-
ANISOU 2158  OD2 ASP A 311    40498  17237  22792   2329  -3253  -2905  A    O1-
ATOM   2159  N   ASN A 322      11.765  33.746 -10.501  1.00183.40      A    N  
ANISOU 2159  N   ASN A 322    31084  19749  18851   3410  -2280  -2855  A    N  
ATOM   2160  CA  ASN A 322      10.774  34.178 -11.478  1.00189.56      A    C  
ANISOU 2160  CA  ASN A 322    31819  20760  19445   4085  -2260  -2788  A    C  
ATOM   2161  C   ASN A 322       9.424  33.507 -11.251  1.00213.32      A    C  
ANISOU 2161  C   ASN A 322    34152  24668  22232   4553  -2101  -3021  A    C  
ATOM   2162  O   ASN A 322       9.198  32.885 -10.213  1.00213.05      A    O  
ANISOU 2162  O   ASN A 322    33819  24977  22151   4408  -1985  -3242  A    O  
ATOM   2163  CB  ASN A 322      11.271  33.895 -12.898  1.00167.96      A    C  
ANISOU 2163  CB  ASN A 322    28922  18018  16878   3787  -2267  -2441  A    C  
ATOM   2164  CG  ASN A 322      12.442  34.776 -13.294  1.00157.27      A    C  
ANISOU 2164  CG  ASN A 322    28283  15782  15690   3428  -2389  -2198  A    C  
ATOM   2165  ND2 ASN A 322      13.650  34.357 -12.933  1.00136.98      A    N  
ANISOU 2165  ND2 ASN A 322    25684  12968  13393   2645  -2409  -2141  A    N  
ATOM   2166  OD1 ASN A 322      12.261  35.824 -13.917  1.00166.43      A    O  
ANISOU 2166  OD1 ASN A 322    30021  16492  16723   3851  -2460  -2066  A    O  
ATOM   2167  N   VAL A 323       8.526  33.649 -12.223  1.00232.59      A    N  
ANISOU 2167  N   VAL A 323    36354  27504  24515   5109  -2093  -2976  A    N  
ATOM   2168  CA  VAL A 323       7.212  33.015 -12.160  1.00229.52      A    C  
ANISOU 2168  CA  VAL A 323    35230  28054  23922   5528  -1944  -3213  A    C  
ATOM   2169  C   VAL A 323       7.370  31.495 -12.207  1.00218.08      A    C  
ANISOU 2169  C   VAL A 323    33018  27188  22654   4833  -1776  -3193  A    C  
ATOM   2170  O   VAL A 323       6.528  30.755 -11.695  1.00226.98      A    O  
ANISOU 2170  O   VAL A 323    33557  29019  23668   4880  -1592  -3429  A    O  
ATOM   2171  CB  VAL A 323       6.287  33.502 -13.304  1.00230.62      A    C  
ANISOU 2171  CB  VAL A 323    35259  28519  23848   6278  -2023  -3169  A    C  
ATOM   2172  CG1 VAL A 323       6.831  33.080 -14.664  1.00225.61      A    C  
ANISOU 2172  CG1 VAL A 323    34470  27876  23376   5912  -2077  -2840  A    C  
ATOM   2173  CG2 VAL A 323       4.861  32.998 -13.104  1.00232.75      A    C  
ANISOU 2173  CG2 VAL A 323    34756  29798  23879   6768  -1883  -3491  A    C  
ATOM   2174  N   VAL A 324       8.461  31.038 -12.815  1.00199.57      A    N  
ANISOU 2174  N   VAL A 324    30710  24537  20582   4184  -1822  -2917  A    N  
ATOM   2175  CA  VAL A 324       8.787  29.619 -12.852  1.00174.74      A    C  
ANISOU 2175  CA  VAL A 324    26970  21800  17622   3511  -1683  -2880  A    C  
ATOM   2176  C   VAL A 324       9.100  29.121 -11.441  1.00168.66      A    C  
ANISOU 2176  C   VAL A 324    26215  20983  16885   3141  -1583  -3039  A    C  
ATOM   2177  O   VAL A 324       8.771  27.990 -11.077  1.00160.71      A    O  
ANISOU 2177  O   VAL A 324    24685  20497  15880   2841  -1397  -3140  A    O  
ATOM   2178  CB  VAL A 324       9.977  29.335 -13.797  1.00159.29      A    C  
ANISOU 2178  CB  VAL A 324    25107  19482  15935   2958  -1764  -2556  A    C  
ATOM   2179  CG1 VAL A 324       9.543  29.485 -15.245  1.00155.07      A    C  
ANISOU 2179  CG1 VAL A 324    24406  19188  15325   3272  -1811  -2406  A    C  
ATOM   2180  CG2 VAL A 324      11.150  30.262 -13.492  1.00153.48      A    C  
ANISOU 2180  CG2 VAL A 324    25107  17874  15334   2744  -1918  -2410  A    C  
ATOM   2181  N   PHE A 325       9.757  29.973 -10.661  1.00172.12      A    N  
ANISOU 2181  N   PHE A 325    27296  20770  17331   3147  -1711  -3058  A    N  
ATOM   2182  CA  PHE A 325      10.062  29.664  -9.275  1.00167.46      A    C  
ANISOU 2182  CA  PHE A 325    26816  20099  16711   2885  -1659  -3223  A    C  
ATOM   2183  C   PHE A 325       8.823  29.812  -8.393  1.00168.72      A    C  
ANISOU 2183  C   PHE A 325    26839  20713  16555   3419  -1502  -3536  A    C  
ATOM   2184  O   PHE A 325       8.651  29.076  -7.422  1.00161.97      A    O  
ANISOU 2184  O   PHE A 325    25767  20161  15614   3201  -1336  -3678  A    O  
ATOM   2185  CB  PHE A 325      11.189  30.553  -8.763  1.00168.51      A    C  
ANISOU 2185  CB  PHE A 325    27670  19411  16947   2697  -1876  -3178  A    C  
ATOM   2186  CG  PHE A 325      11.514  30.327  -7.324  1.00167.57      A    C  
ANISOU 2186  CG  PHE A 325    27714  19205  16751   2489  -1868  -3367  A    C  
ATOM   2187  CD1 PHE A 325      12.127  29.152  -6.919  1.00155.42      A    C  
ANISOU 2187  CD1 PHE A 325    25866  17856  15332   1912  -1807  -3309  A    C  
ATOM   2188  CD2 PHE A 325      11.213  31.286  -6.376  1.00180.76      A    C  
ANISOU 2188  CD2 PHE A 325    29888  20594  18200   2906  -1931  -3607  A    C  
ATOM   2189  CE1 PHE A 325      12.425  28.934  -5.598  1.00159.89      A    C  
ANISOU 2189  CE1 PHE A 325    26615  18355  15780   1761  -1814  -3468  A    C  
ATOM   2190  CE2 PHE A 325      11.509  31.074  -5.054  1.00186.53      A    C  
ANISOU 2190  CE2 PHE A 325    30785  21270  18817   2733  -1932  -3788  A    C  
ATOM   2191  CZ  PHE A 325      12.119  29.895  -4.662  1.00179.62      A    C  
ANISOU 2191  CZ  PHE A 325    29596  20607  18047   2160  -1878  -3709  A    C  
ATOM   2192  N   SER A 326       7.973  30.779  -8.729  1.00175.80      A    N  
ANISOU 2192  N   SER A 326    27886  21656  17256   4142  -1547  -3641  A    N  
ATOM   2193  CA  SER A 326       6.683  30.940  -8.065  1.00192.61      A    C  
ANISOU 2193  CA  SER A 326    29780  24337  19067   4742  -1382  -3957  A    C  
ATOM   2194  C   SER A 326       5.848  29.675  -8.244  1.00199.63      A    C  
ANISOU 2194  C   SER A 326    29789  26141  19920   4549  -1115  -4039  A    C  
ATOM   2195  O   SER A 326       5.114  29.271  -7.341  1.00200.42      A    O  
ANISOU 2195  O   SER A 326    29589  26740  19822   4625   -883  -4280  A    O  
ATOM   2196  CB  SER A 326       5.936  32.160  -8.614  1.00198.27      A    C  
ANISOU 2196  CB  SER A 326    30773  24976  19585   5615  -1507  -4031  A    C  
ATOM   2197  OG  SER A 326       4.579  32.164  -8.205  1.00195.48      A    O  
ANISOU 2197  OG  SER A 326    29989  25357  18929   6227  -1330  -4344  A    O  
ATOM   2198  N   GLU A 327       5.966  29.059  -9.418  1.00207.05      A    N  
ANISOU 2198  N   GLU A 327    30338  27292  21040   4273  -1137  -3846  A    N  
ATOM   2199  CA  GLU A 327       5.326  27.775  -9.679  1.00200.89      A    C  
ANISOU 2199  CA  GLU A 327    28762  27296  20272   3949   -901  -3915  A    C  
ATOM   2200  C   GLU A 327       5.892  26.709  -8.750  1.00187.19      A    C  
ANISOU 2200  C   GLU A 327    26967  25526  18631   3244   -726  -3895  A    C  
ATOM   2201  O   GLU A 327       5.149  25.905  -8.192  1.00184.27      A    O  
ANISOU 2201  O   GLU A 327    26139  25743  18133   3098   -446  -4071  A    O  
ATOM   2202  CB  GLU A 327       5.506  27.351 -11.142  1.00204.64      A    C  
ANISOU 2202  CB  GLU A 327    28931  27900  20923   3761   -996  -3709  A    C  
ATOM   2203  CG  GLU A 327       4.648  28.124 -12.136  1.00206.10      A    C  
ANISOU 2203  CG  GLU A 327    28986  28382  20940   4490  -1125  -3760  A    C  
ATOM   2204  CD  GLU A 327       4.691  27.531 -13.534  1.00200.38      A    C  
ANISOU 2204  CD  GLU A 327    27866  27936  20334   4287  -1187  -3601  A    C  
ATOM   2205  OE1 GLU A 327       5.602  26.722 -13.817  1.00191.52      A    O  
ANISOU 2205  OE1 GLU A 327    26724  26588  19458   3602  -1169  -3404  A    O  
ATOM   2206  OE2 GLU A 327       3.811  27.877 -14.350  1.00204.45      A    O1-
ANISOU 2206  OE2 GLU A 327    28093  28917  20672   4850  -1266  -3689  A    O1-
ATOM   2207  N   PHE A 328       7.210  26.729  -8.569  1.00176.25      A    N  
ANISOU 2207  N   PHE A 328    26063  23454  17450   2819   -887  -3684  A    N  
ATOM   2208  CA  PHE A 328       7.891  25.752  -7.726  1.00162.94      A    C  
ANISOU 2208  CA  PHE A 328    24399  21669  15842   2204   -780  -3635  A    C  
ATOM   2209  C   PHE A 328       7.467  25.846  -6.262  1.00162.12      A    C  
ANISOU 2209  C   PHE A 328    24458  21670  15470   2350   -620  -3861  A    C  
ATOM   2210  O   PHE A 328       7.236  24.823  -5.616  1.00158.21      A    O  
ANISOU 2210  O   PHE A 328    23706  21513  14893   2003   -371  -3909  A    O  
ATOM   2211  CB  PHE A 328       9.402  25.926  -7.829  1.00150.57      A    C  
ANISOU 2211  CB  PHE A 328    23305  19380  14526   1820  -1032  -3400  A    C  
ATOM   2212  CG  PHE A 328      10.179  24.808  -7.208  1.00146.68      A    C  
ANISOU 2212  CG  PHE A 328    22780  18823  14129   1218   -966  -3315  A    C  
ATOM   2213  CD1 PHE A 328       9.659  23.524  -7.163  1.00145.91      A    C  
ANISOU 2213  CD1 PHE A 328    22207  19236  13996    918   -699  -3337  A    C  
ATOM   2214  CD2 PHE A 328      11.417  25.041  -6.647  1.00146.75      A    C  
ANISOU 2214  CD2 PHE A 328    23250  18262  14245    960  -1176  -3227  A    C  
ATOM   2215  CE1 PHE A 328      10.371  22.491  -6.585  1.00137.35      A    C  
ANISOU 2215  CE1 PHE A 328    21176  18042  12970    419   -641  -3241  A    C  
ATOM   2216  CE2 PHE A 328      12.134  24.013  -6.068  1.00144.21      A    C  
ANISOU 2216  CE2 PHE A 328    22912  17903  13978    490  -1144  -3151  A    C  
ATOM   2217  CZ  PHE A 328      11.609  22.735  -6.037  1.00134.65      A    C  
ANISOU 2217  CZ  PHE A 328    21292  17154  12716    245   -875  -3143  A    C  
ATOM   2218  N   GLN A 329       7.381  27.067  -5.739  1.00165.95      A    N  
ANISOU 2218  N   GLN A 329    25417  21837  15798   2859   -753  -3995  A    N  
ATOM   2219  CA  GLN A 329       6.941  27.281  -4.362  1.00178.40      A    C  
ANISOU 2219  CA  GLN A 329    27188  23520  17074   3084   -608  -4238  A    C  
ATOM   2220  C   GLN A 329       5.554  26.691  -4.154  1.00192.34      A    C  
ANISOU 2220  C   GLN A 329    28323  26152  18604   3261   -241  -4449  A    C  
ATOM   2221  O   GLN A 329       5.313  25.947  -3.200  1.00193.74      A    O  
ANISOU 2221  O   GLN A 329    28377  26621  18614   2999     26  -4534  A    O  
ATOM   2222  CB  GLN A 329       6.928  28.771  -4.013  1.00183.31      A    C  
ANISOU 2222  CB  GLN A 329    28414  23683  17553   3697   -815  -4387  A    C  
ATOM   2223  CG  GLN A 329       8.290  29.442  -3.923  1.00171.04      A    C  
ANISOU 2223  CG  GLN A 329    27550  21252  16187   3468  -1150  -4249  A    C  
ATOM   2224  CD  GLN A 329       8.177  30.951  -3.800  1.00171.17      A    C  
ANISOU 2224  CD  GLN A 329    28184  20775  16076   4079  -1346  -4394  A    C  
ATOM   2225  NE2 GLN A 329       9.081  31.555  -3.039  1.00183.81      A    N  
ANISOU 2225  NE2 GLN A 329    30431  21726  17684   3935  -1554  -4447  A    N  
ATOM   2226  OE1 GLN A 329       7.258  31.560  -4.346  1.00163.30      A    O  
ANISOU 2226  OE1 GLN A 329    27097  19995  14954   4696  -1315  -4482  A    O  
ATOM   2227  N   ASP A 330       4.649  27.040  -5.061  1.00207.27      A    N  
ANISOU 2227  N   ASP A 330    29819  28468  20466   3706   -228  -4533  A    N  
ATOM   2228  CA  ASP A 330       3.283  26.541  -5.037  1.00205.81      A    C  
ANISOU 2228  CA  ASP A 330    28924  29198  20078   3884     99  -4767  A    C  
ATOM   2229  C   ASP A 330       3.279  25.029  -5.231  1.00198.40      A    C  
ANISOU 2229  C   ASP A 330    27465  28646  19272   3130    345  -4666  A    C  
ATOM   2230  O   ASP A 330       2.508  24.314  -4.595  1.00197.78      A    O  
ANISOU 2230  O   ASP A 330    26985  29152  19011   2947    705  -4831  A    O  
ATOM   2231  CB  ASP A 330       2.439  27.222  -6.115  1.00210.90      A    C  
ANISOU 2231  CB  ASP A 330    29243  30209  20682   4526    -16  -4865  A    C  
ATOM   2232  CG  ASP A 330       2.409  28.733  -5.971  1.00213.97      A    C  
ANISOU 2232  CG  ASP A 330    30225  30153  20919   5324   -257  -4956  A    C  
ATOM   2233  OD1 ASP A 330       2.649  29.238  -4.853  1.00213.13      A    O  
ANISOU 2233  OD1 ASP A 330    30625  29696  20658   5467   -245  -5067  A    O  
ATOM   2234  OD2 ASP A 330       2.143  29.418  -6.982  1.00214.80      A    O1-
ANISOU 2234  OD2 ASP A 330    30332  30242  21040   5824   -463  -4919  A    O1-
ATOM   2235  N   TRP A 331       4.148  24.555  -6.120  1.00190.62      A    N  
ANISOU 2235  N   TRP A 331    26517  27315  18593   2689    165  -4398  A    N  
ATOM   2236  CA  TRP A 331       4.216  23.139  -6.469  1.00179.33      A    C  
ANISOU 2236  CA  TRP A 331    24661  26163  17312   2000    357  -4296  A    C  
ATOM   2237  C   TRP A 331       4.582  22.243  -5.296  1.00163.59      A    C  
ANISOU 2237  C   TRP A 331    22854  24062  15240   1480    591  -4255  A    C  
ATOM   2238  O   TRP A 331       3.952  21.211  -5.071  1.00154.93      A    O  
ANISOU 2238  O   TRP A 331    21343  23460  14063   1099    933  -4331  A    O  
ATOM   2239  CB  TRP A 331       5.248  22.923  -7.581  1.00173.60      A    C  
ANISOU 2239  CB  TRP A 331    24059  24987  16914   1694     87  -4013  A    C  
ATOM   2240  CG  TRP A 331       5.307  21.515  -8.078  1.00176.19      A    C  
ANISOU 2240  CG  TRP A 331    23981  25570  17395   1055    256  -3928  A    C  
ATOM   2241  CD1 TRP A 331       4.560  20.960  -9.079  1.00184.26      A    C  
ANISOU 2241  CD1 TRP A 331    24394  27157  18460    966    349  -4013  A    C  
ATOM   2242  CD2 TRP A 331       6.116  20.463  -7.558  1.00169.91      A    C  
ANISOU 2242  CD2 TRP A 331    23383  24477  16698    436    352  -3769  A    C  
ATOM   2243  CE2 TRP A 331       5.844  19.299  -8.294  1.00174.98      A    C  
ANISOU 2243  CE2 TRP A 331    23570  25458  17455    -18    512  -3755  A    C  
ATOM   2244  CE3 TRP A 331       7.070  20.387  -6.531  1.00162.63      A    C  
ANISOU 2244  CE3 TRP A 331    23005  23027  15761    244    297  -3647  A    C  
ATOM   2245  NE1 TRP A 331       4.883  19.634  -9.232  1.00186.70      A    N  
ANISOU 2245  NE1 TRP A 331    24545  27484  18908    295    503  -3919  A    N  
ATOM   2246  CZ2 TRP A 331       6.466  18.083  -8.057  1.00168.27      A    C  
ANISOU 2246  CZ2 TRP A 331    22831  24398  16705   -622    634  -3611  A    C  
ATOM   2247  CZ3 TRP A 331       7.692  19.183  -6.289  1.00159.07      A    C  
ANISOU 2247  CZ3 TRP A 331    22629  22413  15395   -322    400  -3496  A    C  
ATOM   2248  CH2 TRP A 331       7.390  18.047  -7.047  1.00159.15      A    C  
ANISOU 2248  CH2 TRP A 331    22223  22724  15520   -738    574  -3471  A    C  
ATOM   2249  N   LEU A 332       5.593  22.652  -4.541  1.00156.36      A    N  
ANISOU 2249  N   LEU A 332    22582  22499  14327   1463    405  -4142  A    N  
ATOM   2250  CA  LEU A 332       6.116  21.826  -3.465  1.00149.48      A    C  
ANISOU 2250  CA  LEU A 332    21981  21449  13366   1011    556  -4063  A    C  
ATOM   2251  C   LEU A 332       5.071  21.695  -2.346  1.00156.33      A    C  
ANISOU 2251  C   LEU A 332    22716  22825  13859   1142    941  -4296  A    C  
ATOM   2252  O   LEU A 332       4.874  20.610  -1.796  1.00154.85      A    O  
ANISOU 2252  O   LEU A 332    22414  22862  13559    685   1260  -4262  A    O  
ATOM   2253  CB  LEU A 332       7.438  22.426  -2.952  1.00142.68      A    C  
ANISOU 2253  CB  LEU A 332    21808  19829  12576   1027    210  -3932  A    C  
ATOM   2254  CG  LEU A 332       8.369  21.730  -1.939  1.00134.21      A    C  
ANISOU 2254  CG  LEU A 332    21144  18411  11440    625    200  -3805  A    C  
ATOM   2255  CD1 LEU A 332       9.819  22.087  -2.237  1.00118.72      A    C  
ANISOU 2255  CD1 LEU A 332    19578  15790   9742    495   -220  -3624  A    C  
ATOM   2256  CD2 LEU A 332       8.051  22.000  -0.469  1.00142.76      A    C  
ANISOU 2256  CD2 LEU A 332    22559  19549  12134    830    349  -3975  A    C  
ATOM   2257  N   GLU A 333       4.391  22.795  -2.030  1.00162.61      A    N  
ANISOU 2257  N   GLU A 333    23543  23798  14443   1775    928  -4531  A    N  
ATOM   2258  CA  GLU A 333       3.366  22.793  -0.988  1.00168.10      A    C  
ANISOU 2258  CA  GLU A 333    24086  25030  14756   1978   1305  -4784  A    C  
ATOM   2259  C   GLU A 333       2.255  21.799  -1.318  1.00179.97      A    C  
ANISOU 2259  C   GLU A 333    24825  27345  16212   1662   1729  -4887  A    C  
ATOM   2260  O   GLU A 333       1.774  21.086  -0.435  1.00188.75      A    O  
ANISOU 2260  O   GLU A 333    25834  28804  17080   1363   2136  -4953  A    O  
ATOM   2261  CB  GLU A 333       2.791  24.198  -0.783  1.00168.75      A    C  
ANISOU 2261  CB  GLU A 333    24293  25187  14638   2802   1192  -5043  A    C  
ATOM   2262  CG  GLU A 333       3.606  25.078   0.171  1.00172.34      A    C  
ANISOU 2262  CG  GLU A 333    25553  24968  14960   3067    945  -5059  A    C  
ATOM   2263  CD  GLU A 333       3.569  24.588   1.616  1.00178.64      A    C  
ANISOU 2263  CD  GLU A 333    26592  25867  15416   2870   1232  -5127  A    C  
ATOM   2264  OE1 GLU A 333       4.269  23.599   1.933  1.00174.05      A    O  
ANISOU 2264  OE1 GLU A 333    26158  25077  14894   2264   1283  -4907  A    O  
ATOM   2265  OE2 GLU A 333       2.850  25.202   2.436  1.00184.03      A    O1-
ANISOU 2265  OE2 GLU A 333    27348  26831  15744   3358   1405  -5398  A    O1-
ATOM   2266  N   LYS A 334       1.839  21.776  -2.581  1.00184.48      A    N  
ANISOU 2266  N   LYS A 334    24877  28225  16994   1719   1639  -4912  A    N  
ATOM   2267  CA  LYS A 334       0.838  20.830  -3.048  1.00190.77      A    C  
ANISOU 2267  CA  LYS A 334    24905  29791  17787   1362   1986  -5038  A    C  
ATOM   2268  C   LYS A 334       1.357  19.401  -2.891  1.00190.88      A    C  
ANISOU 2268  C   LYS A 334    24992  29618  17915    501   2192  -4821  A    C  
ATOM   2269  O   LYS A 334       0.645  18.523  -2.414  1.00197.59      A    O  
ANISOU 2269  O   LYS A 334    25519  30951  18605     78   2636  -4917  A    O  
ATOM   2270  CB  LYS A 334       0.460  21.118  -4.509  1.00191.78      A    C  
ANISOU 2270  CB  LYS A 334    24537  30210  18120   1611   1757  -5094  A    C  
ATOM   2271  CG  LYS A 334      -0.057  22.527  -4.752  1.00191.92      A    C  
ANISOU 2271  CG  LYS A 334    24537  30375  18008   2528   1532  -5285  A    C  
ATOM   2272  CD  LYS A 334      -0.368  22.753  -6.231  1.00185.56      A    C  
ANISOU 2272  CD  LYS A 334    23299  29833  17372   2780   1284  -5301  A    C  
ATOM   2273  CE  LYS A 334      -1.630  22.018  -6.661  1.00185.22      A    C  
ANISOU 2273  CE  LYS A 334    22313  30813  17251   2607   1581  -5572  A    C  
ATOM   2274  NZ  LYS A 334      -2.839  22.510  -5.939  1.00193.56      A    N1+
ANISOU 2274  NZ  LYS A 334    22965  32614  17967   3127   1844  -5935  A    N1+
ATOM   2275  N   HIS A 335       2.594  19.168  -3.315  1.00187.80      A    N  
ANISOU 2275  N   HIS A 335    25034  28528  17794    247   1879  -4532  A    N  
ATOM   2276  CA  HIS A 335       3.123  17.806  -3.377  1.00188.28      A    C  
ANISOU 2276  CA  HIS A 335    25166  28382  17991   -496   2020  -4323  A    C  
ATOM   2277  C   HIS A 335       3.792  17.318  -2.086  1.00197.18      A    C  
ANISOU 2277  C   HIS A 335    26903  29080  18935   -770   2148  -4163  A    C  
ATOM   2278  O   HIS A 335       4.351  16.220  -2.059  1.00194.88      A    O  
ANISOU 2278  O   HIS A 335    26799  28516  18731  -1317   2231  -3961  A    O  
ATOM   2279  CB  HIS A 335       4.116  17.689  -4.540  1.00180.81      A    C  
ANISOU 2279  CB  HIS A 335    24323  26965  17411   -624   1639  -4104  A    C  
ATOM   2280  CG  HIS A 335       3.472  17.723  -5.892  1.00181.53      A    C  
ANISOU 2280  CG  HIS A 335    23799  27509  17664   -544   1575  -4221  A    C  
ATOM   2281  CD2 HIS A 335       3.396  16.780  -6.860  1.00176.40      A    C  
ANISOU 2281  CD2 HIS A 335    22788  27029  17205   -992   1625  -4191  A    C  
ATOM   2282  ND1 HIS A 335       2.808  18.827  -6.374  1.00189.67      A    N  
ANISOU 2282  ND1 HIS A 335    24554  28875  18636     89   1426  -4405  A    N  
ATOM   2283  CE1 HIS A 335       2.351  18.568  -7.588  1.00188.97      A    C  
ANISOU 2283  CE1 HIS A 335    23940  29177  18684     40   1372  -4476  A    C  
ATOM   2284  NE2 HIS A 335       2.695  17.330  -7.904  1.00182.13      A    N  
ANISOU 2284  NE2 HIS A 335    23004  28223  17975   -632   1493  -4360  A    N  
ATOM   2285  N   GLY A 336       3.717  18.114  -1.021  1.00208.42      A    N  
ANISOU 2285  N   GLY A 336    28660  30452  20077   -363   2160  -4262  A    N  
ATOM   2286  CA  GLY A 336       4.400  17.781   0.218  1.00214.56      A    C  
ANISOU 2286  CA  GLY A 336    30065  30822  20637   -532   2218  -4120  A    C  
ATOM   2287  C   GLY A 336       3.923  16.490   0.856  1.00223.44      A    C  
ANISOU 2287  C   GLY A 336    31138  32209  21549  -1106   2722  -4064  A    C  
ATOM   2288  O   GLY A 336       2.758  16.114   0.715  1.00238.98      A    O  
ANISOU 2288  O   GLY A 336    32550  34831  23421  -1282   3129  -4241  A    O  
ATOM   2289  N   ASP A 337       4.808  15.824   1.593  1.00201.33      A    N  
ANISOU 2289  N   ASP A 337    28932  28914  18650  -1393   2705  -3825  A    N  
ATOM   2290  CA  ASP A 337       6.154  16.315   1.854  1.00179.77      A    C  
ANISOU 2290  CA  ASP A 337    26799  25505  16000  -1167   2218  -3668  A    C  
ATOM   2291  C   ASP A 337       7.203  15.225   1.611  1.00162.22      A    C  
ANISOU 2291  C   ASP A 337    24876  22800  13960  -1618   2088  -3369  A    C  
ATOM   2292  O   ASP A 337       6.916  14.034   1.749  1.00154.45      A    O  
ANISOU 2292  O   ASP A 337    23888  21905  12890  -2094   2442  -3258  A    O  
ATOM   2293  CB  ASP A 337       6.243  16.843   3.283  1.00195.85      A    C  
ANISOU 2293  CB  ASP A 337    29346  27449  17617   -864   2254  -3737  A    C  
ATOM   2294  CG  ASP A 337       5.120  17.808   3.615  1.00199.96      A    C  
ANISOU 2294  CG  ASP A 337    29584  28491  17902   -401   2452  -4054  A    C  
ATOM   2295  OD1 ASP A 337       4.025  17.345   3.994  1.00200.64      A    O  
ANISOU 2295  OD1 ASP A 337    29348  29150  17735   -561   2964  -4171  A    O  
ATOM   2296  OD2 ASP A 337       5.331  19.033   3.490  1.00194.52      A    O1-
ANISOU 2296  OD2 ASP A 337    28998  27636  17273    123   2107  -4195  A    O1-
ATOM   2297  N   TYR A 338       8.422  15.633   1.271  1.00159.06      A    N  
ANISOU 2297  N   TYR A 338    24751  21885  13798  -1466   1593  -3248  A    N  
ATOM   2298  CA  TYR A 338       9.486  14.671   0.989  1.00157.33      A    C  
ANISOU 2298  CA  TYR A 338    24783  21236  13761  -1801   1426  -2988  A    C  
ATOM   2299  C   TYR A 338      10.507  14.586   2.110  1.00155.55      A    C  
ANISOU 2299  C   TYR A 338    25212  20583  13307  -1713   1215  -2856  A    C  
ATOM   2300  O   TYR A 338      11.036  15.596   2.576  1.00162.30      A    O  
ANISOU 2300  O   TYR A 338    26314  21248  14104  -1354    887  -2943  A    O  
ATOM   2301  CB  TYR A 338      10.212  15.018  -0.316  1.00158.30      A    C  
ANISOU 2301  CB  TYR A 338    24675  21141  14330  -1753   1033  -2934  A    C  
ATOM   2302  CG  TYR A 338       9.361  14.962  -1.561  1.00164.31      A    C  
ANISOU 2302  CG  TYR A 338    24817  22293  15321  -1849   1179  -3033  A    C  
ATOM   2303  CD1 TYR A 338       8.471  15.982  -1.869  1.00169.10      A    C  
ANISOU 2303  CD1 TYR A 338    25066  23275  15909  -1497   1205  -3255  A    C  
ATOM   2304  CD2 TYR A 338       9.463  13.891  -2.439  1.00159.67      A    C  
ANISOU 2304  CD2 TYR A 338    24022  21698  14949  -2254   1267  -2921  A    C  
ATOM   2305  CE1 TYR A 338       7.698  15.928  -3.012  1.00170.38      A    C  
ANISOU 2305  CE1 TYR A 338    24650  23838  16247  -1541   1300  -3357  A    C  
ATOM   2306  CE2 TYR A 338       8.700  13.830  -3.580  1.00162.68      A    C  
ANISOU 2306  CE2 TYR A 338    23837  22461  15513  -2341   1370  -3038  A    C  
ATOM   2307  CZ  TYR A 338       7.818  14.850  -3.863  1.00170.79      A    C  
ANISOU 2307  CZ  TYR A 338    24485  23901  16505  -1981   1377  -3254  A    C  
ATOM   2308  OH  TYR A 338       7.053  14.792  -5.004  1.00176.75      A    O  
ANISOU 2308  OH  TYR A 338    24662  25085  17411  -2023   1445  -3383  A    O  
ATOM   2309  N   GLU A 339      10.766  13.354   2.534  1.00139.85      A    N  
ANISOU 2309  N   GLU A 339    23524  18440  11173  -2042   1400  -2656  A    N  
ATOM   2310  CA  GLU A 339      11.733  13.060   3.581  1.00136.90      A    C  
ANISOU 2310  CA  GLU A 339    23786  17689  10540  -1957   1205  -2504  A    C  
ATOM   2311  C   GLU A 339      13.179  13.306   3.149  1.00129.59      A    C  
ANISOU 2311  C   GLU A 339    22989  16347   9905  -1819    635  -2414  A    C  
ATOM   2312  O   GLU A 339      14.024  13.639   3.973  1.00128.79      A    O  
ANISOU 2312  O   GLU A 339    23302  16007   9625  -1593    321  -2402  A    O  
ATOM   2313  CB  GLU A 339      11.576  11.616   4.064  1.00137.81      A    C  
ANISOU 2313  CB  GLU A 339    24229  17725  10408  -2329   1577  -2288  A    C  
ATOM   2314  CG  GLU A 339      10.293  11.328   4.827  1.00151.30      A    C  
ANISOU 2314  CG  GLU A 339    25947  19817  11723  -2505   2168  -2354  A    C  
ATOM   2315  CD  GLU A 339      10.460  11.537   6.316  1.00168.22      A    C  
ANISOU 2315  CD  GLU A 339    28683  21887  13345  -2261   2195  -2328  A    C  
ATOM   2316  OE1 GLU A 339      11.499  11.104   6.851  1.00174.36      A    O  
ANISOU 2316  OE1 GLU A 339    30012  22256  13982  -2176   1924  -2135  A    O  
ATOM   2317  OE2 GLU A 339       9.549  12.106   6.956  1.00176.55      A    O1-
ANISOU 2317  OE2 GLU A 339    29654  23321  14107  -2130   2487  -2510  A    O1-
ATOM   2318  N   ALA A 340      13.474  13.115   1.868  1.00124.22      A    N  
ANISOU 2318  N   ALA A 340    21937  15612   9650  -1967    509  -2364  A    N  
ATOM   2319  CA  ALA A 340      14.811  13.403   1.356  1.00124.27      A    C  
ANISOU 2319  CA  ALA A 340    21972  15295   9952  -1860      7  -2299  A    C  
ATOM   2320  C   ALA A 340      14.744  14.021  -0.035  1.00118.41      A    C  
ANISOU 2320  C   ALA A 340    20716  14640   9636  -1865   -116  -2370  A    C  
ATOM   2321  O   ALA A 340      13.743  13.879  -0.732  1.00129.31      A    O  
ANISOU 2321  O   ALA A 340    21714  16315  11103  -1995    178  -2431  A    O  
ATOM   2322  CB  ALA A 340      15.652  12.145   1.335  1.00128.43      A    C  
ANISOU 2322  CB  ALA A 340    22749  15555  10492  -2035    -53  -2073  A    C  
ATOM   2323  N   ILE A 341      15.817  14.697  -0.439  1.00108.65      A    N  
ANISOU 2323  N   ILE A 341    19469  13168   8646  -1736   -549  -2367  A    N  
ATOM   2324  CA  ILE A 341      15.874  15.314  -1.761  1.00115.57      A    C  
ANISOU 2324  CA  ILE A 341    19933  14079   9899  -1736   -676  -2399  A    C  
ATOM   2325  C   ILE A 341      17.253  15.139  -2.402  1.00118.39      A    C  
ANISOU 2325  C   ILE A 341    20260  14175  10548  -1815  -1024  -2275  A    C  
ATOM   2326  O   ILE A 341      18.276  15.236  -1.724  1.00110.43      A    O  
ANISOU 2326  O   ILE A 341    19529  12950   9480  -1742  -1320  -2256  A    O  
ATOM   2327  CB  ILE A 341      15.501  16.817  -1.667  1.00 97.39      A    C  
ANISOU 2327  CB  ILE A 341    17613  11808   7585  -1446   -796  -2584  A    C  
ATOM   2328  CG1 ILE A 341      13.980  16.978  -1.687  1.00 99.24      A    C  
ANISOU 2328  CG1 ILE A 341    17615  12435   7658  -1354   -418  -2719  A    C  
ATOM   2329  CG2 ILE A 341      16.125  17.623  -2.792  1.00 95.09      A    C  
ANISOU 2329  CG2 ILE A 341    17116  11361   7652  -1415  -1079  -2568  A    C  
ATOM   2330  CD1 ILE A 341      13.472  18.100  -0.836  1.00102.18      A    C  
ANISOU 2330  CD1 ILE A 341    18189  12852   7784  -1007   -432  -2919  A    C  
ATOM   2331  N   VAL A 342      17.272  14.878  -3.710  1.00122.02      A    N  
ANISOU 2331  N   VAL A 342    20357  14701  11306  -1955   -988  -2211  A    N  
ATOM   2332  CA  VAL A 342      18.512  14.552  -4.411  1.00107.56      A    C  
ANISOU 2332  CA  VAL A 342    18438  12690   9739  -2045  -1246  -2094  A    C  
ATOM   2333  C   VAL A 342      18.897  15.597  -5.448  1.00105.73      A    C  
ANISOU 2333  C   VAL A 342    17945  12424   9804  -2009  -1444  -2116  A    C  
ATOM   2334  O   VAL A 342      18.049  16.111  -6.179  1.00 87.32      A    O  
ANISOU 2334  O   VAL A 342    15383  10254   7539  -1967  -1303  -2166  A    O  
ATOM   2335  CB  VAL A 342      18.421  13.183  -5.128  1.00102.23      A    C  
ANISOU 2335  CB  VAL A 342    17620  12075   9149  -2260  -1039  -1978  A    C  
ATOM   2336  CG1 VAL A 342      19.813  12.614  -5.379  1.00 87.31      A    C  
ANISOU 2336  CG1 VAL A 342    15776   9988   7412  -2275  -1302  -1864  A    C  
ATOM   2337  CG2 VAL A 342      17.567  12.204  -4.330  1.00 95.62      A    C  
ANISOU 2337  CG2 VAL A 342    17011  11306   8014  -2371   -698  -1962  A    C  
ATOM   2338  N   ASP A 343      20.193  15.881  -5.517  1.00118.29      A    N  
ANISOU 2338  N   ASP A 343    19570  13822  11554  -2027  -1768  -2077  A    N  
ATOM   2339  CA  ASP A 343      20.740  16.764  -6.536  1.00113.22      A    C  
ANISOU 2339  CA  ASP A 343    18710  13111  11197  -2068  -1935  -2061  A    C  
ATOM   2340  C   ASP A 343      20.990  15.949  -7.795  1.00102.45      A    C  
ANISOU 2340  C   ASP A 343    17024  11857  10046  -2214  -1839  -1938  A    C  
ATOM   2341  O   ASP A 343      22.001  15.254  -7.905  1.00103.43      A    O  
ANISOU 2341  O   ASP A 343    17101  11934  10263  -2290  -1965  -1867  A    O  
ATOM   2342  CB  ASP A 343      22.024  17.446  -6.043  1.00111.55      A    C  
ANISOU 2342  CB  ASP A 343    18635  12686  11062  -2089  -2302  -2104  A    C  
ATOM   2343  CG  ASP A 343      22.702  18.280  -7.119  1.00115.23      A    C  
ANISOU 2343  CG  ASP A 343    18889  13065  11827  -2217  -2437  -2065  A    C  
ATOM   2344  OD1 ASP A 343      22.067  18.578  -8.150  1.00130.63      A    O  
ANISOU 2344  OD1 ASP A 343    20669  15084  13880  -2213  -2266  -2008  A    O  
ATOM   2345  OD2 ASP A 343      23.869  18.669  -6.920  1.00109.37      A    O1-
ANISOU 2345  OD2 ASP A 343    18155  12202  11201  -2327  -2713  -2097  A    O1-
ATOM   2346  N   GLY A 344      20.047  16.025  -8.728  1.00 93.57      A    N  
ANISOU 2346  N   GLY A 344    15676  10907   8970  -2216  -1623  -1935  A    N  
ATOM   2347  CA  GLY A 344      20.094  15.217  -9.929  1.00102.27      A    C  
ANISOU 2347  CA  GLY A 344    16490  12146  10224  -2343  -1504  -1852  A    C  
ATOM   2348  C   GLY A 344      21.384  15.318 -10.716  1.00 98.62      A    C  
ANISOU 2348  C   GLY A 344    15879  11592  10002  -2428  -1698  -1758  A    C  
ATOM   2349  O   GLY A 344      21.977  14.301 -11.074  1.00 79.74      A    O  
ANISOU 2349  O   GLY A 344    13390   9229   7680  -2508  -1687  -1700  A    O  
ATOM   2350  N   ALA A 345      21.839  16.545 -10.946  1.00 99.34      A    N  
ANISOU 2350  N   ALA A 345    15977  11564  10206  -2414  -1865  -1751  A    N  
ATOM   2351  CA  ALA A 345      23.041  16.781 -11.742  1.00112.86      A    C  
ANISOU 2351  CA  ALA A 345    17514  13224  12145  -2546  -2010  -1665  A    C  
ATOM   2352  C   ALA A 345      24.247  16.071 -11.141  1.00120.44      A    C  
ANISOU 2352  C   ALA A 345    18473  14148  13141  -2603  -2192  -1669  A    C  
ATOM   2353  O   ALA A 345      24.947  15.326 -11.826  1.00109.58      A    O  
ANISOU 2353  O   ALA A 345    16876  12874  11884  -2661  -2186  -1607  A    O  
