CNRS Nantes University US2B US2B
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***  4OBY  ***

elNémo ID: 241202081356530676

Job options:

ID        	=	 241202081356530676
JOBID     	=	 4OBY
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 4OBY

CRYST1  118.599   94.136   62.717  90.00 110.53  90.00 C 1 2 1       1
ATOM      1  N   MET A   1      30.338  66.097  43.704  1.00 84.66           N  
ANISOU    1  N   MET A   1    11810  10928   9431   1217    470     87       N  
ATOM      2  CA  MET A   1      29.651  66.534  42.495  1.00 79.90           C  
ANISOU    2  CA  MET A   1    11092  10308   8956   1206    531     83       C  
ATOM      3  C   MET A   1      30.239  65.786  41.301  1.00 79.18           C  
ANISOU    3  C   MET A   1    10842  10177   9064   1050    461    111       C  
ATOM      4  O   MET A   1      29.518  65.382  40.384  1.00 93.07           O  
ANISOU    4  O   MET A   1    12452  11968  10943   1018    531    173       O  
ATOM      5  CB  MET A   1      29.793  68.048  42.302  1.00 80.83           C  
ANISOU    5  CB  MET A   1    11343  10337   9032   1264    483    -47       C  
ATOM      6  CG  MET A   1      30.316  68.784  43.535  1.00 76.63           C  
ANISOU    6  CG  MET A   1    11040   9766   8312   1348    415   -141       C  
ATOM      7  SD  MET A   1      29.201  68.633  44.939  1.00137.35           S  
ANISOU    7  SD  MET A   1    18824  17584  15779   1534    577    -82       S  
ATOM      8  CE  MET A   1      30.332  68.402  46.319  1.00 75.54           C  
ANISOU    8  CE  MET A   1    11188   9737   7778   1533    443   -127       C  
ATOM      9  N   ASN A   2      31.561  65.615  41.319  1.00 60.43           N  
ANISOU    9  N   ASN A   2     8503   7734   6724    957    320     62       N  
ATOM     10  CA  ASN A   2      32.256  64.865  40.277  1.00 49.65           C  
ANISOU   10  CA  ASN A   2     6999   6332   5534    822    255     84       C  
ATOM     11  C   ASN A   2      33.192  63.872  40.926  1.00 53.79           C  
ANISOU   11  C   ASN A   2     7525   6859   6053    766    172    119       C  
ATOM     12  O   ASN A   2      34.357  64.178  41.175  1.00 51.65           O  
ANISOU   12  O   ASN A   2     7324   6526   5774    724     43     52       O  
ATOM     13  CB  ASN A   2      33.027  65.795  39.328  1.00 37.82           C  
ANISOU   13  CB  ASN A   2     5513   4734   4123    757    164    -13       C  
ATOM     14  CG  ASN A   2      33.618  65.059  38.110  1.00 55.51           C  
ANISOU   14  CG  ASN A   2     7604   6947   6540    634    126     11       C  
ATOM     15  ND2 ASN A   2      33.633  65.737  36.967  1.00 55.32           N  
ANISOU   15  ND2 ASN A   2     7543   6873   6602    598    122    -31       N  
ATOM     16  OD1 ASN A   2      34.067  63.909  38.201  1.00 62.87           O  
ANISOU   16  OD1 ASN A   2     8463   7899   7523    579    100     66       O  
ATOM     17  N   ILE A   3      32.689  62.669  41.182  1.00 53.10           N  
ANISOU   17  N   ILE A   3     7355   6841   5980    761    239    231       N  
ATOM     18  CA  ILE A   3      33.460  61.707  41.945  1.00 49.80           C  
ANISOU   18  CA  ILE A   3     6954   6429   5538    728    168    278       C  
ATOM     19  C   ILE A   3      34.784  61.383  41.277  1.00 49.27           C  
ANISOU   19  C   ILE A   3     6829   6287   5606    620     36    237       C  
ATOM     20  O   ILE A   3      35.819  61.333  41.941  1.00 51.57           O  
ANISOU   20  O   ILE A   3     7188   6550   5856    604    -78    209       O  
ATOM     21  CB  ILE A   3      32.695  60.408  42.165  1.00 53.43           C  
ANISOU   21  CB  ILE A   3     7320   6960   6022    725    260    417       C  
ATOM     22  CG1 ILE A   3      31.226  60.693  42.487  1.00 65.77           C  
ANISOU   22  CG1 ILE A   3     8881   8607   7502    819    418    475       C  
ATOM     23  CG2 ILE A   3      33.380  59.583  43.256  1.00 51.80           C  
ANISOU   23  CG2 ILE A   3     7175   6765   5741    723    195    471       C  
ATOM     24  CD1 ILE A   3      31.019  61.613  43.672  1.00 77.06           C  
ANISOU   24  CD1 ILE A   3    10484  10073   8722    945    449    433       C  
ATOM     25  N   GLN A   4      34.755  61.181  39.965  1.00 51.07           N  
ANISOU   25  N   GLN A   4     6930   6485   5989    550     52    233       N  
ATOM     26  CA  GLN A   4      35.967  60.788  39.259  1.00 47.90           C  
ANISOU   26  CA  GLN A   4     6458   6023   5719    457    -49    204       C  
ATOM     27  C   GLN A   4      36.979  61.913  39.343  1.00 55.38           C  
ANISOU   27  C   GLN A   4     7487   6909   6645    441   -156    101       C  
ATOM     28  O   GLN A   4      38.175  61.664  39.493  1.00 48.80           O  
ANISOU   28  O   GLN A   4     6643   6040   5857    390   -267     83       O  
ATOM     29  CB  GLN A   4      35.679  60.444  37.798  1.00 43.54           C  
ANISOU   29  CB  GLN A   4     5774   5453   5317    399     -3    212       C  
ATOM     30  CG  GLN A   4      36.928  60.151  36.951  1.00 53.58           C  
ANISOU   30  CG  GLN A   4     6973   6667   6720    317    -88    174       C  
ATOM     31  CD  GLN A   4      37.561  61.378  36.283  1.00 59.57           C  
ANISOU   31  CD  GLN A   4     7753   7373   7507    287   -132     84       C  
ATOM     32  NE2 GLN A   4      38.778  61.197  35.779  1.00 62.24           N  
ANISOU   32  NE2 GLN A   4     8034   7670   7944    223   -207     58       N  
ATOM     33  OE1 GLN A   4      36.975  62.464  36.227  1.00 64.71           O  
ANISOU   33  OE1 GLN A   4     8469   8020   8098    324    -97     44       O  
ATOM     34  N   ALA A   5      36.502  63.153  39.238  1.00 56.10           N  
ANISOU   34  N   ALA A   5     7655   6984   6676    483   -127     38       N  
ATOM     35  CA  ALA A   5      37.410  64.289  39.324  1.00 50.83           C  
ANISOU   35  CA  ALA A   5     7075   6244   5994    460   -235    -58       C  
ATOM     36  C   ALA A   5      38.036  64.337  40.703  1.00 48.30           C  
ANISOU   36  C   ALA A   5     6879   5922   5551    491   -337    -77       C  
ATOM     37  O   ALA A   5      39.260  64.400  40.807  1.00 54.76           O  
ANISOU   37  O   ALA A   5     7696   6692   6419    425   -469   -112       O  
ATOM     38  CB  ALA A   5      36.705  65.593  39.021  1.00 46.61           C  
ANISOU   38  CB  ALA A   5     6617   5681   5412    510   -186   -119       C  
ATOM     39  N   LEU A   6      37.202  64.314  41.750  1.00 35.65           N  
ANISOU   39  N   LEU A   6     5381   4376   3788    591   -275    -52       N  
ATOM     40  CA  LEU A   6      37.684  64.311  43.148  1.00 39.53           C  
ANISOU   40  CA  LEU A   6     6013   4876   4129    636   -366    -66       C  
ATOM     41  C   LEU A   6      38.765  63.236  43.412  1.00 52.64           C  
ANISOU   41  C   LEU A   6     7608   6538   5856    568   -475    -17       C  
ATOM     42  O   LEU A   6      39.883  63.550  43.844  1.00 55.86           O  
ANISOU   42  O   LEU A   6     8071   6896   6258    529   -630    -70       O  
ATOM     43  CB  LEU A   6      36.505  64.106  44.097  1.00 38.55           C  
ANISOU   43  CB  LEU A   6     5974   4838   3833    757   -244    -11       C  
ATOM     44  CG  LEU A   6      36.815  63.776  45.552  1.00 54.63           C  
ANISOU   44  CG  LEU A   6     8149   6911   5699    816   -306      9       C  
ATOM     45  CD1 LEU A   6      37.288  65.034  46.268  1.00 72.57           C  
ANISOU   45  CD1 LEU A   6    10617   9122   7834    861   -419   -115       C  
ATOM     46  CD2 LEU A   6      35.572  63.196  46.229  1.00 54.92           C  
ANISOU   46  CD2 LEU A   6     8204   7052   5609    917   -143    110       C  
ATOM     47  N   LEU A   7      38.425  61.975  43.132  1.00 47.15           N  
ANISOU   47  N   LEU A   7     6791   5891   5233    551   -400     85       N  
ATOM     48  CA  LEU A   7      39.364  60.864  43.260  1.00 48.59           C  
ANISOU   48  CA  LEU A   7     6897   6068   5496    495   -488    140       C  
ATOM     49  C   LEU A   7      40.616  61.050  42.413  1.00 52.78           C  
ANISOU   49  C   LEU A   7     7335   6530   6189    400   -599     85       C  
ATOM     50  O   LEU A   7      41.722  60.678  42.816  1.00 56.01           O  
ANISOU   50  O   LEU A   7     7732   6919   6631    366   -729     89       O  
ATOM     51  CB  LEU A   7      38.689  59.552  42.870  1.00 53.95           C  
ANISOU   51  CB  LEU A   7     7458   6790   6250    488   -380    252       C  
ATOM     52  CG  LEU A   7      37.469  59.203  43.714  1.00 54.07           C  
ANISOU   52  CG  LEU A   7     7536   6882   6125    571   -261    335       C  
ATOM     53  CD1 LEU A   7      36.759  57.992  43.130  1.00 45.79           C  
ANISOU   53  CD1 LEU A   7     6354   5859   5185    541   -161    443       C  
ATOM     54  CD2 LEU A   7      37.892  58.987  45.143  1.00 44.15           C  
ANISOU   54  CD2 LEU A   7     6411   5651   4711    622   -338    363       C  
ATOM     55  N   SER A   8      40.447  61.621  41.231  1.00 62.42           N  
ANISOU   55  N   SER A   8     8484   7719   7512    360   -546     42       N  
ATOM     56  CA  SER A   8      41.564  61.716  40.298  1.00 61.23           C  
ANISOU   56  CA  SER A   8     8225   7516   7525    270   -621      8       C  
ATOM     57  C   SER A   8      42.672  62.664  40.793  1.00 53.70           C  
ANISOU   57  C   SER A   8     7342   6508   6554    234   -777    -66       C  
ATOM     58  O   SER A   8      43.873  62.391  40.609  1.00 54.45           O  
ANISOU   58  O   SER A   8     7351   6577   6761    169   -881    -65       O  
ATOM     59  CB  SER A   8      41.064  62.147  38.932  1.00 31.29           C  
ANISOU   59  CB  SER A   8     4355   3706   3825    241   -522    -14       C  
ATOM     60  OG  SER A   8      41.964  61.695  37.962  1.00 44.76           O  
ANISOU   60  OG  SER A   8     5926   5388   5692    169   -549     -9       O  
ATOM     61  N   GLU A   9      42.277  63.754  41.445  1.00 40.47           N  
ANISOU   61  N   GLU A   9     5822   4813   4744    279   -798   -129       N  
ATOM     62  CA  GLU A   9      43.262  64.702  41.943  1.00 48.99           C  
ANISOU   62  CA  GLU A   9     6983   5826   5803    239   -961   -205       C  
ATOM     63  C   GLU A   9      43.883  64.203  43.254  1.00 50.18           C  
ANISOU   63  C   GLU A   9     7211   5996   5859    262  -1093   -189       C  
ATOM     64  O   GLU A   9      45.012  64.569  43.600  1.00 53.11           O  
ANISOU   64  O   GLU A   9     7594   6320   6264    205  -1262   -228       O  
ATOM     65  CB  GLU A   9      42.629  66.098  42.110  1.00 56.71           C  
ANISOU   65  CB  GLU A   9     8116   6758   6674    281   -946   -290       C  
ATOM     66  CG  GLU A   9      43.612  67.205  42.536  1.00 71.27           C  
ANISOU   66  CG  GLU A   9    10058   8511   8511    227  -1126   -378       C  
ATOM     67  CD  GLU A   9      44.873  67.276  41.671  1.00 76.93           C  
ANISOU   67  CD  GLU A   9    10620   9177   9431     96  -1218   -375       C  
ATOM     68  OE1 GLU A   9      44.768  67.239  40.420  1.00 63.74           O  
ANISOU   68  OE1 GLU A   9     8818   7506   7894     50  -1118   -349       O  
ATOM     69  OE2 GLU A   9      45.978  67.367  42.254  1.00 88.08           O1-
ANISOU   69  OE2 GLU A   9    12042  10557  10869     39  -1391   -394       O1-
ATOM     70  N   LYS A  10      43.161  63.355  43.979  1.00 47.04           N  
ANISOU   70  N   LYS A  10     6860   5668   5345    343  -1023   -123       N  
ATOM     71  CA  LYS A  10      43.720  62.818  45.212  1.00 54.84           C  
ANISOU   71  CA  LYS A  10     7926   6678   6232    371  -1145    -95       C  
ATOM     72  C   LYS A  10      44.746  61.716  44.904  1.00 56.41           C  
ANISOU   72  C   LYS A  10     7962   6880   6590    307  -1219    -29       C  
ATOM     73  O   LYS A  10      45.799  61.657  45.539  1.00 67.18           O  
ANISOU   73  O   LYS A  10     9343   8225   7957    280  -1389    -38       O  
ATOM     74  CB  LYS A  10      42.598  62.328  46.145  1.00 52.24           C  
ANISOU   74  CB  LYS A  10     7712   6425   5713    482  -1037    -36       C  
ATOM     75  CG  LYS A  10      41.802  63.498  46.746  1.00 45.40           C  
ANISOU   75  CG  LYS A  10     7036   5554   4658    567   -998   -114       C  
ATOM     76  CD  LYS A  10      40.879  63.079  47.865  1.00 54.30           C  
ANISOU   76  CD  LYS A  10     8293   6763   5574    685   -909    -55       C  
ATOM     77  CE  LYS A  10      40.422  64.275  48.712  1.00 66.01           C  
ANISOU   77  CE  LYS A  10    10002   8235   6845    783   -919   -151       C  
ATOM     78  NZ  LYS A  10      41.503  64.815  49.608  1.00 73.47           N1+
ANISOU   78  NZ  LYS A  10    11096   9122   7697    769  -1141   -234       N1+
ATOM     79  N   VAL A  11      44.464  60.881  43.907  1.00 44.32           N  
ANISOU   79  N   VAL A  11     6276   5368   5196    285  -1100     31       N  
ATOM     80  CA  VAL A  11      45.387  59.820  43.509  1.00 45.52           C  
ANISOU   80  CA  VAL A  11     6273   5517   5506    239  -1153     89       C  
ATOM     81  C   VAL A  11      46.647  60.410  42.880  1.00 42.80           C  
ANISOU   81  C   VAL A  11     5829   5120   5313    152  -1266     34       C  
ATOM     82  O   VAL A  11      47.752  59.897  43.077  1.00 47.46           O  
ANISOU   82  O   VAL A  11     6338   5703   5991    122  -1387     60       O  
ATOM     83  CB  VAL A  11      44.733  58.821  42.501  1.00 42.12           C  
ANISOU   83  CB  VAL A  11     5714   5107   5183    240   -997    154       C  
ATOM     84  CG1 VAL A  11      45.773  57.872  41.903  1.00 37.44           C  
ANISOU   84  CG1 VAL A  11     4960   4496   4769    197  -1048    191       C  
ATOM     85  CG2 VAL A  11      43.635  58.024  43.168  1.00 37.39           C  
ANISOU   85  CG2 VAL A  11     5182   4558   4465    310   -901    235       C  
ATOM     86  N   ARG A  12      46.476  61.480  42.111  1.00 51.68           N  
ANISOU   86  N   ARG A  12     6952   6210   6476    112  -1223    -33       N  
ATOM     87  CA  ARG A  12      47.609  62.142  41.472  1.00 45.20           C  
ANISOU   87  CA  ARG A  12     6034   5339   5802     20  -1316    -75       C  
ATOM     88  C   ARG A  12      48.555  62.706  42.523  1.00 45.91           C  
ANISOU   88  C   ARG A  12     6202   5395   5844     -8  -1522   -114       C  
ATOM     89  O   ARG A  12      49.777  62.625  42.385  1.00 55.72           O  
ANISOU   89  O   ARG A  12     7328   6620   7222    -75  -1643   -104       O  
ATOM     90  CB  ARG A  12      47.141  63.258  40.540  1.00 56.49           C  
ANISOU   90  CB  ARG A  12     7475   6731   7259    -15  -1231   -133       C  
ATOM     91  CG  ARG A  12      48.296  64.075  39.969  1.00 64.49           C  
ANISOU   91  CG  ARG A  12     8403   7686   8414   -117  -1329   -168       C  
ATOM     92  CD  ARG A  12      47.935  65.520  39.784  1.00 75.00           C  
ANISOU   92  CD  ARG A  12     9843   8954   9700   -145  -1331   -241       C  
ATOM     93  NE  ARG A  12      47.386  65.764  38.457  1.00 84.39           N  
ANISOU   93  NE  ARG A  12    10961  10141  10964   -160  -1178   -234       N  
ATOM     94  CZ  ARG A  12      48.130  65.854  37.364  1.00 92.03           C  
ANISOU   94  CZ  ARG A  12    11778  11094  12096   -239  -1158   -214       C  
ATOM     95  NH1 ARG A  12      49.441  65.709  37.451  1.00 91.43           N1+
ANISOU   95  NH1 ARG A  12    11592  11009  12139   -310  -1275   -195       N1+
ATOM     96  NH2 ARG A  12      47.567  66.082  36.187  1.00 97.31           N  
ANISOU   96  NH2 ARG A  12    12404  11763  12808   -245  -1019   -208       N  
ATOM     97  N   GLN A  13      47.985  63.271  43.581  1.00 48.19           N  
ANISOU   97  N   GLN A  13     6690   5680   5941     48  -1565   -156       N  
ATOM     98  CA  GLN A  13      48.785  63.861  44.643  1.00 50.01           C  
ANISOU   98  CA  GLN A  13     7030   5873   6099     27  -1775   -205       C  
ATOM     99  C   GLN A  13      49.519  62.794  45.450  1.00 51.33           C  
ANISOU   99  C   GLN A  13     7160   6079   6264     46  -1894   -140       C  
ATOM    100  O   GLN A  13      50.660  63.010  45.888  1.00 50.22           O  
ANISOU  100  O   GLN A  13     6996   5908   6176    -11  -2090   -156       O  
ATOM    101  CB  GLN A  13      47.918  64.730  45.567  1.00 48.85           C  
ANISOU  101  CB  GLN A  13     7128   5710   5724    102  -1779   -276       C  
ATOM    102  CG  GLN A  13      48.193  66.227  45.400  1.00 66.88           C  
ANISOU  102  CG  GLN A  13     9494   7900   8019     41  -1869   -380       C  
ATOM    103  CD  GLN A  13      49.685  66.597  45.538  1.00 78.12           C  
ANISOU  103  CD  GLN A  13    10850   9263   9569    -72  -2097   -404       C  
ATOM    104  NE2 GLN A  13      50.065  67.713  44.929  1.00 66.69           N  
ANISOU  104  NE2 GLN A  13     9386   7729   8222   -162  -2146   -462       N  
ATOM    105  OE1 GLN A  13      50.479  65.885  46.180  1.00 87.57           O  
ANISOU  105  OE1 GLN A  13    12004  10488  10779    -80  -2229   -363       O  
ATOM    106  N   ALA A  14      48.857  61.656  45.660  1.00 45.60           N  
ANISOU  106  N   ALA A  14     6431   5417   5480    122  -1784    -60       N  
ATOM    107  CA  ALA A  14      49.483  60.546  46.353  1.00 41.17           C  
ANISOU  107  CA  ALA A  14     5832   4888   4923    147  -1882     16       C  
ATOM    108  C   ALA A  14      50.657  60.085  45.509  1.00 50.37           C  
ANISOU  108  C   ALA A  14     6772   6038   6330     73  -1938     47       C  
ATOM    109  O   ALA A  14      51.777  60.007  45.999  1.00 42.17           O  
ANISOU  109  O   ALA A  14     5689   4988   5347     41  -2121     55       O  
ATOM    110  CB  ALA A  14      48.503  59.417  46.582  1.00 40.59           C  
ANISOU  110  CB  ALA A  14     5783   4872   4766    231  -1736    105       C  
ATOM    111  N   MET A  15      50.392  59.804  44.231  1.00 46.49           N  
ANISOU  111  N   MET A  15     6137   5548   5979     51  -1779     64       N  
ATOM    112  CA  MET A  15      51.435  59.421  43.276  1.00 42.77           C  
ANISOU  112  CA  MET A  15     5448   5067   5734     -8  -1795     89       C  
ATOM    113  C   MET A  15      52.615  60.387  43.320  1.00 47.44           C  
ANISOU  113  C   MET A  15     5988   5620   6418    -97  -1965     40       C  
ATOM    114  O   MET A  15      53.760  59.963  43.493  1.00 47.43           O  
ANISOU  114  O   MET A  15     5865   5623   6534   -122  -2095     77       O  
ATOM    115  CB  MET A  15      50.867  59.360  41.849  1.00 40.99           C  
ANISOU  115  CB  MET A  15     5123   4842   5610    -22  -1598     86       C  
ATOM    116  CG  MET A  15      49.865  58.231  41.612  1.00 37.82           C  
ANISOU  116  CG  MET A  15     4724   4472   5173     49  -1444    144       C  
ATOM    117  SD  MET A  15      49.082  58.224  39.996  1.00 62.90           S  
ANISOU  117  SD  MET A  15     7814   7646   8439     35  -1234    130       S  
ATOM    118  CE  MET A  15      50.465  57.913  38.917  1.00 70.09           C  
ANISOU  118  CE  MET A  15     8507   8546   9580    -16  -1256    139       C  
ATOM    119  N   ILE A  16      52.323  61.684  43.172  1.00 47.04           N  
ANISOU  119  N   ILE A  16     6027   5527   6321   -145  -1967    -37       N  
ATOM    120  CA  ILE A  16      53.353  62.718  43.219  1.00 41.53           C  
ANISOU  120  CA  ILE A  16     5295   4776   5709   -245  -2132    -83       C  
ATOM    121  C   ILE A  16      54.175  62.567  44.493  1.00 43.36           C  
ANISOU  121  C   ILE A  16     5579   5005   5889   -244  -2365    -78       C  
ATOM    122  O   ILE A  16      55.392  62.624  44.435  1.00 59.32           O  
ANISOU  122  O   ILE A  16     7459   7014   8064   -317  -2509    -59       O  
ATOM    123  CB  ILE A  16      52.751  64.156  43.107  1.00 41.48           C  
ANISOU  123  CB  ILE A  16     5434   4706   5619   -281  -2115   -172       C  
ATOM    124  CG1 ILE A  16      52.305  64.431  41.679  1.00 39.97           C  
ANISOU  124  CG1 ILE A  16     5145   4510   5532   -310  -1924   -170       C  
ATOM    125  CG2 ILE A  16      53.773  65.194  43.428  1.00 43.08           C  
ANISOU  125  CG2 ILE A  16     5641   4840   5886   -384  -2322   -221       C  
ATOM    126  CD1 ILE A  16      51.915  65.878  41.414  1.00 45.34           C  
ANISOU  126  CD1 ILE A  16     5936   5116   6174   -358  -1920   -246       C  
ATOM    127  N   ALA A  17      53.512  62.317  45.620  1.00 43.87           N  
ANISOU  127  N   ALA A  17     5838   5089   5741   -158  -2398    -84       N  
ATOM    128  CA  ALA A  17      54.187  62.092  46.911  1.00 50.98           C  
ANISOU  128  CA  ALA A  17     6819   5995   6557   -141  -2620    -75       C  
ATOM    129  C   ALA A  17      55.080  60.873  46.870  1.00 49.08           C  
ANISOU  129  C   ALA A  17     6394   5795   6459   -131  -2677     20       C  
ATOM    130  O   ALA A  17      56.062  60.796  47.592  1.00 56.34           O  
ANISOU  130  O   ALA A  17     7291   6711   7406   -155  -2891     34       O  
ATOM    131  CB  ALA A  17      53.168  61.942  48.040  1.00 47.76           C  
ANISOU  131  CB  ALA A  17     6658   5613   5875    -33  -2599    -85       C  
ATOM    132  N   ALA A  18      54.724  59.924  46.010  1.00 56.72           N  
ANISOU  132  N   ALA A  18     7232   6799   7521    -93  -2489     83       N  
ATOM    133  CA  ALA A  18      55.475  58.681  45.836  1.00 61.49           C  
ANISOU  133  CA  ALA A  18     7660   7434   8269    -65  -2511    173       C  
ATOM    134  C   ALA A  18      56.656  58.822  44.871  1.00 68.50           C  
ANISOU  134  C   ALA A  18     8301   8313   9414   -146  -2544    184       C  
ATOM    135  O   ALA A  18      57.452  57.897  44.737  1.00 76.84           O  
ANISOU  135  O   ALA A  18     9194   9392  10608   -121  -2582    252       O  
ATOM    136  CB  ALA A  18      54.544  57.568  45.358  1.00 54.23           C  
ANISOU  136  CB  ALA A  18     6728   6544   7331     16  -2302    232       C  
ATOM    137  N   GLY A  19      56.773  59.966  44.200  1.00 62.10           N  
ANISOU  137  N   GLY A  19     7457   7468   8670   -236  -2522    123       N  
ATOM    138  CA  GLY A  19      57.905  60.205  43.321  1.00 54.88           C  
ANISOU  138  CA  GLY A  19     6308   6550   7994   -320  -2549    142       C  
ATOM    139  C   GLY A  19      57.481  60.415  41.877  1.00 53.28           C  
ANISOU  139  C   GLY A  19     6012   6348   7884   -343  -2324    133       C  
ATOM    140  O   GLY A  19      58.285  60.807  41.023  1.00 52.90           O  
ANISOU  140  O   GLY A  19     5784   6297   8018   -418  -2311    145       O  
ATOM    141  N   ALA A  20      56.209  60.154  41.599  1.00 52.12           N  
ANISOU  141  N   ALA A  20     5984   6208   7612   -278  -2147    117       N  
ATOM    142  CA  ALA A  20      55.669  60.353  40.260  1.00 50.58           C  
ANISOU  142  CA  ALA A  20     5728   6012   7476   -291  -1939    104       C  
ATOM    143  C   ALA A  20      55.914  61.792  39.809  1.00 64.47           C  
ANISOU  143  C   ALA A  20     7486   7726   9282   -399  -1965     53       C  
ATOM    144  O   ALA A  20      56.022  62.707  40.640  1.00 66.01           O  
ANISOU  144  O   ALA A  20     7804   7878   9400   -447  -2118      5       O  
ATOM    145  CB  ALA A  20      54.182  60.022  40.225  1.00 41.04           C  
ANISOU  145  CB  ALA A  20     4674   4814   6108   -215  -1782     90       C  
ATOM    146  N   PRO A  21      56.062  61.991  38.496  1.00 68.45           N  
ANISOU  146  N   PRO A  21     7855   8235   9916   -438  -1825     65       N  
ATOM    147  CA  PRO A  21      56.162  63.356  37.976  1.00 74.63           C  
ANISOU  147  CA  PRO A  21     8648   8968  10738   -540  -1827     27       C  
ATOM    148  C   PRO A  21      54.849  64.131  38.172  1.00 75.77           C  
ANISOU  148  C   PRO A  21     9018   9070  10699   -519  -1768    -41       C  
ATOM    149  O   PRO A  21      53.828  63.516  38.489  1.00 74.42           O  
ANISOU  149  O   PRO A  21     8961   8925  10390   -425  -1687    -48       O  
ATOM    150  CB  PRO A  21      56.486  63.147  36.487  1.00 74.39           C  
ANISOU  150  CB  PRO A  21     8432   8969  10865   -559  -1657     69       C  
ATOM    151  CG  PRO A  21      56.247  61.691  36.213  1.00 71.04           C  
ANISOU  151  CG  PRO A  21     7946   8602  10444   -451  -1546    107       C  
ATOM    152  CD  PRO A  21      56.464  60.985  37.501  1.00 66.29           C  
ANISOU  152  CD  PRO A  21     7393   8010   9783   -399  -1696    121       C  
ATOM    153  N   ALA A  22      54.892  65.454  37.993  1.00 71.28           N  
ANISOU  153  N   ALA A  22     8507   8437  10140   -605  -1810    -84       N  
ATOM    154  CA  ALA A  22      53.739  66.323  38.213  1.00 64.41           C  
ANISOU  154  CA  ALA A  22     7851   7516   9107   -581  -1771   -153       C  
ATOM    155  C   ALA A  22      52.618  66.067  37.222  1.00 69.28           C  
ANISOU  155  C   ALA A  22     8480   8162   9681   -520  -1546   -147       C  
ATOM    156  O   ALA A  22      51.455  66.345  37.513  1.00 78.76           O  
ANISOU  156  O   ALA A  22     9847   9351  10727   -456  -1486   -189       O  
ATOM    157  CB  ALA A  22      54.159  67.780  38.135  1.00 63.53           C  
ANISOU  157  CB  ALA A  22     7783   7313   9043   -693  -1873   -195       C  
ATOM    158  N   ASP A  23      52.976  65.561  36.043  1.00 67.90           N  
ANISOU  158  N   ASP A  23     8129   8027   9643   -536  -1425    -95       N  
ATOM    159  CA  ASP A  23      52.021  65.388  34.945  1.00 61.66           C  
ANISOU  159  CA  ASP A  23     7340   7259   8828   -492  -1225    -89       C  
ATOM    160  C   ASP A  23      51.544  63.942  34.797  1.00 62.46           C  
ANISOU  160  C   ASP A  23     7399   7428   8906   -396  -1122    -56       C  
ATOM    161  O   ASP A  23      51.021  63.555  33.747  1.00 63.17           O  
ANISOU  161  O   ASP A  23     7443   7543   9014   -367   -968    -42       O  
ATOM    162  CB  ASP A  23      52.641  65.869  33.627  1.00 70.28           C  
ANISOU  162  CB  ASP A  23     8291   8344  10069   -570  -1145    -58       C  
ATOM    163  CG  ASP A  23      53.803  65.004  33.171  1.00 88.38           C  
ANISOU  163  CG  ASP A  23    10370  10691  12521   -584  -1137      3       C  
ATOM    164  OD1 ASP A  23      54.428  64.316  34.015  1.00 89.58           O  
ANISOU  164  OD1 ASP A  23    10474  10865  12698   -563  -1250     20       O  
ATOM    165  OD2 ASP A  23      54.101  65.024  31.955  1.00102.89           O1-
ANISOU  165  OD2 ASP A  23    12088  12550  14455   -608  -1016     38       O1-
ATOM    166  N   CYS A  24      51.729  63.156  35.857  1.00 64.43           N  
ANISOU  166  N   CYS A  24     7670   7699   9111   -350  -1216    -42       N  
ATOM    167  CA  CYS A  24      51.308  61.762  35.891  1.00 57.29           C  
ANISOU  167  CA  CYS A  24     6740   6843   8186   -263  -1143     -5       C  
ATOM    168  C   CYS A  24      49.812  61.612  35.675  1.00 61.60           C  
ANISOU  168  C   CYS A  24     7400   7398   8607   -202  -1009    -19       C  
ATOM    169  O   CYS A  24      49.013  62.516  35.954  1.00 65.77           O  
ANISOU  169  O   CYS A  24     8062   7902   9023   -200  -1000    -60       O  
ATOM    170  CB  CYS A  24      51.701  61.109  37.219  1.00 61.80           C  
ANISOU  170  CB  CYS A  24     7347   7427   8709   -227  -1284     17       C  
ATOM    171  SG  CYS A  24      50.891  61.804  38.695  1.00 77.54           S  
ANISOU  171  SG  CYS A  24     9580   9398  10485   -197  -1381    -29       S  
ATOM    172  N   GLU A  25      49.438  60.450  35.171  1.00 65.85           N  
ANISOU  172  N   GLU A  25     7880   7968   9171   -149   -909     17       N  
ATOM    173  CA  GLU A  25      48.040  60.143  34.973  1.00 69.88           C  
ANISOU  173  CA  GLU A  25     8475   8491   9583    -95   -791     16       C  
ATOM    174  C   GLU A  25      47.619  59.071  35.949  1.00 57.10           C  
ANISOU  174  C   GLU A  25     6908   6894   7893    -32   -816     58       C  
ATOM    175  O   GLU A  25      48.063  57.935  35.846  1.00 66.18           O  
ANISOU  175  O   GLU A  25     7973   8053   9118     -7   -820     99       O  
ATOM    176  CB  GLU A  25      47.787  59.700  33.531  1.00 91.53           C  
ANISOU  176  CB  GLU A  25    11128  11243  12406    -92   -656     22       C  
ATOM    177  CG  GLU A  25      48.066  60.789  32.507  1.00104.56           C  
ANISOU  177  CG  GLU A  25    12742  12877  14111   -152   -611     -7       C  
ATOM    178  CD  GLU A  25      47.010  61.874  32.519  1.00112.50           C  
ANISOU  178  CD  GLU A  25    13874  13862  15008   -156   -576    -43       C  
ATOM    179  OE1 GLU A  25      46.027  61.740  33.286  1.00114.86           O  
ANISOU  179  OE1 GLU A  25    14279  14170  15192   -106   -571    -45       O  
ATOM    180  OE2 GLU A  25      47.167  62.863  31.768  1.00112.81           O1-
ANISOU  180  OE2 GLU A  25    13905  13877  15080   -205   -548    -63       O1-
ATOM    181  N   PRO A  26      46.793  59.443  36.936  1.00 58.70           N  
ANISOU  181  N   PRO A  26     7254   7103   7946      0   -835     51       N  
ATOM    182  CA  PRO A  26      46.216  58.448  37.851  1.00 65.10           C  
ANISOU  182  CA  PRO A  26     8124   7941   8672     62   -835    105       C  
ATOM    183  C   PRO A  26      45.381  57.385  37.096  1.00 67.47           C  
ANISOU  183  C   PRO A  26     8372   8253   9011     90   -707    148       C  
ATOM    184  O   PRO A  26      45.370  56.209  37.492  1.00 66.61           O  
ANISOU  184  O   PRO A  26     8245   8149   8915    123   -717    208       O  
ATOM    185  CB  PRO A  26      45.341  59.299  38.794  1.00 52.58           C  
ANISOU  185  CB  PRO A  26     6702   6364   6911     95   -839     80       C  
ATOM    186  CG  PRO A  26      45.207  60.649  38.107  1.00 48.77           C  
ANISOU  186  CG  PRO A  26     6241   5853   6435     56   -811     10       C  
ATOM    187  CD  PRO A  26      46.449  60.824  37.319  1.00 45.94           C  
ANISOU  187  CD  PRO A  26     5756   5466   6232    -15   -864     -6       C  
ATOM    188  N   GLN A  27      44.729  57.810  36.010  1.00 62.03           N  
ANISOU  188  N   GLN A  27     7661   7560   8346     74   -601    118       N  
ATOM    189  CA  GLN A  27      43.840  56.970  35.197  1.00 60.74           C  
ANISOU  189  CA  GLN A  27     7460   7403   8217     91   -490    147       C  
ATOM    190  C   GLN A  27      42.691  56.362  36.010  1.00 58.05           C  
ANISOU  190  C   GLN A  27     7191   7086   7778    135   -451    205       C  
ATOM    191  O   GLN A  27      42.456  55.146  35.970  1.00 63.20           O  
ANISOU  191  O   GLN A  27     7808   7733   8473    149   -430    261       O  
ATOM    192  CB  GLN A  27      44.620  55.847  34.505  1.00 57.29           C  
ANISOU  192  CB  GLN A  27     6909   6946   7914     89   -493    166       C  
ATOM    193  CG  GLN A  27      45.550  56.248  33.367  1.00 46.79           C  
ANISOU  193  CG  GLN A  27     5482   5602   6693     54   -481    122       C  
ATOM    194  CD  GLN A  27      46.323  55.030  32.842  1.00 58.17           C  
ANISOU  194  CD  GLN A  27     6821   7027   8254     77   -481    142       C  
ATOM    195  NE2 GLN A  27      47.640  55.169  32.679  1.00 53.67           N  
ANISOU  195  NE2 GLN A  27     6160   6457   7776     64   -533    133       N  
ATOM    196  OE1 GLN A  27      45.734  53.969  32.616  1.00 64.83           O  
ANISOU  196  OE1 GLN A  27     7667   7854   9110    107   -438    168       O  
ATOM    197  N   VAL A  28      41.981  57.218  36.738  1.00 45.00           N  
ANISOU  197  N   VAL A  28     5643   5459   5997    157   -439    195       N  
ATOM    198  CA  VAL A  28      40.805  56.802  37.474  1.00 43.90           C  
ANISOU  198  CA  VAL A  28     5567   5357   5757    202   -379    256       C  
ATOM    199  C   VAL A  28      39.583  56.727  36.572  1.00 46.88           C  
ANISOU  199  C   VAL A  28     5909   5746   6157    201   -261    268       C  
ATOM    200  O   VAL A  28      39.079  57.752  36.131  1.00 50.49           O  
ANISOU  200  O   VAL A  28     6391   6210   6582    204   -216    221       O  
ATOM    201  CB  VAL A  28      40.469  57.749  38.616  1.00 43.18           C  
ANISOU  201  CB  VAL A  28     5606   5293   5507    245   -399    239       C  
ATOM    202  CG1 VAL A  28      39.156  57.314  39.264  1.00 32.62           C  
ANISOU  202  CG1 VAL A  28     4318   4008   4069    298   -305    313       C  
ATOM    203  CG2 VAL A  28      41.619  57.831  39.616  1.00 40.95           C  
ANISOU  203  CG2 VAL A  28     5376   4999   5185    247   -536    227       C  
ATOM    204  N   ARG A  29      39.087  55.515  36.344  1.00 43.29           N  
ANISOU  204  N   ARG A  29     5400   5290   5759    197   -221    334       N  
ATOM    205  CA  ARG A  29      37.904  55.305  35.528  1.00 37.72           C  
ANISOU  205  CA  ARG A  29     4654   4595   5085    188   -128    354       C  
ATOM    206  C   ARG A  29      36.844  54.589  36.350  1.00 39.30           C  
ANISOU  206  C   ARG A  29     4872   4830   5229    211    -77    454       C  
ATOM    207  O   ARG A  29      37.162  53.956  37.355  1.00 40.95           O  
ANISOU  207  O   ARG A  29     5115   5043   5400    228   -115    513       O  
ATOM    208  CB  ARG A  29      38.248  54.508  34.270  1.00 47.75           C  
ANISOU  208  CB  ARG A  29     5835   5817   6492    148   -129    337       C  
ATOM    209  CG  ARG A  29      39.238  55.206  33.338  1.00 64.63           C  
ANISOU  209  CG  ARG A  29     7941   7929   8686    126   -156    252       C  
ATOM    210  CD  ARG A  29      38.760  56.628  33.041  1.00 82.55           C  
ANISOU  210  CD  ARG A  29    10251  10221  10892    128   -117    202       C  
ATOM    211  NE  ARG A  29      39.448  57.243  31.909  1.00 99.78           N  
ANISOU  211  NE  ARG A  29    12397  12379  13136     98   -118    136       N  
ATOM    212  CZ  ARG A  29      40.519  58.029  32.012  1.00105.52           C  
ANISOU  212  CZ  ARG A  29    13130  13092  13871     80   -171     94       C  
ATOM    213  NH1 ARG A  29      41.036  58.303  33.204  1.00 98.03           N1+
ANISOU  213  NH1 ARG A  29    12232  12148  12869     91   -242     99       N1+
ATOM    214  NH2 ARG A  29      41.072  58.548  30.920  1.00112.71           N  
ANISOU  214  NH2 ARG A  29    13999  13984  14841     49   -156     51       N  
ATOM    215  N   GLN A  30      35.583  54.720  35.947  1.00 36.92           N  
ANISOU  215  N   GLN A  30     4547   4558   4923    213     10    480       N  
ATOM    216  CA  GLN A  30      34.515  53.922  36.554  1.00 45.58           C  
ANISOU  216  CA  GLN A  30     5630   5689   5998    221     69    591       C  
ATOM    217  C   GLN A  30      34.836  52.423  36.455  1.00 46.07           C  
ANISOU  217  C   GLN A  30     5644   5698   6163    180     27    654       C  
ATOM    218  O   GLN A  30      35.255  51.933  35.411  1.00 57.45           O  
ANISOU  218  O   GLN A  30     7031   7080   7718    141     -7    612       O  
ATOM    219  CB  GLN A  30      33.166  54.224  35.885  1.00 41.73           C  
ANISOU  219  CB  GLN A  30     5090   5235   5529    217    156    608       C  
ATOM    220  CG  GLN A  30      32.698  55.642  36.091  1.00 49.01           C  
ANISOU  220  CG  GLN A  30     6066   6209   6347    274    207    561       C  
ATOM    221  CD  GLN A  30      31.426  55.980  35.339  1.00 53.48           C  
ANISOU  221  CD  GLN A  30     6568   6807   6944    276    283    576       C  
ATOM    222  NE2 GLN A  30      31.040  57.244  35.393  1.00 56.07           N  
ANISOU  222  NE2 GLN A  30     6942   7169   7194    334    324    528       N  
ATOM    223  OE1 GLN A  30      30.796  55.126  34.726  1.00 54.49           O  
ANISOU  223  OE1 GLN A  30     6610   6925   7168    229    297    630       O  
ATOM    224  N   SER A  31      34.656  51.701  37.547  1.00 49.23           N  
ANISOU  224  N   SER A  31     6073   6114   6516    194     30    755       N  
ATOM    225  CA  SER A  31      34.870  50.267  37.541  1.00 46.07           C  
ANISOU  225  CA  SER A  31     5637   5653   6213    158    -10    828       C  
ATOM    226  C   SER A  31      33.996  49.552  36.512  1.00 52.48           C  
ANISOU  226  C   SER A  31     6367   6427   7147    100     22    855       C  
ATOM    227  O   SER A  31      32.815  49.854  36.379  1.00 47.20           O  
ANISOU  227  O   SER A  31     5666   5806   6463     92     98    892       O  
ATOM    228  CB  SER A  31      34.603  49.700  38.920  1.00 44.34           C  
ANISOU  228  CB  SER A  31     5470   5468   5910    182      4    951       C  
ATOM    229  OG  SER A  31      35.528  50.238  39.840  1.00 65.39           O  
ANISOU  229  OG  SER A  31     8221   8157   8466    233    -53    920       O  
ATOM    230  N   ALA A  32      34.591  48.594  35.803  1.00 57.92           N  
ANISOU  230  N   ALA A  32     7024   7026   7957     66    -41    835       N  
ATOM    231  CA  ALA A  32      33.891  47.804  34.789  1.00 56.58           C  
ANISOU  231  CA  ALA A  32     6792   6798   7907      9    -37    847       C  
ATOM    232  C   ALA A  32      32.932  46.802  35.420  1.00 63.94           C  
ANISOU  232  C   ALA A  32     7704   7720   8870    -30    -13    992       C  
ATOM    233  O   ALA A  32      31.862  46.516  34.883  1.00 60.40           O  
ANISOU  233  O   ALA A  32     7199   7266   8486    -81     17   1031       O  
ATOM    234  CB  ALA A  32      34.897  47.077  33.904  1.00 34.74           C  
ANISOU  234  CB  ALA A  32     4017   3933   5248      0   -113    774       C  
ATOM    235  N   LYS A  33      33.342  46.271  36.563  1.00 66.17           N  
ANISOU  235  N   LYS A  33     8031   7999   9110     -8    -32   1076       N  
ATOM    236  CA  LYS A  33      32.602  45.232  37.261  1.00 68.38           C  
ANISOU  236  CA  LYS A  33     8301   8262   9420    -46    -12   1231       C  
ATOM    237  C   LYS A  33      32.436  45.635  38.712  1.00 65.14           C  
ANISOU  237  C   LYS A  33     7946   7946   8859      4     43   1323       C  
ATOM    238  O   LYS A  33      33.355  46.201  39.305  1.00 56.30           O  
ANISOU  238  O   LYS A  33     6896   6856   7641     65     11   1272       O  
ATOM    239  CB  LYS A  33      33.324  43.894  37.154  1.00 68.28           C  
ANISOU  239  CB  LYS A  33     8302   8124   9518    -69   -103   1258       C  
ATOM    240  CG  LYS A  33      33.504  43.402  35.721  1.00 75.49           C  
ANISOU  240  CG  LYS A  33     9178   8935  10571   -108   -158   1161       C  
ATOM    241  CD  LYS A  33      32.154  43.082  35.066  1.00 82.09           C  
ANISOU  241  CD  LYS A  33     9950   9754  11487   -187   -127   1206       C  
ATOM    242  CE  LYS A  33      32.298  42.166  33.839  1.00 83.36           C  
ANISOU  242  CE  LYS A  33    10100   9780  11792   -232   -207   1140       C  
ATOM    243  NZ  LYS A  33      32.771  40.771  34.183  1.00 74.68           N1+
ANISOU  243  NZ  LYS A  33     9038   8555  10784   -246   -280   1208       N1+
ATOM    244  N   VAL A  34      31.272  45.342  39.286  1.00 63.90           N  
ANISOU  244  N   VAL A  34     7759   7838   8683    -21    126   1461       N  
ATOM    245  CA  VAL A  34      30.949  45.870  40.600  1.00 62.29           C  
ANISOU  245  CA  VAL A  34     7611   7744   8313     41    205   1543       C  
ATOM    246  C   VAL A  34      31.885  45.301  41.670  1.00 68.62           C  
ANISOU  246  C   VAL A  34     8506   8521   9047     76    144   1602       C  
ATOM    247  O   VAL A  34      32.147  45.948  42.686  1.00 75.40           O  
ANISOU  247  O   VAL A  34     9450   9459   9740    149    165   1608       O  
ATOM    248  CB  VAL A  34      29.487  45.589  40.968  1.00 64.85           C  
ANISOU  248  CB  VAL A  34     7867   8131   8641      7    320   1697       C  
ATOM    249  CG1 VAL A  34      29.319  44.148  41.451  1.00 56.20           C  
ANISOU  249  CG1 VAL A  34     6761   6967   7627    -56    300   1860       C  
ATOM    250  CG2 VAL A  34      28.988  46.608  42.013  1.00 59.51           C  
ANISOU  250  CG2 VAL A  34     7241   7597   7773     96    435   1732       C  
ATOM    251  N   GLN A  35      32.420  44.113  41.408  1.00 70.80           N  
ANISOU  251  N   GLN A  35     8772   8682   9448     31     57   1635       N  
ATOM    252  CA  GLN A  35      33.394  43.463  42.285  1.00 77.58           C  
ANISOU  252  CA  GLN A  35     9710   9498  10268     65    -23   1689       C  
ATOM    253  C   GLN A  35      34.726  44.205  42.314  1.00 77.46           C  
ANISOU  253  C   GLN A  35     9750   9489  10191    130   -109   1549       C  
ATOM    254  O   GLN A  35      35.638  43.852  43.061  1.00 81.07           O  
ANISOU  254  O   GLN A  35    10273   9925  10605    169   -189   1577       O  
ATOM    255  CB  GLN A  35      33.619  42.024  41.826  1.00 81.16           C  
ANISOU  255  CB  GLN A  35    10133   9809  10894      4    -99   1745       C  
ATOM    256  CG  GLN A  35      33.955  41.930  40.350  1.00 84.43           C  
ANISOU  256  CG  GLN A  35    10486  10134  11458    -29   -155   1605       C  
ATOM    257  CD  GLN A  35      34.063  40.508  39.849  1.00 94.94           C  
ANISOU  257  CD  GLN A  35    11800  11315  12958    -83   -227   1651       C  
ATOM    258  NE2 GLN A  35      33.361  40.221  38.760  1.00 94.20           N  
ANISOU  258  NE2 GLN A  35    11643  11164  12986   -151   -220   1617       N  
ATOM    259  OE1 GLN A  35      34.761  39.671  40.431  1.00103.15           O  
ANISOU  259  OE1 GLN A  35    12889  12284  14018    -61   -296   1715       O  
ATOM    260  N   PHE A  36      34.843  45.227  41.481  1.00 73.71           N  
ANISOU  260  N   PHE A  36     9246   9042   9720    137    -99   1405       N  
ATOM    261  CA  PHE A  36      36.057  46.027  41.440  1.00 76.05           C  
ANISOU  261  CA  PHE A  36     9580   9345   9970    186   -176   1276       C  
ATOM    262  C   PHE A  36      35.821  47.381  42.090  1.00 68.06           C  
ANISOU  262  C   PHE A  36     8632   8442   8785    238   -126   1234       C  
ATOM    263  O   PHE A  36      36.741  48.158  42.260  1.00 65.26           O  
ANISOU  263  O   PHE A  36     8322   8100   8372    274   -192   1139       O  
ATOM    264  CB  PHE A  36      36.544  46.203  39.997  1.00 82.17           C  
ANISOU  264  CB  PHE A  36    10284  10060  10879    158   -210   1141       C  
ATOM    265  CG  PHE A  36      37.187  44.971  39.413  1.00 83.98           C  
ANISOU  265  CG  PHE A  36    10475  10173  11261    135   -286   1147       C  
ATOM    266  CD1 PHE A  36      37.056  43.739  40.032  1.00 83.77           C  
ANISOU  266  CD1 PHE A  36    10469  10089  11272    123   -312   1277       C  
ATOM    267  CD2 PHE A  36      37.940  45.057  38.257  1.00 83.48           C  
ANISOU  267  CD2 PHE A  36    10364  10055  11300    133   -327   1025       C  
ATOM    268  CE1 PHE A  36      37.640  42.619  39.499  1.00 87.15           C  
ANISOU  268  CE1 PHE A  36    10873  10397  11842    113   -384   1276       C  
ATOM    269  CE2 PHE A  36      38.536  43.943  37.727  1.00 84.24           C  
ANISOU  269  CE2 PHE A  36    10434  10044  11528    130   -389   1022       C  
ATOM    270  CZ  PHE A  36      38.384  42.720  38.345  1.00 87.98           C  
ANISOU  270  CZ  PHE A  36    10933  10451  12044    121   -422   1144       C  
ATOM    271  N   GLY A  37      34.579  47.664  42.452  1.00 66.78           N  
ANISOU  271  N   GLY A  37     8472   8354   8547    243    -10   1305       N  
ATOM    272  CA  GLY A  37      34.279  48.895  43.146  1.00 60.18           C  
ANISOU  272  CA  GLY A  37     7712   7618   7536    309     46   1270       C  
ATOM    273  C   GLY A  37      33.466  49.874  42.340  1.00 54.82           C  
ANISOU  273  C   GLY A  37     6983   6979   6867    308    130   1195       C  
ATOM    274  O   GLY A  37      32.734  49.509  41.426  1.00 57.44           O  
ANISOU  274  O   GLY A  37     7216   7287   7321    253    175   1213       O  
ATOM    275  N   ASP A  38      33.581  51.140  42.708  1.00 56.51           N  
ANISOU  275  N   ASP A  38     7273   7248   6948    371    143   1110       N  
ATOM    276  CA  ASP A  38      32.917  52.199  41.974  1.00 55.64           C  
ANISOU  276  CA  ASP A  38     7131   7170   6840    382    211   1029       C  
ATOM    277  C   ASP A  38      33.907  52.807  40.981  1.00 48.84           C  
ANISOU  277  C   ASP A  38     6255   6245   6059    355    120    883       C  
ATOM    278  O   ASP A  38      33.554  53.070  39.825  1.00 46.89           O  
ANISOU  278  O   ASP A  38     5931   5977   5908    319    145    830       O  
ATOM    279  CB  ASP A  38      32.365  53.247  42.942  1.00 57.31           C  
ANISOU  279  CB  ASP A  38     7443   7473   6861    476    288   1025       C  
ATOM    280  CG  ASP A  38      31.394  52.646  43.954  1.00 71.65           C  
ANISOU  280  CG  ASP A  38     9271   9366   8588    511    397   1182       C  
ATOM    281  OD1 ASP A  38      30.177  52.647  43.685  1.00 75.60           O  
ANISOU  281  OD1 ASP A  38     9689   9917   9117    511    517   1248       O  
ATOM    282  OD2 ASP A  38      31.843  52.157  45.013  1.00 76.43           O1-
ANISOU  282  OD2 ASP A  38     9961   9983   9096    538    364   1249       O1-
ATOM    283  N   TYR A  39      35.150  52.998  41.428  1.00 39.59           N  
ANISOU  283  N   TYR A  39     5150   5043   4847    368     11    826       N  
ATOM    284  CA  TYR A  39      36.219  53.527  40.565  1.00 42.39           C  
ANISOU  284  CA  TYR A  39     5481   5341   5284    337    -76    703       C  
ATOM    285  C   TYR A  39      37.499  52.746  40.731  1.00 39.20           C  
ANISOU  285  C   TYR A  39     5067   4881   4946    316   -194    707       C  
ATOM    286  O   TYR A  39      37.726  52.163  41.781  1.00 40.64           O  
ANISOU  286  O   TYR A  39     5305   5076   5061    341   -232    782       O  
ATOM    287  CB  TYR A  39      36.502  54.998  40.880  1.00 34.45           C  
ANISOU  287  CB  TYR A  39     4565   4358   4166    379    -98    603       C  
ATOM    288  CG  TYR A  39      35.334  55.877  40.584  1.00 38.57           C  
ANISOU  288  CG  TYR A  39     5094   4924   4637    411     12    583       C  
ATOM    289  CD1 TYR A  39      34.312  56.015  41.496  1.00 41.60           C  
ANISOU  289  CD1 TYR A  39     5536   5380   4889    477    105    651       C  
ATOM    290  CD2 TYR A  39      35.234  56.543  39.374  1.00 40.86           C  
ANISOU  290  CD2 TYR A  39     5328   5187   5011    381     29    505       C  
ATOM    291  CE1 TYR A  39      33.230  56.803  41.222  1.00 46.12           C  
ANISOU  291  CE1 TYR A  39     6103   5996   5424    518    210    637       C  
ATOM    292  CE2 TYR A  39      34.159  57.337  39.097  1.00 39.97           C  
ANISOU  292  CE2 TYR A  39     5219   5112   4858    417    122    492       C  
ATOM    293  CZ  TYR A  39      33.164  57.470  40.027  1.00 41.77           C  
ANISOU  293  CZ  TYR A  39     5497   5411   4964    488    211    556       C  
ATOM    294  OH  TYR A  39      32.074  58.255  39.747  1.00 53.24           O  
ANISOU  294  OH  TYR A  39     6940   6905   6383    536    309    547       O  
ATOM    295  N   GLN A  40      38.356  52.756  39.713  1.00 31.38           N  
ANISOU  295  N   GLN A  40     4006   3834   4081    276   -250    630       N  
ATOM    296  CA  GLN A  40      39.713  52.249  39.899  1.00 44.90           C  
ANISOU  296  CA  GLN A  40     5705   5503   5854    270   -367    620       C  
ATOM    297  C   GLN A  40      40.750  53.150  39.263  1.00 47.45           C  
ANISOU  297  C   GLN A  40     5998   5803   6227    250   -429    509       C  
ATOM    298  O   GLN A  40      40.495  53.786  38.247  1.00 57.55           O  
ANISOU  298  O   GLN A  40     7237   7078   7552    225   -377    444       O  
ATOM    299  CB  GLN A  40      39.857  50.806  39.374  1.00 46.13           C  
ANISOU  299  CB  GLN A  40     5781   5599   6147    245   -376    678       C  
ATOM    300  CG  GLN A  40      39.223  50.477  38.037  1.00 52.39           C  
ANISOU  300  CG  GLN A  40     6494   6359   7054    206   -304    657       C  
ATOM    301  CD  GLN A  40      39.064  48.962  37.835  1.00 67.64           C  
ANISOU  301  CD  GLN A  40     8384   8227   9090    189   -310    735       C  
ATOM    302  NE2 GLN A  40      38.002  48.559  37.141  1.00 74.88           N  
ANISOU  302  NE2 GLN A  40     9264   9129  10060    154   -241    760       N  
ATOM    303  OE1 GLN A  40      39.875  48.173  38.317  1.00 72.06           O  
ANISOU  303  OE1 GLN A  40     8949   8747   9685    206   -386    774       O  
ATOM    304  N   ALA A  41      41.916  53.213  39.896  1.00 49.53           N  
ANISOU  304  N   ALA A  41     6281   6057   6482    258   -546    495       N  
ATOM    305  CA  ALA A  41      43.065  53.890  39.321  1.00 51.79           C  
ANISOU  305  CA  ALA A  41     6514   6318   6846    229   -617    409       C  
ATOM    306  C   ALA A  41      43.892  52.909  38.498  1.00 53.35           C  
ANISOU  306  C   ALA A  41     6593   6469   7208    214   -642    417       C  
ATOM    307  O   ALA A  41      44.381  51.909  39.021  1.00 59.15           O  
ANISOU  307  O   ALA A  41     7314   7185   7975    237   -703    477       O  
ATOM    308  CB  ALA A  41      43.918  54.515  40.413  1.00 47.58           C  
ANISOU  308  CB  ALA A  41     6053   5796   6229    242   -744    389       C  
ATOM    309  N   ASN A  42      44.070  53.217  37.221  1.00 61.32           N  
ANISOU  309  N   ASN A  42     7523   7461   8315    184   -593    356       N  
ATOM    310  CA  ASN A  42      44.661  52.273  36.271  1.00 64.62           C  
ANISOU  310  CA  ASN A  42     7836   7837   8878    183   -584    355       C  
ATOM    311  C   ASN A  42      46.126  52.560  35.887  1.00 58.86           C  
ANISOU  311  C   ASN A  42     7017   7098   8249    173   -652    311       C  
ATOM    312  O   ASN A  42      46.778  51.733  35.264  1.00 51.74           O  
ANISOU  312  O   ASN A  42     6029   6167   7464    192   -652    315       O  
ATOM    313  CB  ASN A  42      43.811  52.263  34.994  1.00 74.69           C  
ANISOU  313  CB  ASN A  42     9084   9102  10193    165   -472    324       C  
ATOM    314  CG  ASN A  42      42.472  51.595  35.183  1.00 85.23           C  
ANISOU  314  CG  ASN A  42    10465  10435  11484    170   -410    383       C  
ATOM    315  ND2 ASN A  42      41.713  51.455  34.099  1.00 87.55           N  
ANISOU  315  ND2 ASN A  42    10732  10714  11818    151   -333    361       N  
ATOM    316  OD1 ASN A  42      42.115  51.220  36.288  1.00 94.93           O  
ANISOU  316  OD1 ASN A  42    11751  11677  12642    188   -434    453       O  
ATOM    317  N   GLY A  43      46.653  53.715  36.279  1.00 57.11           N  
ANISOU  317  N   GLY A  43     6813   6899   7986    147   -712    273       N  
ATOM    318  CA  GLY A  43      47.918  54.159  35.733  1.00 52.38           C  
ANISOU  318  CA  GLY A  43     6111   6296   7495    120   -758    235       C  
ATOM    319  C   GLY A  43      49.160  54.001  36.581  1.00 54.87           C  
ANISOU  319  C   GLY A  43     6383   6612   7852    126   -899    259       C  
ATOM    320  O   GLY A  43      50.134  54.735  36.414  1.00 66.62           O  
ANISOU  320  O   GLY A  43     7802   8107   9405     87   -958    229       O  
ATOM    321  N   MET A  44      49.144  53.032  37.482  1.00 52.62           N  
ANISOU  321  N   MET A  44     6134   6321   7538    172   -958    320       N  
ATOM    322  CA  MET A  44      50.253  52.843  38.394  1.00 56.66           C  
ANISOU  322  CA  MET A  44     6616   6835   8076    185  -1108    351       C  
ATOM    323  C   MET A  44      51.423  52.233  37.682  1.00 62.65           C  
ANISOU  323  C   MET A  44     7213   7580   9011    202  -1126    358       C  
ATOM    324  O   MET A  44      52.563  52.669  37.842  1.00 80.91           O  
ANISOU  324  O   MET A  44     9439   9905  11397    180  -1226    350       O  
ATOM    325  CB  MET A  44      49.847  51.963  39.570  1.00 61.29           C  
ANISOU  325  CB  MET A  44     7299   7419   8571    235  -1163    426       C  
ATOM    326  CG  MET A  44      48.854  52.635  40.514  1.00 72.46           C  
ANISOU  326  CG  MET A  44     8877   8861   9795    231  -1160    427       C  
ATOM    327  SD  MET A  44      49.335  54.301  41.016  1.00 75.80           S  
ANISOU  327  SD  MET A  44     9358   9303  10139    181  -1262    349       S  
ATOM    328  CE  MET A  44      47.793  54.891  41.671  1.00 56.63           C  
ANISOU  328  CE  MET A  44     7116   6902   7498    204  -1178    342       C  
ATOM    329  N   MET A  45      51.132  51.230  36.877  1.00 55.53           N  
ANISOU  329  N   MET A  45     6269   6651   8179    243  -1029    371       N  
ATOM    330  CA  MET A  45      52.167  50.413  36.280  1.00 66.09           C  
ANISOU  330  CA  MET A  45     7467   7970   9674    288  -1036    383       C  
ATOM    331  C   MET A  45      53.099  51.231  35.367  1.00 66.16           C  
ANISOU  331  C   MET A  45     7342   8007   9787    252  -1010    335       C  
ATOM    332  O   MET A  45      54.318  51.016  35.350  1.00 64.96           O  
ANISOU  332  O   MET A  45     7060   7866   9757    274  -1074    354       O  
ATOM    333  CB  MET A  45      51.527  49.263  35.516  1.00 72.44           C  
ANISOU  333  CB  MET A  45     8281   8728  10516    338   -930    390       C  
ATOM    334  CG  MET A  45      52.432  48.069  35.350  1.00 81.87           C  
ANISOU  334  CG  MET A  45     9380   9884  11842    416   -963    422       C  
ATOM    335  SD  MET A  45      51.898  47.080  33.953  1.00171.56           S  
ANISOU  335  SD  MET A  45    20731  21184  23268    464   -821    386       S  
ATOM    336  CE  MET A  45      52.219  48.246  32.624  1.00 57.82           C  
ANISOU  336  CE  MET A  45     6241   6832   8895    422   -714    303       C  
ATOM    337  N   ALA A  46      52.536  52.182  34.629  1.00 48.85           N  
ANISOU  337  N   ALA A  46     5177   5829   7553    197   -917    282       N  
ATOM    338  CA  ALA A  46      53.359  53.036  33.791  1.00 49.17           C  
ANISOU  338  CA  ALA A  46     5101   5897   7684    153   -887    250       C  
ATOM    339  C   ALA A  46      54.410  53.771  34.623  1.00 64.71           C  
ANISOU  339  C   ALA A  46     7011   7886   9690    105  -1036    266       C  
ATOM    340  O   ALA A  46      55.609  53.707  34.316  1.00 74.17           O  
ANISOU  340  O   ALA A  46     8052   9103  11027    108  -1067    285       O  
ATOM    341  CB  ALA A  46      52.496  54.022  33.028  1.00 47.49           C  
ANISOU  341  CB  ALA A  46     4954   5690   7400     99   -781    200       C  
ATOM    342  N   VAL A  47      53.961  54.441  35.688  1.00 59.34           N  
ANISOU  342  N   VAL A  47     6458   7203   8887     66  -1131    260       N  
ATOM    343  CA  VAL A  47      54.866  55.185  36.565  1.00 52.83           C  
ANISOU  343  CA  VAL A  47     5608   6388   8079     14  -1298    266       C  
ATOM    344  C   VAL A  47      55.797  54.271  37.356  1.00 55.37           C  
ANISOU  344  C   VAL A  47     5855   6714   8470     65  -1431    324       C  
ATOM    345  O   VAL A  47      56.956  54.612  37.609  1.00 63.94           O  
ANISOU  345  O   VAL A  47     6824   7814   9657     31  -1551    340       O  
ATOM    346  CB  VAL A  47      54.092  56.073  37.562  1.00 49.59           C  
ANISOU  346  CB  VAL A  47     5381   5966   7496    -23  -1369    236       C  
ATOM    347  CG1 VAL A  47      55.056  57.001  38.291  1.00 52.79           C  
ANISOU  347  CG1 VAL A  47     5765   6368   7925    -91  -1547    225       C  
ATOM    348  CG2 VAL A  47      53.040  56.877  36.842  1.00 37.05           C  
ANISOU  348  CG2 VAL A  47     3876   4369   5832    -54  -1236    186       C  
ATOM    349  N   ALA A  48      55.279  53.117  37.758  1.00 53.57           N  
ANISOU  349  N   ALA A  48     5692   6470   8192    144  -1417    361       N  
ATOM    350  CA  ALA A  48      56.070  52.144  38.500  1.00 61.39           C  
ANISOU  350  CA  ALA A  48     6626   7457   9242    206  -1539    424       C  
ATOM    351  C   ALA A  48      57.302  51.680  37.718  1.00 64.70           C  
ANISOU  351  C   ALA A  48     6831   7888   9864    237  -1529    443       C  
ATOM    352  O   ALA A  48      58.390  51.519  38.285  1.00 59.68           O  
ANISOU  352  O   ALA A  48     6092   7267   9317    250  -1671    484       O  
ATOM    353  CB  ALA A  48      55.210  50.954  38.872  1.00 63.45           C  
ANISOU  353  CB  ALA A  48     6995   7688   9426    281  -1498    467       C  
ATOM    354  N   LYS A  49      57.130  51.457  36.419  1.00 77.09           N  
ANISOU  354  N   LYS A  49     8333   9455  11504    258  -1360    416       N  
ATOM    355  CA  LYS A  49      58.246  51.015  35.581  1.00 81.70           C  
ANISOU  355  CA  LYS A  49     8716  10057  12271    304  -1319    431       C  
ATOM    356  C   LYS A  49      59.326  52.099  35.482  1.00 83.50           C  
ANISOU  356  C   LYS A  49     8797  10331  12600    223  -1386    433       C  
ATOM    357  O   LYS A  49      60.505  51.778  35.355  1.00 85.72           O  
ANISOU  357  O   LYS A  49     8895  10639  13036    257  -1430    473       O  
ATOM    358  CB  LYS A  49      57.764  50.606  34.181  1.00 73.64           C  
ANISOU  358  CB  LYS A  49     7679   9024  11275    346  -1118    393       C  
ATOM    359  N   LYS A  50      58.933  53.374  35.567  1.00 74.01           N  
ANISOU  359  N   LYS A  50     7669   9134  11317    117  -1400    395       N  
ATOM    360  CA  LYS A  50      59.917  54.476  35.535  1.00 55.52           C  
ANISOU  360  CA  LYS A  50     5201   6821   9075     21  -1481    401       C  
ATOM    361  C   LYS A  50      60.490  54.838  36.914  1.00 47.66           C  
ANISOU  361  C   LYS A  50     4224   5822   8063    -24  -1718    424       C  
ATOM    362  O   LYS A  50      61.564  55.414  36.985  1.00 65.23           O  
ANISOU  362  O   LYS A  50     6302   8069  10415    -89  -1820    448       O  
ATOM    363  CB  LYS A  50      59.321  55.733  34.881  1.00 52.83           C  
ANISOU  363  CB  LYS A  50     4926   6474   8673    -75  -1389    350       C  
ATOM    364  CG  LYS A  50      58.934  55.551  33.398  1.00 53.77           C  
ANISOU  364  CG  LYS A  50     5005   6605   8820    -44  -1166    330       C  
ATOM    365  CD  LYS A  50      58.308  56.796  32.737  1.00 49.65           C  
ANISOU  365  CD  LYS A  50     4557   6075   8234   -134  -1078    287       C  
ATOM    366  CE  LYS A  50      58.677  58.112  33.404  1.00 56.26           C  
ANISOU  366  CE  LYS A  50     5411   6895   9069   -254  -1222    283       C  
ATOM    367  NZ  LYS A  50      57.642  59.132  33.038  1.00 60.26           N1+
ANISOU  367  NZ  LYS A  50     6069   7371   9457   -311  -1148    232       N1+
ATOM    368  N   LEU A  51      59.787  54.506  37.995  1.00 54.51           N  
ANISOU  368  N   LEU A  51     5272   6663   8776      8  -1806    421       N  
ATOM    369  CA  LEU A  51      60.306  54.721  39.343  1.00 62.50           C  
ANISOU  369  CA  LEU A  51     6325   7672   9750    -17  -2037    443       C  
ATOM    370  C   LEU A  51      61.161  53.556  39.819  1.00 70.72           C  
ANISOU  370  C   LEU A  51     7252   8726  10890     71  -2139    514       C  
ATOM    371  O   LEU A  51      61.658  53.567  40.949  1.00 75.81           O  
ANISOU  371  O   LEU A  51     7923   9372  11508     65  -2344    543       O  
ATOM    372  CB  LEU A  51      59.163  54.966  40.332  1.00 59.15           C  
ANISOU  372  CB  LEU A  51     6159   7222   9095    -16  -2082    411       C  
ATOM    373  CG  LEU A  51      58.645  56.406  40.307  1.00 60.21           C  
ANISOU  373  CG  LEU A  51     6407   7337   9134   -115  -2079    340       C  
ATOM    374  CD1 LEU A  51      57.414  56.581  41.151  1.00 51.60           C  
ANISOU  374  CD1 LEU A  51     5566   6228   7812    -91  -2079    307       C  
ATOM    375  CD2 LEU A  51      59.744  57.340  40.774  1.00 44.54           C  
ANISOU  375  CD2 LEU A  51     4345   5349   7231   -211  -2276    334       C  
ATOM    376  N   GLY A  52      61.328  52.555  38.958  1.00 70.24           N  
ANISOU  376  N   GLY A  52     7077   8673  10940    159  -2002    541       N  
ATOM    377  CA  GLY A  52      62.136  51.387  39.289  1.00 77.84           C  
ANISOU  377  CA  GLY A  52     7925   9640  12013    261  -2081    610       C  
ATOM    378  C   GLY A  52      61.434  50.461  40.266  1.00 72.39           C  
ANISOU  378  C   GLY A  52     7411   8911  11181    336  -2142    641       C  
ATOM    379  O   GLY A  52      62.075  49.793  41.073  1.00 56.97           O  
ANISOU  379  O   GLY A  52     5423   6957   9266    394  -2292    703       O  
ATOM    380  N   MET A  53      60.107  50.414  40.147  1.00 75.64           N  
ANISOU  380  N   MET A  53     8008   9295  11437    336  -2018    606       N  
ATOM    381  CA  MET A  53      59.214  49.849  41.155  1.00 71.73           C  
ANISOU  381  CA  MET A  53     7713   8770  10770    376  -2063    636       C  
ATOM    382  C   MET A  53      58.303  48.740  40.629  1.00 72.31           C  
ANISOU  382  C   MET A  53     7852   8800  10821    452  -1904    651       C  
ATOM    383  O   MET A  53      57.980  48.678  39.434  1.00 68.93           O  
ANISOU  383  O   MET A  53     7374   8363  10452    455  -1735    609       O  
ATOM    384  CB  MET A  53      58.322  50.957  41.724  1.00 59.12           C  
ANISOU  384  CB  MET A  53     6301   7181   8982    295  -2080    586       C  
ATOM    385  CG  MET A  53      58.662  51.411  43.109  1.00 54.12           C  
ANISOU  385  CG  MET A  53     5760   6559   8242    270  -2295    603       C  
ATOM    386  SD  MET A  53      57.619  52.791  43.562  1.00100.99           S  
ANISOU  386  SD  MET A  53    11910  12499  13963    188  -2282    525       S  
ATOM    387  CE  MET A  53      58.308  53.225  45.133  1.00 52.30           C  
ANISOU  387  CE  MET A  53     5834   6342   7696    171  -2563    539       C  
ATOM    388  N   ALA A  54      57.854  47.889  41.545  1.00 62.80           N  
ANISOU  388  N   ALA A  54     6773   7567   9524    508  -1963    713       N  
ATOM    389  CA  ALA A  54      56.777  46.957  41.246  1.00 54.24           C  
ANISOU  389  CA  ALA A  54     5789   6432   8388    554  -1830    733       C  
ATOM    390  C   ALA A  54      55.448  47.704  41.247  1.00 56.20           C  
ANISOU  390  C   ALA A  54     6192   6693   8469    487  -1729    689       C  
ATOM    391  O   ALA A  54      55.231  48.591  42.079  1.00 59.93           O  
ANISOU  391  O   ALA A  54     6764   7199   8806    438  -1807    677       O  
ATOM    392  CB  ALA A  54      56.760  45.818  42.260  1.00 56.09           C  
ANISOU  392  CB  ALA A  54     6101   6628   8583    629  -1930    830       C  
ATOM    393  N   PRO A  55      54.549  47.351  40.316  1.00 58.79           N  
ANISOU  393  N   PRO A  55     6544   6991   8804    491  -1561    663       N  
ATOM    394  CA  PRO A  55      53.275  48.071  40.223  1.00 56.34           C  
ANISOU  394  CA  PRO A  55     6359   6696   8350    432  -1458    625       C  
ATOM    395  C   PRO A  55      52.562  48.104  41.573  1.00 56.35           C  
ANISOU  395  C   PRO A  55     6528   6711   8170    432  -1524    680       C  
ATOM    396  O   PRO A  55      52.125  49.191  42.002  1.00 46.36           O  
ANISOU  396  O   PRO A  55     5352   5485   6776    383  -1532    641       O  
ATOM    397  CB  PRO A  55      52.481  47.258  39.196  1.00 54.26           C  
ANISOU  397  CB  PRO A  55     6095   6386   8137    456  -1304    618       C  
ATOM    398  CG  PRO A  55      53.525  46.562  38.391  1.00 61.84           C  
ANISOU  398  CG  PRO A  55     6903   7316   9277    513  -1302    610       C  
ATOM    399  CD  PRO A  55      54.644  46.257  39.335  1.00 61.01           C  
ANISOU  399  CD  PRO A  55     6744   7218   9218    555  -1466    668       C  
ATOM    400  N   ARG A  56      52.482  46.936  42.223  1.00 53.12           N  
ANISOU  400  N   ARG A  56     6165   6267   7753    491  -1568    770       N  
ATOM    401  CA  ARG A  56      51.850  46.793  43.533  1.00 47.97           C  
ANISOU  401  CA  ARG A  56     5671   5629   6926    503  -1623    843       C  
ATOM    402  C   ARG A  56      52.585  47.642  44.546  1.00 52.32           C  
ANISOU  402  C   ARG A  56     6261   6228   7390    490  -1787    831       C  
ATOM    403  O   ARG A  56      51.965  48.361  45.354  1.00 49.45           O  
ANISOU  403  O   ARG A  56     6039   5904   6845    470  -1801    824       O  
ATOM    404  CB  ARG A  56      51.819  45.327  43.991  1.00 51.29           C  
ANISOU  404  CB  ARG A  56     6118   5993   7377    568  -1654    955       C  
ATOM    405  CG  ARG A  56      50.852  44.443  43.196  1.00 58.24           C  
ANISOU  405  CG  ARG A  56     7004   6812   8311    571  -1505    978       C  
ATOM    406  CD  ARG A  56      50.798  42.989  43.692  1.00 59.88           C  
ANISOU  406  CD  ARG A  56     7251   6946   8554    628  -1544   1096       C  
ATOM    407  NE  ARG A  56      49.916  42.768  44.842  1.00 70.56           N  
ANISOU  407  NE  ARG A  56     8756   8316   9738    624  -1547   1199       N  
ATOM    408  CZ  ARG A  56      48.580  42.741  44.781  1.00 74.23           C  
ANISOU  408  CZ  ARG A  56     9298   8784  10120    584  -1418   1228       C  
ATOM    409  NH1 ARG A  56      47.953  42.971  43.632  1.00 61.97           N1+
ANISOU  409  NH1 ARG A  56     7694   7219   8633    541  -1290   1153       N1+
ATOM    410  NH2 ARG A  56      47.859  42.509  45.875  1.00 76.42           N  
ANISOU  410  NH2 ARG A  56     9704   9086  10246    587  -1415   1335       N  
ATOM    411  N   GLN A  57      53.910  47.589  44.471  1.00 54.05           N  
ANISOU  411  N   GLN A  57     6350   6444   7742    504  -1911    825       N  
ATOM    412  CA  GLN A  57      54.764  48.312  45.412  1.00 61.94           C  
ANISOU  412  CA  GLN A  57     7366   7481   8687    487  -2100    816       C  
ATOM    413  C   GLN A  57      54.495  49.825  45.445  1.00 65.93           C  
ANISOU  413  C   GLN A  57     7935   8024   9091    410  -2099    722       C  
ATOM    414  O   GLN A  57      54.255  50.398  46.514  1.00 61.73           O  
ANISOU  414  O   GLN A  57     7554   7518   8384    403  -2191    719       O  
ATOM    415  CB  GLN A  57      56.222  48.058  45.080  1.00 44.76           C  
ANISOU  415  CB  GLN A  57     4998   5298   6710    505  -2213    821       C  
ATOM    416  CG  GLN A  57      57.167  48.812  45.962  1.00 54.75           C  
ANISOU  416  CG  GLN A  57     6258   6598   7946    475  -2425    811       C  
ATOM    417  CD  GLN A  57      58.592  48.600  45.546  1.00 61.66           C  
ANISOU  417  CD  GLN A  57     6912   7475   9041    487  -2525    823       C  
ATOM    418  NE2 GLN A  57      59.522  48.914  46.433  1.00 55.46           N  
ANISOU  418  NE2 GLN A  57     6105   6712   8254    477  -2744    843       N  
ATOM    419  OE1 GLN A  57      58.858  48.158  44.426  1.00 72.40           O  
ANISOU  419  OE1 GLN A  57     8120   8819  10570    510  -2406    813       O  
ATOM    420  N   LEU A  58      54.548  50.456  44.273  1.00 62.72           N  
ANISOU  420  N   LEU A  58     7422   7617   8792    358  -1996    646       N  
ATOM    421  CA  LEU A  58      54.171  51.858  44.122  1.00 59.56           C  
ANISOU  421  CA  LEU A  58     7083   7236   8311    286  -1968    558       C  
ATOM    422  C   LEU A  58      52.766  52.119  44.638  1.00 62.61           C  
ANISOU  422  C   LEU A  58     7665   7634   8489    297  -1877    555       C  
ATOM    423  O   LEU A  58      52.551  52.968  45.511  1.00 64.50           O  
ANISOU  423  O   LEU A  58     8044   7894   8571    283  -1953    523       O  
ATOM    424  CB  LEU A  58      54.239  52.276  42.658  1.00 60.59           C  
ANISOU  424  CB  LEU A  58     7078   7359   8585    241  -1834    498       C  
ATOM    425  CG  LEU A  58      53.516  53.588  42.362  1.00 63.96           C  
ANISOU  425  CG  LEU A  58     7590   7794   8919    177  -1761    417       C  
ATOM    426  CD1 LEU A  58      54.324  54.773  42.883  1.00 56.46           C  
ANISOU  426  CD1 LEU A  58     6647   6848   7958    112  -1923    368       C  
ATOM    427  CD2 LEU A  58      53.238  53.717  40.884  1.00 70.80           C  
ANISOU  427  CD2 LEU A  58     8355   8652   9894    152  -1590    378       C  
ATOM    428  N   ALA A  59      51.816  51.385  44.062  1.00 55.90           N  
ANISOU  428  N   ALA A  59     6821   6772   7646    324  -1712    586       N  
ATOM    429  CA  ALA A  59      50.417  51.456  44.447  1.00 47.67           C  
ANISOU  429  CA  ALA A  59     5932   5747   6434    339  -1600    603       C  
ATOM    430  C   ALA A  59      50.256  51.375  45.948  1.00 50.42           C  
ANISOU  430  C   ALA A  59     6440   6122   6596    381  -1703    658       C  
ATOM    431  O   ALA A  59      49.445  52.076  46.531  1.00 55.17           O  
ANISOU  431  O   ALA A  59     7187   6755   7022    386  -1667    636       O  
ATOM    432  CB  ALA A  59      49.646  50.359  43.790  1.00 38.42           C  
ANISOU  432  CB  ALA A  59     4725   4550   5325    364  -1457    658       C  
ATOM    433  N   GLU A  60      51.038  50.514  46.579  1.00 54.04           N  
ANISOU  433  N   GLU A  60     6876   6568   7088    419  -1830    732       N  
ATOM    434  CA  GLU A  60      50.951  50.386  48.018  1.00 59.34           C  
ANISOU  434  CA  GLU A  60     7706   7266   7573    464  -1938    792       C  
ATOM    435  C   GLU A  60      51.464  51.650  48.664  1.00 56.77           C  
ANISOU  435  C   GLU A  60     7462   6966   7144    436  -2081    709       C  
ATOM    436  O   GLU A  60      50.845  52.181  49.583  1.00 54.14           O  
ANISOU  436  O   GLU A  60     7309   6665   6596    460  -2090    701       O  
ATOM    437  CB  GLU A  60      51.743  49.183  48.518  1.00 74.71           C  
ANISOU  437  CB  GLU A  60     9609   9190   9589    514  -2058    894       C  
ATOM    438  CG  GLU A  60      51.241  48.652  49.846  1.00 94.04           C  
ANISOU  438  CG  GLU A  60    12232  11661  11837    572  -2098    996       C  
ATOM    439  CD  GLU A  60      50.001  47.794  49.689  1.00113.09           C  
ANISOU  439  CD  GLU A  60    14690  14065  14217    593  -1915   1084       C  
ATOM    440  OE1 GLU A  60      49.901  47.085  48.664  1.00118.57           O  
ANISOU  440  OE1 GLU A  60    15257  14708  15086    581  -1820   1096       O  
ATOM    441  OE2 GLU A  60      49.130  47.824  50.587  1.00119.76           O1-
ANISOU  441  OE2 GLU A  60    15695  14949  14859    622  -1868   1142       O1-
ATOM    442  N   GLN A  61      52.607  52.133  48.187  1.00 56.71           N  
ANISOU  442  N   GLN A  61     7320   6939   7287    387  -2193    649       N  
ATOM    443  CA  GLN A  61      53.132  53.376  48.714  1.00 54.02           C  
ANISOU  443  CA  GLN A  61     7046   6606   6872    344  -2343    565       C  
ATOM    444  C   GLN A  61      52.132  54.487  48.430  1.00 50.58           C  
ANISOU  444  C   GLN A  61     6717   6176   6325    316  -2216    478       C  
ATOM    445  O   GLN A  61      51.819  55.277  49.315  1.00 55.72           O  
ANISOU  445  O   GLN A  61     7546   6840   6786    328  -2280    433       O  
ATOM    446  CB  GLN A  61      54.496  53.717  48.133  1.00 64.54           C  
ANISOU  446  CB  GLN A  61     8190   7917   8415    281  -2470    527       C  
ATOM    447  CG  GLN A  61      55.068  54.979  48.772  1.00 85.95           C  
ANISOU  447  CG  GLN A  61    10979  10624  11054    224  -2654    446       C  
ATOM    448  CD  GLN A  61      56.461  55.322  48.293  1.00 94.97           C  
ANISOU  448  CD  GLN A  61    11922  11748  12413    152  -2796    424       C  
ATOM    449  NE2 GLN A  61      56.935  56.523  48.642  1.00 82.54           N  
ANISOU  449  NE2 GLN A  61    10397  10155  10810     78  -2947    346       N  
ATOM    450  OE1 GLN A  61      57.099  54.528  47.602  1.00104.03           O  
ANISOU  450  OE1 GLN A  61    12872  12897  13756    162  -2767    478       O  
ATOM    451  N   VAL A  62      51.589  54.516  47.219  1.00 47.13           N  
ANISOU  451  N   VAL A  62     6183   5728   5997    290  -2036    455       N  
ATOM    452  CA  VAL A  62      50.560  55.497  46.889  1.00 50.94           C  
ANISOU  452  CA  VAL A  62     6757   6215   6382    274  -1905    383       C  
ATOM    453  C   VAL A  62      49.436  55.483  47.930  1.00 47.27           C  
ANISOU  453  C   VAL A  62     6500   5788   5674    343  -1849    413       C  
ATOM    454  O   VAL A  62      48.998  56.527  48.400  1.00 50.09           O  
ANISOU  454  O   VAL A  62     7002   6152   5880    351  -1858    343       O  
ATOM    455  CB  VAL A  62      49.958  55.247  45.470  1.00 66.86           C  
ANISOU  455  CB  VAL A  62     8648   8221   8534    252  -1706    380       C  
ATOM    456  CG1 VAL A  62      48.727  56.104  45.248  1.00 54.68           C  
ANISOU  456  CG1 VAL A  62     7211   6689   6874    254  -1565    327       C  
ATOM    457  CG2 VAL A  62      51.001  55.490  44.372  1.00 64.63           C  
ANISOU  457  CG2 VAL A  62     8176   7910   8469    186  -1735    339       C  
ATOM    458  N   LEU A  63      49.008  54.290  48.322  1.00 50.32           N  
ANISOU  458  N   LEU A  63     6901   6195   6023    399  -1795    521       N  
ATOM    459  CA  LEU A  63      47.834  54.139  49.171  1.00 48.22           C  
ANISOU  459  CA  LEU A  63     6804   5974   5544    465  -1699    573       C  
ATOM    460  C   LEU A  63      48.077  54.616  50.591  1.00 56.92           C  
ANISOU  460  C   LEU A  63     8097   7102   6428    511  -1845    561       C  
ATOM    461  O   LEU A  63      47.145  54.718  51.386  1.00 68.80           O  
ANISOU  461  O   LEU A  63     9764   8653   7724    575  -1768    590       O  
ATOM    462  CB  LEU A  63      47.377  52.689  49.180  1.00 47.44           C  
ANISOU  462  CB  LEU A  63     6661   5882   5483    499  -1610    706       C  
ATOM    463  CG  LEU A  63      45.868  52.581  49.337  1.00 62.05           C  
ANISOU  463  CG  LEU A  63     8599   7774   7202    537  -1418    757       C  
ATOM    464  CD1 LEU A  63      45.227  52.815  47.996  1.00 74.08           C  
ANISOU  464  CD1 LEU A  63    10006   9280   8860    492  -1262    710       C  
ATOM    465  CD2 LEU A  63      45.452  51.230  49.873  1.00 68.74           C  
ANISOU  465  CD2 LEU A  63     9465   8632   8021    576  -1373    907       C  
ATOM    466  N   THR A  64      49.325  54.942  50.898  1.00 45.38           N  
ANISOU  466  N   THR A  64     6615   5614   5013    479  -2056    517       N  
ATOM    467  CA  THR A  64      49.664  55.533  52.183  1.00 54.87           C  
ANISOU  467  CA  THR A  64     8005   6831   6013    513  -2228    483       C  
ATOM    468  C   THR A  64      49.524  57.074  52.161  1.00 64.39           C  
ANISOU  468  C   THR A  64     9315   8015   7136    485  -2256    341       C  
ATOM    469  O   THR A  64      49.134  57.698  53.151  1.00 72.72           O  
ANISOU  469  O   THR A  64    10585   9089   7958    540  -2298    299       O  
ATOM    470  CB  THR A  64      51.092  55.127  52.598  1.00 60.03           C  
ANISOU  470  CB  THR A  64     8589   7463   6757    490  -2469    509       C  
ATOM    471  CG2 THR A  64      51.293  53.618  52.385  1.00 57.16           C  
ANISOU  471  CG2 THR A  64     8095   7102   6521    517  -2434    642       C  
ATOM    472  OG1 THR A  64      52.045  55.843  51.806  1.00 71.76           O  
ANISOU  472  OG1 THR A  64     9926   8902   8436    400  -2566    422       O  
ATOM    473  N   HIS A  65      49.822  57.682  51.023  1.00 65.54           N  
ANISOU  473  N   HIS A  65     9318   8116   7468    404  -2227    269       N  
ATOM    474  CA  HIS A  65      49.670  59.126  50.868  1.00 62.75           C  
ANISOU  474  CA  HIS A  65     9052   7726   7064    371  -2244    141       C  
ATOM    475  C   HIS A  65      48.225  59.488  50.511  1.00 62.60           C  
ANISOU  475  C   HIS A  65     9107   7730   6948    419  -2012    123       C  
ATOM    476  O   HIS A  65      47.871  60.652  50.411  1.00 66.54           O  
ANISOU  476  O   HIS A  65     9701   8199   7383    414  -1995     24       O  
ATOM    477  CB  HIS A  65      50.624  59.646  49.793  1.00 55.22           C  
ANISOU  477  CB  HIS A  65     7911   6715   6355    260  -2311     86       C  
ATOM    478  CG  HIS A  65      52.056  59.283  50.025  1.00 60.91           C  
ANISOU  478  CG  HIS A  65     8519   7420   7206    209  -2527    113       C  
ATOM    479  CD2 HIS A  65      52.905  58.503  49.310  1.00 46.26           C  
ANISOU  479  CD2 HIS A  65     6436   5564   5579    168  -2545    174       C  
ATOM    480  ND1 HIS A  65      52.787  59.767  51.092  1.00 65.06           N  
ANISOU  480  ND1 HIS A  65     9164   7927   7629    201  -2766     72       N  
ATOM    481  CE1 HIS A  65      54.015  59.284  51.037  1.00 62.62           C  
ANISOU  481  CE1 HIS A  65     8695   7611   7488    153  -2925    116       C  
ATOM    482  NE2 HIS A  65      54.111  58.514  49.963  1.00 57.08           N  
ANISOU  482  NE2 HIS A  65     7779   6922   6989    138  -2788    178       N  
ATOM    483  N   LEU A  66      47.389  58.474  50.347  1.00 62.40           N  
ANISOU  483  N   LEU A  66     9038   7754   6916    468  -1840    225       N  
ATOM    484  CA  LEU A  66      46.036  58.672  49.864  1.00 59.57           C  
ANISOU  484  CA  LEU A  66     8701   7423   6509    505  -1616    226       C  
ATOM    485  C   LEU A  66      44.985  58.777  50.989  1.00 73.82           C  
ANISOU  485  C   LEU A  66    10715   9289   8045    614  -1535    252       C  
ATOM    486  O   LEU A  66      44.650  57.796  51.646  1.00 66.29           O  
ANISOU  486  O   LEU A  66     9795   8388   7006    667  -1493    363       O  
ATOM    487  CB  LEU A  66      45.695  57.529  48.919  1.00 48.84           C  
ANISOU  487  CB  LEU A  66     7160   6077   5321    483  -1474    321       C  
ATOM    488  CG  LEU A  66      44.507  57.780  48.031  1.00 45.99           C  
ANISOU  488  CG  LEU A  66     6757   5729   4989    487  -1266    312       C  
ATOM    489  CD1 LEU A  66      44.761  59.069  47.263  1.00 39.61           C  
ANISOU  489  CD1 LEU A  66     5929   4870   4250    433  -1288    189       C  
ATOM    490  CD2 LEU A  66      44.291  56.573  47.104  1.00 39.26           C  
ANISOU  490  CD2 LEU A  66     5730   4876   4311    457  -1160    400       C  
ATOM    491  N   ASP A  67      44.458  59.979  51.193  1.00 92.38           N  
ANISOU  491  N   ASP A  67    13205  11631  10264    651  -1505    152       N  
ATOM    492  CA  ASP A  67      43.442  60.217  52.217  1.00107.32           C  
ANISOU  492  CA  ASP A  67    15300  13585  11892    769  -1411    164       C  
ATOM    493  C   ASP A  67      42.028  60.102  51.651  1.00105.63           C  
ANISOU  493  C   ASP A  67    15034  13421  11679    812  -1156    212       C  
ATOM    494  O   ASP A  67      41.519  61.050  51.049  1.00115.48           O  
ANISOU  494  O   ASP A  67    16286  14644  12948    815  -1079    129       O  
ATOM    495  CB  ASP A  67      43.650  61.602  52.845  1.00122.79           C  
ANISOU  495  CB  ASP A  67    17462  15501  13690    803  -1529     20       C  
ATOM    496  CG  ASP A  67      42.537  61.992  53.807  1.00134.24           C  
ANISOU  496  CG  ASP A  67    19129  17016  14862    943  -1408     14       C  
ATOM    497  OD1 ASP A  67      42.555  61.527  54.969  1.00139.42           O  
ANISOU  497  OD1 ASP A  67    19926  17725  15323   1017  -1452     69       O  
ATOM    498  OD2 ASP A  67      41.656  62.786  53.404  1.00137.51           O1-
ANISOU  498  OD2 ASP A  67    19574  17426  15246    986  -1269    -45       O1-
ATOM    499  N   LEU A  68      41.390  58.949  51.849  1.00 89.05           N  
ANISOU  499  N   LEU A  68    12884  11388   9564    844  -1032    353       N  
ATOM    500  CA  LEU A  68      40.045  58.725  51.308  1.00 77.22           C  
ANISOU  500  CA  LEU A  68    11311   9940   8088    874   -799    416       C  
ATOM    501  C   LEU A  68      38.958  58.405  52.342  1.00 78.02           C  
ANISOU  501  C   LEU A  68    11536  10138   7968    987   -654    514       C  
ATOM    502  O   LEU A  68      37.912  57.851  51.980  1.00 80.53           O  
ANISOU  502  O   LEU A  68    11760  10508   8331    998   -471    613       O  
ATOM    503  CB  LEU A  68      40.072  57.596  50.270  1.00 59.91           C  
ANISOU  503  CB  LEU A  68     8899   7732   6133    788   -744    508       C  
ATOM    504  CG  LEU A  68      40.698  57.977  48.935  1.00 61.56           C  
ANISOU  504  CG  LEU A  68     8958   7864   6566    691   -794    421       C  
ATOM    505  CD1 LEU A  68      40.652  56.818  47.956  1.00 65.59           C  
ANISOU  505  CD1 LEU A  68     9275   8361   7286    625   -732    506       C  
ATOM    506  CD2 LEU A  68      39.998  59.194  48.369  1.00 62.70           C  
ANISOU  506  CD2 LEU A  68     9129   8000   6693    709   -703    324       C  
ATOM    507  N   ASN A  69      39.180  58.753  53.609  1.00 70.52           N  
ANISOU  507  N   ASN A  69    10795   9217   6783   1070   -734    491       N  
ATOM    508  CA  ASN A  69      38.146  58.553  54.617  1.00 70.64           C  
ANISOU  508  CA  ASN A  69    10941   9334   6566   1191   -583    580       C  
ATOM    509  C   ASN A  69      36.953  59.494  54.376  1.00 64.69           C  
ANISOU  509  C   ASN A  69    10222   8618   5740   1271   -398    526       C  
ATOM    510  O   ASN A  69      37.104  60.643  53.936  1.00 59.43           O  
ANISOU  510  O   ASN A  69     9595   7892   5095   1270   -444    379       O  
ATOM    511  CB  ASN A  69      38.722  58.729  56.024  1.00 85.40           C  
ANISOU  511  CB  ASN A  69    13044  11224   8182   1269   -722    559       C  
ATOM    512  CG  ASN A  69      39.039  60.172  56.349  1.00106.37           C  
ANISOU  512  CG  ASN A  69    15881  13832  10701   1318   -831    376       C  
ATOM    513  ND2 ASN A  69      38.233  60.779  57.218  1.00118.65           N  
ANISOU  513  ND2 ASN A  69    17636  15451  11995   1459   -726    351       N  
ATOM    514  OD1 ASN A  69      40.012  60.730  55.845  1.00108.31           O  
ANISOU  514  OD1 ASN A  69    16094  13982  11076   1233  -1008    261       O  
ATOM    515  N   GLY A  70      35.756  58.977  54.619  1.00 58.87           N  
ANISOU  515  N   GLY A  70     9455   7977   4934   1336   -185    655       N  
ATOM    516  CA  GLY A  70      34.552  59.739  54.372  1.00 60.36           C  
ANISOU  516  CA  GLY A  70     9646   8215   5072   1419      6    627       C  
ATOM    517  C   GLY A  70      34.117  59.648  52.924  1.00 72.04           C  
ANISOU  517  C   GLY A  70    10897   9661   6816   1327     86    633       C  
ATOM    518  O   GLY A  70      32.970  59.947  52.595  1.00 80.92           O  
ANISOU  518  O   GLY A  70    11963  10838   7943   1380    266    659       O  
ATOM    519  N   ILE A  71      35.036  59.230  52.059  1.00 64.44           N  
ANISOU  519  N   ILE A  71     9802   8613   6070   1194    -49    610       N  
ATOM    520  CA  ILE A  71      34.767  59.118  50.629  1.00 60.21           C  
ANISOU  520  CA  ILE A  71     9062   8036   5781   1102      3    606       C  
ATOM    521  C   ILE A  71      34.535  57.676  50.211  1.00 65.71           C  
ANISOU  521  C   ILE A  71     9587   8750   6632   1024     60    759       C  
ATOM    522  O   ILE A  71      33.548  57.357  49.524  1.00 65.57           O  
ANISOU  522  O   ILE A  71     9432   8762   6718   1005    204    828       O  
ATOM    523  CB  ILE A  71      35.932  59.681  49.796  1.00 50.13           C  
ANISOU  523  CB  ILE A  71     7746   6649   4653   1008   -171    472       C  
ATOM    524  CG1 ILE A  71      35.962  61.213  49.872  1.00 49.67           C  
ANISOU  524  CG1 ILE A  71     7825   6552   4495   1066   -207    317       C  
ATOM    525  CG2 ILE A  71      35.840  59.202  48.364  1.00 41.39           C  
ANISOU  525  CG2 ILE A  71     6424   5504   3799    903   -132    495       C  
ATOM    526  CD1 ILE A  71      37.344  61.794  49.679  1.00 43.48           C  
ANISOU  526  CD1 ILE A  71     7078   5666   3775    990   -422    196       C  
ATOM    527  N   ALA A  72      35.455  56.808  50.626  1.00 57.66           N  
ANISOU  527  N   ALA A  72     8575   7702   5630    979    -66    811       N  
ATOM    528  CA  ALA A  72      35.382  55.413  50.247  1.00 50.68           C  
ANISOU  528  CA  ALA A  72     7546   6810   4900    903    -40    948       C  
ATOM    529  C   ALA A  72      35.317  54.484  51.479  1.00 63.18           C  
ANISOU  529  C   ALA A  72     9216   8449   6341    948    -29   1094       C  
ATOM    530  O   ALA A  72      36.175  54.520  52.373  1.00 59.90           O  
ANISOU  530  O   ALA A  72     8935   8026   5797    981   -162   1075       O  
ATOM    531  CB  ALA A  72      36.555  55.068  49.357  1.00 45.93           C  
ANISOU  531  CB  ALA A  72     6837   6109   4503    799   -193    889       C  
ATOM    532  N   SER A  73      34.277  53.657  51.518  1.00 71.62           N  
ANISOU  532  N   SER A  73    10207   9573   7434    946    128   1248       N  
ATOM    533  CA  SER A  73      34.120  52.666  52.569  1.00 77.68           C  
ANISOU  533  CA  SER A  73    11035  10389   8091    975    159   1414       C  
ATOM    534  C   SER A  73      35.351  51.773  52.652  1.00 76.48           C  
ANISOU  534  C   SER A  73    10876  10157   8027    913    -24   1440       C  
ATOM    535  O   SER A  73      35.780  51.418  53.743  1.00 85.40           O  
ANISOU  535  O   SER A  73    12134  11310   9003    961    -90   1506       O  
ATOM    536  CB  SER A  73      32.860  51.824  52.338  1.00 89.92           C  
ANISOU  536  CB  SER A  73    12455  11988   9723    946    345   1583       C  
ATOM    537  OG  SER A  73      32.950  51.070  51.141  1.00 95.88           O  
ANISOU  537  OG  SER A  73    13029  12658  10744    828    313   1599       O  
ATOM    538  N   LYS A  74      35.920  51.417  51.502  1.00 68.33           N  
ANISOU  538  N   LYS A  74     9698   9031   7234    816   -104   1389       N  
ATOM    539  CA  LYS A  74      37.165  50.656  51.480  1.00 64.51           C  
ANISOU  539  CA  LYS A  74     9194   8467   6851    768   -281   1396       C  
ATOM    540  C   LYS A  74      37.898  50.773  50.143  1.00 63.84           C  
ANISOU  540  C   LYS A  74     8970   8291   6997    687   -367   1277       C  
ATOM    541  O   LYS A  74      37.302  50.990  49.096  1.00 66.25           O  
ANISOU  541  O   LYS A  74     9164   8583   7427    645   -276   1237       O  
ATOM    542  CB  LYS A  74      36.898  49.189  51.810  1.00 63.72           C  
ANISOU  542  CB  LYS A  74     9055   8355   6802    742   -247   1584       C  
ATOM    543  CG  LYS A  74      36.579  48.314  50.635  1.00 61.45           C  
ANISOU  543  CG  LYS A  74     8588   7995   6764    649   -202   1629       C  
ATOM    544  CD  LYS A  74      35.909  47.045  51.112  1.00 68.33           C  
ANISOU  544  CD  LYS A  74     9443   8871   7648    631   -123   1832       C  
ATOM    545  CE  LYS A  74      35.607  46.101  49.958  1.00 74.03           C  
ANISOU  545  CE  LYS A  74    10000   9503   8623    533    -99   1874       C  
ATOM    546  NZ  LYS A  74      36.850  45.462  49.441  1.00 77.49           N1+
ANISOU  546  NZ  LYS A  74    10397   9828   9220    498   -264   1823       N1+
ATOM    547  N   VAL A  75      39.213  50.643  50.194  1.00 65.92           N  
ANISOU  547  N   VAL A  75     9240   8495   7312    670   -544   1225       N  
ATOM    548  CA  VAL A  75      40.035  50.872  49.021  1.00 56.93           C  
ANISOU  548  CA  VAL A  75     7979   7281   6370    606   -627   1109       C  
ATOM    549  C   VAL A  75      41.142  49.807  48.995  1.00 64.40           C  
ANISOU  549  C   VAL A  75     8866   8158   7443    579   -765   1157       C  
ATOM    550  O   VAL A  75      42.097  49.846  49.755  1.00 71.28           O  
ANISOU  550  O   VAL A  75     9810   9027   8248    607   -913   1149       O  
ATOM    551  CB  VAL A  75      40.589  52.338  49.001  1.00 45.56           C  
ANISOU  551  CB  VAL A  75     6603   5847   4861    619   -705    948       C  
ATOM    552  CG1 VAL A  75      41.495  52.612  50.158  1.00 50.84           C  
ANISOU  552  CG1 VAL A  75     7409   6526   5382    663   -866    930       C  
ATOM    553  CG2 VAL A  75      41.334  52.610  47.741  1.00 64.50           C  
ANISOU  553  CG2 VAL A  75     8867   8178   7461    550   -762    844       C  
ATOM    554  N   GLU A  76      40.965  48.806  48.142  1.00 62.96           N  
ANISOU  554  N   GLU A  76     8557   7919   7444    531   -719   1213       N  
ATOM    555  CA  GLU A  76      41.883  47.672  48.092  1.00 54.53           C  
ANISOU  555  CA  GLU A  76     7434   6778   6505    519   -830   1270       C  
ATOM    556  C   GLU A  76      42.747  47.674  46.816  1.00 60.24           C  
ANISOU  556  C   GLU A  76     8017   7431   7440    475   -888   1165       C  
ATOM    557  O   GLU A  76      42.370  48.243  45.786  1.00 68.74           O  
ANISOU  557  O   GLU A  76     9023   8504   8590    439   -808   1079       O  
ATOM    558  CB  GLU A  76      41.093  46.362  48.204  1.00 62.70           C  
ANISOU  558  CB  GLU A  76     8451   7786   7586    506   -747   1428       C  
ATOM    559  CG  GLU A  76      40.034  46.135  47.113  1.00 82.02           C  
ANISOU  559  CG  GLU A  76    10796  10212  10157    450   -604   1431       C  
ATOM    560  CD  GLU A  76      39.309  44.784  47.224  1.00 93.55           C  
ANISOU  560  CD  GLU A  76    12234  11628  11684    422   -543   1593       C  
ATOM    561  OE1 GLU A  76      38.716  44.499  48.291  1.00 97.98           O  
ANISOU  561  OE1 GLU A  76    12880  12240  12106    448   -494   1725       O  
ATOM    562  OE2 GLU A  76      39.321  44.015  46.235  1.00 95.25           O1-
ANISOU  562  OE2 GLU A  76    12350  11754  12087    373   -543   1590       O1-
ATOM    563  N   ILE A  77      43.919  47.054  46.891  1.00 53.46           N  
ANISOU  563  N   ILE A  77     7118   6519   6674    486  -1023   1176       N  
ATOM    564  CA  ILE A  77      44.771  46.918  45.722  1.00 48.82           C  
ANISOU  564  CA  ILE A  77     6393   5870   6288    458  -1065   1093       C  
ATOM    565  C   ILE A  77      44.428  45.596  45.010  1.00 55.32           C  
ANISOU  565  C   ILE A  77     7140   6614   7265    444  -1006   1163       C  
ATOM    566  O   ILE A  77      43.949  44.653  45.640  1.00 55.74           O  
ANISOU  566  O   ILE A  77     7246   6647   7286    457   -992   1289       O  
ATOM    567  CB  ILE A  77      46.255  47.007  46.119  1.00 54.08           C  
ANISOU  567  CB  ILE A  77     7036   6523   6987    484  -1242   1063       C  
ATOM    568  CG1 ILE A  77      46.553  48.431  46.583  1.00 63.42           C  
ANISOU  568  CG1 ILE A  77     8286   7768   8044    479  -1302    969       C  
ATOM    569  CG2 ILE A  77      47.178  46.654  44.969  1.00 67.86           C  
ANISOU  569  CG2 ILE A  77     8626   8207   8949    470  -1273   1003       C  
ATOM    570  CD1 ILE A  77      47.949  48.643  47.076  1.00 73.23           C  
ANISOU  570  CD1 ILE A  77     9511   9006   9309    492  -1492    941       C  
ATOM    571  N   ALA A  78      44.635  45.544  43.695  1.00 50.90           N  
ANISOU  571  N   ALA A  78     6468   6008   6866    415   -970   1081       N  
ATOM    572  CA  ALA A  78      44.168  44.426  42.902  1.00 46.50           C  
ANISOU  572  CA  ALA A  78     5855   5370   6444    398   -908   1123       C  
ATOM    573  C   ALA A  78      45.014  44.218  41.654  1.00 63.24           C  
ANISOU  573  C   ALA A  78     7860   7429   8740    400   -928   1029       C  
ATOM    574  O   ALA A  78      45.343  45.176  40.956  1.00 62.21           O  
ANISOU  574  O   ALA A  78     7676   7332   8628    383   -910    919       O  
ATOM    575  CB  ALA A  78      42.717  44.643  42.518  1.00 42.63           C  
ANISOU  575  CB  ALA A  78     5380   4904   5913    352   -767   1136       C  
ATOM    576  N   GLY A  79      45.344  42.956  41.372  1.00 67.47           N  
ANISOU  576  N   GLY A  79     8361   7871   9402    424   -961   1076       N  
ATOM    577  CA  GLY A  79      46.108  42.590  40.193  1.00 54.41           C  
ANISOU  577  CA  GLY A  79     6607   6154   7913    445   -968    994       C  
ATOM    578  C   GLY A  79      47.461  43.265  40.143  1.00 48.51           C  
ANISOU  578  C   GLY A  79     5787   5447   7199    477  -1048    921       C  
ATOM    579  O   GLY A  79      48.107  43.434  41.170  1.00 62.38           O  
ANISOU  579  O   GLY A  79     7569   7237   8897    504  -1152    964       O  
ATOM    580  N   PRO A  80      47.900  43.661  38.944  1.00 54.65           N  
ANISOU  580  N   PRO A  80     6472   6222   8070    474  -1002    816       N  
ATOM    581  CA  PRO A  80      49.177  44.363  38.743  1.00 61.29           C  
ANISOU  581  CA  PRO A  80     7219   7105   8965    493  -1062    749       C  
ATOM    582  C   PRO A  80      49.126  45.881  38.999  1.00 56.86           C  
ANISOU  582  C   PRO A  80     6674   6634   8296    439  -1062    695       C  
ATOM    583  O   PRO A  80      49.374  46.662  38.083  1.00 57.24           O  
ANISOU  583  O   PRO A  80     6654   6706   8387    412  -1010    609       O  
ATOM    584  CB  PRO A  80      49.483  44.094  37.278  1.00 60.43           C  
ANISOU  584  CB  PRO A  80     7015   6955   8990    510   -985    670       C  
ATOM    585  CG  PRO A  80      48.132  43.983  36.653  1.00 67.47           C  
ANISOU  585  CG  PRO A  80     7970   7823   9844    466   -874    656       C  
ATOM    586  CD  PRO A  80      47.260  43.305  37.668  1.00 62.83           C  
ANISOU  586  CD  PRO A  80     7484   7207   9182    455   -897    763       C  
ATOM    587  N   GLY A  81      48.805  46.283  40.224  1.00 52.84           N  
ANISOU  587  N   GLY A  81     6263   6167   7645    428  -1120    744       N  
ATOM    588  CA  GLY A  81      48.951  47.667  40.625  1.00 57.67           C  
ANISOU  588  CA  GLY A  81     6905   6848   8158    391  -1154    690       C  
ATOM    589  C   GLY A  81      47.686  48.505  40.659  1.00 60.32           C  
ANISOU  589  C   GLY A  81     7336   7225   8360    351  -1055    666       C  
ATOM    590  O   GLY A  81      47.744  49.684  41.013  1.00 70.76           O  
ANISOU  590  O   GLY A  81     8701   8594   9592    326  -1083    616       O  
ATOM    591  N   PHE A  82      46.547  47.926  40.286  1.00 50.15           N  
ANISOU  591  N   PHE A  82     6077   5915   7064    345   -945    700       N  
ATOM    592  CA  PHE A  82      45.291  48.669  40.335  1.00 50.14           C  
ANISOU  592  CA  PHE A  82     6151   5957   6942    316   -846    688       C  
ATOM    593  C   PHE A  82      44.919  48.996  41.773  1.00 50.24           C  
ANISOU  593  C   PHE A  82     6288   6020   6780    336   -886    746       C  
ATOM    594  O   PHE A  82      45.204  48.237  42.709  1.00 45.18           O  
ANISOU  594  O   PHE A  82     5690   5369   6105    370   -959    832       O  
ATOM    595  CB  PHE A  82      44.133  47.898  39.693  1.00 51.51           C  
ANISOU  595  CB  PHE A  82     6319   6098   7156    300   -733    727       C  
ATOM    596  CG  PHE A  82      44.415  47.416  38.322  1.00 59.85           C  
ANISOU  596  CG  PHE A  82     7279   7097   8366    290   -697    673       C  
ATOM    597  CD1 PHE A  82      44.357  48.274  37.251  1.00 64.83           C  
ANISOU  597  CD1 PHE A  82     7863   7745   9023    262   -637    579       C  
ATOM    598  CD2 PHE A  82      44.727  46.085  38.095  1.00 72.29           C  
ANISOU  598  CD2 PHE A  82     8820   8595  10052    316   -724    718       C  
ATOM    599  CE1 PHE A  82      44.618  47.818  35.973  1.00 67.97           C  
ANISOU  599  CE1 PHE A  82     8185   8094   9545    262   -599    528       C  
ATOM    600  CE2 PHE A  82      44.983  45.624  36.823  1.00 74.01           C  
ANISOU  600  CE2 PHE A  82     8966   8758  10398    319   -689    659       C  
ATOM    601  CZ  PHE A  82      44.929  46.489  35.760  1.00 71.18           C  
ANISOU  601  CZ  PHE A  82     8565   8427  10054    294   -624    563       C  
ATOM    602  N   ILE A  83      44.287  50.147  41.926  1.00 49.55           N  
ANISOU  602  N   ILE A  83     6266   5986   6577    324   -836    698       N  
ATOM    603  CA  ILE A  83      43.720  50.577  43.186  1.00 49.09           C  
ANISOU  603  CA  ILE A  83     6340   5981   6329    354   -840    739       C  
ATOM    604  C   ILE A  83      42.219  50.555  42.991  1.00 47.48           C  
ANISOU  604  C   ILE A  83     6163   5806   6071    350   -688    778       C  
ATOM    605  O   ILE A  83      41.704  51.172  42.053  1.00 53.93           O  
ANISOU  605  O   ILE A  83     6937   6627   6928    323   -606    712       O  
ATOM    606  CB  ILE A  83      44.210  51.992  43.588  1.00 58.56           C  
ANISOU  606  CB  ILE A  83     7605   7214   7433    354   -912    645       C  
ATOM    607  CG1 ILE A  83      45.730  51.976  43.807  1.00 51.81           C  
ANISOU  607  CG1 ILE A  83     6705   6334   6649    348  -1077    618       C  
ATOM    608  CG2 ILE A  83      43.457  52.502  44.819  1.00 55.81           C  
ANISOU  608  CG2 ILE A  83     7414   6923   6866    400   -893    674       C  
ATOM    609  CD1 ILE A  83      46.267  53.163  44.576  1.00 49.73           C  
ANISOU  609  CD1 ILE A  83     6531   6093   6272    347  -1191    551       C  
ATOM    610  N   ASN A  84      41.509  49.826  43.842  1.00 40.96           N  
ANISOU  610  N   ASN A  84     5399   5001   5161    376   -650    893       N  
ATOM    611  CA  ASN A  84      40.064  49.704  43.662  1.00 41.42           C  
ANISOU  611  CA  ASN A  84     5459   5090   5188    368   -503    949       C  
ATOM    612  C   ASN A  84      39.335  50.341  44.808  1.00 51.40           C  
ANISOU  612  C   ASN A  84     6846   6437   6247    419   -451    988       C  
ATOM    613  O   ASN A  84      39.711  50.165  45.961  1.00 60.76           O  
ANISOU  613  O   ASN A  84     8128   7646   7314    461   -516   1042       O  
ATOM    614  CB  ASN A  84      39.661  48.249  43.502  1.00 41.69           C  
ANISOU  614  CB  ASN A  84     5442   5075   5324    345   -473   1066       C  
ATOM    615  CG  ASN A  84      39.825  47.767  42.080  1.00 57.35           C  
ANISOU  615  CG  ASN A  84     7308   6983   7499    297   -465   1013       C  
ATOM    616  ND2 ASN A  84      38.799  47.953  41.278  1.00 64.47           N  
ANISOU  616  ND2 ASN A  84     8163   7893   8438    263   -362    998       N  
ATOM    617  OD1 ASN A  84      40.864  47.237  41.709  1.00 69.54           O  
ANISOU  617  OD1 ASN A  84     8804   8464   9152    297   -552    985       O  
ATOM    618  N   ILE A  85      38.283  51.077  44.471  1.00 43.07           N  
ANISOU  618  N   ILE A  85     5790   5427   5147    422   -331    960       N  
ATOM    619  CA  ILE A  85      37.684  52.049  45.365  1.00 38.55           C  
ANISOU  619  CA  ILE A  85     5335   4933   4378    486   -276    950       C  
ATOM    620  C   ILE A  85      36.195  51.819  45.504  1.00 48.84           C  
ANISOU  620  C   ILE A  85     6624   6297   5635    502   -114   1050       C  
ATOM    621  O   ILE A  85      35.432  52.016  44.556  1.00 52.99           O  
ANISOU  621  O   ILE A  85     7061   6823   6251    472    -27   1029       O  
ATOM    622  CB  ILE A  85      37.937  53.495  44.851  1.00 43.31           C  
ANISOU  622  CB  ILE A  85     5958   5534   4962    490   -296    799       C  
ATOM    623  CG1 ILE A  85      39.430  53.824  44.920  1.00 45.72           C  
ANISOU  623  CG1 ILE A  85     6283   5790   5297    473   -463    713       C  
ATOM    624  CG2 ILE A  85      37.120  54.512  45.621  1.00 36.51           C  
ANISOU  624  CG2 ILE A  85     5218   4745   3908    566   -217    781       C  
ATOM    625  CD1 ILE A  85      39.904  54.850  43.860  1.00 42.96           C  
ANISOU  625  CD1 ILE A  85     5880   5402   5040    432   -491    581       C  
ATOM    626  N   PHE A  86      35.782  51.399  46.692  1.00 50.02           N  
ANISOU  626  N   PHE A  86     6859   6503   5644    551    -73   1165       N  
ATOM    627  CA  PHE A  86      34.372  51.201  46.964  1.00 50.31           C  
ANISOU  627  CA  PHE A  86     6878   6612   5627    573     91   1277       C  
ATOM    628  C   PHE A  86      33.875  52.415  47.718  1.00 60.86           C  
ANISOU  628  C   PHE A  86     8333   8036   6756    669    163   1230       C  
ATOM    629  O   PHE A  86      34.385  52.731  48.790  1.00 62.99           O  
ANISOU  629  O   PHE A  86     8748   8334   6853    735    105   1218       O  