ATOM   2354  CB  ALA A 345      23.313  18.279 -11.864  1.00127.13      A    C  
ANISOU 2354  CB  ALA A 345    19425  14842  14036  -2574  -2146  -1666  A    C  
ATOM   2355  N   ASN A 346      24.458  16.291  -9.848  1.00133.56      A    N  
ANISOU 2355  N   ASN A 346    20389  15686  14669  -2542  -2361  -1757  A    N  
ATOM   2356  CA  ASN A 346      25.610  15.762  -9.127  1.00130.10      A    C  
ANISOU 2356  CA  ASN A 346    19976  15234  14220  -2531  -2598  -1785  A    C  
ATOM   2357  C   ASN A 346      25.792  14.248  -9.261  1.00109.31      A    C  
ANISOU 2357  C   ASN A 346    17292  12704  11539  -2454  -2507  -1718  A    C  
ATOM   2358  O   ASN A 346      26.902  13.769  -9.490  1.00104.31      A    O  
ANISOU 2358  O   ASN A 346    16481  12141  11011  -2442  -2658  -1701  A    O  
ATOM   2359  CB  ASN A 346      25.506  16.146  -7.651  1.00143.06      A    C  
ANISOU 2359  CB  ASN A 346    21966  16752  15638  -2426  -2761  -1902  A    C  
ATOM   2360  CG  ASN A 346      26.680  15.656  -6.842  1.00154.65      A    C  
ANISOU 2360  CG  ASN A 346    23471  18240  17048  -2363  -3054  -1949  A    C  
ATOM   2361  ND2 ASN A 346      27.870  16.145  -7.168  1.00137.93      A    N  
ANISOU 2361  ND2 ASN A 346    21099  16170  15139  -2497  -3294  -1995  A    N  
ATOM   2362  OD1 ASN A 346      26.524  14.832  -5.943  1.00183.72      A    O  
ANISOU 2362  OD1 ASN A 346    27404  21915  20486  -2194  -3059  -1946  A    O  
ATOM   2363  N   ILE A 347      24.699  13.507  -9.113  1.00102.60      A    N  
ANISOU 2363  N   ILE A 347    16601  11860  10521  -2402  -2254  -1694  A    N  
ATOM   2364  CA  ILE A 347      24.725  12.048  -9.185  1.00108.26      A    C  
ANISOU 2364  CA  ILE A 347    17383  12589  11163  -2353  -2131  -1634  A    C  
ATOM   2365  C   ILE A 347      25.198  11.521 -10.534  1.00 95.65      A    C  
ANISOU 2365  C   ILE A 347    15467  11100   9777  -2410  -2067  -1582  A    C  
ATOM   2366  O   ILE A 347      26.151  10.743 -10.617  1.00 82.23      A    O  
ANISOU 2366  O   ILE A 347    13725   9405   8114  -2311  -2180  -1558  A    O  
ATOM   2367  CB  ILE A 347      23.329  11.459  -8.904  1.00102.87      A    C  
ANISOU 2367  CB  ILE A 347    16905  11900  10282  -2394  -1813  -1635  A    C  
ATOM   2368  CG1 ILE A 347      22.664  12.160  -7.711  1.00109.26      A    C  
ANISOU 2368  CG1 ILE A 347    17981  12663  10871  -2337  -1812  -1702  A    C  
ATOM   2369  CG2 ILE A 347      23.429   9.942  -8.696  1.00 83.32      A    C  
ANISOU 2369  CG2 ILE A 347    14648   9328   7682  -2365  -1701  -1572  A    C  
ATOM   2370  CD1 ILE A 347      23.323  11.884  -6.404  1.00110.52      A    C  
ANISOU 2370  CD1 ILE A 347    18483  12689  10820  -2191  -2013  -1700  A    C  
ATOM   2371  N   GLY A 348      24.524  11.974 -11.585  1.00 93.84      A    N  
ANISOU 2371  N   GLY A 348    15020  10976   9658  -2526  -1894  -1576  A    N  
ATOM   2372  CA  GLY A 348      24.760  11.496 -12.931  1.00 87.39      A    C  
ANISOU 2372  CA  GLY A 348    13924  10287   8992  -2580  -1790  -1538  A    C  
ATOM   2373  C   GLY A 348      26.140  11.700 -13.521  1.00 98.51      A    C  
ANISOU 2373  C   GLY A 348    15069  11772  10590  -2574  -1966  -1506  A    C  
ATOM   2374  O   GLY A 348      26.614  10.840 -14.264  1.00102.97      A    O  
ANISOU 2374  O   GLY A 348    15487  12423  11215  -2533  -1911  -1492  A    O  
ATOM   2375  N   LEU A 349      26.792  12.818 -13.214  1.00106.73      A    N  
ANISOU 2375  N   LEU A 349    16041  12791  11718  -2630  -2165  -1514  A    N  
ATOM   2376  CA  LEU A 349      28.104  13.064 -13.798  1.00104.94      A    C  
ANISOU 2376  CA  LEU A 349    15503  12691  11679  -2692  -2301  -1499  A    C  
ATOM   2377  C   LEU A 349      29.201  12.422 -12.958  1.00 98.37      A    C  
ANISOU 2377  C   LEU A 349    14668  11893  10816  -2542  -2542  -1559  A    C  
ATOM   2378  O   LEU A 349      30.283  12.124 -13.460  1.00 84.65      A    O  
ANISOU 2378  O   LEU A 349    12628  10337   9199  -2514  -2622  -1569  A    O  
ATOM   2379  CB  LEU A 349      28.335  14.564 -13.960  1.00 97.43      A    C  
ANISOU 2379  CB  LEU A 349    14477  11693  10847  -2889  -2382  -1488  A    C  
ATOM   2380  CG  LEU A 349      27.392  15.195 -14.992  1.00108.65      A    C  
ANISOU 2380  CG  LEU A 349    15889  13106  12287  -2965  -2160  -1404  A    C  
ATOM   2381  CD1 LEU A 349      26.451  16.204 -14.358  1.00103.79      A    C  
ANISOU 2381  CD1 LEU A 349    15565  12298  11573  -2950  -2173  -1433  A    C  
ATOM   2382  CD2 LEU A 349      28.181  15.835 -16.126  1.00131.64      A    C  
ANISOU 2382  CD2 LEU A 349    18532  16115  15372  -3147  -2124  -1317  A    C  
ATOM   2383  N   TYR A 350      28.901  12.193 -11.683  1.00 97.86      A    N  
ANISOU 2383  N   TYR A 350    14938  11683  10561  -2415  -2652  -1602  A    N  
ATOM   2384  CA  TYR A 350      29.760  11.405 -10.808  1.00107.76      A    C  
ANISOU 2384  CA  TYR A 350    16284  12956  11703  -2184  -2880  -1645  A    C  
ATOM   2385  C   TYR A 350      29.638   9.983 -11.321  1.00126.54      A    C  
ANISOU 2385  C   TYR A 350    18728  15327  14026  -2010  -2708  -1589  A    C  
ATOM   2386  O   TYR A 350      28.521   9.532 -11.546  1.00145.71      A    O  
ANISOU 2386  O   TYR A 350    21364  17631  16369  -2066  -2445  -1544  A    O  
ATOM   2387  CB  TYR A 350      29.315  11.511  -9.347  1.00113.20      A    C  
ANISOU 2387  CB  TYR A 350    17393  13474  12144  -2082  -3000  -1684  A    C  
ATOM   2388  CG  TYR A 350      30.273  10.926  -8.328  1.00128.76      A    C  
ANISOU 2388  CG  TYR A 350    19488  15479  13958  -1810  -3306  -1734  A    C  
ATOM   2389  CD1 TYR A 350      30.364   9.552  -8.132  1.00124.92      A    C  
ANISOU 2389  CD1 TYR A 350    19232  14927  13307  -1531  -3267  -1668  A    C  
ATOM   2390  CD2 TYR A 350      31.063  11.751  -7.534  1.00139.31      A    C  
ANISOU 2390  CD2 TYR A 350    20749  16897  15284  -1818  -3648  -1859  A    C  
ATOM   2391  CE1 TYR A 350      31.230   9.017  -7.192  1.00122.02      A    C  
ANISOU 2391  CE1 TYR A 350    19017  14592  12752  -1206  -3571  -1703  A    C  
ATOM   2392  CE2 TYR A 350      31.931  11.224  -6.590  1.00133.40      A    C  
ANISOU 2392  CE2 TYR A 350    20096  16233  14357  -1525  -3968  -1924  A    C  
ATOM   2393  CZ  TYR A 350      32.011   9.859  -6.423  1.00124.79      A    C  
ANISOU 2393  CZ  TYR A 350    19237  15090  13086  -1188  -3932  -1834  A    C  
ATOM   2394  OH  TYR A 350      32.875   9.341  -5.484  1.00112.19      A    O  
ANISOU 2394  OH  TYR A 350    17770  13581  11274   -825  -4273  -1888  A    O  
ATOM   2395  N   GLN A 351      30.736   9.268 -11.539  1.00129.29      A    N  
ANISOU 2395  N   GLN A 351    18896  15813  14417  -1803  -2845  -1612  A    N  
ATOM   2396  CA  GLN A 351      32.103   9.720 -11.338  1.00121.85      A    C  
ANISOU 2396  CA  GLN A 351    17609  15108  13579  -1741  -3154  -1699  A    C  
ATOM   2397  C   GLN A 351      32.885   9.661 -12.642  1.00128.95      A    C  
ANISOU 2397  C   GLN A 351    18014  16282  14699  -1790  -3077  -1709  A    C  
ATOM   2398  O   GLN A 351      34.108   9.796 -12.663  1.00134.48      A    O  
ANISOU 2398  O   GLN A 351    18337  17262  15496  -1722  -3288  -1796  A    O  
ATOM   2399  CB  GLN A 351      32.849   8.765 -10.402  1.00123.13      A    C  
ANISOU 2399  CB  GLN A 351    17951  15283  13550  -1337  -3410  -1739  A    C  
ATOM   2400  CG  GLN A 351      34.086   9.337  -9.732  1.00134.87      A    C  
ANISOU 2400  CG  GLN A 351    19150  17030  15066  -1260  -3808  -1874  A    C  
ATOM   2401  CD  GLN A 351      34.660   8.402  -8.678  1.00134.67      A    C  
ANISOU 2401  CD  GLN A 351    19388  17005  14776   -785  -4088  -1907  A    C  
ATOM   2402  NE2 GLN A 351      35.776   8.799  -8.076  1.00132.63      A    N  
ANISOU 2402  NE2 GLN A 351    18839  17039  14514   -669  -4477  -2058  A    N  
ATOM   2403  OE1 GLN A 351      34.104   7.336  -8.409  1.00128.49      A    O  
ANISOU 2403  OE1 GLN A 351    19081  15961  13780   -532  -3959  -1801  A    O  
ATOM   2404  N   GLN A 352      32.154   9.442 -13.731  1.00134.69      A    N  
ANISOU 2404  N   GLN A 352    18726  16966  15483  -1906  -2767  -1637  A    N  
ATOM   2405  CA  GLN A 352      32.825   9.349 -15.047  1.00133.76      A    C  
ANISOU 2405  CA  GLN A 352    18171  17117  15533  -1941  -2650  -1640  A    C  
ATOM   2406  C   GLN A 352      33.247  10.668 -15.633  1.00133.16      A    C  
ANISOU 2406  C   GLN A 352    17722  17221  15651  -2280  -2641  -1627  A    C  
ATOM   2407  O   GLN A 352      32.672  11.701 -15.288  1.00118.61      A    O  
ANISOU 2407  O   GLN A 352    16025  15219  13822  -2520  -2650  -1595  A    O  
ATOM   2408  CB  GLN A 352      31.874   8.642 -16.003  1.00126.65      A    C  
ANISOU 2408  CB  GLN A 352    17418  16114  14589  -1943  -2338  -1587  A    C  
ATOM   2409  CG  GLN A 352      30.651   9.432 -16.356  1.00109.39      A    C  
ANISOU 2409  CG  GLN A 352    15346  13810  12408  -2225  -2149  -1520  A    C  
ATOM   2410  CD  GLN A 352      29.666   9.444 -15.213  1.00 96.61      A    C  
ANISOU 2410  CD  GLN A 352    14150  11925  10632  -2229  -2171  -1516  A    C  
ATOM   2411  NE2 GLN A 352      28.530  10.100 -15.421  1.00 86.39      A    N  
ANISOU 2411  NE2 GLN A 352    12947  10559   9317  -2415  -2016  -1484  A    N  
ATOM   2412  OE1 GLN A 352      29.911   8.856 -14.160  1.00113.83      A    O  
ANISOU 2412  OE1 GLN A 352    16578  13985  12685  -2039  -2320  -1542  A    O  
ATOM   2413  N   ASN A 353      34.280  10.636 -16.466  1.00149.37      A    N  
ANISOU 2413  N   ASN A 353    19321  19596  17836  -2292  -2619  -1657  A    N  
ATOM   2414  CA  ASN A 353      34.893  11.821 -17.048  1.00154.88      A    C  
ANISOU 2414  CA  ASN A 353    19643  20488  18715  -2653  -2588  -1639  A    C  
ATOM   2415  C   ASN A 353      34.110  12.629 -18.074  1.00156.09      A    C  
ANISOU 2415  C   ASN A 353    19852  20538  18915  -2947  -2310  -1498  A    C  
ATOM   2416  O   ASN A 353      33.137  12.136 -18.636  1.00142.68      A    O  
ANISOU 2416  O   ASN A 353    18368  18724  17120  -2846  -2112  -1433  A    O  
ATOM   2417  CB  ASN A 353      36.133  11.196 -17.688  1.00163.64      A    C  
ANISOU 2417  CB  ASN A 353    20264  22014  19897  -2495  -2587  -1717  A    C  
ATOM   2418  CG  ASN A 353      37.268  12.183 -17.848  1.00171.16      A    C  
ANISOU 2418  CG  ASN A 353    20719  23284  21031  -2824  -2662  -1773  A    C  
ATOM   2419  ND2 ASN A 353      38.485  11.724 -17.584  1.00173.13      A    N  
ANISOU 2419  ND2 ASN A 353    20547  23918  21317  -2631  -2852  -1928  A    N  
ATOM   2420  OD1 ASN A 353      37.057  13.346 -18.187  1.00176.06      A    O  
ANISOU 2420  OD1 ASN A 353    21342  23805  21749  -3247  -2551  -1688  A    O  
ATOM   2421  N   PHE A 354      34.528  13.872 -18.308  1.00172.81      A    N  
ANISOU 2421  N   PHE A 354    21801  22693  21165  -3312  -2303  -1458  A    N  
ATOM   2422  CA  PHE A 354      33.828  14.759 -19.236  1.00164.94      A    C  
ANISOU 2422  CA  PHE A 354    20926  21562  20181  -3560  -2062  -1300  A    C  
ATOM   2423  C   PHE A 354      34.072  14.369 -20.693  1.00166.25      A    C  
ANISOU 2423  C   PHE A 354    20824  21993  20349  -3550  -1788  -1218  A    C  
ATOM   2424  O   PHE A 354      34.542  15.164 -21.507  1.00149.82      A    O  
ANISOU 2424  O   PHE A 354    18554  20026  18344  -3839  -1635  -1119  A    O  
ATOM   2425  CB  PHE A 354      34.246  16.212 -19.009  1.00180.33      A    C  
ANISOU 2425  CB  PHE A 354    22867  23397  22254  -3968  -2129  -1273  A    C  
ATOM   2426  CG  PHE A 354      33.429  16.920 -17.964  1.00199.94      A    C  
ANISOU 2426  CG  PHE A 354    25792  25500  24679  -3995  -2285  -1298  A    C  
ATOM   2427  CD1 PHE A 354      32.249  16.362 -17.495  1.00204.63      A    C  
ANISOU 2427  CD1 PHE A 354    26731  25910  25109  -3701  -2283  -1302  A    C  
ATOM   2428  CD2 PHE A 354      33.834  18.148 -17.458  1.00204.09      A    C  
ANISOU 2428  CD2 PHE A 354    26390  25854  25302  -4332  -2416  -1335  A    C  
ATOM   2429  CE1 PHE A 354      31.491  17.012 -16.535  1.00201.80      A    C  
ANISOU 2429  CE1 PHE A 354    26756  25247  24673  -3697  -2401  -1339  A    C  
ATOM   2430  CE2 PHE A 354      33.079  18.804 -16.498  1.00205.25      A    C  
ANISOU 2430  CE2 PHE A 354    26969  25646  25371  -4315  -2556  -1382  A    C  
ATOM   2431  CZ  PHE A 354      31.906  18.234 -16.037  1.00203.99      A    C  
ANISOU 2431  CZ  PHE A 354    27124  25348  25034  -3974  -2544  -1382  A    C  
ATOM   2432  N   VAL A 355      33.729  13.122 -20.995  1.00183.33      A    N  
ANISOU 2432  N   VAL A 355    23019  24231  22405  -3223  -1717  -1262  A    N  
ATOM   2433  CA  VAL A 355      33.880  12.519 -22.316  1.00190.84      A    C  
ANISOU 2433  CA  VAL A 355    23766  25433  23312  -3129  -1475  -1231  A    C  
ATOM   2434  C   VAL A 355      32.906  12.986 -23.429  1.00152.78      A    C  
ANISOU 2434  C   VAL A 355    19113  20544  18392  -3233  -1229  -1084  A    C  
ATOM   2435  O   VAL A 355      33.377  13.281 -24.530  1.00158.74      A    O  
ANISOU 2435  O   VAL A 355    19643  21525  19145  -3352  -1032   -999  A    O  
ATOM   2436  CB  VAL A 355      33.784  10.973 -22.218  1.00159.89      A    C  
ANISOU 2436  CB  VAL A 355    19909  21549  19293  -2732  -1498  -1358  A    C  
ATOM   2437  CG1 VAL A 355      34.177  10.326 -23.535  1.00162.63      A    C  
ANISOU 2437  CG1 VAL A 355    20008  22191  19593  -2608  -1274  -1375  A    C  
ATOM   2438  CG2 VAL A 355      34.663  10.452 -21.086  1.00160.71      A    C  
ANISOU 2438  CG2 VAL A 355    19921  21703  19439  -2531  -1768  -1489  A    C  
ATOM   2439  N   ASP A 356      31.586  13.076 -23.192  1.00129.78      A    N  
ANISOU 2439  N   ASP A 356    16567  17370  15374  -3177  -1231  -1058  A    N  
ATOM   2440  CA  ASP A 356      30.960  13.438 -21.907  1.00136.41      A    C  
ANISOU 2440  CA  ASP A 356    17704  17912  16215  -3184  -1419  -1092  A    C  
ATOM   2441  C   ASP A 356      30.831  12.360 -20.834  1.00148.02      A    C  
ANISOU 2441  C   ASP A 356    19315  19286  17640  -2956  -1571  -1230  A    C  
ATOM   2442  O   ASP A 356      30.725  12.698 -19.653  1.00153.16      A    O  
ANISOU 2442  O   ASP A 356    20148  19750  18296  -2974  -1751  -1266  A    O  
ATOM   2443  CB  ASP A 356      29.558  13.999 -22.144  1.00131.40      A    C  
ANISOU 2443  CB  ASP A 356    17364  17101  15461  -3191  -1330  -1018  A    C  
ATOM   2444  CG  ASP A 356      28.701  13.082 -22.977  1.00141.92      A    C  
ANISOU 2444  CG  ASP A 356    18720  18551  16652  -3022  -1172  -1059  A    C  
ATOM   2445  OD1 ASP A 356      29.067  12.838 -24.144  1.00140.24      A    O  
ANISOU 2445  OD1 ASP A 356    18316  18560  16410  -3012  -1022  -1023  A    O  
ATOM   2446  OD2 ASP A 356      27.691  12.566 -22.455  1.00151.83      A    O1-
ANISOU 2446  OD2 ASP A 356    20177  19696  17816  -2918  -1190  -1146  A    O1-
ATOM   2447  N   GLY A 357      30.802  11.087 -21.219  1.00142.14      A    N  
ANISOU 2447  N   GLY A 357    18548  18634  16825  -2740  -1492  -1306  A    N  
ATOM   2448  CA  GLY A 357      30.667  10.002 -20.256  1.00135.44      A    C  
ANISOU 2448  CA  GLY A 357    17922  17635  15902  -2520  -1605  -1409  A    C  
ATOM   2449  C   GLY A 357      29.364   9.976 -19.473  1.00125.63      A    C  
ANISOU 2449  C   GLY A 357    17062  16126  14546  -2543  -1600  -1416  A    C  
ATOM   2450  O   GLY A 357      29.026   8.972 -18.843  1.00125.31      A    O  
ANISOU 2450  O   GLY A 357    17274  15933  14404  -2399  -1613  -1480  A    O  
ATOM   2451  N   SER A 358      28.629  11.081 -19.520  1.00120.27      A    N  
ANISOU 2451  N   SER A 358    16442  15389  13868  -2714  -1565  -1348  A    N  
ATOM   2452  CA  SER A 358      27.326  11.175 -18.892  1.00121.25      A    C  
ANISOU 2452  CA  SER A 358    16855  15340  13874  -2728  -1527  -1370  A    C  
ATOM   2453  C   SER A 358      26.390  10.317 -19.736  1.00148.39      A    C  
ANISOU 2453  C   SER A 358    20313  18855  17212  -2702  -1322  -1424  A    C  
ATOM   2454  O   SER A 358      26.660  10.097 -20.918  1.00166.87      A    O  
ANISOU 2454  O   SER A 358    22456  21374  19574  -2694  -1219  -1417  A    O  
ATOM   2455  CB  SER A 358      26.875  12.638 -18.820  1.00126.14      A    C  
ANISOU 2455  CB  SER A 358    17517  15898  14514  -2853  -1554  -1299  A    C  
ATOM   2456  OG  SER A 358      26.931  13.254 -20.095  1.00144.20      A    O  
ANISOU 2456  OG  SER A 358    19625  18325  16839  -2929  -1440  -1207  A    O  
ATOM   2457  N   PHE A 359      25.294   9.828 -19.167  1.00140.27      A    N  
ANISOU 2457  N   PHE A 359    19512  17720  16065  -2712  -1249  -1495  A    N  
ATOM   2458  CA  PHE A 359      24.747  10.268 -17.892  1.00118.71      A    C  
ANISOU 2458  CA  PHE A 359    17010  14826  13266  -2729  -1319  -1500  A    C  
ATOM   2459  C   PHE A 359      24.249   9.047 -17.138  1.00125.41      A    C  
ANISOU 2459  C   PHE A 359    18130  15530  13988  -2715  -1238  -1574  A    C  
ATOM   2460  O   PHE A 359      23.464   8.265 -17.676  1.00143.97      A    O  
ANISOU 2460  O   PHE A 359    20499  17930  16274  -2791  -1056  -1652  A    O  
ATOM   2461  CB  PHE A 359      23.630  11.281 -18.152  1.00102.81      A    C  
ANISOU 2461  CB  PHE A 359    14966  12895  11202  -2782  -1246  -1495  A    C  
ATOM   2462  CG  PHE A 359      22.945  11.778 -16.922  1.00 86.92      A    C  
ANISOU 2462  CG  PHE A 359    13174  10756   9094  -2770  -1284  -1525  A    C  
ATOM   2463  CD1 PHE A 359      23.440  12.863 -16.229  1.00 94.10      A    C  
ANISOU 2463  CD1 PHE A 359    14170  11535  10047  -2745  -1457  -1477  A    C  
ATOM   2464  CD2 PHE A 359      21.782  11.178 -16.479  1.00 86.87      A    C  
ANISOU 2464  CD2 PHE A 359    13285  10778   8944  -2805  -1129  -1619  A    C  
ATOM   2465  CE1 PHE A 359      22.794  13.332 -15.105  1.00 98.12      A    C  
ANISOU 2465  CE1 PHE A 359    14903  11938  10441  -2702  -1487  -1527  A    C  
ATOM   2466  CE2 PHE A 359      21.134  11.638 -15.356  1.00 90.54      A    C  
ANISOU 2466  CE2 PHE A 359    13937  11170   9293  -2779  -1131  -1655  A    C  
ATOM   2467  CZ  PHE A 359      21.641  12.717 -14.666  1.00 93.80      A    C  
ANISOU 2467  CZ  PHE A 359    14459  11448   9734  -2700  -1316  -1610  A    C  
ATOM   2468  N   SER A 360      24.707   8.863 -15.904  1.00109.96      A    N  
ANISOU 2468  N   SER A 360    16410  13392  11979  -2633  -1369  -1555  A    N  
ATOM   2469  CA  SER A 360      24.421   7.616 -15.206  1.00102.10      A    C  
ANISOU 2469  CA  SER A 360    15748  12207  10839  -2605  -1284  -1587  A    C  
ATOM   2470  C   SER A 360      23.116   7.648 -14.433  1.00 89.91      A    C  
ANISOU 2470  C   SER A 360    14425  10602   9134  -2741  -1124  -1622  A    C  
ATOM   2471  O   SER A 360      23.084   7.998 -13.256  1.00 90.44      A    O  
ANISOU 2471  O   SER A 360    14709  10559   9094  -2691  -1206  -1593  A    O  
ATOM   2472  CB  SER A 360      25.565   7.261 -14.256  1.00 80.16      A    C  
ANISOU 2472  CB  SER A 360    13158   9275   8024  -2394  -1506  -1542  A    C  
ATOM   2473  OG  SER A 360      26.598   6.583 -14.951  1.00102.77      A    O  
ANISOU 2473  OG  SER A 360    15886  12186  10976  -2236  -1571  -1549  A    O  
ATOM   2474  N   LEU A 361      22.044   7.251 -15.115  1.00 94.09      A    N  
ANISOU 2474  N   LEU A 361    14877  11242   9632  -2916   -891  -1705  A    N  
ATOM   2475  CA  LEU A 361      20.761   7.005 -14.473  1.00 99.66      A    C  
ANISOU 2475  CA  LEU A 361    15745  11944  10176  -3090   -679  -1771  A    C  
ATOM   2476  C   LEU A 361      20.913   5.764 -13.605  1.00108.20      A    C  
ANISOU 2476  C   LEU A 361    17273  12722  11114  -3121   -594  -1739  A    C  
ATOM   2477  O   LEU A 361      20.145   5.541 -12.671  1.00115.43      A    O  
ANISOU 2477  O   LEU A 361    18441  13560  11856  -3246   -436  -1745  A    O  
ATOM   2478  CB  LEU A 361      19.641   6.835 -15.504  1.00102.16      A    C  
ANISOU 2478  CB  LEU A 361    15801  12517  10500  -3289   -472  -1906  A    C  
ATOM   2479  CG  LEU A 361      18.222   6.688 -14.945  1.00113.12      A    C  
ANISOU 2479  CG  LEU A 361    17226  14022  11733  -3508   -231  -2015  A    C  
ATOM   2480  CD1 LEU A 361      17.234   7.435 -15.813  1.00108.83      A    C  
ANISOU 2480  CD1 LEU A 361    16264  13879  11209  -3541   -177  -2138  A    C  
ATOM   2481  CD2 LEU A 361      17.823   5.220 -14.850  1.00132.55      A    C  
ANISOU 2481  CD2 LEU A 361    19943  16315  14106  -3779      4  -2088  A    C  
ATOM   2482  N   SER A 362      21.904   4.947 -13.946  1.00105.50      A    N  
ANISOU 2482  N   SER A 362    17046  12212  10826  -2987   -684  -1703  A    N  
ATOM   2483  CA  SER A 362      22.227   3.765 -13.164  1.00112.30      A    C  
ANISOU 2483  CA  SER A 362    18406  12728  11535  -2924   -645  -1646  A    C  
ATOM   2484  C   SER A 362      22.569   4.180 -11.742  1.00127.42      A    C  
ANISOU 2484  C   SER A 362    20593  14520  13300  -2758   -796  -1540  A    C  
ATOM   2485  O   SER A 362      22.129   3.558 -10.775  1.00139.68      A    O  
ANISOU 2485  O   SER A 362    22591  15847  14632  -2821   -658  -1488  A    O  
ATOM   2486  CB  SER A 362      23.399   3.004 -13.785  1.00100.95      A    C  
ANISOU 2486  CB  SER A 362    17005  11170  10181  -2683   -779  -1633  A    C  
ATOM   2487  OG  SER A 362      24.476   3.875 -14.088  1.00 83.67      A    O  
ANISOU 2487  OG  SER A 362    14459   9186   8148  -2452  -1051  -1601  A    O  
ATOM   2488  N   GLN A 363      23.351   5.248 -11.626  1.00120.76      A    N  
ANISOU 2488  N   GLN A 363    19496  13826  12560  -2570  -1073  -1514  A    N  
ATOM   2489  CA  GLN A 363      23.726   5.789 -10.325  1.00112.97      A    C  
ANISOU 2489  CA  GLN A 363    18721  12769  11433  -2409  -1267  -1455  A    C  
ATOM   2490  C   GLN A 363      22.585   6.544  -9.649  1.00 84.70      A    C  
ANISOU 2490  C   GLN A 363    15187   9267   7727  -2575  -1121  -1487  A    C  
ATOM   2491  O   GLN A 363      22.472   6.540  -8.428  1.00 93.39      A    O  
ANISOU 2491  O   GLN A 363    16635  10246   8601  -2506  -1140  -1445  A    O  
ATOM   2492  CB  GLN A 363      24.947   6.688 -10.473  1.00 84.26      A    C  
ANISOU 2492  CB  GLN A 363    14775   9276   7964  -2217  -1609  -1458  A    C  
ATOM   2493  CG  GLN A 363      26.235   5.906 -10.654  1.00 85.49      A    C  
ANISOU 2493  CG  GLN A 363    14893   9400   8190  -1974  -1781  -1438  A    C  
ATOM   2494  CD  GLN A 363      27.427   6.804 -10.870  1.00 94.66      A    C  
ANISOU 2494  CD  GLN A 363    15658  10778   9532  -1859  -2085  -1468  A    C  
ATOM   2495  NE2 GLN A 363      27.362   8.006 -10.314  1.00 94.85      A    N  
ANISOU 2495  NE2 GLN A 363    15579  10881   9581  -1960  -2202  -1492  A    N  
ATOM   2496  OE1 GLN A 363      28.404   6.423 -11.518  1.00 93.37      A    O  
ANISOU 2496  OE1 GLN A 363    15286  10713   9477  -1689  -2204  -1483  A    O  
ATOM   2497  N   LEU A 364      21.763   7.220 -10.443  1.00 82.91      A    N  
ANISOU 2497  N   LEU A 364    14609   9270   7623  -2749   -987  -1568  A    N  
ATOM   2498  CA  LEU A 364      20.543   7.849  -9.941  1.00 91.69      A    C  
ANISOU 2498  CA  LEU A 364    15715  10513   8610  -2873   -809  -1631  A    C  
ATOM   2499  C   LEU A 364      19.540   6.830  -9.405  1.00108.63      A    C  
ANISOU 2499  C   LEU A 364    18154  12583  10539  -3089   -474  -1643  A    C  
ATOM   2500  O   LEU A 364      18.912   7.043  -8.369  1.00 92.75      A    O  
ANISOU 2500  O   LEU A 364    16350  10577   8313  -3118   -355  -1647  A    O  
ATOM   2501  CB  LEU A 364      19.874   8.677 -11.035  1.00 94.51      A    C  
ANISOU 2501  CB  LEU A 364    15628  11157   9126  -2953   -747  -1720  A    C  
ATOM   2502  CG  LEU A 364      20.175  10.173 -11.019  1.00107.63      A    C  
ANISOU 2502  CG  LEU A 364    17120  12897  10877  -2796   -968  -1723  A    C  
ATOM   2503  CD1 LEU A 364      21.421  10.472 -11.836  1.00121.74      A    C  
ANISOU 2503  CD1 LEU A 364    18714  14656  12887  -2718  -1203  -1661  A    C  
ATOM   2504  CD2 LEU A 364      18.978  10.958 -11.528  1.00106.50      A    C  
ANISOU 2504  CD2 LEU A 364    16721  13015  10729  -2827   -824  -1819  A    C  
ATOM   2505  N   GLU A 365      19.369   5.738 -10.144  1.00128.74      A    N  
ANISOU 2505  N   GLU A 365    20718  15061  13135  -3266   -301  -1662  A    N  
ATOM   2506  CA  GLU A 365      18.408   4.706  -9.779  1.00133.77      A    C  
ANISOU 2506  CA  GLU A 365    21633  15600  13591  -3568     53  -1688  A    C  
ATOM   2507  C   GLU A 365      18.852   4.037  -8.486  1.00142.72      A    C  
ANISOU 2507  C   GLU A 365    23376  16379  14472  -3468     56  -1538  A    C  
ATOM   2508  O   GLU A 365      18.023   3.658  -7.657  1.00157.39      A    O  
ANISOU 2508  O   GLU A 365    25527  18181  16094  -3676    339  -1520  A    O  
ATOM   2509  CB  GLU A 365      18.256   3.672 -10.901  1.00137.81      A    C  
ANISOU 2509  CB  GLU A 365    22081  16061  14221  -3787    201  -1764  A    C  
ATOM   2510  CG  GLU A 365      16.911   2.952 -10.904  1.00141.31      A    C  
ANISOU 2510  CG  GLU A 365    22569  16572  14551  -4238    603  -1883  A    C  
ATOM   2511  CD  GLU A 365      16.827   1.861 -11.954  1.00135.61      A    C  
ANISOU 2511  CD  GLU A 365    21860  15739  13928  -4476    728  -1986  A    C  
ATOM   2512  OE1 GLU A 365      17.816   1.665 -12.693  1.00133.22      A    O  
ANISOU 2512  OE1 GLU A 365    21533  15317  13769  -4242    509  -1959  A    O  
ATOM   2513  OE2 GLU A 365      15.768   1.206 -12.040  1.00135.79      A    O1-
ANISOU 2513  OE2 GLU A 365    21904  15813  13877  -4910   1052  -2116  A    O1-
ATOM   2514  N   SER A 366      20.165   3.901  -8.322  1.00117.31      A    N  
ANISOU 2514  N   SER A 366    20336  12954  11281  -3137   -256  -1433  A    N  
ATOM   2515  CA  SER A 366      20.734   3.287  -7.128  1.00110.76      A    C  
ANISOU 2515  CA  SER A 366    20099  11801  10184  -2937   -328  -1283  A    C  
ATOM   2516  C   SER A 366      20.392   4.063  -5.859  1.00123.12      A    C  
ANISOU 2516  C   SER A 366    21823  13444  11511  -2872   -343  -1255  A    C  
ATOM   2517  O   SER A 366      19.921   3.471  -4.889  1.00139.92      A    O  
ANISOU 2517  O   SER A 366    24443  15388  13332  -2958   -124  -1165  A    O  
ATOM   2518  CB  SER A 366      22.252   3.155  -7.260  1.00 93.43      A    C  
ANISOU 2518  CB  SER A 366    17933   9490   8077  -2531   -719  -1220  A    C  
ATOM   2519  OG  SER A 366      22.605   2.331  -8.355  1.00 93.20      A    O  
ANISOU 2519  OG  SER A 366    17826   9366   8219  -2540   -687  -1249  A    O  
ATOM   2520  N   VAL A 367      20.607   5.380  -5.868  1.00114.57      A    N  
ANISOU 2520  N   VAL A 367    20366  12616  10551  -2733   -580  -1335  A    N  
ATOM   2521  CA  VAL A 367      20.354   6.196  -4.676  1.00112.34      A    C  
ANISOU 2521  CA  VAL A 367    20246  12401  10038  -2628   -631  -1344  A    C  
ATOM   2522  C   VAL A 367      18.884   6.105  -4.279  1.00112.11      A    C  
ANISOU 2522  C   VAL A 367    20286  12493   9816  -2922   -196  -1390  A    C  
ATOM   2523  O   VAL A 367      18.556   6.124  -3.095  1.00131.32      A    O  
ANISOU 2523  O   VAL A 367    23089  14880  11928  -2885    -91  -1345  A    O  
ATOM   2524  CB  VAL A 367      20.773   7.698  -4.854  1.00 97.10      A    C  
ANISOU 2524  CB  VAL A 367    17917  10683   8294  -2468   -945  -1453  A    C  
ATOM   2525  CG1 VAL A 367      22.208   7.821  -5.349  1.00 90.04      A    C  
ANISOU 2525  CG1 VAL A 367    16854   9741   7618  -2259  -1335  -1432  A    C  
ATOM   2526  CG2 VAL A 367      19.826   8.448  -5.768  1.00101.32      A    C  
ANISOU 2526  CG2 VAL A 367    17984  11488   9023  -2650   -774  -1575  A    C  
ATOM   2527  N   MET A 368      18.005   5.993  -5.268  1.00 97.16      A    N  
ANISOU 2527  N   MET A 368    18021  10796   8099  -3209     58  -1492  A    N  
ATOM   2528  CA  MET A 368      16.587   5.818  -5.004  1.00109.88      A    C  
ANISOU 2528  CA  MET A 368    19599  12601   9548  -3529    489  -1572  A    C  
ATOM   2529  C   MET A 368      16.327   4.490  -4.298  1.00121.54      A    C  
ANISOU 2529  C   MET A 368    21645  13785  10750  -3762    803  -1443  A    C  
ATOM   2530  O   MET A 368      15.506   4.415  -3.384  1.00119.77      A    O  
ANISOU 2530  O   MET A 368    21639  13630  10240  -3922   1108  -1435  A    O  
ATOM   2531  CB  MET A 368      15.797   5.893  -6.307  1.00125.67      A    C  
ANISOU 2531  CB  MET A 368    21046  14905  11798  -3775    643  -1733  A    C  
ATOM   2532  CG  MET A 368      15.851   7.248  -6.989  1.00123.50      A    C  
ANISOU 2532  CG  MET A 368    20267  14919  11740  -3551    395  -1842  A    C  
ATOM   2533  SD  MET A 368      14.423   8.263  -6.558  1.00134.31      A    S  
ANISOU 2533  SD  MET A 368    21338  16735  12960  -3560    620  -2020  A    S  
ATOM   2534  CE  MET A 368      13.098   7.147  -7.013  1.00139.86      A    C  
ANISOU 2534  CE  MET A 368    21845  17682  13612  -4067   1103  -2142  A    C  
ATOM   2535  N   LYS A 369      17.040   3.450  -4.722  1.00137.87      A    N  
ANISOU 2535  N   LYS A 369    23984  15512  12887  -3768    740  -1339  A    N  
ATOM   2536  CA  LYS A 369      16.873   2.118  -4.149  1.00159.78      A    C  
ANISOU 2536  CA  LYS A 369    27398  17907  15405  -3978   1030  -1195  A    C  
ATOM   2537  C   LYS A 369      17.320   2.050  -2.687  1.00175.46      A    C  
ANISOU 2537  C   LYS A 369    30005  19656  17005  -3711    959  -1008  A    C  
ATOM   2538  O   LYS A 369      16.587   1.545  -1.835  1.00199.62      A    O  
ANISOU 2538  O   LYS A 369    33489  22616  19743  -3955   1330   -924  A    O  
ATOM   2539  CB  LYS A 369      17.637   1.080  -4.976  1.00166.39      A    C  
ANISOU 2539  CB  LYS A 369    28421  18398  16401  -3944    927  -1141  A    C  
ATOM   2540  CG  LYS A 369      16.983   0.723  -6.306  1.00165.65      A    C  
ANISOU 2540  CG  LYS A 369    27908  18454  16578  -4324   1123  -1321  A    C  
ATOM   2541  CD  LYS A 369      17.720  -0.429  -6.980  1.00166.37      A    C  
ANISOU 2541  CD  LYS A 369    28317  18137  16759  -4276   1059  -1272  A    C  
ATOM   2542  CE  LYS A 369      18.170  -0.062  -8.386  1.00166.54      A    C  
ANISOU 2542  CE  LYS A 369    27755  18387  17135  -4158    820  -1420  A    C  
ATOM   2543  NZ  LYS A 369      19.612  -0.374  -8.600  1.00160.91      A    N1+
ANISOU 2543  NZ  LYS A 369    27228  17419  16491  -3688    466  -1320  A    N1+
ATOM   2544  N   GLU A 370      18.515   2.553  -2.396  1.00165.35      A    N  
ANISOU 2544  N   GLU A 370    28774  18312  15738  -3228    491   -952  A    N  
ATOM   2545  CA  GLU A 370      19.047   2.498  -1.036  1.00156.54      A    C  
ANISOU 2545  CA  GLU A 370    28240  17002  14236  -2913    348   -795  A    C  
ATOM   2546  C   GLU A 370      18.261   3.397  -0.090  1.00146.16      A    C  
ANISOU 2546  C   GLU A 370    26894  15960  12680  -2959    494   -859  A    C  
ATOM   2547  O   GLU A 370      18.037   3.049   1.070  1.00165.75      A    O  
ANISOU 2547  O   GLU A 370    29940  18298  14737  -2933    664   -727  A    O  
ATOM   2548  CB  GLU A 370      20.525   2.891  -1.015  1.00150.52      A    C  
ANISOU 2548  CB  GLU A 370    27424  16198  13569  -2401   -226   -779  A    C  