ATOM    630  CB  PHE A  86      34.149  49.921  47.753  1.00 52.09           C  
ANISOU  630  CB  PHE A  86     7112   6845   5834    565    112   1454       C  
ATOM    631  CG  PHE A  86      34.645  48.688  47.049  1.00 62.10           C  
ANISOU  631  CG  PHE A  86     8278   8010   7305    479     35   1498       C  
ATOM    632  CD1 PHE A  86      36.002  48.379  47.021  1.00 61.85           C  
ANISOU  632  CD1 PHE A  86     8267   7905   7328    469   -124   1443       C  
ATOM    633  CD2 PHE A  86      33.757  47.836  46.408  1.00 64.73           C  
ANISOU  633  CD2 PHE A  86     8495   8318   7783    412    116   1593       C  
ATOM    634  CE1 PHE A  86      36.465  47.237  46.367  1.00 55.04           C  
ANISOU  634  CE1 PHE A  86     7317   6944   6652    408   -190   1479       C  
ATOM    635  CE2 PHE A  86      34.214  46.699  45.755  1.00 59.10           C  
ANISOU  635  CE2 PHE A  86     7705   7496   7253    341     38   1623       C  
ATOM    636  CZ  PHE A  86      35.572  46.401  45.734  1.00 50.55           C  
ANISOU  636  CZ  PHE A  86     6651   6340   6215    346   -109   1563       C  
ATOM    637  N   LEU A  87      32.911  53.126  47.142  1.00 60.64           N  
ANISOU  637  N   LEU A  87     8252   8046   6743    684    280   1195       N  
ATOM    638  CA  LEU A  87      32.426  54.341  47.785  1.00 58.66           C  
ANISOU  638  CA  LEU A  87     8118   7868   6301    790    352   1136       C  
ATOM    639  C   LEU A  87      31.631  54.009  49.036  1.00 60.56           C  
ANISOU  639  C   LEU A  87     8437   8210   6363    871    473   1275       C  
ATOM    640  O   LEU A  87      30.891  53.009  49.083  1.00 54.98           O  
ANISOU  640  O   LEU A  87     7637   7535   5718    836    568   1431       O  
ATOM    641  CB  LEU A  87      31.572  55.180  46.830  1.00 53.64           C  
ANISOU  641  CB  LEU A  87     7401   7246   5734    795    447   1070       C  
ATOM    642  CG  LEU A  87      32.342  55.860  45.696  1.00 49.87           C  
ANISOU  642  CG  LEU A  87     6885   6681   5382    739    339    916       C  
ATOM    643  CD1 LEU A  87      31.417  56.740  44.950  1.00 42.33           C  
ANISOU  643  CD1 LEU A  87     5876   5749   4457    765    438    866       C  
ATOM    644  CD2 LEU A  87      33.553  56.654  46.173  1.00 45.99           C  
ANISOU  644  CD2 LEU A  87     6533   6147   4795    765    197    792       C  
ATOM    645  N   ASP A  88      31.834  54.861  50.043  1.00 59.42           N  
ANISOU  645  N   ASP A  88     8471   8112   5996    977    462   1214       N  
ATOM    646  CA  ASP A  88      31.128  54.851  51.319  1.00 58.59           C  
ANISOU  646  CA  ASP A  88     8482   8115   5666   1088    584   1316       C  
ATOM    647  C   ASP A  88      29.656  55.218  51.139  1.00 61.88           C  
ANISOU  647  C   ASP A  88     8821   8622   6069   1146    796   1373       C  
ATOM    648  O   ASP A  88      29.345  56.224  50.512  1.00 67.31           O  
ANISOU  648  O   ASP A  88     9490   9301   6785   1175    824   1258       O  
ATOM    649  CB  ASP A  88      31.815  55.834  52.267  1.00 67.06           C  
ANISOU  649  CB  ASP A  88     9778   9193   6508   1188    493   1194       C  
ATOM    650  CG  ASP A  88      31.286  55.775  53.696  1.00 83.37           C  
ANISOU  650  CG  ASP A  88    12000  11368   8306   1314    599   1292       C  
ATOM    651  OD1 ASP A  88      30.173  55.255  53.937  1.00 80.58           O  
ANISOU  651  OD1 ASP A  88    11577  11106   7932   1343    786   1446       O  
ATOM    652  OD2 ASP A  88      31.995  56.298  54.590  1.00 92.45           O1-
ANISOU  652  OD2 ASP A  88    13350  12515   9261   1385    492   1211       O1-
ATOM    653  N   PRO A  89      28.747  54.394  51.682  1.00 63.38           N  
ANISOU  653  N   PRO A  89     8958   8898   6225   1160    944   1560       N  
ATOM    654  CA  PRO A  89      27.299  54.645  51.664  1.00 62.57           C  
ANISOU  654  CA  PRO A  89     8767   8901   6104   1222   1159   1646       C  
ATOM    655  C   PRO A  89      26.907  55.981  52.281  1.00 67.05           C  
ANISOU  655  C   PRO A  89     9483   9542   6452   1387   1247   1546       C  
ATOM    656  O   PRO A  89      25.946  56.593  51.814  1.00 70.79           O  
ANISOU  656  O   PRO A  89     9870  10064   6964   1436   1375   1533       O  
ATOM    657  CB  PRO A  89      26.736  53.500  52.500  1.00 60.29           C  
ANISOU  657  CB  PRO A  89     8451   8690   5766   1217   1272   1871       C  
ATOM    658  CG  PRO A  89      27.701  52.401  52.327  1.00 59.91           C  
ANISOU  658  CG  PRO A  89     8383   8540   5840   1095   1112   1912       C  
ATOM    659  CD  PRO A  89      29.062  53.043  52.177  1.00 63.39           C  
ANISOU  659  CD  PRO A  89     8946   8887   6252   1096    908   1717       C  
ATOM    660  N   ALA A  90      27.621  56.410  53.321  1.00 67.87           N  
ANISOU  660  N   ALA A  90     9808   9651   6327   1477   1174   1478       N  
ATOM    661  CA  ALA A  90      27.371  57.717  53.931  1.00 62.98           C  
ANISOU  661  CA  ALA A  90     9364   9080   5485   1640   1232   1359       C  
ATOM    662  C   ALA A  90      27.549  58.775  52.875  1.00 59.83           C  
ANISOU  662  C   ALA A  90     8931   8597   5207   1621   1159   1178       C  
ATOM    663  O   ALA A  90      26.632  59.541  52.589  1.00 62.37           O  
ANISOU  663  O   ALA A  90     9214   8963   5520   1705   1291   1148       O  
ATOM    664  CB  ALA A  90      28.308  57.977  55.100  1.00 51.77           C  
ANISOU  664  CB  ALA A  90     8199   7651   3820   1715   1111   1291       C  
ATOM    665  N   PHE A  91      28.751  58.788  52.304  1.00 47.37           N  
ANISOU  665  N   PHE A  91     7360   6895   3743   1513    950   1068       N  
ATOM    666  CA  PHE A  91      29.122  59.672  51.223  1.00 45.75           C  
ANISOU  666  CA  PHE A  91     7115   6593   3674   1467    857    908       C  
ATOM    667  C   PHE A  91      28.079  59.655  50.126  1.00 61.13           C  
ANISOU  667  C   PHE A  91     8858   8563   5806   1433    984    955       C  
ATOM    668  O   PHE A  91      27.738  60.705  49.577  1.00 76.04           O  
ANISOU  668  O   PHE A  91    10749  10430   7713   1482   1010    849       O  
ATOM    669  CB  PHE A  91      30.480  59.273  50.663  1.00 58.29           C  
ANISOU  669  CB  PHE A  91     8673   8065   5409   1327    643    846       C  
ATOM    670  CG  PHE A  91      30.915  60.100  49.504  1.00 67.81           C  
ANISOU  670  CG  PHE A  91     9826   9173   6764   1266    552    700       C  
ATOM    671  CD1 PHE A  91      31.668  61.241  49.709  1.00 70.92           C  
ANISOU  671  CD1 PHE A  91    10379   9500   7067   1303    429    538       C  
ATOM    672  CD2 PHE A  91      30.571  59.742  48.203  1.00 75.26           C  
ANISOU  672  CD2 PHE A  91    10569  10088   7937   1169    585    728       C  
ATOM    673  CE1 PHE A  91      32.067  62.017  48.641  1.00 79.03           C  
ANISOU  673  CE1 PHE A  91    11358  10436   8235   1242    351    417       C  
ATOM    674  CE2 PHE A  91      30.959  60.514  47.128  1.00 75.34           C  
ANISOU  674  CE2 PHE A  91    10539  10015   8073   1118    509    603       C  
ATOM    675  CZ  PHE A  91      31.710  61.653  47.344  1.00 80.64           C  
ANISOU  675  CZ  PHE A  91    11361  10622   8658   1152    398    453       C  
ATOM    676  N   LEU A  92      27.567  58.471  49.799  1.00 55.95           N  
ANISOU  676  N   LEU A  92     8027   7943   5289   1348   1054   1114       N  
ATOM    677  CA  LEU A  92      26.540  58.381  48.769  1.00 53.92           C  
ANISOU  677  CA  LEU A  92     7569   7709   5212   1308   1162   1167       C  
ATOM    678  C   LEU A  92      25.251  59.048  49.224  1.00 56.75           C  
ANISOU  678  C   LEU A  92     7930   8182   5449   1455   1362   1210       C  
ATOM    679  O   LEU A  92      24.717  59.895  48.520  1.00 70.47           O  
ANISOU  679  O   LEU A  92     9615   9914   7245   1494   1403   1137       O  
ATOM    680  CB  LEU A  92      26.287  56.931  48.368  1.00 45.81           C  
ANISOU  680  CB  LEU A  92     6363   6681   4360   1179   1177   1328       C  
ATOM    681  CG  LEU A  92      27.515  56.309  47.687  1.00 57.59           C  
ANISOU  681  CG  LEU A  92     7830   8050   6002   1042    985   1272       C  
ATOM    682  CD1 LEU A  92      27.312  54.842  47.349  1.00 57.89           C  
ANISOU  682  CD1 LEU A  92     7718   8070   6206    922    988   1424       C  
ATOM    683  CD2 LEU A  92      27.955  57.099  46.439  1.00 51.17           C  
ANISOU  683  CD2 LEU A  92     6977   7148   5319    994    889   1112       C  
ATOM    684  N   ALA A  93      24.769  58.692  50.407  1.00 53.57           N  
ANISOU  684  N   ALA A  93     7594   7887   4874   1545   1487   1330       N  
ATOM    685  CA  ALA A  93      23.540  59.271  50.941  1.00 59.07           C  
ANISOU  685  CA  ALA A  93     8292   8710   5443   1702   1698   1385       C  
ATOM    686  C   ALA A  93      23.636  60.790  51.109  1.00 65.86           C  
ANISOU  686  C   ALA A  93     9323   9547   6152   1849   1690   1200       C  
ATOM    687  O   ALA A  93      22.657  61.508  50.880  1.00 61.28           O  
ANISOU  687  O   ALA A  93     8689   9025   5570   1953   1825   1191       O  
ATOM    688  CB  ALA A  93      23.180  58.607  52.290  1.00 50.97           C  
ANISOU  688  CB  ALA A  93     7337   7802   4226   1778   1830   1546       C  
ATOM    689  N   GLU A  94      24.810  61.278  51.510  1.00 70.00           N  
ANISOU  689  N   GLU A  94    10054   9985   6558   1858   1523   1054       N  
ATOM    690  CA  GLU A  94      24.988  62.713  51.712  1.00 70.38           C  
ANISOU  690  CA  GLU A  94    10288   9990   6463   1988   1491    872       C  
ATOM    691  C   GLU A  94      24.873  63.416  50.384  1.00 62.76           C  
ANISOU  691  C   GLU A  94     9211   8941   5693   1936   1444    772       C  
ATOM    692  O   GLU A  94      24.126  64.380  50.256  1.00 61.25           O  
ANISOU  692  O   GLU A  94     9039   8773   5461   2059   1543    716       O  
ATOM    693  CB  GLU A  94      26.335  63.044  52.373  1.00 75.13           C  
ANISOU  693  CB  GLU A  94    11123  10502   6920   1983   1293    740       C  
ATOM    694  CG  GLU A  94      26.510  64.530  52.685  1.00 77.89           C  
ANISOU  694  CG  GLU A  94    11689  10795   7110   2118   1249    550       C  
ATOM    695  CD  GLU A  94      25.572  65.017  53.800  1.00 88.39           C  
ANISOU  695  CD  GLU A  94    13163  12243   8179   2337   1440    573       C  
ATOM    696  OE1 GLU A  94      25.191  64.200  54.669  1.00 90.91           O  
ANISOU  696  OE1 GLU A  94    13488  12680   8376   2382   1557    720       O  
ATOM    697  OE2 GLU A  94      25.201  66.214  53.802  1.00 88.09           O1-
ANISOU  697  OE2 GLU A  94    13234  12179   8056   2471   1480    449       O1-
ATOM    698  N   HIS A  95      25.584  62.914  49.379  1.00 68.27           N  
ANISOU  698  N   HIS A  95     9790   9546   6604   1760   1300    757       N  
ATOM    699  CA  HIS A  95      25.600  63.581  48.075  1.00 61.50           C  
ANISOU  699  CA  HIS A  95     8841   8602   5922   1703   1240    660       C  
ATOM    700  C   HIS A  95      24.310  63.350  47.271  1.00 64.35           C  
ANISOU  700  C   HIS A  95     8982   9035   6435   1701   1389    766       C  
ATOM    701  O   HIS A  95      23.957  64.168  46.426  1.00 62.72           O  
ANISOU  701  O   HIS A  95     8730   8790   6311   1722   1392    693       O  
ATOM    702  CB  HIS A  95      26.838  63.158  47.283  1.00 53.19           C  
ANISOU  702  CB  HIS A  95     7748   7432   5030   1528   1043    604       C  
ATOM    703  CG  HIS A  95      28.074  63.909  47.680  1.00 64.88           C  
ANISOU  703  CG  HIS A  95     9427   8815   6410   1532    874    451       C  
ATOM    704  CD2 HIS A  95      28.598  65.072  47.200  1.00 77.18           C  
ANISOU  704  CD2 HIS A  95    11072  10269   7983   1535    771    296       C  
ATOM    705  ND1 HIS A  95      28.882  63.518  48.711  1.00 74.36           N  
ANISOU  705  ND1 HIS A  95    10764  10015   7475   1534    787    453       N  
ATOM    706  CE1 HIS A  95      29.876  64.395  48.857  1.00 80.87           C  
ANISOU  706  CE1 HIS A  95    11746  10741   8241   1533    629    301       C  
ATOM    707  NE2 HIS A  95      29.717  65.335  47.947  1.00 85.82           N  
ANISOU  707  NE2 HIS A  95    12344  11302   8962   1530    620    207       N  
ATOM    708  N   VAL A  96      23.580  62.274  47.557  1.00 63.15           N  
ANISOU  708  N   VAL A  96     8694   8984   6316   1678   1509    943       N  
ATOM    709  CA  VAL A  96      22.260  62.087  46.949  1.00 59.83           C  
ANISOU  709  CA  VAL A  96     8064   8645   6025   1688   1655   1056       C  
ATOM    710  C   VAL A  96      21.228  63.081  47.487  1.00 69.97           C  
ANISOU  710  C   VAL A  96     9395  10022   7168   1889   1827   1048       C  
ATOM    711  O   VAL A  96      20.434  63.629  46.727  1.00 74.61           O  
ANISOU  711  O   VAL A  96     9868  10623   7857   1926   1886   1039       O  
ATOM    712  CB  VAL A  96      21.735  60.647  47.166  1.00 57.82           C  
ANISOU  712  CB  VAL A  96     7647   8471   5853   1601   1736   1261       C  
ATOM    713  CG1 VAL A  96      20.232  60.554  46.909  1.00 46.21           C  
ANISOU  713  CG1 VAL A  96     5977   7114   4467   1647   1917   1396       C  
ATOM    714  CG2 VAL A  96      22.482  59.673  46.267  1.00 49.33           C  
ANISOU  714  CG2 VAL A  96     6471   7296   4977   1402   1579   1271       C  
ATOM    715  N   GLN A  97      21.222  63.306  48.796  1.00 72.07           N  
ANISOU  715  N   GLN A  97     9833  10355   7196   2027   1909   1053       N  
ATOM    716  CA  GLN A  97      20.276  64.256  49.362  1.00 75.91           C  
ANISOU  716  CA  GLN A  97    10382  10929   7530   2239   2082   1037       C  
ATOM    717  C   GLN A  97      20.662  65.634  48.865  1.00 67.59           C  
ANISOU  717  C   GLN A  97     9461   9761   6460   2304   1982    834       C  
ATOM    718  O   GLN A  97      19.816  66.395  48.405  1.00 66.50           O  
ANISOU  718  O   GLN A  97     9258   9645   6366   2404   2072    813       O  
ATOM    719  CB  GLN A  97      20.249  64.204  50.903  1.00 78.28           C  
ANISOU  719  CB  GLN A  97    10867  11323   7553   2383   2189   1077       C  
ATOM    720  N   GLN A  98      21.955  65.915  48.935  1.00 66.16           N  
ANISOU  720  N   GLN A  98     9455   9454   6229   2240   1789    695       N  
ATOM    721  CA  GLN A  98      22.516  67.213  48.607  1.00 74.03           C  
ANISOU  721  CA  GLN A  98    10611  10324   7193   2287   1671    500       C  
ATOM    722  C   GLN A  98      22.148  67.576  47.175  1.00 75.16           C  
ANISOU  722  C   GLN A  98    10584  10411   7562   2219   1645    479       C  
ATOM    723  O   GLN A  98      21.788  68.723  46.883  1.00 78.77           O  
ANISOU  723  O   GLN A  98    11102  10825   8001   2329   1665    382       O  
ATOM    724  CB  GLN A  98      24.029  67.165  48.818  1.00 81.27           C  
ANISOU  724  CB  GLN A  98    11687  11121   8072   2178   1453    392       C  
ATOM    725  CG  GLN A  98      24.832  68.355  48.333  1.00 91.58           C  
ANISOU  725  CG  GLN A  98    13133  12272   9393   2166   1289    202       C  
ATOM    726  CD  GLN A  98      26.330  68.168  48.606  1.00 96.04           C  
ANISOU  726  CD  GLN A  98    13824  12735   9932   2046   1076    121       C  
ATOM    727  NE2 GLN A  98      27.178  68.422  47.599  1.00 92.87           N  
ANISOU  727  NE2 GLN A  98    13377  12209   9698   1905    916     42       N  
ATOM    728  OE1 GLN A  98      26.709  67.782  49.709  1.00 96.11           O  
ANISOU  728  OE1 GLN A  98    13962  12783   9774   2082   1058    138       O  
ATOM    729  N   ALA A  99      22.182  66.570  46.301  1.00 63.99           N  
ANISOU  729  N   ALA A  99     8961   9000   6354   2047   1606    577       N  
ATOM    730  CA  ALA A  99      21.832  66.737  44.891  1.00 52.78           C  
ANISOU  730  CA  ALA A  99     7370   7535   5150   1967   1574    573       C  
ATOM    731  C   ALA A  99      20.330  66.876  44.700  1.00 54.69           C  
ANISOU  731  C   ALA A  99     7452   7890   5436   2076   1756    675       C  
ATOM    732  O   ALA A  99      19.864  67.530  43.757  1.00 57.96           O  
ANISOU  732  O   ALA A  99     7789   8271   5961   2093   1751    638       O  
ATOM    733  CB  ALA A  99      22.348  65.581  44.078  1.00 52.20           C  
ANISOU  733  CB  ALA A  99     7143   7428   5263   1760   1472    639       C  
ATOM    734  N   LEU A 100      19.571  66.265  45.599  1.00 49.61           N  
ANISOU  734  N   LEU A 100     6756   7385   4709   2150   1918    811       N  
ATOM    735  CA  LEU A 100      18.125  66.402  45.568  1.00 58.15           C  
ANISOU  735  CA  LEU A 100     7679   8592   5824   2268   2108    921       C  
ATOM    736  C   LEU A 100      17.669  67.799  46.006  1.00 65.10           C  
ANISOU  736  C   LEU A 100     8706   9479   6552   2497   2196    817       C  
ATOM    737  O   LEU A 100      16.476  68.128  45.897  1.00 59.73           O  
ANISOU  737  O   LEU A 100     7898   8892   5903   2620   2350    887       O  
ATOM    738  CB  LEU A 100      17.460  65.343  46.442  1.00 59.76           C  
ANISOU  738  CB  LEU A 100     7778   8945   5981   2281   2267   1112       C  
ATOM    739  CG  LEU A 100      17.050  64.076  45.688  1.00 72.62           C  
ANISOU  739  CG  LEU A 100     9143  10608   7840   2097   2257   1272       C  
ATOM    740  CD1 LEU A 100      16.431  63.053  46.646  1.00 77.98           C  
ANISOU  740  CD1 LEU A 100     9734  11428   8467   2106   2416   1471       C  
ATOM    741  CD2 LEU A 100      16.115  64.391  44.515  1.00 64.74           C  
ANISOU  741  CD2 LEU A 100     7936   9622   7038   2087   2276   1299       C  
ATOM    742  N   ALA A 101      18.616  68.615  46.482  1.00 65.82           N  
ANISOU  742  N   ALA A 101     9060   9463   6485   2552   2093    649       N  
ATOM    743  CA  ALA A 101      18.317  69.981  46.933  1.00 73.01           C  
ANISOU  743  CA  ALA A 101    10152  10349   7238   2769   2152    526       C  
ATOM    744  C   ALA A 101      18.408  71.023  45.810  1.00 80.03           C  
ANISOU  744  C   ALA A 101    11048  11108   8250   2763   2047    404       C  
ATOM    745  O   ALA A 101      17.676  72.008  45.814  1.00 85.21           O  
ANISOU  745  O   ALA A 101    11741  11770   8863   2941   2136    359       O  
ATOM    746  CB  ALA A 101      19.243  70.371  48.073  1.00 71.26           C  
ANISOU  746  CB  ALA A 101    10228  10071   6775   2838   2086    404       C  
ATOM    747  N   SER A 102      19.319  70.810  44.866  1.00 81.85           N  
ANISOU  747  N   SER A 102    11248  11221   8629   2566   1860    356       N  
ATOM    748  CA  SER A 102      19.472  71.684  43.709  1.00 82.97           C  
ANISOU  748  CA  SER A 102    11385  11241   8900   2533   1754    261       C  
ATOM    749  C   SER A 102      18.529  71.240  42.585  1.00 86.37           C  
ANISOU  749  C   SER A 102    11539  11736   9542   2474   1807    381       C  
ATOM    750  O   SER A 102      18.236  70.050  42.457  1.00 92.75           O  
ANISOU  750  O   SER A 102    12161  12635  10443   2365   1845    518       O  
ATOM    751  CB  SER A 102      20.933  71.677  43.233  1.00 85.19           C  
ANISOU  751  CB  SER A 102    11765  11371   9233   2353   1537    157       C  
ATOM    752  OG  SER A 102      21.152  72.561  42.141  1.00 83.86           O  
ANISOU  752  OG  SER A 102    11607  11079   9176   2318   1435     69       O  
ATOM    753  N   ASP A 103      18.051  72.197  41.787  1.00 85.40           N  
ANISOU  753  N   ASP A 103    11395  11559   9492   2545   1799    332       N  
ATOM    754  CA  ASP A 103      17.207  71.917  40.618  1.00 82.95           C  
ANISOU  754  CA  ASP A 103    10840  11294   9383   2489   1817    430       C  
ATOM    755  C   ASP A 103      18.091  71.614  39.419  1.00 77.66           C  
ANISOU  755  C   ASP A 103    10130  10513   8863   2276   1635    393       C  
ATOM    756  O   ASP A 103      17.639  71.265  38.324  1.00 73.56           O  
ANISOU  756  O   ASP A 103     9428  10009   8512   2190   1607    459       O  
ATOM    757  CB  ASP A 103      16.295  73.091  40.301  1.00 90.99           C  
ANISOU  757  CB  ASP A 103    11858  12306  10408   2672   1887    399       C  
ATOM    758  CG  ASP A 103      15.076  72.673  39.518  1.00106.42           C  
ANISOU  758  CG  ASP A 103    13535  14369  12532   2669   1963    540       C  
ATOM    759  OD1 ASP A 103      14.497  71.616  39.851  1.00110.69           O  
ANISOU  759  OD1 ASP A 103    13900  15046  13112   2630   2061    683       O  
ATOM    760  OD2 ASP A 103      14.708  73.385  38.561  1.00115.20           O1-
ANISOU  760  OD2 ASP A 103    14600  15426  13743   2700   1916    514       O1-
ATOM    761  N   ARG A 104      19.375  71.761  39.680  1.00 73.83           N  
ANISOU  761  N   ARG A 104     9827   9919   8308   2200   1512    285       N  
ATOM    762  CA  ARG A 104      20.449  71.464  38.773  1.00 58.78           C  
ANISOU  762  CA  ARG A 104     7917   7907   6511   2006   1346    239       C  
ATOM    763  C   ARG A 104      21.052  70.087  39.105  1.00 66.50           C  
ANISOU  763  C   ARG A 104     8833   8929   7507   1859   1315    307       C  
ATOM    764  O   ARG A 104      22.073  69.677  38.538  1.00 61.31           O  
ANISOU  764  O   ARG A 104     8179   8194   6924   1701   1185    272       O  
ATOM    765  CB  ARG A 104      21.478  72.569  38.918  1.00 57.70           C  
ANISOU  765  CB  ARG A 104     8013   7621   6289   2023   1232     83       C  
ATOM    766  CG  ARG A 104      22.182  72.890  37.705  1.00 72.63           C  
ANISOU  766  CG  ARG A 104     9897   9394   8304   1892   1095     30       C  
ATOM    767  CD  ARG A 104      23.332  73.767  38.044  1.00 78.72           C  
ANISOU  767  CD  ARG A 104    10890  10026   8995   1880    977   -107       C  
ATOM    768  NE  ARG A 104      24.325  73.668  36.989  1.00 81.25           N  
ANISOU  768  NE  ARG A 104    11181  10251   9440   1703    841   -134       N  
ATOM    769  CZ  ARG A 104      24.141  74.123  35.760  1.00 89.47           C  
ANISOU  769  CZ  ARG A 104    12159  11240  10596   1666    807   -131       C  
ATOM    770  NH1 ARG A 104      23.012  74.734  35.427  1.00 85.45           N1+
ANISOU  770  NH1 ARG A 104    11609  10756  10101   1792    886   -106       N1+
ATOM    771  NH2 ARG A 104      25.100  73.982  34.863  1.00103.78           N  
ANISOU  771  NH2 ARG A 104    13950  12977  12506   1507    696   -151       N  
ATOM    772  N   LEU A 105      20.417  69.402  40.062  1.00 64.61           N  
ANISOU  772  N   LEU A 105     8541   8814   7195   1923   1443    407       N  
ATOM    773  CA  LEU A 105      20.883  68.126  40.618  1.00 59.27           C  
ANISOU  773  CA  LEU A 105     7826   8185   6508   1815   1434    484       C  
ATOM    774  C   LEU A 105      22.323  68.212  41.148  1.00 63.84           C  
ANISOU  774  C   LEU A 105     8598   8666   6991   1757   1303    377       C  
ATOM    775  O   LEU A 105      23.039  67.205  41.255  1.00 55.71           O  
ANISOU  775  O   LEU A 105     7540   7631   5995   1629   1237    415       O  
ATOM    776  CB  LEU A 105      20.750  66.998  39.588  1.00 54.37           C  
ANISOU  776  CB  LEU A 105     6993   7579   6084   1645   1390    580       C  
ATOM    777  CG  LEU A 105      19.339  66.717  39.037  1.00 52.57           C  
ANISOU  777  CG  LEU A 105     6547   7450   5975   1672   1495    704       C  
ATOM    778  CD1 LEU A 105      19.321  65.479  38.161  1.00 49.14           C  
ANISOU  778  CD1 LEU A 105     5933   7019   5720   1492   1431    792       C  
ATOM    779  CD2 LEU A 105      18.312  66.588  40.130  1.00 50.24           C  
ANISOU  779  CD2 LEU A 105     6210   7294   5585   1812   1677    810       C  
ATOM    780  N   GLY A 106      22.723  69.424  41.519  1.00 65.78           N  
ANISOU  780  N   GLY A 106     9042   8834   7119   1856   1264    245       N  
ATOM    781  CA  GLY A 106      24.017  69.657  42.130  1.00 57.75           C  
ANISOU  781  CA  GLY A 106     8217   7725   6000   1817   1135    140       C  
ATOM    782  C   GLY A 106      25.121  69.809  41.108  1.00 55.63           C  
ANISOU  782  C   GLY A 106     7946   7328   5861   1658    966     64       C  
ATOM    783  O   GLY A 106      26.292  69.986  41.455  1.00 62.07           O  
ANISOU  783  O   GLY A 106     8894   8060   6630   1600    839    -19       O  
ATOM    784  N   VAL A 107      24.760  69.731  39.837  1.00 54.80           N  
ANISOU  784  N   VAL A 107     7689   7212   5922   1588    962     98       N  
ATOM    785  CA  VAL A 107      25.775  69.779  38.811  1.00 59.73           C  
ANISOU  785  CA  VAL A 107     8296   7729   6668   1439    821     43       C  
ATOM    786  C   VAL A 107      26.430  71.150  38.832  1.00 60.85           C  
ANISOU  786  C   VAL A 107     8622   7745   6754   1476    732    -92       C  
ATOM    787  O   VAL A 107      25.761  72.161  38.718  1.00 64.12           O  
ANISOU  787  O   VAL A 107     9092   8134   7136   1592    779   -130       O  
ATOM    788  CB  VAL A 107      25.206  69.470  37.425  1.00 48.61           C  
ANISOU  788  CB  VAL A 107     6706   6336   5430   1369    836    103       C  
ATOM    789  CG1 VAL A 107      26.256  69.728  36.375  1.00 38.44           C  
ANISOU  789  CG1 VAL A 107     5428   4935   4242   1239    705     37       C  
ATOM    790  CG2 VAL A 107      24.735  68.024  37.373  1.00 47.27           C  
ANISOU  790  CG2 VAL A 107     6361   6266   5333   1300    891    230       C  
ATOM    791  N   ALA A 108      27.745  71.164  39.007  1.00 58.28           N  
ANISOU  791  N   ALA A 108     8386   7335   6422   1378    598   -159       N  
ATOM    792  CA  ALA A 108      28.496  72.401  39.100  1.00 62.38           C  
ANISOU  792  CA  ALA A 108     9081   7722   6897   1388    492   -283       C  
ATOM    793  C   ALA A 108      28.298  73.305  37.883  1.00 70.93           C  
ANISOU  793  C   ALA A 108    10141   8724   8086   1374    474   -312       C  
ATOM    794  O   ALA A 108      27.986  72.844  36.780  1.00 64.85           O  
ANISOU  794  O   ALA A 108     9210   7984   7446   1305    500   -246       O  
ATOM    795  CB  ALA A 108      29.973  72.093  39.289  1.00 58.24           C  
ANISOU  795  CB  ALA A 108     8604   7132   6395   1252    343   -326       C  
ATOM    796  N   THR A 109      28.458  74.605  38.108  1.00 77.47           N  
ANISOU  796  N   THR A 109    11141   9443   8851   1444    424   -412       N  
ATOM    797  CA  THR A 109      28.519  75.569  37.019  1.00 73.61           C  
ANISOU  797  CA  THR A 109    10664   8847   8459   1415    379   -447       C  
ATOM    798  C   THR A 109      29.921  76.148  36.929  1.00 68.97           C  
ANISOU  798  C   THR A 109    10185   8118   7902   1295    218   -529       C  
ATOM    799  O   THR A 109      30.235  77.172  37.543  1.00 68.40           O  
ANISOU  799  O   THR A 109    10303   7939   7748   1350    150   -624       O  
ATOM    800  CB  THR A 109      27.517  76.714  37.180  1.00 70.64           C  
ANISOU  800  CB  THR A 109    10392   8435   8011   1593    447   -488       C  
ATOM    801  CG2 THR A 109      27.599  77.635  35.982  1.00 69.63           C  
ANISOU  801  CG2 THR A 109    10268   8194   7993   1553    394   -507       C  
ATOM    802  OG1 THR A 109      26.193  76.182  37.266  1.00 63.92           O  
ANISOU  802  OG1 THR A 109     9417   7726   7144   1707    601   -400       O  
ATOM    803  N   PRO A 110      30.766  75.486  36.143  1.00 63.25           N  
ANISOU  803  N   PRO A 110     9339   7393   7302   1130    158   -489       N  
ATOM    804  CA  PRO A 110      32.173  75.820  35.917  1.00 66.12           C  
ANISOU  804  CA  PRO A 110     9749   7644   7729    988     14   -538       C  
ATOM    805  C   PRO A 110      32.385  77.236  35.375  1.00 67.06           C  
ANISOU  805  C   PRO A 110     9982   7614   7885    983    -51   -600       C  
ATOM    806  O   PRO A 110      31.421  77.949  35.073  1.00 70.22           O  
ANISOU  806  O   PRO A 110    10421   7994   8265   1094     15   -604       O  
ATOM    807  CB  PRO A 110      32.612  74.772  34.889  1.00 62.82           C  
ANISOU  807  CB  PRO A 110     9136   7285   7449    851     20   -459       C  
ATOM    808  CG  PRO A 110      31.346  74.358  34.209  1.00 53.08           C  
ANISOU  808  CG  PRO A 110     7782   6143   6242    917    147   -385       C  
ATOM    809  CD  PRO A 110      30.298  74.408  35.254  1.00 52.50           C  
ANISOU  809  CD  PRO A 110     7771   6135   6041   1076    234   -387       C  
ATOM    810  N   GLU A 111      33.650  77.631  35.268  1.00 65.77           N  
ANISOU  810  N   GLU A 111     9866   7345   7781    854   -184   -641       N  
ATOM    811  CA  GLU A 111      34.014  78.954  34.780  1.00 68.84           C  
ANISOU  811  CA  GLU A 111    10364   7575   8217    822   -264   -691       C  
ATOM    812  C   GLU A 111      33.366  79.152  33.427  1.00 68.03           C  
ANISOU  812  C   GLU A 111    10162   7479   8205    822   -183   -625       C  
ATOM    813  O   GLU A 111      33.661  78.400  32.497  1.00 72.22           O  
ANISOU  813  O   GLU A 111    10532   8072   8835    720   -158   -553       O  
ATOM    814  CB  GLU A 111      35.536  79.090  34.685  1.00 76.77           C  
ANISOU  814  CB  GLU A 111    11370   8490   9310    648   -409   -710       C  
ATOM    815  CG  GLU A 111      36.051  80.511  34.738  1.00 88.23           C  
ANISOU  815  CG  GLU A 111    12989   9756  10777    617   -528   -784       C  
ATOM    816  CD  GLU A 111      35.640  81.216  36.013  1.00109.11           C  
ANISOU  816  CD  GLU A 111    15853  12335  13267    755   -570   -889       C  
ATOM    817  OE1 GLU A 111      35.968  80.709  37.112  1.00115.35           O  
ANISOU  817  OE1 GLU A 111    16692  13170  13964    772   -617   -928       O  
ATOM    818  OE2 GLU A 111      34.974  82.271  35.916  1.00117.14           O1-
ANISOU  818  OE2 GLU A 111    17002  13257  14251    856   -554   -932       O1-
ATOM    819  N   LYS A 112      32.464  80.127  33.323  1.00 64.86           N  
ANISOU  819  N   LYS A 112     9861   7018   7764    947   -144   -651       N  
ATOM    820  CA  LYS A 112      31.685  80.297  32.101  1.00 60.14           C  
ANISOU  820  CA  LYS A 112     9173   6440   7237    971    -67   -583       C  
ATOM    821  C   LYS A 112      32.586  80.635  30.933  1.00 63.84           C  
ANISOU  821  C   LYS A 112     9600   6825   7832    814   -133   -549       C  
ATOM    822  O   LYS A 112      33.619  81.281  31.088  1.00 62.09           O  
ANISOU  822  O   LYS A 112     9468   6479   7643    719   -243   -592       O  
ATOM    823  CB  LYS A 112      30.615  81.375  32.243  1.00 57.82           C  
ANISOU  823  CB  LYS A 112     9004   6084   6882   1142    -25   -619       C  
ATOM    824  CG  LYS A 112      29.314  81.000  31.517  1.00 60.79           C  
ANISOU  824  CG  LYS A 112     9246   6574   7278   1237     99   -538       C  
ATOM    825  CD  LYS A 112      28.367  82.170  31.349  1.00 55.57           C  
ANISOU  825  CD  LYS A 112     8688   5834   6592   1391    129   -558       C  
ATOM    826  CE  LYS A 112      29.130  83.375  30.885  1.00 55.32           C  
ANISOU  826  CE  LYS A 112     8796   5610   6611   1322     20   -599       C  
ATOM    827  NZ  LYS A 112      28.209  84.379  30.301  1.00 73.67           N1+
ANISOU  827  NZ  LYS A 112    11179   7863   8949   1447     49   -587       N1+
ATOM    828  N   GLN A 113      32.173  80.164  29.763  1.00 69.17           N  
ANISOU  828  N   GLN A 113    10133   7573   8576    786    -65   -467       N  
ATOM    829  CA  GLN A 113      32.921  80.313  28.526  1.00 63.85           C  
ANISOU  829  CA  GLN A 113     9398   6851   8011    647    -97   -416       C  
ATOM    830  C   GLN A 113      31.971  80.711  27.418  1.00 60.38           C  
ANISOU  830  C   GLN A 113     8930   6416   7596    709    -37   -360       C  
ATOM    831  O   GLN A 113      30.780  80.369  27.471  1.00 60.14           O  
ANISOU  831  O   GLN A 113     8851   6477   7522    831     42   -339       O  
ATOM    832  CB  GLN A 113      33.632  79.011  28.171  1.00 62.78           C  
ANISOU  832  CB  GLN A 113     9100   6823   7931    528    -84   -369       C  
ATOM    833  CG  GLN A 113      34.697  78.627  29.176  1.00 73.43           C  
ANISOU  833  CG  GLN A 113    10467   8163   9271    455   -159   -414       C  
ATOM    834  CD  GLN A 113      35.489  77.409  28.761  1.00 80.76           C  
ANISOU  834  CD  GLN A 113    11236   9180  10267    341   -151   -367       C  
ATOM    835  NE2 GLN A 113      36.777  77.606  28.496  1.00 79.50           N  
ANISOU  835  NE2 GLN A 113    11060   8958  10188    208   -224   -363       N  
ATOM    836  OE1 GLN A 113      34.956  76.302  28.681  1.00 90.72           O  
ANISOU  836  OE1 GLN A 113    12390  10562  11515    373    -80   -331       O  
ATOM    837  N   THR A 114      32.472  81.457  26.436  1.00 55.06           N  
ANISOU  837  N   THR A 114     8285   5644   6991    627    -75   -328       N  
ATOM    838  CA  THR A 114      31.708  81.648  25.212  1.00 57.40           C  
ANISOU  838  CA  THR A 114     8534   5960   7314    663    -24   -258       C  
ATOM    839  C   THR A 114      32.164  80.569  24.258  1.00 51.91           C  
ANISOU  839  C   THR A 114     7682   5369   6671    550      8   -193       C  
ATOM    840  O   THR A 114      33.309  80.564  23.804  1.00 52.31           O  
ANISOU  840  O   THR A 114     7713   5382   6782    415    -27   -174       O  
ATOM    841  CB  THR A 114      31.901  83.026  24.574  1.00 66.61           C  
ANISOU  841  CB  THR A 114     9824   6968   8518    647    -74   -245       C  
ATOM    842  CG2 THR A 114      31.434  84.121  25.524  1.00 74.09           C  
ANISOU  842  CG2 THR A 114    10944   7795   9410    772   -112   -320       C  
ATOM    843  OG1 THR A 114      33.288  83.217  24.278  1.00 75.85           O  
ANISOU  843  OG1 THR A 114    10999   8062   9758    479   -136   -231       O  
ATOM    844  N   ILE A 115      31.271  79.629  23.993  1.00 51.26           N  
ANISOU  844  N   ILE A 115     7486   5420   6570    609     75   -160       N  
ATOM    845  CA  ILE A 115      31.559  78.545  23.070  1.00 45.74           C  
ANISOU  845  CA  ILE A 115     6650   4818   5910    521    104   -108       C  
ATOM    846  C   ILE A 115      30.757  78.737  21.791  1.00 52.28           C  
ANISOU  846  C   ILE A 115     7450   5668   6746    557    132    -46       C  
ATOM    847  O   ILE A 115      29.516  78.862  21.823  1.00 49.00           O  
ANISOU  847  O   ILE A 115     7027   5289   6302    676    158    -34       O  
ATOM    848  CB  ILE A 115      31.205  77.158  23.638  1.00 38.59           C  
ANISOU  848  CB  ILE A 115     5631   4045   4986    540    144   -112       C  
ATOM    849  CG1 ILE A 115      31.570  77.030  25.111  1.00 34.17           C  
ANISOU  849  CG1 ILE A 115     5117   3478   4389    557    123   -172       C  
ATOM    850  CG2 ILE A 115      31.884  76.071  22.794  1.00 50.09           C  
ANISOU  850  CG2 ILE A 115     6973   5570   6490    429    155    -77       C  
ATOM    851  CD1 ILE A 115      33.052  76.872  25.349  1.00 50.27           C  
ANISOU  851  CD1 ILE A 115     7161   5473   6467    430     66   -195       C  
ATOM    852  N   VAL A 116      31.463  78.752  20.668  1.00 30.26           N  
ANISOU  852  N   VAL A 116     4641   2861   3993    457    126     -1       N  
ATOM    853  CA  VAL A 116      30.816  78.769  19.379  1.00 30.22           C  
ANISOU  853  CA  VAL A 116     4609   2890   3983    479    146     60       C  
ATOM    854  C   VAL A 116      30.746  77.344  18.855  1.00 40.77           C  
ANISOU  854  C   VAL A 116     5816   4354   5322    440    176     78       C  
ATOM    855  O   VAL A 116      31.746  76.608  18.826  1.00 36.74           O  
ANISOU  855  O   VAL A 116     5253   3872   4835    345    184     68       O  
ATOM    856  CB  VAL A 116      31.565  79.690  18.390  1.00 36.53           C  
ANISOU  856  CB  VAL A 116     5481   3593   4805    403    128    107       C  
ATOM    857  CG1 VAL A 116      31.123  79.439  16.965  1.00 30.71           C  
ANISOU  857  CG1 VAL A 116     4707   2912   4049    404    149    173       C  
ATOM    858  CG2 VAL A 116      31.301  81.111  18.744  1.00 31.92           C  
ANISOU  858  CG2 VAL A 116     5033   2875   4220    463     90     98       C  
ATOM    859  N   VAL A 117      29.537  76.957  18.473  1.00 36.20           N  
ANISOU  859  N   VAL A 117     5184   3849   4723    519    188    102       N  
ATOM    860  CA  VAL A 117      29.297  75.669  17.901  1.00 33.13           C  
ANISOU  860  CA  VAL A 117     4685   3565   4336    489    201    118       C  
ATOM    861  C   VAL A 117      28.791  75.831  16.466  1.00 37.91           C  
ANISOU  861  C   VAL A 117     5295   4186   4922    499    188    170       C  
ATOM    862  O   VAL A 117      27.715  76.385  16.213  1.00 38.24           O  
ANISOU  862  O   VAL A 117     5352   4226   4951    588    170    199       O  
ATOM    863  CB  VAL A 117      28.301  74.851  18.746  1.00 40.96           C  
ANISOU  863  CB  VAL A 117     5592   4642   5330    557    215    105       C  
ATOM    864  CG1 VAL A 117      28.384  73.356  18.374  1.00 34.49           C  
ANISOU  864  CG1 VAL A 117     4664   3912   4528    496    219    109       C  
ATOM    865  CG2 VAL A 117      28.603  75.029  20.197  1.00 38.94           C  
ANISOU  865  CG2 VAL A 117     5367   4360   5069    580    227     59       C  
ATOM    866  N   ASP A 118      29.620  75.331  15.552  1.00 35.53           N  
ANISOU  866  N   ASP A 118     4982   3901   4616    412    197    183       N  
ATOM    867  CA  ASP A 118      29.384  75.311  14.122  1.00 36.31           C  
ANISOU  867  CA  ASP A 118     5095   4022   4677    405    186    228       C  
ATOM    868  C   ASP A 118      28.703  74.015  13.753  1.00 34.46           C  
ANISOU  868  C   ASP A 118     4770   3887   4436    413    170    219       C  
ATOM    869  O   ASP A 118      29.378  72.996  13.627  1.00 39.63           O  
ANISOU  869  O   ASP A 118     5380   4581   5096    350    187    193       O  
ATOM    870  CB  ASP A 118      30.723  75.455  13.385  1.00 45.95           C  
ANISOU  870  CB  ASP A 118     6358   5212   5890    311    218    246       C  
ATOM    871  CG  ASP A 118      30.572  75.719  11.888  1.00 56.98           C  
ANISOU  871  CG  ASP A 118     7805   6616   7227    311    215    302       C  
ATOM    872  OD1 ASP A 118      29.669  75.158  11.239  1.00 71.01           O  
ANISOU  872  OD1 ASP A 118     9557   8457   8967    355    183    309       O  
ATOM    873  OD2 ASP A 118      31.393  76.486  11.349  1.00 49.94           O1-
ANISOU  873  OD2 ASP A 118     6982   5668   6326    263    242    344       O1-
ATOM    874  N   TYR A 119      27.384  74.032  13.561  1.00 32.07           N  
ANISOU  874  N   TYR A 119     4437   3620   4127    490    131    243       N  
ATOM    875  CA  TYR A 119      26.693  72.791  13.191  1.00 36.17           C  
ANISOU  875  CA  TYR A 119     4867   4225   4651    485     98    238       C  
ATOM    876  C   TYR A 119      25.503  72.963  12.245  1.00 39.59           C  
ANISOU  876  C   TYR A 119     5292   4689   5060    543     34    282       C  
ATOM    877  O   TYR A 119      25.005  74.071  12.043  1.00 46.87           O  
ANISOU  877  O   TYR A 119     6267   5573   5969    609     19    320       O  
ATOM    878  CB  TYR A 119      26.248  72.044  14.458  1.00 40.69           C  
ANISOU  878  CB  TYR A 119     5343   4841   5276    501    110    213       C  
ATOM    879  CG  TYR A 119      25.158  72.700  15.275  1.00 33.27           C  
ANISOU  879  CG  TYR A 119     4377   3906   4359    600    112    235       C  
ATOM    880  CD1 TYR A 119      25.386  73.893  15.962  1.00 42.97           C  
ANISOU  880  CD1 TYR A 119     5684   5064   5579    650    141    228       C  
ATOM    881  CD2 TYR A 119      23.916  72.099  15.405  1.00 34.68           C  
ANISOU  881  CD2 TYR A 119     4449   4156   4571    645     86    263       C  
ATOM    882  CE1 TYR A 119      24.374  74.497  16.737  1.00 45.50           C  
ANISOU  882  CE1 TYR A 119     5987   5388   5912    761    153    242       C  
ATOM    883  CE2 TYR A 119      22.896  72.693  16.165  1.00 45.65           C  
ANISOU  883  CE2 TYR A 119     5800   5561   5983    748    103    289       C  
ATOM    884  CZ  TYR A 119      23.134  73.886  16.827  1.00 51.02           C  
ANISOU  884  CZ  TYR A 119     6569   6173   6642    814    141    275       C  
ATOM    885  OH  TYR A 119      22.133  74.451  17.575  1.00 59.09           O  
ANISOU  885  OH  TYR A 119     7561   7213   7679    932    168    296       O  
ATOM    886  N   SER A 120      25.083  71.838  11.663  1.00 37.84           N  
ANISOU  886  N   SER A 120     5010   4531   4836    515    -12    274       N  
ATOM    887  CA  SER A 120      24.013  71.747  10.658  1.00 38.28           C  
ANISOU  887  CA  SER A 120     5051   4625   4869    551    -96    310       C  
ATOM    888  C   SER A 120      24.568  72.163   9.328  1.00 44.19           C  
ANISOU  888  C   SER A 120     5913   5348   5529    532   -110    325       C  
ATOM    889  O   SER A 120      24.943  71.320   8.519  1.00 57.28           O  
ANISOU  889  O   SER A 120     7590   7032   7141    482   -130    299       O  
ATOM    890  CB  SER A 120      22.797  72.599  11.010  1.00 42.97           C  
ANISOU  890  CB  SER A 120     5608   5223   5497    650   -124    359       C  
ATOM    891  OG  SER A 120      21.723  72.354  10.122  1.00 42.26           O  
ANISOU  891  OG  SER A 120     5476   5179   5400    679   -219    395       O  
ATOM    892  N   ALA A 121      24.623  73.472   9.123  1.00 47.20           N  
ANISOU  892  N   ALA A 121     6377   5674   5884    576    -96    368       N  
ATOM    893  CA  ALA A 121      25.288  74.098   7.972  1.00 45.43           C  
ANISOU  893  CA  ALA A 121     6274   5413   5573    557    -87    401       C  
ATOM    894  C   ALA A 121      24.889  73.572   6.581  1.00 43.17           C  
ANISOU  894  C   ALA A 121     6023   5175   5204    555   -160    414       C  
ATOM    895  O   ALA A 121      25.753  73.205   5.791  1.00 35.42           O  
ANISOU  895  O   ALA A 121     5107   4201   4149    505   -129    401       O  
ATOM    896  CB  ALA A 121      26.807  73.988   8.149  1.00 39.68           C  
ANISOU  896  CB  ALA A 121     5586   4655   4838    476      4    373       C  
ATOM    897  N   PRO A 122      23.581  73.561   6.268  1.00 47.97           N  
ANISOU  897  N   PRO A 122     6590   5818   5820    615   -259    442       N  
ATOM    898  CA  PRO A 122      23.139  73.185   4.920  1.00 47.59           C  
ANISOU  898  CA  PRO A 122     6591   5809   5683    620   -351    457       C  
ATOM    899  C   PRO A 122      23.510  74.195   3.839  1.00 59.32           C  
ANISOU  899  C   PRO A 122     8221   7257   7061    641   -345    517       C  
ATOM    900  O   PRO A 122      24.075  75.241   4.142  1.00 69.93           O  
ANISOU  900  O   PRO A 122     9621   8535   8412    649   -273    554       O  
ATOM    901  CB  PRO A 122      21.623  73.125   5.065  1.00 43.11           C  
ANISOU  901  CB  PRO A 122     5922   5280   5177    682   -460    485       C  
ATOM    902  CG  PRO A 122      21.322  74.041   6.171  1.00 43.67           C  
ANISOU  902  CG  PRO A 122     5946   5316   5332    743   -408    514       C  
ATOM    903  CD  PRO A 122      22.434  73.867   7.141  1.00 43.65           C  
ANISOU  903  CD  PRO A 122     5942   5281   5362    687   -293    464       C  
ATOM    904  N   ASN A 123      23.160  73.889   2.592  1.00 63.32           N  
ANISOU  904  N   ASN A 123     8793   7801   7467    650   -429    530       N  
ATOM    905  CA  ASN A 123      23.430  74.773   1.458  1.00 56.74           C  
ANISOU  905  CA  ASN A 123     8106   6942   6513    675   -431    598       C  
ATOM    906  C   ASN A 123      22.152  75.282   0.795  1.00 60.28           C  
ANISOU  906  C   ASN A 123     8569   7401   6932    755   -568    660       C  
ATOM    907  O   ASN A 123      21.175  74.544   0.697  1.00 62.30           O  
ANISOU  907  O   ASN A 123     8744   7711   7215    770   -682    635       O  
ATOM    908  CB  ASN A 123      24.282  74.046   0.424  1.00 53.87           C  
ANISOU  908  CB  ASN A 123     7838   6611   6018    626   -402    565       C  
ATOM    909  CG  ASN A 123      25.627  73.616   0.973  1.00 55.13           C  
ANISOU  909  CG  ASN A 123     7982   6760   6204    556   -262    516       C  
ATOM    910  ND2 ASN A 123      26.060  72.437   0.583  1.00 49.11           N  
ANISOU  910  ND2 ASN A 123     7226   6043   5391    520   -255    445       N  
ATOM    911  OD1 ASN A 123      26.273  74.342   1.728  1.00 65.20           O  
ANISOU  911  OD1 ASN A 123     9244   7983   7547    536   -170    541       O  
ATOM    912  N   VAL A 124      22.157  76.534   0.333  1.00 61.13           N  
ANISOU  912  N   VAL A 124     8778   7456   6991    804   -562    746       N  
ATOM    913  CA  VAL A 124      20.972  77.110  -0.295  1.00 52.01           C  
ANISOU  913  CA  VAL A 124     7642   6308   5812    890   -695    815       C  
ATOM    914  C   VAL A 124      20.793  76.522  -1.692  1.00 53.20           C  
ANISOU  914  C   VAL A 124     7884   6516   5814    884   -794    816       C  
ATOM    915  O   VAL A 124      21.772  76.346  -2.432  1.00 50.45           O  
ANISOU  915  O   VAL A 124     7657   6172   5341    838   -727    810       O  
ATOM    916  CB  VAL A 124      21.053  78.657  -0.378  1.00 43.59           C  
ANISOU  916  CB  VAL A 124     6671   5153   4738    949   -663    912       C  
ATOM    917  N   ALA A 125      19.543  76.202  -2.023  1.00 54.70           N  
ANISOU  917  N   ALA A 125     8011   6754   6019    931   -954    824       N  
ATOM    918  CA  ALA A 125      19.134  75.653  -3.325  1.00 61.06           C  
ANISOU  918  CA  ALA A 125     8901   7612   6687    935  -1091    822       C  
ATOM    919  C   ALA A 125      19.512  74.175  -3.534  1.00 62.89           C  
ANISOU  919  C   ALA A 125     9123   7894   6877    857  -1105    713       C  
ATOM    920  O   ALA A 125      19.148  73.577  -4.546  1.00 70.37           O  
ANISOU  920  O   ALA A 125    10142   8882   7713    857  -1231    690       O  
ATOM    921  CB  ALA A 125      19.691  76.507  -4.472  1.00 59.78           C  
ANISOU  921  CB  ALA A 125     8939   7423   6353    962  -1067    899       C  
ATOM    922  N   LYS A 126      20.241  73.592  -2.591  1.00 60.80           N  
ANISOU  922  N   LYS A 126     8783   7621   6698    795   -983    645       N  
ATOM    923  CA  LYS A 126      20.423  72.142  -2.569  1.00 66.28           C  
ANISOU  923  CA  LYS A 126     9438   8351   7393    729  -1009    541       C  
ATOM    924  C   LYS A 126      19.588  71.578  -1.442  1.00 60.13           C  
ANISOU  924  C   LYS A 126     8461   7587   6798    713  -1058    514       C  
ATOM    925  O   LYS A 126      19.335  72.255  -0.440  1.00 63.26           O  
ANISOU  925  O   LYS A 126     8758   7963   7316    742  -1000    556       O  
ATOM    926  CB  LYS A 126      21.889  71.755  -2.400  1.00 69.24           C  
ANISOU  926  CB  LYS A 126     9872   8711   7726    673   -840    485       C  
ATOM    927  CG  LYS A 126      22.732  72.047  -3.620  1.00 78.25           C  
ANISOU  927  CG  LYS A 126    11202   9855   8673    683   -786    506       C  
ATOM    928  CD  LYS A 126      24.185  72.258  -3.259  1.00 84.68           C  
ANISOU  928  CD  LYS A 126    12046  10645   9482    643   -587    503       C  
ATOM    929  CE  LYS A 126      25.019  72.405  -4.518  1.00 93.42           C  
ANISOU  929  CE  LYS A 126    13331  11771  10393    654   -522    527       C  
ATOM    930  NZ  LYS A 126      24.872  71.193  -5.370  1.00 94.89           N1+
ANISOU  930  NZ  LYS A 126    13589  12006  10460    658   -607    438       N1+
ATOM    931  N   GLU A 127      19.119  70.351  -1.607  1.00 56.00           N  
ANISOU  931  N   GLU A 127     7885   7096   6295    668  -1168    448       N  
ATOM    932  CA  GLU A 127      18.290  69.761  -0.563  1.00 60.02           C  
ANISOU  932  CA  GLU A 127     8199   7624   6983    644  -1215    437       C  
ATOM    933  C   GLU A 127      19.171  69.468   0.645  1.00 53.69           C  
ANISOU  933  C   GLU A 127     7332   6799   6268    600  -1048    395       C  
ATOM    934  O   GLU A 127      20.344  69.109   0.493  1.00 55.33           O  
ANISOU  934  O   GLU A 127     7632   6987   6403    562   -949    340       O  
ATOM    935  CB  GLU A 127      17.579  68.499  -1.069  1.00 71.55           C  
ANISOU  935  CB  GLU A 127     9621   9112   8452    593  -1387    382       C  
ATOM    936  CG  GLU A 127      16.413  68.018  -0.194  1.00 81.48           C  
ANISOU  936  CG  GLU A 127    10663  10398   9899    572  -1472    406       C  
ATOM    937  CD  GLU A 127      15.230  68.981  -0.159  1.00 86.69           C  
ANISOU  937  CD  GLU A 127    11225  11087  10624    651  -1554    508       C  
ATOM    938  OE1 GLU A 127      15.159  69.896  -1.004  1.00 86.58           O  
ANISOU  938  OE1 GLU A 127    11325  11069  10502    718  -1593    556       O  
ATOM    939  OE2 GLU A 127      14.366  68.821   0.727  1.00 86.19           O1-
ANISOU  939  OE2 GLU A 127    10970  11054  10725    652  -1573    546       O1-
ATOM    940  N   MET A 128      18.629  69.663   1.841  1.00 54.02           N  
ANISOU  940  N   MET A 128     7219   6847   6461    614  -1014    426       N  
ATOM    941  CA  MET A 128      19.372  69.327   3.053  1.00 52.14           C  
ANISOU  941  CA  MET A 128     6916   6591   6305    574   -875    388       C  
ATOM    942  C   MET A 128      19.482  67.815   3.096  1.00 45.59           C  
ANISOU  942  C   MET A 128     6044   5773   5504    493   -920    312       C  
ATOM    943  O   MET A 128      18.497  67.136   2.822  1.00 48.08           O  
ANISOU  943  O   MET A 128     6286   6115   5865    473  -1061    313       O  
ATOM    944  CB  MET A 128      18.689  69.872   4.314  1.00 44.60           C  
ANISOU  944  CB  MET A 128     5815   5645   5487    620   -831    439       C  
ATOM    945  CG  MET A 128      19.666  70.417   5.313  1.00 41.04           C  
ANISOU  945  CG  MET A 128     5384   5154   5057    623   -668    427       C  
ATOM    946  SD  MET A 128      19.263  70.234   7.085  1.00 72.39           S  
ANISOU  946  SD  MET A 128     9185   9141   9181    634   -589    433       S  
ATOM    947  CE  MET A 128      17.764  71.172   7.248  1.00 47.84           C  
ANISOU  947  CE  MET A 128     5978   6062   6138    746   -651    521       C  
ATOM    948  N   HIS A 129      20.671  67.295   3.407  1.00 36.93           N  
ANISOU  948  N   HIS A 129     4995   4651   4386    447   -810    251       N  
ATOM    949  CA  HIS A 129      20.890  65.857   3.346  1.00 54.09           C  
ANISOU  949  CA  HIS A 129     7156   6821   6575    378   -851    173       C  
ATOM    950  C   HIS A 129      21.366  65.254   4.686  1.00 53.59           C  
ANISOU  950  C   HIS A 129     6991   6746   6627    335   -751    149       C  
ATOM    951  O   HIS A 129      21.533  65.962   5.669  1.00 59.60           O  
ANISOU  951  O   HIS A 129     7695   7505   7446    359   -651    187       O  
ATOM    952  CB  HIS A 129      21.881  65.520   2.219  1.00 52.72           C  
ANISOU  952  CB  HIS A 129     7154   6631   6248    369   -834    110       C  
ATOM    953  CG  HIS A 129      23.251  66.091   2.413  1.00 49.36           C  
ANISOU  953  CG  HIS A 129     6800   6185   5768    378   -662    106       C  
ATOM    954  CD2 HIS A 129      24.015  66.862   1.607  1.00 51.19           C  
ANISOU  954  CD2 HIS A 129     7165   6413   5871    408   -592    126       C  
ATOM    955  ND1 HIS A 129      24.009  65.849   3.542  1.00 49.74           N  
ANISOU  955  ND1 HIS A 129     6778   6216   5904    347   -545     86       N  
ATOM    956  CE1 HIS A 129      25.167  66.473   3.433  1.00 47.78           C  
ANISOU  956  CE1 HIS A 129     6607   5953   5594    356   -419     93       C  
ATOM    957  NE2 HIS A 129      25.200  67.090   2.265  1.00 51.44           N  
ANISOU  957  NE2 HIS A 129     7192   6425   5929    390   -438    120       N  
ATOM    958  N   VAL A 130      21.588  63.946   4.706  1.00 47.43           N  
ANISOU  958  N   VAL A 130     6200   5950   5873    275   -786     84       N  
ATOM    959  CA  VAL A 130      21.780  63.234   5.959  1.00 48.32           C  
ANISOU  959  CA  VAL A 130     6202   6052   6104    232   -726     73       C  
ATOM    960  C   VAL A 130      23.014  63.695   6.746  1.00 47.21           C  
ANISOU  960  C   VAL A 130     6085   5895   5958    242   -560     64       C  
ATOM    961  O   VAL A 130      23.037  63.587   7.959  1.00 48.94           O  
ANISOU  961  O   VAL A 130     6208   6115   6270    230   -499     82       O  
ATOM    962  CB  VAL A 130      21.872  61.717   5.717  1.00 57.31           C  
ANISOU  962  CB  VAL A 130     7348   7161   7265    166   -802      2       C  
ATOM    963  CG1 VAL A 130      20.513  61.183   5.342  1.00 64.97           C  
ANISOU  963  CG1 VAL A 130     8247   8144   8296    135   -976     23       C  
ATOM    964  CG2 VAL A 130      22.893  61.397   4.637  1.00 60.31           C  
ANISOU  964  CG2 VAL A 130     7894   7514   7507    173   -787    -78       C  
ATOM    965  N   GLY A 131      24.029  64.218   6.071  1.00 47.68           N  
ANISOU  965  N   GLY A 131     6269   5941   5908    263   -490     42       N  
ATOM    966  CA  GLY A 131      25.199  64.722   6.774  1.00 41.76           C  
ANISOU  966  CA  GLY A 131     5533   5174   5162    264   -347     42       C  
ATOM    967  C   GLY A 131      24.842  65.923   7.635  1.00 50.30           C  
ANISOU  967  C   GLY A 131     6560   6257   6293    301   -300    107       C  
ATOM    968  O   GLY A 131      25.232  66.012   8.799  1.00 59.89           O  
ANISOU  968  O   GLY A 131     7717   7462   7575    293   -225    110       O  
ATOM    969  N   HIS A 132      24.083  66.846   7.054  1.00 42.31           N  
ANISOU  969  N   HIS A 132     5577   5255   5242    350   -351    158       N  
ATOM    970  CA  HIS A 132      23.558  67.971   7.790  1.00 44.05           C  
ANISOU  970  CA  HIS A 132     5753   5473   5511    402   -323    218       C  
ATOM    971  C   HIS A 132      22.633  67.467   8.860  1.00 47.62           C  
ANISOU  971  C   HIS A 132     6063   5955   6077    404   -347    233       C  
ATOM    972  O   HIS A 132      22.542  68.056   9.942  1.00 53.78           O  
ANISOU  972  O   HIS A 132     6794   6730   6910    438   -282    258       O  
ATOM    973  CB  HIS A 132      22.807  68.930   6.876  1.00 42.20           C  
ANISOU  973  CB  HIS A 132     5573   5243   5218    461   -390    272       C  
ATOM    974  CG  HIS A 132      23.584  69.357   5.678  1.00 43.20           C  
ANISOU  974  CG  HIS A 132     5845   5349   5219    459   -375    271       C  
ATOM    975  CD2 HIS A 132      24.810  69.923   5.565  1.00 34.81           C  
ANISOU  975  CD2 HIS A 132     4872   4252   4104    444   -270    270       C  
ATOM    976  ND1 HIS A 132      23.093  69.235   4.400  1.00 55.18           N  
ANISOU  976  ND1 HIS A 132     7431   6887   6648    473   -475    279       N  
ATOM    977  CE1 HIS A 132      23.985  69.712   3.542  1.00 51.31           C  
ANISOU  977  CE1 HIS A 132     7074   6378   6043    474   -421    285       C  
ATOM    978  NE2 HIS A 132      25.028  70.142   4.227  1.00 38.45           N  
ANISOU  978  NE2 HIS A 132     5452   4717   4442    453   -294    285       N  
ATOM    979  N   LEU A 133      21.932  66.381   8.553  1.00 45.38           N  
ANISOU  979  N   LEU A 133     5716   5698   5829    368   -443    221       N  
ATOM    980  CA  LEU A 133      21.007  65.830   9.517  1.00 47.72           C  
ANISOU  980  CA  LEU A 133     5864   6027   6241    361   -466    252       C  
ATOM    981  C   LEU A 133      21.799  65.416  10.729  1.00 40.10           C  
ANISOU  981  C   LEU A 133     4868   5048   5322    331   -362    227       C  
ATOM    982  O   LEU A 133      21.474  65.803  11.838  1.00 39.21           O  
ANISOU  982  O   LEU A 133     4682   4953   5265    366   -302    263       O  
ATOM    983  CB  LEU A 133      20.221  64.643   8.966  1.00 53.91           C  
ANISOU  983  CB  LEU A 133     6586   6829   7066    306   -596    243       C  
ATOM    984  CG  LEU A 133      19.290  64.099  10.062  1.00 57.89           C  
ANISOU  984  CG  LEU A 133     6921   7371   7705    290   -602    294       C  
ATOM    985  CD1 LEU A 133      18.384  65.223  10.568  1.00 54.04           C  
ANISOU  985  CD1 LEU A 133     6353   6924   7254    378   -573    371       C  
ATOM    986  CD2 LEU A 133      18.471  62.879   9.613  1.00 52.94           C  
ANISOU  986  CD2 LEU A 133     6217   6752   7146    218   -741    296       C  
ATOM    987  N   ARG A 134      22.861  64.659  10.508  1.00 38.12           N  
ANISOU  987  N   ARG A 134     4679   4766   5038    277   -338    165       N  
ATOM    988  CA  ARG A 134      23.671  64.175  11.617  1.00 46.76           C  
ANISOU  988  CA  ARG A 134     5746   5846   6176    247   -253    142       C  
ATOM    989  C   ARG A 134      24.247  65.368  12.401  1.00 54.20           C  
ANISOU  989  C   ARG A 134     6718   6775   7100    292   -152    158       C  
ATOM    990  O   ARG A 134      24.060  65.470  13.613  1.00 58.21           O  
ANISOU  990  O   ARG A 134     7162   7294   7661    310   -104    180       O  
ATOM    991  CB  ARG A 134      24.793  63.261  11.110  1.00 44.56           C  
ANISOU  991  CB  ARG A 134     5536   5533   5860    196   -245     73       C  
ATOM    992  CG  ARG A 134      24.365  61.803  10.959  1.00 51.91           C  
ANISOU  992  CG  ARG A 134     6421   6458   6845    142   -329     48       C  
ATOM    993  CD  ARG A 134      25.532  60.848  10.969  1.00 47.32           C  
ANISOU  993  CD  ARG A 134     5887   5838   6257    106   -294    -18       C  
ATOM    994  NE  ARG A 134      25.685  60.371  12.335  1.00 46.82           N  
ANISOU  994  NE  ARG A 134     5738   5771   6279     85   -246      3       N  
ATOM    995  CZ  ARG A 134      26.660  59.586  12.761  1.00 56.04           C  
ANISOU  995  CZ  ARG A 134     6918   6908   7468     60   -206    -36       C  
ATOM    996  NH1 ARG A 134      27.598  59.145  11.926  1.00 56.93           N1+
ANISOU  996  NH1 ARG A 134     7115   6990   7526     57   -199   -102       N1+
ATOM    997  NH2 ARG A 134      26.690  59.251  14.037  1.00 58.95           N  
ANISOU  997  NH2 ARG A 134     7213   7279   7907     46   -169     -5       N  
ATOM    998  N   SER A 135      24.924  66.267  11.687  1.00 52.97           N  
ANISOU  998  N   SER A 135     6667   6592   6868    310   -125    148       N  
ATOM    999  CA  SER A 135      25.490  67.508  12.234  1.00 43.17           C  
ANISOU  999  CA  SER A 135     5475   5320   5609    345    -48    163       C  
ATOM   1000  C   SER A 135      24.527  68.258  13.137  1.00 43.38           C  
ANISOU 1000  C   SER A 135     5446   5359   5677    412    -40    207       C  
ATOM   1001  O   SER A 135      24.901  68.781  14.182  1.00 39.92           O  
ANISOU 1001  O   SER A 135     5014   4900   5255    432     23    204       O  
ATOM   1002  CB  SER A 135      25.905  68.446  11.093  1.00 40.61           C  
ANISOU 1002  CB  SER A 135     5261   4967   5202    359    -47    174       C  
ATOM   1003  OG  SER A 135      26.327  69.690  11.620  1.00 43.38           O  
ANISOU 1003  OG  SER A 135     5659   5274   5548    388     11    195       O  
ATOM   1004  N   THR A 136      23.279  68.313  12.700  1.00 38.21           N  
ANISOU 1004  N   THR A 136     4740   4740   5039    451   -107    247       N  
ATOM   1005  CA  THR A 136      22.237  69.000  13.427  1.00 40.29           C  
ANISOU 1005  CA  THR A 136     4939   5027   5344    532    -98    296       C  
ATOM   1006  C   THR A 136      21.947  68.317  14.747  1.00 42.79           C  
ANISOU 1006  C   THR A 136     5152   5379   5728    528    -54    302       C  
ATOM   1007  O   THR A 136      21.865  68.983  15.782  1.00 47.14           O  
ANISOU 1007  O   THR A 136     5699   5926   6285    589     12    312       O  
ATOM   1008  CB  THR A 136      20.942  69.080  12.584  1.00 46.98           C  
ANISOU 1008  CB  THR A 136     5732   5913   6205    571   -191    345       C  
ATOM   1009  CG2 THR A 136      19.849  69.732  13.378  1.00 32.03           C  
ANISOU 1009  CG2 THR A 136     3752   4053   4365    666   -170    400       C  
ATOM   1010  OG1 THR A 136      21.190  69.819  11.364  1.00 45.28           O  
ANISOU 1010  OG1 THR A 136     5629   5665   5913    585   -232    348       O  
ATOM   1011  N   ILE A 137      21.809  66.989  14.722  1.00 41.91           N  
ANISOU 1011  N   ILE A 137     4966   5297   5660    459    -91    296       N  
ATOM   1012  CA  ILE A 137      21.468  66.241  15.932  1.00 33.30           C  
ANISOU 1012  CA  ILE A 137     3772   4243   4636    448    -52    318       C  
ATOM   1013  C   ILE A 137      22.595  66.277  16.938  1.00 36.82           C  
ANISOU 1013  C   ILE A 137     4274   4658   5060    436     32    280       C  
ATOM   1014  O   ILE A 137      22.405  66.657  18.099  1.00 46.74           O  
ANISOU 1014  O   ILE A 137     5507   5931   6322    488     97    299       O  
ATOM   1015  CB  ILE A 137      21.148  64.782  15.665  1.00 38.79           C  
ANISOU 1015  CB  ILE A 137     4388   4958   5392    366   -118    323       C  
ATOM   1016  CG1 ILE A 137      20.280  64.614  14.404  1.00 42.97           C  
ANISOU 1016  CG1 ILE A 137     4891   5503   5932    354   -233    342       C  
ATOM   1017  CG2 ILE A 137      20.498  64.184  16.897  1.00 34.17           C  
ANISOU 1017  CG2 ILE A 137     3680   4420   4882    367    -76    377       C  
ATOM   1018  CD1 ILE A 137      18.965  65.304  14.442  1.00 38.93           C  
ANISOU 1018  CD1 ILE A 137     4289   5043   5461    427   -256    413       C  
ATOM   1019  N   ILE A 138      23.779  65.894  16.487  1.00 33.34           N  
ANISOU 1019  N   ILE A 138     3907   4174   4587    373     28    225       N  
ATOM   1020  CA  ILE A 138      24.934  65.839  17.373  1.00 33.93           C  
ANISOU 1020  CA  ILE A 138     4025   4219   4650    351     90    189       C  
ATOM   1021  C   ILE A 138      25.301  67.231  17.908  1.00 50.26           C  
ANISOU 1021  C   ILE A 138     6168   6254   6674    411    142    182       C  
ATOM   1022  O   ILE A 138      25.470  67.410  19.123  1.00 49.78           O  
ANISOU 1022  O   ILE A 138     6106   6194   6613    437    190    180       O  
ATOM   1023  CB  ILE A 138      26.132  65.206  16.662  1.00 26.16           C  
ANISOU 1023  CB  ILE A 138     3095   3199   3647    281     77    138       C  
ATOM   1024  CG1 ILE A 138      25.742  63.813  16.124  1.00 26.34           C  
ANISOU 1024  CG1 ILE A 138     3061   3238   3710    229     15    134       C  
ATOM   1025  CG2 ILE A 138      27.291  65.030  17.630  1.00 29.15           C  
ANISOU 1025  CG2 ILE A 138     3493   3552   4029    257    129    108       C  
ATOM   1026  CD1 ILE A 138      26.784  63.156  15.249  1.00 26.14           C  
ANISOU 1026  CD1 ILE A 138     3096   3178   3657    180      1     78       C  
ATOM   1027  N   GLY A 139      25.376  68.220  17.015  1.00 43.29           N  
ANISOU 1027  N   GLY A 139     5358   5339   5751    434    127    181       N  
ATOM   1028  CA  GLY A 139      25.691  69.586  17.407  1.00 27.01           C  
ANISOU 1028  CA  GLY A 139     3380   3227   3655    486    162    176       C  
ATOM   1029  C   GLY A 139      24.701  70.191  18.402  1.00 36.19           C  
ANISOU 1029  C   GLY A 139     4515   4411   4827    582    190    202       C  
ATOM   1030  O   GLY A 139      25.101  70.707  19.455  1.00 36.00           O  
ANISOU 1030  O   GLY A 139     4537   4357   4785    612    233    180       O  
ATOM   1031  N   ASP A 140      23.406  70.127  18.092  1.00 38.16           N  
ANISOU 1031  N   ASP A 140     4686   4711   5102    635    166    250       N  
ATOM   1032  CA  ASP A 140      22.375  70.601  19.032  1.00 42.71           C  
ANISOU 1032  CA  ASP A 140     5213   5323   5691    740    208    284       C  
ATOM   1033  C   ASP A 140      22.528  70.018  20.425  1.00 53.79           C  
ANISOU 1033  C   ASP A 140     6579   6758   7100    741    268    276       C  
ATOM   1034  O   ASP A 140      22.320  70.703  21.423  1.00 62.48           O  
ANISOU 1034  O   ASP A 140     7713   7856   8173    827    324    272       O  
ATOM   1035  CB  ASP A 140      20.991  70.245  18.540  1.00 35.41           C  
ANISOU 1035  CB  ASP A 140     4166   4470   4817    775    170    347       C  
ATOM   1036  CG  ASP A 140      19.931  71.185  19.062  1.00 50.34           C  
ANISOU 1036  CG  ASP A 140     6027   6385   6714    910    209    387       C  
ATOM   1037  OD1 ASP A 140      20.174  72.411  19.074  1.00 36.51           O  
ANISOU 1037  OD1 ASP A 140     4385   4568   4918    980    224    364       O  
ATOM   1038  OD2 ASP A 140      18.846  70.694  19.452  1.00 72.53           O1-
ANISOU 1038  OD2 ASP A 140     8702   9278   9579    948    224    445       O1-
ATOM   1039  N   ALA A 141      22.864  68.734  20.482  1.00 52.78           N  
ANISOU 1039  N   ALA A 141     6391   6659   7004    651    255    276       N  
ATOM   1040  CA  ALA A 141      23.001  68.055  21.748  1.00 41.07           C  
ANISOU 1040  CA  ALA A 141     4870   5208   5525    645    306    282       C  
ATOM   1041  C   ALA A 141      24.148  68.689  22.527  1.00 39.29           C  
ANISOU 1041  C   ALA A 141     4765   4922   5241    651    336    223       C  
ATOM   1042  O   ALA A 141      24.074  68.869  23.741  1.00 48.85           O  
ANISOU 1042  O   ALA A 141     5994   6149   6420    707    388    222       O  
ATOM   1043  CB  ALA A 141      23.229  66.566  21.526  1.00 35.09           C  
ANISOU 1043  CB  ALA A 141     4040   4473   4818    542    272    292       C  
ATOM   1044  N   ALA A 142      25.204  69.052  21.813  1.00 34.06           N  
ANISOU 1044  N   ALA A 142     4186   4192   4562    595    301    177       N  
ATOM   1045  CA  ALA A 142      26.378  69.629  22.452  1.00 37.97           C  
ANISOU 1045  CA  ALA A 142     4784   4623   5019    581    311    124       C  
ATOM   1046  C   ALA A 142      26.034  71.018  22.916  1.00 40.89           C  
ANISOU 1046  C   ALA A 142     5240   4952   5345    678    332    111       C  
ATOM   1047  O   ALA A 142      26.458  71.472  23.961  1.00 43.28           O  
ANISOU 1047  O   ALA A 142     5614   5222   5607    710    350     77       O  
ATOM   1048  CB  ALA A 142      27.559  69.650  21.486  1.00 40.64           C  
ANISOU 1048  CB  ALA A 142     5169   4906   5365    491    275     93       C  
ATOM   1049  N   VAL A 143      25.244  71.695  22.104  1.00 47.36           N  
ANISOU 1049  N   VAL A 143     6059   5765   6170    732    321    138       N  
ATOM   1050  CA  VAL A 143      24.747  73.003  22.462  1.00 44.10           C  
ANISOU 1050  CA  VAL A 143     5724   5309   5722    843    339    130       C  
ATOM   1051  C   VAL A 143      23.937  72.960  23.761  1.00 42.10           C  
ANISOU 1051  C   VAL A 143     5441   5112   5444    947    402    140       C  
ATOM   1052  O   VAL A 143      24.226  73.699  24.703  1.00 45.17           O  
ANISOU 1052  O   VAL A 143     5932   5452   5778   1008    425     96       O  
ATOM   1053  CB  VAL A 143      23.899  73.579  21.326  1.00 36.74           C  
ANISOU 1053  CB  VAL A 143     4776   4375   4810    890    313    171       C  
ATOM   1054  CG1 VAL A 143      23.032  74.714  21.838  1.00 37.89           C  
ANISOU 1054  CG1 VAL A 143     4967   4499   4931   1036    343    177       C  
ATOM   1055  CG2 VAL A 143      24.809  74.040  20.195  1.00 30.53           C  
ANISOU 1055  CG2 VAL A 143     4070   3512   4019    812    264    158       C  
ATOM   1056  N   ARG A 144      22.927  72.096  23.800  1.00 37.65           N  
ANISOU 1056  N   ARG A 144     4740   4647   4917    967    429    200       N  
ATOM   1057  CA  ARG A 144      22.116  71.903  24.997  1.00 40.09           C  
ANISOU 1057  CA  ARG A 144     4998   5029   5205   1060    506    229       C  
ATOM   1058  C   ARG A 144      22.953  71.564  26.242  1.00 42.81           C  
ANISOU 1058  C   ARG A 144     5407   5367   5494   1039    535    188       C  
ATOM   1059  O   ARG A 144      22.747  72.138  27.293  1.00 47.00           O  
ANISOU 1059  O   ARG A 144     6004   5897   5957   1141    588    168       O  
ATOM   1060  CB  ARG A 144      21.108  70.798  24.765  1.00 30.51           C  
ANISOU 1060  CB  ARG A 144     3610   3922   4061   1040    519    311       C  
ATOM   1061  CG  ARG A 144      20.047  71.115  23.789  1.00 41.18           C  
ANISOU 1061  CG  ARG A 144     4880   5301   5465   1085    492    361       C  
ATOM   1062  CD  ARG A 144      19.088  69.955  23.722  1.00 31.39           C  
ANISOU 1062  CD  ARG A 144     3460   4164   4303   1051    497    444       C  
ATOM   1063  NE  ARG A 144      18.042  70.152  22.731  1.00 35.01           N  
ANISOU 1063  NE  ARG A 144     3823   4656   4824   1082    449    498       N  
ATOM   1064  CZ  ARG A 144      16.861  70.676  23.007  1.00 43.42           C  
ANISOU 1064  CZ  ARG A 144     4805   5780   5912   1206    497    556       C  
ATOM   1065  NH1 ARG A 144      16.609  71.060  24.250  1.00 45.94           N1+
ANISOU 1065  NH1 ARG A 144     5138   6132   6185   1316    605    561       N1+
ATOM   1066  NH2 ARG A 144      15.942  70.823  22.048  1.00 44.16           N  
ANISOU 1066  NH2 ARG A 144     4805   5905   6071   1228    437    609       N  
ATOM   1067  N   THR A 145      23.874  70.615  26.118  1.00 41.96           N  
ANISOU 1067  N   THR A 145     5281   5252   5408    914    497    176       N  
ATOM   1068  CA  THR A 145      24.735  70.249  27.228  1.00 40.60           C  
ANISOU 1068  CA  THR A 145     5167   5070   5188    887    507    143       C  
ATOM   1069  C   THR A 145      25.573  71.423  27.726  1.00 39.07           C  
ANISOU 1069  C   THR A 145     5137   4782   4926    920    484     64       C  
ATOM   1070  O   THR A 145      25.703  71.657  28.924  1.00 38.71           O  
ANISOU 1070  O   THR A 145     5166   4735   4806    980    511     35       O  
ATOM   1071  CB  THR A 145      25.677  69.092  26.835  1.00 39.68           C  
ANISOU 1071  CB  THR A 145     5006   4950   5121    750    458    141       C  
ATOM   1072  CG2 THR A 145      26.526  68.627  28.026  1.00 34.98           C  
ANISOU 1072  CG2 THR A 145     4459   4353   4481    726    460    117       C  
ATOM   1073  OG1 THR A 145      24.895  67.987  26.373  1.00 47.05           O  
ANISOU 1073  OG1 THR A 145     5801   5955   6120    714    465    209       O  
ATOM   1074  N   LEU A 146      26.170  72.156  26.810  1.00 39.84           N  
ANISOU 1074  N   LEU A 146     5295   4795   5046    875    428     30       N  
ATOM   1075  CA  LEU A 146      27.047  73.237  27.219  1.00 45.81           C  
ANISOU 1075  CA  LEU A 146     6203   5447   5758    882    391    -40       C  
ATOM   1076  C   LEU A 146      26.191  74.355  27.809  1.00 46.39           C  
ANISOU 1076  C   LEU A 146     6362   5496   5769   1032    429    -59       C  
ATOM   1077  O   LEU A 146      26.601  75.091  28.692  1.00 42.72           O  
ANISOU 1077  O   LEU A 146     6029   4966   5238   1079    416   -121       O  
ATOM   1078  CB  LEU A 146      27.865  73.727  26.028  1.00 50.22           C  
ANISOU 1078  CB  LEU A 146     6794   5923   6365    790    330    -54       C  
ATOM   1079  CG  LEU A 146      28.869  72.729  25.444  1.00 37.80           C  
ANISOU 1079  CG  LEU A 146     5153   4364   4845    653    298    -45       C  
ATOM   1080  CD1 LEU A 146      29.242  73.145  24.017  1.00 32.96           C  
ANISOU 1080  CD1 LEU A 146     4545   3703   4275    590    268    -32       C  
ATOM   1081  CD2 LEU A 146      30.092  72.700  26.291  1.00 31.08           C  
ANISOU 1081  CD2 LEU A 146     4363   3469   3979    595    260    -93       C  
ATOM   1082  N   GLU A 147      24.978  74.470  27.304  1.00 49.53           N  
ANISOU 1082  N   GLU A 147     6684   5945   6190   1113    473     -7       N  
ATOM   1083  CA  GLU A 147      24.065  75.455  27.817  1.00 53.27           C  
ANISOU 1083  CA  GLU A 147     7219   6407   6613   1274    521    -18       C  
ATOM   1084  C   GLU A 147      23.671  75.098  29.239  1.00 58.70           C  
ANISOU 1084  C   GLU A 147     7913   7167   7224   1364    597    -21       C  
ATOM   1085  O   GLU A 147      23.612  75.977  30.111  1.00 55.06           O  
ANISOU 1085  O   GLU A 147     7585   6658   6679   1477    619    -78       O  
ATOM   1086  CB  GLU A 147      22.842  75.568  26.916  1.00 52.75           C  
ANISOU 1086  CB  GLU A 147     7047   6394   6604   1340    546     51       C  
ATOM   1087  CG  GLU A 147      23.098  76.522  25.773  1.00 65.09           C  
ANISOU 1087  CG  GLU A 147     8679   7853   8198   1319    480     39       C  
ATOM   1088  CD  GLU A 147      21.847  76.942  25.052  1.00 64.10           C  
ANISOU 1088  CD  GLU A 147     8484   7762   8110   1420    496     97       C  
ATOM   1089  OE1 GLU A 147      20.834  76.198  25.104  1.00 65.15           O  
ANISOU 1089  OE1 GLU A 147     8465   8014   8275   1460    543    162       O  
ATOM   1090  OE2 GLU A 147      21.887  78.039  24.459  1.00 54.78           O1-
ANISOU 1090  OE2 GLU A 147     7399   6483   6930   1460    457     83       O1-
ATOM   1091  N   PHE A 148      23.411  73.813  29.474  1.00 43.25           N  
ANISOU 1091  N   PHE A 148     5822   5321   5291   1316    635     40       N  
ATOM   1092  CA  PHE A 148      23.075  73.376  30.806  1.00 44.24           C  
ANISOU 1092  CA  PHE A 148     5948   5523   5340   1390    713     52       C  
ATOM   1093  C   PHE A 148      24.266  73.581  31.732  1.00 47.57           C  
ANISOU 1093  C   PHE A 148     6524   5873   5676   1359    667    -30       C  
ATOM   1094  O   PHE A 148      24.112  73.933  32.875  1.00 45.32           O  
ANISOU 1094  O   PHE A 148     6337   5598   5286   1465    713    -62       O  
ATOM   1095  CB  PHE A 148      22.643  71.906  30.846  1.00 49.68           C  
ANISOU 1095  CB  PHE A 148     6463   6330   6082   1324    754    144       C  
ATOM   1096  CG  PHE A 148      22.379  71.413  32.249  1.00 59.70           C  
ANISOU 1096  CG  PHE A 148     7739   7679   7264   1391    839    171       C  
ATOM   1097  CD1 PHE A 148      21.313  71.932  32.996  1.00 57.57           C  
ANISOU 1097  CD1 PHE A 148     7473   7472   6927   1561    948    196       C  
ATOM   1098  CD2 PHE A 148      23.230  70.493  32.849  1.00 64.89           C  
ANISOU 1098  CD2 PHE A 148     8410   8346   7899   1298    812    170       C  
ATOM   1099  CE1 PHE A 148      21.078  71.507  34.302  1.00 57.10           C  
ANISOU 1099  CE1 PHE A 148     7432   7494   6771   1631   1039    225       C  
ATOM   1100  CE2 PHE A 148      23.002  70.056  34.161  1.00 69.03           C  
ANISOU 1100  CE2 PHE A 148     8955   8944   8330   1363    890    202       C  
ATOM   1101  CZ  PHE A 148      21.922  70.565  34.886  1.00 64.69           C  
ANISOU 1101  CZ  PHE A 148     8411   8463   7703   1529   1007    230       C  
ATOM   1102  N   LEU A 149      25.466  73.364  31.230  1.00 47.50           N  
ANISOU 1102  N   LEU A 149     6540   5796   5712   1216    573    -63       N  
ATOM   1103  CA  LEU A 149      26.632  73.505  32.075  1.00 36.42           C  
ANISOU 1103  CA  LEU A 149     5265   4329   4245   1174    512   -134       C  
ATOM   1104  C   LEU A 149      26.875  74.957  32.426  1.00 43.29           C  
ANISOU 1104  C   LEU A 149     6317   5082   5048   1252    474   -222       C  
ATOM   1105  O   LEU A 149      27.678  75.247  33.316  1.00 51.13           O  
ANISOU 1105  O   LEU A 149     7441   6018   5969   1246    420   -290       O  
ATOM   1106  CB  LEU A 149      27.865  72.895  31.397  1.00 45.35           C  
ANISOU 1106  CB  LEU A 149     6353   5421   5457   1003    425   -139       C  
ATOM   1107  CG  LEU A 149      28.183  71.446  31.788  1.00 50.18           C  
ANISOU 1107  CG  LEU A 149     6867   6114   6085    929    432    -92       C  
ATOM   1108  CD1 LEU A 149      28.545  71.355  33.231  1.00 43.73           C  
ANISOU 1108  CD1 LEU A 149     6146   5307   5162    972    430   -123       C  
ATOM   1109  CD2 LEU A 149      27.000  70.562  31.541  1.00 59.61           C  
ANISOU 1109  CD2 LEU A 149     7913   7418   7317    958    515     -2       C  
ATOM   1110  N   GLY A 150      26.209  75.877  31.719  1.00 46.15           N  
ANISOU 1110  N   GLY A 150     6697   5400   5437   1323    489   -222       N  
ATOM   1111  CA  GLY A 150      26.262  77.286  32.082  1.00 40.24           C  
ANISOU 1111  CA  GLY A 150     6130   4532   4626   1419    460   -303       C  
ATOM   1112  C   GLY A 150      26.772  78.244  31.035  1.00 50.79           C  
ANISOU 1112  C   GLY A 150     7528   5737   6034   1356    378   -328       C  
ATOM   1113  O   GLY A 150      26.548  79.448  31.115  1.00 60.15           O  
ANISOU 1113  O   GLY A 150     8847   6818   7188   1449    361   -377       O  
ATOM   1114  N   HIS A 151      27.454  77.716  30.034  1.00 51.33           N  
ANISOU 1114  N   HIS A 151     7503   5804   6197   1202    331   -289       N  
ATOM   1115  CA  HIS A 151      28.188  78.567  29.103  1.00 47.47           C  
ANISOU 1115  CA  HIS A 151     7078   5188   5770   1117    251   -306       C  
ATOM   1116  C   HIS A 151      27.336  79.437  28.211  1.00 48.22           C  
ANISOU 1116  C   HIS A 151     7186   5241   5895   1198    270   -277       C  
ATOM   1117  O   HIS A 151      26.164  79.144  27.960  1.00 57.33           O  
ANISOU 1117  O   HIS A 151     8244   6488   7052   1291    342   -224       O  
ATOM   1118  CB  HIS A 151      29.086  77.702  28.250  1.00 40.63           C  
ANISOU 1118  CB  HIS A 151     6099   4350   4987    947    216   -265       C  
ATOM   1119  CG  HIS A 151      30.010  76.869  29.063  1.00 44.46           C  
ANISOU 1119  CG  HIS A 151     6569   4867   5456    866    186   -289       C  
ATOM   1120  CD2 HIS A 151      30.026  75.544  29.316  1.00 49.85           C  
ANISOU 1120  CD2 HIS A 151     7134   5662   6145    828    218   -254       C  
ATOM   1121  ND1 HIS A 151      31.056  77.412  29.776  1.00 46.99           N  
ANISOU 1121  ND1 HIS A 151     7010   5091   5752    819    103   -356       N  
ATOM   1122  CE1 HIS A 151      31.694  76.449  30.416  1.00 46.16           C  
ANISOU 1122  CE1 HIS A 151     6857   5045   5638    758     86   -359       C  
ATOM   1123  NE2 HIS A 151      31.089  75.306  30.155  1.00 56.39           N  
ANISOU 1123  NE2 HIS A 151     8011   6464   6950    765    158   -296       N  
ATOM   1124  N   LYS A 152      27.931  80.531  27.749  1.00 38.98           N  
ANISOU 1124  N   LYS A 152     6135   3926   4751   1159    199   -306       N  
ATOM   1125  CA  LYS A 152      27.317  81.284  26.670  1.00 38.93           C  
ANISOU 1125  CA  LYS A 152     6133   3870   4787   1204    202   -262       C  
ATOM   1126  C   LYS A 152      27.625  80.507  25.426  1.00 47.98           C  
ANISOU 1126  C   LYS A 152     7143   5080   6007   1073    198   -189       C  
ATOM   1127  O   LYS A 152      28.758  80.558  24.940  1.00 48.68           O  
ANISOU 1127  O   LYS A 152     7250   5108   6139    934    144   -189       O  
ATOM   1128  CB  LYS A 152      27.865  82.707  26.564  1.00 41.73           C  
ANISOU 1128  CB  LYS A 152     6667   4038   5150   1199    126   -307       C  
ATOM   1129  CG  LYS A 152      27.271  83.476  25.403  1.00 46.27           C  
ANISOU 1129  CG  LYS A 152     7252   4558   5769   1241    124   -250       C  
ATOM   1130  CD  LYS A 152      27.899  84.854  25.222  1.00 58.30           C  
ANISOU 1130  CD  LYS A 152     8954   5882   7315   1214     42   -281       C  
ATOM   1131  CE  LYS A 152      27.388  85.518  23.939  1.00 69.48           C  
ANISOU 1131  CE  LYS A 152    10372   7249   8778   1239     37   -205       C  
ATOM   1132  NZ  LYS A 152      27.514  87.013  23.945  1.00 78.35           N1+
ANISOU 1132  NZ  LYS A 152    11687   8170   9910   1286    -27   -234       N1+
ATOM   1133  N   VAL A 153      26.647  79.745  24.947  1.00 43.30           N  
ANISOU 1133  N   VAL A 153     6411   4613   5429   1118    254   -129       N  
ATOM   1134  CA  VAL A 153      26.796  79.033  23.700  1.00 35.33           C  
ANISOU 1134  CA  VAL A 153     5288   3660   4477   1014    246    -66       C  
ATOM   1135  C   VAL A 153      26.250  79.850  22.529  1.00 52.44           C  
ANISOU 1135  C   VAL A 153     7480   5778   6668   1052    228    -18       C  
ATOM   1136  O   VAL A 153      25.070  80.204  22.505  1.00 53.79           O  
ANISOU 1136  O   VAL A 153     7633   5975   6830   1185    255      6       O  
ATOM   1137  CB  VAL A 153      26.088  77.682  23.722  1.00 46.00           C  
ANISOU 1137  CB  VAL A 153     6476   5165   5838   1019    295    -24       C  
ATOM   1138  CG1 VAL A 153      26.518  76.843  22.476  1.00 38.33           C  
ANISOU 1138  CG1 VAL A 153     5411   4237   4917    891    272     20       C  
ATOM   1139  CG2 VAL A 153      26.415  76.936  25.001  1.00 60.35           C  
ANISOU 1139  CG2 VAL A 153     8277   7033   7621   1010    321    -61       C  
ATOM   1140  N   ILE A 154      27.118  80.133  21.555  1.00 49.94           N  
ANISOU 1140  N   ILE A 154     7197   5394   6382    939    186      4       N  
ATOM   1141  CA  ILE A 154      26.705  80.775  20.312  1.00 45.52           C  
ANISOU 1141  CA  ILE A 154     6659   4797   5840    957    165     63       C  
ATOM   1142  C   ILE A 154      26.502  79.794  19.155  1.00 43.22           C  
ANISOU 1142  C   ILE A 154     6245   4612   5565    895    170    123       C  
ATOM   1143  O   ILE A 154      27.462  79.355  18.533  1.00 50.84           O  
ANISOU 1143  O   ILE A 154     7194   5579   6543    770    161    134       O  
ATOM   1144  CB  ILE A 154      27.744  81.805  19.837  1.00 51.36           C  
ANISOU 1144  CB  ILE A 154     7526   5390   6597    874    119     67       C  
ATOM   1145  CG1 ILE A 154      28.022  82.856  20.905  1.00 52.16           C  
ANISOU 1145  CG1 ILE A 154     7773   5360   6687    923     91      1       C  
ATOM   1146  CG2 ILE A 154      27.288  82.471  18.551  1.00 33.56           C  
ANISOU 1146  CG2 ILE A 154     5303   3097   4350    899    100    139       C  
ATOM   1147  CD1 ILE A 154      29.115  83.803  20.482  1.00 53.58           C  
ANISOU 1147  CD1 ILE A 154     8067   5389   6902    817     36     11       C  
ATOM   1148  N   ARG A 155      25.258  79.475  18.840  1.00 44.67           N  
ANISOU 1148  N   ARG A 155     6343   4880   5748    985    181    161       N  
ATOM   1149  CA  ARG A 155      24.968  78.673  17.651  1.00 46.69           C  
ANISOU 1149  CA  ARG A 155     6505   5220   6014    934    164    214       C  
ATOM   1150  C   ARG A 155      25.438  79.348  16.372  1.00 44.11           C  
ANISOU 1150  C   ARG A 155     6260   4823   5677    883    128    256       C  
ATOM   1151  O   ARG A 155      25.057  80.463  16.102  1.00 49.08           O  
ANISOU 1151  O   ARG A 155     6975   5373   6302    956    107    283       O  
ATOM   1152  CB  ARG A 155      23.475  78.407  17.552  1.00 40.42           C  
ANISOU 1152  CB  ARG A 155     5610   4515   5233   1045    164    253       C  
ATOM   1153  CG  ARG A 155      22.930  77.709  18.764  1.00 46.56           C  
ANISOU 1153  CG  ARG A 155     6295   5374   6021   1096    213    230       C  
ATOM   1154  CD  ARG A 155      21.434  77.895  18.835  1.00 51.15           C  
ANISOU 1154  CD  ARG A 155     6794   6017   6622   1235    223    276       C  
ATOM   1155  NE  ARG A 155      20.868  77.091  19.904  1.00 54.42           N  
ANISOU 1155  NE  ARG A 155     7099   6529   7050   1274    281    273       N  
ATOM   1156  CZ  ARG A 155      20.990  77.382  21.195  1.00 50.75           C  
ANISOU 1156  CZ  ARG A 155     6684   6046   6552   1339    340    229       C  
ATOM   1157  NH1 ARG A 155      21.663  78.464  21.583  1.00 48.48           N1+
ANISOU 1157  NH1 ARG A 155     6557   5639   6225   1368    337    174       N1+
ATOM   1158  NH2 ARG A 155      20.438  76.590  22.102  1.00 43.44           N  
ANISOU 1158  NH2 ARG A 155     5652   5220   5632   1373    400    242       N  
ATOM   1159  N   ALA A 156      26.234  78.656  15.572  1.00 47.81           N  
ANISOU 1159  N   ALA A 156     6702   5322   6139    766    125    268       N  
ATOM   1160  CA  ALA A 156      26.706  79.205  14.308  1.00 37.37           C  
ANISOU 1160  CA  ALA A 156     5454   3950   4794    716    105    319       C  
ATOM   1161  C   ALA A 156      26.336  78.328  13.099  1.00 42.26           C  
ANISOU 1161  C   ALA A 156     6009   4664   5384    690     85    356       C  
ATOM   1162  O   ALA A 156      27.162  77.565  12.612  1.00 46.06           O  
ANISOU 1162  O   ALA A 156     6469   5182   5851    595    103    347       O  
ATOM   1163  CB  ALA A 156      28.209  79.392  14.371  1.00 34.25           C  
ANISOU 1163  CB  ALA A 156     5116   3488   4410    597    128    304       C  
ATOM   1164  N   ASN A 157      25.103  78.439  12.617  1.00 47.99           N  
ANISOU 1164  N   ASN A 157     6706   5428   6099    780     43    394       N  
ATOM   1165  CA  ASN A 157      24.678  77.732  11.402  1.00 51.57           C  
ANISOU 1165  CA  ASN A 157     7119   5959   6517    761      0    428       C  
ATOM   1166  C   ASN A 157      25.368  78.250  10.133  1.00 49.46           C  
ANISOU 1166  C   ASN A 157     6958   5645   6188    710     -7    476       C  
ATOM   1167  O   ASN A 157      24.876  79.169   9.464  1.00 49.80           O  
ANISOU 1167  O   ASN A 157     7074   5644   6204    770    -45    535       O  
ATOM   1168  CB  ASN A 157      23.161  77.826  11.213  1.00 42.48           C  
ANISOU 1168  CB  ASN A 157     5906   4856   5380    872    -58    465       C  
ATOM   1169  CG  ASN A 157      22.628  76.703  10.361  1.00 33.87           C  
ANISOU 1169  CG  ASN A 157     4734   3865   4271    842   -115    475       C  
ATOM   1170  ND2 ASN A 157      21.320  76.512  10.355  1.00 38.39           N  
ANISOU 1170  ND2 ASN A 157     5212   4497   4878    918   -171    504       N  
ATOM   1171  OD1 ASN A 157      23.397  76.010   9.712  1.00 41.40           O  
ANISOU 1171  OD1 ASN A 157     5708   4838   5183    751   -111    457       O  
ATOM   1172  N   HIS A 158      26.491  77.620   9.801  1.00 46.81           N  
ANISOU 1172  N   HIS A 158     6629   5327   5829    606     34    455       N  
ATOM   1173  CA  HIS A 158      27.400  78.074   8.744  1.00 46.10           C  
ANISOU 1173  CA  HIS A 158     6635   5198   5681    545     58    503       C  
ATOM   1174  C   HIS A 158      26.884  77.734   7.351  1.00 40.79           C  
ANISOU 1174  C   HIS A 158     5988   4586   4926    563     12    544       C  
ATOM   1175  O   HIS A 158      27.469  76.937   6.625  1.00 43.35           O  
ANISOU 1175  O   HIS A 158     6314   4963   5195    505     34    532       O  
ATOM   1176  CB  HIS A 158      28.770  77.442   8.968  1.00 54.22           C  
ANISOU 1176  CB  HIS A 158     7641   6237   6723    439    128    466       C  
ATOM   1177  CG  HIS A 158      29.893  78.137   8.267  1.00 47.53           C  
ANISOU 1177  CG  HIS A 158     6880   5332   5846    370    178    520       C  
ATOM   1178  CD2 HIS A 158      30.568  77.814   7.139  1.00 36.81           C  
ANISOU 1178  CD2 HIS A 158     5554   4014   4420    319    219    555       C  
ATOM   1179  ND1 HIS A 158      30.459  79.301   8.742  1.00 47.88           N  
ANISOU 1179  ND1 HIS A 158     6989   5267   5937    344    195    550       N  
ATOM   1180  CE1 HIS A 158      31.443  79.659   7.935  1.00 44.31           C  
ANISOU 1180  CE1 HIS A 158     6590   4789   5456    270    245    610       C  
ATOM   1181  NE2 HIS A 158      31.525  78.777   6.954  1.00 41.56           N  
ANISOU 1181  NE2 HIS A 158     6223   4535   5033    260    269    615       N  
ATOM   1182  N   VAL A 159      25.778  78.347   6.977  1.00 39.14           N  
ANISOU 1182  N   VAL A 159     5803   4366   4701    652    -57    590       N  
ATOM   1183  CA  VAL A 159      25.122  77.984   5.738  1.00 45.72           C  
ANISOU 1183  CA  VAL A 159     6656   5262   5455    678   -126    624       C  
ATOM   1184  C   VAL A 159      25.938  78.338   4.476  1.00 51.80           C  
ANISOU 1184  C   VAL A 159     7549   6012   6120    632    -98    681       C  
ATOM   1185  O   VAL A 159      26.465  79.445   4.357  1.00 56.71           O  
ANISOU 1185  O   VAL A 159     8263   6548   6738    623    -61    741       O  
ATOM   1186  CB  VAL A 159      23.745  78.653   5.669  1.00 41.97           C  
ANISOU 1186  CB  VAL A 159     6171   4777   4998    791   -213    671       C  
ATOM   1187  CG1 VAL A 159      23.074  78.358   4.349  1.00 50.49           C  
ANISOU 1187  CG1 VAL A 159     7279   5914   5990    817   -305    712       C  
ATOM   1188  CG2 VAL A 159      22.890  78.182   6.817  1.00 39.33           C  
ANISOU 1188  CG2 VAL A 159     5702   4484   4758    841   -229    624       C  
ATOM   1189  N   GLY A 160      26.029  77.379   3.547  1.00 46.88           N  
ANISOU 1189  N   GLY A 160     6931   5468   5412    604   -115    664       N  
ATOM   1190  CA  GLY A 160      26.596  77.595   2.227  1.00 46.17           C  
ANISOU 1190  CA  GLY A 160     6960   5384   5197    581    -93    720       C  
ATOM   1191  C   GLY A 160      25.694  78.467   1.367  1.00 48.13           C  
ANISOU 1191  C   GLY A 160     7296   5611   5380    658   -181    805       C  
ATOM   1192  O   GLY A 160      24.920  77.972   0.537  1.00 47.67           O  
ANISOU 1192  O   GLY A 160     7251   5616   5245    698   -274    806       O  
ATOM   1193  N   ASP A 161      25.792  79.775   1.575  1.00 39.95           N  
ANISOU 1193  N   ASP A 161     6324   4479   4378    681   -161    876       N  
ATOM   1194  CA  ASP A 161      24.943  80.730   0.869  1.00 44.96           C  
ANISOU 1194  CA  ASP A 161     7043   5075   4965    764   -244    965       C  
ATOM   1195  C   ASP A 161      25.756  81.635  -0.046  1.00 40.44           C  
ANISOU 1195  C   ASP A 161     6621   4442   4304    731   -188   1068       C  
ATOM   1196  O   ASP A 161      25.365  82.757  -0.319  1.00 63.99           O  
ANISOU 1196  O   ASP A 161     9688   7346   7281    786   -227   1155       O  
ATOM   1197  CB  ASP A 161      24.123  81.570   1.864  1.00 46.96           C  
ANISOU 1197  CB  ASP A 161     7253   5254   5335    846   -285    972       C  
ATOM   1198  CG  ASP A 161      24.974  82.534   2.689  1.00 50.42           C  
ANISOU 1198  CG  ASP A 161     7735   5572   5849    809   -201    985       C  
ATOM   1199  OD1 ASP A 161      26.200  82.320   2.876  1.00 48.79           O  
ANISOU 1199  OD1 ASP A 161     7537   5354   5648    706   -107    964       O  
ATOM   1200  OD2 ASP A 161      24.386  83.520   3.180  1.00 58.65           O1-
ANISOU 1200  OD2 ASP A 161     8803   6528   6953    889   -236   1013       O1-
ATOM   1201  N   TRP A 162      26.883  81.136  -0.526  1.00 56.00           N  
ANISOU 1201  N   TRP A 162     8622   6450   6206    646    -92   1063       N  
ATOM   1202  CA  TRP A 162      27.719  81.890  -1.453  1.00 61.53           C  
ANISOU 1202  CA  TRP A 162     9453   7110   6815    606    -21   1171       C  
ATOM   1203  C   TRP A 162      28.495  80.961  -2.395  1.00 71.04           C  
ANISOU 1203  C   TRP A 162    10690   8415   7888    558     52   1159       C  
ATOM   1204  O   TRP A 162      28.847  79.850  -2.014  1.00 85.40           O  
ANISOU 1204  O   TRP A 162    12419  10301   9730    523     87   1059       O  
ATOM   1205  CB  TRP A 162      28.677  82.790  -0.674  1.00 66.67           C  
ANISOU 1205  CB  TRP A 162    10109   7649   7575    535     70   1208       C  
ATOM   1206  CG  TRP A 162      29.029  83.978  -1.455  1.00 87.35           C  
ANISOU 1206  CG  TRP A 162    12865  10184  10140    523     97   1347       C  
ATOM   1207  CD1 TRP A 162      30.248  84.289  -1.976  1.00 97.73           C  
ANISOU 1207  CD1 TRP A 162    14236  11481  11416    431    214   1428       C  
ATOM   1208  CD2 TRP A 162      28.138  85.010  -1.875  1.00 87.53           C  
ANISOU 1208  CD2 TRP A 162    12987  10132  10139    607      5   1435       C  
ATOM   1209  CE2 TRP A 162      28.879  85.937  -2.631  1.00 89.47           C  
ANISOU 1209  CE2 TRP A 162    13358  10307  10330    557     70   1571       C  
ATOM   1210  CE3 TRP A 162      26.772  85.254  -1.679  1.00 87.15           C  
ANISOU 1210  CE3 TRP A 162    12927  10069  10117    725   -124   1420       C  
ATOM   1211  NE1 TRP A 162      30.178  85.472  -2.676  1.00 95.61           N  
ANISOU 1211  NE1 TRP A 162    14101  11124  11101    445    202   1566       N  
ATOM   1212  CZ2 TRP A 162      28.327  87.083  -3.184  1.00 91.87           C  
ANISOU 1212  CZ2 TRP A 162    13787  10517  10602    618      5   1689       C  
ATOM   1213  CZ3 TRP A 162      26.211  86.397  -2.232  1.00 95.00           C  
ANISOU 1213  CZ3 TRP A 162    14038  10975  11081    794   -190   1533       C  
ATOM   1214  CH2 TRP A 162      26.990  87.297  -2.975  1.00 95.31           C  
ANISOU 1214  CH2 TRP A 162    14215  10936  11063    741   -129   1665       C  
ATOM   1215  N   GLY A 163      28.749  81.389  -3.626  1.00 74.95           N  
ANISOU 1215  N   GLY A 163    11318   8919   8239    564     77   1259       N  
ATOM   1216  CA  GLY A 163      29.463  80.533  -4.561  1.00 67.50           C  
ANISOU 1216  CA  GLY A 163    10421   8075   7153    537    155   1246       C  
ATOM   1217  C   GLY A 163      29.107  80.824  -5.999  1.00 73.35           C  
ANISOU 1217  C   GLY A 163    11319   8851   7700    592    115   1336       C  
ATOM   1218  O   GLY A 163      28.113  81.485  -6.277  1.00 83.27           O  
ANISOU 1218  O   GLY A 163    12633  10069   8936    660     -5   1392       O  
ATOM   1219  N   THR A 164      29.920  80.326  -6.922  1.00 70.70           N  
ANISOU 1219  N   THR A 164    11056   8591   7216    571    216   1352       N  
ATOM   1220  CA  THR A 164      29.708  80.586  -8.343  1.00 70.99           C  
ANISOU 1220  CA  THR A 164    11263   8669   7040    624    194   1442       C  
ATOM   1221  C   THR A 164      28.361  80.055  -8.823  1.00 72.47           C  
ANISOU 1221  C   THR A 164    11487   8905   7142    714      3   1382       C  
ATOM   1222  O   THR A 164      27.811  80.525  -9.818  1.00 73.84           O  
ANISOU 1222  O   THR A 164    11798   9087   7171    774    -76   1466       O  
ATOM   1223  CB  THR A 164      30.824  79.964  -9.190  1.00 68.22           C  
ANISOU 1223  CB  THR A 164    10976   8408   6535    599    349   1448       C  
ATOM   1224  N   GLN A 165      27.834  79.077  -8.100  1.00 76.24           N  
ANISOU 1224  N   GLN A 165    11839   9414   7714    718    -78   1244       N  
ATOM   1225  CA  GLN A 165      26.594  78.405  -8.478  1.00 82.38           C  
ANISOU 1225  CA  GLN A 165    12623  10242   8435    785   -265   1175       C  
ATOM   1226  C   GLN A 165      25.384  79.342  -8.534  1.00 80.26           C  
ANISOU 1226  C   GLN A 165    12373   9921   8200    853   -419   1255       C  
ATOM   1227  O   GLN A 165      24.421  79.097  -9.254  1.00 73.35           O  
ANISOU 1227  O   GLN A 165    11553   9088   7228    916   -577   1251       O  
ATOM   1228  CB  GLN A 165      26.303  77.251  -7.504  1.00 80.23           C  
ANISOU 1228  CB  GLN A 165    12188   9997   8299    760   -309   1027       C  
ATOM   1229  CG  GLN A 165      25.974  77.683  -6.087  1.00 86.64           C  
ANISOU 1229  CG  GLN A 165    12843  10739   9335    742   -317   1015       C  
ATOM   1230  CD  GLN A 165      27.196  78.002  -5.229  1.00 99.03           C  
ANISOU 1230  CD  GLN A 165    14353  12259  11012    667   -143   1022       C  
ATOM   1231  NE2 GLN A 165      26.954  78.476  -4.003  1.00101.73           N  
ANISOU 1231  NE2 GLN A 165    14585  12534  11532    657   -149   1014       N  
ATOM   1232  OE1 GLN A 165      28.333  77.818  -5.654  1.00 99.13           O  
ANISOU 1232  OE1 GLN A 165    14418  12298  10951    621     -8   1035       O  
ATOM   1233  N   PHE A 166      25.426  80.408  -7.754  1.00 81.37           N  
ANISOU 1233  N   PHE A 166    12467   9966   8482    845   -380   1324       N  
ATOM   1234  CA  PHE A 166      24.282  81.291  -7.674  1.00 83.37           C  
ANISOU 1234  CA  PHE A 166    12724  10164   8791    923   -518   1392       C  
ATOM   1235  C   PHE A 166      23.991  81.971  -9.004  1.00 77.73           C  
ANISOU 1235  C   PHE A 166    12188   9450   7894    981   -583   1516       C  
ATOM   1236  O   PHE A 166      22.826  82.148  -9.367  1.00 76.27           O  
ANISOU 1236  O   PHE A 166    12018   9274   7687   1064   -753   1542       O  
ATOM   1237  CB  PHE A 166      24.491  82.327  -6.581  1.00 86.01           C  
ANISOU 1237  CB  PHE A 166    12996  10382   9302    908   -453   1435       C  
ATOM   1238  CG  PHE A 166      24.036  81.861  -5.247  1.00 84.59           C  
ANISOU 1238  CG  PHE A 166    12638  10197   9305    906   -479   1327       C  
ATOM   1239  CD1 PHE A 166      22.690  81.891  -4.921  1.00 86.03           C  
ANISOU 1239  CD1 PHE A 166    12739  10385   9562    992   -626   1311       C  
ATOM   1240  CD2 PHE A 166      24.938  81.358  -4.331  1.00 85.90           C  
ANISOU 1240  CD2 PHE A 166    12711  10360   9565    824   -357   1248       C  
ATOM   1241  CE1 PHE A 166      22.247  81.445  -3.693  1.00 86.56           C  
ANISOU 1241  CE1 PHE A 166    12639  10458   9790    995   -639   1221       C  
ATOM   1242  CE2 PHE A 166      24.504  80.904  -3.090  1.00 91.64           C  
ANISOU 1242  CE2 PHE A 166    13283  11089  10448    827   -380   1154       C  
ATOM   1243  CZ  PHE A 166      23.152  80.949  -2.772  1.00 89.43           C  
ANISOU 1243  CZ  PHE A 166    12927  10817  10236    913   -515   1142       C  
ATOM   1244  N   GLY A 167      25.048  82.321  -9.732  1.00 66.34           N  
ANISOU 1244  N   GLY A 167    10878   8004   6323    940   -448   1599       N  
ATOM   1245  CA  GLY A 167      24.902  83.004 -10.999  1.00 66.57           C  
ANISOU 1245  CA  GLY A 167    11094   8035   6166    991   -487   1732       C  
ATOM   1246  C   GLY A 167      23.927  82.261 -11.879  1.00 69.02           C  
ANISOU 1246  C   GLY A 167    11460   8438   6327   1064   -664   1685       C  
ATOM   1247  O   GLY A 167      23.037  82.855 -12.491  1.00 70.37           O  
ANISOU 1247  O   GLY A 167    11712   8593   6431   1143   -809   1768       O  
ATOM   1248  N   MET A 168      24.089  80.945 -11.899  1.00 65.11           N  
ANISOU 1248  N   MET A 168    10917   8032   5790   1037   -663   1547       N  
ATOM   1249  CA  MET A 168      23.205  80.050 -12.630  1.00 72.51           C  
ANISOU 1249  CA  MET A 168    11895   9053   6604   1089   -843   1472       C  
ATOM   1250  C   MET A 168      21.805  80.024 -12.022  1.00 72.04           C  
ANISOU 1250  C   MET A 168    11696   8976   6700   1136  -1044   1437       C  
ATOM   1251  O   MET A 168      20.797  80.179 -12.730  1.00 63.72           O  
ANISOU 1251  O   MET A 168    10702   7943   5565   1208  -1230   1477       O  
ATOM   1252  CB  MET A 168      23.799  78.644 -12.639  1.00 84.73           C  
ANISOU 1252  CB  MET A 168    13416  10677   8100   1042   -782   1325       C  
ATOM   1253  CG  MET A 168      22.852  77.555 -13.094  1.00 91.73           C  
ANISOU 1253  CG  MET A 168    14307  11631   8916   1076   -984   1214       C  
ATOM   1254  SD  MET A 168      23.408  75.947 -12.500  1.00 99.77           S  
ANISOU 1254  SD  MET A 168    15218  12693   9995   1009   -920   1024       S  
ATOM   1255  CE  MET A 168      25.103  75.954 -13.091  1.00 72.31           C  
ANISOU 1255  CE  MET A 168    11879   9246   6351    984   -656   1053       C  
ATOM   1256  N   LEU A 169      21.753  79.819 -10.706  1.00 70.73           N  
ANISOU 1256  N   LEU A 169    11340   8778   6757   1098  -1003   1365       N  
ATOM   1257  CA  LEU A 169      20.492  79.768  -9.979  1.00 68.11           C  
ANISOU 1257  CA  LEU A 169    10848   8437   6594   1141  -1159   1334       C  
ATOM   1258  C   LEU A 169      19.691  81.053 -10.117  1.00 79.95           C  
ANISOU 1258  C   LEU A 169    12378   9872   8126   1229  -1251   1465       C  
ATOM   1259  O   LEU A 169      18.488  81.026 -10.390  1.00 88.47           O  
ANISOU 1259  O   LEU A 169    13419  10979   9218   1299  -1442   1479       O  
ATOM   1260  CB  LEU A 169      20.756  79.480  -8.515  1.00 60.19           C  
ANISOU 1260  CB  LEU A 169     9659   7403   5806   1088  -1059   1254       C  