ATOM   2549  CG  GLU A 370      21.167   2.901   0.373  1.00154.52      A    C  
ANISOU 2549  CG  GLU A 370    28486  16562  13661  -2015   -461   -652  A    C  
ATOM   2550  CD  GLU A 370      21.099   1.555   1.076  1.00154.04      A    C  
ANISOU 2550  CD  GLU A 370    29250  16074  13206  -1999   -226   -413  A    C  
ATOM   2551  OE1 GLU A 370      21.508   0.545   0.468  1.00150.03      A    O  
ANISOU 2551  OE1 GLU A 370    28941  15269  12795  -1969   -215   -327  A    O  
ATOM   2552  OE2 GLU A 370      20.660   1.509   2.246  1.00154.83      A    O1-
ANISOU 2552  OE2 GLU A 370    29842  16112  12875  -1994    -51   -307  A    O1-
ATOM   2553  N   LEU A 371      17.850   4.557  -0.586  1.00115.45      A    N  
ANISOU 2553  N   LEU A 371    22379  12455   9032  -2995    431  -1060  A    N  
ATOM   2554  CA  LEU A 371      17.158   5.524   0.253  1.00128.78      A    C  
ANISOU 2554  CA  LEU A 371    24007  14417  10506  -2958    529  -1159  A    C  
ATOM   2555  C   LEU A 371      15.806   5.001   0.716  1.00144.09      A    C  
ANISOU 2555  C   LEU A 371    26105  16464  12180  -3352   1112  -1150  A    C  
ATOM   2556  O   LEU A 371      15.438   5.187   1.875  1.00157.50      A    O  
ANISOU 2556  O   LEU A 371    28142  18210  13490  -3292   1268  -1115  A    O  
ATOM   2557  CB  LEU A 371      16.980   6.853  -0.478  1.00125.59      A    C  
ANISOU 2557  CB  LEU A 371    22938  14357  10424  -2884    345  -1375  A    C  
ATOM   2558  CG  LEU A 371      16.456   8.033   0.345  1.00125.17      A    C  
ANISOU 2558  CG  LEU A 371    22829  14554  10175  -2724    345  -1512  A    C  
ATOM   2559  CD1 LEU A 371      17.042   9.315  -0.213  1.00120.41      A    C  
ANISOU 2559  CD1 LEU A 371    21824  14054   9874  -2480    -72  -1653  A    C  
ATOM   2560  CD2 LEU A 371      14.926   8.116   0.369  1.00129.27      A    C  
ANISOU 2560  CD2 LEU A 371    23114  15415  10587  -3005    844  -1631  A    C  
ATOM   2561  N   TYR A 372      15.072   4.357  -0.186  1.00144.29      A    N  
ANISOU 2561  N   TYR A 372    25871  16554  12398  -3771   1439  -1201  A    N  
ATOM   2562  CA  TYR A 372      13.738   3.862   0.135  1.00163.92      A    C  
ANISOU 2562  CA  TYR A 372    28396  19212  14675  -4237   2021  -1234  A    C  
ATOM   2563  C   TYR A 372      13.782   2.916   1.343  1.00184.17      A    C  
ANISOU 2563  C   TYR A 372    31788  21414  16772  -4322   2282   -992  A    C  
ATOM   2564  O   TYR A 372      12.960   3.034   2.249  1.00192.97      A    O  
ANISOU 2564  O   TYR A 372    33058  22716  17547  -4471   2644   -993  A    O  
ATOM   2565  CB  TYR A 372      13.103   3.167  -1.074  1.00168.13      A    C  
ANISOU 2565  CB  TYR A 372    28561  19824  15497  -4705   2278  -1340  A    C  
ATOM   2566  CG  TYR A 372      11.667   2.735  -0.843  1.00177.07      A    C  
ANISOU 2566  CG  TYR A 372    29590  21232  16456  -5258   2881  -1435  A    C  
ATOM   2567  CD1 TYR A 372      10.628   3.646  -0.996  1.00180.98      A    C  
ANISOU 2567  CD1 TYR A 372    29432  22334  16998  -5323   3038  -1683  A    C  
ATOM   2568  CD2 TYR A 372      11.347   1.437  -0.464  1.00185.18      A    C  
ANISOU 2568  CD2 TYR A 372    31171  21926  17262  -5712   3300  -1288  A    C  
ATOM   2569  CE1 TYR A 372       9.311   3.280  -0.787  1.00191.69      A    C  
ANISOU 2569  CE1 TYR A 372    30597  24039  18198  -5830   3592  -1806  A    C  
ATOM   2570  CE2 TYR A 372      10.025   1.060  -0.249  1.00191.53      A    C  
ANISOU 2570  CE2 TYR A 372    31835  23025  17913  -6293   3883  -1394  A    C  
ATOM   2571  CZ  TYR A 372       9.013   1.988  -0.413  1.00191.15      A    C  
ANISOU 2571  CZ  TYR A 372    31041  23661  17927  -6352   4025  -1666  A    C  
ATOM   2572  OH  TYR A 372       7.700   1.629  -0.204  1.00189.52      A    O  
ANISOU 2572  OH  TYR A 372    30605  23835  17569  -6930   4607  -1804  A    O  
ATOM   2573  N   ARG A 373      14.733   1.983   1.361  1.00189.06      A    N  
ANISOU 2573  N   ARG A 373    32960  21526  17348  -4196   2109   -781  A    N  
ATOM   2574  CA  ARG A 373      14.830   1.051   2.485  1.00198.08      A    C  
ANISOU 2574  CA  ARG A 373    34984  22266  18013  -4220   2336   -515  A    C  
ATOM   2575  C   ARG A 373      15.308   1.767   3.753  1.00194.04      A    C  
ANISOU 2575  C   ARG A 373    34800  21804  17123  -3744   2087   -442  A    C  
ATOM   2576  O   ARG A 373      14.885   1.426   4.856  1.00207.35      A    O  
ANISOU 2576  O   ARG A 373    37049  23402  18332  -3824   2406   -293  A    O  
ATOM   2577  CB  ARG A 373      15.759  -0.129   2.157  1.00203.88      A    C  
ANISOU 2577  CB  ARG A 373    36264  22423  18776  -4113   2178   -313  A    C  
ATOM   2578  CG  ARG A 373      17.245   0.200   2.122  1.00203.20      A    C  
ANISOU 2578  CG  ARG A 373    36224  22198  18785  -3459   1523   -266  A    C  
ATOM   2579  CD  ARG A 373      18.094  -0.965   2.618  1.00214.31      A    C  
ANISOU 2579  CD  ARG A 373    38502  23027  19899  -3186   1423     12  A    C  
ATOM   2580  NE  ARG A 373      17.751  -1.348   3.986  1.00222.46      A    N  
ANISOU 2580  NE  ARG A 373    40308  23864  20354  -3190   1698    233  A    N  
ATOM   2581  CZ  ARG A 373      18.423  -2.243   4.704  1.00228.00      A    C  
ANISOU 2581  CZ  ARG A 373    41890  24075  20665  -2872   1614    510  A    C  
ATOM   2582  NH1 ARG A 373      19.483  -2.849   4.188  1.00226.32      A    N1+
ANISOU 2582  NH1 ARG A 373    41860  23536  20594  -2496   1249    579  A    N1+
ATOM   2583  NH2 ARG A 373      18.037  -2.531   5.941  1.00234.82      A    N  
ANISOU 2583  NH2 ARG A 373    43464  24787  20969  -2894   1899    721  A    N  
ATOM   2584  N   GLU A 374      16.190   2.752   3.596  1.00176.83      A    N  
ANISOU 2584  N   GLU A 374    32285  19764  15138  -3274   1528   -555  A    N  
ATOM   2585  CA  GLU A 374      16.654   3.549   4.729  1.00172.90      A    C  
ANISOU 2585  CA  GLU A 374    32028  19353  14314  -2837   1239   -555  A    C  
ATOM   2586  C   GLU A 374      15.528   4.433   5.267  1.00183.50      A    C  
ANISOU 2586  C   GLU A 374    33114  21124  15485  -2979   1554   -724  A    C  
ATOM   2587  O   GLU A 374      15.282   4.479   6.472  1.00199.00      A    O  
ANISOU 2587  O   GLU A 374    35548  23101  16960  -2878   1713   -648  A    O  
ATOM   2588  CB  GLU A 374      17.866   4.402   4.336  1.00157.90      A    C  
ANISOU 2588  CB  GLU A 374    29778  17505  12710  -2388    575   -674  A    C  
ATOM   2589  CG  GLU A 374      19.206   3.834   4.790  1.00151.00      A    C  
ANISOU 2589  CG  GLU A 374    29419  16295  11660  -1956    143   -499  A    C  
ATOM   2590  CD  GLU A 374      19.389   3.901   6.297  1.00155.71      A    C  
ANISOU 2590  CD  GLU A 374    30658  16832  11671  -1650     70   -394  A    C  
ATOM   2591  OE1 GLU A 374      18.750   4.764   6.935  1.00153.34      A    O  
ANISOU 2591  OE1 GLU A 374    30270  16809  11183  -1674    191   -526  A    O  
ATOM   2592  OE2 GLU A 374      20.173   3.096   6.846  1.00160.85      A    O1-
ANISOU 2592  OE2 GLU A 374    31922  17169  12024  -1345   -118   -187  A    O1-
ATOM   2593  N   SER A 375      14.847   5.123   4.357  1.00176.58      A    N  
ANISOU 2593  N   SER A 375    31497  20609  14986  -3174   1643   -958  A    N  
ATOM   2594  CA  SER A 375      13.670   5.932   4.677  1.00179.98      A    C  
ANISOU 2594  CA  SER A 375    31583  21501  15300  -3292   1968  -1156  A    C  
ATOM   2595  C   SER A 375      12.503   5.075   5.154  1.00192.12      A    C  
ANISOU 2595  C   SER A 375    33353  23126  16519  -3773   2652  -1075  A    C  
ATOM   2596  O   SER A 375      11.669   5.523   5.944  1.00184.08      A    O  
ANISOU 2596  O   SER A 375    32328  22431  15182  -3801   2969  -1164  A    O  
ATOM   2597  CB  SER A 375      13.235   6.767   3.467  1.00173.36      A    C  
ANISOU 2597  CB  SER A 375    29911  21016  14941  -3350   1884  -1410  A    C  
ATOM   2598  OG  SER A 375      12.727   5.945   2.430  1.00166.53      A    O  
ANISOU 2598  OG  SER A 375    28759  20170  14345  -3791   2159  -1410  A    O  
ATOM   2599  N   GLY A 376      12.459   3.838   4.672  1.00202.97      A    N  
ANISOU 2599  N   GLY A 376    34943  24204  17971  -4162   2891   -918  A    N  
ATOM   2600  CA  GLY A 376      11.350   2.937   4.920  1.00191.79      A    C  
ANISOU 2600  CA  GLY A 376    33703  22839  16330  -4751   3567   -855  A    C  
ATOM   2601  C   GLY A 376      10.265   3.015   3.861  1.00183.24      A    C  
ANISOU 2601  C   GLY A 376    31826  22195  15600  -5217   3873  -1111  A    C  
ATOM   2602  O   GLY A 376      10.380   3.745   2.880  1.00172.58      A    O  
ANISOU 2602  O   GLY A 376    29824  21084  14665  -5047   3551  -1314  A    O  
ATOM   2603  N   ASN A 377       9.190   2.270   4.086  1.00207.18      A    N  
ANISOU 2603  N   ASN A 377    34920  25358  18441  -5816   4507  -1106  A    N  
ATOM   2604  CA  ASN A 377       8.134   2.068   3.093  1.00226.38      A    C  
ANISOU 2604  CA  ASN A 377    36646  28195  21172  -6362   4840  -1351  A    C  
ATOM   2605  C   ASN A 377       7.181   3.223   2.785  1.00230.88      A    C  
ANISOU 2605  C   ASN A 377    36310  29540  21874  -6276   4896  -1699  A    C  
ATOM   2606  O   ASN A 377       6.176   3.017   2.101  1.00236.95      A    O  
ANISOU 2606  O   ASN A 377    36482  30736  22812  -6743   5221  -1921  A    O  
ATOM   2607  CB  ASN A 377       7.287   0.869   3.526  1.00242.95      A    C  
ANISOU 2607  CB  ASN A 377    39127  30191  22993  -7099   5535  -1246  A    C  
ATOM   2608  CG  ASN A 377       8.072  -0.429   3.523  1.00250.44      A    C  
ANISOU 2608  CG  ASN A 377    40937  30339  23881  -7272   5525   -936  A    C  
ATOM   2609  ND2 ASN A 377       8.581  -0.813   4.686  1.00252.25      A    N  
ANISOU 2609  ND2 ASN A 377    42061  30132  23649  -7076   5583   -620  A    N  
ATOM   2610  OD1 ASN A 377       8.221  -1.078   2.488  1.00253.05      A    O  
ANISOU 2610  OD1 ASN A 377    41155  30443  24549  -7540   5457   -985  A    O  
ATOM   2611  N   ASN A 378       7.468   4.429   3.262  1.00228.98      A    N  
ANISOU 2611  N   ASN A 378    35960  29494  21549  -5676   4575  -1770  A    N  
ATOM   2612  CA  ASN A 378       6.471   5.495   3.147  1.00232.15      A    C  
ANISOU 2612  CA  ASN A 378    35612  30612  21982  -5547   4691  -2090  A    C  
ATOM   2613  C   ASN A 378       6.738   6.565   2.080  1.00212.37      A    C  
ANISOU 2613  C   ASN A 378    32476  28311  19904  -5117   4180  -2296  A    C  
ATOM   2614  O   ASN A 378       5.826   6.945   1.346  1.00209.98      A    O  
ANISOU 2614  O   ASN A 378    31441  28555  19785  -5219   4306  -2562  A    O  
ATOM   2615  CB  ASN A 378       6.287   6.173   4.511  1.00249.38      A    C  
ANISOU 2615  CB  ASN A 378    38094  32961  23696  -5209   4814  -2085  A    C  
ATOM   2616  CG  ASN A 378       7.584   6.724   5.068  1.00254.07      A    C  
ANISOU 2616  CG  ASN A 378    39239  33095  24203  -4606   4253  -1929  A    C  
ATOM   2617  ND2 ASN A 378       7.477   7.595   6.065  1.00253.63      A    N  
ANISOU 2617  ND2 ASN A 378    39331  33229  23809  -4204   4229  -2008  A    N  
ATOM   2618  OD1 ASN A 378       8.671   6.367   4.611  1.00256.34      A    O  
ANISOU 2618  OD1 ASN A 378    39798  32886  24713  -4501   3844  -1762  A    O  
ATOM   2619  N   LYS A 379       7.979   7.035   1.984  1.00196.24      A    N  
ANISOU 2619  N   LYS A 379    30714  25846  18002  -4648   3613  -2176  A    N  
ATOM   2620  CA  LYS A 379       8.307   8.184   1.134  1.00176.43      A    C  
ANISOU 2620  CA  LYS A 379    27721  23477  15836  -4212   3139  -2339  A    C  
ATOM   2621  C   LYS A 379       9.429   7.948   0.122  1.00169.78      A    C  
ANISOU 2621  C   LYS A 379    26908  22221  15380  -4143   2689  -2222  A    C  
ATOM   2622  O   LYS A 379      10.360   7.178   0.358  1.00164.25      A    O  
ANISOU 2622  O   LYS A 379    26743  21022  14642  -4186   2559  -1992  A    O  
ATOM   2623  CB  LYS A 379       8.642   9.402   2.001  1.00166.91      A    C  
ANISOU 2623  CB  LYS A 379    26702  22285  14431  -3647   2870  -2394  A    C  
ATOM   2624  CG  LYS A 379       7.444   9.945   2.770  1.00163.39      A    C  
ANISOU 2624  CG  LYS A 379    26050  22375  13655  -3586   3268  -2596  A    C  
ATOM   2625  CD  LYS A 379       6.355  10.420   1.812  1.00150.71      A    C  
ANISOU 2625  CD  LYS A 379    23619  21370  12275  -3623   3411  -2879  A    C  
ATOM   2626  CE  LYS A 379       5.126  10.932   2.552  1.00147.76      A    C  
ANISOU 2626  CE  LYS A 379    22968  21608  11566  -3528   3827  -3110  A    C  
ATOM   2627  NZ  LYS A 379       4.411   9.854   3.295  1.00145.91      A    N1+
ANISOU 2627  NZ  LYS A 379    22894  21544  11001  -4082   4448  -3042  A    N1+
ATOM   2628  N   TRP A 380       9.309   8.631  -1.012  1.00169.31      A    N  
ANISOU 2628  N   TRP A 380    26266  22400  15665  -4003   2462  -2386  A    N  
ATOM   2629  CA  TRP A 380      10.263   8.539  -2.107  1.00164.34      A    C  
ANISOU 2629  CA  TRP A 380    25553  21482  15405  -3932   2069  -2310  A    C  
ATOM   2630  C   TRP A 380      10.984   9.879  -2.241  1.00143.27      A    C  
ANISOU 2630  C   TRP A 380    22808  18751  12877  -3410   1589  -2348  A    C  
ATOM   2631  O   TRP A 380      10.393  10.933  -1.995  1.00144.11      A    O  
ANISOU 2631  O   TRP A 380    22692  19163  12900  -3142   1590  -2514  A    O  
ATOM   2632  CB  TRP A 380       9.545   8.197  -3.412  1.00183.01      A    C  
ANISOU 2632  CB  TRP A 380    27333  24167  18035  -4232   2209  -2463  A    C  
ATOM   2633  CG  TRP A 380       9.205   6.752  -3.587  1.00201.93      A    C  
ANISOU 2633  CG  TRP A 380    29862  26457  20405  -4804   2568  -2413  A    C  
ATOM   2634  CD1 TRP A 380       7.980   6.174  -3.432  1.00212.88      A    C  
ANISOU 2634  CD1 TRP A 380    31033  28205  21646  -5273   3067  -2551  A    C  
ATOM   2635  CD2 TRP A 380      10.096   5.706  -3.981  1.00202.62      A    C  
ANISOU 2635  CD2 TRP A 380    30333  26036  20618  -4979   2462  -2233  A    C  
ATOM   2636  CE2 TRP A 380       9.343   4.516  -4.032  1.00206.94      A    C  
ANISOU 2636  CE2 TRP A 380    30950  26595  21082  -5569   2913  -2264  A    C  
ATOM   2637  CE3 TRP A 380      11.457   5.659  -4.289  1.00197.66      A    C  
ANISOU 2637  CE3 TRP A 380    29988  24959  20155  -4692   2038  -2065  A    C  
ATOM   2638  NE1 TRP A 380       8.055   4.828  -3.691  1.00212.74      A    N  
ANISOU 2638  NE1 TRP A 380    31293  27880  21658  -5776   3284  -2460  A    N  
ATOM   2639  CZ2 TRP A 380       9.910   3.293  -4.380  1.00207.73      A    C  
ANISOU 2639  CZ2 TRP A 380    31466  26209  21253  -5843   2940  -2125  A    C  
ATOM   2640  CZ3 TRP A 380      12.016   4.447  -4.634  1.00195.25      A    C  
ANISOU 2640  CZ3 TRP A 380    30034  24239  19914  -4920   2064  -1934  A    C  
ATOM   2641  CH2 TRP A 380      11.245   3.279  -4.676  1.00202.03      A    C  
ANISOU 2641  CH2 TRP A 380    31027  25055  20680  -5473   2506  -1961  A    C  
ATOM   2642  N   PRO A 381      12.266   9.848  -2.638  1.00122.72      A    N  
ANISOU 2642  N   PRO A 381    20394  15752  10483  -3270   1188  -2206  A    N  
ATOM   2643  CA  PRO A 381      13.055  11.082  -2.688  1.00115.03      A    C  
ANISOU 2643  CA  PRO A 381    19406  14664   9635  -2857    746  -2232  A    C  
ATOM   2644  C   PRO A 381      12.921  11.826  -4.013  1.00125.28      A    C  
ANISOU 2644  C   PRO A 381    20190  16150  11262  -2757    580  -2336  A    C  
ATOM   2645  O   PRO A 381      13.073  11.234  -5.081  1.00144.89      A    O  
ANISOU 2645  O   PRO A 381    22445  18629  13978  -2949    574  -2297  A    O  
ATOM   2646  CB  PRO A 381      14.485  10.579  -2.492  1.00101.42      A    C  
ANISOU 2646  CB  PRO A 381    18083  12488   7965  -2804    431  -2040  A    C  
ATOM   2647  CG  PRO A 381      14.479   9.201  -3.088  1.00 98.00      A    C  
ANISOU 2647  CG  PRO A 381    17670  11947   7617  -3144    631  -1932  A    C  
ATOM   2648  CD  PRO A 381      13.063   8.665  -3.009  1.00108.50      A    C  
ANISOU 2648  CD  PRO A 381    18847  13587   8792  -3484   1137  -2027  A    C  
ATOM   2649  N   LEU A 382      12.633  13.120  -3.934  1.00112.81      A    N  
ANISOU 2649  N   LEU A 382    18478  14716   9671  -2434    449  -2468  A    N  
ATOM   2650  CA  LEU A 382      12.499  13.945  -5.128  1.00112.10      A    C  
ANISOU 2650  CA  LEU A 382    17986  14769   9838  -2274    282  -2544  A    C  
ATOM   2651  C   LEU A 382      13.854  14.199  -5.786  1.00115.23      A    C  
ANISOU 2651  C   LEU A 382    18469  14802  10509  -2220   -106  -2406  A    C  
ATOM   2652  O   LEU A 382      14.857  14.387  -5.099  1.00123.10      A    O  
ANISOU 2652  O   LEU A 382    19818  15478  11478  -2139   -346  -2328  A    O  
ATOM   2653  CB  LEU A 382      11.812  15.267  -4.776  1.00103.53      A    C  
ANISOU 2653  CB  LEU A 382    16833  13880   8623  -1895    257  -2718  A    C  
ATOM   2654  CG  LEU A 382      11.636  16.316  -5.871  1.00 98.17      A    C  
ANISOU 2654  CG  LEU A 382    15856  13301   8141  -1624     68  -2785  A    C  
ATOM   2655  CD1 LEU A 382      10.336  17.042  -5.653  1.00 98.86      A    C  
ANISOU 2655  CD1 LEU A 382    15718  13811   8033  -1324    252  -3004  A    C  
ATOM   2656  CD2 LEU A 382      12.783  17.305  -5.857  1.00101.28      A    C  
ANISOU 2656  CD2 LEU A 382    16562  13252   8670  -1418   -327  -2707  A    C  
ATOM   2657  N   ILE A 383      13.875  14.212  -7.117  1.00103.55      A    N  
ANISOU 2657  N   ILE A 383    16647  13418   9278  -2268   -165  -2391  A    N  
ATOM   2658  CA  ILE A 383      15.103  14.476  -7.859  1.00 98.81      A    C  
ANISOU 2658  CA  ILE A 383    16067  12540   8937  -2241   -482  -2265  A    C  
ATOM   2659  C   ILE A 383      14.951  15.695  -8.758  1.00112.24      A    C  
ANISOU 2659  C   ILE A 383    17558  14313  10775  -2012   -632  -2305  A    C  
ATOM   2660  O   ILE A 383      13.994  15.794  -9.528  1.00122.20      A    O  
ANISOU 2660  O   ILE A 383    18492  15901  12038  -1960   -491  -2390  A    O  
ATOM   2661  CB  ILE A 383      15.525  13.280  -8.729  1.00 91.36      A    C  
ANISOU 2661  CB  ILE A 383    14987  11571   8154  -2509   -430  -2169  A    C  
ATOM   2662  CG1 ILE A 383      15.430  11.973  -7.947  1.00 88.56      A    C  
ANISOU 2662  CG1 ILE A 383    14876  11140   7634  -2741   -215  -2130  A    C  
ATOM   2663  CG2 ILE A 383      16.940  13.468  -9.230  1.00101.38      A    C  
ANISOU 2663  CG2 ILE A 383    16311  12562   9645  -2476   -739  -2040  A    C  
ATOM   2664  CD1 ILE A 383      15.385  10.751  -8.832  1.00 86.26      A    C  
ANISOU 2664  CD1 ILE A 383    14444  10878   7454  -3018    -65  -2101  A    C  
ATOM   2665  N   LEU A 384      15.905  16.616  -8.667  1.00115.88      A    N  
ANISOU 2665  N   LEU A 384    18223  14467  11339  -1881   -924  -2247  A    N  
ATOM   2666  CA  LEU A 384      15.896  17.799  -9.520  1.00113.83      A    C  
ANISOU 2666  CA  LEU A 384    17878  14171  11202  -1684  -1067  -2244  A    C  
ATOM   2667  C   LEU A 384      16.983  17.765 -10.582  1.00104.77      A    C  
ANISOU 2667  C   LEU A 384    16636  12857  10314  -1829  -1235  -2089  A    C  
ATOM   2668  O   LEU A 384      18.180  17.748 -10.281  1.00 83.39      A    O  
ANISOU 2668  O   LEU A 384    14088   9882   7713  -1951  -1427  -2013  A    O  
ATOM   2669  CB  LEU A 384      16.017  19.066  -8.676  1.00129.26      A    C  
ANISOU 2669  CB  LEU A 384    20168  15886  13061  -1441  -1234  -2321  A    C  
ATOM   2670  CG  LEU A 384      14.682  19.424  -8.023  1.00132.32      A    C  
ANISOU 2670  CG  LEU A 384    20557  16532  13186  -1174  -1042  -2500  A    C  
ATOM   2671  CD1 LEU A 384      14.884  20.124  -6.705  1.00124.89      A    C  
ANISOU 2671  CD1 LEU A 384    20027  15357  12068  -1013  -1154  -2604  A    C  
ATOM   2672  CD2 LEU A 384      13.854  20.287  -8.960  1.00128.51      A    C  
ANISOU 2672  CD2 LEU A 384    19883  16229  12715   -873  -1023  -2552  A    C  
ATOM   2673  N   LEU A 385      16.531  17.757 -11.832  1.00115.40      A    N  
ANISOU 2673  N   LEU A 385    17695  14414  11737  -1802  -1159  -2060  A    N  
ATOM   2674  CA  LEU A 385      17.404  17.705 -12.991  1.00122.51      A    C  
ANISOU 2674  CA  LEU A 385    18471  15232  12846  -1923  -1260  -1916  A    C  
ATOM   2675  C   LEU A 385      16.918  18.717 -14.017  1.00126.41      A    C  
ANISOU 2675  C   LEU A 385    18886  15800  13344  -1700  -1285  -1885  A    C  
ATOM   2676  O   LEU A 385      15.724  19.024 -14.082  1.00102.45      A    O  
ANISOU 2676  O   LEU A 385    15750  13020  10155  -1461  -1185  -1996  A    O  
ATOM   2677  CB  LEU A 385      17.415  16.300 -13.596  1.00108.15      A    C  
ANISOU 2677  CB  LEU A 385    16402  13614  11078  -2143  -1117  -1899  A    C  
ATOM   2678  CG  LEU A 385      18.643  15.427 -13.350  1.00 87.83      A    C  
ANISOU 2678  CG  LEU A 385    13910  10844   8618  -2352  -1197  -1813  A    C  
ATOM   2679  CD1 LEU A 385      18.405  14.020 -13.869  1.00 83.16      A    C  
ANISOU 2679  CD1 LEU A 385    13147  10423   8029  -2523  -1021  -1834  A    C  
ATOM   2680  CD2 LEU A 385      19.867  16.040 -13.996  1.00 79.02      A    C  
ANISOU 2680  CD2 LEU A 385    12781   9549   7694  -2384  -1391  -1687  A    C  
ATOM   2681  N   HIS A 386      17.843  19.246 -14.807  1.00136.61      A    N  
ANISOU 2681  N   HIS A 386    20228  16887  14792  -1762  -1414  -1733  A    N  
ATOM   2682  CA  HIS A 386      17.490  20.234 -15.813  1.00148.77      A    C  
ANISOU 2682  CA  HIS A 386    21787  18432  16308  -1543  -1440  -1656  A    C  
ATOM   2683  C   HIS A 386      16.633  19.591 -16.895  1.00139.36      A    C  
ANISOU 2683  C   HIS A 386    20240  17668  15041  -1465  -1303  -1685  A    C  
ATOM   2684  O   HIS A 386      16.690  18.379 -17.097  1.00145.96      A    O  
ANISOU 2684  O   HIS A 386    20834  18706  15918  -1683  -1202  -1724  A    O  
ATOM   2685  CB  HIS A 386      18.738  20.861 -16.421  1.00164.19      A    C  
ANISOU 2685  CB  HIS A 386    23886  20065  18431  -1707  -1562  -1469  A    C  
ATOM   2686  CG  HIS A 386      18.484  22.179 -17.080  1.00187.64      A    C  
ANISOU 2686  CG  HIS A 386    27092  22857  21343  -1471  -1611  -1367  A    C  
ATOM   2687  CD2 HIS A 386      18.549  23.442 -16.599  1.00195.58      A    C  
ANISOU 2687  CD2 HIS A 386    28509  23485  22319  -1335  -1720  -1359  A    C  
ATOM   2688  ND1 HIS A 386      18.105  22.291 -18.401  1.00202.83      A    N  
ANISOU 2688  ND1 HIS A 386    28893  24971  23205  -1326  -1547  -1256  A    N  
ATOM   2689  CE1 HIS A 386      17.949  23.567 -18.705  1.00209.79      A    C  
ANISOU 2689  CE1 HIS A 386    30117  25585  24009  -1091  -1610  -1158  A    C  
ATOM   2690  NE2 HIS A 386      18.214  24.287 -17.629  1.00207.99      A    N  
ANISOU 2690  NE2 HIS A 386    30230  24988  23811  -1102  -1710  -1222  A    N  
ATOM   2691  N   LYS A 387      15.838  20.399 -17.588  1.00124.81      A    N  
ANISOU 2691  N   LYS A 387    18391  15957  13072  -1136  -1312  -1680  A    N  
ATOM   2692  CA  LYS A 387      15.069  19.895 -18.719  1.00107.05      A    C  
ANISOU 2692  CA  LYS A 387    15796  14149  10731  -1037  -1229  -1721  A    C  
ATOM   2693  C   LYS A 387      15.981  19.323 -19.788  1.00114.45      A    C  
ANISOU 2693  C   LYS A 387    16622  15071  11795  -1289  -1224  -1572  A    C  
ATOM   2694  O   LYS A 387      15.642  18.320 -20.412  1.00130.97      A    O  
ANISOU 2694  O   LYS A 387    18400  17500  13861  -1397  -1133  -1657  A    O  
ATOM   2695  CB  LYS A 387      14.192  20.987 -19.325  1.00 98.23      A    C  
ANISOU 2695  CB  LYS A 387    14741  13155   9428   -565  -1291  -1716  A    C  
ATOM   2696  CG  LYS A 387      13.098  21.473 -18.407  1.00102.59      A    C  
ANISOU 2696  CG  LYS A 387    15314  13852   9815   -231  -1274  -1912  A    C  
ATOM   2697  CD  LYS A 387      12.203  22.458 -19.125  1.00118.33      A    C  
ANISOU 2697  CD  LYS A 387    17337  16025  11600    317  -1352  -1919  A    C  
ATOM   2698  CE  LYS A 387      11.390  21.756 -20.189  1.00112.39      A    C  
ANISOU 2698  CE  LYS A 387    16097  15874  10731    395  -1304  -2021  A    C  
ATOM   2699  NZ  LYS A 387      10.508  20.738 -19.562  1.00108.85      A    N1+
ANISOU 2699  NZ  LYS A 387    15205  15910  10244    233  -1148  -2304  A    N1+
ATOM   2700  N   ARG A 388      17.130  19.959 -20.001  1.00105.36      A    N  
ANISOU 2700  N   ARG A 388    15721  13543  10770  -1397  -1309  -1371  A    N  
ATOM   2701  CA  ARG A 388      18.116  19.428 -20.935  1.00112.40      A    C  
ANISOU 2701  CA  ARG A 388    16493  14435  11780  -1643  -1280  -1234  A    C  
ATOM   2702  C   ARG A 388      18.467  17.982 -20.605  1.00103.28      A    C  
ANISOU 2702  C   ARG A 388    15109  13409  10724  -1922  -1208  -1342  A    C  
ATOM   2703  O   ARG A 388      18.446  17.119 -21.478  1.00108.08      A    O  
ANISOU 2703  O   ARG A 388    15481  14265  11319  -2000  -1128  -1368  A    O  
ATOM   2704  CB  ARG A 388      19.381  20.274 -20.971  1.00127.02      A    C  
ANISOU 2704  CB  ARG A 388    18611  15877  13773  -1805  -1356  -1034  A    C  
ATOM   2705  CG  ARG A 388      20.213  19.934 -22.194  1.00147.90      A    C  
ANISOU 2705  CG  ARG A 388    21108  18610  16478  -1976  -1288   -880  A    C  
ATOM   2706  CD  ARG A 388      21.424  20.829 -22.331  1.00165.09      A    C  
ANISOU 2706  CD  ARG A 388    23508  20433  18785  -2186  -1321   -682  A    C  
ATOM   2707  NE  ARG A 388      21.045  22.237 -22.283  1.00174.76      A    N  
ANISOU 2707  NE  ARG A 388    25130  21354  19916  -1995  -1378   -581  A    N  
ATOM   2708  CZ  ARG A 388      21.004  23.036 -23.345  1.00178.80      A    C  
ANISOU 2708  CZ  ARG A 388    25841  21786  20310  -1878  -1327   -377  A    C  
ATOM   2709  NH1 ARG A 388      21.333  22.568 -24.545  1.00175.41      A    N1+
ANISOU 2709  NH1 ARG A 388    25213  21600  19835  -1948  -1213   -258  A    N1+
ATOM   2710  NH2 ARG A 388      20.645  24.307 -23.209  1.00183.84      A    N  
ANISOU 2710  NH2 ARG A 388    26922  22081  20850  -1671  -1386   -288  A    N  
ATOM   2711  N   ARG A 389      18.809  17.724 -19.350  1.00103.35      A    N  
ANISOU 2711  N   ARG A 389    15233  13227  10808  -2050  -1242  -1407  A    N  
ATOM   2712  CA  ARG A 389      19.115  16.366 -18.920  1.00109.89      A    C  
ANISOU 2712  CA  ARG A 389    15941  14116  11696  -2264  -1179  -1493  A    C  
ATOM   2713  C   ARG A 389      17.892  15.460 -19.016  1.00106.31      A    C  
ANISOU 2713  C   ARG A 389    15286  13996  11112  -2254  -1028  -1670  A    C  
ATOM   2714  O   ARG A 389      17.994  14.306 -19.432  1.00111.80      A    O  
ANISOU 2714  O   ARG A 389    15836  14812  11831  -2419   -939  -1726  A    O  
ATOM   2715  CB  ARG A 389      19.620  16.369 -17.481  1.00120.04      A    C  
ANISOU 2715  CB  ARG A 389    17447  15138  13026  -2342  -1263  -1521  A    C  
ATOM   2716  CG  ARG A 389      21.047  16.822 -17.273  1.00126.28      A    C  
ANISOU 2716  CG  ARG A 389    18353  15651  13976  -2466  -1420  -1405  A    C  
ATOM   2717  CD  ARG A 389      22.010  15.773 -17.792  1.00114.49      A    C  
ANISOU 2717  CD  ARG A 389    16676  14228  12598  -2625  -1401  -1365  A    C  
ATOM   2718  NE  ARG A 389      23.396  16.127 -17.513  1.00114.82      A    N  
ANISOU 2718  NE  ARG A 389    16745  14091  12790  -2750  -1553  -1293  A    N  
ATOM   2719  CZ  ARG A 389      24.160  16.831 -18.335  1.00117.19      A    C  
ANISOU 2719  CZ  ARG A 389    16964  14362  13199  -2847  -1576  -1172  A    C  
ATOM   2720  NH1 ARG A 389      23.664  17.248 -19.488  1.00125.33      A    N1+
ANISOU 2720  NH1 ARG A 389    17941  15499  14178  -2787  -1462  -1085  A    N1+
ATOM   2721  NH2 ARG A 389      25.412  17.115 -18.003  1.00108.99      A    N  
ANISOU 2721  NH2 ARG A 389    15895  13213  12302  -3009  -1708  -1144  A    N  
ATOM   2722  N   VAL A 390      16.737  15.994 -18.635  1.00 98.26      A    N  
ANISOU 2722  N   VAL A 390    14256  13131   9948  -2066   -996  -1778  A    N  
ATOM   2723  CA  VAL A 390      15.498  15.232 -18.660  1.00103.44      A    C  
ANISOU 2723  CA  VAL A 390    14663  14164  10474  -2094   -840  -1980  A    C  
ATOM   2724  C   VAL A 390      15.072  14.890 -20.091  1.00119.39      A    C  
ANISOU 2724  C   VAL A 390    16390  16527  12446  -2070   -808  -2029  A    C  
ATOM   2725  O   VAL A 390      14.664  13.761 -20.370  1.00124.53      A    O  
ANISOU 2725  O   VAL A 390    16841  17399  13077  -2281   -687  -2176  A    O  
ATOM   2726  CB  VAL A 390      14.371  16.003 -17.938  1.00 97.66      A    C  
ANISOU 2726  CB  VAL A 390    13933  13589   9584  -1846   -814  -2102  A    C  
ATOM   2727  CG1 VAL A 390      12.999  15.470 -18.318  1.00100.59      A    C  
ANISOU 2727  CG1 VAL A 390    13927  14483   9811  -1834   -667  -2327  A    C  
ATOM   2728  CG2 VAL A 390      14.578  15.939 -16.429  1.00 89.48      A    C  
ANISOU 2728  CG2 VAL A 390    13153  12306   8541  -1930   -786  -2123  A    C  
ATOM   2729  N   LYS A 391      15.200  15.851 -21.001  1.00121.73      A    N  
ANISOU 2729  N   LYS A 391    16703  16842  12706  -1825   -918  -1905  A    N  
ATOM   2730  CA  LYS A 391      14.797  15.641 -22.390  1.00110.65      A    C  
ANISOU 2730  CA  LYS A 391    15053  15785  11203  -1742   -915  -1943  A    C  
ATOM   2731  C   LYS A 391      15.674  14.605 -23.086  1.00103.33      A    C  
ANISOU 2731  C   LYS A 391    14066  14814  10381  -2013   -867  -1909  A    C  
ATOM   2732  O   LYS A 391      15.164  13.738 -23.791  1.00129.43      A    O  
ANISOU 2732  O   LYS A 391    17131  18432  13616  -2109   -802  -2073  A    O  
ATOM   2733  CB  LYS A 391      14.824  16.958 -23.169  1.00107.47      A    C  
ANISOU 2733  CB  LYS A 391    14783  15349  10701  -1390  -1038  -1770  A    C  
ATOM   2734  CG  LYS A 391      13.591  17.820 -22.953  1.00110.14      A    C  
ANISOU 2734  CG  LYS A 391    15081  15919  10849   -995  -1090  -1875  A    C  
ATOM   2735  CD  LYS A 391      13.507  18.941 -23.975  1.00113.76      A    C  
ANISOU 2735  CD  LYS A 391    15689  16384  11151   -600  -1209  -1706  A    C  
ATOM   2736  CE  LYS A 391      12.367  19.890 -23.639  1.00122.76      A    C  
ANISOU 2736  CE  LYS A 391    16853  17695  12096   -118  -1284  -1805  A    C  
ATOM   2737  NZ  LYS A 391      11.076  19.168 -23.468  1.00124.96      A    N1+
ANISOU 2737  NZ  LYS A 391    16654  18571  12254    -74  -1223  -2134  A    N1+
ATOM   2738  N   THR A 392      16.988  14.699 -22.891  1.00 78.72      A    N  
ANISOU 2738  N   THR A 392    11155  11331   7424  -2129   -905  -1723  A    N  
ATOM   2739  CA  THR A 392      17.928  13.733 -23.463  1.00 77.65      A    C  
ANISOU 2739  CA  THR A 392    10967  11150   7387  -2331   -859  -1697  A    C  
ATOM   2740  C   THR A 392      17.655  12.339 -22.916  1.00105.22      A    C  
ANISOU 2740  C   THR A 392    14406  14667  10905  -2561   -753  -1889  A    C  
ATOM   2741  O   THR A 392      17.803  11.337 -23.616  1.00 91.47      A    O  
ANISOU 2741  O   THR A 392    12565  13029   9160  -2683   -686  -1981  A    O  
ATOM   2742  CB  THR A 392      19.387  14.118 -23.182  1.00 98.11      A    C  
ANISOU 2742  CB  THR A 392    13734  13397  10148  -2405   -924  -1494  A    C  
ATOM   2743  CG2 THR A 392      20.337  13.063 -23.729  1.00 89.62      A    C  
ANISOU 2743  CG2 THR A 392    12567  12326   9157  -2553   -870  -1498  A    C  
ATOM   2744  OG1 THR A 392      19.677  15.373 -23.808  1.00102.91      A    O  