ATOM   1261  CG  LEU A 169      21.197  78.037  -8.306  1.00 73.39           C  
ANISOU 1261  CG  LEU A 169    11269   9142   7475   1017  -1024   1114       C  
ATOM   1262  CD1 LEU A 169      21.920  77.858  -6.987  1.00 75.13           C  
ANISOU 1262  CD1 LEU A 169    11356   9328   7863    951   -872   1055       C  
ATOM   1263  CD2 LEU A 169      19.975  77.140  -8.387  1.00 79.03           C  
ANISOU 1263  CD2 LEU A 169    11892   9914   8221   1040  -1225   1044       C  
ATOM   1264  N   ILE A 170      20.363  82.179  -9.923  1.00 70.16           N  
ANISOU 1264  N   ILE A 170    11205   8543   6910   1224  -1121   1563       N  
ATOM   1265  CA  ILE A 170      19.696  83.461  -9.995  1.00 72.28           C  
ANISOU 1265  CA  ILE A 170    11513   8729   7219   1311  -1195   1689       C  
ATOM   1266  C   ILE A 170      19.176  83.718 -11.403  1.00 71.36           C  
ANISOU 1266  C   ILE A 170    11562   8648   6902   1379  -1335   1782       C  
ATOM   1267  O   ILE A 170      18.055  84.200 -11.571  1.00 76.55           O  
ANISOU 1267  O   ILE A 170    12199   9292   7594   1474  -1501   1840       O  
ATOM   1268  CB  ILE A 170      20.633  84.590  -9.534  1.00 79.55           C  
ANISOU 1268  CB  ILE A 170    12492   9531   8202   1278  -1027   1773       C  
ATOM   1269  CG1 ILE A 170      20.475  84.788  -8.026  1.00 81.10           C  
ANISOU 1269  CG1 ILE A 170    12517   9662   8634   1275   -983   1710       C  
ATOM   1270  CG2 ILE A 170      20.340  85.888 -10.262  1.00 73.25           C  
ANISOU 1270  CG2 ILE A 170    11845   8652   7334   1352  -1082   1937       C  
ATOM   1271  CD1 ILE A 170      21.318  85.894  -7.473  1.00 84.42           C  
ANISOU 1271  CD1 ILE A 170    12991   9952   9135   1240   -845   1778       C  
ATOM   1272  N   ALA A 171      19.968  83.363 -12.411  1.00 68.09           N  
ANISOU 1272  N   ALA A 171    11308   8286   6278   1339  -1271   1796       N  
ATOM   1273  CA  ALA A 171      19.509  83.461 -13.796  1.00 58.92           C  
ANISOU 1273  CA  ALA A 171    10321   7173   4895   1403  -1408   1872       C  
ATOM   1274  C   ALA A 171      18.275  82.607 -14.050  1.00 59.39           C  
ANISOU 1274  C   ALA A 171    10305   7312   4946   1451  -1643   1790       C  
ATOM   1275  O   ALA A 171      17.381  83.007 -14.774  1.00 84.19           O  
ANISOU 1275  O   ALA A 171    13514  10463   8011   1535  -1823   1867       O  
ATOM   1276  CB  ALA A 171      20.612  83.066 -14.754  1.00 62.36           C  
ANISOU 1276  CB  ALA A 171    10932   7664   5097   1353  -1279   1880       C  
ATOM   1277  N   TRP A 172      18.221  81.426 -13.457  1.00 83.83           N  
ANISOU 1277  N   TRP A 172    13259  10464   8128   1395  -1650   1640       N  
ATOM   1278  CA  TRP A 172      17.093  80.541 -13.701  1.00 84.11           C  
ANISOU 1278  CA  TRP A 172    13218  10572   8168   1422  -1877   1562       C  
ATOM   1279  C   TRP A 172      15.876  81.136 -12.999  1.00 86.17           C  
ANISOU 1279  C   TRP A 172    13308  10797   8636   1492  -2008   1610       C  
ATOM   1280  O   TRP A 172      14.757  81.081 -13.519  1.00 86.77           O  
ANISOU 1280  O   TRP A 172    13365  10910   8693   1557  -2230   1637       O  
ATOM   1281  CB  TRP A 172      17.397  79.101 -13.228  1.00 74.86           C  
ANISOU 1281  CB  TRP A 172    11943   9457   7044   1336  -1844   1393       C  
ATOM   1282  CG  TRP A 172      16.320  78.092 -13.608  1.00 71.10           C  
ANISOU 1282  CG  TRP A 172    11410   9050   6556   1344  -2087   1311       C  
ATOM   1283  CD1 TRP A 172      15.491  77.431 -12.754  1.00 62.97           C  
ANISOU 1283  CD1 TRP A 172    10160   8037   5731   1321  -2188   1236       C  
ATOM   1284  CD2 TRP A 172      15.946  77.666 -14.929  1.00 70.58           C  
ANISOU 1284  CD2 TRP A 172    11512   9040   6266   1374  -2266   1302       C  
ATOM   1285  CE2 TRP A 172      14.890  76.749 -14.802  1.00 72.69           C  
ANISOU 1285  CE2 TRP A 172    11644   9349   6626   1359  -2483   1217       C  
ATOM   1286  CE3 TRP A 172      16.400  77.974 -16.221  1.00 78.20           C  
ANISOU 1286  CE3 TRP A 172    12735  10026   6953   1413  -2267   1363       C  
ATOM   1287  NE1 TRP A 172      14.635  76.620 -13.451  1.00 69.30           N  
ANISOU 1287  NE1 TRP A 172    10970   8897   6466   1324  -2422   1184       N  
ATOM   1288  CZ2 TRP A 172      14.281  76.120 -15.897  1.00 76.44           C  
ANISOU 1288  CZ2 TRP A 172    12233   9876   6934   1376  -2715   1179       C  
ATOM   1289  CZ3 TRP A 172      15.790  77.353 -17.320  1.00 78.77           C  
ANISOU 1289  CZ3 TRP A 172    12932  10157   6840   1442  -2489   1323       C  
ATOM   1290  CH2 TRP A 172      14.749  76.437 -17.146  1.00 73.59           C  
ANISOU 1290  CH2 TRP A 172    12139   9534   6290   1421  -2716   1228       C  
ATOM   1291  N   LEU A 173      16.112  81.735 -11.835  1.00 87.81           N  
ANISOU 1291  N   LEU A 173    13394  10932   9036   1487  -1871   1624       N  
ATOM   1292  CA  LEU A 173      15.055  82.426 -11.101  1.00 91.02           C  
ANISOU 1292  CA  LEU A 173    13648  11297   9638   1571  -1958   1675       C  
ATOM   1293  C   LEU A 173      14.483  83.581 -11.925  1.00 89.49           C  
ANISOU 1293  C   LEU A 173    13580  11060   9362   1681  -2074   1826       C  
ATOM   1294  O   LEU A 173      13.267  83.793 -11.950  1.00 90.95           O  
ANISOU 1294  O   LEU A 173    13669  11261   9627   1771  -2254   1866       O  
ATOM   1295  CB  LEU A 173      15.575  82.934  -9.747  1.00 81.07           C  
ANISOU 1295  CB  LEU A 173    12281   9955   8565   1550  -1772   1659       C  
ATOM   1296  CG  LEU A 173      14.578  83.693  -8.861  1.00 69.22           C  
ANISOU 1296  CG  LEU A 173    10628   8404   7266   1651  -1826   1702       C  
ATOM   1297  CD1 LEU A 173      13.327  82.891  -8.622  1.00 73.68           C  
ANISOU 1297  CD1 LEU A 173    10998   9060   7939   1683  -1995   1650       C  
ATOM   1298  CD2 LEU A 173      15.207  84.041  -7.541  1.00 55.44           C  
ANISOU 1298  CD2 LEU A 173     8804   6584   5677   1620  -1639   1662       C  
ATOM   1299  N   GLU A 174      15.364  84.308 -12.609  1.00 79.65           N  
ANISOU 1299  N   GLU A 174    12543   9760   7960   1673  -1970   1917       N  
ATOM   1300  CA  GLU A 174      14.950  85.423 -13.450  1.00 81.06           C  
ANISOU 1300  CA  GLU A 174    12869   9887   8041   1771  -2067   2074       C  
ATOM   1301  C   GLU A 174      14.029  84.956 -14.575  1.00 86.22           C  
ANISOU 1301  C   GLU A 174    13581  10632   8546   1826  -2310   2089       C  
ATOM   1302  O   GLU A 174      12.991  85.574 -14.841  1.00 97.09           O  
ANISOU 1302  O   GLU A 174    14938  11993   9958   1934  -2484   2179       O  
ATOM   1303  CB  GLU A 174      16.176  86.140 -14.026  1.00 79.03           C  
ANISOU 1303  CB  GLU A 174    12831   9567   7631   1730  -1897   2171       C  
ATOM   1304  CG  GLU A 174      15.847  87.404 -14.777  1.00 90.46           C  
ANISOU 1304  CG  GLU A 174    14438  10938   8996   1825  -1972   2349       C  
ATOM   1305  CD  GLU A 174      17.078  88.157 -15.242  1.00101.11           C  
ANISOU 1305  CD  GLU A 174    15985  12213  10219   1772  -1787   2459       C  
ATOM   1306  OE1 GLU A 174      17.615  87.820 -16.314  1.00110.39           O  
ANISOU 1306  OE1 GLU A 174    17329  13455  11159   1741  -1764   2490       O  
ATOM   1307  OE2 GLU A 174      17.502  89.105 -14.552  1.00102.00           O1-
ANISOU 1307  OE2 GLU A 174    16090  12201  10467   1763  -1668   2521       O1-
ATOM   1308  N   LYS A 175      14.400  83.859 -15.228  1.00 79.06           N  
ANISOU 1308  N   LYS A 175    12748   9817   7476   1757  -2330   1999       N  
ATOM   1309  CA  LYS A 175      13.627  83.375 -16.363  1.00 87.14           C  
ANISOU 1309  CA  LYS A 175    13857  10922   8331   1800  -2567   2003       C  
ATOM   1310  C   LYS A 175      12.290  82.811 -15.880  1.00 95.44           C  
ANISOU 1310  C   LYS A 175    14678  12021   9564   1830  -2780   1941       C  
ATOM   1311  O   LYS A 175      11.277  82.896 -16.575  1.00 99.61           O  
ANISOU 1311  O   LYS A 175    15219  12586  10043   1904  -3018   1994       O  
ATOM   1312  CB  LYS A 175      14.425  82.332 -17.162  1.00 80.84           C  
ANISOU 1312  CB  LYS A 175    13214  10200   7303   1723  -2525   1909       C  
ATOM   1313  CG  LYS A 175      13.604  81.147 -17.631  1.00 90.36           C  
ANISOU 1313  CG  LYS A 175    14380  11498   8456   1713  -2759   1798       C  
ATOM   1314  CD  LYS A 175      14.214  80.449 -18.840  1.00102.46           C  
ANISOU 1314  CD  LYS A 175    16153  13094   9683   1689  -2772   1748       C  
ATOM   1315  CE  LYS A 175      13.331  79.273 -19.248  1.00110.88           C  
ANISOU 1315  CE  LYS A 175    17179  14234  10717   1675  -3031   1629       C  
ATOM   1316  NZ  LYS A 175      12.694  78.662 -18.019  1.00106.65           N1+
ANISOU 1316  NZ  LYS A 175    16344  13695  10483   1624  -3075   1537       N1+
ATOM   1317  N   GLN A 176      12.287  82.266 -14.669  1.00 94.97           N  
ANISOU 1317  N   GLN A 176    14402  11963   9720   1774  -2693   1839       N  
ATOM   1318  CA  GLN A 176      11.069  81.718 -14.086  1.00 98.77           C  
ANISOU 1318  CA  GLN A 176    14639  12492  10398   1793  -2862   1790       C  
ATOM   1319  C   GLN A 176      10.086  82.831 -13.749  1.00103.18           C  
ANISOU 1319  C   GLN A 176    15090  13005  11107   1920  -2948   1912       C  
ATOM   1320  O   GLN A 176       8.870  82.642 -13.814  1.00102.84           O  
ANISOU 1320  O   GLN A 176    14902  13013  11159   1975  -3159   1930       O  
ATOM   1321  CB  GLN A 176      11.396  80.902 -12.837  1.00102.67           C  
ANISOU 1321  CB  GLN A 176    14940  12996  11076   1702  -2721   1664       C  
ATOM   1322  N   GLN A 177      10.628  83.992 -13.390  1.00106.82           N  
ANISOU 1322  N   GLN A 177    15623  13366  11597   1967  -2784   1998       N  
ATOM   1323  CA  GLN A 177       9.824  85.179 -13.115  1.00101.74           C  
ANISOU 1323  CA  GLN A 177    14920  12658  11080   2103  -2845   2119       C  
ATOM   1324  C   GLN A 177       9.456  85.883 -14.418  1.00 97.26           C  
ANISOU 1324  C   GLN A 177    14544  12079  10331   2192  -3010   2254       C  
ATOM   1325  O   GLN A 177       8.555  85.442 -15.131  1.00 95.58           O  
ANISOU 1325  O   GLN A 177    14305  11947  10066   2226  -3246   2263       O  
ATOM   1326  CB  GLN A 177      10.571  86.130 -12.168  1.00 92.06           C  
ANISOU 1326  CB  GLN A 177    13706  11310   9962   2114  -2612   2147       C  
ATOM   1327  CG  GLN A 177      10.652  85.613 -10.733  1.00 87.17           C  
ANISOU 1327  CG  GLN A 177    12869  10698   9554   2065  -2479   2032       C  
ATOM   1328  CD  GLN A 177      11.598  86.414  -9.846  1.00 86.07           C  
ANISOU 1328  CD  GLN A 177    12775  10439   9489   2049  -2247   2037       C  
ATOM   1329  NE2 GLN A 177      11.520  86.179  -8.540  1.00 80.26           N  
ANISOU 1329  NE2 GLN A 177    11855   9698   8942   2039  -2147   1954       N  
ATOM   1330  OE1 GLN A 177      12.391  87.226 -10.326  1.00 92.33           O  
ANISOU 1330  OE1 GLN A 177    13768  11145  10169   2043  -2162   2116       O  
ATOM   1331  N   ASP A 188      10.278  72.266  -5.135  1.00 77.96           N  
ANISOU 1331  N   ASP A 188    10247  10110   9264   1022  -2483    900       N  
ATOM   1332  CA  ASP A 188      11.348  71.320  -5.442  1.00 80.66           C  
ANISOU 1332  CA  ASP A 188    10734  10428   9484    926  -2425    786       C  
ATOM   1333  C   ASP A 188      12.686  72.042  -5.575  1.00 80.34           C  
ANISOU 1333  C   ASP A 188    10891  10339   9296    953  -2221    779       C  
ATOM   1334  O   ASP A 188      13.048  72.490  -6.664  1.00 66.66           O  
ANISOU 1334  O   ASP A 188     9357   8596   7374    988  -2256    798       O  
ATOM   1335  CB  ASP A 188      11.031  70.537  -6.727  1.00 83.58           C  
ANISOU 1335  CB  ASP A 188    11221  10816   9719    884  -2651    737       C  
ATOM   1336  N   LEU A 189      13.410  72.165  -4.459  1.00 94.33           N  
ANISOU 1336  N   LEU A 189    12603  12082  11155    934  -2013    759       N  
ATOM   1337  CA  LEU A 189      14.757  72.745  -4.467  1.00 98.43           C  
ANISOU 1337  CA  LEU A 189    13284  12553  11563    938  -1815    749       C  
ATOM   1338  C   LEU A 189      15.657  71.978  -5.426  1.00110.74           C  
ANISOU 1338  C   LEU A 189    15028  14113  12937    880  -1813    668       C  
ATOM   1339  O   LEU A 189      16.379  72.568  -6.247  1.00106.74           O  
ANISOU 1339  O   LEU A 189    14709  13588  12258    909  -1755    695       O  
ATOM   1340  CB  LEU A 189      15.378  72.730  -3.069  1.00 88.80           C  
ANISOU 1340  CB  LEU A 189    11957  11307  10476    907  -1620    721       C  
ATOM   1341  CG  LEU A 189      14.593  73.247  -1.863  1.00 90.22           C  
ANISOU 1341  CG  LEU A 189    11942  11490  10848    959  -1587    774       C  
ATOM   1342  CD1 LEU A 189      15.538  73.428  -0.676  1.00 85.55           C  
ANISOU 1342  CD1 LEU A 189    11326  10859  10322    936  -1377    742       C  
ATOM   1343  CD2 LEU A 189      13.846  74.537  -2.166  1.00 91.21           C  
ANISOU 1343  CD2 LEU A 189    12077  11604  10975   1075  -1647    882       C  
ATOM   1344  N   GLU A 190      15.600  70.654  -5.275  1.00114.37           N  
ANISOU 1344  N   GLU A 190    15428  14589  13438    802  -1870    573       N  
ATOM   1345  CA  GLU A 190      16.229  69.686  -6.161  1.00106.66           C  
ANISOU 1345  CA  GLU A 190    14607  13614  12303    753  -1906    476       C  
ATOM   1346  C   GLU A 190      15.910  69.952  -7.622  1.00 92.51           C  
ANISOU 1346  C   GLU A 190    12995  11841  10313    801  -2059    500       C  
ATOM   1347  O   GLU A 190      16.806  69.996  -8.452  1.00 85.14           O  
ANISOU 1347  O   GLU A 190    12262  10904   9184    814  -1990    475       O  
ATOM   1348  CB  GLU A 190      15.771  68.275  -5.784  1.00115.94           C  
ANISOU 1348  CB  GLU A 190    15665  14796  13591    670  -2013    387       C  
ATOM   1349  CG  GLU A 190      14.429  68.267  -5.058  1.00129.76           C  
ANISOU 1349  CG  GLU A 190    17181  16571  15550    665  -2135    445       C  
ATOM   1350  CD  GLU A 190      14.116  66.936  -4.398  1.00142.00           C  
ANISOU 1350  CD  GLU A 190    18588  18118  17247    570  -2190    375       C  
ATOM   1351  OE1 GLU A 190      14.400  65.884  -5.008  1.00148.05           O  
ANISOU 1351  OE1 GLU A 190    19457  18865  17932    512  -2273    278       O  
ATOM   1352  OE2 GLU A 190      13.585  66.942  -3.266  1.00144.68           O1-
ANISOU 1352  OE2 GLU A 190    18718  18471  17781    556  -2149    419       O1-
ATOM   1353  N   GLY A 191      14.624  70.118  -7.925  1.00 91.98           N  
ANISOU 1353  N   GLY A 191    12851  11800  10298    830  -2269    554       N  
ATOM   1354  CA  GLY A 191      14.165  70.353  -9.287  1.00 91.74           C  
ANISOU 1354  CA  GLY A 191    12980  11790  10086    878  -2450    582       C  
ATOM   1355  C   GLY A 191      14.685  71.656  -9.877  1.00 91.46           C  
ANISOU 1355  C   GLY A 191    13109  11744   9898    962  -2351    678       C  
ATOM   1356  O   GLY A 191      15.052  71.710 -11.056  1.00 90.38           O  
ANISOU 1356  O   GLY A 191    13189  11617   9533    989  -2392    673       O  
ATOM   1357  N   PHE A 192      14.723  72.702  -9.050  1.00 83.00           N  
ANISOU 1357  N   PHE A 192    11941  10648   8949   1004  -2220    766       N  
ATOM   1358  CA  PHE A 192      15.223  74.009  -9.460  1.00 77.25           C  
ANISOU 1358  CA  PHE A 192    11353   9890   8109   1075  -2116    869       C  
ATOM   1359  C   PHE A 192      16.676  73.947  -9.925  1.00 76.75           C  
ANISOU 1359  C   PHE A 192    11482   9812   7869   1046  -1933    834       C  
ATOM   1360  O   PHE A 192      17.015  74.415 -11.013  1.00 84.04           O  
ANISOU 1360  O   PHE A 192    12605  10740   8587   1087  -1939    884       O  
ATOM   1361  CB  PHE A 192      15.084  75.012  -8.308  1.00 73.74           C  
ANISOU 1361  CB  PHE A 192    10764   9405   7851   1114  -1997    945       C  
ATOM   1362  CG  PHE A 192      15.313  76.445  -8.714  1.00 62.27           C  
ANISOU 1362  CG  PHE A 192     9437   7906   6317   1194  -1938   1067       C  
ATOM   1363  CD1 PHE A 192      14.331  77.149  -9.411  1.00 64.17           C  
ANISOU 1363  CD1 PHE A 192     9709   8153   6519   1283  -2111   1164       C  
ATOM   1364  CD2 PHE A 192      16.499  77.091  -8.398  1.00 57.52           C  
ANISOU 1364  CD2 PHE A 192     8920   7248   5686   1178  -1721   1090       C  
ATOM   1365  CE1 PHE A 192      14.524  78.478  -9.793  1.00 60.18           C  
ANISOU 1365  CE1 PHE A 192     9328   7594   5942   1359  -2063   1284       C  
ATOM   1366  CE2 PHE A 192      16.709  78.413  -8.767  1.00 68.37           C  
ANISOU 1366  CE2 PHE A 192    10413   8567   6996   1242  -1672   1209       C  
ATOM   1367  CZ  PHE A 192      15.715  79.114  -9.473  1.00 69.95           C  
ANISOU 1367  CZ  PHE A 192    10656   8769   7154   1335  -1842   1308       C  
ATOM   1368  N   TYR A 193      17.532  73.367  -9.097  1.00 76.32           N  
ANISOU 1368  N   TYR A 193    11362   9743   7893    979  -1767    755       N  
ATOM   1369  CA  TYR A 193      18.948  73.289  -9.413  1.00 82.29           C  
ANISOU 1369  CA  TYR A 193    12265  10490   8511    952  -1576    726       C  
ATOM   1370  C   TYR A 193      19.178  72.496 -10.708  1.00 84.60           C  
ANISOU 1370  C   TYR A 193    12747  10823   8572    954  -1656    661       C  
ATOM   1371  O   TYR A 193      19.978  72.904 -11.555  1.00 86.74           O  
ANISOU 1371  O   TYR A 193    13205  11103   8651    981  -1559    699       O  
ATOM   1372  CB  TYR A 193      19.707  72.659  -8.241  1.00 80.41           C  
ANISOU 1372  CB  TYR A 193    11900  10234   8419    880  -1416    646       C  
ATOM   1373  CG  TYR A 193      21.183  72.992  -8.166  1.00 83.40           C  
ANISOU 1373  CG  TYR A 193    12365  10592   8733    858  -1181    655       C  
ATOM   1374  CD1 TYR A 193      22.107  72.376  -9.010  1.00 86.78           C  
ANISOU 1374  CD1 TYR A 193    12945  11048   8980    846  -1109    600       C  
ATOM   1375  CD2 TYR A 193      21.660  73.895  -7.225  1.00 81.37           C  
ANISOU 1375  CD2 TYR A 193    12030  10286   8601    849  -1033    717       C  
ATOM   1376  CE1 TYR A 193      23.463  72.672  -8.929  1.00 84.59           C  
ANISOU 1376  CE1 TYR A 193    12721  10760   8658    823   -888    620       C  
ATOM   1377  CE2 TYR A 193      23.013  74.191  -7.135  1.00 80.67           C  
ANISOU 1377  CE2 TYR A 193    12002  10176   8472    815   -830    732       C  
ATOM   1378  CZ  TYR A 193      23.907  73.579  -7.986  1.00 82.89           C  
ANISOU 1378  CZ  TYR A 193    12415  10496   8585    802   -755    689       C  
ATOM   1379  OH  TYR A 193      25.246  73.886  -7.884  1.00 88.27           O  
ANISOU 1379  OH  TYR A 193    13133  11164   9241    768   -549    715       O  
ATOM   1380  N   ARG A 194      18.454  71.386 -10.866  1.00 78.35           N  
ANISOU 1380  N   ARG A 194    11914  10056   7801    927  -1837    566       N  
ATOM   1381  CA  ARG A 194      18.664  70.471 -11.993  1.00 76.36           C  
ANISOU 1381  CA  ARG A 194    11844   9831   7338    927  -1924    474       C  
ATOM   1382  C   ARG A 194      18.296  71.113 -13.302  1.00 86.28           C  
ANISOU 1382  C   ARG A 194    13293  11115   8376   1001  -2045    548       C  
ATOM   1383  O   ARG A 194      19.035  71.009 -14.274  1.00100.76           O  
ANISOU 1383  O   ARG A 194    15341  12970   9974   1030  -1983    529       O  
ATOM   1384  CB  ARG A 194      17.855  69.182 -11.822  1.00 77.13           C  
ANISOU 1384  CB  ARG A 194    11846   9931   7528    873  -2121    361       C  
ATOM   1385  N   ASP A 195      17.136  71.758 -13.325  1.00 88.64           N  
ANISOU 1385  N   ASP A 195    13514  11414   8749   1037  -2218    635       N  
ATOM   1386  CA  ASP A 195      16.674  72.486 -14.504  1.00 87.61           C  
ANISOU 1386  CA  ASP A 195    13554  11306   8429   1114  -2351    726       C  
ATOM   1387  C   ASP A 195      17.605  73.637 -14.851  1.00 74.92           C  
ANISOU 1387  C   ASP A 195    12091   9686   6691   1161  -2149    840       C  
ATOM   1388  O   ASP A 195      17.835  73.933 -16.017  1.00 73.31           O  
ANISOU 1388  O   ASP A 195    12107   9507   6242   1213  -2173    884       O  
ATOM   1389  CB  ASP A 195      15.261  73.014 -14.279  1.00 95.92           C  
ANISOU 1389  CB  ASP A 195    14455  12359   9630   1148  -2560    808       C  
ATOM   1390  CG  ASP A 195      14.235  71.907 -14.206  1.00104.64           C  
ANISOU 1390  CG  ASP A 195    15438  13484  10836   1100  -2801    717       C  
ATOM   1391  OD1 ASP A 195      14.304  70.970 -15.035  1.00107.96           O  
ANISOU 1391  OD1 ASP A 195    16002  13922  11096   1077  -2919    616       O  
ATOM   1392  OD2 ASP A 195      13.360  71.973 -13.317  1.00108.06           O1-
ANISOU 1392  OD2 ASP A 195    15634  13914  11510   1086  -2870    747       O1-
ATOM   1393  N   ALA A 196      18.131  74.296 -13.828  1.00 72.79           N  
ANISOU 1393  N   ALA A 196    11698   9373   6584   1141  -1953    892       N  
ATOM   1394  CA  ALA A 196      19.113  75.340 -14.052  1.00 68.93           C  
ANISOU 1394  CA  ALA A 196    11330   8859   6000   1164  -1750    999       C  
ATOM   1395  C   ALA A 196      20.401  74.721 -14.574  1.00 67.23           C  
ANISOU 1395  C   ALA A 196    11264   8674   5607   1136  -1578    933       C  
ATOM   1396  O   ALA A 196      21.014  75.239 -15.507  1.00 72.40           O  
ANISOU 1396  O   ALA A 196    12111   9345   6051   1173  -1494   1009       O  
ATOM   1397  CB  ALA A 196      19.364  76.119 -12.783  1.00 54.47           C  
ANISOU 1397  CB  ALA A 196     9333   6967   4397   1141  -1600   1055       C  
ATOM   1398  N   LYS A 197      20.799  73.607 -13.969  1.00 64.07           N  
ANISOU 1398  N   LYS A 197    10771   8282   5293   1075  -1523    797       N  
ATOM   1399  CA  LYS A 197      21.989  72.892 -14.399  1.00 67.18           C  
ANISOU 1399  CA  LYS A 197    11285   8706   5536   1059  -1363    720       C  
ATOM   1400  C   LYS A 197      21.847  72.484 -15.867  1.00 76.88           C  
ANISOU 1400  C   LYS A 197    12752   9985   6472   1118  -1478    690       C  
ATOM   1401  O   LYS A 197      22.642  72.920 -16.700  1.00 86.84           O  
ANISOU 1401  O   LYS A 197    14194  11276   7526   1157  -1345    755       O  
ATOM   1402  CB  LYS A 197      22.240  71.666 -13.511  1.00 53.53           C  
ANISOU 1402  CB  LYS A 197     9413   6969   3957    994  -1331    572       C  
ATOM   1403  N   LYS A 198      20.837  71.667 -16.178  1.00 74.51           N  
ANISOU 1403  N   LYS A 198    12455   9698   6158   1122  -1727    599       N  
ATOM   1404  CA  LYS A 198      20.583  71.247 -17.553  1.00 85.15           C  
ANISOU 1404  CA  LYS A 198    14037  11088   7228   1179  -1876    558       C  
ATOM   1405  C   LYS A 198      20.594  72.459 -18.486  1.00 91.76           C  
ANISOU 1405  C   LYS A 198    15046  11946   7870   1253  -1862    717       C  
ATOM   1406  O   LYS A 198      21.434  72.533 -19.380  1.00 99.83           O  
ANISOU 1406  O   LYS A 198    16277  13007   8646   1297  -1733    736       O  
ATOM   1407  CB  LYS A 198      19.253  70.488 -17.673  1.00 80.66           C  
ANISOU 1407  CB  LYS A 198    13417  10515   6715   1165  -2192    474       C  
ATOM   1408  N   HIS A 199      19.716  73.432 -18.243  1.00 83.65           N  
ANISOU 1408  N   HIS A 199    13929  10893   6960   1270  -1975    838       N  
ATOM   1409  CA  HIS A 199      19.606  74.587 -19.132  1.00 86.86           C  
ANISOU 1409  CA  HIS A 199    14501  11309   7192   1343  -1992    997       C  
ATOM   1410  C   HIS A 199      20.873  75.447 -19.193  1.00 87.23           C  
ANISOU 1410  C   HIS A 199    14630  11347   7165   1346  -1698   1110       C  
ATOM   1411  O   HIS A 199      21.135  76.097 -20.202  1.00 87.40           O  
ANISOU 1411  O   HIS A 199    14857  11394   6958   1403  -1665   1219       O  
ATOM   1412  CB  HIS A 199      18.419  75.472 -18.744  1.00 81.22           C  
ANISOU 1412  CB  HIS A 199    13653  10558   6649   1368  -2165   1105       C  
ATOM   1413  CG  HIS A 199      17.846  76.218 -19.904  1.00 90.19           C  
ANISOU 1413  CG  HIS A 199    14976  11714   7578   1454  -2320   1224       C  
ATOM   1414  CD2 HIS A 199      16.895  75.870 -20.804  1.00 89.89           C  
ANISOU 1414  CD2 HIS A 199    15042  11714   7400   1500  -2597   1200       C  
ATOM   1415  ND1 HIS A 199      18.303  77.460 -20.289  1.00100.28           N  
ANISOU 1415  ND1 HIS A 199    16372  12969   8760   1499  -2193   1393       N  
ATOM   1416  CE1 HIS A 199      17.637  77.862 -21.357  1.00 97.27           C  
ANISOU 1416  CE1 HIS A 199    16157  12613   8187   1576  -2381   1473       C  
ATOM   1417  NE2 HIS A 199      16.779  76.915 -21.690  1.00 98.45           N  
ANISOU 1417  NE2 HIS A 199    16286  12802   8318   1573  -2622   1353       N  
ATOM   1418  N   TYR A 200      21.662  75.454 -18.126  1.00 81.51           N  
ANISOU 1418  N   TYR A 200    13748  10589   6632   1280  -1489   1092       N  
ATOM   1419  CA  TYR A 200      22.955  76.122 -18.185  1.00 81.90           C  
ANISOU 1419  CA  TYR A 200    13865  10634   6621   1267  -1210   1188       C  
ATOM   1420  C   TYR A 200      23.869  75.388 -19.166  1.00 83.62           C  
ANISOU 1420  C   TYR A 200    14279  10925   6569   1293  -1093   1126       C  
ATOM   1421  O   TYR A 200      24.536  76.007 -20.000  1.00 87.83           O  
ANISOU 1421  O   TYR A 200    14984  11487   6900   1330   -959   1241       O  
ATOM   1422  CB  TYR A 200      23.592  76.190 -16.800  1.00 79.05           C  
ANISOU 1422  CB  TYR A 200    13286  10221   6528   1187  -1034   1166       C  
ATOM   1423  CG  TYR A 200      25.045  76.569 -16.824  1.00 85.20           C  
ANISOU 1423  CG  TYR A 200    14111  11004   7257   1155   -747   1232       C  
ATOM   1424  CD1 TYR A 200      25.430  77.896 -16.834  1.00 85.46           C  
ANISOU 1424  CD1 TYR A 200    14175  10989   7308   1149   -634   1406       C  
ATOM   1425  CD2 TYR A 200      26.034  75.601 -16.833  1.00 91.22           C  
ANISOU 1425  CD2 TYR A 200    14881  11814   7964   1131   -594   1126       C  
ATOM   1426  CE1 TYR A 200      26.750  78.248 -16.852  1.00 84.78           C  
ANISOU 1426  CE1 TYR A 200    14115  10905   7193   1108   -378   1478       C  
ATOM   1427  CE2 TYR A 200      27.359  75.947 -16.859  1.00 93.75           C  
ANISOU 1427  CE2 TYR A 200    15224  12146   8251   1102   -332   1195       C  
ATOM   1428  CZ  TYR A 200      27.710  77.275 -16.866  1.00 90.89           C  
ANISOU 1428  CZ  TYR A 200    14880  11739   7915   1085   -226   1375       C  
ATOM   1429  OH  TYR A 200      29.033  77.635 -16.881  1.00 99.63           O  
ANISOU 1429  OH  TYR A 200    15992  12856   9005   1043     30   1456       O  
ATOM   1430  N   ASP A 201      23.872  74.061 -19.059  1.00 79.75           N  
ANISOU 1430  N   ASP A 201    13765  10462   6076   1279  -1145    948       N  
ATOM   1431  CA  ASP A 201      24.640  73.202 -19.954  1.00 90.14           C  
ANISOU 1431  CA  ASP A 201    15267  11844   7139   1319  -1055    858       C  
ATOM   1432  C   ASP A 201      24.070  73.149 -21.387  1.00 99.82           C  
ANISOU 1432  C   ASP A 201    16755  13120   8052   1408  -1229    867       C  
ATOM   1433  O   ASP A 201      24.839  73.138 -22.360  1.00 98.08           O  
ANISOU 1433  O   ASP A 201    16745  12960   7562   1467  -1093    893       O  
ATOM   1434  CB  ASP A 201      24.724  71.787 -19.365  1.00 89.20           C  
ANISOU 1434  CB  ASP A 201    15046  11718   7127   1281  -1084    658       C  
ATOM   1435  CG  ASP A 201      25.713  71.690 -18.206  1.00 94.36           C  
ANISOU 1435  CG  ASP A 201    15506  12345   8000   1211   -849    643       C  
ATOM   1436  OD1 ASP A 201      26.745  72.394 -18.250  1.00100.85           O  
ANISOU 1436  OD1 ASP A 201    16348  13182   8787   1208   -610    752       O  
ATOM   1437  OD2 ASP A 201      25.471  70.904 -17.255  1.00 88.43           O1-
ANISOU 1437  OD2 ASP A 201    14583  11560   7457   1156   -906    527       O1-
ATOM   1438  N   GLU A 202      22.737  73.120 -21.506  1.00103.45           N  
ANISOU 1438  N   GLU A 202    17197  13560   8548   1420  -1526    850       N  
ATOM   1439  CA  GLU A 202      22.053  72.978 -22.803  1.00103.59           C  
ANISOU 1439  CA  GLU A 202    17453  13621   8287   1499  -1743    842       C  
ATOM   1440  C   GLU A 202      22.461  74.082 -23.784  1.00100.75           C  
ANISOU 1440  C   GLU A 202    17222  13294   7765   1540  -1610   1007       C  
ATOM   1441  O   GLU A 202      22.632  75.244 -23.402  1.00101.31           O  
ANISOU 1441  O   GLU A 202    17242  13332   7919   1532  -1508   1176       O  
ATOM   1442  CB  GLU A 202      20.518  72.990 -22.638  1.00102.21           C  
ANISOU 1442  CB  GLU A 202    17174  13414   8247   1489  -2078    832       C  
ATOM   1443  CG  GLU A 202      19.872  71.844 -21.824  1.00 97.77           C  
ANISOU 1443  CG  GLU A 202    16425  12820   7905   1421  -2242    664       C  
ATOM   1444  CD  GLU A 202      20.138  70.443 -22.371  1.00100.49           C  
ANISOU 1444  CD  GLU A 202    16912  13186   8085   1428  -2299    472       C  
ATOM   1445  OE1 GLU A 202      20.112  70.249 -23.603  1.00106.07           O  
ANISOU 1445  OE1 GLU A 202    17793  13929   8580   1470  -2346    439       O  
ATOM   1446  OE2 GLU A 202      20.364  69.524 -21.556  1.00 97.55           O1-
ANISOU 1446  OE2 GLU A 202    16395  12782   7887   1363  -2257    343       O1-
ATOM   1447  N   GLU A 205      21.502  81.753 -25.124  1.00121.50           N  
ANISOU 1447  N   GLU A 205    19934  15726  10503   1624  -1498   2102       N  
ATOM   1448  CA  GLU A 205      22.433  80.966 -24.318  1.00115.77           C  
ANISOU 1448  CA  GLU A 205    19149  15008   9832   1574  -1317   1996       C  
ATOM   1449  C   GLU A 205      22.391  81.336 -22.853  1.00115.86           C  
ANISOU 1449  C   GLU A 205    18991  14922  10108   1538  -1287   2021       C  
ATOM   1450  O   GLU A 205      22.655  82.478 -22.479  1.00113.16           O  
ANISOU 1450  O   GLU A 205    18620  14500   9876   1521  -1187   2174       O  
ATOM   1451  CB  GLU A 205      23.862  81.141 -24.812  1.00112.91           C  
ANISOU 1451  CB  GLU A 205    18883  14687   9331   1543  -1014   2064       C  
ATOM   1452  CG  GLU A 205      24.878  80.357 -24.003  1.00103.09           C  
ANISOU 1452  CG  GLU A 205    17568  13455   8148   1494   -814   1964       C  
ATOM   1453  CD  GLU A 205      24.725  78.860 -24.190  1.00104.16           C  
ANISOU 1453  CD  GLU A 205    17729  13662   8186   1517   -903   1747       C  
ATOM   1454  OE1 GLU A 205      23.977  78.221 -23.408  1.00 99.61           O  
ANISOU 1454  OE1 GLU A 205    17050  13055   7741   1514  -1080   1628       O  
ATOM   1455  OE2 GLU A 205      25.346  78.328 -25.140  1.00106.06           O1-
ANISOU 1455  OE2 GLU A 205    18093  13986   8220   1541   -798   1697       O1-
ATOM   1456  N   PHE A 206      22.102  80.345 -22.022  1.00114.07           N  
ANISOU 1456  N   PHE A 206    18659  14698   9986   1526  -1371   1868       N  
ATOM   1457  CA  PHE A 206      21.989  80.545 -20.587  1.00104.71           C  
ANISOU 1457  CA  PHE A 206    17222  13433   9130   1465  -1335   1840       C  
ATOM   1458  C   PHE A 206      23.318  80.902 -19.921  1.00102.51           C  
ANISOU 1458  C   PHE A 206    16874  13117   8959   1386  -1034   1882       C  
ATOM   1459  O   PHE A 206      23.403  81.859 -19.141  1.00 87.09           O  
ANISOU 1459  O   PHE A 206    14814  11071   7204   1354   -967   1976       O  
ATOM   1460  CB  PHE A 206      21.420  79.283 -19.940  1.00101.08           C  
ANISOU 1460  CB  PHE A 206    16599  13002   8807   1436  -1467   1638       C  
ATOM   1461  CG  PHE A 206      20.527  79.561 -18.783  1.00 91.52           C  
ANISOU 1461  CG  PHE A 206    15151  11724   7899   1420  -1581   1625       C  
ATOM   1462  CD1 PHE A 206      19.256  80.085 -18.991  1.00 92.51           C  
ANISOU 1462  CD1 PHE A 206    15263  11831   8058   1488  -1819   1692       C  
ATOM   1463  CD2 PHE A 206      20.960  79.335 -17.490  1.00 75.51           C  
ANISOU 1463  CD2 PHE A 206    12917   9656   6117   1346  -1445   1555       C  
ATOM   1464  CE1 PHE A 206      18.425  80.360 -17.932  1.00 86.57           C  
ANISOU 1464  CE1 PHE A 206    14287  11024   7580   1487  -1909   1686       C  
ATOM   1465  CE2 PHE A 206      20.133  79.611 -16.416  1.00 74.99           C  
ANISOU 1465  CE2 PHE A 206    12641   9535   6316   1342  -1537   1546       C  
ATOM   1466  CZ  PHE A 206      18.865  80.126 -16.637  1.00 81.63           C  
ANISOU 1466  CZ  PHE A 206    13466  10362   7189   1416  -1762   1613       C  
ATOM   1467  N   ALA A 207      24.343  80.118 -20.245  1.00116.84           N  
ANISOU 1467  N   ALA A 207    18752  15002  10640   1360   -863   1809       N  
ATOM   1468  CA  ALA A 207      25.615  80.122 -19.527  1.00118.59           C  
ANISOU 1468  CA  ALA A 207    18869  15206  10984   1277   -592   1807       C  
ATOM   1469  C   ALA A 207      26.271  81.490 -19.428  1.00112.06           C  
ANISOU 1469  C   ALA A 207    18062  14306  10210   1241   -427   2006       C  
ATOM   1470  O   ALA A 207      26.831  81.839 -18.386  1.00111.50           O  
ANISOU 1470  O   ALA A 207    17831  14167  10367   1163   -299   2017       O  
ATOM   1471  CB  ALA A 207      26.579  79.138 -20.180  1.00124.02           C  
ANISOU 1471  CB  ALA A 207    19661  15993  11466   1283   -439   1723       C  
ATOM   1472  N   GLU A 208      26.216  82.259 -20.507  1.00110.08           N  
ANISOU 1472  N   GLU A 208    18014  14063   9748   1295   -436   2165       N  
ATOM   1473  CA  GLU A 208      26.907  83.531 -20.507  1.00103.81           C  
ANISOU 1473  CA  GLU A 208    17256  13195   8992   1254   -273   2366       C  
ATOM   1474  C   GLU A 208      26.244  84.469 -19.509  1.00102.46           C  
ANISOU 1474  C   GLU A 208    16948  12889   9095   1234   -375   2417       C  
ATOM   1475  O   GLU A 208      26.920  85.030 -18.642  1.00106.68           O  
ANISOU 1475  O   GLU A 208    17365  13339   9828   1152   -232   2462       O  
ATOM   1476  CB  GLU A 208      26.936  84.152 -21.900  1.00103.31           C  
ANISOU 1476  CB  GLU A 208    17384  13175   8696   1296   -266   2508       C  
ATOM   1477  CG  GLU A 208      27.980  85.245 -21.988  1.00107.38           C  
ANISOU 1477  CG  GLU A 208    17905  13638   9258   1220    -40   2695       C  
ATOM   1478  CD  GLU A 208      27.745  86.221 -23.116  1.00113.23           C  
ANISOU 1478  CD  GLU A 208    18766  14378   9877   1243    -79   2854       C  
ATOM   1479  OE1 GLU A 208      27.278  85.804 -24.198  1.00122.85           O  
ANISOU 1479  OE1 GLU A 208    20098  15693  10885   1311   -182   2815       O  
ATOM   1480  OE2 GLU A 208      28.027  87.419 -22.912  1.00111.67           O1-
ANISOU 1480  OE2 GLU A 208    18553  14077   9800   1191    -11   3020       O1-
ATOM   1481  N   ARG A 209      24.924  84.612 -19.614  1.00101.78           N  
ANISOU 1481  N   ARG A 209    16871  12781   9018   1312   -626   2405       N  
ATOM   1482  CA  ARG A 209      24.175  85.471 -18.697  1.00 94.74           C  
ANISOU 1482  CA  ARG A 209    15854  11767   8377   1320   -734   2445       C  
ATOM   1483  C   ARG A 209      24.391  85.047 -17.246  1.00 98.31           C  
ANISOU 1483  C   ARG A 209    16066  12180   9107   1246   -671   2309       C  
ATOM   1484  O   ARG A 209      24.418  85.894 -16.357  1.00 96.75           O  
ANISOU 1484  O   ARG A 209    15774  11867   9119   1218   -637   2361       O  
ATOM   1485  CB  ARG A 209      22.679  85.461 -19.029  1.00 83.50           C  
ANISOU 1485  CB  ARG A 209    14449  10353   6925   1424  -1021   2430       C  
ATOM   1486  N   ALA A 210      24.578  83.742 -17.027  1.00 99.32           N  
ANISOU 1486  N   ALA A 210    16110  12399   9226   1219   -654   2136       N  
ATOM   1487  CA  ALA A 210      24.692  83.163 -15.681  1.00 98.03           C  
ANISOU 1487  CA  ALA A 210    15723  12214   9308   1157   -615   1994       C  
ATOM   1488  C   ALA A 210      26.071  83.359 -15.052  1.00 93.65           C  
ANISOU 1488  C   ALA A 210    15105  11623   8854   1056   -367   2014       C  
ATOM   1489  O   ALA A 210      26.180  83.585 -13.843  1.00 97.05           O  
ANISOU 1489  O   ALA A 210    15375  11979   9519   1006   -330   1976       O  
ATOM   1490  CB  ALA A 210      24.349  81.683 -15.716  1.00 96.96           C  
ANISOU 1490  CB  ALA A 210    15532  12180   9128   1165   -704   1810       C  
ATOM   1491  N   ARG A 211      27.124  83.249 -15.854  1.00 88.43           N  
ANISOU 1491  N   ARG A 211    14563  11019   8016   1028   -197   2072       N  
ATOM   1492  CA  ARG A 211      28.441  83.613 -15.362  1.00 89.15           C  
ANISOU 1492  CA  ARG A 211    14595  11073   8206    930     35   2128       C  
ATOM   1493  C   ARG A 211      28.435  85.115 -15.099  1.00100.31           C  
ANISOU 1493  C   ARG A 211    16032  12348   9731    907     46   2298       C  
ATOM   1494  O   ARG A 211      28.952  85.568 -14.080  1.00 96.44           O  
ANISOU 1494  O   ARG A 211    15421  11768   9453    829    130   2304       O  
ATOM   1495  CB  ARG A 211      29.533  83.225 -16.356  1.00 87.90           C  
ANISOU 1495  CB  ARG A 211    14557  11014   7827    917    221   2174       C  
ATOM   1496  N   ASN A 212      27.813  85.867 -16.015  1.00106.15           N  
ANISOU 1496  N   ASN A 212    16938  13065  10328    978    -53   2432       N  
ATOM   1497  CA  ASN A 212      27.694  87.325 -15.923  1.00101.15           C  
ANISOU 1497  CA  ASN A 212    16362  12291   9780    973    -66   2605       C  
ATOM   1498  C   ASN A 212      26.782  87.786 -14.781  1.00 94.55           C  
ANISOU 1498  C   ASN A 212    15395  11341   9188   1000   -211   2550       C  
ATOM   1499  O   ASN A 212      26.915  88.899 -14.275  1.00 95.39           O  
ANISOU 1499  O   ASN A 212    15499  11306   9438    972   -188   2650       O  
ATOM   1500  CB  ASN A 212      27.193  87.896 -17.254  1.00106.21           C  
ANISOU 1500  CB  ASN A 212    17221  12947  10185   1058   -151   2757       C  
ATOM   1501  N   TYR A 213      25.854  86.933 -14.367  1.00 89.95           N  
ANISOU 1501  N   TYR A 213    14706  10816   8656   1055   -360   2393       N  
ATOM   1502  CA  TYR A 213      25.093  87.217 -13.155  1.00 85.19           C  
ANISOU 1502  CA  TYR A 213    13950  10125   8293   1079   -462   2324       C  
ATOM   1503  C   TYR A 213      25.906  86.878 -11.895  1.00 83.67           C  
ANISOU 1503  C   TYR A 213    13591   9903   8296    979   -325   2220       C  
ATOM   1504  O   TYR A 213      25.667  87.451 -10.822  1.00 80.16           O  
ANISOU 1504  O   TYR A 213    13050   9352   8055    976   -347   2202       O  
ATOM   1505  CB  TYR A 213      23.766  86.454 -13.139  1.00 79.52           C  
ANISOU 1505  CB  TYR A 213    13160   9481   7572   1170   -669   2210       C  
ATOM   1506  CG  TYR A 213      22.689  87.041 -14.023  1.00 76.85           C  
ANISOU 1506  CG  TYR A 213    12943   9134   7122   1282   -853   2313       C  
ATOM   1507  CD1 TYR A 213      22.984  88.031 -14.967  1.00 79.62           C  
ANISOU 1507  CD1 TYR A 213    13488   9434   7332   1302   -823   2495       C  
ATOM   1508  CD2 TYR A 213      21.372  86.626 -13.901  1.00 69.03           C  
ANISOU 1508  CD2 TYR A 213    11867   8184   6176   1369  -1061   2240       C  
ATOM   1509  CE1 TYR A 213      22.002  88.561 -15.776  1.00 71.45           C  
ANISOU 1509  CE1 TYR A 213    12567   8390   6191   1410  -1001   2594       C  
ATOM   1510  CE2 TYR A 213      20.378  87.162 -14.705  1.00 77.89           C  
ANISOU 1510  CE2 TYR A 213    13089   9301   7205   1475  -1243   2338       C  
ATOM   1511  CZ  TYR A 213      20.700  88.129 -15.640  1.00 75.84           C  
ANISOU 1511  CZ  TYR A 213    13031   8989   6795   1499  -1215   2513       C  
ATOM   1512  OH  TYR A 213      19.713  88.655 -16.434  1.00 83.69           O  
ANISOU 1512  OH  TYR A 213    14127   9977   7694   1610  -1404   2614       O  
ATOM   1513  N   VAL A 214      26.860  85.953 -12.022  1.00 76.92           N  
ANISOU 1513  N   VAL A 214    12708   9143   7375    907   -189   2150       N  
ATOM   1514  CA  VAL A 214      27.749  85.635 -10.908  1.00 74.60           C  
ANISOU 1514  CA  VAL A 214    12265   8826   7254    810    -55   2066       C  
ATOM   1515  C   VAL A 214      28.694  86.817 -10.653  1.00 74.52           C  
ANISOU 1515  C   VAL A 214    12290   8692   7334    727     77   2204       C  
ATOM   1516  O   VAL A 214      29.135  87.052  -9.526  1.00 69.17           O  
ANISOU 1516  O   VAL A 214    11498   7934   6849    661    129   2162       O  
ATOM   1517  CB  VAL A 214      28.564  84.341 -11.163  1.00 54.04           C  
ANISOU 1517  CB  VAL A 214     9624   6353   4556    763     59   1964       C  
ATOM   1518  N   VAL A 215      28.988  87.571 -11.705  1.00 76.73           N  
ANISOU 1518  N   VAL A 215    12733   8951   7469    730    122   2372       N  
ATOM   1519  CA  VAL A 215      29.820  88.753 -11.565  1.00 81.23           C  
ANISOU 1519  CA  VAL A 215    13348   9392   8124    646    232   2524       C  
ATOM   1520  C   VAL A 215      28.957  89.904 -11.032  1.00 83.00           C  
ANISOU 1520  C   VAL A 215    13598   9453   8484    699     95   2577       C  
ATOM   1521  O   VAL A 215      29.388  90.665 -10.158  1.00 84.62           O  
ANISOU 1521  O   VAL A 215    13758   9520   8872    632    135   2602       O  
ATOM   1522  CB  VAL A 215      30.534  89.126 -12.920  1.00 60.38           C  
ANISOU 1522  CB  VAL A 215    10874   6793   5274    622    352   2704       C  
ATOM   1523  CG1 VAL A 215      30.864  87.864 -13.703  1.00 60.48           C  
ANISOU 1523  CG1 VAL A 215    10903   6991   5086    643    424   2628       C  
ATOM   1524  CG2 VAL A 215      29.729  90.088 -13.782  1.00 72.03           C  
ANISOU 1524  CG2 VAL A 215    12528   8204   6636    707    236   2856       C  
ATOM   1525  N   LYS A 216      27.724  89.991 -11.524  1.00 82.62           N  
ANISOU 1525  N   LYS A 216    13618   9420   8352    824    -73   2585       N  
ATOM   1526  CA  LYS A 216      26.816  91.062 -11.139  1.00 85.03           C  
ANISOU 1526  CA  LYS A 216    13957   9581   8770    901   -208   2641       C  
ATOM   1527  C   LYS A 216      26.443  90.977  -9.662  1.00 91.29           C  
ANISOU 1527  C   LYS A 216    14584  10309   9791    909   -253   2498       C  
ATOM   1528  O   LYS A 216      26.299  92.004  -9.002  1.00 97.75           O  
ANISOU 1528  O   LYS A 216    15417  10968  10756    920   -282   2541       O  
ATOM   1529  CB  LYS A 216      25.556  91.030 -12.000  1.00 78.21           C  
ANISOU 1529  CB  LYS A 216    13179   8771   7766   1040   -385   2672       C  
ATOM   1530  N   LEU A 217      26.293  89.762  -9.136  1.00 89.32           N  
ANISOU 1530  N   LEU A 217    14190  10179   9570    906   -259   2329       N  
ATOM   1531  CA  LEU A 217      25.959  89.611  -7.719  1.00 85.39           C  
ANISOU 1531  CA  LEU A 217    13536   9635   9274    914   -290   2195       C  
ATOM   1532  C   LEU A 217      27.192  89.830  -6.854  1.00 88.42           C  
ANISOU 1532  C   LEU A 217    13865   9941   9789    785   -145   2177       C  
ATOM   1533  O   LEU A 217      27.092  90.349  -5.740  1.00 84.82           O  
ANISOU 1533  O   LEU A 217    13352   9372   9503    786   -162   2132       O  
ATOM   1534  CB  LEU A 217      25.343  88.234  -7.427  1.00 83.75           C  
ANISOU 1534  CB  LEU A 217    13189   9574   9059    950   -351   2032       C  
ATOM   1535  CG  LEU A 217      25.117  87.833  -5.952  1.00 81.82           C  
ANISOU 1535  CG  LEU A 217    12770   9313   9004    947   -357   1888       C  
ATOM   1536  CD1 LEU A 217      24.311  88.871  -5.178  1.00 90.42           C  
ANISOU 1536  CD1 LEU A 217    13851  10269  10235   1035   -440   1908       C  
ATOM   1537  CD2 LEU A 217      24.437  86.490  -5.834  1.00 70.69           C  
ANISOU 1537  CD2 LEU A 217    11237   8047   7574    981   -427   1754       C  
ATOM   1538  N   GLN A 218      28.358  89.454  -7.368  1.00 96.44           N  
ANISOU 1538  N   GLN A 218    14900  11018  10723    679     -3   2215       N  
ATOM   1539  CA  GLN A 218      29.600  89.694  -6.644  1.00 97.51           C  
ANISOU 1539  CA  GLN A 218    14980  11085  10986    546    131   2217       C  
ATOM   1540  C   GLN A 218      29.721  91.180  -6.340  1.00 99.34           C  
ANISOU 1540  C   GLN A 218    15300  11116  11328    524    114   2336       C  
ATOM   1541  O   GLN A 218      30.304  91.569  -5.324  1.00 93.41           O  
ANISOU 1541  O   GLN A 218    14490  10259  10742    447    151   2302       O  
ATOM   1542  CB  GLN A 218      30.809  89.210  -7.447  1.00 96.53           C  
ANISOU 1542  CB  GLN A 218    14874  11057  10744    449    291   2278       C  
ATOM   1543  N   SER A 219      29.120  91.993  -7.211  1.00103.27           N  
ANISOU 1543  N   SER A 219    15945  11557  11735    597     43   2469       N  
ATOM   1544  CA  SER A 219      29.226  93.444  -7.143  1.00106.59           C  
ANISOU 1544  CA  SER A 219    16482  11777  12240    581     22   2606       C  
ATOM   1545  C   SER A 219      27.882  94.177  -6.965  1.00101.86           C  
ANISOU 1545  C   SER A 219    15944  11077  11682    734   -144   2612       C  
ATOM   1546  O   SER A 219      27.190  94.464  -7.944  1.00112.07           O  
ANISOU 1546  O   SER A 219    17347  12388  12847    825   -221   2711       O  
ATOM   1547  CB  SER A 219      29.925  93.957  -8.409  1.00111.71           C  
ANISOU 1547  CB  SER A 219    17273  12421  12750    518    111   2806       C  
ATOM   1548  N   GLY A 220      27.531  94.487  -5.717  1.00 88.85           N  
ANISOU 1548  N   GLY A 220    14226   9324  10208    767   -198   2509       N  
ATOM   1549  CA  GLY A 220      26.425  95.385  -5.414  1.00 85.19           C  
ANISOU 1549  CA  GLY A 220    13824   8731   9814    909   -333   2525       C  
ATOM   1550  C   GLY A 220      25.065  95.007  -5.972  1.00 88.51           C  
ANISOU 1550  C   GLY A 220    14235   9257  10137   1072   -461   2511       C  
ATOM   1551  O   GLY A 220      24.319  94.301  -5.316  1.00 84.06           O  
ANISOU 1551  O   GLY A 220    13538   8780   9622   1148   -516   2372       O  
ATOM   1552  N   ASP A 221      24.751  95.515  -7.165  1.00 96.14           N  
ANISOU 1552  N   ASP A 221    15343  10213  10973   1122   -513   2664       N  
ATOM   1553  CA  ASP A 221      23.540  95.186  -7.937  1.00103.67           C  
ANISOU 1553  CA  ASP A 221    16307  11274  11809   1265   -648   2679       C  
ATOM   1554  C   ASP A 221      22.383  94.602  -7.126  1.00100.95           C  
ANISOU 1554  C   ASP A 221    15803  10998  11554   1386   -752   2528       C  
ATOM   1555  O   ASP A 221      22.178  93.388  -7.083  1.00101.57           O  
ANISOU 1555  O   ASP A 221    15756  11245  11590   1376   -756   2415       O  
ATOM   1556  CB  ASP A 221      23.903  94.221  -9.066  1.00107.84           C  
ANISOU 1556  CB  ASP A 221    16857  11986  12132   1211   -605   2702       C  
ATOM   1557  N   GLU A 222      21.632  95.490  -6.492  1.00 98.59           N  
ANISOU 1557  N   GLU A 222    15513  10563  11384   1503   -833   2534       N  
ATOM   1558  CA  GLU A 222      20.590  95.114  -5.550  1.00 91.87           C  
ANISOU 1558  CA  GLU A 222    14505   9756  10647   1622   -908   2402       C  
ATOM   1559  C   GLU A 222      19.524  94.213  -6.163  1.00 81.21           C  
ANISOU 1559  C   GLU A 222    13062   8586   9206   1712  -1024   2375       C  
ATOM   1560  O   GLU A 222      19.010  93.317  -5.504  1.00 84.19           O  
ANISOU 1560  O   GLU A 222    13269   9075   9644   1738  -1042   2245       O  
ATOM   1561  CB  GLU A 222      19.949  96.374  -4.972  1.00102.32           C  
ANISOU 1561  CB  GLU A 222    15888  10892  12099   1755   -974   2441       C  
ATOM   1562  CG  GLU A 222      20.070  96.485  -3.462  1.00113.05           C  
ANISOU 1562  CG  GLU A 222    17157  12171  13627   1761   -918   2306       C  
ATOM   1563  CD  GLU A 222      19.188  95.492  -2.728  1.00123.19           C  
ANISOU 1563  CD  GLU A 222    18236  13608  14964   1842   -949   2163       C  
ATOM   1564  OE1 GLU A 222      19.702  94.748  -1.864  1.00126.16           O  
ANISOU 1564  OE1 GLU A 222    18502  14043  15391   1756   -862   2037       O  
ATOM   1565  OE2 GLU A 222      17.974  95.468  -3.012  1.00127.69           O1-
ANISOU 1565  OE2 GLU A 222    18750  14236  15530   1993  -1062   2184       O1-
ATOM   1566  N   TYR A 223      19.189  94.456  -7.419  1.00 81.46           N  
ANISOU 1566  N   TYR A 223    13211   8643   9095   1757  -1110   2502       N  
ATOM   1567  CA  TYR A 223      18.326  93.551  -8.171  1.00 82.78           C  
ANISOU 1567  CA  TYR A 223    13315   8986   9152   1816  -1231   2483       C  
ATOM   1568  C   TYR A 223      18.716  92.072  -7.991  1.00 71.22           C  
ANISOU 1568  C   TYR A 223    11721   7691   7650   1710  -1170   2342       C  
ATOM   1569  O   TYR A 223      17.870  91.191  -7.819  1.00 60.63           O  
ANISOU 1569  O   TYR A 223    10234   6473   6330   1760  -1260   2251       O  
ATOM   1570  CB  TYR A 223      18.368  93.922  -9.654  1.00 62.50           C  
ANISOU 1570  CB  TYR A 223    10932   6425   6389   1827  -1293   2641       C  
ATOM   1571  CG  TYR A 223      17.675  92.926 -10.532  1.00 66.40           C  
ANISOU 1571  CG  TYR A 223    11389   7100   6739   1863  -1417   2616       C  
ATOM   1572  CD1 TYR A 223      16.346  92.588 -10.308  1.00 67.13           C  
ANISOU 1572  CD1 TYR A 223    11340   7262   6904   1986  -1578   2563       C  
ATOM   1573  CD2 TYR A 223      18.342  92.318 -11.593  1.00 75.53           C  
ANISOU 1573  CD2 TYR A 223    12653   8358   7688   1775  -1378   2645       C  
ATOM   1574  CE1 TYR A 223      15.699  91.662 -11.109  1.00 74.81           C  
ANISOU 1574  CE1 TYR A 223    12278   8392   7754   2008  -1713   2537       C  
ATOM   1575  CE2 TYR A 223      17.701  91.392 -12.407  1.00 77.57           C  
ANISOU 1575  CE2 TYR A 223    12896   8772   7806   1808  -1508   2611       C  
ATOM   1576  CZ  TYR A 223      16.378  91.066 -12.156  1.00 84.73           C  