ANISOU 2744  OG1 THR A 392    14430  13944  10726  -2265   -983  -1304  A    O  
ATOM   2745  N   LEU A 393      17.270  12.282 -21.647  1.00112.38      A    N  
ANISOU 2745  N   LEU A 393    15431  15450  11820  -2620   -728  -1948  A    N  
ATOM   2746  CA  LEU A 393      16.870  11.025 -21.030  1.00110.28      A    C  
ANISOU 2746  CA  LEU A 393    15185  15174  11541  -2857   -592  -2110  A    C  
ATOM   2747  C   LEU A 393      15.567  10.497 -21.638  1.00 98.27      A    C  
ANISOU 2747  C   LEU A 393    13393  14057   9889  -2950   -474  -2347  A    C  
ATOM   2748  O   LEU A 393      15.425   9.297 -21.859  1.00 97.09      A    O  
ANISOU 2748  O   LEU A 393    13220  13933   9737  -3196   -359  -2490  A    O  
ATOM   2749  CB  LEU A 393      16.724  11.207 -19.520  1.00116.82      A    C  
ANISOU 2749  CB  LEU A 393    16226  15800  12359  -2882   -575  -2097  A    C  
ATOM   2750  CG  LEU A 393      17.895  10.650 -18.710  1.00121.02      A    C  
ANISOU 2750  CG  LEU A 393    17038  15952  12991  -2967   -621  -1989  A    C  
ATOM   2751  CD1 LEU A 393      17.963   9.153 -18.871  1.00128.73      A    C  
ANISOU 2751  CD1 LEU A 393    18074  16872  13968  -3179   -490  -2081  A    C  
ATOM   2752  CD2 LEU A 393      19.213  11.288 -19.149  1.00122.07      A    C  
ANISOU 2752  CD2 LEU A 393    17193  15929  13260  -2848   -794  -1812  A    C  
ATOM   2753  N   LEU A 394      14.627  11.399 -21.910  1.00 80.24      A    N  
ANISOU 2753  N   LEU A 394    10911  12090   7486  -2743   -514  -2404  A    N  
ATOM   2754  CA  LEU A 394      13.377  11.058 -22.585  1.00 89.87      A    C  
ANISOU 2754  CA  LEU A 394    11786  13798   8564  -2782   -449  -2656  A    C  
ATOM   2755  C   LEU A 394      13.623  10.521 -23.995  1.00116.53      A    C  
ANISOU 2755  C   LEU A 394    15022  17340  11912  -2818   -485  -2711  A    C  
ATOM   2756  O   LEU A 394      12.911   9.637 -24.474  1.00109.54      A    O  
ANISOU 2756  O   LEU A 394    13920  16743  10956  -3031   -404  -2963  A    O  
ATOM   2757  CB  LEU A 394      12.456  12.277 -22.659  1.00100.13      A    C  
ANISOU 2757  CB  LEU A 394    12909  15418   9721  -2425   -536  -2685  A    C  
ATOM   2758  CG  LEU A 394      11.653  12.648 -21.410  1.00 96.84      A    C  
ANISOU 2758  CG  LEU A 394    12481  15068   9248  -2381   -454  -2774  A    C  
ATOM   2759  CD1 LEU A 394      10.581  13.682 -21.744  1.00105.14      A    C  
ANISOU 2759  CD1 LEU A 394    13276  16554  10119  -1972   -541  -2875  A    C  
ATOM   2760  CD2 LEU A 394      11.041  11.416 -20.755  1.00 88.24      A    C  
ANISOU 2760  CD2 LEU A 394    11283  14091   8153  -2806   -227  -2991  A    C  
ATOM   2761  N   GLU A 395      14.630  11.082 -24.657  1.00135.29      A    N  
ANISOU 2761  N   GLU A 395    17528  19546  14332  -2630   -596  -2487  A    N  
ATOM   2762  CA  GLU A 395      14.977  10.703 -26.021  1.00132.30      A    C  
ANISOU 2762  CA  GLU A 395    17051  19325  13894  -2611   -624  -2507  A    C  
ATOM   2763  C   GLU A 395      15.480   9.266 -26.082  1.00136.71      A    C  
ANISOU 2763  C   GLU A 395    17683  19722  14540  -2920   -516  -2629  A    C  
ATOM   2764  O   GLU A 395      15.244   8.565 -27.061  1.00150.80      A    O  
ANISOU 2764  O   GLU A 395    19330  21733  16234  -3000   -494  -2807  A    O  
ATOM   2765  CB  GLU A 395      16.039  11.649 -26.581  1.00125.19      A    C  
ANISOU 2765  CB  GLU A 395    16304  18243  13019  -2382   -717  -2210  A    C  
ATOM   2766  CG  GLU A 395      15.492  12.911 -27.230  1.00118.35      A    C  
ANISOU 2766  CG  GLU A 395    15388  17604  11976  -2032   -826  -2112  A    C  
ATOM   2767  CD  GLU A 395      16.596  13.869 -27.631  1.00123.78      A    C  
ANISOU 2767  CD  GLU A 395    16308  18022  12702  -1892   -871  -1788  A    C  
ATOM   2768  OE1 GLU A 395      17.727  13.401 -27.891  1.00126.04      A    O  
ANISOU 2768  OE1 GLU A 395    16657  18127  13103  -2055   -815  -1692  A    O  
ATOM   2769  OE2 GLU A 395      16.336  15.089 -27.681  1.00125.79      A    O1-
ANISOU 2769  OE2 GLU A 395    16690  18243  12864  -1623   -952  -1637  A    O1-
ATOM   2770  N   ASN A 396      16.178   8.828 -25.038  1.00125.90      A    N  
ANISOU 2770  N   ASN A 396    16561  17951  13323  -3063   -461  -2542  A    N  
ATOM   2771  CA  ASN A 396      16.639   7.448 -24.979  1.00117.57      A    C  
ANISOU 2771  CA  ASN A 396    15659  16680  12332  -3303   -360  -2647  A    C  
ATOM   2772  C   ASN A 396      15.451   6.518 -24.767  1.00116.40      A    C  
ANISOU 2772  C   ASN A 396    15432  16686  12109  -3613   -221  -2939  A    C  
ATOM   2773  O   ASN A 396      14.666   6.712 -23.840  1.00111.85      A    O  
ANISOU 2773  O   ASN A 396    14832  16157  11511  -3714   -152  -2986  A    O  
ATOM   2774  CB  ASN A 396      17.675   7.257 -23.869  1.00114.26      A    C  
ANISOU 2774  CB  ASN A 396    15548  15810  12058  -3312   -365  -2472  A    C  
ATOM   2775  CG  ASN A 396      18.444   5.948 -24.005  1.00107.91      A    C  
ANISOU 2775  CG  ASN A 396    14948  14749  11305  -3417   -303  -2530  A    C  
ATOM   2776  ND2 ASN A 396      19.765   6.047 -24.060  1.00101.33      A    N  
ANISOU 2776  ND2 ASN A 396    14205  13727  10568  -3242   -386  -2361  A    N  
ATOM   2777  OD1 ASN A 396      17.859   4.866 -24.058  1.00106.38      A    O  
ANISOU 2777  OD1 ASN A 396    14833  14528  11060  -3653   -179  -2737  A    O  
ATOM   2778  N   PRO A 397      15.311   5.511 -25.642  1.00125.53      A    N  
ANISOU 2778  N   PRO A 397    16546  17935  13214  -3786   -165  -3153  A    N  
ATOM   2779  CA  PRO A 397      14.183   4.573 -25.629  1.00132.93      A    C  
ANISOU 2779  CA  PRO A 397    17386  19041  14078  -4161    -25  -3475  A    C  
ATOM   2780  C   PRO A 397      14.183   3.687 -24.389  1.00125.04      A    C  
ANISOU 2780  C   PRO A 397    16728  17631  13152  -4473    153  -3480  A    C  
ATOM   2781  O   PRO A 397      13.117   3.383 -23.847  1.00133.36      A    O  
ANISOU 2781  O   PRO A 397    17690  18828  14153  -4786    302  -3657  A    O  
ATOM   2782  CB  PRO A 397      14.405   3.741 -26.893  1.00148.99      A    C  
ANISOU 2782  CB  PRO A 397    19403  21153  16054  -4228    -38  -3667  A    C  
ATOM   2783  CG  PRO A 397      15.873   3.843 -27.161  1.00143.42      A    C  
ANISOU 2783  CG  PRO A 397    18923  20141  15431  -3945   -112  -3419  A    C  
ATOM   2784  CD  PRO A 397      16.251   5.229 -26.741  1.00128.16      A    C  
ANISOU 2784  CD  PRO A 397    16919  18232  13546  -3643   -223  -3118  A    C  
ATOM   2785  N   THR A 398      15.375   3.287 -23.954  1.00123.18      A    N  
ANISOU 2785  N   THR A 398    16876  16912  13013  -4374    142  -3286  A    N  
ATOM   2786  CA  THR A 398      15.550   2.444 -22.775  1.00133.03      A    C  
ANISOU 2786  CA  THR A 398    18546  17705  14293  -4583    286  -3238  A    C  
ATOM   2787  C   THR A 398      14.940   3.083 -21.528  1.00125.81      A    C  
ANISOU 2787  C   THR A 398    17623  16827  13350  -4634    350  -3145  A    C  
ATOM   2788  O   THR A 398      14.108   2.486 -20.839  1.00118.75      A    O  
ANISOU 2788  O   THR A 398    16834  15894  12392  -4986    558  -3266  A    O  
ATOM   2789  CB  THR A 398      17.053   2.175 -22.494  1.00 87.39      A    C  
ANISOU 2789  CB  THR A 398    13124  11477   8601  -4313    189  -3013  A    C  
ATOM   2790  CG2 THR A 398      17.228   1.153 -21.380  1.00 98.60      A    C  
ANISOU 2790  CG2 THR A 398    15055  12405  10003  -4483    325  -2971  A    C  
ATOM   2791  OG1 THR A 398      17.716   1.734 -23.686  1.00 85.57      A    O  
ANISOU 2791  OG1 THR A 398    12862  11265   8386  -4183    127  -3087  A    O  
ATOM   2792  N   HIS A 399      15.366   4.314 -21.261  1.00117.75      A    N  
ANISOU 2792  N   HIS A 399    16490  15881  12367  -4293    186  -2939  A    N  
ATOM   2793  CA  HIS A 399      15.035   5.016 -20.028  1.00110.41      A    C  
ANISOU 2793  CA  HIS A 399    15618  14926  11404  -4247    211  -2829  A    C  
ATOM   2794  C   HIS A 399      13.653   5.676 -19.996  1.00118.31      A    C  
ANISOU 2794  C   HIS A 399    16242  16406  12305  -4311    285  -2991  A    C  
ATOM   2795  O   HIS A 399      13.115   5.916 -18.917  1.00132.18      A    O  
ANISOU 2795  O   HIS A 399    18058  18169  13994  -4375    395  -2980  A    O  
ATOM   2796  CB  HIS A 399      16.102   6.082 -19.762  1.00103.43      A    C  
ANISOU 2796  CB  HIS A 399    14799  13896  10603  -3871    -10  -2572  A    C  
ATOM   2797  CG  HIS A 399      17.508   5.582 -19.915  1.00107.43      A    C  
ANISOU 2797  CG  HIS A 399    15549  14061  11209  -3747   -114  -2436  A    C  
ATOM   2798  CD2 HIS A 399      18.616   6.181 -20.416  1.00 93.93      A    C  
ANISOU 2798  CD2 HIS A 399    13771  12319   9598  -3489   -295  -2286  A    C  
ATOM   2799  ND1 HIS A 399      17.893   4.319 -19.529  1.00119.82      A    N  
ANISOU 2799  ND1 HIS A 399    17470  15289  12768  -3883    -20  -2456  A    N  
ATOM   2800  CE1 HIS A 399      19.184   4.158 -19.780  1.00115.40      A    C  
ANISOU 2800  CE1 HIS A 399    17019  14534  12294  -3656   -160  -2338  A    C  
ATOM   2801  NE2 HIS A 399      19.643   5.272 -20.317  1.00 95.26      A    N  
ANISOU 2801  NE2 HIS A 399    14186  12190   9817  -3446   -317  -2240  A    N  
ATOM   2802  N   ARG A 400      13.085   5.958 -21.167  1.00113.01      A    N  
ANISOU 2802  N   ARG A 400    15181  16162  11597  -4260    221  -3151  A    N  
ATOM   2803  CA  ARG A 400      11.912   6.835 -21.267  1.00119.35      A    C  
ANISOU 2803  CA  ARG A 400    15573  17483  12292  -4150    211  -3285  A    C  
ATOM   2804  C   ARG A 400      10.723   6.446 -20.382  1.00138.44      A    C  
ANISOU 2804  C   ARG A 400    17872  20112  14618  -4474    454  -3482  A    C  
ATOM   2805  O   ARG A 400      10.106   7.313 -19.757  1.00144.36      A    O  
ANISOU 2805  O   ARG A 400    18463  21096  15292  -4295    465  -3482  A    O  
ATOM   2806  CB  ARG A 400      11.440   6.926 -22.720  1.00120.23      A    C  
ANISOU 2806  CB  ARG A 400    15301  18046  12335  -4073    106  -3468  A    C  
ATOM   2807  CG  ARG A 400      10.268   7.878 -22.904  1.00120.37      A    C  
ANISOU 2807  CG  ARG A 400    14882  18640  12214  -3852     48  -3609  A    C  
ATOM   2808  CD  ARG A 400      10.063   8.289 -24.350  1.00114.57      A    C  
ANISOU 2808  CD  ARG A 400    13847  18307  11376  -3594   -141  -3694  A    C  
ATOM   2809  NE  ARG A 400       9.042   9.327 -24.492  1.00119.97      A    N  
ANISOU 2809  NE  ARG A 400    14164  19516  11903  -3251   -241  -3790  A    N  
ATOM   2810  CZ  ARG A 400       7.743   9.138 -24.274  1.00131.72      A    C  
ANISOU 2810  CZ  ARG A 400    15237  21526  13283  -3397   -144  -4100  A    C  
ATOM   2811  NH1 ARG A 400       7.287   7.940 -23.933  1.00124.07      A    N1+
ANISOU 2811  NH1 ARG A 400    14187  20601  12352  -3958     78  -4341  A    N1+
ATOM   2812  NH2 ARG A 400       6.893  10.145 -24.417  1.00146.47      A    N  
ANISOU 2812  NH2 ARG A 400    16776  23883  14995  -2980   -263  -4179  A    N  
ATOM   2813  N   ASN A 401      10.399   5.158 -20.324  1.00155.79      A    N  
ANISOU 2813  N   ASN A 401    20162  22221  16810  -4956    666  -3655  A    N  
ATOM   2814  CA  ASN A 401       9.271   4.709 -19.509  1.00169.06      A    C  
ANISOU 2814  CA  ASN A 401    21728  24110  18396  -5357    951  -3845  A    C  
ATOM   2815  C   ASN A 401       9.500   4.973 -18.023  1.00167.23      A    C  
ANISOU 2815  C   ASN A 401    21847  23565  18128  -5306   1067  -3632  A    C  
ATOM   2816  O   ASN A 401       8.582   5.370 -17.306  1.00170.57      A    O  
ANISOU 2816  O   ASN A 401    22060  24310  18440  -5357   1223  -3725  A    O  
ATOM   2817  CB  ASN A 401       8.986   3.221 -19.742  1.00178.86      A    C  
ANISOU 2817  CB  ASN A 401    23105  25210  19642  -5948   1175  -4054  A    C  
ATOM   2818  CG  ASN A 401      10.185   2.340 -19.450  1.00180.15      A    C  
ANISOU 2818  CG  ASN A 401    23919  24644  19885  -6010   1192  -3842  A    C  
ATOM   2819  ND2 ASN A 401       9.932   1.173 -18.868  1.00176.21      A    N  
ANISOU 2819  ND2 ASN A 401    23773  23831  19349  -6509   1475  -3910  A    N  
ATOM   2820  OD1 ASN A 401      11.324   2.701 -19.744  1.00184.19      A    O  
ANISOU 2820  OD1 ASN A 401    24618  24886  20480  -5611    962  -3624  A    O  
ATOM   2821  N   LEU A 402      10.730   4.754 -17.569  1.00155.91      A    N  
ANISOU 2821  N   LEU A 402    20930  21542  16765  -5178    984  -3363  A    N  
ATOM   2822  CA  LEU A 402      11.069   4.918 -16.161  1.00134.07      A    C  
ANISOU 2822  CA  LEU A 402    18557  18447  13935  -5113   1059  -3160  A    C  
ATOM   2823  C   LEU A 402      11.045   6.381 -15.712  1.00118.90      A    C  
ANISOU 2823  C   LEU A 402    16482  16713  11982  -4667    893  -3062  A    C  
ATOM   2824  O   LEU A 402      10.443   6.712 -14.688  1.00119.62      A    O  
ANISOU 2824  O   LEU A 402    16593  16915  11941  -4681   1044  -3077  A    O  
ATOM   2825  CB  LEU A 402      12.448   4.311 -15.889  1.00128.60      A    C  
ANISOU 2825  CB  LEU A 402    18417  17131  13315  -5029    954  -2925  A    C  
ATOM   2826  CG  LEU A 402      13.058   4.501 -14.500  1.00127.24      A    C  
ANISOU 2826  CG  LEU A 402    18696  16589  13062  -4872    942  -2694  A    C  
ATOM   2827  CD1 LEU A 402      12.114   3.974 -13.426  1.00137.32      A    C  
ANISOU 2827  CD1 LEU A 402    20144  17882  14149  -5232   1290  -2752  A    C  
ATOM   2828  CD2 LEU A 402      14.411   3.814 -14.411  1.00117.57      A    C  
ANISOU 2828  CD2 LEU A 402    17942  14830  11900  -4748    803  -2505  A    C  
ATOM   2829  N   VAL A 403      11.684   7.255 -16.485  1.00107.43      A    N  
ANISOU 2829  N   VAL A 403    14904  15283  10631  -4282    603  -2967  A    N  
ATOM   2830  CA  VAL A 403      11.776   8.669 -16.123  1.00106.64      A    C  
ANISOU 2830  CA  VAL A 403    14751  15258  10510  -3859    427  -2864  A    C  
ATOM   2831  C   VAL A 403      10.409   9.338 -16.143  1.00122.68      A    C  
ANISOU 2831  C   VAL A 403    16355  17848  12410  -3765    517  -3072  A    C  
ATOM   2832  O   VAL A 403      10.093  10.152 -15.274  1.00125.59      A    O  
ANISOU 2832  O   VAL A 403    16765  18274  12682  -3545    529  -3054  A    O  
ATOM   2833  CB  VAL A 403      12.731   9.439 -17.056  1.00 96.18      A    C  
ANISOU 2833  CB  VAL A 403    13406  13824   9316  -3529    133  -2714  A    C  
ATOM   2834  CG1 VAL A 403      12.785  10.914 -16.677  1.00 83.61      A    C  
ANISOU 2834  CG1 VAL A 403    11830  12243   7696  -3133    -33  -2617  A    C  
ATOM   2835  CG2 VAL A 403      14.118   8.824 -17.020  1.00 82.32      A    C  
ANISOU 2835  CG2 VAL A 403    11999  11592   7685  -3580     39  -2532  A    C  
ATOM   2836  N   GLU A 404       9.595   8.985 -17.132  1.00135.64      A    N  
ANISOU 2836  N   GLU A 404    17576  19930  14032  -3907    571  -3296  A    N  
ATOM   2837  CA  GLU A 404       8.248   9.529 -17.225  1.00162.87      A    C  
ANISOU 2837  CA  GLU A 404    20535  24007  17342  -3799    644  -3538  A    C  
ATOM   2838  C   GLU A 404       7.431   9.077 -16.019  1.00165.47      A    C  
ANISOU 2838  C   GLU A 404    20854  24470  17546  -4109    971  -3662  A    C  
ATOM   2839  O   GLU A 404       6.610   9.833 -15.496  1.00166.52      A    O  
ANISOU 2839  O   GLU A 404    20749  24977  17545  -3884   1034  -3770  A    O  
ATOM   2840  CB  GLU A 404       7.574   9.101 -18.533  1.00176.91      A    C  
ANISOU 2840  CB  GLU A 404    21845  26265  19108  -3933    619  -3787  A    C  
ATOM   2841  CG  GLU A 404       6.102   9.501 -18.646  1.00194.47      A    C  
ANISOU 2841  CG  GLU A 404    23474  29244  21172  -3851    696  -4096  A    C  
ATOM   2842  CD  GLU A 404       5.850  10.955 -18.273  1.00199.55      A    C  
ANISOU 2842  CD  GLU A 404    24058  30047  21715  -3239    552  -4025  A    C  
ATOM   2843  OE1 GLU A 404       6.602  11.833 -18.746  1.00204.47      A    O  
ANISOU 2843  OE1 GLU A 404    24900  30408  22383  -2803    283  -3808  A    O  
ATOM   2844  OE2 GLU A 404       4.902  11.221 -17.501  1.00195.71      A    O1-
ANISOU 2844  OE2 GLU A 404    23327  29939  21095  -3200    724  -4193  A    O1-
ATOM   2845  N   GLU A 405       7.679   7.849 -15.572  1.00156.90      A    N  
ANISOU 2845  N   GLU A 405    20066  23064  16485  -4605   1191  -3636  A    N  
ATOM   2846  CA  GLU A 405       6.999   7.313 -14.401  1.00161.19      A    C  
ANISOU 2846  CA  GLU A 405    20697  23660  16886  -4965   1548  -3708  A    C  
ATOM   2847  C   GLU A 405       7.291   8.187 -13.186  1.00158.43      A    C  
ANISOU 2847  C   GLU A 405    20645  23117  16433  -4612   1521  -3530  A    C  
ATOM   2848  O   GLU A 405       6.406   8.468 -12.382  1.00178.11      A    O  
ANISOU 2848  O   GLU A 405    22975  25945  18756  -4628   1744  -3650  A    O  
ATOM   2849  CB  GLU A 405       7.426   5.868 -14.138  1.00174.38      A    C  
ANISOU 2849  CB  GLU A 405    22808  24860  18589  -5505   1759  -3640  A    C  
ATOM   2850  CG  GLU A 405       6.642   5.177 -13.029  1.00198.13      A    C  
ANISOU 2850  CG  GLU A 405    25936  27920  21424  -5978   2190  -3712  A    C  
ATOM   2851  CD  GLU A 405       5.252   4.754 -13.473  1.00208.76      A    C  
ANISOU 2851  CD  GLU A 405    26685  29918  22718  -6432   2458  -4079  A    C  
ATOM   2852  OE1 GLU A 405       5.147   4.045 -14.496  1.00207.73      A    O  
ANISOU 2852  OE1 GLU A 405    26384  29851  22694  -6735   2431  -4245  A    O  
ATOM   2853  OE2 GLU A 405       4.267   5.124 -12.798  1.00213.12      A    O1-
ANISOU 2853  OE2 GLU A 405    26918  30946  23111  -6487   2697  -4224  A    O1-
ATOM   2854  N   TRP A 406       8.538   8.624 -13.064  1.00144.06      A    N  
ANISOU 2854  N   TRP A 406    19241  20788  14708  -4299   1248  -3267  A    N  
ATOM   2855  CA  TRP A 406       8.931   9.519 -11.982  1.00124.17      A    C  
ANISOU 2855  CA  TRP A 406    17027  18055  12097  -3951   1159  -3119  A    C  
ATOM   2856  C   TRP A 406       8.244  10.871 -12.092  1.00116.87      A    C  
ANISOU 2856  C   TRP A 406    15756  17549  11102  -3494   1048  -3241  A    C  
ATOM   2857  O   TRP A 406       7.713  11.383 -11.110  1.00117.53      A    O  
ANISOU 2857  O   TRP A 406    15870  17777  11009  -3347   1175  -3299  A    O  
ATOM   2858  CB  TRP A 406      10.448   9.694 -11.966  1.00108.07      A    C  
ANISOU 2858  CB  TRP A 406    15432  15434  10195  -3750    859  -2854  A    C  
ATOM   2859  CG  TRP A 406      11.152   8.452 -11.548  1.00103.05      A    C  
ANISOU 2859  CG  TRP A 406    15228  14358   9568  -4074    958  -2721  A    C  
ATOM   2860  CD1 TRP A 406      10.576   7.304 -11.085  1.00113.82      A    C  
ANISOU 2860  CD1 TRP A 406    16720  15714  10813  -4519   1299  -2782  A    C  
ATOM   2861  CD2 TRP A 406      12.565   8.216 -11.564  1.00 95.67      A    C  
ANISOU 2861  CD2 TRP A 406    14673  12926   8751  -3964    721  -2508  A    C  
ATOM   2862  CE2 TRP A 406      12.770   6.904 -11.088  1.00100.87      A    C  
ANISOU 2862  CE2 TRP A 406    15710  13278   9339  -4286    913  -2444  A    C  
ATOM   2863  CE3 TRP A 406      13.672   8.985 -11.929  1.00 91.47      A    C  
ANISOU 2863  CE3 TRP A 406    14194  12192   8370  -3634    377  -2372  A    C  
ATOM   2864  NE1 TRP A 406      11.544   6.371 -10.802  1.00116.23      A    N  
ANISOU 2864  NE1 TRP A 406    17530  15494  11140  -4646   1276  -2602  A    N  
ATOM   2865  CZ2 TRP A 406      14.046   6.347 -10.970  1.00 90.44      A    C  
ANISOU 2865  CZ2 TRP A 406    14797  11484   8080  -4204    739  -2259  A    C  
ATOM   2866  CZ3 TRP A 406      14.937   8.426 -11.812  1.00 89.96      A    C  
ANISOU 2866  CZ3 TRP A 406    14340  11583   8258  -3615    223  -2206  A    C  
ATOM   2867  CH2 TRP A 406      15.112   7.120 -11.335  1.00 86.64      A    C  
ANISOU 2867  CH2 TRP A 406    14273  10892   7752  -3858    390  -2156  A    C  
ATOM   2868  N   ILE A 407       8.242  11.436 -13.295  1.00112.74      A    N  
ANISOU 2868  N   ILE A 407    14934  17215  10688  -3242    819  -3281  A    N  
ATOM   2869  CA  ILE A 407       7.640  12.745 -13.529  1.00114.12      A    C  
ANISOU 2869  CA  ILE A 407    14843  17735  10783  -2732    677  -3376  A    C  
ATOM   2870  C   ILE A 407       6.140  12.733 -13.230  1.00122.06      A    C  
ANISOU 2870  C   ILE A 407    15365  19414  11597  -2758    939  -3673  A    C  
ATOM   2871  O   ILE A 407       5.608  13.681 -12.651  1.00124.39      A    O  
ANISOU 2871  O   ILE A 407    15600  19917  11745  -2360    941  -3752  A    O  
ATOM   2872  CB  ILE A 407       7.864  13.215 -14.981  1.00108.44      A    C  
ANISOU 2872  CB  ILE A 407    13916  17111  10175  -2481    406  -3350  A    C  
ATOM   2873  CG1 ILE A 407       9.358  13.240 -15.306  1.00 90.95      A    C  
ANISOU 2873  CG1 ILE A 407    12120  14291   8145  -2480    182  -3069  A    C  
ATOM   2874  CG2 ILE A 407       7.213  14.575 -15.217  1.00 96.70      A    C  
ANISOU 2874  CG2 ILE A 407    12231  15941   8569  -1896    256  -3431  A    C  
ATOM   2875  CD1 ILE A 407       9.706  14.026 -16.549  1.00 89.76      A    C  
ANISOU 2875  CD1 ILE A 407    11885  14156   8064  -2152    -80  -2982  A    C  
ATOM   2876  N   SER A 408       5.461  11.665 -13.636  1.00133.61      A    N  
ANISOU 2876  N   SER A 408    16474  21231  13059  -3229   1163  -3861  A    N  
ATOM   2877  CA  SER A 408       4.027  11.542 -13.393  1.00150.73      A    C  
ANISOU 2877  CA  SER A 408    18096  24118  15057  -3348   1441  -4180  A    C  
ATOM   2878  C   SER A 408       3.752  11.329 -11.907  1.00151.31      A    C  
ANISOU 2878  C   SER A 408    18395  24129  14966  -3543   1772  -4172  A    C  
ATOM   2879  O   SER A 408       2.805  11.892 -11.357  1.00146.01      A    O  
ANISOU 2879  O   SER A 408    17412  23957  14109  -3323   1927  -4362  A    O  
ATOM   2880  CB  SER A 408       3.429  10.397 -14.214  1.00169.89      A    C  
ANISOU 2880  CB  SER A 408    20102  26913  17536  -3901   1598  -4405  A    C  
ATOM   2881  OG  SER A 408       4.015   9.155 -13.870  1.00174.96      A    O  
ANISOU 2881  OG  SER A 408    21157  27059  18258  -4498   1793  -4281  A    O  
ATOM   2882  N   ASN A 409       4.580  10.506 -11.267  1.00161.54      A    N  
ANISOU 2882  N   ASN A 409    20243  24831  16303  -3920   1882  -3954  A    N  
ATOM   2883  CA  ASN A 409       4.468  10.258  -9.831  1.00169.01      A    C  
ANISOU 2883  CA  ASN A 409    21527  25633  17056  -4095   2184  -3892  A    C  
ATOM   2884  C   ASN A 409       4.763  11.503  -8.997  1.00172.00      A    C  
ANISOU 2884  C   ASN A 409    22174  25866  17314  -3506   2020  -3801  A    C  
ATOM   2885  O   ASN A 409       4.097  11.762  -7.993  1.00181.23      A    O  
ANISOU 2885  O   ASN A 409    23315  27294  18249  -3443   2271  -3902  A    O  
ATOM   2886  CB  ASN A 409       5.411   9.127  -9.403  1.00156.45      A    C  
ANISOU 2886  CB  ASN A 409    20550  23380  15516  -4534   2272  -3648  A    C  
ATOM   2887  CG  ASN A 409       4.889   7.748  -9.774  1.00144.73      A    C  
ANISOU 2887  CG  ASN A 409    18921  22011  14058  -5230   2589  -3770  A    C  
ATOM   2888  ND2 ASN A 409       5.805   6.810  -9.992  1.00134.05      A    N  
ANISOU 2888  ND2 ASN A 409    18032  20075  12826  -5504   2536  -3584  A    N  
ATOM   2889  OD1 ASN A 409       3.680   7.526  -9.855  1.00141.05      A    O  
ANISOU 2889  OD1 ASN A 409    17936  22156  13501  -5520   2881  -4047  A    O  
ATOM   2890  N   GLY A 410       5.767  12.268  -9.415  1.00156.58      A    N  
ANISOU 2890  N   GLY A 410    20489  23494  15509  -3099   1613  -3623  A    N  
ATOM   2891  CA  GLY A 410       6.190  13.438  -8.669  1.00141.05      A    C  
ANISOU 2891  CA  GLY A 410    18857  21283  13453  -2589   1420  -3540  A    C  
ATOM   2892  C   GLY A 410       7.543  13.202  -8.028  1.00128.12      A    C  
ANISOU 2892  C   GLY A 410    17871  18940  11869  -2671   1265  -3266  A    C  
ATOM   2893  O   GLY A 410       7.948  13.920  -7.116  1.00135.74      A    O  
ANISOU 2893  O   GLY A 410    19204  19654  12718  -2384   1158  -3206  A    O  
ATOM   2894  N   VAL A 411       8.237  12.175  -8.503  1.00112.73      A    N  
ANISOU 2894  N   VAL A 411    16060  16691  10080  -3045   1244  -3126  A    N  
ATOM   2895  CA  VAL A 411       9.540  11.809  -7.966  1.00109.87      A    C  
ANISOU 2895  CA  VAL A 411    16264  15716   9765  -3110   1085  -2882  A    C  
ATOM   2896  C   VAL A 411      10.645  12.495  -8.772  1.00103.78      A    C  
ANISOU 2896  C   VAL A 411    15564  14634   9235  -2837    668  -2751  A    C  
ATOM   2897  O   VAL A 411      11.823  12.445  -8.414  1.00 95.21      A    O  
ANISOU 2897  O   VAL A 411    14870  13094   8211  -2804    460  -2575  A    O  
ATOM   2898  CB  VAL A 411       9.741  10.282  -7.974  1.00122.80      A    C  
ANISOU 2898  CB  VAL A 411    18078  17161  11418  -3620   1298  -2798  A    C  
ATOM   2899  CG1 VAL A 411      10.868   9.893  -7.041  1.00122.71      A    C  
ANISOU 2899  CG1 VAL A 411    18689  16600  11337  -3614   1192  -2571  A    C  
ATOM   2900  CG2 VAL A 411       8.465   9.587  -7.540  1.00131.86      A    C  
ANISOU 2900  CG2 VAL A 411    19026  18706  12369  -3998   1760  -2963  A    C  
ATOM   2901  N   LEU A 412      10.263  13.107  -9.888  1.00109.33      A    N  
ANISOU 2901  N   LEU A 412    15873  15611  10057  -2651    553  -2840  A    N  
ATOM   2902  CA  LEU A 412      11.202  13.895 -10.675  1.00104.11      A    C  
ANISOU 2902  CA  LEU A 412    15280  14687   9592  -2396    203  -2712  A    C  
ATOM   2903  C   LEU A 412      10.629  15.278 -10.999  1.00100.96      A    C  
ANISOU 2903  C   LEU A 412    14709  14504   9146  -1942     76  -2808  A    C  
ATOM   2904  O   LEU A 412       9.425  15.426 -11.222  1.00101.37      A    O  
ANISOU 2904  O   LEU A 412    14387  15050   9079  -1830    231  -3000  A    O  
ATOM   2905  CB  LEU A 412      11.584  13.161 -11.960  1.00106.56      A    C  
ANISOU 2905  CB  LEU A 412    15392  15000  10096  -2611    153  -2660  A    C  
ATOM   2906  CG  LEU A 412      12.852  13.710 -12.614  1.00107.86      A    C  
ANISOU 2906  CG  LEU A 412    15714  14810  10458  -2458   -162  -2475  A    C  
ATOM   2907  CD1 LEU A 412      14.075  12.981 -12.110  1.00108.05      A    C  
ANISOU 2907  CD1 LEU A 412    16084  14407  10561  -2649   -236  -2318  A    C  
ATOM   2908  CD2 LEU A 412      12.762  13.619 -14.125  1.00118.69      A    C  
ANISOU 2908  CD2 LEU A 412    16758  16389  11948  -2461   -218  -2488  A    C  
ATOM   2909  N   TYR A 413      11.492  16.290 -10.988  1.00101.19      A    N  
ANISOU 2909  N   TYR A 413    15027  14161   9258  -1679   -205  -2685  A    N  
ATOM   2910  CA  TYR A 413      11.105  17.640 -11.386  1.00108.98      A    C  
ANISOU 2910  CA  TYR A 413    15976  15221  10209  -1227   -354  -2735  A    C  
ATOM   2911  C   TYR A 413      12.152  18.230 -12.328  1.00113.42      A    C  
ANISOU 2911  C   TYR A 413    16684  15433  10977  -1163   -626  -2545  A    C  
ATOM   2912  O   TYR A 413      13.354  18.054 -12.128  1.00102.95      A    O  
ANISOU 2912  O   TYR A 413    15618  13707   9791  -1363   -758  -2395  A    O  
ATOM   2913  CB  TYR A 413      10.922  18.530 -10.154  1.00125.97      A    C  
ANISOU 2913  CB  TYR A 413    18440  17237  12185   -941   -374  -2817  A    C  
ATOM   2914  CG  TYR A 413      10.266  19.875 -10.406  1.00129.44      A    C  
ANISOU 2914  CG  TYR A 413    18875  17782  12525   -411   -475  -2918  A    C  
ATOM   2915  CD1 TYR A 413      11.001  20.958 -10.880  1.00125.98      A    C  
ANISOU 2915  CD1 TYR A 413    18743  16924  12198   -185   -750  -2790  A    C  
ATOM   2916  CD2 TYR A 413       8.918  20.071 -10.134  1.00132.69      A    C  
ANISOU 2916  CD2 TYR A 413    18997  18704  12714   -129   -285  -3147  A    C  
ATOM   2917  CE1 TYR A 413      10.405  22.192 -11.096  1.00126.48      A    C  
ANISOU 2917  CE1 TYR A 413    18902  17010  12146    337   -844  -2868  A    C  
ATOM   2918  CE2 TYR A 413       8.313  21.302 -10.347  1.00138.20      A    C  
ANISOU 2918  CE2 TYR A 413    19722  19494  13294    442   -393  -3248  A    C  
ATOM   2919  CZ  TYR A 413       9.061  22.359 -10.828  1.00127.03      A    C  
ANISOU 2919  CZ  TYR A 413    18694  17588  11984    689   -678  -3099  A    C  
ATOM   2920  OH  TYR A 413       8.465  23.583 -11.040  1.00115.53      A    O  
ANISOU 2920  OH  TYR A 413    17356  16151  10389   1291   -786  -3184  A    O  
ATOM   2921  N   ALA A 414      11.687  18.946 -13.343  1.00133.33      A    N  
ANISOU 2921  N   ALA A 414    19036  18132  13493   -869   -705  -2555  A    N  
ATOM   2922  CA  ALA A 414      12.574  19.509 -14.348  1.00134.03      A    C  
ANISOU 2922  CA  ALA A 414    19260  17928  13739   -824   -911  -2361  A    C  
ATOM   2923  C   ALA A 414      12.807  20.993 -14.097  1.00135.21      A    C  
ANISOU 2923  C   ALA A 414    19802  17719  13853   -469  -1092  -2308  A    C  
ATOM   2924  O   ALA A 414      11.898  21.808 -14.254  1.00139.94      A    O  
ANISOU 2924  O   ALA A 414    20384  18495  14293    -36  -1102  -2404  A    O  
ATOM   2925  CB  ALA A 414      12.007  19.288 -15.739  1.00137.45      A    C  
ANISOU 2925  CB  ALA A 414    19321  18744  14160   -742   -889  -2372  A    C  
ATOM   2926  N   THR A 415      14.023  21.341 -13.693  1.00123.30      A    N  
ANISOU 2926  N   THR A 415    18656  15710  12484   -646  -1240  -2176  A    N  
ATOM   2927  CA  THR A 415      14.377  22.741 -13.522  1.00118.65      A    C  
ANISOU 2927  CA  THR A 415    18497  14697  11888   -402  -1416  -2125  A    C  
ATOM   2928  C   THR A 415      14.438  23.409 -14.894  1.00125.93      A    C  
ANISOU 2928  C   THR A 415    19439  15559  12849   -235  -1489  -1965  A    C  
ATOM   2929  O   THR A 415      15.051  22.879 -15.819  1.00123.33      A    O  
ANISOU 2929  O   THR A 415    18939  15264  12658   -493  -1483  -1816  A    O  
ATOM   2930  CB  THR A 415      15.722  22.899 -12.787  1.00 99.71      A    C  
ANISOU 2930  CB  THR A 415    16430  11817   9639   -711  -1567  -2053  A    C  
ATOM   2931  CG2 THR A 415      15.687  22.165 -11.464  1.00101.10      A    C  
ANISOU 2931  CG2 THR A 415    16618  12067   9729   -846  -1505  -2188  A    C  
ATOM   2932  OG1 THR A 415      16.777  22.351 -13.584  1.00 96.41      A    O  
ANISOU 2932  OG1 THR A 415    15875  11322   9435  -1065  -1608  -1876  A    O  
ATOM   2933  N   PRO A 416      13.805  24.584 -15.026  1.00136.78      A    N  
ANISOU 2933  N   PRO A 416    21062  16833  14074    230  -1554  -1992  A    N  
ATOM   2934  CA  PRO A 416      13.734  25.291 -16.312  1.00146.62      A    C  
ANISOU 2934  CA  PRO A 416    22406  18014  15287    475  -1619  -1823  A    C  
ATOM   2935  C   PRO A 416      15.079  25.889 -16.743  1.00151.07      A    C  
ANISOU 2935  C   PRO A 416    23352  18010  16036    178  -1726  -1576  A    C  
ATOM   2936  O   PRO A 416      16.005  25.925 -15.934  1.00152.85      A    O  
ANISOU 2936  O   PRO A 416    23777  17891  16409   -159  -1787  -1581  A    O  
ATOM   2937  CB  PRO A 416      12.706  26.398 -16.031  1.00151.99      A    C  
ANISOU 2937  CB  PRO A 416    23339  18680  15730   1104  -1667  -1946  A    C  
ATOM   2938  CG  PRO A 416      11.928  25.910 -14.847  1.00145.15      A    C  
ANISOU 2938  CG  PRO A 416    22249  18151  14752   1182  -1557  -2221  A    C  
ATOM   2939  CD  PRO A 416      12.952  25.219 -14.010  1.00138.35      A    C  
ANISOU 2939  CD  PRO A 416    21439  17054  14075    625  -1544  -2200  A    C  
ATOM   2940  N   PRO A 417      15.190  26.336 -18.009  1.00146.00      A    N  
ANISOU 2940  N   PRO A 417    22797  17307  15367    289  -1743  -1370  A    N  
ATOM   2941  CA  PRO A 417      16.450  26.879 -18.531  1.00148.56      A    C  
ANISOU 2941  CA  PRO A 417    23451  17141  15856    -47  -1789  -1121  A    C  
ATOM   2942  C   PRO A 417      16.853  28.217 -17.894  1.00168.86      A    C  
ANISOU 2942  C   PRO A 417    26664  19060  18435      4  -1902  -1096  A    C  
ATOM   2943  O   PRO A 417      16.026  28.891 -17.272  1.00172.01      A    O  
ANISOU 2943  O   PRO A 417    27323  19369  18664    447  -1954  -1245  A    O  
ATOM   2944  CB  PRO A 417      16.155  27.044 -20.027  1.00139.82      A    C  
ANISOU 2944  CB  PRO A 417    22300  16204  14622    172  -1749   -923  A    C  
ATOM   2945  CG  PRO A 417      14.679  27.220 -20.090  1.00143.68      A    C  
ANISOU 2945  CG  PRO A 417    22676  17072  14842    795  -1766  -1081  A    C  
ATOM   2946  CD  PRO A 417      14.179  26.237 -19.076  1.00140.95      A    C  
ANISOU 2946  CD  PRO A 417    21900  17121  14531    691  -1706  -1361  A    C  
ATOM   2947  N   GLY A 418      18.122  28.584 -18.050  1.00174.93      A    N  
ANISOU 2947  N   GLY A 418    27676  19393  19398   -460  -1931   -932  A    N  
ATOM   2948  CA  GLY A 418      18.625  29.853 -17.555  1.00173.51      A    C  
ANISOU 2948  CA  GLY A 418    28132  18545  19249   -525  -2032   -909  A    C  
ATOM   2949  C   GLY A 418      19.020  29.813 -16.090  1.00181.45      A    C  
ANISOU 2949  C   GLY A 418    29212  19379  20350   -741  -2143  -1150  A    C  
ATOM   2950  O   GLY A 418      19.562  30.784 -15.559  1.00185.38      A    O  
ANISOU 2950  O   GLY A 418    30216  19322  20900   -889  -2249  -1184  A    O  
ATOM   2951  N   SER A 419      18.751  28.687 -15.438  1.00191.26      A    N  
ANISOU 2951  N   SER A 419    29986  21086  21599   -770  -2119  -1323  A    N  
ATOM   2952  CA  SER A 419      19.018  28.541 -14.014  1.00198.74      A    C  
ANISOU 2952  CA  SER A 419    30997  21944  22571   -906  -2222  -1552  A    C  
ATOM   2953  C   SER A 419      18.943  27.077 -13.584  1.00205.56      A    C  
ANISOU 2953  C   SER A 419    31320  23325  23458  -1044  -2153  -1647  A    C  
ATOM   2954  O   SER A 419      18.066  26.359 -14.062  1.00212.89      A    O  
ANISOU 2954  O   SER A 419    31896  24707  24287   -825  -2014  -1646  A    O  
ATOM   2955  CB  SER A 419      18.020  29.370 -13.199  1.00197.78      A    C  
ANISOU 2955  CB  SER A 419    31264  21665  22219   -398  -2267  -1750  A    C  
ATOM   2956  OG  SER A 419      16.715  28.825 -13.273  1.00196.40      A    O  
ANISOU 2956  OG  SER A 419    30759  22018  21845     52  -2139  -1843  A    O  
ATOM   2957  N   ASN A 420      19.828  26.604 -12.697  1.00200.08      A    N  
ANISOU 2957  N   ASN A 420    30570  22575  22876  -1396  -2252  -1736  A    N  
ATOM   2958  CA  ASN A 420      21.023  27.285 -12.181  1.00182.24      A    C  
ANISOU 2958  CA  ASN A 420    28609  19871  20762  -1754  -2440  -1766  A    C  
ATOM   2959  C   ASN A 420      21.819  26.189 -11.465  1.00183.65      A    C  
ANISOU 2959  C   ASN A 420    28470  20279  21029  -2060  -2515  -1845  A    C  
ATOM   2960  O   ASN A 420      21.591  25.001 -11.706  1.00184.53      A    O  
ANISOU 2960  O   ASN A 420    28184  20796  21133  -2047  -2396  -1802  A    O  
ATOM   2961  CB  ASN A 420      20.665  28.414 -11.201  1.00161.53      A    C  
ANISOU 2961  CB  ASN A 420    26532  16848  17995  -1527  -2564  -1957  A    C  
ATOM   2962  CG  ASN A 420      21.843  29.309 -10.869  1.00157.34      A    C  
ANISOU 2962  CG  ASN A 420    26362  15803  17618  -1931  -2758  -1997  A    C  
ATOM   2963  ND2 ASN A 420      21.569  30.596 -10.678  1.00166.42      A    N  
ANISOU 2963  ND2 ASN A 420    28094  16456  18683  -1757  -2824  -2066  A    N  
ATOM   2964  OD1 ASN A 420      22.981  28.854 -10.782  1.00153.27      A    O  
ANISOU 2964  OD1 ASN A 420    25605  15341  17289  -2388  -2851  -1986  A    O  
ATOM   2965  N   ASP A 421      22.745  26.567 -10.584  1.00183.78      A    N  
ANISOU 2965  N   ASP A 421    28678  20035  21113  -2322  -2725  -1973  A    N  
ATOM   2966  CA  ASP A 421      23.395  25.598  -9.702  1.00170.87      A    C  
ANISOU 2966  CA  ASP A 421    26816  18619  19488  -2491  -2841  -2081  A    C  
ATOM   2967  C   ASP A 421      22.350  25.424  -8.612  1.00161.74      A    C  
ANISOU 2967  C   ASP A 421    25841  17560  18053  -2124  -2807  -2252  A    C  
ATOM   2968  O   ASP A 421      22.572  25.755  -7.446  1.00141.42      A    O  
ANISOU 2968  O   ASP A 421    23538  14829  15365  -2113  -2980  -2445  A    O  
ATOM   2969  CB  ASP A 421      24.731  26.095  -9.150  1.00159.72      A    C  
ANISOU 2969  CB  ASP A 421    25508  16961  18218  -2878  -3106  -2189  A    C  
ATOM   2970  CG  ASP A 421      25.519  25.002  -8.440  1.00145.52      A    C  
ANISOU 2970  CG  ASP A 421    23411  15453  16427  -3011  -3249  -2268  A    C  
ATOM   2971  OD1 ASP A 421      24.906  24.174  -7.733  1.00132.77      A    O  
ANISOU 2971  OD1 ASP A 421    21775  14058  14612  -2752  -3201  -2323  A    O  
ATOM   2972  OD2 ASP A 421      26.759  24.971  -8.593  1.00149.31      A    O1-
ANISOU 2972  OD2 ASP A 421    23680  15952  17100  -3367  -3402  -2273  A    O1-
ATOM   2973  N   ASP A 422      21.212  24.878  -9.029  1.00169.96      A    N  
ANISOU 2973  N   ASP A 422    26702  18900  18975  -1840  -2573  -2194  A    N  
ATOM   2974  CA  ASP A 422      19.913  25.189  -8.450  1.00167.14      A    C  
ANISOU 2974  CA  ASP A 422    26533  18615  18357  -1426  -2460  -2331  A    C  
ATOM   2975  C   ASP A 422      19.796  25.124  -6.943  1.00162.81      A    C  
ANISOU 2975  C   ASP A 422    26221  18048  17590  -1325  -2540  -2543  A    C  
ATOM   2976  O   ASP A 422      20.263  24.195  -6.284  1.00147.74      A    O  
ANISOU 2976  O   ASP A 422    24195  16294  15644  -1483  -2580  -2562  A    O  
ATOM   2977  CB  ASP A 422      18.855  24.260  -9.048  1.00167.77      A    C  
ANISOU 2977  CB  ASP A 422    26233  19155  18357  -1250  -2195  -2264  A    C  
ATOM   2978  CG  ASP A 422      18.659  24.478 -10.532  1.00162.07      A    C  
ANISOU 2978  CG  ASP A 422    25331  18490  17760  -1216  -2109  -2091  A    C  
ATOM   2979  OD1 ASP A 422      18.427  25.638 -10.936  1.00156.02      A    O  
ANISOU 2979  OD1 ASP A 422    24845  17460  16975  -1016  -2156  -2070  A    O  
ATOM   2980  OD2 ASP A 422      18.744  23.488 -11.291  1.00161.36      A    O1-
ANISOU 2980  OD2 ASP A 422    24862  18687  17762  -1371  -1998  -1976  A    O1-
ATOM   2981  N   TRP A 423      19.143  26.150  -6.420  1.00175.66      A    N  
ANISOU 2981  N   TRP A 423    28223  19476  19045  -1015  -2561  -2702  A    N  
ATOM   2982  CA  TRP A 423      18.750  26.190  -5.035  1.00190.50      A    C  
ANISOU 2982  CA  TRP A 423    30353  21382  20645   -817  -2584  -2923  A    C  
ATOM   2983  C   TRP A 423      17.448  25.415  -4.932  1.00176.93      A    C  
ANISOU 2983  C   TRP A 423    28370  20143  18715   -541  -2275  -2939  A    C  
ATOM   2984  O   TRP A 423      16.928  25.201  -3.840  1.00179.93      A    O  
ANISOU 2984  O   TRP A 423    28873  20672  18822   -372  -2194  -3095  A    O  
ATOM   2985  CB  TRP A 423      18.570  27.632  -4.572  1.00216.52      A    C  
ANISOU 2985  CB  TRP A 423    34176  24259  23833   -573  -2720  -3111  A    C  
ATOM   2986  CG  TRP A 423      17.630  28.390  -5.459  1.00240.22      A    C  
ANISOU 2986  CG  TRP A 423    37239  27214  26819   -207  -2585  -3062  A    C  
ATOM   2987  CD1 TRP A 423      16.286  28.546  -5.284  1.00250.99      A    C  
ANISOU 2987  CD1 TRP A 423    38591  28841  27933    298  -2391  -3176  A    C  
ATOM   2988  CD2 TRP A 423      17.957  29.071  -6.690  1.00251.31      A    C  
ANISOU 2988  CD2 TRP A 423    38715  28329  28443   -289  -2629  -2881  A    C  
ATOM   2989  CE2 TRP A 423      16.754  29.618  -7.179  1.00258.50      A    C  
ANISOU 2989  CE2 TRP A 423    39693  29326  29200    234  -2486  -2892  A    C  
ATOM   2990  CE3 TRP A 423      19.142  29.264  -7.397  1.00254.14      A    C  
ANISOU 2990  CE3 TRP A 423    39083  28394  29087   -744  -2762  -2716  A    C  
ATOM   2991  NE1 TRP A 423      15.759  29.291  -6.316  1.00255.24      A    N  
ANISOU 2991  NE1 TRP A 423    39191  29273  28515    586  -2350  -3088  A    N  
ATOM   2992  CZ2 TRP A 423      16.719  30.358  -8.372  1.00265.20      A    C  
ANISOU 2992  CZ2 TRP A 423    40684  29926  30154    337  -2491  -2715  A    C  
ATOM   2993  CZ3 TRP A 423      19.092  30.000  -8.574  1.00262.42      A    C  
ANISOU 2993  CZ3 TRP A 423    40268  29196  30245   -693  -2725  -2536  A    C  
ATOM   2994  CH2 TRP A 423      17.890  30.537  -9.047  1.00268.25      A    C  
ANISOU 2994  CH2 TRP A 423    41136  29979  30805   -142  -2599  -2526  A    C  
ATOM   2995  N   TYR A 424      16.931  25.007  -6.092  1.00161.91      A    N  
ANISOU 2995  N   TYR A 424    26095  18497  16925   -520  -2097  -2789  A    N  
ATOM   2996  CA  TYR A 424      15.700  24.229  -6.181  1.00149.93      A    C  
ANISOU 2996  CA  TYR A 424    24236  17484  15246   -339  -1797  -2816  A    C  
ATOM   2997  C   TYR A 424      15.693  23.080  -5.181  1.00139.37      A    C  
ANISOU 2997  C   TYR A 424    22830  16375  13751   -511  -1675  -2854  A    C  
ATOM   2998  O   TYR A 424      14.707  22.867  -4.484  1.00139.82      A    O  
ANISOU 2998  O   TYR A 424    22863  16718  13545   -314  -1459  -2986  A    O  
ATOM   2999  CB  TYR A 424      15.492  23.706  -7.617  1.00145.57      A    C  
ANISOU 2999  CB  TYR A 424    23257  17173  14879   -436  -1682  -2642  A    C  
ATOM   3000  CG  TYR A 424      14.973  24.752  -8.594  1.00133.64      A    C  
ANISOU 3000  CG  TYR A 424    21789  15593  13395   -113  -1708  -2616  A    C  
ATOM   3001  CD1 TYR A 424      15.792  25.778  -9.051  1.00127.26      A    C  
ANISOU 3001  CD1 TYR A 424    21316  14297  12740   -153  -1921  -2520  A    C  
ATOM   3002  CD2 TYR A 424      13.664  24.703  -9.067  1.00121.10      A    C  
ANISOU 3002  CD2 TYR A 424    19912  14438  11662    230  -1519  -2688  A    C  
ATOM   3003  CE1 TYR A 424      15.319  26.732  -9.943  1.00122.98      A    C  
ANISOU 3003  CE1 TYR A 424    20902  13640  12183    172  -1937  -2464  A    C  
ATOM   3004  CE2 TYR A 424      13.184  25.653  -9.957  1.00118.40      A    C  
ANISOU 3004  CE2 TYR A 424    19640  14044  11302    603  -1570  -2657  A    C  
ATOM   3005  CZ  TYR A 424      14.017  26.662 -10.392  1.00119.29      A    C  
ANISOU 3005  CZ  TYR A 424    20170  13610  11548    587  -1776  -2527  A    C  
ATOM   3006  OH  TYR A 424      13.551  27.609 -11.275  1.00114.82      A    O  
ANISOU 3006  OH  TYR A 424    19762  12937  10928    983  -1821  -2464  A    O  
ATOM   3007  N   TRP A 425      16.801  22.353  -5.097  1.00138.54      A    N  
ANISOU 3007  N   TRP A 425    22708  16147  13784   -860  -1806  -2736  A    N  
ATOM   3008  CA  TRP A 425      16.934  21.313  -4.082  1.00143.11      A    C  
ANISOU 3008  CA  TRP A 425    23343  16852  14181   -988  -1732  -2746  A    C  
ATOM   3009  C   TRP A 425      17.357  21.875  -2.725  1.00144.93      A    C  
ANISOU 3009  C   TRP A 425    24017  16855  14196   -884  -1927  -2902  A    C  
ATOM   3010  O   TRP A 425      16.906  21.391  -1.688  1.00145.93      A    O  
ANISOU 3010  O   TRP A 425    24287  17137  14023   -803  -1785  -2975  A    O  
ATOM   3011  CB  TRP A 425      17.910  20.222  -4.552  1.00136.78      A    C  
ANISOU 3011  CB  TRP A 425    22351  16040  13578  -1321  -1798  -2564  A    C  
ATOM   3012  CG  TRP A 425      19.271  20.711  -4.947  1.00138.80      A    C  
ANISOU 3012  CG  TRP A 425    22652  15995  14091  -1491  -2125  -2505  A    C  
ATOM   3013  CD1 TRP A 425      20.299  21.052  -4.122  1.00141.51      A    C  
ANISOU 3013  CD1 TRP A 425    23251  16102  14413  -1561  -2422  -2579  A    C  
ATOM   3014  CD2 TRP A 425      19.748  20.898  -6.283  1.00145.37      A    C  
ANISOU 3014  CD2 TRP A 425    23233  16776  15227  -1637  -2172  -2372  A    C  
ATOM   3015  CE2 TRP A 425      21.077  21.357  -6.190  1.00141.73      A    C  
ANISOU 3015  CE2 TRP A 425    22870  16051  14929  -1826  -2474  -2370  A    C  
ATOM   3016  CE3 TRP A 425      19.180  20.720  -7.547  1.00166.76      A    C  
ANISOU 3016  CE3 TRP A 425    25636  19665  18061  -1631  -1988  -2267  A    C  
ATOM   3017  NE1 TRP A 425      21.390  21.446  -4.861  1.00133.83      A    N  
ANISOU 3017  NE1 TRP A 425    22163  14952  13733  -1777  -2640  -2512  A    N  
ATOM   3018  CZ2 TRP A 425      21.844  21.646  -7.316  1.00163.42      A    C  
ANISOU 3018  CZ2 TRP A 425    25423  18707  17963  -2029  -2554  -2248  A    C  
ATOM   3019  CZ3 TRP A 425      19.943  21.005  -8.663  1.00182.88      A    C  
ANISOU 3019  CZ3 TRP A 425    27528  21595  20363  -1792  -2088  -2137  A    C  
ATOM   3020  CH2 TRP A 425      21.260  21.466  -8.541  1.00188.86      A    C  
ANISOU 3020  CH2 TRP A 425    28393  22085  21282  -1999  -2348  -2120  A    C  
ATOM   3021  N   LEU A 426      18.207  22.897  -2.731  1.00133.66      A    N  
ANISOU 3021  N   LEU A 426    22822  15062  12902   -906  -2239  -2962  A    N  
ATOM   3022  CA  LEU A 426      18.613  23.546  -1.489  1.00113.08      A    C  
ANISOU 3022  CA  LEU A 426    20651  12225  10090   -813  -2463  -3158  A    C  
ATOM   3023  C   LEU A 426      17.401  24.160  -0.789  1.00119.98      A    C  
ANISOU 3023  C   LEU A 426    21751  13191  10644   -419  -2281  -3354  A    C  
ATOM   3024  O   LEU A 426      17.226  23.992   0.416  1.00134.97      A    O  
ANISOU 3024  O   LEU A 426    23901  15161  12222   -300  -2258  -3486  A    O  
ATOM   3025  CB  LEU A 426      19.672  24.618  -1.748  1.00110.78      A    C  
ANISOU 3025  CB  LEU A 426    20553  11512  10028   -968  -2810  -3215  A    C  
ATOM   3026  CG  LEU A 426      21.123  24.153  -1.918  1.00114.99      A    C  
ANISOU 3026  CG  LEU A 426    20938  11965  10789  -1347  -3076  -3124  A    C  
ATOM   3027  CD1 LEU A 426      22.056  25.333  -2.183  1.00105.13      A    C  
ANISOU 3027  CD1 LEU A 426    19864  10320   9762  -1557  -3372  -3212  A    C  
ATOM   3028  CD2 LEU A 426      21.610  23.352  -0.716  1.00124.62      A    C  
ANISOU 3028  CD2 LEU A 426    22271  13311  11767  -1360  -3206  -3190  A    C  
ATOM   3029  N   TYR A 427      16.567  24.866  -1.550  1.00106.13      A    N  
ANISOU 3029  N   TYR A 427    19911  11461   8953   -181  -2150  -3376  A    N  
ATOM   3030  CA  TYR A 427      15.325  25.430  -1.025  1.00117.28      A    C  
ANISOU 3030  CA  TYR A 427    21455  13040  10067    262  -1951  -3572  A    C  
ATOM   3031  C   TYR A 427      14.421  24.330  -0.507  1.00140.69      A    C  
ANISOU 3031  C   TYR A 427    24166  16513  12777    290  -1595  -3570  A    C  
ATOM   3032  O   TYR A 427      13.902  24.416   0.602  1.00175.56      A    O  
ANISOU 3032  O   TYR A 427    28801  21057  16848    503  -1478  -3742  A    O  
ATOM   3033  CB  TYR A 427      14.590  26.238  -2.101  1.00112.89      A    C  
ANISOU 3033  CB  TYR A 427    20781  12482   9630    552  -1880  -3565  A    C  
ATOM   3034  CG  TYR A 427      13.137  26.558  -1.782  1.00120.04      A    C  
ANISOU 3034  CG  TYR A 427    21627  13743  10238   1052  -1614  -3752  A    C  
ATOM   3035  CD1 TYR A 427      12.800  27.663  -1.009  1.00125.98      A    C  
ANISOU 3035  CD1 TYR A 427    22828  14284  10754   1472  -1689  -4001  A    C  
ATOM   3036  CD2 TYR A 427      12.103  25.759  -2.263  1.00122.92      A    C  
ANISOU 3036  CD2 TYR A 427    21470  14680  10555   1106  -1289  -3708  A    C  
ATOM   3037  CE1 TYR A 427      11.474  27.964  -0.721  1.00130.83      A    C  
ANISOU 3037  CE1 TYR A 427    23349  15277  11083   1983  -1439  -4193  A    C  
ATOM   3038  CE2 TYR A 427      10.774  26.051  -1.977  1.00124.92      A    C  
ANISOU 3038  CE2 TYR A 427    21584  15344  10534   1562  -1040  -3908  A    C  
ATOM   3039  CZ  TYR A 427      10.466  27.155  -1.207  1.00128.02      A    C  
ANISOU 3039  CZ  TYR A 427    22406  15548  10688   2025  -1112  -4147  A    C  
ATOM   3040  OH  TYR A 427       9.149  27.448  -0.922  1.00128.73      A    O  
ANISOU 3040  OH  TYR A 427    22323  16098  10492   2529   -857  -4366  A    O  
ATOM   3041  N   ALA A 428      14.244  23.291  -1.315  1.00125.52      A    N  
ANISOU 3041  N   ALA A 428    21805  14874  11015     47  -1408  -3381  A    N  
ATOM   3042  CA  ALA A 428      13.344  22.205  -0.965  1.00121.54      A    C  
ANISOU 3042  CA  ALA A 428    21043  14836  10300    -14  -1031  -3370  A    C  
ATOM   3043  C   ALA A 428      13.861  21.435   0.251  1.00130.47      A    C  
ANISOU 3043  C   ALA A 428    22464  15915  11194   -192  -1027  -3344  A    C  
ATOM   3044  O   ALA A 428      13.084  21.039   1.120  1.00130.31      A    O  
ANISOU 3044  O   ALA A 428    22500  16176  10837   -112   -737  -3424  A    O  
ATOM   3045  CB  ALA A 428      13.151  21.282  -2.150  1.00111.86      A    C  
ANISOU 3045  CB  ALA A 428    19335  13851   9317   -280   -872  -3193  A    C  
ATOM   3046  N   ALA A 429      15.173  21.237   0.325  1.00105.24      A    N  
ANISOU 3046  N   ALA A 429    19453  12387   8148   -414  -1345  -3235  A    N  
ATOM   3047  CA  ALA A 429      15.753  20.555   1.476  1.00106.38      A    C  
ANISOU 3047  CA  ALA A 429    19912  12469   8038   -513  -1407  -3208  A    C  
ATOM   3048  C   ALA A 429      15.552  21.385   2.746  1.00132.30      A    C  
ANISOU 3048  C   ALA A 429    23631  15682  10955   -214  -1479  -3442  A    C  
ATOM   3049  O   ALA A 429      15.133  20.861   3.779  1.00125.45      A    O  
ANISOU 3049  O   ALA A 429    22966  14994   9705   -154  -1273  -3471  A    O  
ATOM   3050  CB  ALA A 429      17.234  20.276   1.246  1.00104.45      A    C  
ANISOU 3050  CB  ALA A 429    19719  11935   8031   -747  -1783  -3083  A    C  
ATOM   3051  N   ALA A 430      15.843  22.680   2.655  1.00129.04      A    N  
ANISOU 3051  N   ALA A 430    23397  14989  10643    -35  -1756  -3611  A    N  
ATOM   3052  CA  ALA A 430      15.724  23.594   3.789  1.00126.52      A    C  
ANISOU 3052  CA  ALA A 430    23534  14541   9996    263  -1872  -3877  A    C  
ATOM   3053  C   ALA A 430      14.272  23.836   4.188  1.00131.67      A    C  
ANISOU 3053  C   ALA A 430    24161  15535  10333    618  -1481  -4030  A    C  
ATOM   3054  O   ALA A 430      13.953  23.894   5.377  1.00130.48      A    O  
ANISOU 3054  O   ALA A 430    24325  15487   9764    813  -1388  -4186  A    O  
ATOM   3055  CB  ALA A 430      16.403  24.914   3.470  1.00116.55      A    C  
ANISOU 3055  CB  ALA A 430    22494  12833   8956    316  -2254  -4021  A    C  
ATOM   3056  N   LYS A 431      13.402  23.995   3.193  1.00117.35      A    N  
ANISOU 3056  N   LYS A 431    21958  13934   8697    723  -1258  -4002  A    N  
ATOM   3057  CA  LYS A 431      11.986  24.263   3.437  1.00133.45      A    C  
ANISOU 3057  CA  LYS A 431    23859  16381  10464   1092   -891  -4174  A    C  
ATOM   3058  C   LYS A 431      11.334  23.087   4.156  1.00144.41      A    C  
ANISOU 3058  C   LYS A 431    25110  18225  11536    944   -475  -4118  A    C  
ATOM   3059  O   LYS A 431      10.463  23.267   5.009  1.00156.29      A    O  
ANISOU 3059  O   LYS A 431    26702  20028  12654   1218   -202  -4302  A    O  
ATOM   3060  CB  LYS A 431      11.252  24.550   2.126  1.00124.35      A    C  
ANISOU 3060  CB  LYS A 431    22252  15421   9575   1222   -774  -4143  A    C  
ATOM   3061  CG  LYS A 431       9.850  25.115   2.296  1.00135.98      A    C  
ANISOU 3061  CG  LYS A 431    23568  17310  10788   1718   -483  -4378  A    C  
ATOM   3062  CD  LYS A 431       9.891  26.539   2.831  1.00153.84      A    C  
ANISOU 3062  CD  LYS A 431    26338  19220  12893   2208   -711  -4633  A    C  
ATOM   3063  CE  LYS A 431       8.500  27.150   2.896  1.00165.71      A    C  
ANISOU 3063  CE  LYS A 431    27662  21154  14146   2795   -441  -4880  A    C  
ATOM   3064  NZ  LYS A 431       8.540  28.565   3.361  1.00172.25      A    N1+
ANISOU 3064  NZ  LYS A 431    29052  21574  14820   3320   -673  -5139  A    N1+
ATOM   3065  N   LEU A 432      11.771  21.881   3.809  1.00139.88      A    N  
ANISOU 3065  N   LEU A 432    24349  17687  11113    508   -411  -3862  A    N  
ATOM   3066  CA  LEU A 432      11.251  20.669   4.429  1.00144.06      A    C  
ANISOU 3066  CA  LEU A 432    24822  18555  11361    283     -8  -3762  A    C  
ATOM   3067  C   LEU A 432      12.101  20.278   5.627  1.00140.52      A    C  
ANISOU 3067  C   LEU A 432    24910  17865  10617    211   -161  -3704  A    C  
ATOM   3068  O   LEU A 432      11.764  19.341   6.355  1.00126.34      A    O  
ANISOU 3068  O   LEU A 432    23233  16270   8500     60    158  -3609  A    O  
ATOM   3069  CB  LEU A 432      11.212  19.514   3.423  1.00146.59      A    C  
ANISOU 3069  CB  LEU A 432    24719  19008  11969   -137    163  -3526  A    C  
ATOM   3070  CG  LEU A 432      10.021  19.430   2.466  1.00134.01      A    C  
ANISOU 3070  CG  LEU A 432    22531  17874  10514   -142    486  -3587  A    C  
ATOM   3071  CD1 LEU A 432       8.702  19.390   3.213  1.00140.03      A    C  
ANISOU 3071  CD1 LEU A 432    23160  19159  10887      4    952  -3769  A    C  
ATOM   3072  CD2 LEU A 432      10.053  20.597   1.523  1.00121.06      A    C  
ANISOU 3072  CD2 LEU A 432    20728  16115   9155    166    204  -3688  A    C  
ATOM   3073  N   LYS A 433      13.215  20.988   5.804  1.00150.34      A    N  
ANISOU 3073  N   LYS A 433    26480  18681  11961    301   -653  -3762  A    N  
ATOM   3074  CA  LYS A 433      14.168  20.712   6.875  1.00147.84      A    C  
ANISOU 3074  CA  LYS A 433    26651  18141  11382    270   -908  -3738  A    C  
ATOM   3075  C   LYS A 433      14.624  19.261   6.803  1.00147.99      A    C  
ANISOU 3075  C   LYS A 433    26636  18176  11418    -72   -816  -3437  A    C  
ATOM   3076  O   LYS A 433      14.965  18.640   7.813  1.00153.81      A    O  
ANISOU 3076  O   LYS A 433    27764  18887  11789    -77   -817  -3363  A    O  
ATOM   3077  CB  LYS A 433      13.550  21.039   8.234  1.00146.24      A    C  
ANISOU 3077  CB  LYS A 433    26839  18107  10620    570   -725  -3938  A    C  
ATOM   3078  CG  LYS A 433      13.446  22.531   8.486  1.00150.47      A    C  
ANISOU 3078  CG  LYS A 433    27582  18485  11104    953   -952  -4266  A    C  
ATOM   3079  CD  LYS A 433      12.668  22.840   9.747  1.00156.07      A    C  
ANISOU 3079  CD  LYS A 433    28603  19434  11261   1289   -699  -4479  A    C  
ATOM   3080  CE  LYS A 433      11.222  22.398   9.604  1.00158.58      A    C  
ANISOU 3080  CE  LYS A 433    28557  20286  11409   1339    -87  -4472  A    C  
ATOM   3081  NZ  LYS A 433      10.372  22.929  10.702  1.00161.50      A    N1+
ANISOU 3081  NZ  LYS A 433    29153  20935  11274   1732    179  -4731  A    N1+
ATOM   3082  N   CYS A 434      14.609  18.730   5.585  1.00133.96      A    N  
ANISOU 3082  N   CYS A 434    24425  16430  10044   -328   -736  -3268  A    N  
ATOM   3083  CA  CYS A 434      14.899  17.327   5.345  1.00130.39      A    C  
ANISOU 3083  CA  CYS A 434    23921  15980   9640   -645   -597  -2995  A    C  
ATOM   3084  C   CYS A 434      16.338  17.105   4.900  1.00121.98      A    C  
ANISOU 3084  C   CYS A 434    22885  14592   8871   -757  -1058  -2870  A    C  
ATOM   3085  O   CYS A 434      17.175  18.003   4.994  1.00111.93      A    O  
ANISOU 3085  O   CYS A 434    21718  13104   7707   -629  -1488  -3000  A    O  
ATOM   3086  CB  CYS A 434      13.928  16.763   4.302  1.00137.25      A    C  
ANISOU 3086  CB  CYS A 434    24290  17126  10731   -872   -192  -2917  A    C  
ATOM   3087  SG  CYS A 434      14.174  17.383   2.627  1.00125.53      A    S  
ANISOU 3087  SG  CYS A 434    22290  15570   9834   -913   -424  -2929  A    S  
ATOM   3088  N   LEU A 435      16.606  15.908   4.388  1.00123.71      A    N  
ANISOU 3088  N   LEU A 435    22994  14787   9222  -1007   -954  -2637  A    N  
ATOM   3089  CA  LEU A 435      17.950  15.537   3.967  1.00125.12      A    C  
ANISOU 3089  CA  LEU A 435    23164  14723   9653  -1083  -1349  -2514  A    C  
ATOM   3090  C   LEU A 435      18.265  16.077   2.580  1.00118.43      A    C  
ANISOU 3090  C   LEU A 435    21849  13829   9319  -1188  -1513  -2534  A    C  
ATOM   3091  O   LEU A 435      17.368  16.305   1.773  1.00114.60      A    O  
ANISOU 3091  O   LEU A 435    21031  13508   9003  -1251  -1253  -2563  A    O  
ATOM   3092  CB  LEU A 435      18.123  14.012   3.984  1.00126.08      A    C  
ANISOU 3092  CB  LEU A 435    23423  14802   9680  -1252  -1168  -2261  A    C  
ATOM   3093  CG  LEU A 435      18.273  13.269   5.317  1.00131.55      A    C  
ANISOU 3093  CG  LEU A 435    24692  15429   9861  -1143  -1115  -2156  A    C  
ATOM   3094  CD1 LEU A 435      16.979  13.244   6.121  1.00138.47      A    C  
ANISOU 3094  CD1 LEU A 435    25766  16517  10328  -1150   -632  -2198  A    C  
ATOM   3095  CD2 LEU A 435      18.772  11.850   5.067  1.00125.80      A    C  
ANISOU 3095  CD2 LEU A 435    24110  14540   9147  -1273  -1063  -1893  A    C  
ATOM   3096  N   LEU A 436      19.549  16.297   2.320  1.00115.97      A    N  
ANISOU 3096  N   LEU A 436    21506  13325   9232  -1199  -1945  -2526  A    N  
ATOM   3097  CA  LEU A 436      20.020  16.668   0.991  1.00119.89      A    C  
ANISOU 3097  CA  LEU A 436    21590  13766  10198  -1337  -2089  -2500  A    C  
ATOM   3098  C   LEU A 436      21.087  15.684   0.536  1.00132.77      A    C  
ANISOU 3098  C   LEU A 436    23111  15331  12003  -1457  -2257  -2333  A    C  
ATOM   3099  O   LEU A 436      21.957  15.302   1.319  1.00160.16      A    O  
ANISOU 3099  O   LEU A 436    26830  18725  15299  -1363  -2516  -2318  A    O  
ATOM   3100  CB  LEU A 436      20.576  18.091   0.979  1.00118.69      A    C  
ANISOU 3100  CB  LEU A 436    21452  13452  10192  -1270  -2437  -2687  A    C  
ATOM   3101  CG  LEU A 436      21.002  18.610  -0.396  1.00111.00      A    C  
ANISOU 3101  CG  LEU A 436    20100  12404   9670  -1429  -2543  -2647  A    C  
ATOM   3102  CD1 LEU A 436      19.822  19.231  -1.120  1.00106.75      A    C  
ANISOU 3102  CD1 LEU A 436    19396  11952   9214  -1365  -2265  -2681  A    C  
ATOM   3103  CD2 LEU A 436      22.147  19.604  -0.280  1.00115.76      A    C  
ANISOU 3103  CD2 LEU A 436    20770  12789  10427  -1485  -2974  -2779  A    C  
ATOM   3104  N   VAL A 437      21.024  15.272  -0.726  1.00106.65      A    N  
ANISOU 3104  N   VAL A 437    19435  12073   9012  -1624  -2123  -2222  A    N  
ATOM   3105  CA  VAL A 437      22.027  14.362  -1.262  1.00 94.81      A    C  
ANISOU 3105  CA  VAL A 437    17809  10525   7690  -1700  -2268  -2084  A    C  
ATOM   3106  C   VAL A 437      22.812  15.036  -2.371  1.00110.04      A    C  
ANISOU 3106  C   VAL A 437    19352  12435  10023  -1805  -2491  -2108  A    C  
ATOM   3107  O   VAL A 437      22.285  15.301  -3.450  1.00117.64      A    O  
ANISOU 3107  O   VAL A 437    20025  13463  11210  -1915  -2312  -2083  A    O  
ATOM   3108  CB  VAL A 437      21.409  13.078  -1.811  1.00 93.67      A    C  
ANISOU 3108  CB  VAL A 437    17605  10440   7544  -1826  -1907  -1928  A    C  
ATOM   3109  CG1 VAL A 437      22.484  12.012  -1.955  1.00 93.79      A    C  
ANISOU 3109  CG1 VAL A 437    17672  10355   7609  -1794  -2075  -1798  A    C  
ATOM   3110  CG2 VAL A 437      20.295  12.589  -0.899  1.00 96.60      A    C  
ANISOU 3110  CG2 VAL A 437    18299  10864   7540  -1824  -1556  -1912  A    C  
ATOM   3111  N   THR A 438      24.076  15.324  -2.094  1.00110.34      A    N  
ANISOU 3111  N   THR A 438    19383  12410  10132  -1775  -2881  -2162  A    N  
ATOM   3112  CA  THR A 438      24.922  16.047  -3.032  1.00115.31      A    C  
ANISOU 3112  CA  THR A 438    19662  13028  11124  -1925  -3089  -2196  A    C  
ATOM   3113  C   THR A 438      26.363  15.791  -2.652  1.00120.47      A    C  
ANISOU 3113  C   THR A 438    20257  13713  11805  -1892  -3475  -2236  A    C  
ATOM   3114  O   THR A 438      26.664  15.499  -1.497  1.00119.50      A    O  
ANISOU 3114  O   THR A 438    20427  13586  11394  -1716  -3661  -2293  A    O  
ATOM   3115  CB  THR A 438      24.651  17.567  -3.027  1.00120.45      A    C  
ANISOU 3115  CB  THR A 438    20356  13560  11849  -1982  -3166  -2344  A    C  
ATOM   3116  CG2 THR A 438      25.307  18.233  -4.217  1.00107.51      A    C  
ANISOU 3116  CG2 THR A 438    18378  11886  10585  -2197  -3256  -2321  A    C  
ATOM   3117  OG1 THR A 438      23.243  17.817  -3.071  1.00144.83      A    O  
ANISOU 3117  OG1 THR A 438    23550  16665  14812  -1899  -2841  -2348  A    O  
ATOM   3118  N   ASN A 439      27.254  15.866  -3.629  1.00124.68      A    N  
ANISOU 3118  N   ASN A 439    20396  14317  12659  -2040  -3590  -2211  A    N  
ATOM   3119  CA  ASN A 439      28.661  15.695  -3.352  1.00129.24      A    C  
ANISOU 3119  CA  ASN A 439    20809  15009  13289  -2011  -3964  -2285  A    C  
ATOM   3120  C   ASN A 439      29.351  17.062  -3.352  1.00114.71      A    C  
ANISOU 3120  C   ASN A 439    18819  13133  11633  -2244  -4235  -2468  A    C  
ATOM   3121  O   ASN A 439      30.573  17.154  -3.215  1.00102.29      A    O  
ANISOU 3121  O   ASN A 439    17007  11705  10154  -2306  -4562  -2580  A    O  
ATOM   3122  CB  ASN A 439      29.276  14.769  -4.404  1.00135.27      A    C  
ANISOU 3122  CB  ASN A 439    21207  15924  14266  -2016  -3898  -2156  A    C  
ATOM   3123  CG  ASN A 439      30.222  13.756  -3.810  1.00130.88      A    C  
ANISOU 3123  CG  ASN A 439    20672  15499  13556  -1749  -4151  -2159  A    C  
ATOM   3124  ND2 ASN A 439      31.349  13.537  -4.474  1.00142.28      A    N  
ANISOU 3124  ND2 ASN A 439    21686  17151  15224  -1766  -4316  -2181  A    N  
ATOM   3125  OD1 ASN A 439      29.937  13.166  -2.769  1.00118.20      A    O  
ANISOU 3125  OD1 ASN A 439    19476  13822  11611  -1504  -4188  -2137  A    O  
ATOM   3126  N   ASP A 440      28.560  18.126  -3.485  1.00110.89      A    N  
ANISOU 3126  N   ASP A 440    18487  12458  11188  -2370  -4099  -2513  A    N  
ATOM   3127  CA  ASP A 440      29.122  19.470  -3.565  1.00137.10      A    C  
ANISOU 3127  CA  ASP A 440    21752  15649  14688  -2634  -4309  -2675  A    C  
ATOM   3128  C   ASP A 440      29.550  19.995  -2.206  1.00160.89      A    C  
ANISOU 3128  C   ASP A 440    25046  18607  17479  -2584  -4664  -2922  A    C  
ATOM   3129  O   ASP A 440      28.719  20.213  -1.323  1.00162.50      A    O  
ANISOU 3129  O   ASP A 440    25666  18684  17393  -2392  -4616  -2994  A    O  
ATOM   3130  CB  ASP A 440      28.113  20.444  -4.187  1.00149.10      A    C  
ANISOU 3130  CB  ASP A 440    23418  16936  16298  -2721  -4050  -2635  A    C  
ATOM   3131  CG  ASP A 440      28.418  20.760  -5.638  1.00143.43      A    C  
ANISOU 3131  CG  ASP A 440    22361  16218  15920  -2977  -3912  -2500  A    C  
ATOM   3132  OD1 ASP A 440      29.614  20.826  -5.997  1.00133.48      A    O  
ANISOU 3132  OD1 ASP A 440    20784  15064  14868  -3218  -4092  -2530  A    O  
ATOM   3133  OD2 ASP A 440      27.460  20.953  -6.418  1.00140.01      A    O1-
ANISOU 3133  OD2 ASP A 440    21964  15709  15523  -2928  -3621  -2373  A    O1-
ATOM   3134  N   GLU A 441      30.849  20.216  -2.049  1.00176.74      A    N  
ANISOU 3134  N   GLU A 441    26799  20745  19608  -2762  -5021  -3075  A    N  