ANISOU 1576  CZ  TYR A 223    13660   9736   8797   1919  -1684   2556       C  
ATOM   1577  OH  TYR A 223      15.728  90.146 -12.951  1.00 96.79           O  
ANISOU 1577  OH  TYR A 223    15170  11409  10198   1941  -1833   2519       O  
ATOM   1578  N   PHE A 224      20.015  91.825  -8.028  1.00 61.44           N  
ANISOU 1578  N   PHE A 224    10533   6451   6361   1564  -1018   2331       N  
ATOM   1579  CA  PHE A 224      20.538  90.487  -7.981  1.00 60.67           C  
ANISOU 1579  CA  PHE A 224    10342   6499   6211   1463   -949   2213       C  
ATOM   1580  C   PHE A 224      20.586  90.013  -6.540  1.00 64.57           C  
ANISOU 1580  C   PHE A 224    10659   6993   6884   1437   -891   2066       C  
ATOM   1581  O   PHE A 224      20.259  88.874  -6.222  1.00 63.18           O  
ANISOU 1581  O   PHE A 224    10343   6940   6723   1426   -914   1948       O  
ATOM   1582  CB  PHE A 224      21.920  90.461  -8.634  1.00 58.55           C  
ANISOU 1582  CB  PHE A 224    10195   6232   5820   1331   -802   2274       C  
ATOM   1583  CG  PHE A 224      21.872  90.650 -10.110  1.00 75.23           C  
ANISOU 1583  CG  PHE A 224    12476   8386   7721   1356   -850   2404       C  
ATOM   1584  CD1 PHE A 224      21.285  89.688 -10.911  1.00 74.10           C  
ANISOU 1584  CD1 PHE A 224    12330   8395   7431   1396   -952   2361       C  
ATOM   1585  CD2 PHE A 224      22.382  91.789 -10.702  1.00 82.79           C  
ANISOU 1585  CD2 PHE A 224    13606   9227   8623   1341   -803   2573       C  
ATOM   1586  CE1 PHE A 224      21.224  89.853 -12.280  1.00 83.44           C  
ANISOU 1586  CE1 PHE A 224    13683   9619   8400   1427  -1005   2477       C  
ATOM   1587  CE2 PHE A 224      22.317  91.962 -12.069  1.00 86.17           C  
ANISOU 1587  CE2 PHE A 224    14199   9699   8842   1370   -845   2701       C  
ATOM   1588  CZ  PHE A 224      21.744  90.992 -12.861  1.00 86.71           C  
ANISOU 1588  CZ  PHE A 224    14270   9927   8750   1417   -946   2650       C  
ATOM   1589  N   ARG A 225      20.978  90.927  -5.669  1.00 62.56           N  
ANISOU 1589  N   ARG A 225    10420   6588   6760   1428   -823   2079       N  
ATOM   1590  CA  ARG A 225      21.153  90.601  -4.288  1.00 65.13           C  
ANISOU 1590  CA  ARG A 225    10607   6899   7239   1399   -758   1949       C  
ATOM   1591  C   ARG A 225      19.790  90.282  -3.669  1.00 78.67           C  
ANISOU 1591  C   ARG A 225    12175   8670   9046   1532   -867   1875       C  
ATOM   1592  O   ARG A 225      19.694  89.385  -2.821  1.00 90.87           O  
ANISOU 1592  O   ARG A 225    13567  10296  10663   1508   -837   1751       O  
ATOM   1593  CB  ARG A 225      21.885  91.723  -3.542  1.00 68.96           C  
ANISOU 1593  CB  ARG A 225    11168   7199   7835   1362   -677   1980       C  
ATOM   1594  CG  ARG A 225      22.644  91.161  -2.318  1.00 94.27           C  
ANISOU 1594  CG  ARG A 225    14260  10411  11146   1265   -569   1848       C  
ATOM   1595  CD  ARG A 225      23.227  92.202  -1.364  1.00100.71           C  
ANISOU 1595  CD  ARG A 225    15134  11042  12091   1238   -516   1847       C  
ATOM   1596  NE  ARG A 225      24.678  92.234  -1.502  1.00 99.40           N  
ANISOU 1596  NE  ARG A 225    15020  10840  11909   1069   -400   1880       N  
ATOM   1597  CZ  ARG A 225      25.530  91.525  -0.769  1.00 94.89           C  
ANISOU 1597  CZ  ARG A 225    14353  10314  11388    959   -310   1781       C  
ATOM   1598  NH1 ARG A 225      25.093  90.702   0.194  1.00 79.96           N1+
ANISOU 1598  NH1 ARG A 225    12318   8505   9560    995   -319   1641       N1+
ATOM   1599  NH2 ARG A 225      26.833  91.649  -1.015  1.00103.58           N  
ANISOU 1599  NH2 ARG A 225    15499  11379  12477    811   -210   1834       N  
ATOM   1600  N   GLU A 226      18.743  90.982  -4.096  1.00 84.38           N  
ANISOU 1600  N   GLU A 226    12938   9356   9768   1671   -991   1958       N  
ATOM   1601  CA  GLU A 226      17.400  90.615  -3.671  1.00 85.96           C  
ANISOU 1601  CA  GLU A 226    12981   9633  10049   1799  -1100   1906       C  
ATOM   1602  C   GLU A 226      17.036  89.233  -4.159  1.00 75.42           C  
ANISOU 1602  C   GLU A 226    11536   8482   8640   1759  -1161   1845       C  
ATOM   1603  O   GLU A 226      16.351  88.484  -3.461  1.00 68.00           O  
ANISOU 1603  O   GLU A 226    10418   7630   7791   1790  -1190   1755       O  
ATOM   1604  CB  GLU A 226      16.361  91.613  -4.166  1.00 98.92           C  
ANISOU 1604  CB  GLU A 226    14682  11206  11697   1961  -1230   2018       C  
ATOM   1605  CG  GLU A 226      16.435  92.947  -3.456  1.00120.83           C  
ANISOU 1605  CG  GLU A 226    17539  13789  14582   2037  -1191   2056       C  
ATOM   1606  CD  GLU A 226      16.304  92.813  -1.941  1.00133.09           C  
ANISOU 1606  CD  GLU A 226    18956  15322  16290   2069  -1118   1929       C  
ATOM   1607  OE1 GLU A 226      15.487  91.985  -1.479  1.00136.58           O  
ANISOU 1607  OE1 GLU A 226    19214  15895  16786   2121  -1153   1852       O  
ATOM   1608  OE2 GLU A 226      17.031  93.524  -1.211  1.00135.03           O1-
ANISOU 1608  OE2 GLU A 226    19282  15422  16600   2036  -1027   1908       O1-
ATOM   1609  N   MET A 227      17.468  88.902  -5.368  1.00 72.76           N  
ANISOU 1609  N   MET A 227    11310   8200   8135   1693  -1182   1897       N  
ATOM   1610  CA  MET A 227      17.157  87.593  -5.892  1.00 73.07           C  
ANISOU 1610  CA  MET A 227    11271   8401   8093   1654  -1252   1832       C  
ATOM   1611  C   MET A 227      17.894  86.567  -5.075  1.00 71.84           C  
ANISOU 1611  C   MET A 227    11007   8301   7988   1539  -1132   1700       C  
ATOM   1612  O   MET A 227      17.336  85.519  -4.739  1.00 74.60           O  
ANISOU 1612  O   MET A 227    11205   8755   8383   1533  -1183   1609       O  
ATOM   1613  CB  MET A 227      17.523  87.478  -7.359  1.00 80.71           C  
ANISOU 1613  CB  MET A 227    12405   9411   8850   1618  -1292   1909       C  
ATOM   1614  CG  MET A 227      16.700  88.358  -8.259  1.00 74.81           C  
ANISOU 1614  CG  MET A 227    11764   8626   8034   1736  -1437   2043       C  
ATOM   1615  SD  MET A 227      17.148  87.993  -9.946  1.00 96.18           S  
ANISOU 1615  SD  MET A 227    14666  11411  10467   1688  -1479   2114       S  
ATOM   1616  CE  MET A 227      16.141  86.554 -10.226  1.00 95.76           C  
ANISOU 1616  CE  MET A 227    14473  11527  10386   1703  -1652   2004       C  
ATOM   1617  N   TRP A 228      19.138  86.877  -4.725  1.00 50.59           N  
ANISOU 1617  N   TRP A 228     8387   5534   5300   1445   -977   1695       N  
ATOM   1618  CA  TRP A 228      19.907  85.974  -3.870  1.00 50.35           C  
ANISOU 1618  CA  TRP A 228     8255   5547   5330   1339   -861   1574       C  
ATOM   1619  C   TRP A 228      19.280  85.838  -2.478  1.00 53.94           C  
ANISOU 1619  C   TRP A 228     8540   5995   5961   1390   -861   1489       C  
ATOM   1620  O   TRP A 228      19.190  84.735  -1.955  1.00 66.85           O  
ANISOU 1620  O   TRP A 228    10041   7723   7638   1348   -850   1388       O  
ATOM   1621  CB  TRP A 228      21.353  86.435  -3.763  1.00 51.28           C  
ANISOU 1621  CB  TRP A 228     8473   5580   5431   1232   -705   1600       C  
ATOM   1622  CG  TRP A 228      22.086  85.811  -2.596  1.00 61.29           C  
ANISOU 1622  CG  TRP A 228     9628   6857   6803   1145   -592   1484       C  
ATOM   1623  CD1 TRP A 228      22.745  84.596  -2.569  1.00 56.33           C  
ANISOU 1623  CD1 TRP A 228     8936   6328   6139   1050   -528   1397       C  
ATOM   1624  CD2 TRP A 228      22.238  86.375  -1.299  1.00 54.79           C  
ANISOU 1624  CD2 TRP A 228     8752   5935   6129   1152   -538   1445       C  
ATOM   1625  CE2 TRP A 228      22.990  85.462  -0.528  1.00 61.89           C  
ANISOU 1625  CE2 TRP A 228     9554   6885   7076   1056   -446   1338       C  
ATOM   1626  CE3 TRP A 228      21.799  87.562  -0.704  1.00 65.73           C  
ANISOU 1626  CE3 TRP A 228    10173   7190   7610   1238   -563   1484       C  
ATOM   1627  NE1 TRP A 228      23.287  84.384  -1.327  1.00 51.81           N  
ANISOU 1627  NE1 TRP A 228     8269   5728   5690    996   -440   1313       N  
ATOM   1628  CZ2 TRP A 228      23.318  85.706   0.804  1.00 68.11           C  
ANISOU 1628  CZ2 TRP A 228    10282   7603   7994   1039   -384   1274       C  
ATOM   1629  CZ3 TRP A 228      22.130  87.805   0.619  1.00 67.97           C  
ANISOU 1629  CZ3 TRP A 228    10405   7400   8019   1224   -497   1412       C  
ATOM   1630  CH2 TRP A 228      22.881  86.884   1.356  1.00 67.72           C  
ANISOU 1630  CH2 TRP A 228    10279   7427   8024   1123   -411   1309       C  
ATOM   1631  N   ARG A 229      18.839  86.950  -1.892  1.00 50.83           N  
ANISOU 1631  N   ARG A 229     8160   5490   5663   1485   -871   1532       N  
ATOM   1632  CA  ARG A 229      18.071  86.911  -0.657  1.00 47.66           C  
ANISOU 1632  CA  ARG A 229     7608   5089   5411   1566   -877   1464       C  
ATOM   1633  C   ARG A 229      16.831  86.006  -0.760  1.00 55.63           C  
ANISOU 1633  C   ARG A 229     8455   6237   6446   1628   -993   1434       C  
ATOM   1634  O   ARG A 229      16.648  85.110   0.077  1.00 66.70           O  
ANISOU 1634  O   ARG A 229     9703   7715   7925   1601   -963   1343       O  
ATOM   1635  CB  ARG A 229      17.666  88.319  -0.246  1.00 52.91           C  
ANISOU 1635  CB  ARG A 229     8340   5611   6152   1687   -889   1526       C  
ATOM   1636  CG  ARG A 229      18.189  88.690   1.129  1.00 71.18           C  
ANISOU 1636  CG  ARG A 229    10635   7832   8577   1675   -779   1451       C  
ATOM   1637  CD  ARG A 229      17.783  90.087   1.532  1.00 83.59           C  
ANISOU 1637  CD  ARG A 229    12292   9248  10220   1805   -797   1502       C  
ATOM   1638  NE  ARG A 229      18.051  91.057   0.476  1.00 97.95           N  
ANISOU 1638  NE  ARG A 229    14292  10962  11964   1809   -839   1627       N  
ATOM   1639  CZ  ARG A 229      19.204  91.707   0.323  1.00103.22           C  
ANISOU 1639  CZ  ARG A 229    15109  11504  12605   1707   -769   1668       C  
ATOM   1640  NH1 ARG A 229      20.216  91.491   1.158  1.00101.58           N1+
ANISOU 1640  NH1 ARG A 229    14890  11262  12443   1593   -662   1587       N1+
ATOM   1641  NH2 ARG A 229      19.350  92.570  -0.675  1.00103.29           N  
ANISOU 1641  NH2 ARG A 229    15278  11423  12545   1716   -810   1797       N  
ATOM   1642  N   LYS A 230      16.009  86.220  -1.788  1.00 50.83           N  
ANISOU 1642  N   LYS A 230     7880   5660   5773   1704  -1130   1517       N  
ATOM   1643  CA  LYS A 230      14.831  85.380  -2.061  1.00 59.06           C  
ANISOU 1643  CA  LYS A 230     8773   6831   6835   1751  -1267   1503       C  
ATOM   1644  C   LYS A 230      15.131  83.870  -2.122  1.00 66.01           C  
ANISOU 1644  C   LYS A 230     9569   7832   7682   1627  -1262   1407       C  
ATOM   1645  O   LYS A 230      14.314  83.058  -1.693  1.00 68.05           O  
ANISOU 1645  O   LYS A 230     9650   8180   8025   1640  -1322   1360       O  
ATOM   1646  CB  LYS A 230      14.166  85.799  -3.372  1.00 51.59           C  
ANISOU 1646  CB  LYS A 230     7916   5897   5788   1823  -1424   1610       C  
ATOM   1647  N   LEU A 231      16.297  83.498  -2.645  1.00 61.26           N  
ANISOU 1647  N   LEU A 231     9088   7227   6960   1510  -1187   1383       N  
ATOM   1648  CA  LEU A 231      16.669  82.085  -2.775  1.00 61.52           C  
ANISOU 1648  CA  LEU A 231     9066   7359   6950   1401  -1180   1289       C  
ATOM   1649  C   LEU A 231      17.070  81.509  -1.436  1.00 60.89           C  
ANISOU 1649  C   LEU A 231     8856   7286   6994   1344  -1062   1192       C  
ATOM   1650  O   LEU A 231      16.592  80.442  -1.017  1.00 59.66           O  
ANISOU 1650  O   LEU A 231     8553   7214   6902   1316  -1100   1124       O  
ATOM   1651  CB  LEU A 231      17.812  81.910  -3.778  1.00 61.21           C  
ANISOU 1651  CB  LEU A 231     9201   7317   6737   1312  -1123   1298       C  
ATOM   1652  CG  LEU A 231      17.342  82.001  -5.230  1.00 58.90           C  
ANISOU 1652  CG  LEU A 231     9029   7062   6287   1352  -1264   1371       C  
ATOM   1653  CD1 LEU A 231      18.475  82.007  -6.252  1.00 54.10           C  
ANISOU 1653  CD1 LEU A 231     8614   6450   5492   1285  -1188   1399       C  
ATOM   1654  CD2 LEU A 231      16.378  80.874  -5.476  1.00 52.54           C  
ANISOU 1654  CD2 LEU A 231     8107   6364   5491   1355  -1419   1312       C  
ATOM   1655  N   VAL A 232      17.958  82.241  -0.778  1.00 56.02           N  
ANISOU 1655  N   VAL A 232     8302   6574   6410   1324   -926   1193       N  
ATOM   1656  CA  VAL A 232      18.417  81.916   0.559  1.00 46.54           C  
ANISOU 1656  CA  VAL A 232     7004   5361   5320   1281   -812   1110       C  
ATOM   1657  C   VAL A 232      17.226  81.731   1.483  1.00 54.40           C  
ANISOU 1657  C   VAL A 232     7822   6398   6449   1367   -859   1088       C  
ATOM   1658  O   VAL A 232      17.191  80.818   2.310  1.00 56.93           O  
ANISOU 1658  O   VAL A 232     8011   6777   6841   1324   -821   1012       O  
ATOM   1659  CB  VAL A 232      19.318  83.024   1.115  1.00 42.80           C  
ANISOU 1659  CB  VAL A 232     6633   4758   4872   1273   -696   1132       C  
ATOM   1660  CG1 VAL A 232      19.619  82.769   2.558  1.00 41.48           C  
ANISOU 1660  CG1 VAL A 232     6367   4577   4819   1250   -602   1047       C  
ATOM   1661  CG2 VAL A 232      20.599  83.162   0.323  1.00 42.85           C  
ANISOU 1661  CG2 VAL A 232     6788   4728   4765   1172   -625   1161       C  
ATOM   1662  N   ASP A 233      16.252  82.617   1.325  1.00 61.05           N  
ANISOU 1662  N   ASP A 233     8661   7211   7324   1495   -938   1162       N  
ATOM   1663  CA  ASP A 233      15.054  82.610   2.141  1.00 63.06           C  
ANISOU 1663  CA  ASP A 233     8745   7507   7708   1602   -975   1161       C  
ATOM   1664  C   ASP A 233      14.202  81.371   1.878  1.00 61.07           C  
ANISOU 1664  C   ASP A 233     8331   7389   7482   1574  -1080   1141       C  
ATOM   1665  O   ASP A 233      13.541  80.867   2.779  1.00 68.63           O  
ANISOU 1665  O   ASP A 233     9115   8408   8555   1600  -1067   1111       O  
ATOM   1666  CB  ASP A 233      14.240  83.880   1.881  1.00 74.13           C  
ANISOU 1666  CB  ASP A 233    10190   8843   9132   1755  -1042   1254       C  
ATOM   1667  CG  ASP A 233      13.153  84.107   2.920  1.00 93.01           C  
ANISOU 1667  CG  ASP A 233    12415  11258  11665   1887  -1036   1253       C  
ATOM   1668  OD1 ASP A 233      13.289  83.605   4.055  1.00 85.89           O  
ANISOU 1668  OD1 ASP A 233    11412  10386  10837   1863   -939   1181       O  
ATOM   1669  OD2 ASP A 233      12.161  84.803   2.606  1.00109.87           O1-
ANISOU 1669  OD2 ASP A 233    14525  13385  13835   2024  -1125   1330       O1-
ATOM   1670  N   ILE A 234      14.206  80.862   0.655  1.00 52.93           N  
ANISOU 1670  N   ILE A 234     7362   6404   6345   1520  -1188   1157       N  
ATOM   1671  CA  ILE A 234      13.339  79.729   0.386  1.00 54.20           C  
ANISOU 1671  CA  ILE A 234     7376   6678   6540   1492  -1312   1138       C  
ATOM   1672  C   ILE A 234      13.934  78.497   1.025  1.00 55.48           C  
ANISOU 1672  C   ILE A 234     7464   6883   6731   1370  -1234   1039       C  
ATOM   1673  O   ILE A 234      13.229  77.659   1.592  1.00 62.16           O  
ANISOU 1673  O   ILE A 234     8132   7802   7683   1355  -1269   1014       O  
ATOM   1674  CB  ILE A 234      13.136  79.492  -1.107  1.00 59.16           C  
ANISOU 1674  CB  ILE A 234     8103   7339   7036   1472  -1467   1173       C  
ATOM   1675  CG1 ILE A 234      12.313  80.614  -1.706  1.00 53.64           C  
ANISOU 1675  CG1 ILE A 234     7444   6611   6326   1604  -1573   1282       C  
ATOM   1676  CG2 ILE A 234      12.352  78.217  -1.352  1.00 64.93           C  
ANISOU 1676  CG2 ILE A 234     8692   8174   7806   1419  -1605   1138       C  
ATOM   1677  CD1 ILE A 234      12.218  80.516  -3.217  1.00 53.63           C  
ANISOU 1677  CD1 ILE A 234     7577   6633   6167   1590  -1724   1324       C  
ATOM   1678  N   THR A 235      15.250  78.397   0.945  1.00 53.59           N  
ANISOU 1678  N   THR A 235     7359   6599   6406   1283  -1126    991       N  
ATOM   1679  CA  THR A 235      15.931  77.242   1.494  1.00 49.59           C  
ANISOU 1679  CA  THR A 235     6800   6125   5919   1172  -1051    899       C  
ATOM   1680  C   THR A 235      15.886  77.279   3.025  1.00 54.57           C  
ANISOU 1680  C   THR A 235     7304   6746   6685   1191   -939    869       C  
ATOM   1681  O   THR A 235      15.666  76.254   3.683  1.00 52.22           O  
ANISOU 1681  O   THR A 235     6871   6506   6464   1141   -930    820       O  
ATOM   1682  CB  THR A 235      17.394  77.176   1.011  1.00 60.11           C  
ANISOU 1682  CB  THR A 235     8299   7412   7126   1084   -956    863       C  
ATOM   1683  CG2 THR A 235      18.004  75.847   1.371  1.00 67.46           C  
ANISOU 1683  CG2 THR A 235     9176   8386   8070    978   -909    769       C  
ATOM   1684  OG1 THR A 235      17.437  77.317  -0.412  1.00 76.19           O  
ANISOU 1684  OG1 THR A 235    10475   9456   9018   1087  -1044    903       O  
ATOM   1685  N   MET A 236      16.100  78.458   3.601  1.00 47.37           N  
ANISOU 1685  N   MET A 236     6445   5755   5797   1264   -854    898       N  
ATOM   1686  CA  MET A 236      16.185  78.532   5.043  1.00 41.90           C  
ANISOU 1686  CA  MET A 236     5666   5047   5205   1285   -742    860       C  
ATOM   1687  C   MET A 236      14.798  78.448   5.676  1.00 57.69           C  
ANISOU 1687  C   MET A 236     7483   7114   7324   1383   -787    891       C  
ATOM   1688  O   MET A 236      14.649  77.942   6.795  1.00 58.15           O  
ANISOU 1688  O   MET A 236     7420   7209   7466   1378   -715    855       O  
ATOM   1689  CB  MET A 236      16.906  79.800   5.479  1.00 44.86           C  
ANISOU 1689  CB  MET A 236     6172   5305   5566   1328   -646    870       C  
ATOM   1690  CG  MET A 236      18.426  79.770   5.317  1.00 40.24           C  
ANISOU 1690  CG  MET A 236     5721   4661   4905   1213   -560    831       C  
ATOM   1691  SD  MET A 236      19.220  78.183   5.528  1.00 92.52           S  
ANISOU 1691  SD  MET A 236    12279  11357  11518   1070   -515    742       S  
ATOM   1692  CE  MET A 236      18.796  77.768   7.224  1.00 94.40           C  
ANISOU 1692  CE  MET A 236    12357  11626  11883   1100   -448    692       C  
ATOM   1693  N   THR A 237      13.773  78.911   4.961  1.00 62.91           N  
ANISOU 1693  N   THR A 237     8115   7795   7992   1474   -904    965       N  
ATOM   1694  CA  THR A 237      12.410  78.764   5.473  1.00 67.84           C  
ANISOU 1694  CA  THR A 237     8540   8497   8739   1565   -951   1007       C  
ATOM   1695  C   THR A 237      12.064  77.281   5.613  1.00 62.57           C  
ANISOU 1695  C   THR A 237     7713   7933   8128   1463   -996    975       C  
ATOM   1696  O   THR A 237      11.502  76.855   6.626  1.00 63.66           O  
ANISOU 1696  O   THR A 237     7684   8128   8375   1484   -944    975       O  
ATOM   1697  CB  THR A 237      11.371  79.438   4.572  1.00 68.39           C  
ANISOU 1697  CB  THR A 237     8595   8578   8811   1674  -1091   1098       C  
ATOM   1698  CG2 THR A 237      10.043  79.576   5.300  1.00 71.13           C  
ANISOU 1698  CG2 THR A 237     8733   8993   9300   1799  -1102   1149       C  
ATOM   1699  OG1 THR A 237      11.833  80.738   4.227  1.00 69.80           O  
ANISOU 1699  OG1 THR A 237     8955   8645   8918   1746  -1064   1130       O  
ATOM   1700  N   GLN A 238      12.421  76.501   4.597  1.00 56.65           N  
ANISOU 1700  N   GLN A 238     7026   7200   7298   1354  -1089    950       N  
ATOM   1701  CA  GLN A 238      12.145  75.074   4.606  1.00 58.25           C  
ANISOU 1701  CA  GLN A 238     7104   7480   7549   1248  -1152    915       C  
ATOM   1702  C   GLN A 238      12.923  74.354   5.687  1.00 52.38           C  
ANISOU 1702  C   GLN A 238     6330   6733   6841   1168  -1014    844       C  
ATOM   1703  O   GLN A 238      12.387  73.481   6.355  1.00 49.39           O  
ANISOU 1703  O   GLN A 238     5785   6417   6564   1132  -1015    842       O  
ATOM   1704  CB  GLN A 238      12.457  74.445   3.253  1.00 61.55           C  
ANISOU 1704  CB  GLN A 238     7633   7902   7853   1160  -1280    889       C  
ATOM   1705  CG  GLN A 238      11.386  74.674   2.216  1.00 73.08           C  
ANISOU 1705  CG  GLN A 238     9064   9398   9304   1214  -1467    958       C  
ATOM   1706  CD  GLN A 238      11.563  73.784   1.011  1.00 81.04           C  
ANISOU 1706  CD  GLN A 238    10161  10423  10207   1118  -1609    918       C  
ATOM   1707  NE2 GLN A 238      10.497  73.623   0.237  1.00 91.30           N  
ANISOU 1707  NE2 GLN A 238    11394  11771  11525   1139  -1802    966       N  
ATOM   1708  OE1 GLN A 238      12.640  73.234   0.784  1.00 75.28           O  
ANISOU 1708  OE1 GLN A 238     9558   9664   9382   1031  -1549    842       O  
ATOM   1709  N   ASN A 239      14.185  74.721   5.853  1.00 53.34           N  
ANISOU 1709  N   ASN A 239     6605   6781   6879   1137   -901    794       N  
ATOM   1710  CA  ASN A 239      15.031  74.046   6.819  1.00 48.01           C  
ANISOU 1710  CA  ASN A 239     5916   6100   6227   1059   -781    726       C  
ATOM   1711  C   ASN A 239      14.605  74.357   8.236  1.00 49.57           C  
ANISOU 1711  C   ASN A 239     5996   6311   6525   1132   -678    740       C  
ATOM   1712  O   ASN A 239      14.656  73.503   9.120  1.00 53.27           O  
ANISOU 1712  O   ASN A 239     6366   6819   7057   1081   -622    711       O  
ATOM   1713  CB  ASN A 239      16.490  74.433   6.623  1.00 38.69           C  
ANISOU 1713  CB  ASN A 239     4918   4839   4942   1011   -692    678       C  
ATOM   1714  CG  ASN A 239      17.077  73.830   5.381  1.00 44.30           C  
ANISOU 1714  CG  ASN A 239     5735   5550   5546    926   -759    649       C  
ATOM   1715  ND2 ASN A 239      18.265  74.278   5.009  1.00 52.39           N  
ANISOU 1715  ND2 ASN A 239     6916   6515   6476    894   -687    629       N  
ATOM   1716  OD1 ASN A 239      16.475  72.957   4.768  1.00 48.16           O  
ANISOU 1716  OD1 ASN A 239     6168   6093   6039    889   -875    645       O  
ATOM   1717  N   GLN A 240      14.182  75.589   8.453  1.00 53.85           N  
ANISOU 1717  N   GLN A 240     6561   6820   7079   1260   -652    785       N  
ATOM   1718  CA  GLN A 240      13.775  75.977   9.786  1.00 57.88           C  
ANISOU 1718  CA  GLN A 240     6983   7342   7667   1351   -547    793       C  
ATOM   1719  C   GLN A 240      12.612  75.112  10.209  1.00 55.91           C  
ANISOU 1719  C   GLN A 240     6511   7203   7530   1358   -581    835       C  
ATOM   1720  O   GLN A 240      12.486  74.748  11.374  1.00 67.25           O  
ANISOU 1720  O   GLN A 240     7849   8677   9026   1369   -483    827       O  
ATOM   1721  CB  GLN A 240      13.391  77.451   9.847  1.00 58.86           C  
ANISOU 1721  CB  GLN A 240     7172   7406   7787   1504   -529    836       C  
ATOM   1722  CG  GLN A 240      12.994  77.893  11.242  1.00 55.80           C  
ANISOU 1722  CG  GLN A 240     6712   7025   7463   1616   -412    833       C  
ATOM   1723  CD  GLN A 240      14.148  77.782  12.220  1.00 58.30           C  
ANISOU 1723  CD  GLN A 240     7118   7290   7742   1556   -291    754       C  
ATOM   1724  NE2 GLN A 240      13.915  77.064  13.319  1.00 56.71           N  
ANISOU 1724  NE2 GLN A 240     6795   7158   7594   1550   -214    738       N  
ATOM   1725  OE1 GLN A 240      15.247  78.302  11.979  1.00 55.03           O  
ANISOU 1725  OE1 GLN A 240     6877   6778   7254   1509   -271    712       O  
ATOM   1726  N   ILE A 241      11.767  74.789   9.241  1.00 47.50           N  
ANISOU 1726  N   ILE A 241     5368   6189   6493   1350   -724    886       N  
ATOM   1727  CA  ILE A 241      10.643  73.899   9.453  1.00 54.83           C  
ANISOU 1727  CA  ILE A 241     6073   7220   7539   1333   -785    937       C  
ATOM   1728  C   ILE A 241      11.125  72.496   9.854  1.00 60.37           C  
ANISOU 1728  C   ILE A 241     6725   7949   8265   1184   -764    888       C  
ATOM   1729  O   ILE A 241      10.584  71.856  10.768  1.00 56.77           O  
ANISOU 1729  O   ILE A 241     6102   7558   7910   1173   -713    916       O  
ATOM   1730  CB  ILE A 241       9.782  73.846   8.195  1.00 63.76           C  
ANISOU 1730  CB  ILE A 241     7157   8385   8683   1336   -971    993       C  
ATOM   1731  CG1 ILE A 241       8.985  75.140   8.094  1.00 68.07           C  
ANISOU 1731  CG1 ILE A 241     7684   8927   9252   1507   -985   1066       C  
ATOM   1732  CG2 ILE A 241       8.865  72.629   8.203  1.00 71.27           C  
ANISOU 1732  CG2 ILE A 241     7897   9429   9752   1256  -1068   1031       C  
ATOM   1733  CD1 ILE A 241       8.419  75.394   6.738  1.00 70.10           C  
ANISOU 1733  CD1 ILE A 241     7966   9190   9480   1525  -1168   1116       C  
ATOM   1734  N   THR A 242      12.168  72.030   9.190  1.00 54.85           N  
ANISOU 1734  N   THR A 242     6174   7196   7471   1075   -794    817       N  
ATOM   1735  CA  THR A 242      12.751  70.761   9.571  1.00 59.77           C  
ANISOU 1735  CA  THR A 242     6774   7827   8110    946   -768    763       C  
ATOM   1736  C   THR A 242      13.298  70.850  11.004  1.00 55.30           C  
ANISOU 1736  C   THR A 242     6198   7251   7563    966   -596    739       C  
ATOM   1737  O   THR A 242      13.016  69.986  11.832  1.00 60.04           O  
ANISOU 1737  O   THR A 242     6669   7900   8244    922   -557    752       O  
ATOM   1738  CB  THR A 242      13.849  70.362   8.597  1.00 57.74           C  
ANISOU 1738  CB  THR A 242     6691   7511   7737    850   -814    688       C  
ATOM   1739  CG2 THR A 242      14.097  68.888   8.672  1.00 46.09           C  
ANISOU 1739  CG2 THR A 242     5167   6049   6295    722   -847    644       C  
ATOM   1740  OG1 THR A 242      13.425  70.698   7.275  1.00 65.03           O  
ANISOU 1740  OG1 THR A 242     7673   8431   8603    870   -954    713       O  
ATOM   1741  N   TYR A 243      14.058  71.912  11.281  1.00 43.55           N  
ANISOU 1741  N   TYR A 243     4851   5697   6000   1031   -503    709       N  
ATOM   1742  CA  TYR A 243      14.601  72.180  12.612  1.00 43.62           C  
ANISOU 1742  CA  TYR A 243     4878   5685   6009   1064   -354    680       C  
ATOM   1743  C   TYR A 243      13.497  72.167  13.678  1.00 45.95           C  
ANISOU 1743  C   TYR A 243     4997   6058   6402   1152   -294    741       C  
ATOM   1744  O   TYR A 243      13.672  71.620  14.775  1.00 43.73           O  
ANISOU 1744  O   TYR A 243     4661   5806   6150   1130   -201    731       O  
ATOM   1745  CB  TYR A 243      15.325  73.528  12.641  1.00 45.50           C  
ANISOU 1745  CB  TYR A 243     5287   5834   6167   1138   -294    652       C  
ATOM   1746  CG  TYR A 243      16.565  73.649  11.771  1.00 50.30           C  
ANISOU 1746  CG  TYR A 243     6069   6365   6679   1055   -316    601       C  
ATOM   1747  CD1 TYR A 243      17.275  72.520  11.351  1.00 33.85           C  
ANISOU 1747  CD1 TYR A 243     4001   4290   4571    925   -344    556       C  
ATOM   1748  CD2 TYR A 243      17.046  74.909  11.393  1.00 42.81           C  
ANISOU 1748  CD2 TYR A 243     5270   5331   5665   1110   -302    602       C  
ATOM   1749  CE1 TYR A 243      18.417  72.630  10.583  1.00 33.30           C  
ANISOU 1749  CE1 TYR A 243     4080   4161   4412    861   -344    514       C  
ATOM   1750  CE2 TYR A 243      18.202  75.040  10.609  1.00 44.51           C  
ANISOU 1750  CE2 TYR A 243     5634   5484   5795   1031   -306    569       C  
ATOM   1751  CZ  TYR A 243      18.881  73.893  10.202  1.00 57.56           C  
ANISOU 1751  CZ  TYR A 243     7288   7161   7422    910   -322    526       C  
ATOM   1752  OH  TYR A 243      20.016  74.011   9.422  1.00 46.33           O  
ANISOU 1752  OH  TYR A 243     6001   5686   5914    843   -312    500       O  
ATOM   1753  N   ASP A 244      12.361  72.767  13.344  1.00 44.41           N  
ANISOU 1753  N   ASP A 244     4713   5903   6256   1256   -345    812       N  
ATOM   1754  CA  ASP A 244      11.215  72.826  14.246  1.00 58.51           C  
ANISOU 1754  CA  ASP A 244     6317   7776   8140   1357   -284    884       C  
ATOM   1755  C   ASP A 244      10.677  71.442  14.588  1.00 62.90           C  
ANISOU 1755  C   ASP A 244     6685   8419   8794   1257   -302    926       C  
ATOM   1756  O   ASP A 244      10.469  71.131  15.753  1.00 68.96           O  
ANISOU 1756  O   ASP A 244     7359   9237   9603   1281   -188    949       O  
ATOM   1757  CB  ASP A 244      10.090  73.666  13.635  1.00 67.02           C  
ANISOU 1757  CB  ASP A 244     7322   8881   9263   1483   -357    959       C  
ATOM   1758  CG  ASP A 244      10.357  75.152  13.726  1.00 70.58           C  
ANISOU 1758  CG  ASP A 244     7923   9250   9644   1626   -301    938       C  
ATOM   1759  OD1 ASP A 244      11.350  75.530  14.384  1.00 74.32           O  
ANISOU 1759  OD1 ASP A 244     8543   9651  10044   1626   -200    868       O  
ATOM   1760  OD2 ASP A 244       9.563  75.940  13.163  1.00 71.83           O1-
ANISOU 1760  OD2 ASP A 244     8053   9412   9827   1738   -365    995       O1-
ATOM   1761  N   ARG A 245      10.446  70.623  13.567  1.00 63.43           N  
ANISOU 1761  N   ARG A 245     6706   8500   8894   1146   -450    937       N  
ATOM   1762  CA  ARG A 245       9.932  69.271  13.767  1.00 57.42           C  
ANISOU 1762  CA  ARG A 245     5775   7804   8237   1033   -494    978       C  
ATOM   1763  C   ARG A 245      10.880  68.431  14.602  1.00 50.48           C  
ANISOU 1763  C   ARG A 245     4946   6900   7333    938   -400    923       C  
ATOM   1764  O   ARG A 245      10.452  67.581  15.381  1.00 53.12           O  
ANISOU 1764  O   ARG A 245     5135   7292   7755    892   -357    973       O  
ATOM   1765  CB  ARG A 245       9.697  68.574  12.430  1.00 49.08           C  
ANISOU 1765  CB  ARG A 245     4711   6739   7198    924   -688    975       C  
ATOM   1766  CG  ARG A 245       8.619  69.184  11.601  1.00 60.16           C  
ANISOU 1766  CG  ARG A 245     6032   8181   8645   1000   -810   1043       C  
ATOM   1767  CD  ARG A 245       8.566  68.538  10.227  1.00 64.92           C  
ANISOU 1767  CD  ARG A 245     6677   8761   9230    891  -1013   1020       C  
ATOM   1768  NE  ARG A 245       7.911  67.241  10.275  1.00 70.40           N  
ANISOU 1768  NE  ARG A 245     7198   9501  10049    769  -1105   1060       N  
ATOM   1769  CZ  ARG A 245       7.951  66.351   9.292  1.00 72.74           C  
ANISOU 1769  CZ  ARG A 245     7531   9768  10339    645  -1277   1023       C  
ATOM   1770  NH1 ARG A 245       8.638  66.618   8.185  1.00 70.75           N1+
ANISOU 1770  NH1 ARG A 245     7484   9452   9948    636  -1361    947       N1+
ATOM   1771  NH2 ARG A 245       7.317  65.189   9.426  1.00 71.31           N  
ANISOU 1771  NH2 ARG A 245     7187   9620  10289    531  -1364   1065       N  
ATOM   1772  N   LEU A 246      12.170  68.664  14.401  1.00 48.45           N  
ANISOU 1772  N   LEU A 246     4892   6557   6961    907   -373    829       N  
ATOM   1773  CA  LEU A 246      13.214  67.961  15.131  1.00 53.24           C  
ANISOU 1773  CA  LEU A 246     5565   7130   7535    825   -291    770       C  
ATOM   1774  C   LEU A 246      13.456  68.547  16.507  1.00 61.13           C  
ANISOU 1774  C   LEU A 246     6579   8138   8509    916   -129    770       C  
ATOM   1775  O   LEU A 246      14.425  68.176  17.162  1.00 63.79           O  
ANISOU 1775  O   LEU A 246     6995   8440   8801    867    -59    717       O  
ATOM   1776  CB  LEU A 246      14.529  67.985  14.351  1.00 44.39           C  
ANISOU 1776  CB  LEU A 246     4641   5919   6306    758   -326    675       C  
ATOM   1777  CG  LEU A 246      14.567  67.106  13.124  1.00 48.54           C  
ANISOU 1777  CG  LEU A 246     5183   6429   6832    650   -471    651       C  
ATOM   1778  CD1 LEU A 246      15.973  67.031  12.574  1.00 52.00           C  
ANISOU 1778  CD1 LEU A 246     5806   6789   7161    592   -464    559       C  
ATOM   1779  CD2 LEU A 246      14.074  65.744  13.533  1.00 55.93           C  
ANISOU 1779  CD2 LEU A 246     5973   7405   7873    555   -505    684       C  
ATOM   1780  N   ASN A 247      12.590  69.469  16.925  1.00 68.84           N  
ANISOU 1780  N   ASN A 247     7490   9159   9509   1057    -74    825       N  
ATOM   1781  CA  ASN A 247      12.760  70.208  18.173  1.00 74.14           C  
ANISOU 1781  CA  ASN A 247     8202   9831  10137   1171     76    814       C  
ATOM   1782  C   ASN A 247      14.225  70.556  18.429  1.00 72.09           C  
ANISOU 1782  C   ASN A 247     8149   9474   9767   1141    121    713       C  
ATOM   1783  O   ASN A 247      14.770  70.307  19.511  1.00 69.25           O  
ANISOU 1783  O   ASN A 247     7821   9114   9378   1134    216    687       O  
ATOM   1784  CB  ASN A 247      12.203  69.415  19.351  1.00 79.76           C  
ANISOU 1784  CB  ASN A 247     8758  10632  10914   1169    170    878       C  
ATOM   1785  CG  ASN A 247      11.898  70.293  20.544  1.00 86.90           C  
ANISOU 1785  CG  ASN A 247     9669  11568  11782   1331    319    892       C  
ATOM   1786  ND2 ASN A 247      12.218  69.797  21.733  1.00 83.91           N  
ANISOU 1786  ND2 ASN A 247     9286  11217  11378   1321    428    891       N  
ATOM   1787  OD1 ASN A 247      11.404  71.418  20.397  1.00 93.10           O  
ANISOU 1787  OD1 ASN A 247    10474  12347  12554   1471    333    901       O  
ATOM   1788  N   VAL A 248      14.868  71.091  17.398  1.00 61.30           N  
ANISOU 1788  N   VAL A 248     6920   8029   8344   1116     47    664       N  
ATOM   1789  CA  VAL A 248      16.238  71.558  17.505  1.00 55.34           C  
ANISOU 1789  CA  VAL A 248     6350   7179   7497   1086     81    580       C  
ATOM   1790  C   VAL A 248      16.251  73.072  17.855  1.00 48.33           C  
ANISOU 1790  C   VAL A 248     5571   6233   6559   1225    135    565       C  
ATOM   1791  O   VAL A 248      15.344  73.840  17.500  1.00 41.99           O  
ANISOU 1791  O   VAL A 248     4735   5443   5779   1333    113    611       O  
ATOM   1792  CB  VAL A 248      17.008  71.244  16.207  1.00 54.23           C  
ANISOU 1792  CB  VAL A 248     6299   6986   7321    976    -16    542       C  
ATOM   1793  CG1 VAL A 248      18.242  72.085  16.081  1.00 54.57           C  
ANISOU 1793  CG1 VAL A 248     6524   6931   7279    969     13    479       C  
ATOM   1794  CG2 VAL A 248      17.353  69.744  16.140  1.00 48.72           C  
ANISOU 1794  CG2 VAL A 248     5541   6316   6654    841    -48    526       C  
ATOM   1795  N   THR A 249      17.255  73.485  18.614  1.00 49.07           N  
ANISOU 1795  N   THR A 249     5793   6261   6591   1225    202    500       N  
ATOM   1796  CA  THR A 249      17.309  74.850  19.107  1.00 51.15           C  
ANISOU 1796  CA  THR A 249     6171   6456   6808   1350    252    476       C  
ATOM   1797  C   THR A 249      17.758  75.854  18.060  1.00 54.89           C  
ANISOU 1797  C   THR A 249     6781   6829   7246   1353    187    461       C  
ATOM   1798  O   THR A 249      17.798  77.042  18.356  1.00 52.46           O  
ANISOU 1798  O   THR A 249     6580   6444   6907   1454    212    442       O  
ATOM   1799  CB  THR A 249      18.249  74.965  20.295  1.00 47.06           C  
ANISOU 1799  CB  THR A 249     5753   5891   6235   1343    327    408       C  
ATOM   1800  CG2 THR A 249      17.753  74.113  21.449  1.00 44.84           C  
ANISOU 1800  CG2 THR A 249     5355   5709   5974   1363    406    433       C  
ATOM   1801  OG1 THR A 249      19.557  74.534  19.890  1.00 47.71           O  
ANISOU 1801  OG1 THR A 249     5918   5919   6292   1199    289    359       O  
ATOM   1802  N   LEU A 250      18.092  75.389  16.853  1.00 33.42           N  
ANISOU 1802  N   LEU A 250     4067   4106   4526   1247    105    470       N  
ATOM   1803  CA  LEU A 250      18.501  76.308  15.797  1.00 47.70           C  
ANISOU 1803  CA  LEU A 250     6004   5827   6293   1247     49    471       C  
ATOM   1804  C   LEU A 250      17.381  77.265  15.376  1.00 50.96           C  
ANISOU 1804  C   LEU A 250     6402   6236   6726   1385     13    530       C  
ATOM   1805  O   LEU A 250      16.231  76.869  15.199  1.00 57.83           O  
ANISOU 1805  O   LEU A 250     7127   7196   7651   1434    -19    586       O  
ATOM   1806  CB  LEU A 250      19.009  75.544  14.588  1.00 44.68           C  
ANISOU 1806  CB  LEU A 250     5629   5457   5892   1118    -24    473       C  
ATOM   1807  CG  LEU A 250      20.475  75.132  14.667  1.00 49.48           C  
ANISOU 1807  CG  LEU A 250     6322   6019   6460    996      7    413       C  
ATOM   1808  CD1 LEU A 250      20.791  74.309  13.465  1.00 47.36           C  
ANISOU 1808  CD1 LEU A 250     6048   5776   6169    896    -57    415       C  
ATOM   1809  CD2 LEU A 250      21.392  76.342  14.729  1.00 42.53           C  
ANISOU 1809  CD2 LEU A 250     5600   5024   5537   1007     35    389       C  
ATOM   1810  N   THR A 251      17.727  78.543  15.254  1.00 50.41           N  
ANISOU 1810  N   THR A 251     6478   6057   6618   1448     16    520       N  
ATOM   1811  CA  THR A 251      16.787  79.549  14.769  1.00 55.43           C  
ANISOU 1811  CA  THR A 251     7125   6667   7269   1584    -25    576       C  
ATOM   1812  C   THR A 251      17.413  80.386  13.666  1.00 55.80           C  
ANISOU 1812  C   THR A 251     7329   6608   7266   1551    -86    591       C  
ATOM   1813  O   THR A 251      18.616  80.313  13.406  1.00 58.00           O  
ANISOU 1813  O   THR A 251     7710   6828   7500   1433    -79    556       O  
ATOM   1814  CB  THR A 251      16.325  80.474  15.890  1.00 65.40           C  
ANISOU 1814  CB  THR A 251     8416   7890   8542   1744     50    559       C  
ATOM   1815  CG2 THR A 251      16.090  79.676  17.179  1.00 60.91           C  
ANISOU 1815  CG2 THR A 251     7735   7411   7995   1757    139    532       C  
ATOM   1816  OG1 THR A 251      17.317  81.487  16.107  1.00 73.17           O  
ANISOU 1816  OG1 THR A 251     9596   8727   9477   1740     67    508       O  
ATOM   1817  N   ARG A 252      16.610  81.202  13.013  1.00 63.02           N  
ANISOU 1817  N   ARG A 252     8257   7497   8188   1659   -143    652       N  
ATOM   1818  CA  ARG A 252      17.163  81.922  11.887  1.00 61.54           C  
ANISOU 1818  CA  ARG A 252     8217   7217   7949   1622   -203    682       C  
ATOM   1819  C   ARG A 252      18.081  83.058  12.329  1.00 56.94           C  
ANISOU 1819  C   ARG A 252     7814   6480   7339   1631   -157    648       C  
ATOM   1820  O   ARG A 252      18.995  83.433  11.596  1.00 59.85           O  
ANISOU 1820  O   ARG A 252     8309   6769   7663   1542   -178    661       O  
ATOM   1821  CB  ARG A 252      16.048  82.398  10.979  1.00 55.75           C  
ANISOU 1821  CB  ARG A 252     7448   6503   7229   1728   -293    766       C  
ATOM   1822  CG  ARG A 252      15.683  81.266  10.024  1.00 55.43           C  
ANISOU 1822  CG  ARG A 252     7299   6580   7183   1642   -377    797       C  
ATOM   1823  CD  ARG A 252      15.959  81.659   8.591  1.00 63.96           C  
ANISOU 1823  CD  ARG A 252     8497   7615   8189   1605   -465    848       C  
ATOM   1824  NE  ARG A 252      14.730  81.714   7.811  1.00 71.71           N  
ANISOU 1824  NE  ARG A 252     9397   8658   9193   1691   -578    923       N  
ATOM   1825  CZ  ARG A 252      14.621  82.303   6.629  1.00 83.23           C  
ANISOU 1825  CZ  ARG A 252    10954  10078  10592   1712   -669    987       C  
ATOM   1826  NH1 ARG A 252      13.460  82.290   5.993  1.00 93.00           N1+
ANISOU 1826  NH1 ARG A 252    12102  11379  11856   1792   -783   1054       N1+
ATOM   1827  NH2 ARG A 252      15.666  82.916   6.091  1.00 90.01           N  
ANISOU 1827  NH2 ARG A 252    11998  10835  11368   1654   -647    992       N  
ATOM   1828  N   ASP A 253      17.906  83.540  13.555  1.00 52.67           N  
ANISOU 1828  N   ASP A 253     7287   5900   6824   1728    -93    602       N  
ATOM   1829  CA  ASP A 253      18.887  84.446  14.133  1.00 60.20           C  
ANISOU 1829  CA  ASP A 253     8411   6706   7757   1713    -58    551       C  
ATOM   1830  C   ASP A 253      20.263  83.764  14.312  1.00 57.46           C  
ANISOU 1830  C   ASP A 253     8093   6354   7384   1532    -28    498       C  
ATOM   1831  O   ASP A 253      21.284  84.438  14.489  1.00 60.36           O  
ANISOU 1831  O   ASP A 253     8599   6597   7738   1472    -21    470       O  
ATOM   1832  CB  ASP A 253      18.373  84.995  15.469  1.00 65.32           C  
ANISOU 1832  CB  ASP A 253     9072   7323   8425   1863      3    500       C  
ATOM   1833  N   ASP A 254      20.300  82.435  14.240  1.00 57.07           N  
ANISOU 1833  N   ASP A 254     7912   6433   7337   1444    -18    490       N  
ATOM   1834  CA  ASP A 254      21.566  81.711  14.370  1.00 58.78           C  
ANISOU 1834  CA  ASP A 254     8142   6654   7535   1285      9    444       C  
ATOM   1835  C   ASP A 254      22.230  81.424  13.029  1.00 62.99           C  
ANISOU 1835  C   ASP A 254     8708   7192   8035   1166    -29    484       C  
ATOM   1836  O   ASP A 254      23.276  80.778  12.987  1.00 63.66           O  
ANISOU 1836  O   ASP A 254     8793   7289   8106   1040     -4    454       O  
ATOM   1837  CB  ASP A 254      21.383  80.376  15.097  1.00 55.32           C  
ANISOU 1837  CB  ASP A 254     7559   6342   7117   1251     47    408       C  
ATOM   1838  CG  ASP A 254      20.460  80.472  16.273  1.00 63.43           C  
ANISOU 1838  CG  ASP A 254     8523   7406   8170   1382     92    390       C  
ATOM   1839  OD1 ASP A 254      20.194  81.587  16.744  1.00 76.29           O  
ANISOU 1839  OD1 ASP A 254    10241   8950   9796   1497    106    380       O  
ATOM   1840  OD2 ASP A 254      19.990  79.422  16.734  1.00 68.68           O1-
ANISOU 1840  OD2 ASP A 254     9051   8186   8860   1374    118    388       O1-
ATOM   1841  N   VAL A 255      21.630  81.858  11.926  1.00 53.39           N  
ANISOU 1841  N   VAL A 255     7516   5971   6799   1212    -87    554       N  
ATOM   1842  CA  VAL A 255      22.287  81.608  10.657  1.00 52.40           C  
ANISOU 1842  CA  VAL A 255     7439   5852   6621   1107   -115    592       C  
ATOM   1843  C   VAL A 255      23.442  82.575  10.473  1.00 56.61           C  
ANISOU 1843  C   VAL A 255     8123   6253   7135   1043    -91    606       C  
ATOM   1844  O   VAL A 255      23.262  83.784  10.513  1.00 63.44           O  
ANISOU 1844  O   VAL A 255     9088   7006   8009   1114   -108    637       O  
ATOM   1845  CB  VAL A 255      21.344  81.718   9.471  1.00 50.28           C  
ANISOU 1845  CB  VAL A 255     7160   5624   6321   1168   -195    665       C  
ATOM   1846  CG1 VAL A 255      22.131  81.537   8.208  1.00 51.00           C  
ANISOU 1846  CG1 VAL A 255     7328   5714   6335   1066   -210    702       C  
ATOM   1847  CG2 VAL A 255      20.252  80.661   9.571  1.00 49.94           C  
ANISOU 1847  CG2 VAL A 255     6952   5714   6309   1206   -232    658       C  
ATOM   1848  N   MET A 256      24.640  82.020  10.332  1.00 59.63           N  
ANISOU 1848  N   MET A 256     8513   6645   7500    909    -50    583       N  
ATOM   1849  CA  MET A 256      25.851  82.782  10.051  1.00 53.03           C  
ANISOU 1849  CA  MET A 256     7794   5700   6655    820    -23    609       C  
ATOM   1850  C   MET A 256      26.481  82.112   8.845  1.00 55.61           C  
ANISOU 1850  C   MET A 256     8116   6092   6919    724     -8    647       C  
ATOM   1851  O   MET A 256      27.295  81.193   8.991  1.00 66.74           O  
ANISOU 1851  O   MET A 256     9468   7560   8330    632     37    605       O  
ATOM   1852  CB  MET A 256      26.811  82.799  11.259  1.00 40.45           C  
ANISOU 1852  CB  MET A 256     6204   4052   5112    755     22    540       C  
ATOM   1853  CG  MET A 256      26.126  83.175  12.556  1.00 42.31           C  
ANISOU 1853  CG  MET A 256     6434   4253   5389    861     15    483       C  
ATOM   1854  SD  MET A 256      27.075  83.021  14.081  1.00 67.21           S  
ANISOU 1854  SD  MET A 256     9588   7364   8584    801     50    389       S  
ATOM   1855  CE  MET A 256      28.207  84.405  14.019  1.00 69.87           C  
ANISOU 1855  CE  MET A 256    10086   7514   8948    724     32    413       C  
ATOM   1856  N   GLY A 257      26.069  82.547   7.659  1.00 48.28           N  
ANISOU 1856  N   GLY A 257     7253   5159   5931    756    -47    726       N  
ATOM   1857  CA  GLY A 257      26.447  81.877   6.429  1.00 54.64           C  
ANISOU 1857  CA  GLY A 257     8066   6042   6653    693    -39    761       C  
ATOM   1858  C   GLY A 257      27.793  82.332   5.924  1.00 55.79           C  
ANISOU 1858  C   GLY A 257     8297   6127   6773    587     27    810       C  
ATOM   1859  O   GLY A 257      28.365  83.273   6.477  1.00 60.93           O  
ANISOU 1859  O   GLY A 257     9007   6662   7480    558     49    826       O  
ATOM   1860  N   GLU A 258      28.298  81.673   4.881  1.00 45.33           N  
ANISOU 1860  N   GLU A 258     6981   4879   5365    530     59    835       N  
ATOM   1861  CA  GLU A 258      29.593  82.034   4.320  1.00 47.64           C  
ANISOU 1861  CA  GLU A 258     7338   5133   5630    430    139    895       C  
ATOM   1862  C   GLU A 258      29.602  83.486   3.883  1.00 53.52           C  
ANISOU 1862  C   GLU A 258     8211   5756   6370    443    125   1001       C  
ATOM   1863  O   GLU A 258      30.607  84.194   4.031  1.00 51.91           O  
ANISOU 1863  O   GLU A 258     8052   5461   6210    359    179   1047       O  
ATOM   1864  CB  GLU A 258      29.934  81.154   3.132  1.00 60.97           C  
ANISOU 1864  CB  GLU A 258     9032   6930   7204    400    176    911       C  
ATOM   1865  CG  GLU A 258      30.277  79.725   3.450  1.00 65.61           C  
ANISOU 1865  CG  GLU A 258     9511   7620   7799    366    208    814       C  
ATOM   1866  CD  GLU A 258      30.495  78.956   2.181  1.00 78.32           C  
ANISOU 1866  CD  GLU A 258    11156   9323   9280    359    234    828       C  
ATOM   1867  OE1 GLU A 258      29.522  78.845   1.391  1.00 84.07           O  
ANISOU 1867  OE1 GLU A 258    11931  10091   9921    428    154    844       O  
ATOM   1868  OE2 GLU A 258      31.643  78.517   1.946  1.00 75.68           O1-
ANISOU 1868  OE2 GLU A 258    10807   9021   8927    289    332    825       O1-
ATOM   1869  N   SER A 259      28.465  83.903   3.331  1.00 52.36           N  
ANISOU 1869  N   SER A 259     8117   5603   6173    546     45   1044       N  
ATOM   1870  CA  SER A 259      28.250  85.276   2.905  1.00 59.74           C  
ANISOU 1870  CA  SER A 259     9180   6416   7102    583     13   1148       C  
ATOM   1871  C   SER A 259      28.717  86.262   3.965  1.00 62.25           C  
ANISOU 1871  C   SER A 259     9532   6584   7537    554     25   1140       C  
ATOM   1872  O   SER A 259      29.480  87.171   3.674  1.00 61.99           O  
ANISOU 1872  O   SER A 259     9593   6443   7518    486     56   1223       O  
ATOM   1873  CB  SER A 259      26.770  85.512   2.599  1.00 64.26           C  
ANISOU 1873  CB  SER A 259     9769   7002   7645    723    -94   1166       C  
ATOM   1874  OG  SER A 259      25.983  85.263   3.758  1.00 66.07           O  
ANISOU 1874  OG  SER A 259     9899   7241   7962    797   -133   1074       O  
ATOM   1875  N   LEU A 260      28.262  86.063   5.197  1.00 63.00           N  
ANISOU 1875  N   LEU A 260     9554   6672   7713    604     -1   1040       N  
ATOM   1876  CA  LEU A 260      28.658  86.898   6.325  1.00 59.26           C  
ANISOU 1876  CA  LEU A 260     9117   6059   7340    588     -1   1007       C  
ATOM   1877  C   LEU A 260      30.113  87.363   6.299  1.00 51.96           C  
ANISOU 1877  C   LEU A 260     8240   5048   6455    440     58   1051       C  
ATOM   1878  O   LEU A 260      30.417  88.461   6.740  1.00 55.48           O  
ANISOU 1878  O   LEU A 260     8777   5337   6968    421     35   1075       O  
ATOM   1879  CB  LEU A 260      28.411  86.138   7.635  1.00 64.65           C  
ANISOU 1879  CB  LEU A 260     9688   6798   8080    616      1    879       C  
ATOM   1880  CG  LEU A 260      28.541  86.957   8.923  1.00 66.58           C  
ANISOU 1880  CG  LEU A 260     9980   6907   8411    637    -17    824       C  
ATOM   1881  CD1 LEU A 260      27.340  87.868   9.095  1.00 61.81           C  
ANISOU 1881  CD1 LEU A 260     9446   6223   7815    794    -80    836       C  
ATOM   1882  CD2 LEU A 260      28.734  86.057  10.142  1.00 63.28           C  
ANISOU 1882  CD2 LEU A 260     9454   6557   8031    621      7    708       C  
ATOM   1883  N   TYR A 261      31.005  86.524   5.780  1.00 49.37           N  
ANISOU 1883  N   TYR A 261     7849   4819   6090    337    130   1063       N  
ATOM   1884  CA  TYR A 261      32.439  86.792   5.834  1.00 55.28           C  
ANISOU 1884  CA  TYR A 261     8602   5512   6891    190    195   1103       C  
ATOM   1885  C   TYR A 261      33.027  87.461   4.583  1.00 66.73           C  
ANISOU 1885  C   TYR A 261    10141   6922   8291    123    242   1250       C  
ATOM   1886  O   TYR A 261      34.186  87.863   4.595  1.00 62.95           O  
ANISOU 1886  O   TYR A 261     9667   6381   7871     -2    294   1307       O  
ATOM   1887  CB  TYR A 261      33.178  85.479   6.121  1.00 50.07           C  
ANISOU 1887  CB  TYR A 261     7805   4983   6235    120    260   1029       C  
ATOM   1888  CG  TYR A 261      32.636  84.824   7.354  1.00 56.93           C  
ANISOU 1888  CG  TYR A 261     8592   5890   7151    178    220    899       C  
ATOM   1889  CD1 TYR A 261      32.971  85.298   8.617  1.00 65.84           C  
ANISOU 1889  CD1 TYR A 261     9723   6917   8375    153    190    840       C  
ATOM   1890  CD2 TYR A 261      31.748  83.760   7.265  1.00 56.99           C  
ANISOU 1890  CD2 TYR A 261     8524   6027   7101    261    204    838       C  
ATOM   1891  CE1 TYR A 261      32.451  84.718   9.764  1.00 60.23           C  
ANISOU 1891  CE1 TYR A 261     8947   6246   7693    215    160    728       C  