ATOM   3135  CA  GLU A 441      31.358  20.931  -0.892  1.00194.58      A    C  
ANISOU 3135  CA  GLU A 441    29276  22956  21700  -2800  -5405  -3364  A    C  
ATOM   3136  C   GLU A 441      30.846  22.361  -0.988  1.00190.28      A    C  
ANISOU 3136  C   GLU A 441    29006  22048  21245  -3033  -5343  -3485  A    C  
ATOM   3137  O   GLU A 441      30.627  23.021   0.028  1.00200.88      A    O  
ANISOU 3137  O   GLU A 441    30679  23255  22391  -2935  -5456  -3670  A    O  
ATOM   3138  CB  GLU A 441      32.890  20.872  -0.831  1.00216.96      A    C  
ANISOU 3138  CB  GLU A 441    31678  26077  24681  -2986  -5803  -3530  A    C  
ATOM   3139  CG  GLU A 441      33.619  21.656  -1.924  1.00234.11      A    C  
ANISOU 3139  CG  GLU A 441    33431  28240  27280  -3480  -5786  -3556  A    C  
ATOM   3140  CD  GLU A 441      33.401  21.103  -3.321  1.00236.44      A    C  
ANISOU 3140  CD  GLU A 441    33411  28603  27821  -3518  -5409  -3260  A    C  
ATOM   3141  OE1 GLU A 441      32.925  19.955  -3.448  1.00237.94      A    O  
ANISOU 3141  OE1 GLU A 441    33613  28911  27884  -3174  -5227  -3068  A    O  
ATOM   3142  OE2 GLU A 441      33.705  21.821  -4.296  1.00236.73      A    O1-
ANISOU 3142  OE2 GLU A 441    33224  28560  28163  -3906  -5289  -3223  A    O1-
ATOM   3143  N   MET A 442      30.688  22.815  -2.235  1.00177.21      A    N  
ANISOU 3143  N   MET A 442    27164  20263  19904  -3280  -5095  -3337  A    N  
ATOM   3144  CA  MET A 442      30.177  24.140  -2.601  1.00154.79      A    C  
ANISOU 3144  CA  MET A 442    24603  17031  17178  -3476  -4982  -3383  A    C  
ATOM   3145  C   MET A 442      30.927  25.289  -1.909  1.00134.27      A    C  
ANISOU 3145  C   MET A 442    22103  14270  14643  -3720  -5247  -3653  A    C  
ATOM   3146  O   MET A 442      30.343  26.330  -1.610  1.00137.75      A    O  
ANISOU 3146  O   MET A 442    22932  14369  15035  -3687  -5173  -3740  A    O  
ATOM   3147  CB  MET A 442      28.651  24.236  -2.386  1.00150.00      A    C  
ANISOU 3147  CB  MET A 442    24410  16248  16334  -3114  -4694  -3310  A    C  
ATOM   3148  CG  MET A 442      28.108  24.146  -0.969  1.00147.33      A    C  
ANISOU 3148  CG  MET A 442    24483  15902  15594  -2789  -4800  -3487  A    C  
ATOM   3149  SD  MET A 442      26.314  23.902  -0.935  1.00206.41      A    S  
ANISOU 3149  SD  MET A 442    32240  23364  22822  -2369  -4362  -3353  A    S  
ATOM   3150  CE  MET A 442      26.159  22.251  -1.597  1.00103.51      A    C  
ANISOU 3150  CE  MET A 442    18802  10696   9832  -2284  -4104  -3054  A    C  
ATOM   3151  N   ARG A 443      32.229  25.108  -1.686  1.00145.86      A    N  
ANISOU 3151  N   ARG A 443    23171  16016  16234  -3940  -5521  -3785  A    N  
ATOM   3152  CA  ARG A 443      33.040  26.150  -1.063  1.00162.74      A    C  
ANISOU 3152  CA  ARG A 443    25290  18079  18465  -4212  -5737  -4058  A    C  
ATOM   3153  C   ARG A 443      33.473  27.136  -2.148  1.00185.46      A    C  
ANISOU 3153  C   ARG A 443    28037  20713  21716  -4727  -5604  -4017  A    C  
ATOM   3154  O   ARG A 443      34.638  27.221  -2.535  1.00187.66      A    O  
ANISOU 3154  O   ARG A 443    27852  21208  22244  -5127  -5721  -4097  A    O  
ATOM   3155  CB  ARG A 443      34.254  25.556  -0.327  1.00157.18      A    C  
ANISOU 3155  CB  ARG A 443    24181  17836  17704  -4223  -6104  -4261  A    C  
ATOM   3156  CG  ARG A 443      35.163  24.656  -1.163  1.00153.04      A    C  
ANISOU 3156  CG  ARG A 443    23066  17710  17373  -4375  -6183  -4165  A    C  
ATOM   3157  CD  ARG A 443      36.532  24.473  -0.517  1.00157.93      A    C  
ANISOU 3157  CD  ARG A 443    23229  18783  17995  -4476  -6579  -4444  A    C  
ATOM   3158  NE  ARG A 443      37.138  25.750  -0.143  1.00165.37      A    N  
ANISOU 3158  NE  ARG A 443    24135  19610  19088  -4887  -6687  -4736  A    N  
ATOM   3159  CZ  ARG A 443      38.437  26.024  -0.230  1.00166.79      A    C  
ANISOU 3159  CZ  ARG A 443    23766  20125  19482  -5283  -6900  -4976  A    C  
ATOM   3160  NH1 ARG A 443      39.285  25.112  -0.688  1.00167.05      A    N1+
ANISOU 3160  NH1 ARG A 443    23210  20664  19598  -5286  -7044  -4954  A    N1+
ATOM   3161  NH2 ARG A 443      38.890  27.216   0.136  1.00171.23      A    N  
ANISOU 3161  NH2 ARG A 443    24357  20528  20175  -5677  -6970  -5260  A    N  
ATOM   3162  N   ASP A 444      32.498  27.905  -2.619  1.00194.94      A    N  
ANISOU 3162  N   ASP A 444    29676  21464  22930  -4698  -5348  -3893  A    N  
ATOM   3163  CA  ASP A 444      32.719  28.888  -3.667  1.00195.56      A    C  
ANISOU 3163  CA  ASP A 444    29788  21214  23301  -5130  -5176  -3799  A    C  
ATOM   3164  C   ASP A 444      32.147  30.236  -3.243  1.00213.19      A    C  
ANISOU 3164  C   ASP A 444    32615  22914  25475  -5109  -5130  -3916  A    C  
ATOM   3165  O   ASP A 444      31.258  30.308  -2.397  1.00215.76      A    O  
ANISOU 3165  O   ASP A 444    33339  23122  25519  -4684  -5146  -4001  A    O  
ATOM   3166  CB  ASP A 444      32.080  28.415  -4.978  1.00182.86      A    C  
ANISOU 3166  CB  ASP A 444    28151  19567  21759  -5090  -4894  -3472  A    C  
ATOM   3167  CG  ASP A 444      32.211  29.431  -6.097  1.00181.75      A    C  
ANISOU 3167  CG  ASP A 444    28140  19052  21864  -5497  -4687  -3327  A    C  
ATOM   3168  OD1 ASP A 444      31.423  30.400  -6.115  1.00181.44      A    O  
ANISOU 3168  OD1 ASP A 444    28661  18525  21752  -5388  -4574  -3308  A    O  
ATOM   3169  OD2 ASP A 444      33.095  29.256  -6.961  1.00181.71      A    O1-
ANISOU 3169  OD2 ASP A 444    27699  19242  22102  -5903  -4629  -3225  A    O1-
ATOM   3170  N   HIS A 445      32.660  31.294  -3.863  1.00231.57      A    N  
ANISOU 3170  N   HIS A 445    35012  24916  28056  -5569  -5051  -3911  A    N  
ATOM   3171  CA  HIS A 445      32.393  32.675  -3.472  1.00244.39      A    C  
ANISOU 3171  CA  HIS A 445    37193  26000  29664  -5638  -5041  -4053  A    C  
ATOM   3172  C   HIS A 445      30.906  33.011  -3.463  1.00237.45      A    C  
ANISOU 3172  C   HIS A 445    36943  24740  28539  -5129  -4877  -3945  A    C  
ATOM   3173  O   HIS A 445      30.415  33.664  -2.540  1.00242.24      A    O  
ANISOU 3173  O   HIS A 445    37989  25096  28954  -4876  -4954  -4142  A    O  
ATOM   3174  CB  HIS A 445      33.136  33.620  -4.418  1.00255.15      A    C  
ANISOU 3174  CB  HIS A 445    38540  27057  31347  -6238  -4909  -3976  A    C  
ATOM   3175  CG  HIS A 445      34.557  33.219  -4.671  1.00263.82      A    C  
ANISOU 3175  CG  HIS A 445    38932  28597  32709  -6748  -5011  -4056  A    C  
ATOM   3176  CD2 HIS A 445      35.188  32.853  -5.812  1.00266.52      A    C  
ANISOU 3176  CD2 HIS A 445    38824  29155  33285  -7110  -4854  -3849  A    C  
ATOM   3177  ND1 HIS A 445      35.500  33.135  -3.669  1.00268.10      A    N  
ANISOU 3177  ND1 HIS A 445    39126  29468  33271  -6902  -5313  -4407  A    N  
ATOM   3178  CE1 HIS A 445      36.655  32.752  -4.184  1.00270.02      A    C  
ANISOU 3178  CE1 HIS A 445    38716  30115  33763  -7327  -5349  -4428  A    C  
ATOM   3179  NE2 HIS A 445      36.492  32.573  -5.483  1.00270.97      A    N  
ANISOU 3179  NE2 HIS A 445    38761  30178  34019  -7466  -5059  -4085  A    N  
ATOM   3180  N   ILE A 446      30.201  32.580  -4.504  1.00221.73      A    N  
ANISOU 3180  N   ILE A 446    34979  22726  26543  -4974  -4655  -3656  A    N  
ATOM   3181  CA  ILE A 446      28.764  32.808  -4.609  1.00215.62      A    C  
ANISOU 3181  CA  ILE A 446    34731  21666  25529  -4459  -4500  -3571  A    C  
ATOM   3182  C   ILE A 446      28.048  32.138  -3.442  1.00213.63      A    C  
ANISOU 3182  C   ILE A 446    34520  21694  24955  -3945  -4589  -3733  A    C  
ATOM   3183  O   ILE A 446      27.198  32.739  -2.785  1.00204.01      A    O  
ANISOU 3183  O   ILE A 446    33777  20229  23509  -3566  -4574  -3865  A    O  
ATOM   3184  CB  ILE A 446      28.183  32.273  -5.943  1.00133.84      A    C  
ANISOU 3184  CB  ILE A 446    24304  11343  15206  -4385  -4274  -3266  A    C  
ATOM   3185  CG1 ILE A 446      28.577  33.164  -7.132  1.00137.28      A    C  
ANISOU 3185  CG1 ILE A 446    24918  11370  15873  -4792  -4121  -3066  A    C  
ATOM   3186  CG2 ILE A 446      26.666  32.252  -5.884  1.00123.88      A    C  
ANISOU 3186  CG2 ILE A 446    23452   9965  13651  -3763  -4146  -3248  A    C  
ATOM   3187  CD1 ILE A 446      30.053  33.184  -7.499  1.00138.68      A    C  
ANISOU 3187  CD1 ILE A 446    24613  11714  16365  -5454  -4156  -3043  A    C  
ATOM   3188  N   PHE A 447      28.411  30.885  -3.191  1.00220.89      A    N  
ANISOU 3188  N   PHE A 447    34954  23131  25841  -3926  -4667  -3715  A    N  
ATOM   3189  CA  PHE A 447      27.871  30.118  -2.075  1.00223.64      A    C  
ANISOU 3189  CA  PHE A 447    35319  23781  25873  -3496  -4731  -3833  A    C  
ATOM   3190  C   PHE A 447      28.340  30.632  -0.714  1.00262.41      A    C  
ANISOU 3190  C   PHE A 447    40372  28671  30661  -3483  -4963  -4126  A    C  
ATOM   3191  O   PHE A 447      27.539  30.796   0.206  1.00265.57      A    O  
ANISOU 3191  O   PHE A 447    41120  29022  30763  -3084  -4950  -4256  A    O  
ATOM   3192  CB  PHE A 447      28.250  28.644  -2.218  1.00220.08      A    C  
ANISOU 3192  CB  PHE A 447    34364  23837  25418  -3501  -4759  -3713  A    C  
ATOM   3193  CG  PHE A 447      27.673  27.986  -3.439  1.00207.28      A    C  
ANISOU 3193  CG  PHE A 447    32605  22293  23859  -3463  -4529  -3455  A    C  
ATOM   3194  CD1 PHE A 447      26.357  27.554  -3.455  1.00200.09      A    C  
ANISOU 3194  CD1 PHE A 447    31790  21494  22740  -2994  -4254  -3338  A    C  
ATOM   3195  CD2 PHE A 447      28.451  27.793  -4.570  1.00201.11      A    C  
ANISOU 3195  CD2 PHE A 447    31405  21615  23393  -3823  -4462  -3265  A    C  
ATOM   3196  CE1 PHE A 447      25.825  26.948  -4.578  1.00194.72      A    C  
ANISOU 3196  CE1 PHE A 447    30804  21011  22168  -2895  -3951  -3055  A    C  
ATOM   3197  CE2 PHE A 447      27.927  27.188  -5.692  1.00194.41      A    C  
ANISOU 3197  CE2 PHE A 447    30286  20948  22634  -3693  -4149  -2968  A    C  
ATOM   3198  CZ  PHE A 447      26.612  26.764  -5.697  1.00192.58      A    C  
ANISOU 3198  CZ  PHE A 447    30161  20813  22196  -3233  -3909  -2871  A    C  
ATOM   3199  N   GLU A 448      29.641  30.886  -0.600  1.00301.87      A    N  
ANISOU 3199  N   GLU A 448    45081  33737  35878  -3925  -5170  -4249  A    N  
ATOM   3200  CA  GLU A 448      30.252  31.273   0.671  1.00334.24      A    C  
ANISOU 3200  CA  GLU A 448    49233  37896  39867  -3965  -5434  -4562  A    C  
ATOM   3201  C   GLU A 448      29.843  32.667   1.155  1.00360.33      A    C  
ANISOU 3201  C   GLU A 448    53102  40700  43108  -3927  -5430  -4753  A    C  
ATOM   3202  O   GLU A 448      29.893  32.938   2.351  1.00384.66      A    O  
ANISOU 3202  O   GLU A 448    56367  43809  45977  -3778  -5602  -5013  A    O  
ATOM   3203  CB  GLU A 448      31.779  31.180   0.583  1.00340.45      A    C  
ANISOU 3203  CB  GLU A 448    49499  38942  40915  -4471  -5661  -4685  A    C  
ATOM   3204  CG  GLU A 448      32.462  31.189   1.942  1.00343.59      A    C  
ANISOU 3204  CG  GLU A 448    49827  39583  41140  -4450  -5982  -5021  A    C  
ATOM   3205  CD  GLU A 448      31.878  30.154   2.888  1.00339.34      A    C  
ANISOU 3205  CD  GLU A 448    49364  39364  40204  -3910  -6039  -5003  A    C  
ATOM   3206  OE1 GLU A 448      31.712  28.988   2.469  1.00331.90      A    O  
ANISOU 3206  OE1 GLU A 448    48174  38712  39220  -3735  -5961  -4776  A    O  
ATOM   3207  OE2 GLU A 448      31.577  30.509   4.047  1.00342.28      A    O1-
ANISOU 3207  OE2 GLU A 448    50071  39683  40295  -3668  -6148  -5213  A    O1-
ATOM   3208  N   LEU A 449      29.508  33.571   0.239  1.00316.82      A    N  
ANISOU 3208  N   LEU A 449    47887  34720  37769  -4065  -5250  -4632  A    N  
ATOM   3209  CA  LEU A 449      28.998  34.873   0.659  1.00278.36      A    C  
ANISOU 3209  CA  LEU A 449    43633  29327  32804  -3944  -5233  -4793  A    C  
ATOM   3210  C   LEU A 449      27.723  34.640   1.467  1.00252.59      A    C  
ANISOU 3210  C   LEU A 449    40711  26118  29144  -3281  -5162  -4849  A    C  
ATOM   3211  O   LEU A 449      27.540  35.222   2.538  1.00251.16      A    O  
ANISOU 3211  O   LEU A 449    40859  25813  28757  -3091  -5270  -5105  A    O  
ATOM   3212  CB  LEU A 449      28.740  35.792  -0.537  1.00267.21      A    C  
ANISOU 3212  CB  LEU A 449    42550  27385  31593  -4115  -5030  -4599  A    C  
ATOM   3213  CG  LEU A 449      29.755  36.926  -0.719  1.00255.32      A    C  
ANISOU 3213  CG  LEU A 449    41149  25498  30362  -4705  -5101  -4719  A    C  
ATOM   3214  CD1 LEU A 449      29.704  37.897   0.455  1.00252.53      A    C  
ANISOU 3214  CD1 LEU A 449    41249  24849  29853  -4612  -5259  -5062  A    C  
ATOM   3215  CD2 LEU A 449      31.161  36.372  -0.889  1.00249.10      A    C  
ANISOU 3215  CD2 LEU A 449    39674  25127  29846  -5277  -5237  -4765  A    C  
ATOM   3216  N   LEU A 450      26.851  33.777   0.954  1.00231.41      A    N  
ANISOU 3216  N   LEU A 450    37931  23646  26347  -2947  -4968  -4627  A    N  
ATOM   3217  CA  LEU A 450      25.693  33.324   1.718  1.00209.58      A    C  
ANISOU 3217  CA  LEU A 450    35360  21071  23199  -2358  -4866  -4680  A    C  
ATOM   3218  C   LEU A 450      26.139  32.395   2.840  1.00205.96      A    C  
ANISOU 3218  C   LEU A 450    34623  21084  22547  -2306  -5029  -4795  A    C  
ATOM   3219  O   LEU A 450      25.582  32.420   3.939  1.00202.66      A    O  
ANISOU 3219  O   LEU A 450    34453  20750  21800  -1941  -5036  -4958  A    O  
ATOM   3220  CB  LEU A 450      24.678  32.616   0.822  1.00187.41      A    C  
ANISOU 3220  CB  LEU A 450    32477  18402  20327  -2071  -4605  -4442  A    C  
ATOM   3221  CG  LEU A 450      23.466  33.449   0.404  1.00179.63      A    C  
ANISOU 3221  CG  LEU A 450    31977  17059  19216  -1658  -4412  -4440  A    C  
ATOM   3222  CD1 LEU A 450      23.875  34.525  -0.592  1.00185.89      A    C  
ANISOU 3222  CD1 LEU A 450    33015  17320  20296  -1958  -4418  -4347  A    C  
ATOM   3223  CD2 LEU A 450      22.353  32.565  -0.156  1.00156.78      A    C  
ANISOU 3223  CD2 LEU A 450    28949  14468  16153  -1287  -4168  -4299  A    C  
ATOM   3224  N   GLY A 451      27.141  31.569   2.542  1.00212.13      A    N  
ANISOU 3224  N   GLY A 451    34906  22179  23514  -2643  -5153  -4703  A    N  
ATOM   3225  CA  GLY A 451      27.634  30.576   3.477  1.00217.36      A    C  
ANISOU 3225  CA  GLY A 451    35308  23294  23987  -2565  -5324  -4772  A    C  
ATOM   3226  C   GLY A 451      28.134  31.230   4.744  1.00228.61      A    C  
ANISOU 3226  C   GLY A 451    36926  24678  25257  -2576  -5574  -5091  A    C  
ATOM   3227  O   GLY A 451      28.858  32.220   4.706  1.00246.17      A    O  
ANISOU 3227  O   GLY A 451    39199  26644  27691  -2930  -5724  -5268  A    O  
ATOM   3228  N   SER A 452      27.747  30.676   5.881  1.00221.57      A    N  
ANISOU 3228  N   SER A 452    36161  24042  23983  -2205  -5609  -5172  A    N  
ATOM   3229  CA  SER A 452      28.034  31.324   7.148  1.00214.96      A    C  
ANISOU 3229  CA  SER A 452    35581  23164  22932  -2142  -5824  -5485  A    C  
ATOM   3230  C   SER A 452      28.510  30.347   8.211  1.00190.78      A    C  
ANISOU 3230  C   SER A 452    32363  20556  19569  -1984  -6024  -5545  A    C  
ATOM   3231  O   SER A 452      29.280  29.426   7.943  1.00182.63      A    O  
ANISOU 3231  O   SER A 452    30922  19842  18629  -2127  -6152  -5433  A    O  
ATOM   3232  CB  SER A 452      26.787  32.054   7.647  1.00231.19      A    C  
ANISOU 3232  CB  SER A 452    38173  24948  24722  -1732  -5627  -5577  A    C  
ATOM   3233  OG  SER A 452      25.611  31.302   7.378  1.00226.62      A    O  
ANISOU 3233  OG  SER A 452    37635  24520  23951  -1349  -5312  -5355  A    O  
ATOM   3234  N   THR A 453      28.053  30.590   9.432  1.00182.65      A    N  
ANISOU 3234  N   THR A 453    31696  19545  18159  -1662  -6055  -5726  A    N  
ATOM   3235  CA  THR A 453      28.266  29.689  10.549  1.00175.45      A    C  
ANISOU 3235  CA  THR A 453    30772  19028  16861  -1409  -6196  -5755  A    C  
ATOM   3236  C   THR A 453      27.068  28.745  10.581  1.00164.78      A    C  
ANISOU 3236  C   THR A 453    29562  17824  15223   -997  -5847  -5490  A    C  
ATOM   3237  O   THR A 453      27.179  27.566  10.926  1.00165.69      A    O  
ANISOU 3237  O   THR A 453    29572  18266  15117   -840  -5853  -5332  A    O  
ATOM   3238  CB  THR A 453      28.400  30.453  11.864  1.00180.13      A    C  
ANISOU 3238  CB  THR A 453    31698  19577  17166  -1293  -6397  -6094  A    C  
ATOM   3239  CG2 THR A 453      29.559  31.441  11.776  1.00186.04      A    C  
ANISOU 3239  CG2 THR A 453    32303  20168  18214  -1770  -6716  -6390  A    C  
ATOM   3240  OG1 THR A 453      27.186  31.170  12.129  1.00178.65      A    O  
ANISOU 3240  OG1 THR A 453    31968  19113  16799   -988  -6134  -6150  A    O  
ATOM   3241  N   PHE A 454      25.923  29.293  10.184  1.00173.10      A    N  
ANISOU 3241  N   PHE A 454    30862  18630  16278   -830  -5535  -5452  A    N  
ATOM   3242  CA  PHE A 454      24.675  28.553  10.043  1.00171.46      A    C  
ANISOU 3242  CA  PHE A 454    30746  18563  15839   -497  -5148  -5240  A    C  
ATOM   3243  C   PHE A 454      24.822  27.494   8.950  1.00163.62      A    C  
ANISOU 3243  C   PHE A 454    29381  17722  15066   -666  -5043  -4941  A    C  
ATOM   3244  O   PHE A 454      24.316  26.380   9.084  1.00170.03      A    O  
ANISOU 3244  O   PHE A 454    30170  18792  15640   -484  -4841  -4752  A    O  
ATOM   3245  CB  PHE A 454      23.520  29.517   9.733  1.00177.13      A    C  
ANISOU 3245  CB  PHE A 454    31749  19000  16551   -288  -4881  -5316  A    C  
ATOM   3246  CG  PHE A 454      22.201  28.840   9.458  1.00177.24      A    C  
ANISOU 3246  CG  PHE A 454    31783  19207  16354     21  -4462  -5142  A    C  
ATOM   3247  CD1 PHE A 454      21.863  27.642  10.064  1.00176.66      A    C  
ANISOU 3247  CD1 PHE A 454    31678  19507  15939    186  -4298  -5005  A    C  
ATOM   3248  CD2 PHE A 454      21.293  29.414   8.587  1.00177.63      A    C  
ANISOU 3248  CD2 PHE A 454    31893  19070  16527    143  -4224  -5123  A    C  
ATOM   3249  CE1 PHE A 454      20.661  27.031   9.795  1.00174.96      A    C  
ANISOU 3249  CE1 PHE A 454    31451  19493  15531    399  -3883  -4869  A    C  
ATOM   3250  CE2 PHE A 454      20.082  28.806   8.325  1.00168.20      A    C  
ANISOU 3250  CE2 PHE A 454    30658  18120  15129    413  -3838  -5009  A    C  
ATOM   3251  CZ  PHE A 454      19.764  27.616   8.927  1.00164.31      A    C  
ANISOU 3251  CZ  PHE A 454    30095  18020  14316    509  -3654  -4890  A    C  
ATOM   3252  N   PHE A 455      25.517  27.841   7.871  1.00156.46      A    N  
ANISOU 3252  N   PHE A 455    28202  16647  14600  -1030  -5164  -4900  A    N  
ATOM   3253  CA  PHE A 455      25.637  26.935   6.730  1.00156.90      A    C  
ANISOU 3253  CA  PHE A 455    27906  16822  14885  -1195  -5057  -4632  A    C  
ATOM   3254  C   PHE A 455      26.328  25.614   7.058  1.00129.91      A    C  
ANISOU 3254  C   PHE A 455    24262  13755  11342  -1189  -5195  -4505  A    C  
ATOM   3255  O   PHE A 455      25.846  24.549   6.667  1.00132.49      A    O  
ANISOU 3255  O   PHE A 455    24515  14243  11580  -1089  -4980  -4277  A    O  
ATOM   3256  CB  PHE A 455      26.387  27.625   5.600  1.00158.51      A    C  
ANISOU 3256  CB  PHE A 455    27867  16793  15567  -1611  -5177  -4629  A    C  
ATOM   3257  CG  PHE A 455      26.107  27.046   4.249  1.00159.00      A    C  
ANISOU 3257  CG  PHE A 455    27676  16877  15861  -1729  -4971  -4368  A    C  
ATOM   3258  CD1 PHE A 455      24.806  26.867   3.826  1.00148.16      A    C  
ANISOU 3258  CD1 PHE A 455    26458  15478  14358  -1476  -4633  -4252  A    C  
ATOM   3259  CD2 PHE A 455      27.148  26.725   3.378  1.00154.67      A    C  
ANISOU 3259  CD2 PHE A 455    26713  16399  15654  -2097  -5113  -4267  A    C  
ATOM   3260  CE1 PHE A 455      24.537  26.333   2.580  1.00132.68      A    C  
ANISOU 3260  CE1 PHE A 455    24266  13557  12589  -1589  -4455  -4037  A    C  
ATOM   3261  CE2 PHE A 455      26.880  26.202   2.127  1.00125.59      A    C  
ANISOU 3261  CE2 PHE A 455    22811  12739  12168  -2201  -4920  -4034  A    C  
ATOM   3262  CZ  PHE A 455      25.566  26.007   1.734  1.00116.73      A    C  
ANISOU 3262  CZ  PHE A 455    21873  11579  10902  -1949  -4599  -3921  A    C  
ATOM   3263  N   GLN A 456      27.427  25.689   7.801  1.00133.68      A    N  
ANISOU 3263  N   GLN A 456    24660  14349  11784  -1273  -5554  -4667  A    N  
ATOM   3264  CA  GLN A 456      28.141  24.507   8.260  1.00140.29      A    C  
ANISOU 3264  CA  GLN A 456    25344  15518  12443  -1179  -5743  -4578  A    C  
ATOM   3265  C   GLN A 456      27.296  23.689   9.232  1.00145.95      A    C  
ANISOU 3265  C   GLN A 456    26420  16381  12654   -770  -5548  -4471  A    C  
ATOM   3266  O   GLN A 456      27.417  22.470   9.291  1.00142.18      A    O  
ANISOU 3266  O   GLN A 456    25913  16102  12007   -639  -5525  -4270  A    O  
ATOM   3267  CB  GLN A 456      29.476  24.904   8.892  1.00166.96      A    C  
ANISOU 3267  CB  GLN A 456    28550  19023  15862  -1334  -6193  -4830  A    C  
ATOM   3268  CG  GLN A 456      30.638  24.987   7.907  1.00186.80      A    C  
ANISOU 3268  CG  GLN A 456    30552  21603  18822  -1744  -6405  -4852  A    C  
ATOM   3269  CD  GLN A 456      30.280  25.706   6.612  1.00185.12      A    C  
ANISOU 3269  CD  GLN A 456    30235  21080  19021  -2054  -6175  -4775  A    C  
ATOM   3270  NE2 GLN A 456      30.732  25.157   5.490  1.00166.54      A    N  
ANISOU 3270  NE2 GLN A 456    27491  18823  16965  -2267  -6149  -4602  A    N  
ATOM   3271  OE1 GLN A 456      29.614  26.744   6.621  1.00191.96      A    O  
ANISOU 3271  OE1 GLN A 456    31393  21623  19919  -2074  -6027  -4869  A    O  
ATOM   3272  N   LYS A 457      26.461  24.368  10.013  1.00160.04      A    N  
ANISOU 3272  N   LYS A 457    28568  18060  14180   -567  -5399  -4608  A    N  
ATOM   3273  CA  LYS A 457      25.558  23.681  10.932  1.00165.33      A    C  
ANISOU 3273  CA  LYS A 457    29586  18879  14355   -210  -5144  -4510  A    C  
ATOM   3274  C   LYS A 457      24.526  22.890  10.143  1.00157.36      A    C  
ANISOU 3274  C   LYS A 457    28556  17902  13333   -175  -4711  -4249  A    C  
ATOM   3275  O   LYS A 457      24.283  21.712  10.415  1.00162.11      A    O  
ANISOU 3275  O   LYS A 457    29263  18676  13657    -44  -4550  -4040  A    O  
ATOM   3276  CB  LYS A 457      24.848  24.676  11.852  1.00165.81      A    C  
ANISOU 3276  CB  LYS A 457    30001  18839  14161     -4  -5053  -4741  A    C  
ATOM   3277  CG  LYS A 457      25.743  25.378  12.854  1.00167.72      A    C  
ANISOU 3277  CG  LYS A 457    30344  19077  14304     -6  -5454  -5024  A    C  
ATOM   3278  CD  LYS A 457      25.039  26.594  13.439  1.00174.48      A    C  
ANISOU 3278  CD  LYS A 457    31526  19739  15028    137  -5360  -5281  A    C  
ATOM   3279  CE  LYS A 457      23.653  26.240  13.964  1.00173.21      A    C  
ANISOU 3279  CE  LYS A 457    31666  19692  14453    499  -4924  -5189  A    C  
ATOM   3280  NZ  LYS A 457      22.885  27.455  14.364  1.00181.37      A    N1+
ANISOU 3280  NZ  LYS A 457    32985  20538  15389    679  -4805  -5442  A    N1+
ATOM   3281  N   TRP A 458      23.941  23.547   9.150  1.00143.61      A    N  
ANISOU 3281  N   TRP A 458    26698  15984  11884   -304  -4526  -4265  A    N  
ATOM   3282  CA  TRP A 458      22.931  22.928   8.313  1.00135.30      A    C  
ANISOU 3282  CA  TRP A 458    25582  14987  10841   -297  -4124  -4068  A    C  
ATOM   3283  C   TRP A 458      23.499  21.796   7.466  1.00132.54      A    C  
ANISOU 3283  C   TRP A 458    24958  14727  10675   -494  -4160  -3830  A    C  
ATOM   3284  O   TRP A 458      22.834  20.781   7.258  1.00135.00      A    O  
ANISOU 3284  O   TRP A 458    25315  15168  10813   -452  -3853  -3638  A    O  
ATOM   3285  CB  TRP A 458      22.292  23.973   7.405  1.00137.93      A    C  
ANISOU 3285  CB  TRP A 458    25851  15110  11446   -354  -3985  -4161  A    C  
ATOM   3286  CG  TRP A 458      21.007  23.525   6.795  1.00138.38      A    C  
ANISOU 3286  CG  TRP A 458    25889  15288  11400   -256  -3545  -4045  A    C  
ATOM   3287  CD1 TRP A 458      19.776  23.496   7.384  1.00123.05      A    C  
ANISOU 3287  CD1 TRP A 458    24155  13513   9086     23  -3189  -4102  A    C  
ATOM   3288  CD2 TRP A 458      20.834  22.999   5.474  1.00127.90      A    C  
ANISOU 3288  CD2 TRP A 458    24286  13981  10328   -452  -3404  -3873  A    C  
ATOM   3289  CE2 TRP A 458      19.469  22.691   5.325  1.00126.74      A    C  
ANISOU 3289  CE2 TRP A 458    24116  14041   9997   -286  -2945  -3818  A    C  
ATOM   3290  CE3 TRP A 458      21.703  22.768   4.403  1.00130.37      A    C  
ANISOU 3290  CE3 TRP A 458    24284  14207  11043   -754  -3589  -3746  A    C  
ATOM   3291  NE1 TRP A 458      18.843  23.007   6.500  1.00120.01      A    N  
ANISOU 3291  NE1 TRP A 458    23615  13271   8712      0  -2835  -3994  A    N  
ATOM   3292  CZ2 TRP A 458      18.954  22.158   4.145  1.00127.17      A    C  
ANISOU 3292  CZ2 TRP A 458    23739  14240  10341   -413  -2650  -3598  A    C  
ATOM   3293  CZ3 TRP A 458      21.190  22.242   3.237  1.00110.51      A    C  
ANISOU 3293  CZ3 TRP A 458    21380  11813   8797   -852  -3279  -3512  A    C  
ATOM   3294  CH2 TRP A 458      19.828  21.943   3.116  1.00115.23      A    C  
ANISOU 3294  CH2 TRP A 458    21917  12621   9246   -685  -2830  -3447  A    C  
ATOM   3295  N   LYS A 459      24.725  21.967   6.976  1.00121.88      A    N  
ANISOU 3295  N   LYS A 459    23323  13319   9668   -722  -4518  -3857  A    N  
ATOM   3296  CA  LYS A 459      25.355  20.931   6.156  1.00118.90      A    C  
ANISOU 3296  CA  LYS A 459    22664  13039   9472   -878  -4584  -3657  A    C  
ATOM   3297  C   LYS A 459      25.613  19.643   6.939  1.00140.28      A    C  
ANISOU 3297  C   LYS A 459    25553  15935  11813   -670  -4621  -3513  A    C  
ATOM   3298  O   LYS A 459      25.285  18.563   6.463  1.00142.39      A    O  
ANISOU 3298  O   LYS A 459    25834  16256  12011   -671  -4408  -3296  A    O  
ATOM   3299  CB  LYS A 459      26.659  21.451   5.532  1.00119.29      A    C  
ANISOU 3299  CB  LYS A 459    22334  13043   9946  -1162  -4954  -3749  A    C  
ATOM   3300  CG  LYS A 459      26.442  22.348   4.311  1.00117.04      A    C  
ANISOU 3300  CG  LYS A 459    21852  12547  10073  -1433  -4846  -3764  A    C  
ATOM   3301  CD  LYS A 459      27.748  22.843   3.695  1.00118.04      A    C  
ANISOU 3301  CD  LYS A 459    21600  12644  10604  -1775  -5157  -3841  A    C  
ATOM   3302  CE  LYS A 459      28.748  21.717   3.482  1.00117.37      A    C  
ANISOU 3302  CE  LYS A 459    21202  12827  10567  -1815  -5363  -3738  A    C  
ATOM   3303  NZ  LYS A 459      30.109  22.255   3.183  1.00119.89      A    N1+
ANISOU 3303  NZ  LYS A 459    21126  13215  11211  -2129  -5697  -3886  A    N1+
ATOM   3304  N   GLU A 460      26.167  19.754   8.142  1.00153.80      A    N  
ANISOU 3304  N   GLU A 460    27447  17728  13263   -483  -4881  -3631  A    N  
ATOM   3305  CA  GLU A 460      26.379  18.583   8.987  1.00171.43      A    C  
ANISOU 3305  CA  GLU A 460    29941  20110  15087   -222  -4919  -3479  A    C  
ATOM   3306  C   GLU A 460      25.021  18.006   9.356  1.00172.68      A    C  
ANISOU 3306  C   GLU A 460    30479  20263  14866    -82  -4420  -3315  A    C  
ATOM   3307  O   GLU A 460      24.856  16.794   9.472  1.00186.14      A    O  
ANISOU 3307  O   GLU A 460    32394  22013  16319     14  -4251  -3079  A    O  
ATOM   3308  CB  GLU A 460      27.191  18.939  10.236  1.00188.34      A    C  
ANISOU 3308  CB  GLU A 460    32205  22357  16998    -33  -5301  -3663  A    C  
ATOM   3309  CG  GLU A 460      28.453  19.734   9.954  1.00197.74      A    C  
ANISOU 3309  CG  GLU A 460    32987  23588  18556   -242  -5759  -3898  A    C  
ATOM   3310  CD  GLU A 460      29.544  18.967   9.205  1.00202.35      A    C  
ANISOU 3310  CD  GLU A 460    33191  24319  19374   -324  -6021  -3805  A    C  
ATOM   3311  OE1 GLU A 460      29.323  17.829   8.741  1.00201.61      A    O  
ANISOU 3311  OE1 GLU A 460    33156  24240  19207   -226  -5853  -3549  A    O  
ATOM   3312  OE2 GLU A 460      30.630  19.552   9.021  1.00204.41      A    O1-
ANISOU 3312  OE2 GLU A 460    33073  24684  19911   -515  -6383  -4009  A    O1-
ATOM   3313  N   ARG A 461      24.047  18.892   9.514  1.00150.12      A    N  
ANISOU 3313  N   ARG A 461    27713  17355  11971    -77  -4170  -3449  A    N  
ATOM   3314  CA  ARG A 461      22.687  18.499   9.851  1.00142.05      A    C  
ANISOU 3314  CA  ARG A 461    26974  16400  10600     28  -3661  -3348  A    C  
ATOM   3315  C   ARG A 461      21.985  17.710   8.733  1.00135.43      A    C  
ANISOU 3315  C   ARG A 461    26003  15571   9883   -169  -3286  -3149  A    C  
ATOM   3316  O   ARG A 461      21.239  16.774   9.018  1.00126.71      A    O  
ANISOU 3316  O   ARG A 461    25141  14555   8450   -144  -2901  -2971  A    O  
ATOM   3317  CB  ARG A 461      21.870  19.741  10.220  1.00146.93      A    C  
ANISOU 3317  CB  ARG A 461    27661  16996  11168    124  -3522  -3588  A    C  
ATOM   3318  CG  ARG A 461      20.400  19.496  10.531  1.00150.16      A    C  
ANISOU 3318  CG  ARG A 461    28270  17553  11230    237  -2973  -3543  A    C  
ATOM   3319  CD  ARG A 461      20.207  18.535  11.686  1.00157.01      A    C  
ANISOU 3319  CD  ARG A 461    29513  18563  11580    397  -2790  -3383  A    C  
ATOM   3320  NE  ARG A 461      18.795  18.219  11.893  1.00170.58      A    N  
ANISOU 3320  NE  ARG A 461    31360  20469  12982    425  -2202  -3327  A    N  
ATOM   3321  CZ  ARG A 461      18.165  17.175  11.361  1.00178.88      A    C  
ANISOU 3321  CZ  ARG A 461    32396  21606  13963    233  -1790  -3104  A    C  
ATOM   3322  NH1 ARG A 461      18.819  16.319  10.587  1.00178.58      A    N1+
ANISOU 3322  NH1 ARG A 461    32269  21445  14140     37  -1915  -2906  A    N1+
ATOM   3323  NH2 ARG A 461      16.876  16.986  11.606  1.00182.98      A    N  
ANISOU 3323  NH2 ARG A 461    32977  22354  14194    223  -1238  -3095  A    N  
ATOM   3324  N   HIS A 462      22.198  18.087   7.472  1.00138.14      A    N  
ANISOU 3324  N   HIS A 462    25979  15827  10682   -391  -3372  -3181  A    N  
ATOM   3325  CA  HIS A 462      21.330  17.587   6.400  1.00128.61      A    C  
ANISOU 3325  CA  HIS A 462    24449  14686   9731   -563  -2922  -2989  A    C  
ATOM   3326  C   HIS A 462      21.997  16.939   5.176  1.00132.65      A    C  
ANISOU 3326  C   HIS A 462    24541  15166  10694   -778  -2988  -2799  A    C  
ATOM   3327  O   HIS A 462      21.340  16.212   4.427  1.00129.95      A    O  
ANISOU 3327  O   HIS A 462    23991  14896  10487   -911  -2617  -2617  A    O  
ATOM   3328  CB  HIS A 462      20.442  18.736   5.929  1.00113.83      A    C  
ANISOU 3328  CB  HIS A 462    22416  12811   8025   -559  -2747  -3160  A    C  
ATOM   3329  CG  HIS A 462      19.302  19.018   6.854  1.00117.45      A    C  
ANISOU 3329  CG  HIS A 462    23177  13403   8046   -345  -2433  -3281  A    C  
ATOM   3330  CD2 HIS A 462      18.717  18.252   7.804  1.00119.80      A    C  