ATOM   1892  CE2 TYR A 261      31.226  83.172   8.404  1.00 53.85           C  
ANISOU 1892  CE2 TYR A 261     8049   5666   6747    313    175    734       C  
ATOM   1893  CZ  TYR A 261      31.580  83.654   9.646  1.00 51.17           C  
ANISOU 1893  CZ  TYR A 261     7717   5234   6491    294    159    682       C  
ATOM   1894  OH  TYR A 261      31.055  83.082  10.772  1.00 50.83           O  
ANISOU 1894  OH  TYR A 261     7606   5233   6476    352    139    586       O  
ATOM   1895  N   ASN A 262      32.235  87.583   3.518  1.00 76.12           N  
ANISOU 1895  N   ASN A 262    11399   8149   9375    205    219   1319       N  
ATOM   1896  CA  ASN A 262      32.700  88.184   2.256  1.00 72.35           C  
ANISOU 1896  CA  ASN A 262    11019   7645   8824    155    266   1470       C  
ATOM   1897  C   ASN A 262      33.496  89.466   2.455  1.00 69.16           C  
ANISOU 1897  C   ASN A 262    10698   7062   8516     59    276   1564       C  
ATOM   1898  O   ASN A 262      34.656  89.539   2.042  1.00 69.14           O  
ANISOU 1898  O   ASN A 262    10682   7062   8527    -68    365   1645       O  
ATOM   1899  CB  ASN A 262      31.526  88.477   1.321  1.00 66.06           C  
ANISOU 1899  CB  ASN A 262    10316   6864   7919    279    199   1531       C  
ATOM   1900  CG  ASN A 262      30.892  87.217   0.770  1.00 82.36           C  
ANISOU 1900  CG  ASN A 262    12315   9108   9870    347    190   1470       C  
ATOM   1901  ND2 ASN A 262      30.140  87.368  -0.310  1.00 81.53           N  
ANISOU 1901  ND2 ASN A 262    12293   9039   9646    426    143   1543       N  
ATOM   1902  OD1 ASN A 262      31.070  86.118   1.311  1.00 92.85           O  
ANISOU 1902  OD1 ASN A 262    13523  10536  11218    328    216   1360       O  
ATOM   1903  N   PRO A 263      32.879  90.472   3.102  1.00 62.98           N  
ANISOU 1903  N   PRO A 263     9999   6123   7807    120    184   1553       N  
ATOM   1904  CA  PRO A 263      33.510  91.769   3.391  1.00 64.74           C  
ANISOU 1904  CA  PRO A 263    10320   6144   8134     36    165   1629       C  
ATOM   1905  C   PRO A 263      34.923  91.653   3.995  1.00 70.26           C  
ANISOU 1905  C   PRO A 263    10941   6817   8940   -133    223   1617       C  
ATOM   1906  O   PRO A 263      35.754  92.536   3.743  1.00 68.42           O  
ANISOU 1906  O   PRO A 263    10768   6457   8769   -251    242   1731       O  
ATOM   1907  CB  PRO A 263      32.545  92.415   4.399  1.00 51.57           C  
ANISOU 1907  CB  PRO A 263     8713   4350   6532    156     55   1541       C  
ATOM   1908  N   MET A 264      35.213  90.591   4.751  1.00 63.65           N  
ANISOU 1908  N   MET A 264     9967   6092   8126   -151    248   1492       N  
ATOM   1909  CA  MET A 264      36.527  90.521   5.385  1.00 58.96           C  
ANISOU 1909  CA  MET A 264     9293   5466   7643   -305    285   1480       C  
ATOM   1910  C   MET A 264      37.546  89.689   4.591  1.00 63.53           C  
ANISOU 1910  C   MET A 264     9763   6193   8181   -405    413   1544       C  
ATOM   1911  O   MET A 264      38.730  89.700   4.929  1.00 61.35           O  
ANISOU 1911  O   MET A 264     9411   5895   8003   -542    454   1567       O  
ATOM   1912  CB  MET A 264      36.402  90.002   6.826  1.00 52.81           C  
ANISOU 1912  CB  MET A 264     8440   4695   6932   -277    229   1313       C  
ATOM   1913  CG  MET A 264      35.560  88.762   6.998  1.00 60.45           C  
ANISOU 1913  CG  MET A 264     9320   5833   7817   -159    236   1202       C  
ATOM   1914  SD  MET A 264      35.196  88.328   8.715  1.00 70.14           S  
ANISOU 1914  SD  MET A 264    10489   7052   9110   -101    166   1024       S  
ATOM   1915  CE  MET A 264      36.865  88.061   9.360  1.00 44.85           C  
ANISOU 1915  CE  MET A 264     7187   3836   6016   -284    200   1011       C  
ATOM   1916  N   LEU A 265      37.101  89.033   3.514  1.00 62.79           N  
ANISOU 1916  N   LEU A 265     9668   6242   7946   -334    471   1579       N  
ATOM   1917  CA  LEU A 265      37.956  88.111   2.746  1.00 63.23           C  
ANISOU 1917  CA  LEU A 265     9629   6455   7940   -395    599   1620       C  
ATOM   1918  C   LEU A 265      39.133  88.803   2.020  1.00 56.81           C  
ANISOU 1918  C   LEU A 265     8830   5594   7159   -534    695   1789       C  
ATOM   1919  O   LEU A 265      40.277  88.353   2.153  1.00 59.49           O  
ANISOU 1919  O   LEU A 265     9049   5992   7561   -640    782   1802       O  
ATOM   1920  CB  LEU A 265      37.109  87.289   1.737  1.00 57.07           C  
ANISOU 1920  CB  LEU A 265     8873   5827   6986   -275    621   1608       C  
ATOM   1921  CG  LEU A 265      35.995  86.390   2.318  1.00 56.56           C  
ANISOU 1921  CG  LEU A 265     8763   5840   6887   -151    541   1453       C  
ATOM   1922  CD1 LEU A 265      35.245  85.547   1.278  1.00 42.79           C  
ANISOU 1922  CD1 LEU A 265     7039   4240   4980    -53    549   1444       C  
ATOM   1923  CD2 LEU A 265      36.555  85.513   3.422  1.00 56.56           C  
ANISOU 1923  CD2 LEU A 265     8622   5890   6979   -196    554   1330       C  
ATOM   1924  N   PRO A 266      38.873  89.880   1.247  1.00 58.36           N  
ANISOU 1924  N   PRO A 266     9166   5688   7319   -534    685   1929       N  
ATOM   1925  CA  PRO A 266      40.049  90.557   0.677  1.00 58.31           C  
ANISOU 1925  CA  PRO A 266     9160   5629   7365   -682    780   2099       C  
ATOM   1926  C   PRO A 266      40.955  91.145   1.748  1.00 53.38           C  
ANISOU 1926  C   PRO A 266     8475   4865   6942   -825    740   2092       C  
ATOM   1927  O   PRO A 266      42.156  91.201   1.526  1.00 57.90           O  
ANISOU 1927  O   PRO A 266     8961   5453   7586   -964    835   2191       O  
ATOM   1928  CB  PRO A 266      39.447  91.669  -0.201  1.00 63.27           C  
ANISOU 1928  CB  PRO A 266     9967   6147   7924   -645    749   2243       C  
ATOM   1929  CG  PRO A 266      38.031  91.793   0.208  1.00 62.87           C  
ANISOU 1929  CG  PRO A 266    10003   6048   7836   -490    611   2135       C  
ATOM   1930  CD  PRO A 266      37.608  90.467   0.759  1.00 65.01           C  
ANISOU 1930  CD  PRO A 266    10157   6474   8069   -407    601   1956       C  
ATOM   1931  N   GLY A 267      40.390  91.562   2.881  1.00 53.28           N  
ANISOU 1931  N   GLY A 267     8505   4721   7017   -788    601   1977       N  
ATOM   1932  CA  GLY A 267      41.184  92.024   4.008  1.00 56.72           C  
ANISOU 1932  CA  GLY A 267     8893   5026   7633   -912    538   1940       C  
ATOM   1933  C   GLY A 267      42.132  90.960   4.555  1.00 68.80           C  
ANISOU 1933  C   GLY A 267    10233   6688   9222   -985    598   1865       C  
ATOM   1934  O   GLY A 267      43.139  91.285   5.189  1.00 68.75           O  
ANISOU 1934  O   GLY A 267    10156   6602   9365  -1127    577   1883       O  
ATOM   1935  N   ILE A 268      41.808  89.691   4.298  1.00 65.60           N  
ANISOU 1935  N   ILE A 268     9747   6477   8703   -889    662   1784       N  
ATOM   1936  CA  ILE A 268      42.561  88.562   4.826  1.00 54.29           C  
ANISOU 1936  CA  ILE A 268     8140   5175   7313   -927    712   1698       C  
ATOM   1937  C   ILE A 268      43.572  88.049   3.823  1.00 57.21           C  
ANISOU 1937  C   ILE A 268     8407   5681   7651   -998    876   1813       C  
ATOM   1938  O   ILE A 268      44.730  87.812   4.162  1.00 61.16           O  
ANISOU 1938  O   ILE A 268     8768   6208   8263  -1113    925   1836       O  
ATOM   1939  CB  ILE A 268      41.635  87.416   5.235  1.00 51.77           C  
ANISOU 1939  CB  ILE A 268     7790   4977   6901   -782    681   1534       C  
ATOM   1940  CG1 ILE A 268      40.730  87.874   6.377  1.00 47.92           C  
ANISOU 1940  CG1 ILE A 268     7382   4368   6458   -712    534   1417       C  
ATOM   1941  CG2 ILE A 268      42.455  86.217   5.692  1.00 58.15           C  
ANISOU 1941  CG2 ILE A 268     8424   5918   7750   -819    739   1459       C  
ATOM   1942  CD1 ILE A 268      39.740  86.879   6.795  1.00 52.71           C  
ANISOU 1942  CD1 ILE A 268     7961   5081   6985   -574    501   1276       C  
ATOM   1943  N   VAL A 269      43.143  87.871   2.583  1.00 55.08           N  
ANISOU 1943  N   VAL A 269     8204   5502   7224   -923    962   1887       N  
ATOM   1944  CA  VAL A 269      44.082  87.483   1.557  1.00 65.81           C  
ANISOU 1944  CA  VAL A 269     9487   6985   8532   -977   1132   2008       C  
ATOM   1945  C   VAL A 269      45.172  88.561   1.477  1.00 79.43           C  
ANISOU 1945  C   VAL A 269    11186   8595  10399  -1150   1171   2176       C  
ATOM   1946  O   VAL A 269      46.351  88.263   1.253  1.00 80.88           O  
ANISOU 1946  O   VAL A 269    11228   8857  10646  -1248   1292   2255       O  
ATOM   1947  CB  VAL A 269      43.383  87.294   0.203  1.00 71.86           C  
ANISOU 1947  CB  VAL A 269    10368   7846   9089   -865   1202   2069       C  
ATOM   1948  CG1 VAL A 269      44.387  87.353  -0.951  1.00 74.21           C  
ANISOU 1948  CG1 VAL A 269    10633   8230   9335   -935   1384   2243       C  
ATOM   1949  CG2 VAL A 269      42.599  85.982   0.190  1.00 61.22           C  
ANISOU 1949  CG2 VAL A 269     9002   6644   7615   -720   1187   1910       C  
ATOM   1950  N   ALA A 270      44.781  89.811   1.704  1.00 75.40           N  
ANISOU 1950  N   ALA A 270    10806   7892   9952  -1189   1064   2231       N  
ATOM   1951  CA  ALA A 270      45.747  90.902   1.685  1.00 73.11           C  
ANISOU 1951  CA  ALA A 270    10503   7464   9812  -1365   1076   2392       C  
ATOM   1952  C   ALA A 270      46.753  90.749   2.818  1.00 67.15           C  
ANISOU 1952  C   ALA A 270     9587   6674   9253  -1494   1032   2334       C  
ATOM   1953  O   ALA A 270      47.955  90.878   2.611  1.00 72.53           O  
ANISOU 1953  O   ALA A 270    10142   7375  10043  -1639   1121   2457       O  
ATOM   1954  CB  ALA A 270      45.034  92.268   1.772  1.00 64.43           C  
ANISOU 1954  CB  ALA A 270     9595   6141   8743  -1368    948   2445       C  
ATOM   1955  N   ASP A 271      46.250  90.462   4.013  1.00 62.54           N  
ANISOU 1955  N   ASP A 271     9005   6045   8712  -1438    893   2150       N  
ATOM   1956  CA  ASP A 271      47.086  90.340   5.204  1.00 68.14           C  
ANISOU 1956  CA  ASP A 271     9586   6709   9595  -1547    818   2077       C  
ATOM   1957  C   ASP A 271      48.053  89.174   4.998  1.00 75.36           C  
ANISOU 1957  C   ASP A 271    10290   7822  10520  -1576    954   2082       C  
ATOM   1958  O   ASP A 271      49.258  89.298   5.288  1.00 84.02           O  
ANISOU 1958  O   ASP A 271    11242   8908  11775  -1726    975   2152       O  
ATOM   1959  CB  ASP A 271      46.188  90.175   6.441  1.00 78.90           C  
ANISOU 1959  CB  ASP A 271    11016   8005  10956  -1446    657   1875       C  
ATOM   1960  CG  ASP A 271      46.951  89.886   7.738  1.00 98.93           C  
ANISOU 1960  CG  ASP A 271    13432  10516  13641  -1533    568   1774       C  
ATOM   1961  OD1 ASP A 271      48.010  89.234   7.740  1.00106.06           O  
ANISOU 1961  OD1 ASP A 271    14154  11528  14615  -1616    644   1805       O  
ATOM   1962  OD2 ASP A 271      46.464  90.358   8.787  1.00104.88           O1-
ANISOU 1962  OD2 ASP A 271    14280  11130  14438  -1511    414   1663       O1-
ATOM   1963  N   LEU A 272      47.531  88.068   4.466  1.00 68.47           N  
ANISOU 1963  N   LEU A 272     9403   7129   9485  -1432   1043   2014       N  
ATOM   1964  CA  LEU A 272      48.322  86.862   4.271  1.00 60.40           C  
ANISOU 1964  CA  LEU A 272     8200   6296   8454  -1425   1170   1996       C  
ATOM   1965  C   LEU A 272      49.482  87.057   3.293  1.00 59.90           C  
ANISOU 1965  C   LEU A 272     8032   6299   8427  -1533   1343   2191       C  
ATOM   1966  O   LEU A 272      50.533  86.488   3.505  1.00 62.59           O  
ANISOU 1966  O   LEU A 272     8188   6730   8865  -1598   1414   2206       O  
ATOM   1967  CB  LEU A 272      47.429  85.713   3.800  1.00 59.83           C  
ANISOU 1967  CB  LEU A 272     8166   6378   8190  -1245   1220   1887       C  
ATOM   1968  CG  LEU A 272      46.492  85.115   4.847  1.00 59.91           C  
ANISOU 1968  CG  LEU A 272     8206   6377   8179  -1140   1083   1689       C  
ATOM   1969  CD1 LEU A 272      45.548  84.087   4.253  1.00 52.36           C  
ANISOU 1969  CD1 LEU A 272     7298   5557   7038   -976   1124   1603       C  
ATOM   1970  CD2 LEU A 272      47.304  84.513   5.986  1.00 56.60           C  
ANISOU 1970  CD2 LEU A 272     7625   5979   7900  -1201   1041   1602       C  
ATOM   1971  N   LYS A 273      49.310  87.829   2.223  1.00 54.17           N  
ANISOU 1971  N   LYS A 273     7419   5540   7623  -1547   1417   2345       N  
ATOM   1972  CA  LYS A 273      50.454  88.080   1.340  1.00 72.31           C  
ANISOU 1972  CA  LYS A 273     9612   7900   9963  -1658   1591   2547       C  
ATOM   1973  C   LYS A 273      51.504  88.928   2.056  1.00 83.95           C  
ANISOU 1973  C   LYS A 273    10974   9238  11687  -1864   1529   2640       C  
ATOM   1974  O   LYS A 273      52.704  88.797   1.799  1.00 84.77           O  
ANISOU 1974  O   LYS A 273    10896   9419  11893  -1972   1653   2761       O  
ATOM   1975  CB  LYS A 273      50.032  88.755   0.033  1.00 79.12           C  
ANISOU 1975  CB  LYS A 273    10632   8752  10679  -1630   1684   2707       C  
ATOM   1976  CG  LYS A 273      48.901  88.056  -0.695  1.00 80.87           C  
ANISOU 1976  CG  LYS A 273    10990   9086  10653  -1433   1712   2619       C  
ATOM   1977  CD  LYS A 273      48.543  88.790  -1.972  1.00 87.67           C  
ANISOU 1977  CD  LYS A 273    12010   9930  11368  -1412   1792   2788       C  
ATOM   1978  CE  LYS A 273      49.596  88.555  -3.042  1.00 99.52           C  
ANISOU 1978  CE  LYS A 273    13415  11578  12818  -1457   2026   2961       C  
ATOM   1979  NZ  LYS A 273      50.346  87.284  -2.806  1.00105.11           N1+
ANISOU 1979  NZ  LYS A 273    13927  12460  13548  -1427   2128   2868       N1+
ATOM   1980  N   ALA A 274      51.056  89.766   2.988  1.00 89.15           N  
ANISOU 1980  N   ALA A 274    11733   9694  12444  -1914   1332   2576       N  
ATOM   1981  CA  ALA A 274      51.970  90.618   3.738  1.00 94.14           C  
ANISOU 1981  CA  ALA A 274    12284  10171  13314  -2113   1235   2646       C  
ATOM   1982  C   ALA A 274      52.928  89.789   4.600  1.00 93.83           C  
ANISOU 1982  C   ALA A 274    12018  10221  13412  -2171   1223   2568       C  
ATOM   1983  O   ALA A 274      53.859  90.344   5.194  1.00 98.03           O  
ANISOU 1983  O   ALA A 274    12441  10654  14153  -2346   1150   2631       O  
ATOM   1984  CB  ALA A 274      51.190  91.617   4.602  1.00 93.59           C  
ANISOU 1984  CB  ALA A 274    12399   9863  13299  -2126   1015   2563       C  
ATOM   1985  N   LYS A 275      52.705  88.471   4.667  1.00 84.53           N  
ANISOU 1985  N   LYS A 275    10770   9223  12125  -2027   1283   2434       N  
ATOM   1986  CA  LYS A 275      53.664  87.572   5.310  1.00 55.89           C  
ANISOU 1986  CA  LYS A 275     6916   5706   8613  -2065   1299   2379       C  
ATOM   1987  C   LYS A 275      54.329  86.581   4.287  1.00 79.27           C  
ANISOU 1987  C   LYS A 275     9723   8898  11498  -2007   1539   2459       C  
ATOM   1988  O   LYS A 275      55.431  86.911   3.859  1.00 88.68           O  
ANISOU 1988  O   LYS A 275    10765  10119  12809  -2137   1648   2631       O  
ATOM   1989  CB  LYS A 275      52.991  86.933   6.503  1.00 54.98           C  
ANISOU 1989  CB  LYS A 275     6839   5574   8476  -1966   1140   2152       C  
ATOM   1990  CG  LYS A 275      52.205  87.974   7.279  1.00 64.51           C  
ANISOU 1990  CG  LYS A 275     8235   6561   9713  -1991    939   2085       C  
ATOM   1991  CD  LYS A 275      51.141  87.373   8.176  1.00 66.20           C  
ANISOU 1991  CD  LYS A 275     8546   6775   9832  -1841    817   1870       C  
ATOM   1992  CE  LYS A 275      50.577  88.435   9.125  1.00 63.14           C  
ANISOU 1992  CE  LYS A 275     8321   6165   9503  -1875    616   1801       C  
ATOM   1993  NZ  LYS A 275      49.491  87.888  10.004  1.00 61.71           N1+
ANISOU 1993  NZ  LYS A 275     8235   5990   9222  -1721    511   1601       N1+
ATOM   1994  N   GLY A 276      53.795  85.426   3.856  1.00 75.87           N  
ANISOU 1994  N   GLY A 276     9312   8629  10887  -1829   1631   2355       N  
ATOM   1995  CA  GLY A 276      52.651  84.686   4.365  1.00 80.75           C  
ANISOU 1995  CA  GLY A 276    10043   9262  11375  -1669   1529   2149       C  
ATOM   1996  C   GLY A 276      51.926  83.911   3.278  1.00 76.97           C  
ANISOU 1996  C   GLY A 276     9658   8926  10663  -1499   1659   2121       C  
ATOM   1997  O   GLY A 276      51.271  82.896   3.537  1.00 63.31           O  
ANISOU 1997  O   GLY A 276     7952   7270   8832  -1363   1628   1962       O  
ATOM   1998  N   LEU A 277      52.073  84.388   2.048  1.00 78.71           N  
ANISOU 1998  N   LEU A 277     9930   9180  10796  -1511   1804   2283       N  
ATOM   1999  CA  LEU A 277      51.246  83.935   0.943  1.00 78.47           C  
ANISOU 1999  CA  LEU A 277    10041   9249  10526  -1358   1898   2269       C  
ATOM   2000  C   LEU A 277      51.921  84.199  -0.400  1.00 84.14           C  
ANISOU 2000  C   LEU A 277    10742  10059  11170  -1384   2111   2467       C  
ATOM   2001  O   LEU A 277      52.559  85.240  -0.601  1.00 91.48           O  
ANISOU 2001  O   LEU A 277    11641  10907  12209  -1529   2146   2644       O  
ATOM   2002  CB  LEU A 277      49.897  84.634   1.002  1.00 74.99           C  
ANISOU 2002  CB  LEU A 277     9820   8676   9995  -1305   1752   2221       C  
ATOM   2003  CG  LEU A 277      48.774  84.228   0.067  1.00 80.67           C  
ANISOU 2003  CG  LEU A 277    10709   9469  10475  -1143   1781   2178       C  
ATOM   2004  CD1 LEU A 277      48.971  84.696  -1.366  1.00 93.58           C  
ANISOU 2004  CD1 LEU A 277    12422  11155  11978  -1143   1939   2360       C  
ATOM   2005  CD2 LEU A 277      48.710  82.785   0.113  1.00 78.79           C  
ANISOU 2005  CD2 LEU A 277    10399   9382  10157  -1025   1824   2035       C  
ATOM   2006  N   ALA A 278      51.749  83.261  -1.325  1.00 79.58           N  
ANISOU 2006  N   ALA A 278    10193   9644  10399  -1242   2250   2438       N  
ATOM   2007  CA  ALA A 278      52.398  83.343  -2.624  1.00 74.34           C  
ANISOU 2007  CA  ALA A 278     9517   9096   9633  -1239   2474   2613       C  
ATOM   2008  C   ALA A 278      51.391  83.534  -3.735  1.00 85.06           C  
ANISOU 2008  C   ALA A 278    11106  10472  10741  -1127   2502   2640       C  
ATOM   2009  O   ALA A 278      50.286  82.994  -3.701  1.00 89.78           O  
ANISOU 2009  O   ALA A 278    11835  11075  11203   -997   2398   2485       O  
ATOM   2010  CB  ALA A 278      53.219  82.100  -2.886  1.00 58.10           C  
ANISOU 2010  CB  ALA A 278     7299   7227   7549  -1161   2640   2573       C  
ATOM   2011  N   VAL A 279      51.790  84.309  -4.731  1.00 92.19           N  
ANISOU 2011  N   VAL A 279    12055  11385  11588  -1181   2640   2848       N  
ATOM   2012  CA  VAL A 279      51.052  84.385  -5.977  1.00 93.42           C  
ANISOU 2012  CA  VAL A 279    12418  11596  11483  -1067   2707   2900       C  
ATOM   2013  C   VAL A 279      51.536  83.270  -6.901  1.00106.29           C  
ANISOU 2013  C   VAL A 279    14008  13438  12939   -942   2917   2889       C  
ATOM   2014  O   VAL A 279      51.251  83.273  -8.094  1.00113.16           O  
ANISOU 2014  O   VAL A 279    15026  14389  13582   -853   3027   2963       O  
ATOM   2015  CB  VAL A 279      51.225  85.754  -6.664  1.00 84.69           C  
ANISOU 2015  CB  VAL A 279    11401  10400  10379  -1176   2761   3140       C  
ATOM   2016  N   GLU A 280      52.267  82.312  -6.339  1.00114.44           N  
ANISOU 2016  N   GLU A 280    14849  14559  14072   -927   2969   2793       N  
ATOM   2017  CA  GLU A 280      52.826  81.210  -7.122  1.00127.94           C  
ANISOU 2017  CA  GLU A 280    16506  16465  15638   -801   3173   2772       C  
ATOM   2018  C   GLU A 280      51.736  80.308  -7.711  1.00127.96           C  
ANISOU 2018  C   GLU A 280    16706  16535  15379   -609   3128   2606       C  
ATOM   2019  O   GLU A 280      50.544  80.592  -7.580  1.00121.08           O  
ANISOU 2019  O   GLU A 280    16001  15567  14438   -578   2947   2528       O  
ATOM   2020  CB  GLU A 280      53.795  80.379  -6.271  1.00133.05           C  
ANISOU 2020  CB  GLU A 280    16903  17174  16474   -823   3210   2694       C  
ATOM   2021  N   SER A 281      52.168  79.215  -8.340  1.00130.42           N  
ANISOU 2021  N   SER A 281    16989  17009  15554   -478   3290   2552       N  
ATOM   2022  CA  SER A 281      51.326  78.415  -9.230  1.00125.49           C  
ANISOU 2022  CA  SER A 281    16567  16467  14646   -297   3293   2436       C  
ATOM   2023  C   SER A 281      50.829  79.297 -10.379  1.00120.79           C  
ANISOU 2023  C   SER A 281    16182  15865  13846   -284   3337   2586       C  
ATOM   2024  O   SER A 281      51.525  80.230 -10.787  1.00121.94           O  
ANISOU 2024  O   SER A 281    16287  16010  14035   -385   3471   2802       O  
ATOM   2025  CB  SER A 281      50.162  77.765  -8.472  1.00122.36           C  
ANISOU 2025  CB  SER A 281    16245  15997  14250   -233   3052   2206       C  
ATOM   2026  OG  SER A 281      50.632  76.790  -7.554  1.00120.39           O  
ANISOU 2026  OG  SER A 281    15822  15773  14149   -219   3032   2067       O  
ATOM   2027  N   GLU A 282      49.642  79.009 -10.907  1.00114.97           N  
ANISOU 2027  N   GLU A 282    15665  15124  12893   -165   3222   2481       N  
ATOM   2028  CA  GLU A 282      49.157  79.714 -12.096  1.00111.73           C  
ANISOU 2028  CA  GLU A 282    15471  14726  12256   -128   3264   2616       C  
ATOM   2029  C   GLU A 282      48.393  80.989 -11.742  1.00 97.63           C  
ANISOU 2029  C   GLU A 282    13768  12769  10556   -234   3087   2700       C  
ATOM   2030  O   GLU A 282      47.170  81.047 -11.857  1.00 99.64           O  
ANISOU 2030  O   GLU A 282    14192  12965  10701   -168   2909   2616       O  
ATOM   2031  CB  GLU A 282      48.271  78.794 -12.941  1.00114.47           C  
ANISOU 2031  CB  GLU A 282    16026  15156  12313     56   3221   2471       C  
ATOM   2032  N   GLY A 283      49.117  82.026 -11.347  1.00 85.17           N  
ANISOU 2032  N   GLY A 283    12074  11109   9177   -396   3135   2872       N  
ATOM   2033  CA  GLY A 283      48.460  83.187 -10.796  1.00 84.01           C  
ANISOU 2033  CA  GLY A 283    11988  10779   9155   -498   2952   2927       C  
ATOM   2034  C   GLY A 283      47.893  82.734  -9.465  1.00105.32           C  
ANISOU 2034  C   GLY A 283    14607  13390  12020   -502   2742   2717       C  
ATOM   2035  O   GLY A 283      48.553  81.988  -8.732  1.00112.30           O  
ANISOU 2035  O   GLY A 283    15310  14319  13041   -521   2774   2621       O  
ATOM   2036  N   ALA A 284      46.671  83.165  -9.158  1.00107.30           N  
ANISOU 2036  N   ALA A 284    14991  13522  12256   -478   2533   2649       N  
ATOM   2037  CA  ALA A 284      45.999  82.788  -7.913  1.00 97.90           C  
ANISOU 2037  CA  ALA A 284    13743  12250  11205   -471   2333   2456       C  
ATOM   2038  C   ALA A 284      46.843  83.110  -6.679  1.00100.17           C  
ANISOU 2038  C   ALA A 284    13833  12452  11776   -616   2315   2462       C  
ATOM   2039  O   ALA A 284      47.882  83.758  -6.765  1.00108.83           O  
ANISOU 2039  O   ALA A 284    14837  13533  12982   -737   2434   2625       O  
ATOM   2040  CB  ALA A 284      45.634  81.312  -7.936  1.00 90.28           C  
ANISOU 2040  CB  ALA A 284    12770  11405  10128   -335   2317   2256       C  
ATOM   2041  N   THR A 285      46.383  82.664  -5.522  1.00101.33           N  
ANISOU 2041  N   THR A 285    13915  12545  12042   -606   2159   2289       N  
ATOM   2042  CA  THR A 285      47.065  82.962  -4.270  1.00 96.40           C  
ANISOU 2042  CA  THR A 285    13125  11830  11674   -734   2108   2275       C  
ATOM   2043  C   THR A 285      47.058  81.741  -3.359  1.00 77.08           C  
ANISOU 2043  C   THR A 285    10556   9439   9290   -682   2051   2077       C  
ATOM   2044  O   THR A 285      46.016  81.362  -2.821  1.00 72.78           O  
ANISOU 2044  O   THR A 285    10073   8860   8721   -607   1899   1928       O  
ATOM   2045  CB  THR A 285      46.407  84.153  -3.540  1.00104.73           C  
ANISOU 2045  CB  THR A 285    14257  12690  12846   -806   1930   2294       C  
ATOM   2046  CG2 THR A 285      46.735  85.467  -4.238  1.00108.95           C  
ANISOU 2046  CG2 THR A 285    14871  13140  13385   -901   1991   2514       C  
ATOM   2047  OG1 THR A 285      44.987  83.975  -3.510  1.00103.64           O  
ANISOU 2047  OG1 THR A 285    14261  12524  12593   -684   1783   2174       O  
ATOM   2048  N   VAL A 286      48.219  81.123  -3.182  1.00 74.77           N  
ANISOU 2048  N   VAL A 286    10088   9236   9086   -719   2175   2084       N  
ATOM   2049  CA  VAL A 286      48.281  79.897  -2.389  1.00 78.41           C  
ANISOU 2049  CA  VAL A 286    10437   9756   9599   -661   2132   1907       C  
ATOM   2050  C   VAL A 286      49.196  80.005  -1.170  1.00 74.60           C  
ANISOU 2050  C   VAL A 286     9760   9220   9363   -783   2095   1900       C  
ATOM   2051  O   VAL A 286      50.319  80.501  -1.250  1.00 79.02           O  
ANISOU 2051  O   VAL A 286    10198   9785  10040   -894   2200   2039       O  
ATOM   2052  CB  VAL A 286      48.748  78.682  -3.251  1.00 72.20           C  
ANISOU 2052  CB  VAL A 286     9618   9145   8669   -548   2300   1872       C  
ATOM   2053  CG1 VAL A 286      47.643  78.217  -4.183  1.00 65.34           C  
ANISOU 2053  CG1 VAL A 286     8946   8327   7553   -404   2276   1803       C  
ATOM   2054  CG2 VAL A 286      49.984  79.035  -4.048  1.00 85.18           C  
ANISOU 2054  CG2 VAL A 286    11178  10869  10319   -604   2518   2055       C  
ATOM   2055  N   VAL A 287      48.688  79.583  -0.022  1.00 74.57           N  
ANISOU 2055  N   VAL A 287     9730   9162   9442   -766   1937   1745       N  
ATOM   2056  CA  VAL A 287      49.559  79.289   1.100  1.00 76.24           C  
ANISOU 2056  CA  VAL A 287     9755   9360   9852   -845   1905   1704       C  
ATOM   2057  C   VAL A 287      50.116  77.892   0.907  1.00 70.81           C  
ANISOU 2057  C   VAL A 287     8955   8822   9126   -755   2015   1629       C  
ATOM   2058  O   VAL A 287      49.359  76.965   0.639  1.00 79.44           O  
ANISOU 2058  O   VAL A 287    10130   9975  10080   -625   1998   1507       O  
ATOM   2059  CB  VAL A 287      48.834  79.350   2.442  1.00 67.55           C  
ANISOU 2059  CB  VAL A 287     8675   8148   8843   -854   1700   1569       C  
ATOM   2060  CG1 VAL A 287      49.839  79.337   3.557  1.00 61.75           C  
ANISOU 2060  CG1 VAL A 287     7763   7381   8318   -961   1659   1561       C  
ATOM   2061  CG2 VAL A 287      47.999  80.596   2.527  1.00 72.94           C  
ANISOU 2061  CG2 VAL A 287     9509   8685   9518   -893   1587   1613       C  
ATOM   2062  N   PHE A 288      51.430  77.741   1.028  1.00 64.50           N  
ANISOU 2062  N   PHE A 288     7968   8080   8457   -822   2125   1702       N  
ATOM   2063  CA  PHE A 288      52.055  76.422   0.928  1.00 61.78           C  
ANISOU 2063  CA  PHE A 288     7502   7871   8099   -731   2230   1632       C  
ATOM   2064  C   PHE A 288      52.368  75.893   2.321  1.00 71.64           C  
ANISOU 2064  C   PHE A 288     8612   9086   9523   -765   2106   1525       C  
ATOM   2065  O   PHE A 288      53.074  76.548   3.089  1.00 79.97           O  
ANISOU 2065  O   PHE A 288     9545  10073  10766   -898   2052   1589       O  
ATOM   2066  CB  PHE A 288      53.338  76.467   0.078  1.00 58.76           C  
ANISOU 2066  CB  PHE A 288     6989   7601   7738   -758   2454   1787       C  
ATOM   2067  CG  PHE A 288      53.097  76.552  -1.418  1.00 57.72           C  
ANISOU 2067  CG  PHE A 288     6995   7551   7384   -674   2614   1868       C  
ATOM   2068  CD1 PHE A 288      52.588  75.474  -2.120  1.00 58.66           C  
ANISOU 2068  CD1 PHE A 288     7219   7767   7302   -505   2670   1756       C  
ATOM   2069  CD2 PHE A 288      53.417  77.699  -2.124  1.00 68.38           C  
ANISOU 2069  CD2 PHE A 288     8376   8879   8727   -766   2706   2060       C  
ATOM   2070  CE1 PHE A 288      52.389  75.540  -3.487  1.00 60.66           C  
ANISOU 2070  CE1 PHE A 288     7612   8098   7338   -423   2810   1826       C  
ATOM   2071  CE2 PHE A 288      53.214  77.771  -3.500  1.00 66.68           C  
ANISOU 2071  CE2 PHE A 288     8297   8746   8294   -684   2856   2141       C  
ATOM   2072  CZ  PHE A 288      52.700  76.689  -4.174  1.00 61.48           C  
ANISOU 2072  CZ  PHE A 288     7748   8188   7423   -509   2906   2020       C  
ATOM   2073  N   LEU A 289      51.846  74.710   2.643  1.00 67.24           N  
ANISOU 2073  N   LEU A 289     8076   8568   8903   -647   2053   1364       N  
ATOM   2074  CA  LEU A 289      52.020  74.137   3.972  1.00 66.37           C  
ANISOU 2074  CA  LEU A 289     7856   8425   8936   -664   1928   1258       C  
ATOM   2075  C   LEU A 289      52.883  72.869   3.939  1.00 79.04           C  
ANISOU 2075  C   LEU A 289     9312  10147  10572   -585   2031   1213       C  
ATOM   2076  O   LEU A 289      52.449  71.840   3.417  1.00 79.65           O  
ANISOU 2076  O   LEU A 289     9459  10292  10512   -449   2077   1120       O  
ATOM   2077  CB  LEU A 289      50.660  73.801   4.593  1.00 64.55           C  
ANISOU 2077  CB  LEU A 289     7764   8129   8634   -600   1760   1110       C  
ATOM   2078  CG  LEU A 289      49.475  74.758   4.490  1.00 56.35           C  
ANISOU 2078  CG  LEU A 289     6905   6991   7514   -616   1659   1116       C  
ATOM   2079  CD1 LEU A 289      48.198  74.111   5.070  1.00 39.61           C  
ANISOU 2079  CD1 LEU A 289     4883   4842   5326   -529   1520    964       C  
ATOM   2080  CD2 LEU A 289      49.798  76.063   5.175  1.00 56.25           C  
ANISOU 2080  CD2 LEU A 289     6867   6861   7646   -759   1579   1200       C  
ATOM   2081  N   ASP A 290      54.081  72.942   4.527  1.00 88.19           N  
ANISOU 2081  N   ASP A 290    10270  11321  11917   -668   2054   1276       N  
ATOM   2082  CA  ASP A 290      55.024  71.821   4.585  1.00 85.54           C  
ANISOU 2082  CA  ASP A 290     9767  11092  11643   -597   2148   1249       C  
ATOM   2083  C   ASP A 290      54.469  70.667   5.414  1.00 80.87           C  
ANISOU 2083  C   ASP A 290     9199  10486  11042   -504   2026   1077       C  
ATOM   2084  O   ASP A 290      54.964  69.529   5.343  1.00 86.43           O  
ANISOU 2084  O   ASP A 290     9816  11271  11750   -403   2096   1022       O  
ATOM   2085  CB  ASP A 290      56.360  72.260   5.192  1.00 96.75           C  
ANISOU 2085  CB  ASP A 290    10955  12516  13290   -724   2160   1358       C  
ATOM   2086  CG  ASP A 290      56.798  73.639   4.734  1.00106.50           C  
ANISOU 2086  CG  ASP A 290    12168  13714  14584   -867   2216   1533       C  
ATOM   2087  OD1 ASP A 290      56.201  74.644   5.195  1.00109.86           O  
ANISOU 2087  OD1 ASP A 290    12697  14011  15033   -969   2075   1544       O  
ATOM   2088  OD2 ASP A 290      57.759  73.717   3.935  1.00107.38           O1-
ANISOU 2088  OD2 ASP A 290    12154  13922  14723   -877   2404   1665       O1-
ATOM   2089  N   GLU A 291      53.456  70.972   6.223  1.00 66.24           N  
ANISOU 2089  N   GLU A 291     7460   8528   9180   -537   1845    998       N  
ATOM   2090  CA  GLU A 291      52.823  69.961   7.056  1.00 60.94           C  
ANISOU 2090  CA  GLU A 291     6821   7836   8498   -461   1723    848       C  
ATOM   2091  C   GLU A 291      52.067  68.979   6.175  1.00 68.64           C  
ANISOU 2091  C   GLU A 291     7922   8866   9291   -314   1784    760       C  
ATOM   2092  O   GLU A 291      51.831  67.839   6.544  1.00 70.57           O  
ANISOU 2092  O   GLU A 291     8166   9126   9523   -227   1741    651       O  
ATOM   2093  CB  GLU A 291      51.878  70.603   8.078  1.00 55.43           C  
ANISOU 2093  CB  GLU A 291     6219   7020   7823   -526   1532    797       C  
ATOM   2094  N   PHE A 292      51.711  69.435   4.987  1.00 73.29           N  
ANISOU 2094  N   PHE A 292     8627   9482   9738   -289   1879    814       N  
ATOM   2095  CA  PHE A 292      50.867  68.660   4.111  1.00 71.34           C  
ANISOU 2095  CA  PHE A 292     8531   9274   9303   -160   1910    730       C  
ATOM   2096  C   PHE A 292      51.564  68.367   2.787  1.00 72.21           C  
ANISOU 2096  C   PHE A 292     8635   9492   9308    -82   2115    788       C  
ATOM   2097  O   PHE A 292      50.968  68.530   1.724  1.00 71.07           O  
ANISOU 2097  O   PHE A 292     8644   9370   8988    -28   2168    797       O  
ATOM   2098  CB  PHE A 292      49.554  69.406   3.887  1.00 67.29           C  
ANISOU 2098  CB  PHE A 292     8197   8690   8679   -179   1811    722       C  
ATOM   2099  CG  PHE A 292      48.844  69.760   5.164  1.00 62.02           C  
ANISOU 2099  CG  PHE A 292     7540   7922   8103   -243   1627    670       C  
ATOM   2100  CD1 PHE A 292      47.914  68.899   5.714  1.00 60.09           C  
ANISOU 2100  CD1 PHE A 292     7351   7653   7827   -180   1512    544       C  
ATOM   2101  CD2 PHE A 292      49.119  70.945   5.825  1.00 66.94           C  
ANISOU 2101  CD2 PHE A 292     8119   8470   8843   -366   1570    750       C  
ATOM   2102  CE1 PHE A 292      47.268  69.218   6.896  1.00 62.47           C  
ANISOU 2102  CE1 PHE A 292     7661   7872   8202   -229   1359    502       C  
ATOM   2103  CE2 PHE A 292      48.473  71.268   7.015  1.00 63.19           C  
ANISOU 2103  CE2 PHE A 292     7667   7904   8438   -410   1407    694       C  
ATOM   2104  CZ  PHE A 292      47.550  70.408   7.548  1.00 58.18           C  
ANISOU 2104  CZ  PHE A 292     7084   7260   7762   -338   1309    573       C  
ATOM   2105  N   LYS A 293      52.820  67.925   2.868  1.00 72.09           N  
ANISOU 2105  N   LYS A 293     8445   9546   9398    -69   2229    826       N  
ATOM   2106  CA  LYS A 293      53.615  67.588   1.688  1.00 77.95           C  
ANISOU 2106  CA  LYS A 293     9160  10405  10054     19   2446    884       C  
ATOM   2107  C   LYS A 293      53.005  66.426   0.883  1.00 83.26           C  
ANISOU 2107  C   LYS A 293     9984  11119  10531    187   2482    756       C  
ATOM   2108  O   LYS A 293      52.400  65.514   1.457  1.00 77.85           O  
ANISOU 2108  O   LYS A 293     9342  10388   9848    242   2357    618       O  
ATOM   2109  CB  LYS A 293      55.052  67.244   2.109  1.00 75.29           C  
ANISOU 2109  CB  LYS A 293     8580  10132   9894      9   2543    940       C  
ATOM   2110  N   ASN A 294      53.154  66.487  -0.445  1.00 89.85           N  
ANISOU 2110  N   ASN A 294    10909  12035  11196    264   2648    805       N  
ATOM   2111  CA  ASN A 294      52.870  65.362  -1.351  1.00 87.05           C  
ANISOU 2111  CA  ASN A 294    10688  11735  10652    436   2716    692       C  
ATOM   2112  C   ASN A 294      53.796  64.191  -1.027  1.00101.91           C  
ANISOU 2112  C   ASN A 294    12428  13666  12626    534   2790    628       C  
ATOM   2113  O   ASN A 294      54.750  64.347  -0.263  1.00110.03           O  
ANISOU 2113  O   ASN A 294    13243  14708  13854    468   2815    695       O  
ATOM   2114  CB  ASN A 294      53.044  65.776  -2.830  1.00 63.37           C  
ANISOU 2114  CB  ASN A 294     7800   8826   7452    498   2903    780       C  
ATOM   2115  N   LYS A 295      53.531  63.020  -1.603  1.00 99.75           N  
ANISOU 2115  N   LYS A 295    12271  13415  12213    692   2818    498       N  
ATOM   2116  CA  LYS A 295      54.427  61.881  -1.410  1.00 88.54           C  
ANISOU 2116  CA  LYS A 295    10733  12040  10869    808   2902    435       C  
ATOM   2117  C   LYS A 295      55.769  62.184  -2.053  1.00 80.73           C  
ANISOU 2117  C   LYS A 295     9595  11176   9901    845   3152    569       C  
ATOM   2118  O   LYS A 295      56.804  61.629  -1.665  1.00 80.89           O  
ANISOU 2118  O   LYS A 295     9429  11243  10061    894   3235    580       O  
ATOM   2119  CB  LYS A 295      53.833  60.604  -1.999  1.00 93.49           C  
ANISOU 2119  CB  LYS A 295    11544  12652  11327    975   2879    266       C  
ATOM   2120  N   GLU A 296      55.747  63.078  -3.037  1.00 71.85           N  
ANISOU 2120  N   GLU A 296     8549  10109   8641    821   3274    681       N  
ATOM   2121  CA  GLU A 296      56.972  63.494  -3.691  1.00 72.55           C  
ANISOU 2121  CA  GLU A 296     8497  10324   8746    840   3524    834       C  
ATOM   2122  C   GLU A 296      57.626  64.563  -2.821  1.00 78.93           C  
ANISOU 2122  C   GLU A 296     9078  11113   9798    647   3496    991       C  
ATOM   2123  O   GLU A 296      58.820  64.870  -2.956  1.00 79.22           O  
ANISOU 2123  O   GLU A 296     8913  11242   9947    627   3669   1130       O  
ATOM   2124  CB  GLU A 296      56.686  64.000  -5.105  1.00 75.48           C  
ANISOU 2124  CB  GLU A 296     9052  10762   8863    893   3669    899       C  
ATOM   2125  CG  GLU A 296      57.871  64.638  -5.798  1.00 89.68           C  
ANISOU 2125  CG  GLU A 296    10707  12691  10675    887   3934   1092       C  
ATOM   2126  CD  GLU A 296      57.524  65.227  -7.158  1.00100.75           C  
ANISOU 2126  CD  GLU A 296    12308  14156  11816    928   4067   1170       C  
ATOM   2127  OE1 GLU A 296      56.344  65.109  -7.566  1.00105.53           O  
ANISOU 2127  OE1 GLU A 296    13167  14701  12229    966   3939   1064       O  
ATOM   2128  OE2 GLU A 296      58.436  65.799  -7.815  1.00 95.66           O1-
ANISOU 2128  OE2 GLU A 296    11571  13600  11176    893   4204   1309       O1-
ATOM   2129  N   GLY A 297      56.837  65.102  -1.894  1.00 81.41           N  
ANISOU 2129  N   GLY A 297     9424  11306  10201    509   3270    966       N  
ATOM   2130  CA  GLY A 297      57.342  66.083  -0.953  1.00 80.67           C  
ANISOU 2130  CA  GLY A 297     9145  11168  10336    324   3201   1088       C  
ATOM   2131  C   GLY A 297      57.051  67.487  -1.429  1.00 81.59           C  
ANISOU 2131  C   GLY A 297     9335  11263  10404    195   3218   1230       C  
ATOM   2132  O   GLY A 297      57.700  68.450  -1.015  1.00 71.20           O  
ANISOU 2132  O   GLY A 297     7865   9932   9256     45   3226   1373       O  
ATOM   2133  N   GLU A 298      56.079  67.599  -2.325  1.00 88.09           N  
ANISOU 2133  N   GLU A 298    10397  12077  10997    255   3218   1193       N  
ATOM   2134  CA  GLU A 298      55.666  68.904  -2.802  1.00 90.59           C  
ANISOU 2134  CA  GLU A 298    10810  12359  11249    146   3218   1321       C  
ATOM   2135  C   GLU A 298      54.671  69.428  -1.785  1.00 95.16           C  
ANISOU 2135  C   GLU A 298    11454  12792  11909     33   2963   1262       C  
ATOM   2136  O   GLU A 298      53.716  68.739  -1.428  1.00 98.16           O  
ANISOU 2136  O   GLU A 298    11950  13118  12229     96   2814   1104       O  
ATOM   2137  CB  GLU A 298      55.067  68.835  -4.214  1.00 82.58           C  
ANISOU 2137  CB  GLU A 298    10026  11403   9948    263   3322   1316       C  
ATOM   2138  N   PRO A 299      54.922  70.634  -1.272  1.00 95.43           N  
ANISOU 2138  N   PRO A 299    11406  12760  12091   -135   2913   1389       N  
ATOM   2139  CA  PRO A 299      54.008  71.254  -0.312  1.00 88.55           C  
ANISOU 2139  CA  PRO A 299    10603  11749  11294   -237   2683   1340       C  
ATOM   2140  C   PRO A 299      52.619  71.446  -0.909  1.00 78.64           C  
ANISOU 2140  C   PRO A 299     9598  10447   9833   -183   2600   1282       C  
ATOM   2141  O   PRO A 299      52.447  71.613  -2.115  1.00 78.25           O  
ANISOU 2141  O   PRO A 299     9673  10457   9602   -122   2718   1338       O  
ATOM   2142  CB  PRO A 299      54.667  72.602  -0.017  1.00 91.72           C  
ANISOU 2142  CB  PRO A 299    10894  12098  11856   -414   2691   1513       C  
ATOM   2143  CG  PRO A 299      56.107  72.408  -0.377  1.00 94.19           C  
ANISOU 2143  CG  PRO A 299    11000  12526  12260   -418   2893   1629       C  
ATOM   2144  CD  PRO A 299      56.102  71.470  -1.537  1.00 94.95           C  
ANISOU 2144  CD  PRO A 299    11180  12750  12148   -238   3067   1585       C  
ATOM   2145  N   MET A 300      51.622  71.407  -0.049  1.00 71.02           N  
ANISOU 2145  N   MET A 300     8704   9382   8898   -202   2396   1172       N  
ATOM   2146  CA  MET A 300      50.249  71.568  -0.472  1.00 70.30           C  
ANISOU 2146  CA  MET A 300     8826   9243   8641   -155   2294   1113       C  
ATOM   2147  C   MET A 300      49.998  73.031  -0.785  1.00 74.60           C  
ANISOU 2147  C   MET A 300     9445   9723   9176   -255   2282   1252       C  
ATOM   2148  O   MET A 300      50.246  73.899   0.054  1.00 77.33           O  
ANISOU 2148  O   MET A 300     9712   9982   9687   -382   2207   1312       O  
ATOM   2149  CB  MET A 300      49.304  71.062   0.624  1.00 72.25           C  
ANISOU 2149  CB  MET A 300     9099   9409   8942   -144   2090    963       C  
ATOM   2150  CG  MET A 300      47.832  71.233   0.340  1.00 72.80           C  
ANISOU 2150  CG  MET A 300     9361   9426   8873   -103   1963    902       C  
ATOM   2151  SD  MET A 300      47.219  70.362  -1.103  1.00139.43           S  
ANISOU 2151  SD  MET A 300    17976  17951  17052     51   2028    837       S  
ATOM   2152  CE  MET A 300      45.512  70.917  -1.080  1.00 78.22           C  
ANISOU 2152  CE  MET A 300    10398  10109   9212     50   1834    797       C  
ATOM   2153  N   GLY A 301      49.542  73.309  -2.003  1.00 73.25           N  
ANISOU 2153  N   GLY A 301     9433   9589   8809   -198   2353   1304       N  
ATOM   2154  CA  GLY A 301      49.162  74.658  -2.381  1.00 65.22           C  
ANISOU 2154  CA  GLY A 301     8517   8503   7763   -277   2331   1434       C  
ATOM   2155  C   GLY A 301      47.683  74.833  -2.098  1.00 72.61           C  
ANISOU 2155  C   GLY A 301     9607   9348   8633   -248   2135   1341       C  
ATOM   2156  O   GLY A 301      46.835  74.334  -2.836  1.00 81.75           O  
ANISOU 2156  O   GLY A 301    10911  10543   9607   -140   2111   1273       O  
ATOM   2157  N   VAL A 302      47.373  75.513  -1.001  1.00 72.21           N  
ANISOU 2157  N   VAL A 302     9520   9180   8736   -340   1990   1333       N  
ATOM   2158  CA  VAL A 302      45.989  75.724  -0.591  1.00 66.84           C  
ANISOU 2158  CA  VAL A 302     8961   8414   8020   -311   1808   1249       C  
ATOM   2159  C   VAL A 302      45.521  77.076  -1.083  1.00 62.85           C  
ANISOU 2159  C   VAL A 302     8580   7830   7470   -358   1782   1373       C  
ATOM   2160  O   VAL A 302      45.844  78.101  -0.479  1.00 64.08           O  
ANISOU 2160  O   VAL A 302     8694   7886   7767   -469   1745   1453       O  
ATOM   2161  CB  VAL A 302      45.826  75.655   0.947  1.00 58.45           C  
ANISOU 2161  CB  VAL A 302     7805   7268   7136   -364   1664   1156       C  
ATOM   2162  CG1 VAL A 302      44.383  75.832   1.328  1.00 50.57           C  
ANISOU 2162  CG1 VAL A 302     6924   6197   6094   -319   1497   1076       C  
ATOM   2163  CG2 VAL A 302      46.367  74.337   1.484  1.00 46.37           C  
ANISOU 2163  CG2 VAL A 302     6147   5808   5663   -323   1687   1047       C  
ATOM   2164  N   ILE A 303      44.773  77.073  -2.184  1.00 60.90           N  
ANISOU 2164  N   ILE A 303     8491   7620   7027   -273   1793   1389       N  
ATOM   2165  CA  ILE A 303      44.294  78.304  -2.815  1.00 65.44           C  
ANISOU 2165  CA  ILE A 303     9202   8128   7534   -299   1774   1517       C  
ATOM   2166  C   ILE A 303      43.317  79.035  -1.922  1.00 64.60           C  
ANISOU 2166  C   ILE A 303     9140   7886   7518   -325   1589   1479       C  
ATOM   2167  O   ILE A 303      42.349  78.432  -1.469  1.00 64.55           O  
ANISOU 2167  O   ILE A 303     9158   7876   7491   -254   1466   1346       O  
ATOM   2168  CB  ILE A 303      43.582  78.030  -4.165  1.00 66.86           C  
ANISOU 2168  CB  ILE A 303     9553   8383   7467   -185   1800   1525       C  
ATOM   2169  CG1 ILE A 303      44.424  77.114  -5.071  1.00 64.99           C  
ANISOU 2169  CG1 ILE A 303     9296   8291   7106   -123   1981   1528       C  
ATOM   2170  CG2 ILE A 303      43.226  79.344  -4.852  1.00 65.67           C  
ANISOU 2170  CG2 ILE A 303     9538   8164   7250   -215   1792   1680       C  
ATOM   2171  CD1 ILE A 303      43.822  76.908  -6.464  1.00 63.95           C  
ANISOU 2171  CD1 ILE A 303     9354   8234   6712    -12   2012   1544       C  
ATOM   2172  N   ILE A 304      43.552  80.318  -1.659  1.00 62.86           N  
ANISOU 2172  N   ILE A 304     8931   7552   7400   -424   1570   1596       N  
ATOM   2173  CA  ILE A 304      42.575  81.068  -0.873  1.00 64.48           C  
ANISOU 2173  CA  ILE A 304     9201   7624   7676   -429   1400   1559       C  
ATOM   2174  C   ILE A 304      41.805  82.041  -1.736  1.00 60.60           C  
ANISOU 2174  C   ILE A 304     8880   7074   7071   -397   1366   1663       C  
ATOM   2175  O   ILE A 304      40.705  82.455  -1.387  1.00 65.81           O  
ANISOU 2175  O   ILE A 304     9620   7654   7729   -348   1227   1619       O  
ATOM   2176  CB  ILE A 304      43.219  81.830   0.292  1.00 60.67           C  
ANISOU 2176  CB  ILE A 304     8626   7020   7405   -553   1355   1582       C  
ATOM   2177  CG1 ILE A 304      44.331  82.732  -0.212  1.00 57.02           C  
ANISOU 2177  CG1 ILE A 304     8140   6525   7002   -672   1469   1762       C  
ATOM   2178  CG2 ILE A 304      43.736  80.852   1.348  1.00 46.21           C  
ANISOU 2178  CG2 ILE A 304     6637   5233   5687   -568   1341   1457       C  
ATOM   2179  CD1 ILE A 304      45.007  83.463   0.899  1.00 60.60           C  
ANISOU 2179  CD1 ILE A 304     8505   6853   7668   -805   1410   1783       C  
ATOM   2180  N   GLN A 305      42.394  82.404  -2.864  1.00 65.50           N  
ANISOU 2180  N   GLN A 305     9552   7740   7597   -420   1499   1808       N  
ATOM   2181  CA  GLN A 305      41.716  83.211  -3.865  1.00 65.27           C  
ANISOU 2181  CA  GLN A 305     9695   7676   7429   -378   1481   1920       C  
ATOM   2182  C   GLN A 305      42.192  82.742  -5.227  1.00 74.80           C  
ANISOU 2182  C   GLN A 305    10952   9022   8447   -335   1642   1998       C  
ATOM   2183  O   GLN A 305      43.390  82.598  -5.470  1.00 78.32           O  
ANISOU 2183  O   GLN A 305    11304   9532   8923   -399   1803   2074       O  
ATOM   2184  CB  GLN A 305      41.987  84.705  -3.668  1.00 61.74           C  
ANISOU 2184  CB  GLN A 305     9288   7071   7098   -486   1461   2068       C  
ATOM   2185  CG  GLN A 305      41.412  85.584  -4.764  1.00 67.88           C  
ANISOU 2185  CG  GLN A 305    10246   7809   7734   -449   1456   2209       C  
ATOM   2186  CD  GLN A 305      41.592  87.056  -4.479  1.00 71.89           C  
ANISOU 2186  CD  GLN A 305    10804   8137   8373   -552   1414   2345       C  
ATOM   2187  NE2 GLN A 305      40.526  87.824  -4.671  1.00 69.04           N  
ANISOU 2187  NE2 GLN A 305    10594   7676   7963   -488   1292   2374       N  
ATOM   2188  OE1 GLN A 305      42.663  87.498  -4.061  1.00 76.27           O  
ANISOU 2188  OE1 GLN A 305    11262   8636   9081   -687   1479   2422       O  
ATOM   2189  N   LYS A 306      41.244  82.482  -6.111  1.00 70.54           N  
ANISOU 2189  N   LYS A 306    10557   8535   7709   -220   1595   1977       N  
ATOM   2190  CA  LYS A 306      41.569  81.943  -7.406  1.00 68.57           C  
ANISOU 2190  CA  LYS A 306    10381   8422   7248   -155   1732   2026       C  
ATOM   2191  C   LYS A 306      42.151  83.025  -8.301  1.00 77.52           C  
ANISOU 2191  C   LYS A 306    11596   9535   8323   -214   1854   2247       C  
ATOM   2192  O   LYS A 306      42.050  84.215  -7.990  1.00 80.36           O  
ANISOU 2192  O   LYS A 306    11985   9757   8792   -293   1797   2354       O  
ATOM   2193  CB  LYS A 306      40.312  81.336  -8.002  1.00 67.55           C  
ANISOU 2193  CB  LYS A 306    10389   8344   6931    -18   1613   1925       C  
ATOM   2194  CG  LYS A 306      39.565  80.542  -6.950  1.00 69.55           C  
ANISOU 2194  CG  LYS A 306    10561   8579   7285     18   1461   1732       C  
ATOM   2195  CD  LYS A 306      38.433  79.736  -7.520  1.00 81.29           C  
ANISOU 2195  CD  LYS A 306    12153  10131   8604    142   1347   1622       C  
ATOM   2196  CE  LYS A 306      37.222  80.585  -7.801  1.00 92.04           C  
ANISOU 2196  CE  LYS A 306    13643  11415   9912    185   1195   1673       C  
ATOM   2197  NZ  LYS A 306      36.155  79.722  -8.377  1.00 95.97           N1+
ANISOU 2197  NZ  LYS A 306    14228  11985  10252    298   1075   1565       N1+
ATOM   2198  N   LYS A 307      42.779  82.609  -9.397  1.00 81.07           N  
ANISOU 2198  N   LYS A 307    12086  10116   8601   -175   2027   2318       N  
ATOM   2199  CA  LYS A 307      43.125  83.534 -10.474  1.00 85.95           C  
ANISOU 2199  CA  LYS A 307    12819  10736   9102   -202   2144   2533       C  
ATOM   2200  C   LYS A 307      41.847  84.261 -10.922  1.00 83.58           C  
ANISOU 2200  C   LYS A 307    12715  10353   8690   -141   1982   2570       C  
ATOM   2201  O   LYS A 307      41.821  85.486 -11.007  1.00 76.17           O  
ANISOU 2201  O   LYS A 307    11838   9297   7805   -211   1962   2728       O  
ATOM   2202  CB  LYS A 307      43.792  82.790 -11.641  1.00 84.10           C  
ANISOU 2202  CB  LYS A 307    12624  10678   8651   -128   2347   2573       C  
ATOM   2203  CG  LYS A 307      43.342  83.214 -13.029  1.00 91.14           C  
ANISOU 2203  CG  LYS A 307    13737  11614   9276    -51   2383   2699       C  
ATOM   2204  CD  LYS A 307      43.606  82.117 -14.055  1.00 96.24           C  
ANISOU 2204  CD  LYS A 307    14455  12442   9670     76   2520   2643       C  
ATOM   2205  CE  LYS A 307      42.921  82.400 -15.387  1.00 97.02           C  
ANISOU 2205  CE  LYS A 307    14804  12586   9475    177   2505   2727       C  
ATOM   2206  NZ  LYS A 307      42.757  81.143 -16.167  1.00 94.09           N1+
ANISOU 2206  NZ  LYS A 307    14531  12364   8856    328   2543   2589       N1+
ATOM   2207  N   ASP A 308      40.779  83.493 -11.145  1.00 81.98           N  