ANISOU 3330  CD2 HIS A 462    23788  13861   7871   -246  -2137  -3198  A    C  
ATOM   3331  ND1 HIS A 462      18.618  20.214   6.854  1.00122.76      A    N  
ANISOU 3331  ND1 HIS A 462    23864  14059   8720   -193  -2374  -3514  A    N  
ATOM   3332  CE1 HIS A 462      17.670  20.179   7.772  1.00121.37      A    C  
ANISOU 3332  CE1 HIS A 462    23950  14072   8094     11  -2062  -3593  A    C  
ATOM   3333  NE2 HIS A 462      17.706  18.997   8.361  1.00125.01      A    N  
ANISOU 3333  NE2 HIS A 462    24591  14648   8259    -46  -1897  -3397  A    N  
ATOM   3334  N   GLN A 463      23.285  17.190   4.967  1.00131.88      A    N  
ANISOU 3334  N   GLN A 463    24300  14991  10818   -823  -3449  -2863  A    N  
ATOM   3335  CA  GLN A 463      23.946  16.729   3.743  1.00125.27      A    C  
ANISOU 3335  CA  GLN A 463    23023  14154  10421  -1013  -3509  -2719  A    C  
ATOM   3336  C   GLN A 463      24.350  15.256   3.774  1.00132.33      A    C  
ANISOU 3336  C   GLN A 463    23977  15094  11207   -948  -3466  -2488  A    C  
ATOM   3337  O   GLN A 463      24.913  14.765   4.757  1.00134.21      A    O  
ANISOU 3337  O   GLN A 463    24544  15342  11106   -739  -3688  -2480  A    O  
ATOM   3338  CB  GLN A 463      25.174  17.585   3.440  1.00122.09      A    C  
ANISOU 3338  CB  GLN A 463    22382  13693  10312  -1124  -3980  -2889  A    C  
ATOM   3339  CG  GLN A 463      25.360  17.868   1.959  1.00111.32      A    C  
ANISOU 3339  CG  GLN A 463    20535  12305   9458  -1380  -3910  -2818  A    C  
ATOM   3340  CD  GLN A 463      26.679  18.543   1.661  1.00125.83      A    C  
ANISOU 3340  CD  GLN A 463    22116  14118  11577  -1553  -4339  -2960  A    C  
ATOM   3341  NE2 GLN A 463      26.860  18.964   0.416  1.00129.24      A    N  
ANISOU 3341  NE2 GLN A 463    22175  14511  12421  -1796  -4270  -2907  A    N  
ATOM   3342  OE1 GLN A 463      27.531  18.681   2.539  1.00135.83      A    O  
ANISOU 3342  OE1 GLN A 463    23508  15425  12676  -1482  -4724  -3122  A    O  
ATOM   3343  N   VAL A 464      24.064  14.572   2.669  1.00125.98      A    N  
ANISOU 3343  N   VAL A 464    22883  14305  10679  -1105  -3192  -2310  A    N  
ATOM   3344  CA  VAL A 464      24.401  13.166   2.486  1.00121.39      A    C  
ANISOU 3344  CA  VAL A 464    22362  13708  10051  -1059  -3115  -2092  A    C  
ATOM   3345  C   VAL A 464      25.508  13.051   1.445  1.00102.90      A    C  
ANISOU 3345  C   VAL A 464    19578  11398   8119  -1130  -3373  -2075  A    C  
ATOM   3346  O   VAL A 464      25.561  13.839   0.506  1.00128.56      A    O  
ANISOU 3346  O   VAL A 464    22432  14680  11736  -1322  -3387  -2150  A    O  
ATOM   3347  CB  VAL A 464      23.176  12.355   2.035  1.00103.10      A    C  
ANISOU 3347  CB  VAL A 464    20082  11386   7706  -1211  -2572  -1927  A    C  
ATOM   3348  CG1 VAL A 464      23.522  10.882   1.894  1.00103.64      A    C  
ANISOU 3348  CG1 VAL A 464    20321  11355   7702  -1170  -2486  -1710  A    C  
ATOM   3349  CG2 VAL A 464      22.035  12.530   3.019  1.00105.25      A    C  
ANISOU 3349  CG2 VAL A 464    20713  11697   7581  -1175  -2267  -1962  A    C  
ATOM   3350  N   ARG A 465      26.411  12.095   1.626  1.00111.23      A    N  
ANISOU 3350  N   ARG A 465    20720  12455   9088   -946  -3576  -1979  A    N  
ATOM   3351  CA  ARG A 465      27.550  11.964   0.729  1.00124.53      A    C  
ANISOU 3351  CA  ARG A 465    21961  14233  11123   -963  -3833  -1990  A    C  
ATOM   3352  C   ARG A 465      27.611  10.537   0.196  1.00133.21      A    C  
ANISOU 3352  C   ARG A 465    23117  15269  12229   -869  -3643  -1781  A    C  
ATOM   3353  O   ARG A 465      27.174   9.605   0.870  1.00141.66      A    O  
ANISOU 3353  O   ARG A 465    24672  16200  12953   -716  -3471  -1638  A    O  
ATOM   3354  CB  ARG A 465      28.842  12.299   1.461  1.00139.65      A    C  
ANISOU 3354  CB  ARG A 465    23843  16275  12941   -764  -4374  -2149  A    C  
ATOM   3355  CG  ARG A 465      28.834  13.652   2.137  1.00138.26      A    C  
ANISOU 3355  CG  ARG A 465    23710  16116  12705   -857  -4595  -2389  A    C  
ATOM   3356  CD  ARG A 465      30.234  14.091   2.499  1.00151.90      A    C  
ANISOU 3356  CD  ARG A 465    25211  18028  14477   -787  -5148  -2599  A    C  
ATOM   3357  NE  ARG A 465      30.216  15.324   3.281  1.00174.63      A    N  
ANISOU 3357  NE  ARG A 465    28228  20879  17244   -877  -5377  -2857  A    N  
ATOM   3358  CZ  ARG A 465      30.045  16.542   2.779  1.00179.85      A    C  
ANISOU 3358  CZ  ARG A 465    28686  21454  18197  -1201  -5350  -3003  A    C  
ATOM   3359  NH1 ARG A 465      29.870  16.714   1.475  1.00182.41      A    N1+
ANISOU 3359  NH1 ARG A 465    28638  21737  18932  -1460  -5103  -2899  A    N1+
ATOM   3360  NH2 ARG A 465      30.046  17.593   3.589  1.00176.90      A    N  
ANISOU 3360  NH2 ARG A 465    28528  21009  17675  -1247  -5574  -3257  A    N  
ATOM   3361  N   TYR A 466      28.141  10.353  -1.009  1.00129.51      A    N  
ANISOU 3361  N   TYR A 466    22198  14878  12131   -964  -3654  -1761  A    N  
ATOM   3362  CA  TYR A 466      28.221   9.011  -1.570  1.00121.21      A    C  
ANISOU 3362  CA  TYR A 466    21222  13740  11092   -858  -3481  -1594  A    C  
ATOM   3363  C   TYR A 466      29.582   8.738  -2.199  1.00119.68      A    C  
ANISOU 3363  C   TYR A 466    20636  13713  11123   -691  -3793  -1636  A    C  
ATOM   3364  O   TYR A 466      30.287   9.663  -2.604  1.00119.69      A    O  
ANISOU 3364  O   TYR A 466    20166  13922  11389   -810  -4028  -1782  A    O  
ATOM   3365  CB  TYR A 466      27.111   8.792  -2.601  1.00120.97      A    C  
ANISOU 3365  CB  TYR A 466    21071  13640  11254  -1160  -3015  -1517  A    C  
ATOM   3366  CG  TYR A 466      27.115   9.764  -3.759  1.00132.93      A    C  
ANISOU 3366  CG  TYR A 466    22028  15308  13170  -1417  -2996  -1609  A    C  
ATOM   3367  CD1 TYR A 466      27.885   9.520  -4.890  1.00144.39      A    C  
ANISOU 3367  CD1 TYR A 466    23071  16870  14921  -1434  -3062  -1603  A    C  
ATOM   3368  CD2 TYR A 466      26.357  10.925  -3.722  1.00131.89      A    C  
ANISOU 3368  CD2 TYR A 466    21815  15208  13090  -1610  -2904  -1698  A    C  
ATOM   3369  CE1 TYR A 466      27.895  10.398  -5.952  1.00141.27      A    C  
ANISOU 3369  CE1 TYR A 466    22221  16603  14851  -1670  -3021  -1658  A    C  
ATOM   3370  CE2 TYR A 466      26.363  11.813  -4.780  1.00138.42      A    C  
ANISOU 3370  CE2 TYR A 466    22215  16131  14246  -1812  -2885  -1753  A    C  
ATOM   3371  CZ  TYR A 466      27.133  11.544  -5.894  1.00142.48      A    C  
ANISOU 3371  CZ  TYR A 466    22351  16746  15041  -1859  -2936  -1721  A    C  
ATOM   3372  OH  TYR A 466      27.143  12.424  -6.954  1.00147.17      A    O  
ANISOU 3372  OH  TYR A 466    22571  17424  15925  -2064  -2894  -1747  A    O  
ATOM   3373  N   THR A 467      29.951   7.462  -2.254  1.00123.53      A    N  
ANISOU 3373  N   THR A 467    21342  14106  11488   -412  -3782  -1514  A    N  
ATOM   3374  CA  THR A 467      31.116   7.029  -3.016  1.00136.14      A    C  
ANISOU 3374  CA  THR A 467    22548  15879  13299   -216  -3995  -1550  A    C  
ATOM   3375  C   THR A 467      30.744   5.827  -3.884  1.00143.80      A    C  
ANISOU 3375  C   THR A 467    23656  16654  14326   -190  -3664  -1408  A    C  
ATOM   3376  O   THR A 467      29.991   4.954  -3.454  1.00155.97      A    O  
ANISOU 3376  O   THR A 467    25767  17889  15605   -144  -3413  -1263  A    O  
ATOM   3377  CB  THR A 467      32.300   6.661  -2.101  1.00142.72      A    C  
ANISOU 3377  CB  THR A 467    23498  16846  13882    266  -4461  -1602  A    C  
ATOM   3378  CG2 THR A 467      33.543   6.336  -2.923  1.00138.59      A    C  
ANISOU 3378  CG2 THR A 467    22452  16604  13601    480  -4689  -1684  A    C  
ATOM   3379  OG1 THR A 467      32.587   7.758  -1.230  1.00156.25      A    O  
ANISOU 3379  OG1 THR A 467    25126  18731  15511    212  -4778  -1767  A    O  
ATOM   3380  N   PHE A 468      31.271   5.791  -5.103  1.00138.60      A    N  
ANISOU 3380  N   PHE A 468    22496  16168  13997   -245  -3648  -1460  A    N  
ATOM   3381  CA  PHE A 468      30.943   4.747  -6.060  1.00128.97      A    C  
ANISOU 3381  CA  PHE A 468    21360  14784  12860   -247  -3346  -1373  A    C  
ATOM   3382  C   PHE A 468      32.222   4.085  -6.562  1.00147.16      A    C  
ANISOU 3382  C   PHE A 468    23417  17254  15245    147  -3577  -1420  A    C  
ATOM   3383  O   PHE A 468      33.066   4.749  -7.160  1.00154.96      A    O  
ANISOU 3383  O   PHE A 468    23788  18599  16489    113  -3760  -1545  A    O  
ATOM   3384  CB  PHE A 468      30.173   5.341  -7.233  1.00120.82      A    C  
ANISOU 3384  CB  PHE A 468    19951  13825  12132   -697  -3038  -1403  A    C  
ATOM   3385  CG  PHE A 468      28.683   5.320  -7.066  1.00113.45      A    C  
ANISOU 3385  CG  PHE A 468    19345  12671  11089  -1009  -2668  -1335  A    C  
ATOM   3386  CD1 PHE A 468      27.972   4.143  -7.190  1.00117.86      A    C  
ANISOU 3386  CD1 PHE A 468    20325  12947  11510  -1041  -2362  -1244  A    C  
ATOM   3387  CD2 PHE A 468      27.991   6.485  -6.789  1.00105.62      A    C  
ANISOU 3387  CD2 PHE A 468    18235  11766  10130  -1276  -2619  -1384  A    C  
ATOM   3388  CE1 PHE A 468      26.597   4.134  -7.042  1.00110.72      A    C  
ANISOU 3388  CE1 PHE A 468    19644  11913  10512  -1375  -2008  -1212  A    C  
ATOM   3389  CE2 PHE A 468      26.619   6.479  -6.638  1.00 92.83      A    C  
ANISOU 3389  CE2 PHE A 468    16844  10024   8402  -1530  -2277  -1349  A    C  
ATOM   3390  CZ  PHE A 468      25.923   5.306  -6.768  1.00 92.16      A    C  
ANISOU 3390  CZ  PHE A 468    17103   9723   8191  -1600  -1967  -1269  A    C  
ATOM   3391  N   VAL A 469      32.377   2.788  -6.322  1.00155.02      A    N  
ANISOU 3391  N   VAL A 469    24899  17991  16010    527  -3558  -1326  A    N  
ATOM   3392  CA  VAL A 469      33.508   2.052  -6.888  1.00160.24      A    C  
ANISOU 3392  CA  VAL A 469    25353  18798  16733    967  -3740  -1382  A    C  
ATOM   3393  C   VAL A 469      33.083   0.692  -7.435  1.00172.12      A    C  
ANISOU 3393  C   VAL A 469    27336  19908  18155   1097  -3443  -1284  A    C  
ATOM   3394  O   VAL A 469      32.718  -0.197  -6.670  1.00169.98      A    O  
ANISOU 3394  O   VAL A 469    27798  19224  17561   1301  -3376  -1146  A    O  
ATOM   3395  CB  VAL A 469      34.628   1.854  -5.847  1.00151.33      A    C  
ANISOU 3395  CB  VAL A 469    24321  17828  15351   1539  -4212  -1419  A    C  
ATOM   3396  CG1 VAL A 469      35.531   3.076  -5.792  1.00144.85      A    C  
ANISOU 3396  CG1 VAL A 469    22764  17542  14731   1452  -4563  -1611  A    C  
ATOM   3397  CG2 VAL A 469      34.034   1.569  -4.481  1.00142.48      A    C  
ANISOU 3397  CG2 VAL A 469    23960  16362  13814   1653  -4231  -1274  A    C  
ATOM   3398  N   LYS A 470      33.111   0.561  -8.764  1.00193.10      A    N  
ANISOU 3398  N   LYS A 470    29609  22673  21088    952  -3253  -1359  A    N  
ATOM   3399  CA  LYS A 470      32.952  -0.710  -9.486  1.00192.52      A    C  
ANISOU 3399  CA  LYS A 470    29885  22286  20979   1113  -3022  -1336  A    C  
ATOM   3400  C   LYS A 470      31.803  -1.541  -8.916  1.00184.25      A    C  
ANISOU 3400  C   LYS A 470    29674  20660  19673    946  -2723  -1184  A    C  
ATOM   3401  O   LYS A 470      31.818  -2.771  -8.943  1.00198.27      A    O  
ANISOU 3401  O   LYS A 470    32026  22033  21274   1216  -2624  -1126  A    O  
ATOM   3402  CB  LYS A 470      34.274  -1.494  -9.450  1.00192.13      A    C  
ANISOU 3402  CB  LYS A 470    29844  22332  20825   1822  -3325  -1388  A    C  
ATOM   3403  CG  LYS A 470      34.374  -2.732 -10.367  1.00192.24      A    C  
ANISOU 3403  CG  LYS A 470    30121  22084  20837   2081  -3137  -1420  A    C  
ATOM   3404  CD  LYS A 470      33.977  -2.463 -11.813  1.00180.30      A    C  
ANISOU 3404  CD  LYS A 470    28130  20740  19637   1657  -2844  -1531  A    C  
ATOM   3405  CE  LYS A 470      34.053  -3.748 -12.632  1.00175.36      A    C  
ANISOU 3405  CE  LYS A 470    27854  19810  18964   1934  -2670  -1589  A    C  
ATOM   3406  NZ  LYS A 470      33.537  -3.573 -14.014  1.00171.77      A    N1+
ANISOU 3406  NZ  LYS A 470    27027  19483  18754   1512  -2372  -1702  A    N1+
ATOM   3407  N   GLY A 471      30.807  -0.840  -8.387  1.00164.66      A    N  
ANISOU 3407  N   GLY A 471    27263  18142  17160    490  -2567  -1127  A    N  
ATOM   3408  CA  GLY A 471      29.651  -1.468  -7.783  1.00162.89      A    C  
ANISOU 3408  CA  GLY A 471    27745  17455  16691    234  -2246   -993  A    C  
ATOM   3409  C   GLY A 471      28.531  -0.480  -7.539  1.00162.13      A    C  
ANISOU 3409  C   GLY A 471    27466  17486  16650   -312  -2042   -997  A    C  
ATOM   3410  O   GLY A 471      28.145   0.289  -8.421  1.00100.55      A    O  
ANISOU 3410  O   GLY A 471    19102   9967   9135   -655  -1936  -1106  A    O  
ATOM   3411  N   ASN A 472      28.028  -0.506  -6.310  1.00154.99      A    N  
ANISOU 3411  N   ASN A 472    27069  16381  15437   -342  -1993   -875  A    N  
ATOM   3412  CA  ASN A 472      26.959   0.374  -5.870  1.00151.69      A    C  
ANISOU 3412  CA  ASN A 472    26558  16079  14999   -777  -1799   -881  A    C  
ATOM   3413  C   ASN A 472      27.347   1.181  -4.641  1.00131.99      A    C  
ANISOU 3413  C   ASN A 472    24117  13733  12301   -564  -2096   -856  A    C  
ATOM   3414  O   ASN A 472      28.374   0.931  -4.024  1.00136.92      A    O  
ANISOU 3414  O   ASN A 472    24927  14343  12752    -89  -2443   -818  A    O  
ATOM   3415  CB  ASN A 472      25.671  -0.413  -5.630  1.00180.02      A    C  
ANISOU 3415  CB  ASN A 472    30692  19314  18395  -1158  -1331   -790  A    C  
ATOM   3416  CG  ASN A 472      24.951  -0.755  -6.929  1.00199.05      A    C  
ANISOU 3416  CG  ASN A 472    32839  21724  21066  -1562  -1013   -899  A    C  
ATOM   3417  ND2 ASN A 472      25.319  -1.878  -7.538  1.00206.31      A    N  
ANISOU 3417  ND2 ASN A 472    34031  22354  22002  -1427   -962   -894  A    N  
ATOM   3418  OD1 ASN A 472      24.074  -0.011  -7.379  1.00204.63      A    O  
ANISOU 3418  OD1 ASN A 472    33115  22697  21938  -1960   -833  -1002  A    O  
ATOM   3419  N   LEU A 473      26.508   2.153  -4.310  1.00119.09      A    N  
ANISOU 3419  N   LEU A 473    22313  12262  10675   -895  -1970   -902  A    N  
ATOM   3420  CA  LEU A 473      26.802   3.174  -3.316  1.00113.55      A    C  
ANISOU 3420  CA  LEU A 473    21550  11754   9840   -763  -2251   -943  A    C  
ATOM   3421  C   LEU A 473      26.819   2.742  -1.856  1.00117.15      A    C  
ANISOU 3421  C   LEU A 473    22695  11997   9819   -506  -2316   -811  A    C  
ATOM   3422  O   LEU A 473      25.973   1.979  -1.397  1.00109.35      A    O  
ANISOU 3422  O   LEU A 473    22270  10714   8563   -649  -1965   -671  A    O  
ATOM   3423  CB  LEU A 473      25.794   4.316  -3.456  1.00102.11      A    C  
ANISOU 3423  CB  LEU A 473    19763  10509   8526  -1165  -2057  -1043  A    C  
ATOM   3424  CG  LEU A 473      24.320   3.901  -3.417  1.00 99.94      A    C  
ANISOU 3424  CG  LEU A 473    19749  10096   8129  -1545  -1552   -990  A    C  
ATOM   3425  CD1 LEU A 473      23.730   3.966  -2.022  1.00102.70      A    C  
ANISOU 3425  CD1 LEU A 473    20604  10351   8067  -1536  -1436   -916  A    C  
ATOM   3426  CD2 LEU A 473      23.538   4.779  -4.340  1.00 96.25      A    C  
ANISOU 3426  CD2 LEU A 473    18718   9891   7961  -1884  -1381  -1125  A    C  
ATOM   3427  N   LYS A 474      27.833   3.236  -1.154  1.00131.57      A    N  
ANISOU 3427  N   LYS A 474    24464  13994  11532   -134  -2776   -867  A    N  
ATOM   3428  CA  LYS A 474      27.896   3.218   0.301  1.00143.82      A    C  
ANISOU 3428  CA  LYS A 474    26567  15461  12617    126  -2925   -791  A    C  
ATOM   3429  C   LYS A 474      27.544   4.649   0.713  1.00127.17      A    C  
ANISOU 3429  C   LYS A 474    24137  13624  10558    -88  -3009   -955  A    C  
ATOM   3430  O   LYS A 474      28.159   5.601   0.228  1.00108.92      A    O  
ANISOU 3430  O   LYS A 474    21231  11595   8560   -125  -3290  -1135  A    O  
ATOM   3431  CB  LYS A 474      29.286   2.808   0.811  1.00154.62      A    C  
ANISOU 3431  CB  LYS A 474    28071  16881  13798    725  -3431   -785  A    C  
ATOM   3432  CG  LYS A 474      29.349   2.338   2.276  1.00155.42      A    C  
ANISOU 3432  CG  LYS A 474    28945  16795  13312   1096  -3551   -638  A    C  
ATOM   3433  CD  LYS A 474      29.231   0.819   2.426  1.00160.81      A    C  
ANISOU 3433  CD  LYS A 474    30395  17013  13692   1334  -3332   -378  A    C  
ATOM   3434  CE  LYS A 474      29.219   0.390   3.896  1.00175.75      A    C  
ANISOU 3434  CE  LYS A 474    33128  18699  14950   1691  -3413   -196  A    C  
ATOM   3435  NZ  LYS A 474      28.047   0.887   4.665  1.00177.75      A    N1+
ANISOU 3435  NZ  LYS A 474    33666  18912  14959   1298  -3058   -149  A    N1+
ATOM   3436  N   LEU A 475      26.520   4.805   1.548  1.00143.25      A    N  
ANISOU 3436  N   LEU A 475    26570  15565  12292   -255  -2729   -899  A    N  
ATOM   3437  CA  LEU A 475      26.014   6.131   1.912  1.00143.86      A    C  
ANISOU 3437  CA  LEU A 475    26402  15861  12396   -447  -2743  -1065  A    C  
ATOM   3438  C   LEU A 475      26.566   6.683   3.228  1.00149.79      A    C  
ANISOU 3438  C   LEU A 475    27425  16704  12782   -133  -3125  -1142  A    C  
ATOM   3439  O   LEU A 475      26.417   6.070   4.287  1.00151.62      A    O  
ANISOU 3439  O   LEU A 475    28295  16780  12533     80  -3076  -1003  A    O  
ATOM   3440  CB  LEU A 475      24.484   6.120   1.994  1.00127.98      A    C  
ANISOU 3440  CB  LEU A 475    24560  13786  10282   -819  -2191  -1015  A    C  
ATOM   3441  CG  LEU A 475      23.720   6.408   0.706  1.00105.34      A    C  
ANISOU 3441  CG  LEU A 475    21162  11024   7838  -1214  -1888  -1089  A    C  
ATOM   3442  CD1 LEU A 475      22.260   6.691   1.004  1.00105.33      A    C  
ANISOU 3442  CD1 LEU A 475    21236  11092   7693  -1517  -1432  -1113  A    C  
ATOM   3443  CD2 LEU A 475      24.360   7.582  -0.005  1.00102.32      A    C  
ANISOU 3443  CD2 LEU A 475    20157  10873   7845  -1211  -2220  -1274  A    C  
ATOM   3444  N   GLU A 476      27.220   7.839   3.146  1.00138.39      A    N  
ANISOU 3444  N   GLU A 476    25522  15505  11556   -121  -3507  -1369  A    N  
ATOM   3445  CA  GLU A 476      27.627   8.564   4.341  1.00123.80      A    C  
ANISOU 3445  CA  GLU A 476    23873  13773   9392     97  -3869  -1513  A    C  
ATOM   3446  C   GLU A 476      26.447   9.428   4.773  1.00120.70      A    C  
ANISOU 3446  C   GLU A 476    23590  13387   8885   -146  -3573  -1598  A    C  
ATOM   3447  O   GLU A 476      25.709   9.945   3.941  1.00116.85      A    O  
ANISOU 3447  O   GLU A 476    22750  12928   8721   -469  -3290  -1647  A    O  
ATOM   3448  CB  GLU A 476      28.869   9.417   4.069  1.00122.39      A    C  
ANISOU 3448  CB  GLU A 476    23158  13844   9499    162  -4406  -1752  A    C  
ATOM   3449  CG  GLU A 476      29.335  10.275   5.246  1.00143.84      A    C  
ANISOU 3449  CG  GLU A 476    26025  16703  11923    333  -4828  -1968  A    C  
ATOM   3450  CD  GLU A 476      30.040   9.472   6.331  1.00160.38      A    C  
ANISOU 3450  CD  GLU A 476    28596  18820  13520    828  -5155  -1899  A    C  
ATOM   3451  OE1 GLU A 476      30.922   8.658   5.990  1.00172.49      A    O  
ANISOU 3451  OE1 GLU A 476    30018  20408  15112   1094  -5365  -1821  A    O  
ATOM   3452  OE2 GLU A 476      29.715   9.655   7.525  1.00152.79      A    O1-
ANISOU 3452  OE2 GLU A 476    28136  17836  12083    991  -5205  -1926  A    O1-
ATOM   3453  N   MET A 477      26.281   9.593   6.078  1.00127.46      A    N  
ANISOU 3453  N   MET A 477    24935  14240   9252     53  -3652  -1626  A    N  
ATOM   3454  CA  MET A 477      25.095  10.238   6.628  1.00124.84      A    C  
ANISOU 3454  CA  MET A 477    24797  13924   8714   -105  -3318  -1693  A    C  
ATOM   3455  C   MET A 477      25.459  11.425   7.504  1.00127.52      A    C  
ANISOU 3455  C   MET A 477    25183  14394   8875     39  -3703  -1965  A    C  
ATOM   3456  O   MET A 477      26.583  11.513   7.996  1.00134.74      A    O  
ANISOU 3456  O   MET A 477    26137  15383   9675    295  -4216  -2067  A    O  
ATOM   3457  CB  MET A 477      24.279   9.227   7.437  1.00128.85      A    C  
ANISOU 3457  CB  MET A 477    25956  14286   8715    -48  -2900  -1454  A    C  
ATOM   3458  CG  MET A 477      23.615   8.151   6.604  1.00119.82      A    C  
ANISOU 3458  CG  MET A 477    24809  12982   7735   -308  -2414  -1223  A    C  
ATOM   3459  SD  MET A 477      22.529   8.863   5.356  1.00146.01      A    S  
ANISOU 3459  SD  MET A 477    27471  16443  11563   -768  -2027  -1352  A    S  
ATOM   3460  CE  MET A 477      21.027   9.111   6.298  1.00117.21      A    C  
ANISOU 3460  CE  MET A 477    24155  12895   7486   -904  -1508  -1368  A    C  
ATOM   3461  N   PRO A 478      24.512  12.356   7.688  1.00128.97      A    N  
ANISOU 3461  N   PRO A 478    25350  14622   9032   -112  -3470  -2113  A    N  
ATOM   3462  CA  PRO A 478      24.715  13.402   8.689  1.00140.83      A    C  
ANISOU 3462  CA  PRO A 478    27047  16199  10264     49  -3784  -2380  A    C  
ATOM   3463  C   PRO A 478      24.930  12.789  10.067  1.00160.04      A    C  
ANISOU 3463  C   PRO A 478    30019  18645  12145    388  -3861  -2274  A    C  
ATOM   3464  O   PRO A 478      24.281  11.795  10.394  1.00173.94      A    O  
ANISOU 3464  O   PRO A 478    32210  20323  13558    423  -3476  -2025  A    O  
ATOM   3465  CB  PRO A 478      23.407  14.199   8.622  1.00136.05      A    C  
ANISOU 3465  CB  PRO A 478    26401  15618   9674   -117  -3367  -2486  A    C  
ATOM   3466  CG  PRO A 478      22.406  13.233   8.061  1.00131.75      A    C  
ANISOU 3466  CG  PRO A 478    25831  15057   9172   -304  -2785  -2224  A    C  
ATOM   3467  CD  PRO A 478      23.194  12.473   7.044  1.00122.04      A    C  
ANISOU 3467  CD  PRO A 478    24292  13750   8326   -395  -2919  -2066  A    C  
ATOM   3468  N   SER A 479      25.837  13.364  10.851  1.00124.15      A    N  
ANISOU 3468  N   SER A 479    19667  15174  12330  -1899   -610  -4390  A    N  
ATOM   3469  CA  SER A 479      26.184  12.803  12.153  1.00129.57      A    C  
ANISOU 3469  CA  SER A 479    20271  15495  13466  -1735   -627  -4211  A    C  
ATOM   3470  C   SER A 479      24.956  12.735  13.058  1.00134.74      A    C  
ANISOU 3470  C   SER A 479    20810  16268  14119  -1878   -868  -3909  A    C  
ATOM   3471  O   SER A 479      24.182  13.690  13.132  1.00146.27      A    O  
ANISOU 3471  O   SER A 479    22135  18122  15318  -1899   -997  -3697  A    O  
ATOM   3472  CB  SER A 479      27.290  13.632  12.815  1.00120.60      A    C  
ANISOU 3472  CB  SER A 479    19013  14322  12489  -1386   -532  -4016  A    C  
ATOM   3473  OG  SER A 479      27.752  13.028  14.010  1.00110.28      A    O  
ANISOU 3473  OG  SER A 479    17649  12642  11610  -1250   -565  -3847  A    O  
ATOM   3474  N   PRO A 480      24.768  11.596  13.743  1.00117.62      A    N  
ANISOU 3474  N   PRO A 480    18683  13747  12261  -1985   -923  -3889  A    N  
ATOM   3475  CA  PRO A 480      23.610  11.439  14.628  1.00115.81      A    C  
ANISOU 3475  CA  PRO A 480    18343  13632  12028  -2167  -1119  -3612  A    C  
ATOM   3476  C   PRO A 480      23.639  12.410  15.809  1.00115.63      A    C  
ANISOU 3476  C   PRO A 480    18131  13791  12011  -1965  -1164  -3235  A    C  
ATOM   3477  O   PRO A 480      22.585  12.687  16.385  1.00 92.45      A    O  
ANISOU 3477  O   PRO A 480    15054  11110   8962  -2097  -1284  -3024  A    O  
ATOM   3478  CB  PRO A 480      23.729   9.986  15.100  1.00113.19      A    C  
ANISOU 3478  CB  PRO A 480    18136  12801  12068  -2302  -1143  -3671  A    C  
ATOM   3479  CG  PRO A 480      25.186   9.671  14.975  1.00103.22      A    C  
ANISOU 3479  CG  PRO A 480    16965  11138  11116  -2037   -970  -3842  A    C  
ATOM   3480  CD  PRO A 480      25.615  10.391  13.729  1.00 98.26      A    C  
ANISOU 3480  CD  PRO A 480    16373  10759  10202  -1950   -805  -4120  A    C  
ATOM   3481  N   PHE A 481      24.823  12.924  16.146  1.00128.73      A    N  
ANISOU 3481  N   PHE A 481    19781  15331  13801  -1664  -1056  -3174  A    N  
ATOM   3482  CA  PHE A 481      24.990  13.816  17.293  1.00115.04      A    C  
ANISOU 3482  CA  PHE A 481    17906  13729  12075  -1483  -1090  -2847  A    C  
ATOM   3483  C   PHE A 481      25.584  15.168  16.905  1.00114.23      A    C  
ANISOU 3483  C   PHE A 481    17737  13875  11789  -1236  -1009  -2834  A    C  
ATOM   3484  O   PHE A 481      26.389  15.271  15.980  1.00121.97      A    O  
ANISOU 3484  O   PHE A 481    18795  14798  12749  -1136   -886  -3049  A    O  
ATOM   3485  CB  PHE A 481      25.879  13.158  18.353  1.00 99.64      A    C  
ANISOU 3485  CB  PHE A 481    15999  11369  10489  -1384  -1099  -2696  A    C  
ATOM   3486  CG  PHE A 481      27.338  13.076  17.967  1.00 92.14      A    C  
ANISOU 3486  CG  PHE A 481    15103  10132   9776  -1134   -969  -2846  A    C  
ATOM   3487  CD1 PHE A 481      27.789  12.092  17.102  1.00105.27      A    C  
ANISOU 3487  CD1 PHE A 481    16884  11473  11639  -1165   -871  -3168  A    C  
ATOM   3488  CD2 PHE A 481      28.261  13.971  18.484  1.00 80.07      A    C  
ANISOU 3488  CD2 PHE A 481    13490   8647   8286   -878   -934  -2682  A    C  
ATOM   3489  CE1 PHE A 481      29.133  12.008  16.756  1.00103.17      A    C  
ANISOU 3489  CE1 PHE A 481    16620  10947  11631   -926   -716  -3331  A    C  
ATOM   3490  CE2 PHE A 481      29.604  13.891  18.139  1.00 83.01      A    C  
ANISOU 3490  CE2 PHE A 481    13864   8770   8905   -657   -810  -2815  A    C  
ATOM   3491  CZ  PHE A 481      30.039  12.910  17.276  1.00 88.29      A    C  
ANISOU 3491  CZ  PHE A 481    14619   9131   9796   -671   -689  -3142  A    C  
ATOM   3492  N   SER A 482      25.176  16.200  17.631  1.00119.34      A    N  
ANISOU 3492  N   SER A 482    18243  14793  12306  -1154  -1065  -2590  A    N  
ATOM   3493  CA  SER A 482      25.705  17.547  17.457  1.00143.25      A    C  
ANISOU 3493  CA  SER A 482    21209  18026  15193   -923  -1014  -2528  A    C  
ATOM   3494  C   SER A 482      27.132  17.706  17.970  1.00145.50      A    C  
ANISOU 3494  C   SER A 482    21528  18068  15686   -695   -928  -2469  A    C  
ATOM   3495  O   SER A 482      27.530  17.059  18.937  1.00156.86      A    O  
ANISOU 3495  O   SER A 482    22986  19246  17368   -690   -960  -2348  A    O  
ATOM   3496  CB  SER A 482      24.813  18.553  18.179  1.00174.90      A    C  
ANISOU 3496  CB  SER A 482    25052  22344  19057   -900  -1092  -2310  A    C  
ATOM   3497  OG  SER A 482      24.856  18.353  19.581  1.00193.94      A    O  
ANISOU 3497  OG  SER A 482    27433  24649  21607   -902  -1104  -2114  A    O  
ATOM   3498  N   VAL A 483      27.896  18.579  17.326  1.00142.51      A    N  
ANISOU 3498  N   VAL A 483    21150  17784  15213   -528   -841  -2530  A    N  
ATOM   3499  CA  VAL A 483      29.141  19.049  17.913  1.00128.29      A    C  
ANISOU 3499  CA  VAL A 483    19326  15842  13578   -310   -784  -2420  A    C  
ATOM   3500  C   VAL A 483      28.896  20.466  18.410  1.00119.27      A    C  
ANISOU 3500  C   VAL A 483    18097  14972  12250   -206   -837  -2219  A    C  
ATOM   3501  O   VAL A 483      29.182  21.444  17.720  1.00117.84      A    O  
ANISOU 3501  O   VAL A 483    17907  14958  11908   -113   -795  -2246  A    O  
ATOM   3502  CB  VAL A 483      30.313  19.021  16.921  1.00116.80      A    C  
ANISOU 3502  CB  VAL A 483    17915  14274  12190   -203   -619  -2634  A    C  
ATOM   3503  CG1 VAL A 483      31.583  19.515  17.591  1.00108.50      A    C  
ANISOU 3503  CG1 VAL A 483    16797  13088  11341      9   -583  -2494  A    C  
ATOM   3504  CG2 VAL A 483      30.513  17.617  16.378  1.00123.14      A    C  
ANISOU 3504  CG2 VAL A 483    18803  14784  13201   -298   -536  -2895  A    C  
ATOM   3505  N   VAL A 484      28.328  20.561  19.605  1.00119.24      A    N  
ANISOU 3505  N   VAL A 484    18039  15005  12261   -243   -924  -2024  A    N  
ATOM   3506  CA  VAL A 484      27.946  21.841  20.185  1.00125.59      A    C  
ANISOU 3506  CA  VAL A 484    18760  16046  12912   -157   -955  -1873  A    C  
ATOM   3507  C   VAL A 484      27.716  21.636  21.687  1.00127.41      A    C  
ANISOU 3507  C   VAL A 484    18974  16228  13207   -223  -1001  -1690  A    C  
ATOM   3508  O   VAL A 484      27.609  20.496  22.145  1.00129.37      A    O  
ANISOU 3508  O   VAL A 484    19269  16300  13585   -370  -1039  -1658  A    O  
ATOM   3509  CB  VAL A 484      26.673  22.407  19.498  1.00115.36      A    C  
ANISOU 3509  CB  VAL A 484    17376  15052  11405   -219   -999  -1920  A    C  
ATOM   3510  CG1 VAL A 484      25.455  21.591  19.876  1.00113.92      A    C  
ANISOU 3510  CG1 VAL A 484    17131  14930  11223   -427  -1051  -1916  A    C  
ATOM   3511  CG2 VAL A 484      26.460  23.876  19.836  1.00122.12      A    C  
ANISOU 3511  CG2 VAL A 484    18141  16102  12157    -69  -1016  -1806  A    C  
ATOM   3512  N   ILE A 485      27.663  22.723  22.454  1.00116.66      A    N  
ANISOU 3512  N   ILE A 485    17565  15010  11750   -138   -998  -1572  A    N  
ATOM   3513  CA  ILE A 485      27.290  22.644  23.861  1.00107.40      A    C  
ANISOU 3513  CA  ILE A 485    16389  13863  10553   -248  -1016  -1425  A    C  
ATOM   3514  C   ILE A 485      25.885  22.051  23.988  1.00116.40      A    C  
ANISOU 3514  C   ILE A 485    17449  15153  11625   -453  -1012  -1451  A    C  
ATOM   3515  O   ILE A 485      24.936  22.534  23.368  1.00112.58      A    O  
ANISOU 3515  O   ILE A 485    16839  14891  11047   -440   -994  -1541  A    O  
ATOM   3516  CB  ILE A 485      27.335  24.029  24.543  1.00105.33      A    C  
ANISOU 3516  CB  ILE A 485    16092  13759  10169   -131   -979  -1363  A    C  
ATOM   3517  CG1 ILE A 485      28.769  24.565  24.579  1.00104.11      A    C  
ANISOU 3517  CG1 ILE A 485    16018  13450  10089     26  -1001  -1307  A    C  
ATOM   3518  CG2 ILE A 485      26.787  23.952  25.956  1.00109.40      A    C  
ANISOU 3518  CG2 ILE A 485    16613  14359  10596   -293   -957  -1258  A    C  
ATOM   3519  CD1 ILE A 485      28.882  26.003  25.064  1.00 93.59      A    C  
ANISOU 3519  CD1 ILE A 485    14675  12242   8644    143   -973  -1276  A    C  
ATOM   3520  N   GLN A 486      25.761  20.993  24.783  1.00130.58      A    N  
ANISOU 3520  N   GLN A 486    19308  16822  13486   -658  -1050  -1351  A    N  
ATOM   3521  CA  GLN A 486      24.484  20.313  24.952  1.00131.89      A    C  
ANISOU 3521  CA  GLN A 486    19399  17115  13600   -899  -1044  -1359  A    C  
ATOM   3522  C   GLN A 486      24.115  20.255  26.439  1.00116.36      A    C  
ANISOU 3522  C   GLN A 486    17442  15233  11534  -1088  -1013  -1193  A    C  
ATOM   3523  O   GLN A 486      24.994  20.127  27.293  1.00 91.31      A    O  
ANISOU 3523  O   GLN A 486    14406  11898   8388  -1107  -1064  -1040  A    O  
ATOM   3524  CB  GLN A 486      24.546  18.908  24.335  1.00147.72      A    C  
ANISOU 3524  CB  GLN A 486    21489  18872  15764  -1043  -1118  -1412  A    C  
ATOM   3525  CG  GLN A 486      23.197  18.220  24.180  1.00158.72      A    C  
ANISOU 3525  CG  GLN A 486    22795  20404  17109  -1302  -1128  -1454  A    C  
ATOM   3526  CD  GLN A 486      22.948  17.151  25.223  1.00162.30      A    C  
ANISOU 3526  CD  GLN A 486    23327  20720  17618  -1589  -1175  -1285  A    C  
ATOM   3527  NE2 GLN A 486      21.692  17.007  25.633  1.00158.83      A    N  
ANISOU 3527  NE2 GLN A 486    22760  20525  17063  -1827  -1133  -1255  A    N  
ATOM   3528  OE1 GLN A 486      23.871  16.460  25.655  1.00172.61      A    O  
ANISOU 3528  OE1 GLN A 486    24795  21704  19085  -1606  -1256  -1167  A    O  
ATOM   3529  N   GLU A 487      22.824  20.398  26.740  1.00129.33      A    N  
ANISOU 3529  N   GLU A 487    18932  17153  13056  -1237   -927  -1225  A    N  
ATOM   3530  CA  GLU A 487      22.309  20.303  28.110  1.00135.77      A    C  
ANISOU 3530  CA  GLU A 487    19746  18107  13731  -1475   -848  -1102  A    C  
ATOM   3531  C   GLU A 487      21.303  19.160  28.251  1.00133.69      A    C  
ANISOU 3531  C   GLU A 487    19435  17890  13473  -1808   -855  -1059  A    C  
ATOM   3532  O   GLU A 487      20.470  18.953  27.367  1.00158.29      A    O  
ANISOU 3532  O   GLU A 487    22396  21107  16640  -1831   -859  -1183  A    O  
ATOM   3533  CB  GLU A 487      21.651  21.621  28.534  1.00142.31      A    C  
ANISOU 3533  CB  GLU A 487    20401  19255  14413  -1369   -675  -1201  A    C  
ATOM   3534  CG  GLU A 487      21.500  21.801  30.047  1.00141.73      A    C  
ANISOU 3534  CG  GLU A 487    20387  19319  14145  -1575   -551  -1110  A    C  
ATOM   3535  CD  GLU A 487      20.144  22.372  30.443  1.00135.76      A    C  
ANISOU 3535  CD  GLU A 487    19375  18921  13285  -1653   -327  -1247  A    C  
ATOM   3536  OE1 GLU A 487      19.514  23.065  29.618  1.00130.12      A    O  
ANISOU 3536  OE1 GLU A 487    18426  18338  12675  -1438   -285  -1407  A    O  
ATOM   3537  OE2 GLU A 487      19.714  22.141  31.591  1.00133.20      A    O1-
ANISOU 3537  OE2 GLU A 487    19076  18751  12782  -1938   -193  -1190  A    O1-
ATOM   3538  N   SER A 488      21.372  18.428  29.360  1.00103.72      A    N  
ANISOU 3538  N   SER A 488    15774  14022   9611  -2095   -878   -866  A    N  
ATOM   3539  CA  SER A 488      20.545  17.238  29.540  1.00124.64      A    C  
ANISOU 3539  CA  SER A 488    18418  16662  12279  -2453   -909   -784  A    C  
ATOM   3540  C   SER A 488      19.603  17.405  30.730  1.00128.45      A    C  
ANISOU 3540  C   SER A 488    18810  17472  12522  -2751   -736   -712  A    C  
ATOM   3541  O   SER A 488      19.846  18.240  31.600  1.00114.95      A    O  
ANISOU 3541  O   SER A 488    17129  15913  10631  -2713   -620   -692  A    O  
ATOM   3542  CB  SER A 488      21.422  16.001  29.726  1.00 81.31      A    C  
ANISOU 3542  CB  SER A 488    13185  10750   6958  -2589  -1116   -587  A    C  
ATOM   3543  OG  SER A 488      20.657  14.811  29.637  1.00 99.07      A    O  
ANISOU 3543  OG  SER A 488    15441  12923   9278  -2913  -1175   -532  A    O  
ATOM   3544  N   GLU A 489      18.515  16.638  30.760  1.00140.85      A    N  
ANISOU 3544  N   GLU A 489    20267  19168  14081  -3066   -699   -696  A    N  
ATOM   3545  CA  GLU A 489      17.562  16.754  31.862  1.00144.40      A    C  
ANISOU 3545  CA  GLU A 489    20603  19964  14300  -3385   -491   -648  A    C  
ATOM   3546  C   GLU A 489      18.135  16.177  33.156  1.00137.29      A    C  
ANISOU 3546  C   GLU A 489    19992  18947  13226  -3703   -548   -365  A    C  
ATOM   3547  O   GLU A 489      17.812  16.640  34.246  1.00141.60      A    O  
ANISOU 3547  O   GLU A 489    20531  19773  13497  -3896   -355   -334  A    O  
ATOM   3548  CB  GLU A 489      16.240  16.055  31.511  1.00150.84      A    C  
ANISOU 3548  CB  GLU A 489    21193  20956  15165  -3667   -443   -693  A    C  
ATOM   3549  CG  GLU A 489      16.350  14.570  31.181  1.00157.70      A    C  
ANISOU 3549  CG  GLU A 489    22245  21491  16185  -3935   -671   -535  A    C  
ATOM   3550  CD  GLU A 489      16.748  14.306  29.740  1.00160.88      A    C  
ANISOU 3550  CD  GLU A 489    22669  21618  16841  -3670   -855   -680  A    C  
ATOM   3551  OE1 GLU A 489      17.006  15.279  29.002  1.00156.36      A    O  
ANISOU 3551  OE1 GLU A 489    21988  21119  16304  -3290   -825   -864  A    O  
ATOM   3552  OE2 GLU A 489      16.799  13.121  29.345  1.00172.92      A    O1-
ANISOU 3552  OE2 GLU A 489    24333  22847  18522  -3864  -1025   -615  A    O1-
ATOM   3553  N   LYS A 490      18.984  15.163  33.025  1.00127.06      A    N  
ANISOU 3553  N   LYS A 490    18950  17231  12096  -3767   -816   -161  A    N  
ATOM   3554  CA  LYS A 490      19.773  14.656  34.136  1.00127.36      A    C  
ANISOU 3554  CA  LYS A 490    19284  17079  12029  -4006   -964    158  A    C  
ATOM   3555  C   LYS A 490      21.107  15.372  34.030  1.00142.00      A    C  
ANISOU 3555  C   LYS A 490    21255  18738  13959  -3628  -1073    151  A    C  
ATOM   3556  O   LYS A 490      21.809  15.173  33.050  1.00149.51      A    O  
ANISOU 3556  O   LYS A 490    22221  19380  15205  -3332  -1219     81  A    O  
ATOM   3557  CB  LYS A 490      19.927  13.131  34.071  1.00136.48      A    C  
ANISOU 3557  CB  LYS A 490    20620  17842  13394  -4279  -1222    403  A    C  
ATOM   3558  CG  LYS A 490      20.223  12.578  32.679  1.00142.43      A    C  
ANISOU 3558  CG  LYS A 490    21342  18243  14530  -4015  -1367    248  A    C  
ATOM   3559  CD  LYS A 490      20.620  11.104  32.713  1.00149.29      A    C  
ANISOU 3559  CD  LYS A 490    22433  18624  15665  -4241  -1641    489  A    C  
ATOM   3560  CE  LYS A 490      19.433  10.193  33.011  1.00151.83      A    C  
ANISOU 3560  CE  LYS A 490    22734  19045  15909  -4729  -1619    596  A    C  
ATOM   3561  NZ  LYS A 490      19.800   8.749  32.914  1.00147.37      A    N1+
ANISOU 3561  NZ  LYS A 490    22390  17942  15660  -4927  -1902    808  A    N1+
ATOM   3562  N   GLY A 491      21.472  16.192  35.014  1.00150.28      A    N  
ANISOU 3562  N   GLY A 491    22390  19970  14740  -3657   -993    209  A    N  
ATOM   3563  CA  GLY A 491      22.648  17.038  34.865  1.00139.42      A    C  
ANISOU 3563  CA  GLY A 491    21083  18462  13428  -3296  -1072    168  A    C  
ATOM   3564  C   GLY A 491      22.294  17.944  33.702  1.00119.34      A    C  
ANISOU 3564  C   GLY A 491    18290  16050  11003  -2901   -909   -176  A    C  
ATOM   3565  O   GLY A 491      21.478  18.848  33.861  1.00104.54      A    O  
ANISOU 3565  O   GLY A 491    16241  14528   8953  -2870   -660   -372  A    O  
ATOM   3566  N   SER A 492      22.914  17.749  32.541  1.00117.80      A    N  
ANISOU 3566  N   SER A 492    18075  15577  11108  -2601  -1045   -253  A    N  
ATOM   3567  CA  SER A 492      24.302  17.331  32.375  1.00110.76      A    C  
ANISOU 3567  CA  SER A 492    17354  14284  10446  -2452  -1284   -104  A    C  
ATOM   3568  C   SER A 492      24.879  18.312  31.376  1.00 95.35      A    C  
ANISOU 3568  C   SER A 492    15298  12321   8607  -2024  -1234   -328  A    C  
ATOM   3569  O   SER A 492      24.162  18.759  30.480  1.00 99.70      A    O  
ANISOU 3569  O   SER A 492    15674  13045   9162  -1880  -1101   -561  A    O  
ATOM   3570  CB  SER A 492      24.448  15.897  31.858  1.00131.46      A    C  
ANISOU 3570  CB  SER A 492    20048  16534  13366  -2553  -1471     -5  A    C  
ATOM   3571  OG  SER A 492      24.089  14.944  32.839  1.00140.83      A    O  
ANISOU 3571  OG  SER A 492    21337  17717  14456  -2980  -1534    226  A    O  
ATOM   3572  N   TRP A 493      26.151  18.657  31.499  1.00 89.31      A    N  
ANISOU 3572  N   TRP A 493    14631  11364   7937  -1840  -1353   -242  A    N  
ATOM   3573  CA  TRP A 493      26.724  19.608  30.554  1.00 96.11      A    C  
ANISOU 3573  CA  TRP A 493    15401  12226   8890  -1469  -1297   -438  A    C  
ATOM   3574  C   TRP A 493      27.882  19.017  29.763  1.00 98.85      A    C  
ANISOU 3574  C   TRP A 493    15784  12201   9572  -1274  -1443   -423  A    C  
ATOM   3575  O   TRP A 493      28.832  18.471  30.329  1.00114.49      A    O  
ANISOU 3575  O   TRP A 493    17873  13917  11711  -1318  -1625   -208  A    O  
ATOM   3576  CB  TRP A 493      27.152  20.878  31.283  1.00 96.39      A    C  
ANISOU 3576  CB  TRP A 493    15468  12431   8723  -1387  -1241   -427  A    C  
ATOM   3577  CG  TRP A 493      25.975  21.717  31.645  1.00 99.61      A    C  
ANISOU 3577  CG  TRP A 493    15772  13208   8866  -1454  -1018   -578  A    C  
ATOM   3578  CD1 TRP A 493      25.065  21.484  32.639  1.00109.72      A    C  
ANISOU 3578  CD1 TRP A 493    17067  14704   9918  -1768   -914   -526  A    C  
ATOM   3579  CD2 TRP A 493      25.569  22.928  31.004  1.00 89.97      A    C  
ANISOU 3579  CD2 TRP A 493    14395  12175   7613  -1198   -863   -812  A    C  
ATOM   3580  CE2 TRP A 493      24.405  23.378  31.659  1.00 95.78      A    C  
ANISOU 3580  CE2 TRP A 493    15030  13218   8145  -1340   -663   -912  A    C  
ATOM   3581  CE3 TRP A 493      26.079  23.676  29.941  1.00 71.17      A    C  
ANISOU 3581  CE3 TRP A 493    11948   9729   5365   -876   -875   -937  A    C  
ATOM   3582  NE1 TRP A 493      24.116  22.480  32.652  1.00 99.23      A    N  
ANISOU 3582  NE1 TRP A 493    15572  13687   8445  -1699   -677   -747  A    N  
ATOM   3583  CZ2 TRP A 493      23.746  24.545  31.282  1.00 96.18      A    C  
ANISOU 3583  CZ2 TRP A 493    14896  13470   8176  -1132   -497  -1131  A    C  
ATOM   3584  CZ3 TRP A 493      25.425  24.829  29.571  1.00 76.20      A    C  
ANISOU 3584  CZ3 TRP A 493    12437  10570   5943   -703   -736  -1118  A    C  
ATOM   3585  CH2 TRP A 493      24.273  25.255  30.239  1.00 86.49      A    C  
ANISOU 3585  CH2 TRP A 493    13625  12140   7098   -812   -559  -1214  A    C  
ATOM   3586  N   HIS A 494      27.784  19.129  28.442  1.00 76.68      A    N  
ANISOU 3586  N   HIS A 494    12874   9382   6877  -1070  -1363   -656  A    N  
ATOM   3587  CA  HIS A 494      28.808  18.599  27.558  1.00 70.65      A    C  
ANISOU 3587  CA  HIS A 494    12124   8300   6422   -885  -1430   -719  A    C  
ATOM   3588  C   HIS A 494      29.394  19.696  26.678  1.00 82.58      A    C  
ANISOU 3588  C   HIS A 494    13558   9905   7916   -596  -1332   -889  A    C  
ATOM   3589  O   HIS A 494      28.658  20.455  26.050  1.00 92.84      A    O  
ANISOU 3589  O   HIS A 494    14775  11461   9038   -532  -1215  -1050  A    O  
ATOM   3590  CB  HIS A 494      28.229  17.476  26.709  1.00 72.18      A    C  
ANISOU 3590  CB  HIS A 494    12313   8350   6762   -977  -1424   -854  A    C  
ATOM   3591  CG  HIS A 494      27.919  16.231  27.485  1.00 82.48      A    C  
ANISOU 3591  CG  HIS A 494    13716   9450   8172  -1259  -1558   -658  A    C  
ATOM   3592  CD2 HIS A 494      28.683  15.153  27.780  1.00 91.44      A    C  
ANISOU 3592  CD2 HIS A 494    14946  10172   9624  -1303  -1729   -502  A    C  
ATOM   3593  ND1 HIS A 494      26.684  15.991  28.048  1.00 81.76      A    N  
ANISOU 3593  ND1 HIS A 494    13623   9572   7871  -1548  -1531   -592  A    N  
ATOM   3594  CE1 HIS A 494      26.701  14.820  28.660  1.00 93.62      A    C  
ANISOU 3594  CE1 HIS A 494    15242  10810   9519  -1787  -1682   -388  A    C  
ATOM   3595  NE2 HIS A 494      27.902  14.291  28.512  1.00 98.32      A    N  
ANISOU 3595  NE2 HIS A 494    15901  11005  10449  -1634  -1820   -322  A    N  
ATOM   3596  N   PHE A 495      30.720  19.801  26.667  1.00 74.28      A    N  
ANISOU 3596  N   PHE A 495    12519   8644   7061   -434  -1397   -829  A    N  
ATOM   3597  CA  PHE A 495      31.388  20.862  25.923  1.00 81.70      A    C  
ANISOU 3597  CA  PHE A 495    13393   9669   7979   -196  -1307   -955  A    C  
ATOM   3598  C   PHE A 495      32.421  20.295  24.964  1.00100.35      A    C  
ANISOU 3598  C   PHE A 495    15716  11766  10645    -39  -1284  -1073  A    C  
ATOM   3599  O   PHE A 495      33.368  19.649  25.395  1.00103.73      A    O  
ANISOU 3599  O   PHE A 495    16143  11909  11361    -12  -1396   -946  A    O  
ATOM   3600  CB  PHE A 495      32.061  21.855  26.880  1.00 87.84      A    C  
ANISOU 3600  CB  PHE A 495    14194  10518   8662   -155  -1368   -790  A    C  
ATOM   3601  CG  PHE A 495      31.147  22.382  27.946  1.00101.55      A    C  
ANISOU 3601  CG  PHE A 495    15982  12496  10105   -325  -1357   -705  A    C  
ATOM   3602  CD1 PHE A 495      31.007  21.710  29.155  1.00113.63      A    C  
ANISOU 3602  CD1 PHE A 495    17609  13970  11594   -565  -1476   -494  A    C  
ATOM   3603  CD2 PHE A 495      30.416  23.541  27.738  1.00 97.48      A    C  
ANISOU 3603  CD2 PHE A 495    15417  12260   9363   -257  -1224   -840  A    C  
ATOM   3604  CE1 PHE A 495      30.159  22.187  30.139  1.00114.85      A    C  
ANISOU 3604  CE1 PHE A 495    17814  14378  11447   -752  -1417   -452  A    C  
ATOM   3605  CE2 PHE A 495      29.564  24.022  28.715  1.00108.93      A    C  
ANISOU 3605  CE2 PHE A 495    16889  13926  10574   -400  -1168   -812  A    C  
ATOM   3606  CZ  PHE A 495      29.437  23.343  29.919  1.00119.57      A    C  
ANISOU 3606  CZ  PHE A 495    18338  15251  11844   -658  -1243   -635  A    C  
ATOM   3607  N   PRO A 496      32.242  20.535  23.658  1.00105.04      A    N  
ANISOU 3607  N   PRO A 496    16270  12457  11182     55  -1140  -1317  A    N  
ATOM   3608  CA  PRO A 496      33.266  20.174  22.673  1.00104.52      A    C  
ANISOU 3608  CA  PRO A 496    16162  12194  11358    200  -1051  -1483  A    C  
ATOM   3609  C   PRO A 496      34.408  21.187  22.690  1.00107.76      A    C  
ANISOU 3609  C   PRO A 496    16504  12640  11799    369  -1024  -1426  A    C  
ATOM   3610  O   PRO A 496      34.223  22.281  23.217  1.00109.13      A    O  
ANISOU 3610  O   PRO A 496    16690  13023  11753    373  -1060  -1308  A    O  
ATOM   3611  CB  PRO A 496      32.504  20.214  21.349  1.00 96.76      A    C  
ANISOU 3611  CB  PRO A 496    15195  11384  10185    168   -914  -1745  A    C  
ATOM   3612  CG  PRO A 496      31.429  21.223  21.578  1.00 91.98      A    C  
ANISOU 3612  CG  PRO A 496    14587  11116   9247    112   -939  -1675  A    C  
ATOM   3613  CD  PRO A 496      31.031  21.084  23.022  1.00 97.36      A    C  
ANISOU 3613  CD  PRO A 496    15286  11786   9922      4  -1059  -1450  A    C  
ATOM   3614  N   VAL A 497      35.563  20.839  22.135  1.00116.20      A    N  
ANISOU 3614  N   VAL A 497    17492  13504  13153    499   -951  -1522  A    N  
ATOM   3615  CA  VAL A 497      36.693  21.764  22.142  1.00129.56      A    C  
ANISOU 3615  CA  VAL A 497    19094  15234  14900    636   -925  -1460  A    C  
ATOM   3616  C   VAL A 497      37.207  22.038  20.723  1.00138.18      A    C  
ANISOU 3616  C   VAL A 497    20128  16396  15979    726   -694  -1721  A    C  
ATOM   3617  O   VAL A 497      37.166  21.169  19.851  1.00144.27      A    O  
ANISOU 3617  O   VAL A 497    20899  17054  16862    720   -557  -1960  A    O  
ATOM   3618  CB  VAL A 497      37.847  21.233  23.030  1.00133.23      A    C  
ANISOU 3618  CB  VAL A 497    19459  15401  15761    700  -1075  -1265  A    C  
ATOM   3619  CG1 VAL A 497      38.562  20.075  22.359  1.00140.49      A    C  
ANISOU 3619  CG1 VAL A 497    20268  16002  17108    802   -980  -1442  A    C  
ATOM   3620  CG2 VAL A 497      38.833  22.346  23.358  1.00130.60      A    C  
ANISOU 3620  CG2 VAL A 497    19041  15159  15422    782  -1112  -1130  A    C  
ATOM   3621  N   SER A 498      37.674  23.264  20.498  1.00138.54      A    N  
ANISOU 3621  N   SER A 498    20143  16632  15866    781   -645  -1679  A    N  
ATOM   3622  CA  SER A 498      38.220  23.663  19.205  1.00123.14      A    C  
ANISOU 3622  CA  SER A 498    18149  14789  13850    823   -425  -1886  A    C  
ATOM   3623  C   SER A 498      39.551  22.968  18.930  1.00109.90      A    C  
ANISOU 3623  C   SER A 498    16303  12869  12585    934   -297  -1998  A    C  
ATOM   3624  O   SER A 498      39.605  21.964  18.218  1.00106.17      A    O  
ANISOU 3624  O   SER A 498    15812  12252  12277    940   -144  -2248  A    O  
ATOM   3625  CB  SER A 498      38.395  25.183  19.143  1.00114.77      A    C  
ANISOU 3625  CB  SER A 498    17105  13966  12535    831   -437  -1765  A    C  
ATOM   3626  OG  SER A 498      37.166  25.848  19.387  1.00116.08      A    O  
ANISOU 3626  OG  SER A 498    17393  14326  12385    762   -546  -1680  A    O  
ATOM   3627  N   SER A 505      37.626  12.600  14.248  1.00172.69      A    N  
ANISOU 3627  N   SER A 505    24733  18741  22140    576    653  -4476  A    N  
ATOM   3628  CA  SER A 505      38.479  13.769  14.429  1.00176.69      A    C  
ANISOU 3628  CA  SER A 505    25061  19499  22576    732    701  -4288  A    C  
ATOM   3629  C   SER A 505      39.128  13.761  15.808  1.00190.80      A    C  
ANISOU 3629  C   SER A 505    26659  21029  24807    927    435  -3869  A    C  
ATOM   3630  O   SER A 505      39.899  14.661  16.149  1.00191.04      A    O  
ANISOU 3630  O   SER A 505    26526  21212  24850   1055    422  -3670  A    O  
ATOM   3631  CB  SER A 505      37.671  15.055  14.233  1.00171.79      A    C  
ANISOU 3631  CB  SER A 505    24559  19428  21284    568    624  -4108  A    C  
ATOM   3632  OG  SER A 505      36.743  15.246  15.288  1.00163.90      A    O  
ANISOU 3632  OG  SER A 505    23625  18496  20153    489    288  -3721  A    O  
ATOM   3633  N   SER A 506      38.817  12.720  16.578  1.00215.14      A    N  
ANISOU 3633  N   SER A 506    29779  23717  28245    917    207  -3731  A    N  
ATOM   3634  CA  SER A 506      39.272  12.555  17.957  1.00211.70      A    C  
ANISOU 3634  CA  SER A 506    29217  23019  28199   1032   -115  -3290  A    C  
ATOM   3635  C   SER A 506      39.053  13.828  18.767  1.00208.80      A    C  
ANISOU 3635  C   SER A 506    28854  23054  27427    981   -311  -2884  A    C  
ATOM   3636  O   SER A 506      39.964  14.320  19.433  1.00221.91      A    O  
ANISOU 3636  O   SER A 506    30338  24686  29291   1126   -418  -2636  A    O  
ATOM   3637  CB  SER A 506      40.755  12.171  17.989  1.00211.30      A    C  
ANISOU 3637  CB  SER A 506    28879  22596  28810   1319    -24  -3362  A    C  
ATOM   3638  OG  SER A 506      40.980  10.926  17.353  1.00211.68      A    O  
ANISOU 3638  OG  SER A 506    28910  22198  29322   1393    155  -3748  A    O  
ATOM   3639  N   ARG A 507      37.831  14.346  18.717  1.00192.81      A    N  
ANISOU 3639  N   ARG A 507    27021  21391  24849    770   -363  -2828  A    N  
ATOM   3640  CA  ARG A 507      37.495  15.581  19.412  1.00168.42      A    C  
ANISOU 3640  CA  ARG A 507    23948  18680  21363    719   -512  -2506  A    C  
ATOM   3641  C   ARG A 507      37.437  15.361  20.915  1.00154.36      A    C  
ANISOU 3641  C   ARG A 507    22169  16741  19739    679   -841  -2081  A    C  
ATOM   3642  O   ARG A 507      37.018  14.300  21.374  1.00158.78      A    O  
ANISOU 3642  O   ARG A 507    22806  17014  20511    581   -989  -2003  A    O  
ATOM   3643  CB  ARG A 507      36.172  16.137  18.893  1.00155.96      A    C  
ANISOU 3643  CB  ARG A 507    22538  17502  19220    523   -470  -2587  A    C  
ATOM   3644  CG  ARG A 507      35.802  17.487  19.467  1.00152.75      A    C  
ANISOU 3644  CG  ARG A 507    22136  17474  18427    497   -577  -2322  A    C  
ATOM   3645  CD  ARG A 507      34.500  17.968  18.883  1.00154.49      A    C  
ANISOU 3645  CD  ARG A 507    22475  18047  18178    332   -547  -2411  A    C  
ATOM   3646  NE  ARG A 507      34.632  18.216  17.450  1.00159.23      A    N  
ANISOU 3646  NE  ARG A 507    23100  18801  18600    329   -322  -2725  A    N  
ATOM   3647  CZ  ARG A 507      35.065  19.359  16.928  1.00167.43      A    C  
ANISOU 3647  CZ  ARG A 507    24102  20094  19418    396   -222  -2733  A    C  
ATOM   3648  NH1 ARG A 507      35.397  20.371  17.719  1.00164.39      A    N1+
ANISOU 3648  NH1 ARG A 507    23651  19821  18990    487   -326  -2464  A    N1+
ATOM   3649  NH2 ARG A 507      35.159  19.494  15.612  1.00177.40      A    N  
ANISOU 3649  NH2 ARG A 507    25415  21504  20485    340    -22  -3008  A    N  
ATOM   3650  N   THR A 508      37.832  16.372  21.681  1.00135.52      A    N  
ANISOU 3650  N   THR A 508    19723  14548  17222    719   -960  -1802  A    N  
ATOM   3651  CA  THR A 508      37.780  16.277  23.134  1.00132.72      A    C  
ANISOU 3651  CA  THR A 508    19400  14104  16925    632  -1272  -1394  A    C  
ATOM   3652  C   THR A 508      36.562  16.999  23.700  1.00120.77      A    C  
ANISOU 3652  C   THR A 508    18042  12962  14885    429  -1342  -1247  A    C  
ATOM   3653  O   THR A 508      36.236  18.112  23.290  1.00117.39      A    O  
ANISOU 3653  O   THR A 508    17624  12888  14089    441  -1216  -1335  A    O  
ATOM   3654  CB  THR A 508      39.053  16.854  23.781  1.00135.11      A    C  
ANISOU 3654  CB  THR A 508    19539  14351  17447    775  -1395  -1164  A    C  
ATOM   3655  CG2 THR A 508      39.115  16.503  25.258  1.00139.07      A    C  
ANISOU 3655  CG2 THR A 508    20087  14692  18060    653  -1750   -739  A    C  
ATOM   3656  OG1 THR A 508      40.209  16.324  23.122  1.00137.58      A    O  
ANISOU 3656  OG1 THR A 508    19644  14365  18265    993  -1273  -1346  A    O  
ATOM   3657  N   TRP A 509      35.911  16.365  24.668  1.00115.01      A    N  
ANISOU 3657  N   TRP A 509    17421  12136  14142    239  -1545  -1015  A    N  
ATOM   3658  CA  TRP A 509      34.689  16.902  25.248  1.00113.14      A    C  
ANISOU 3658  CA  TRP A 509    17305  12237  13446     29  -1578   -906  A    C  
ATOM   3659  C   TRP A 509      34.849  17.068  26.758  1.00115.85      A    C  
ANISOU 3659  C   TRP A 509    17704  12585  13729   -107  -1819   -524  A    C  
ATOM   3660  O   TRP A 509      35.812  16.573  27.346  1.00124.81      A    O  
ANISOU 3660  O   TRP A 509    18799  13423  15201    -67  -2015   -309  A    O  
ATOM   3661  CB  TRP A 509      33.495  15.987  24.948  1.00112.34      A    C  
ANISOU 3661  CB  TRP A 509    17301  12104  13280   -162  -1551  -1017  A    C  
ATOM   3662  CG  TRP A 509      32.957  16.047  23.535  1.00109.20      A    C  
ANISOU 3662  CG  TRP A 509    16895  11843  12753   -123  -1328  -1384  A    C  
ATOM   3663  CD1 TRP A 509      33.513  15.495  22.415  1.00112.52      A    C  
ANISOU 3663  CD1 TRP A 509    17281  12051  13420      2  -1187  -1674  A    C  
ATOM   3664  CD2 TRP A 509      31.736  16.668  23.109  1.00 98.56      A    C  
ANISOU 3664  CD2 TRP A 509    15573  10879  10997   -235  -1234  -1497  A    C  
ATOM   3665  CE2 TRP A 509      31.624  16.463  21.719  1.00 98.76      A    C  
ANISOU 3665  CE2 TRP A 509    15599  10915  11009   -194  -1074  -1825  A    C  
ATOM   3666  CE3 TRP A 509      30.730  17.382  23.768  1.00 90.56      A    C  
ANISOU 3666  CE3 TRP A 509    14568  10200   9642   -367  -1266  -1362  A    C  
ATOM   3667  NE1 TRP A 509      32.722  15.746  21.319  1.00103.70      A    N  
ANISOU 3667  NE1 TRP A 509    16201  11182  12017    -58  -1024  -1949  A    N  
ATOM   3668  CZ2 TRP A 509      30.548  16.949  20.976  1.00 99.75      A    C  
ANISOU 3668  CZ2 TRP A 509    15735  11373  10792   -290   -999  -1973  A    C  
ATOM   3669  CZ3 TRP A 509      29.664  17.862  23.031  1.00 89.58      A    C  
ANISOU 3669  CZ3 TRP A 509    14416  10384   9237   -423  -1169  -1527  A    C  
ATOM   3670  CH2 TRP A 509      29.581  17.645  21.650  1.00 96.07      A    C  
ANISOU 3670  CH2 TRP A 509    15241  11209  10053   -388  -1063  -1807  A    C  
ATOM   3671  N   MET A 510      33.906  17.773  27.378  1.00110.23      A    N  
ANISOU 3671  N   MET A 510    17078  12214  12591   -276  -1806   -445  A    N  
ATOM   3672  CA  MET A 510      33.833  17.867  28.835  1.00109.73      A    C  
ANISOU 3672  CA  MET A 510    17114  12205  12373   -487  -2001   -117  A    C  
ATOM   3673  C   MET A 510      32.501  17.298  29.311  1.00 89.51      A    C  
ANISOU 3673  C   MET A 510    14664   9759   9588   -778  -2000    -62  A    C  
ATOM   3674  O   MET A 510      31.461  17.590  28.735  1.00 91.25      A    O  
ANISOU 3674  O   MET A 510    14859  10225   9585   -805  -1815   -276  A    O  
ATOM   3675  CB  MET A 510      33.987  19.319  29.305  1.00118.90      A    C  
ANISOU 3675  CB  MET A 510    18279  13684  13214   -453  -1954    -90  A    C  
ATOM   3676  CG  MET A 510      35.353  19.664  29.890  1.00121.18      A    C  
ANISOU 3676  CG  MET A 510    18534  13835  13673   -373  -2137    117  A    C  
ATOM   3677  SD  MET A 510      35.351  21.209  30.833  1.00150.34      A    S  
ANISOU 3677  SD  MET A 510    22310  17877  16933   -460  -2135    196  A    S  
ATOM   3678  CE  MET A 510      34.229  20.804  32.167  1.00 75.36      A    C  
ANISOU 3678  CE  MET A 510    13008   8539   7086   -849  -2209    387  A    C  
ATOM   3679  N   CYS A 511      32.528  16.509  30.376  1.00 76.83      A    N  
ANISOU 3679  N   CYS A 511    13168   7987   8037  -1017  -2222    247  A    N  
ATOM   3680  CA  CYS A 511      31.311  15.881  30.873  1.00 98.35      A    C  
ANISOU 3680  CA  CYS A 511    15996  10811  10560  -1339  -2222    327  A    C  
ATOM   3681  C   CYS A 511      30.974  16.378  32.270  1.00110.98      A    C  
ANISOU 3681  C   CYS A 511    17717  12679  11773  -1623  -2286    574  A    C  
ATOM   3682  O   CYS A 511      31.847  16.513  33.127  1.00106.53      A    O  
ANISOU 3682  O   CYS A 511    17225  12024  11226  -1673  -2493    837  A    O  
ATOM   3683  CB  CYS A 511      31.452  14.358  30.881  1.00110.11      A    C  
ANISOU 3683  CB  CYS A 511    17549  11861  12427  -1454  -2416    478  A    C  
ATOM   3684  SG  CYS A 511      29.985  13.468  31.460  1.00180.05      A    S  
ANISOU 3684  SG  CYS A 511    26537  20809  21065  -1901  -2431    604  A    S  
ATOM   3685  N   ILE A 512      29.703  16.694  32.480  1.00115.46      A    N  
ANISOU 3685  N   ILE A 512    18294  13596  11981  -1816  -2099    471  A    N  
ATOM   3686  CA  ILE A 512      29.251  17.166  33.776  1.00118.74      A    C  
ANISOU 3686  CA  ILE A 512    18823  14306  11988  -2116  -2086    638  A    C  
ATOM   3687  C   ILE A 512      28.118  16.280  34.301  1.00137.08      A    C  
ANISOU 3687  C   ILE A 512    21219  16710  14155  -2507  -2069    754  A    C  
ATOM   3688  O   ILE A 512      27.080  16.115  33.661  1.00146.13      A    O  
ANISOU 3688  O   ILE A 512    22256  17993  15274  -2527  -1886    543  A    O  
ATOM   3689  CB  ILE A 512      28.835  18.647  33.696  1.00111.00      A    C  
ANISOU 3689  CB  ILE A 512    17755  13720  10699  -1977  -1825    380  A    C  
ATOM   3690  CG1 ILE A 512      30.032  19.529  34.049  1.00101.20      A    C  
ANISOU 3690  CG1 ILE A 512    16559  12443   9451  -1818  -1927    449  A    C  
ATOM   3691  CG2 ILE A 512      27.703  18.956  34.643  1.00126.55      A    C  
ANISOU 3691  CG2 ILE A 512    19771  16060  12252  -2298  -1656    377  A    C  
ATOM   3692  CD1 ILE A 512      31.036  19.667  32.945  1.00 74.06      A    C  
ANISOU 3692  CD1 ILE A 512    13003   8763   6374  -1443  -1973    339  A    C  
ATOM   3693  N   SER A 513      28.346  15.693  35.470  1.00145.32      A    N  
ANISOU 3693  N   SER A 513    22447  17669  15098  -2845  -2285   1114  A    N  
ATOM   3694  CA  SER A 513      27.414  14.745  36.062  1.00162.77      A    C  
ANISOU 3694  CA  SER A 513    24759  19917  17171  -3273  -2310   1296  A    C  
ATOM   3695  C   SER A 513      27.112  15.102  37.512  1.00171.65      A    C  
ANISOU 3695  C   SER A 513    26052  21362  17805  -3686  -2297   1512  A    C  
ATOM   3696  O   SER A 513      28.005  15.495  38.261  1.00182.60      A    O  
ANISOU 3696  O   SER A 513    27570  22724  19087  -3722  -2473   1711  A    O  
ATOM   3697  CB  SER A 513      27.968  13.320  35.979  1.00172.05      A    C  
ANISOU 3697  CB  SER A 513    26033  20574  18766  -3352  -2640   1581  A    C  
ATOM   3698  OG  SER A 513      27.154  12.424  36.715  1.00180.50      A    O  
ANISOU 3698  OG  SER A 513    27240  21667  19674  -3826  -2708   1829  A    O  
ATOM   3699  N   ARG A 514      25.849  14.973  37.898  1.00165.58      A    N  
ANISOU 3699  N   ARG A 514    25273  20912  16727  -4016  -2077   1458  A    N  
ATOM   3700  CA  ARG A 514      25.458  15.176  39.283  1.00152.04      A    C  
ANISOU 3700  CA  ARG A 514    23732  19523  14512  -4480  -2021   1644  A    C  
ATOM   3701  C   ARG A 514      25.041  13.802  39.854  1.00158.69      A    C  
ANISOU 3701  C   ARG A 514    24737  20215  15341  -4964  -2213   2012  A    C  
ATOM   3702  O   ARG A 514      25.485  12.772  39.345  1.00156.69      A    O  
ANISOU 3702  O   ARG A 514    24512  19503  15518  -4888  -2492   2190  A    O  
ATOM   3703  CB  ARG A 514      24.350  16.244  39.363  1.00135.09      A    C  
ANISOU 3703  CB  ARG A 514    21422  17901  12007  -4489  -1568   1267  A    C  
ATOM   3704  CG  ARG A 514      24.008  16.727  40.770  1.00134.53      A    C  
ANISOU 3704  CG  ARG A 514    21518  18222  11375  -4923  -1416   1346  A    C  
ATOM   3705  CD  ARG A 514      22.882  17.752  40.827  1.00130.12      A    C  
ANISOU 3705  CD  ARG A 514    20754  18148  10538  -4901   -933    930  A    C  
ATOM   3706  NE  ARG A 514      23.304  19.109  40.499  1.00121.47      A    N  
ANISOU 3706  NE  ARG A 514    19562  17131   9459  -4482   -794    620  A    N  
ATOM   3707  CZ  ARG A 514      23.548  20.035  41.421  1.00120.68      A    C  
ANISOU 3707  CZ  ARG A 514    19601  17262   8990  -4599   -669    544  A    C  
ATOM   3708  NH1 ARG A 514      23.427  19.733  42.705  1.00136.74      A    N1+
ANISOU 3708  NH1 ARG A 514    21882  19495  10580  -5131   -666    754  A    N1+
ATOM   3709  NH2 ARG A 514      23.914  21.256  41.071  1.00109.69      A    N  
ANISOU 3709  NH2 ARG A 514    18124  15901   7652  -4217   -554    260  A    N  
ATOM   3710  N   GLN A 515      24.208  13.782  40.892  1.00161.08      A    N  
ANISOU 3710  N   GLN A 515    25148  20887  15168  -5464  -2057   2117  A    N  
ATOM   3711  CA  GLN A 515      23.753  12.547  41.530  1.00151.11      A    C  
ANISOU 3711  CA  GLN A 515    24061  19529  13823  -5997  -2225   2494  A    C  
ATOM   3712  C   GLN A 515      22.468  12.774  42.312  1.00148.21      A    C  
ANISOU 3712  C   GLN A 515    23681  19709  12923  -6471  -1855   2407  A    C  
ATOM   3713  O   GLN A 515      21.504  12.027  42.152  1.00149.59      A    O  
ANISOU 3713  O   GLN A 515    23780  19934  13123  -6734  -1755   2424  A    O  
ATOM   3714  CB  GLN A 515      24.826  11.990  42.474  1.00148.17      A    C  
ANISOU 3714  CB  GLN A 515    24005  18868  13426  -6258  -2687   3022  A    C  
ATOM   3715  CG  GLN A 515      25.221  10.535  42.222  1.00147.65      A    C  
ANISOU 3715  CG  GLN A 515    24043  18223  13836  -6340  -3109   3403  A    C  
ATOM   3716  CD  GLN A 515      25.858  10.325  40.867  1.00139.60      A    C  
ANISOU 3716  CD  GLN A 515    22828  16744  13469  -5745  -3209   3189  A    C  
ATOM   3717  NE2 GLN A 515      27.149  10.623  40.767  1.00134.04      A    N  
ANISOU 3717  NE2 GLN A 515    22133  15766  13032  -5407  -3460   3275  A    N  
ATOM   3718  OE1 GLN A 515      25.193   9.918  39.912  1.00139.43      A    O  
ANISOU 3718  OE1 GLN A 515    22644  16637  13696  -5608  -3051   2935  A    O  
TER   
HETATM 3719 ZN    ZN A1001      29.152  12.567  29.293  1.00113.23      C   ZN  
ANISOU 3719 ZN    ZN A1001    17961  12164  12896  -1737  -2192     58  C   ZN  
CONECT 1934 3719
CONECT 1954 3719
CONECT 3595 3719
CONECT 3684 3719
CONECT 3719 1934 1954 3595 3684
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.