ANISOU 2207  N   ASP A 308    12600  10201   8348    -14   1852   2422       N  
ATOM   2208  CA  ASP A 308      39.442  84.016 -11.431  1.00 84.34           C  
ANISOU 2208  CA  ASP A 308    13055  10428   8560     58   1666   2425       C  
ATOM   2209  C   ASP A 308      39.008  85.151 -10.490  1.00 85.60           C  
ANISOU 2209  C   ASP A 308    13190  10406   8930    -13   1534   2467       C  
ATOM   2210  O   ASP A 308      38.078  85.898 -10.796  1.00 89.57           O  
ANISOU 2210  O   ASP A 308    13824  10829   9379     33   1409   2525       O  
ATOM   2211  CB  ASP A 308      38.428  82.869 -11.357  1.00 91.40           C  
ANISOU 2211  CB  ASP A 308    13969  11390   9368    176   1523   2220       C  
ATOM   2212  CG  ASP A 308      37.060  83.254 -11.898  1.00 94.00           C  
ANISOU 2212  CG  ASP A 308    14463  11684   9570    269   1341   2229       C  
ATOM   2213  OD1 ASP A 308      36.982  84.159 -12.761  1.00 85.28           O  
ANISOU 2213  OD1 ASP A 308    13503  10551   8349    276   1363   2396       O  
ATOM   2214  OD2 ASP A 308      36.063  82.637 -11.462  1.00 97.60           O1-
ANISOU 2214  OD2 ASP A 308    14898  12139  10046    334   1175   2075       O1-
ATOM   2215  N   GLY A 309      39.679  85.268  -9.344  1.00 75.92           N  
ANISOU 2215  N   GLY A 309    11799   9111   7936   -118   1556   2432       N  
ATOM   2216  CA  GLY A 309      39.410  86.323  -8.386  1.00 57.34           C  
ANISOU 2216  CA  GLY A 309     9424   6578   5783   -189   1442   2461       C  
ATOM   2217  C   GLY A 309      38.502  85.875  -7.259  1.00 63.49           C  
ANISOU 2217  C   GLY A 309    10137   7315   6673   -138   1270   2270       C  
ATOM   2218  O   GLY A 309      38.580  86.395  -6.140  1.00 67.75           O  
ANISOU 2218  O   GLY A 309    10601   7732   7410   -205   1206   2240       O  
ATOM   2219  N   GLY A 310      37.626  84.919  -7.547  1.00 57.90           N  
ANISOU 2219  N   GLY A 310     9460   6704   5834    -20   1193   2142       N  
ATOM   2220  CA  GLY A 310      36.722  84.405  -6.529  1.00 61.31           C  
ANISOU 2220  CA  GLY A 310     9820   7113   6362     31   1041   1970       C  
ATOM   2221  C   GLY A 310      37.436  83.757  -5.354  1.00 55.86           C  
ANISOU 2221  C   GLY A 310     8951   6431   5842    -37   1080   1855       C  
ATOM   2222  O   GLY A 310      38.561  83.266  -5.491  1.00 59.12           O  
ANISOU 2222  O   GLY A 310     9284   6917   6260    -95   1225   1870       O  
ATOM   2223  N   TYR A 311      36.794  83.765  -4.192  1.00 48.61           N  
ANISOU 2223  N   TYR A 311     7968   5439   5061    -25    954   1746       N  
ATOM   2224  CA  TYR A 311      37.410  83.190  -2.988  1.00 49.47           C  
ANISOU 2224  CA  TYR A 311     7918   5549   5331    -86    973   1638       C  
ATOM   2225  C   TYR A 311      36.934  81.762  -2.783  1.00 55.28           C  
ANISOU 2225  C   TYR A 311     8587   6398   6020    -12    935   1476       C  
ATOM   2226  O   TYR A 311      36.202  81.221  -3.624  1.00 54.10           O  
ANISOU 2226  O   TYR A 311     8515   6326   5715     78    896   1449       O  
ATOM   2227  CB  TYR A 311      37.108  84.045  -1.762  1.00 56.39           C  
ANISOU 2227  CB  TYR A 311     8767   6275   6382   -122    871   1616       C  
ATOM   2228  CG  TYR A 311      37.686  85.445  -1.876  1.00 61.87           C  
ANISOU 2228  CG  TYR A 311     9525   6835   7147   -212    902   1771       C  
ATOM   2229  CD1 TYR A 311      39.005  85.698  -1.523  1.00 71.65           C  
ANISOU 2229  CD1 TYR A 311    10678   8042   8505   -344    999   1829       C  
ATOM   2230  CD2 TYR A 311      36.917  86.507  -2.355  1.00 55.80           C  
ANISOU 2230  CD2 TYR A 311     8901   5967   6332   -167    828   1866       C  
ATOM   2231  CE1 TYR A 311      39.548  86.971  -1.630  1.00 79.33           C  
ANISOU 2231  CE1 TYR A 311    11706   8882   9555   -441   1020   1977       C  
ATOM   2232  CE2 TYR A 311      37.452  87.789  -2.461  1.00 67.34           C  
ANISOU 2232  CE2 TYR A 311    10430   7291   7867   -255    851   2013       C  
ATOM   2233  CZ  TYR A 311      38.771  88.011  -2.099  1.00 77.14           C  
ANISOU 2233  CZ  TYR A 311    11582   8497   9230   -398    946   2069       C  
ATOM   2234  OH  TYR A 311      39.323  89.264  -2.206  1.00 81.76           O  
ANISOU 2234  OH  TYR A 311    12228   8937   9898   -500    963   2220       O  
ATOM   2235  N   LEU A 312      37.364  81.128  -1.695  1.00 53.65           N  
ANISOU 2235  N   LEU A 312     8242   6198   5944    -51    939   1372       N  
ATOM   2236  CA  LEU A 312      37.091  79.698  -1.554  1.00 47.30           C  
ANISOU 2236  CA  LEU A 312     7372   5500   5100      7    921   1231       C  
ATOM   2237  C   LEU A 312      36.665  79.297  -0.170  1.00 57.22           C  
ANISOU 2237  C   LEU A 312     8525   6721   6496      8    827   1108       C  
ATOM   2238  O   LEU A 312      36.713  80.079   0.784  1.00 50.63           O  
ANISOU 2238  O   LEU A 312     7661   5783   5793    -38    786   1119       O  
ATOM   2239  CB  LEU A 312      38.312  78.875  -1.951  1.00 44.79           C  
ANISOU 2239  CB  LEU A 312     6986   5280   4750    -27   1071   1228       C  
ATOM   2240  CG  LEU A 312      38.701  79.018  -3.424  1.00 63.62           C  
ANISOU 2240  CG  LEU A 312     9478   7735   6960     -5   1183   1336       C  
ATOM   2241  CD1 LEU A 312      40.065  78.468  -3.682  1.00 67.23           C  
ANISOU 2241  CD1 LEU A 312     9851   8274   7419    -47   1356   1359       C  
ATOM   2242  CD2 LEU A 312      37.694  78.317  -4.307  1.00 73.02           C  
ANISOU 2242  CD2 LEU A 312    10779   8998   7966    107   1112   1273       C  
ATOM   2243  N   TYR A 313      36.252  78.042  -0.087  1.00 61.49           N  
ANISOU 2243  N   TYR A 313     9020   7346   6998     63    794    991       N  
ATOM   2244  CA  TYR A 313      35.745  77.445   1.134  1.00 45.03           C  
ANISOU 2244  CA  TYR A 313     6838   5248   5022     76    709    874       C  
ATOM   2245  C   TYR A 313      36.811  77.557   2.228  1.00 40.90           C  
ANISOU 2245  C   TYR A 313     6207   4684   4651    -12    763    862       C  
ATOM   2246  O   TYR A 313      36.528  77.877   3.372  1.00 47.16           O  
ANISOU 2246  O   TYR A 313     6955   5407   5555    -25    696    823       O  
ATOM   2247  CB  TYR A 313      35.341  76.011   0.813  1.00 43.14           C  
ANISOU 2247  CB  TYR A 313     6576   5109   4706    134    685    771       C  
ATOM   2248  CG  TYR A 313      34.640  75.243   1.892  1.00 45.04           C  
ANISOU 2248  CG  TYR A 313     6727   5350   5035    156    593    659       C  
ATOM   2249  CD1 TYR A 313      33.595  75.805   2.605  1.00 44.66           C  
ANISOU 2249  CD1 TYR A 313     6675   5243   5049    186    488    651       C  
ATOM   2250  CD2 TYR A 313      34.991  73.931   2.160  1.00 46.07           C  
ANISOU 2250  CD2 TYR A 313     6780   5543   5182    156    615    566       C  
ATOM   2251  CE1 TYR A 313      32.950  75.108   3.575  1.00 54.05           C  
ANISOU 2251  CE1 TYR A 313     7780   6443   6313    208    419    563       C  
ATOM   2252  CE2 TYR A 313      34.339  73.213   3.135  1.00 49.61           C  
ANISOU 2252  CE2 TYR A 313     7149   5991   5709    172    534    477       C  
ATOM   2253  CZ  TYR A 313      33.327  73.802   3.840  1.00 56.10           C  
ANISOU 2253  CZ  TYR A 313     7962   6762   6589    195    441    479       C  
ATOM   2254  OH  TYR A 313      32.686  73.087   4.820  1.00 53.09           O  
ANISOU 2254  OH  TYR A 313     7497   6390   6285    211    374    403       O  
ATOM   2255  N   THR A 314      38.060  77.351   1.851  1.00 44.30           N  
ANISOU 2255  N   THR A 314     6595   5155   5082    -69    887    904       N  
ATOM   2256  CA  THR A 314      39.170  77.618   2.745  1.00 44.43           C  
ANISOU 2256  CA  THR A 314     6508   5128   5244   -163    935    919       C  
ATOM   2257  C   THR A 314      39.195  79.080   3.277  1.00 50.41           C  
ANISOU 2257  C   THR A 314     7305   5752   6097   -226    889    996       C  
ATOM   2258  O   THR A 314      39.260  79.303   4.482  1.00 46.60           O  
ANISOU 2258  O   THR A 314     6768   5200   5737   -262    826    947       O  
ATOM   2259  CB  THR A 314      40.489  77.304   2.031  1.00 50.81           C  
ANISOU 2259  CB  THR A 314     7267   6009   6031   -209   1087    981       C  
ATOM   2260  CG2 THR A 314      41.644  77.312   3.011  1.00 55.68           C  
ANISOU 2260  CG2 THR A 314     7745   6600   6811   -303   1123    980       C  
ATOM   2261  OG1 THR A 314      40.389  76.024   1.384  1.00 51.11           O  
ANISOU 2261  OG1 THR A 314     7303   6160   5957   -133   1128    909       O  
ATOM   2262  N   THR A 315      39.131  80.063   2.377  1.00 51.85           N  
ANISOU 2262  N   THR A 315     7592   5891   6216   -236    915   1115       N  
ATOM   2263  CA  THR A 315      39.144  81.478   2.749  1.00 39.88           C  
ANISOU 2263  CA  THR A 315     6135   4233   4785   -294    868   1196       C  
ATOM   2264  C   THR A 315      38.074  81.801   3.769  1.00 47.10           C  
ANISOU 2264  C   THR A 315     7078   5065   5755   -238    731   1113       C  
ATOM   2265  O   THR A 315      38.304  82.513   4.753  1.00 49.42           O  
ANISOU 2265  O   THR A 315     7362   5247   6169   -290    681   1104       O  
ATOM   2266  CB  THR A 315      38.883  82.427   1.533  1.00 54.53           C  
ANISOU 2266  CB  THR A 315     8129   6054   6538   -282    894   1335       C  
ATOM   2267  CG2 THR A 315      39.453  83.823   1.816  1.00 45.31           C  
ANISOU 2267  CG2 THR A 315     6997   4737   5482   -383    890   1446       C  
ATOM   2268  OG1 THR A 315      39.428  81.886   0.317  1.00 42.34           O  
ANISOU 2268  OG1 THR A 315     6593   4627   4869   -276   1018   1396       O  
ATOM   2269  N   THR A 316      36.885  81.279   3.497  1.00 42.08           N  
ANISOU 2269  N   THR A 316     6480   4484   5026   -129    670   1054       N  
ATOM   2270  CA  THR A 316      35.734  81.517   4.332  1.00 39.32           C  
ANISOU 2270  CA  THR A 316     6149   4078   4713    -55    554    984       C  
ATOM   2271  C   THR A 316      35.852  80.760   5.667  1.00 58.93           C  
ANISOU 2271  C   THR A 316     8521   6580   7292    -64    526    864       C  
ATOM   2272  O   THR A 316      35.321  81.215   6.672  1.00 68.34           O  
ANISOU 2272  O   THR A 316     9720   7696   8551    -36    452    818       O  
ATOM   2273  CB  THR A 316      34.438  81.144   3.584  1.00 58.24           C  
ANISOU 2273  CB  THR A 316     8600   6538   6990     58    495    970       C  
ATOM   2274  CG2 THR A 316      34.231  79.659   3.535  1.00 71.81           C  
ANISOU 2274  CG2 THR A 316    10238   8385   8663     92    499    873       C  
ATOM   2275  OG1 THR A 316      33.315  81.715   4.248  1.00 67.45           O  
ANISOU 2275  OG1 THR A 316     9797   7634   8197    133    391    941       O  
ATOM   2276  N   ASP A 317      36.556  79.627   5.705  1.00 67.04           N  
ANISOU 2276  N   ASP A 317     9449   7702   8320    -97    588    815       N  
ATOM   2277  CA  ASP A 317      36.772  78.948   6.992  1.00 65.17           C  
ANISOU 2277  CA  ASP A 317     9109   7476   8176   -112    561    715       C  
ATOM   2278  C   ASP A 317      37.890  79.641   7.766  1.00 64.69           C  
ANISOU 2278  C   ASP A 317     9017   7329   8234   -215    576    741       C  
ATOM   2279  O   ASP A 317      37.955  79.535   8.993  1.00 55.66           O  
ANISOU 2279  O   ASP A 317     7826   6151   7170   -226    525    669       O  
ATOM   2280  CB  ASP A 317      37.096  77.456   6.817  1.00 57.02           C  
ANISOU 2280  CB  ASP A 317     7986   6567   7113   -103    609    650       C  
ATOM   2281  CG  ASP A 317      35.853  76.567   6.887  1.00 55.42           C  
ANISOU 2281  CG  ASP A 317     7776   6424   6856    -11    542    571       C  
ATOM   2282  OD1 ASP A 317      35.011  76.762   7.793  1.00 44.36           O  
ANISOU 2282  OD1 ASP A 317     6370   4985   5498     31    465    527       O  
ATOM   2283  OD2 ASP A 317      35.716  75.671   6.022  1.00 52.12           O1-
ANISOU 2283  OD2 ASP A 317     7358   6092   6353     21    567    554       O1-
ATOM   2284  N   ILE A 318      38.765  80.359   7.059  1.00 64.17           N  
ANISOU 2284  N   ILE A 318     8977   7226   8177   -293    640    847       N  
ATOM   2285  CA  ILE A 318      39.757  81.171   7.760  1.00 63.48           C  
ANISOU 2285  CA  ILE A 318     8866   7038   8216   -403    633    884       C  
ATOM   2286  C   ILE A 318      39.099  82.361   8.435  1.00 60.67           C  
ANISOU 2286  C   ILE A 318     8614   6536   7903   -386    531    880       C  
ATOM   2287  O   ILE A 318      39.287  82.582   9.621  1.00 59.44           O  
ANISOU 2287  O   ILE A 318     8440   6309   7835   -414    465    818       O  
ATOM   2288  CB  ILE A 318      40.861  81.709   6.849  1.00 57.37           C  
ANISOU 2288  CB  ILE A 318     8086   6255   7458   -502    729   1016       C  
ATOM   2289  CG1 ILE A 318      41.660  80.571   6.216  1.00 63.87           C  
ANISOU 2289  CG1 ILE A 318     8801   7221   8243   -513    847   1021       C  
ATOM   2290  CG2 ILE A 318      41.807  82.541   7.654  1.00 43.27           C  
ANISOU 2290  CG2 ILE A 318     6268   4354   5819   -624    697   1050       C  
ATOM   2291  CD1 ILE A 318      42.862  81.060   5.425  1.00 54.54           C  
ANISOU 2291  CD1 ILE A 318     7586   6044   7091   -614    961   1158       C  
ATOM   2292  N   ALA A 319      38.332  83.125   7.663  1.00 58.40           N  
ANISOU 2292  N   ALA A 319     8443   6200   7547   -334    515    946       N  
ATOM   2293  CA  ALA A 319      37.629  84.305   8.173  1.00 53.60           C  
ANISOU 2293  CA  ALA A 319     7948   5445   6971   -297    422    948       C  
ATOM   2294  C   ALA A 319      36.791  83.961   9.385  1.00 51.11           C  
ANISOU 2294  C   ALA A 319     7619   5128   6674   -209    343    820       C  
ATOM   2295  O   ALA A 319      36.871  84.601  10.431  1.00 63.72           O  
ANISOU 2295  O   ALA A 319     9251   6614   8347   -223    278    776       O  
ATOM   2296  CB  ALA A 319      36.745  84.903   7.092  1.00 38.87           C  
ANISOU 2296  CB  ALA A 319     6198   3561   5012   -222    416   1028       C  
ATOM   2297  N   CYS A 320      35.984  82.934   9.204  1.00 46.48           N  
ANISOU 2297  N   CYS A 320     6983   4666   6013   -119    351    763       N  
ATOM   2298  CA  CYS A 320      35.076  82.413  10.194  1.00 43.04           C  
ANISOU 2298  CA  CYS A 320     6515   4261   5578    -28    296    657       C  
ATOM   2299  C   CYS A 320      35.790  82.087  11.504  1.00 46.01           C  
ANISOU 2299  C   CYS A 320     6825   4621   6038    -83    280    579       C  
ATOM   2300  O   CYS A 320      35.295  82.403  12.573  1.00 51.57           O  
ANISOU 2300  O   CYS A 320     7559   5266   6768    -30    220    513       O  
ATOM   2301  CB  CYS A 320      34.369  81.203   9.562  1.00 45.62           C  
ANISOU 2301  CB  CYS A 320     6779   4734   5821     40    318    631       C  
ATOM   2302  SG  CYS A 320      34.064  79.822  10.553  1.00 54.43           S  
ANISOU 2302  SG  CYS A 320     7776   5951   6953     74    307    517       S  
ATOM   2303  N   ALA A 321      36.986  81.512  11.437  1.00 44.34           N  
ANISOU 2303  N   ALA A 321     6526   4455   5865   -184    332    588       N  
ATOM   2304  CA  ALA A 321      37.760  81.309  12.668  1.00 37.62           C  
ANISOU 2304  CA  ALA A 321     5617   3578   5098   -245    302    524       C  
ATOM   2305  C   ALA A 321      38.236  82.640  13.264  1.00 43.91           C  
ANISOU 2305  C   ALA A 321     6499   4212   5973   -308    239    544       C  
ATOM   2306  O   ALA A 321      38.038  82.910  14.443  1.00 50.30           O  
ANISOU 2306  O   ALA A 321     7344   4956   6813   -282    167    468       O  
ATOM   2307  CB  ALA A 321      38.928  80.420  12.423  1.00 33.67           C  
ANISOU 2307  CB  ALA A 321     4997   3165   4632   -331    367    538       C  
ATOM   2308  N   LYS A 322      38.859  83.471  12.443  1.00 43.16           N  
ANISOU 2308  N   LYS A 322     6445   4047   5906   -390    265    647       N  
ATOM   2309  CA  LYS A 322      39.333  84.776  12.882  1.00 42.34           C  
ANISOU 2309  CA  LYS A 322     6431   3771   5885   -465    198    678       C  
ATOM   2310  C   LYS A 322      38.175  85.575  13.509  1.00 48.14           C  
ANISOU 2310  C   LYS A 322     7302   4398   6592   -350    114    621       C  
ATOM   2311  O   LYS A 322      38.317  86.141  14.593  1.00 49.12           O  
ANISOU 2311  O   LYS A 322     7484   4410   6769   -362     31    558       O  
ATOM   2312  CB  LYS A 322      39.963  85.526  11.698  1.00 48.43           C  
ANISOU 2312  CB  LYS A 322     7232   4492   6677   -557    251    820       C  
ATOM   2313  CG  LYS A 322      40.685  86.819  12.044  1.00 54.24           C  
ANISOU 2313  CG  LYS A 322     8041   5044   7523   -672    185    873       C  
ATOM   2314  CD  LYS A 322      41.086  87.608  10.788  1.00 52.44           C  
ANISOU 2314  CD  LYS A 322     7859   4765   7303   -748    244   1032       C  
ATOM   2315  CE  LYS A 322      41.216  89.098  11.122  1.00 62.60           C  
ANISOU 2315  CE  LYS A 322     9280   5828   8676   -811    148   1075       C  
ATOM   2316  NZ  LYS A 322      41.634  89.965   9.981  1.00 79.12           N1+
ANISOU 2316  NZ  LYS A 322    11425   7848  10788   -897    199   1243       N1+
ATOM   2317  N   TYR A 323      37.022  85.564  12.844  1.00 48.80           N  
ANISOU 2317  N   TYR A 323     7432   4522   6588   -232    133    638       N  
ATOM   2318  CA  TYR A 323      35.841  86.296  13.291  1.00 46.03           C  
ANISOU 2318  CA  TYR A 323     7197   4085   6209   -103     69    597       C  
ATOM   2319  C   TYR A 323      35.350  85.840  14.659  1.00 55.55           C  
ANISOU 2319  C   TYR A 323     8383   5314   7410    -22     27    469       C  
ATOM   2320  O   TYR A 323      35.048  86.649  15.537  1.00 61.70           O  
ANISOU 2320  O   TYR A 323     9265   5971   8208     28    -40    415       O  
ATOM   2321  CB  TYR A 323      34.721  86.132  12.271  1.00 52.32           C  
ANISOU 2321  CB  TYR A 323     8009   4956   6916      7     99    643       C  
ATOM   2322  CG  TYR A 323      33.415  86.821  12.627  1.00 54.59           C  
ANISOU 2322  CG  TYR A 323     8394   5174   7175    159     42    612       C  
ATOM   2323  CD1 TYR A 323      33.281  88.199  12.519  1.00 47.67           C  
ANISOU 2323  CD1 TYR A 323     7661   4124   6326    176     -9    659       C  
ATOM   2324  CD2 TYR A 323      32.303  86.082  13.020  1.00 55.91           C  
ANISOU 2324  CD2 TYR A 323     8502   5448   7292    287     42    543       C  
ATOM   2325  CE1 TYR A 323      32.086  88.824  12.822  1.00 58.22           C  
ANISOU 2325  CE1 TYR A 323     9084   5399   7640    331    -56    630       C  
ATOM   2326  CE2 TYR A 323      31.100  86.694  13.324  1.00 61.96           C  
ANISOU 2326  CE2 TYR A 323     9340   6165   8040    436      1    523       C  
ATOM   2327  CZ  TYR A 323      30.996  88.067  13.226  1.00 68.95           C  
ANISOU 2327  CZ  TYR A 323    10370   6879   8950    464    -46    563       C  
ATOM   2328  OH  TYR A 323      29.798  88.678  13.534  1.00 72.76           O  
ANISOU 2328  OH  TYR A 323    10919   7310   9415    628    -82    540       O  
ATOM   2329  N   ARG A 324      35.277  84.531  14.829  1.00 50.99           N  
ANISOU 2329  N   ARG A 324     7680   4892   6801     -7     70    424       N  
ATOM   2330  CA  ARG A 324      34.727  83.949  16.033  1.00 50.58           C  
ANISOU 2330  CA  ARG A 324     7599   4888   6732     75     46    319       C  
ATOM   2331  C   ARG A 324      35.576  84.278  17.255  1.00 54.54           C  
ANISOU 2331  C   ARG A 324     8131   5299   7291     10    -13    255       C  
ATOM   2332  O   ARG A 324      35.070  84.384  18.385  1.00 61.38           O  
ANISOU 2332  O   ARG A 324     9046   6138   8137     93    -54    170       O  
ATOM   2333  CB  ARG A 324      34.594  82.437  15.859  1.00 33.35           C  
ANISOU 2333  CB  ARG A 324     5274   2881   4515     84    102    299       C  
ATOM   2334  CG  ARG A 324      33.424  82.066  14.989  1.00 34.57           C  
ANISOU 2334  CG  ARG A 324     5409   3122   4602    182    131    331       C  
ATOM   2335  CD  ARG A 324      33.452  80.615  14.575  1.00 36.29           C  
ANISOU 2335  CD  ARG A 324     5502   3493   4794    165    178    322       C  
ATOM   2336  NE  ARG A 324      32.361  80.359  13.641  1.00 51.50           N  
ANISOU 2336  NE  ARG A 324     7421   5488   6659    246    186    357       N  
ATOM   2337  CZ  ARG A 324      32.173  79.202  13.022  1.00 51.69           C  
ANISOU 2337  CZ  ARG A 324     7361   5632   6647    245    213    356       C  
ATOM   2338  NH1 ARG A 324      33.020  78.202  13.224  1.00 45.24           N1+
ANISOU 2338  NH1 ARG A 324     6461   4878   5851    173    247    325       N1+
ATOM   2339  NH2 ARG A 324      31.160  79.050  12.185  1.00 51.39           N  
ANISOU 2339  NH2 ARG A 324     7326   5645   6556    315    199    387       N  
ATOM   2340  N   TYR A 325      36.869  84.435  17.034  1.00 47.48           N  
ANISOU 2340  N   TYR A 325     7208   4363   6468   -138    -19    297       N  
ATOM   2341  CA  TYR A 325      37.737  84.836  18.120  1.00 54.64           C  
ANISOU 2341  CA  TYR A 325     8148   5172   7439   -215    -96    244       C  
ATOM   2342  C   TYR A 325      37.694  86.356  18.293  1.00 59.94           C  
ANISOU 2342  C   TYR A 325     8985   5644   8146   -221   -175    252       C  
ATOM   2343  O   TYR A 325      37.355  86.856  19.372  1.00 61.54           O  
ANISOU 2343  O   TYR A 325     9291   5755   8334   -156   -249    164       O  
ATOM   2344  CB  TYR A 325      39.163  84.359  17.874  1.00 55.09           C  
ANISOU 2344  CB  TYR A 325     8087   5269   7576   -374    -78    289       C  
ATOM   2345  CG  TYR A 325      40.145  84.944  18.849  1.00 49.55           C  
ANISOU 2345  CG  TYR A 325     7421   4447   6959   -476   -178    253       C  
ATOM   2346  CD1 TYR A 325      40.162  84.527  20.176  1.00 48.84           C  
ANISOU 2346  CD1 TYR A 325     7334   4369   6854   -442   -242    147       C  
ATOM   2347  CD2 TYR A 325      41.051  85.911  18.449  1.00 55.94           C  
ANISOU 2347  CD2 TYR A 325     8262   5129   7863   -611   -215    329       C  
ATOM   2348  CE1 TYR A 325      41.052  85.061  21.081  1.00 55.02           C  
ANISOU 2348  CE1 TYR A 325     8158   5039   7707   -536   -353    108       C  
ATOM   2349  CE2 TYR A 325      41.944  86.459  19.348  1.00 71.13           C  
ANISOU 2349  CE2 TYR A 325    10218   6934   9873   -714   -327    295       C  
ATOM   2350  CZ  TYR A 325      41.942  86.027  20.666  1.00 69.86           C  
ANISOU 2350  CZ  TYR A 325    10066   6787   9689   -675   -401    179       C  
ATOM   2351  OH  TYR A 325      42.837  86.567  21.560  1.00 74.21           O  
ANISOU 2351  OH  TYR A 325    10657   7219  10321   -779   -530    140       O  
ATOM   2352  N   GLU A 326      38.018  87.082  17.227  1.00 59.51           N  
ANISOU 2352  N   GLU A 326     8964   5518   8129   -292   -157    359       N  
ATOM   2353  CA  GLU A 326      38.139  88.541  17.295  1.00 64.54           C  
ANISOU 2353  CA  GLU A 326     9757   5946   8818   -324   -237    384       C  
ATOM   2354  C   GLU A 326      36.823  89.236  17.615  1.00 64.79           C  
ANISOU 2354  C   GLU A 326     9934   5897   8785   -152   -271    331       C  
ATOM   2355  O   GLU A 326      36.787  90.178  18.412  1.00 64.07           O  
ANISOU 2355  O   GLU A 326     9984   5640   8718   -130   -363    272       O  
ATOM   2356  CB  GLU A 326      38.702  89.091  15.981  1.00 65.66           C  
ANISOU 2356  CB  GLU A 326     9897   6044   9008   -433   -194    530       C  
ATOM   2357  CG  GLU A 326      40.151  88.692  15.759  1.00 81.64           C  
ANISOU 2357  CG  GLU A 326    11789   8110  11120   -614   -168    590       C  
ATOM   2358  CD  GLU A 326      40.752  89.309  14.515  1.00 88.47           C  
ANISOU 2358  CD  GLU A 326    12654   8927  12033   -726   -116    746       C  
ATOM   2359  OE1 GLU A 326      40.070  90.163  13.896  1.00 82.76           O  
ANISOU 2359  OE1 GLU A 326    12056   8112  11278   -669   -120    804       O  
ATOM   2360  OE2 GLU A 326      41.898  88.926  14.161  1.00 89.71           O1-
ANISOU 2360  OE2 GLU A 326    12683   9144  12258   -863    -66    815       O1-
ATOM   2361  N   THR A 327      35.738  88.780  17.005  1.00 58.53           N  
ANISOU 2361  N   THR A 327     9108   5217   7912    -25   -203    351       N  
ATOM   2362  CA  THR A 327      34.476  89.469  17.199  1.00 57.03           C  
ANISOU 2362  CA  THR A 327     9039   4958   7672    146   -228    318       C  
ATOM   2363  C   THR A 327      33.540  88.757  18.191  1.00 54.50           C  
ANISOU 2363  C   THR A 327     8683   4742   7282    295   -214    209       C  
ATOM   2364  O   THR A 327      32.993  89.407  19.074  1.00 62.58           O  
ANISOU 2364  O   THR A 327     9822   5668   8286    405   -261    133       O  
ATOM   2365  CB  THR A 327      33.765  89.674  15.862  1.00 57.66           C  
ANISOU 2365  CB  THR A 327     9124   5069   7716    201   -181    424       C  
ATOM   2366  CG2 THR A 327      32.529  90.518  16.052  1.00 53.90           C  
ANISOU 2366  CG2 THR A 327     8773   4502   7206    377   -217    400       C  
ATOM   2367  OG1 THR A 327      34.652  90.334  14.946  1.00 59.60           O  
ANISOU 2367  OG1 THR A 327     9406   5221   8018     61   -184    538       O  
ATOM   2368  N   LEU A 328      33.361  87.442  18.073  1.00 46.38           N  
ANISOU 2368  N   LEU A 328     7501   3905   6216    303   -147    203       N  
ATOM   2369  CA  LEU A 328      32.488  86.739  19.007  1.00 41.50           C  
ANISOU 2369  CA  LEU A 328     6839   3389   5539    433   -126    117       C  
ATOM   2370  C   LEU A 328      33.152  86.530  20.362  1.00 48.86           C  
ANISOU 2370  C   LEU A 328     7788   4297   6479    395   -169     20       C  
ATOM   2371  O   LEU A 328      32.454  86.388  21.356  1.00 53.30           O  
ANISOU 2371  O   LEU A 328     8378   4885   6988    517   -168    -58       O  
ATOM   2372  CB  LEU A 328      32.019  85.380  18.452  1.00 40.73           C  
ANISOU 2372  CB  LEU A 328     6578   3492   5405    451    -51    144       C  
ATOM   2373  CG  LEU A 328      31.157  85.435  17.187  1.00 35.72           C  
ANISOU 2373  CG  LEU A 328     5923   2906   4742    512    -20    227       C  
ATOM   2374  CD1 LEU A 328      30.485  84.144  16.847  1.00 34.64           C  
ANISOU 2374  CD1 LEU A 328     5643   2951   4567    552     31    233       C  
ATOM   2375  CD2 LEU A 328      30.129  86.567  17.272  1.00 42.65           C  
ANISOU 2375  CD2 LEU A 328     6922   3678   5605    657    -52    229       C  
ATOM   2376  N   HIS A 329      34.486  86.526  20.389  1.00 46.40           N  
ANISOU 2376  N   HIS A 329     7458   3941   6233    231   -206     32       N  
ATOM   2377  CA  HIS A 329      35.300  86.292  21.599  1.00 47.82           C  
ANISOU 2377  CA  HIS A 329     7644   4098   6428    169   -264    -50       C  
ATOM   2378  C   HIS A 329      35.207  84.880  22.147  1.00 51.00           C  
ANISOU 2378  C   HIS A 329     7912   4676   6788    192   -216    -90       C  
ATOM   2379  O   HIS A 329      35.285  84.682  23.360  1.00 59.30           O  
ANISOU 2379  O   HIS A 329     8997   5727   7808    225   -255   -174       O  
ATOM   2380  CB  HIS A 329      34.934  87.283  22.709  1.00 44.52           C  
ANISOU 2380  CB  HIS A 329     7404   3532   5978    264   -343   -144       C  
ATOM   2381  CG  HIS A 329      35.087  88.706  22.291  1.00 55.76           C  
ANISOU 2381  CG  HIS A 329     8978   4756   7453    237   -408   -113       C  
ATOM   2382  CD2 HIS A 329      34.176  89.705  22.176  1.00 65.34           C  
ANISOU 2382  CD2 HIS A 329    10331   5856   8639    367   -421   -119       C  
ATOM   2383  ND1 HIS A 329      36.289  89.227  21.874  1.00 56.11           N  
ANISOU 2383  ND1 HIS A 329     9033   4691   7595     58   -466    -57       N  
ATOM   2384  CE1 HIS A 329      36.123  90.497  21.537  1.00 61.14           C  
ANISOU 2384  CE1 HIS A 329     9819   5147   8264     70   -517    -29       C  
ATOM   2385  NE2 HIS A 329      34.851  90.807  21.709  1.00 69.39           N  
ANISOU 2385  NE2 HIS A 329    10948   6184   9232    261   -492    -69       N  
ATOM   2386  N   ALA A 330      35.072  83.901  21.256  1.00 45.33           N  
ANISOU 2386  N   ALA A 330     7053   4101   6068    173   -137    -29       N  
ATOM   2387  CA  ALA A 330      34.981  82.509  21.684  1.00 46.18           C  
ANISOU 2387  CA  ALA A 330     7032   4367   6146    188    -93    -57       C  
ATOM   2388  C   ALA A 330      36.238  82.051  22.414  1.00 49.11           C  
ANISOU 2388  C   ALA A 330     7358   4740   6561     73   -139    -91       C  
ATOM   2389  O   ALA A 330      37.360  82.436  22.069  1.00 45.48           O  
ANISOU 2389  O   ALA A 330     6891   4212   6177    -59   -175    -56       O  
ATOM   2390  CB  ALA A 330      34.697  81.595  20.499  1.00 36.95           C  
ANISOU 2390  CB  ALA A 330     5737   3328   4972    178    -14     12       C  
ATOM   2391  N   ASP A 331      36.023  81.235  23.441  1.00 50.95           N  
ANISOU 2391  N   ASP A 331     7557   5053   6749    126   -139   -152       N  
ATOM   2392  CA  ASP A 331      37.094  80.571  24.158  1.00 39.32           C  
ANISOU 2392  CA  ASP A 331     6023   3609   5309     35   -181   -180       C  
ATOM   2393  C   ASP A 331      37.361  79.256  23.481  1.00 45.97           C  
ANISOU 2393  C   ASP A 331     6700   4591   6175    -10   -111   -132       C  
ATOM   2394  O   ASP A 331      38.390  78.625  23.687  1.00 52.65           O  
ANISOU 2394  O   ASP A 331     7463   5471   7071   -101   -132   -130       O  
ATOM   2395  CB  ASP A 331      36.711  80.330  25.610  1.00 46.17           C  
ANISOU 2395  CB  ASP A 331     6948   4492   6102    123   -215   -264       C  
ATOM   2396  CG  ASP A 331      36.311  81.604  26.332  1.00 57.23           C  
ANISOU 2396  CG  ASP A 331     8533   5755   7458    199   -278   -327       C  
ATOM   2397  OD1 ASP A 331      37.176  82.498  26.528  1.00 47.86           O  
ANISOU 2397  OD1 ASP A 331     7433   4431   6320    112   -373   -347       O  
ATOM   2398  OD2 ASP A 331      35.126  81.698  26.717  1.00 69.94           O1-
ANISOU 2398  OD2 ASP A 331    10197   7392   8985    347   -233   -355       O1-
ATOM   2399  N   ARG A 332      36.410  78.841  22.663  1.00 38.44           N  
ANISOU 2399  N   ARG A 332     5702   3716   5188     58    -35    -96       N  
ATOM   2400  CA  ARG A 332      36.455  77.512  22.107  1.00 43.15           C  
ANISOU 2400  CA  ARG A 332     6161   4443   5791     39     26    -66       C  
ATOM   2401  C   ARG A 332      35.485  77.421  20.950  1.00 44.98           C  
ANISOU 2401  C   ARG A 332     6374   4723   5993     95     86    -19       C  
ATOM   2402  O   ARG A 332      34.400  77.995  21.018  1.00 45.94           O  
ANISOU 2402  O   ARG A 332     6563   4822   6072    194     87    -24       O  
ATOM   2403  CB  ARG A 332      36.131  76.463  23.185  1.00 40.06           C  
ANISOU 2403  CB  ARG A 332     5722   4136   5363     91     27   -112       C  
ATOM   2404  CG  ARG A 332      35.971  75.057  22.629  1.00 43.49           C  
ANISOU 2404  CG  ARG A 332     6027   4693   5803     86     85    -85       C  
ATOM   2405  CD  ARG A 332      36.303  73.992  23.642  1.00 46.55           C  
ANISOU 2405  CD  ARG A 332     6356   5142   6190     82     71   -115       C  
ATOM   2406  NE  ARG A 332      35.144  73.489  24.380  1.00 46.92           N  
ANISOU 2406  NE  ARG A 332     6403   5249   6175    183     94   -131       N  
ATOM   2407  CZ  ARG A 332      34.694  72.236  24.328  1.00 44.46           C  
ANISOU 2407  CZ  ARG A 332     5999   5032   5862    201    132   -113       C  
ATOM   2408  NH1 ARG A 332      35.281  71.317  23.564  1.00 41.73           N1+
ANISOU 2408  NH1 ARG A 332     5564   4729   5564    136    148    -91       N1+
ATOM   2409  NH2 ARG A 332      33.643  71.899  25.049  1.00 44.07           N  
ANISOU 2409  NH2 ARG A 332     5949   5032   5763    286    155   -115       N  
ATOM   2410  N   VAL A 333      35.881  76.728  19.880  1.00 45.23           N  
ANISOU 2410  N   VAL A 333     6319   4820   6046     39    131     27       N  
ATOM   2411  CA  VAL A 333      34.978  76.533  18.742  1.00 38.34           C  
ANISOU 2411  CA  VAL A 333     5431   4000   5136     90    175     68       C  
ATOM   2412  C   VAL A 333      34.865  75.078  18.341  1.00 42.37           C  
ANISOU 2412  C   VAL A 333     5832   4627   5638     87    213     68       C  
ATOM   2413  O   VAL A 333      35.865  74.409  18.070  1.00 43.87           O  
ANISOU 2413  O   VAL A 333     5958   4850   5862     14    234     73       O  
ATOM   2414  CB  VAL A 333      35.416  77.318  17.507  1.00 39.04           C  
ANISOU 2414  CB  VAL A 333     5561   4037   5235     36    192    133       C  
ATOM   2415  CG1 VAL A 333      34.305  77.315  16.486  1.00 40.04           C  
ANISOU 2415  CG1 VAL A 333     5703   4204   5308    109    214    170       C  
ATOM   2416  CG2 VAL A 333      35.823  78.747  17.873  1.00 34.96           C  
ANISOU 2416  CG2 VAL A 333     5153   3381   4749      6    145    140       C  
ATOM   2417  N   LEU A 334      33.629  74.600  18.289  1.00 40.68           N  
ANISOU 2417  N   LEU A 334     5596   4473   5385    170    221     65       N  
ATOM   2418  CA  LEU A 334      33.341  73.216  17.938  1.00 41.80           C  
ANISOU 2418  CA  LEU A 334     5646   4714   5523    172    242     62       C  
ATOM   2419  C   LEU A 334      32.762  73.103  16.515  1.00 45.19           C  
ANISOU 2419  C   LEU A 334     6075   5178   5918    188    255    101       C  
ATOM   2420  O   LEU A 334      31.773  73.754  16.189  1.00 43.37           O  
ANISOU 2420  O   LEU A 334     5886   4933   5659    252    239    124       O  
ATOM   2421  CB  LEU A 334      32.359  72.620  18.946  1.00 43.85           C  
ANISOU 2421  CB  LEU A 334     5866   5022   5772    242    233     38       C  
ATOM   2422  CG  LEU A 334      32.861  72.038  20.261  1.00 48.49           C  
ANISOU 2422  CG  LEU A 334     6424   5622   6379    226    225      1       C  
ATOM   2423  CD1 LEU A 334      33.987  72.838  20.854  1.00 47.45           C  
ANISOU 2423  CD1 LEU A 334     6352   5412   6266    176    200    -21       C  
ATOM   2424  CD2 LEU A 334      31.708  71.970  21.238  1.00 46.45           C  
ANISOU 2424  CD2 LEU A 334     6163   5394   6092    316    228     -7       C  
ATOM   2425  N   TYR A 335      33.379  72.276  15.678  1.00 32.01           N  
ANISOU 2425  N   TYR A 335     4363   3551   4248    138    280    105       N  
ATOM   2426  CA  TYR A 335      32.927  72.090  14.305  1.00 31.30           C  
ANISOU 2426  CA  TYR A 335     4287   3495   4109    152    287    134       C  
ATOM   2427  C   TYR A 335      32.402  70.673  14.100  1.00 44.34           C  
ANISOU 2427  C   TYR A 335     5870   5223   5754    166    274    107       C  
ATOM   2428  O   TYR A 335      33.164  69.690  14.013  1.00 42.74           O  
ANISOU 2428  O   TYR A 335     5623   5049   5568    126    297     82       O  
ATOM   2429  CB  TYR A 335      34.057  72.349  13.320  1.00 35.89           C  
ANISOU 2429  CB  TYR A 335     4897   4063   4677     91    333    164       C  
ATOM   2430  CG  TYR A 335      34.583  73.751  13.303  1.00 37.50           C  
ANISOU 2430  CG  TYR A 335     5171   4184   4893     61    341    207       C  
ATOM   2431  CD1 TYR A 335      35.436  74.204  14.310  1.00 45.77           C  
ANISOU 2431  CD1 TYR A 335     6212   5174   6004     12    335    193       C  
ATOM   2432  CD2 TYR A 335      34.246  74.627  12.268  1.00 32.84           C  
ANISOU 2432  CD2 TYR A 335     4660   3564   4254     78    344    264       C  
ATOM   2433  CE1 TYR A 335      35.948  75.506  14.287  1.00 50.37           C  
ANISOU 2433  CE1 TYR A 335     6864   5665   6609    -28    330    233       C  
ATOM   2434  CE2 TYR A 335      34.741  75.917  12.231  1.00 42.26           C  
ANISOU 2434  CE2 TYR A 335     5923   4668   5467     43    348    312       C  
ATOM   2435  CZ  TYR A 335      35.588  76.356  13.245  1.00 48.31           C  
ANISOU 2435  CZ  TYR A 335     6680   5370   6305    -13    340    294       C  
ATOM   2436  OH  TYR A 335      36.067  77.636  13.207  1.00 43.45           O  
ANISOU 2436  OH  TYR A 335     6138   4651   5719    -57    331    341       O  
ATOM   2437  N   TYR A 336      31.089  70.575  14.023  1.00 39.65           N  
ANISOU 2437  N   TYR A 336     5265   4655   5144    224    234    116       N  
ATOM   2438  CA  TYR A 336      30.443  69.317  13.740  1.00 31.33           C  
ANISOU 2438  CA  TYR A 336     4151   3661   4091    231    205     99       C  
ATOM   2439  C   TYR A 336      30.271  69.165  12.252  1.00 41.49           C  
ANISOU 2439  C   TYR A 336     5480   4967   5317    231    187    111       C  
ATOM   2440  O   TYR A 336      29.211  69.486  11.704  1.00 45.44           O  
ANISOU 2440  O   TYR A 336     5996   5481   5789    275    139    138       O  
ATOM   2441  CB  TYR A 336      29.103  69.249  14.473  1.00 32.37           C  
ANISOU 2441  CB  TYR A 336     4232   3819   4249    287    168    110       C  
ATOM   2442  CG  TYR A 336      29.332  69.041  15.950  1.00 35.95           C  
ANISOU 2442  CG  TYR A 336     4643   4269   4747    287    191     92       C  
ATOM   2443  CD1 TYR A 336      29.602  67.781  16.449  1.00 36.44           C  
ANISOU 2443  CD1 TYR A 336     4640   4361   4843    251    192     68       C  
ATOM   2444  CD2 TYR A 336      29.331  70.102  16.832  1.00 39.07           C  
ANISOU 2444  CD2 TYR A 336     5078   4624   5142    323    208     96       C  
ATOM   2445  CE1 TYR A 336      29.822  67.582  17.774  1.00 38.97           C  
ANISOU 2445  CE1 TYR A 336     4932   4681   5193    253    210     58       C  
ATOM   2446  CE2 TYR A 336      29.562  69.905  18.185  1.00 39.47           C  
ANISOU 2446  CE2 TYR A 336     5107   4674   5215    328    225     75       C  
ATOM   2447  CZ  TYR A 336      29.811  68.639  18.638  1.00 42.19           C  
ANISOU 2447  CZ  TYR A 336     5384   5059   5589    291    227     60       C  
ATOM   2448  OH  TYR A 336      30.044  68.404  19.965  1.00 53.40           O  
ANISOU 2448  OH  TYR A 336     6788   6481   7021    297    240     46       O  
ATOM   2449  N   ILE A 337      31.344  68.721  11.605  1.00 39.11           N  
ANISOU 2449  N   ILE A 337     5199   4670   4992    188    227     93       N  
ATOM   2450  CA  ILE A 337      31.377  68.497  10.161  1.00 45.14           C  
ANISOU 2450  CA  ILE A 337     6019   5455   5677    191    224     97       C  
ATOM   2451  C   ILE A 337      31.788  67.047   9.843  1.00 44.14           C  
ANISOU 2451  C   ILE A 337     5864   5361   5547    172    226     42       C  
ATOM   2452  O   ILE A 337      32.703  66.522  10.483  1.00 43.05           O  
ANISOU 2452  O   ILE A 337     5681   5218   5460    143    269     16       O  
ATOM   2453  CB  ILE A 337      32.398  69.429   9.411  1.00 46.60           C  
ANISOU 2453  CB  ILE A 337     6277   5616   5813    170    292    136       C  
ATOM   2454  CG1 ILE A 337      32.400  70.901   9.891  1.00 43.04           C  
ANISOU 2454  CG1 ILE A 337     5861   5106   5385    171    301    187       C  
ATOM   2455  CG2 ILE A 337      32.268  69.255   7.899  1.00 48.92           C  
ANISOU 2455  CG2 ILE A 337     6647   5940   6002    189    289    147       C  
ATOM   2456  CD1 ILE A 337      31.054  71.533  10.051  1.00 58.09           C  
ANISOU 2456  CD1 ILE A 337     7785   6999   7287    231    235    210       C  
ATOM   2457  N   ASP A 338      31.130  66.442   8.847  1.00 36.68           N  
ANISOU 2457  N   ASP A 338     4954   4441   4542    192    171     25       N  
ATOM   2458  CA  ASP A 338      31.509  65.164   8.247  1.00 39.81           C  
ANISOU 2458  CA  ASP A 338     5361   4855   4912    185    166    -33       C  
ATOM   2459  C   ASP A 338      33.019  64.903   8.205  1.00 39.85           C  
ANISOU 2459  C   ASP A 338     5367   4858   4916    167    267    -53       C  
ATOM   2460  O   ASP A 338      33.790  65.789   7.884  1.00 49.98           O  
ANISOU 2460  O   ASP A 338     6682   6138   6168    159    340    -14       O  
ATOM   2461  CB  ASP A 338      30.955  65.073   6.812  1.00 40.88           C  
ANISOU 2461  CB  ASP A 338     5587   5008   4936    214    114    -39       C  
ATOM   2462  CG  ASP A 338      31.152  63.673   6.185  1.00 57.13           C  
ANISOU 2462  CG  ASP A 338     7675   7074   6959    217     87   -114       C  
ATOM   2463  OD1 ASP A 338      32.298  63.346   5.774  1.00 47.08           O  
ANISOU 2463  OD1 ASP A 338     6436   5805   5646    223    172   -142       O  
ATOM   2464  OD2 ASP A 338      30.164  62.893   6.125  1.00 67.61           O1-
ANISOU 2464  OD2 ASP A 338     8987   8398   8305    215    -21   -143       O1-
ATOM   2465  N   SER A 339      33.433  63.678   8.520  1.00 43.38           N  
ANISOU 2465  N   SER A 339     5773   5305   5406    159    268   -108       N  
ATOM   2466  CA  SER A 339      34.855  63.307   8.537  1.00 36.62           C  
ANISOU 2466  CA  SER A 339     4899   4452   4564    152    360   -128       C  
ATOM   2467  C   SER A 339      35.622  63.569   7.248  1.00 45.29           C  
ANISOU 2467  C   SER A 339     6073   5575   5561    175    440   -122       C  
ATOM   2468  O   SER A 339      36.844  63.805   7.269  1.00 33.66           O  
ANISOU 2468  O   SER A 339     4572   4112   4105    164    539   -102       O  
ATOM   2469  CB  SER A 339      34.986  61.834   8.868  1.00 40.31           C  
ANISOU 2469  CB  SER A 339     5329   4908   5079    157    332   -193       C  
ATOM   2470  OG  SER A 339      34.279  61.561  10.065  1.00 64.19           O  
ANISOU 2470  OG  SER A 339     8282   7914   8192    134    268   -186       O  
ATOM   2471  N   ARG A 340      34.934  63.504   6.114  1.00 29.68           N  
ANISOU 2471  N   ARG A 340     4189   3612   3477    207    398   -134       N  
ATOM   2472  CA  ARG A 340      35.663  63.665   4.859  1.00 39.42           C  
ANISOU 2472  CA  ARG A 340     5507   4876   4593    239    483   -128       C  
ATOM   2473  C   ARG A 340      36.253  65.078   4.684  1.00 41.54           C  
ANISOU 2473  C   ARG A 340     5786   5153   4844    217    569    -37       C  
ATOM   2474  O   ARG A 340      37.218  65.260   3.952  1.00 53.09           O  
ANISOU 2474  O   ARG A 340     7279   6645   6247    229    678    -12       O  
ATOM   2475  CB  ARG A 340      34.756  63.294   3.693  1.00 37.82           C  
ANISOU 2475  CB  ARG A 340     5418   4685   4266    281    403   -163       C  
ATOM   2476  CG  ARG A 340      34.473  61.815   3.645  1.00 31.70           C  
ANISOU 2476  CG  ARG A 340     4652   3893   3500    301    333   -258       C  
ATOM   2477  CD  ARG A 340      33.284  61.500   2.765  1.00 43.46           C  
ANISOU 2477  CD  ARG A 340     6236   5379   4897    323    204   -291       C  
ATOM   2478  NE  ARG A 340      32.022  61.905   3.361  1.00 44.03           N  
ANISOU 2478  NE  ARG A 340     6253   5437   5039    289     90   -253       N  
ATOM   2479  CZ  ARG A 340      30.846  61.792   2.754  1.00 53.42           C  
ANISOU 2479  CZ  ARG A 340     7494   6625   6179    297    -41   -263       C  
ATOM   2480  NH1 ARG A 340      30.778  61.291   1.524  1.00 57.99           N1+
ANISOU 2480  NH1 ARG A 340     8198   7211   6625    334    -84   -317       N1+
ATOM   2481  NH2 ARG A 340      29.739  62.190   3.371  1.00 45.81           N  
ANISOU 2481  NH2 ARG A 340     6455   5655   5293    272   -130   -218       N  
ATOM   2482  N   GLN A 341      35.704  66.067   5.388  1.00 40.52           N  
ANISOU 2482  N   GLN A 341     5629   4995   4773    185    527     16       N  
ATOM   2483  CA  GLN A 341      36.258  67.423   5.352  1.00 42.38           C  
ANISOU 2483  CA  GLN A 341     5875   5215   5012    154    594    102       C  
ATOM   2484  C   GLN A 341      37.417  67.644   6.322  1.00 44.26           C  
ANISOU 2484  C   GLN A 341     6016   5436   5365    102    663    120       C  
ATOM   2485  O   GLN A 341      37.848  68.774   6.503  1.00 48.88           O  
ANISOU 2485  O   GLN A 341     6599   5992   5980     61    699    189       O  
ATOM   2486  CB  GLN A 341      35.174  68.454   5.653  1.00 32.87           C  
ANISOU 2486  CB  GLN A 341     4698   3974   3818    153    514    146       C  
ATOM   2487  CG  GLN A 341      33.918  68.284   4.851  1.00 33.86           C  
ANISOU 2487  CG  GLN A 341     4897   4115   3852    201    421    135       C  
ATOM   2488  CD  GLN A 341      33.217  69.607   4.649  1.00 43.97           C  
ANISOU 2488  CD  GLN A 341     6233   5366   5108    212    384    210       C  
ATOM   2489  NE2 GLN A 341      31.957  69.572   4.212  1.00 36.55           N  
ANISOU 2489  NE2 GLN A 341     5332   4435   4120    255    281    207       N  
ATOM   2490  OE1 GLN A 341      33.809  70.657   4.882  1.00 53.53           O  
ANISOU 2490  OE1 GLN A 341     7451   6541   6349    183    442    272       O  
ATOM   2491  N   HIS A 342      37.918  66.585   6.953  1.00 38.38           N  
ANISOU 2491  N   HIS A 342     5194   4702   4687    101    671     61       N  
ATOM   2492  CA  HIS A 342      38.870  66.760   8.051  1.00 35.83           C  
ANISOU 2492  CA  HIS A 342     4772   4359   4483     52    704     75       C  
ATOM   2493  C   HIS A 342      40.132  67.517   7.604  1.00 30.37           C  
ANISOU 2493  C   HIS A 342     4061   3678   3799     14    814    145       C  
ATOM   2494  O   HIS A 342      40.479  68.531   8.196  1.00 51.39           O  
ANISOU 2494  O   HIS A 342     6697   6301   6529    -43    813    199       O  
ATOM   2495  CB  HIS A 342      39.261  65.415   8.711  1.00 29.96           C  
ANISOU 2495  CB  HIS A 342     3951   3627   3806     65    694      6       C  
ATOM   2496  CG  HIS A 342      40.229  65.559   9.852  1.00 34.78           C  
ANISOU 2496  CG  HIS A 342     4459   4221   4534     18    712     21       C  
ATOM   2497  CD2 HIS A 342      41.497  65.107  10.008  1.00 30.56           C  
ANISOU 2497  CD2 HIS A 342     3843   3707   4061      8    778     21       C  
ATOM   2498  ND1 HIS A 342      39.932  66.262  11.005  1.00 41.28           N  
ANISOU 2498  ND1 HIS A 342     5258   5001   5424    -22    650     39       N  
ATOM   2499  CE1 HIS A 342      40.965  66.207  11.829  1.00 42.06           C  
ANISOU 2499  CE1 HIS A 342     5272   5093   5616    -59    666     45       C  
ATOM   2500  NE2 HIS A 342      41.933  65.521  11.246  1.00 36.10           N  
ANISOU 2500  NE2 HIS A 342     4472   4378   4866    -44    743     39       N  
ATOM   2501  N   GLN A 343      40.844  67.061   6.588  1.00 44.78           N  
ANISOU 2501  N   GLN A 343     5899   5554   5560     44    910    149       N  
ATOM   2502  CA  GLN A 343      42.042  67.808   6.165  1.00 49.27           C  
ANISOU 2502  CA  GLN A 343     6433   6142   6145      3   1027    233       C  
ATOM   2503  C   GLN A 343      41.772  69.186   5.557  1.00 56.04           C  
ANISOU 2503  C   GLN A 343     7372   6974   6948    -30   1042    326       C  
ATOM   2504  O   GLN A 343      42.641  70.067   5.581  1.00 69.13           O  
ANISOU 2504  O   GLN A 343     8988   8618   8661    -94   1107    411       O  
ATOM   2505  CB  GLN A 343      42.888  66.927   5.258  1.00 68.86           C  
ANISOU 2505  CB  GLN A 343     8903   8693   8569     57   1142    216       C  
ATOM   2506  CG  GLN A 343      44.290  67.415   5.135  1.00 95.68           C  
ANISOU 2506  CG  GLN A 343    12208  12120  12028     13   1268    299       C  
ATOM   2507  CD  GLN A 343      45.034  66.610   4.142  1.00 98.77           C  
ANISOU 2507  CD  GLN A 343    12597  12588  12343     86   1398    287       C  
ATOM   2508  NE2 GLN A 343      45.697  67.302   3.199  1.00101.83           N  
ANISOU 2508  NE2 GLN A 343    12998  13020  12672     77   1529    383       N  
ATOM   2509  OE1 GLN A 343      44.893  65.393   4.111  1.00109.41           O  
ANISOU 2509  OE1 GLN A 343    13953  13952  13665    159   1381    192       O  
ATOM   2510  N   HIS A 344      40.541  69.425   5.126  1.00 53.36           N  
ANISOU 2510  N   HIS A 344     7139   6619   6517      7    966    315       N  
ATOM   2511  CA  HIS A 344      40.175  70.784   4.752  1.00 48.16           C  
ANISOU 2511  CA  HIS A 344     6557   5918   5824    -21    957    403       C  
ATOM   2512  C   HIS A 344      40.281  71.667   5.972  1.00 48.13           C  
ANISOU 2512  C   HIS A 344     6500   5837   5950    -90    904    429       C  
ATOM   2513  O   HIS A 344      40.992  72.672   5.964  1.00 52.24           O  
ANISOU 2513  O   HIS A 344     7011   6319   6517   -155    951    513       O  
ATOM   2514  CB  HIS A 344      38.770  70.856   4.185  1.00 33.13           C  
ANISOU 2514  CB  HIS A 344     4765   4010   3814     37    867    385       C  
ATOM   2515  CG  HIS A 344      38.211  72.240   4.152  1.00 52.64           C  
ANISOU 2515  CG  HIS A 344     7304   6418   6281     17    825    463       C  
ATOM   2516  CD2 HIS A 344      37.194  72.801   4.848  1.00 53.80           C  
ANISOU 2516  CD2 HIS A 344     7468   6506   6469     26    719    455       C  
ATOM   2517  ND1 HIS A 344      38.704  73.233   3.332  1.00 68.15           N  
ANISOU 2517  ND1 HIS A 344     9329   8370   8194    -11    899    569       N  
ATOM   2518  CE1 HIS A 344      38.007  74.342   3.515  1.00 64.96           C  
ANISOU 2518  CE1 HIS A 344     8984   7893   7803    -18    830    619       C  
ATOM   2519  NE2 HIS A 344      37.091  74.109   4.438  1.00 57.52           N  
ANISOU 2519  NE2 HIS A 344     8015   6923   6916      9    723    548       N  
ATOM   2520  N   LEU A 345      39.579  71.269   7.030  1.00 40.95           N  
ANISOU 2520  N   LEU A 345     5559   4902   5099    -75    806    356       N  
ATOM   2521  CA  LEU A 345      39.638  71.985   8.290  1.00 31.02           C  
ANISOU 2521  CA  LEU A 345     4263   3573   3951   -125    749    361       C  
ATOM   2522  C   LEU A 345      41.045  72.090   8.846  1.00 43.42           C  
ANISOU 2522  C   LEU A 345     5736   5134   5627   -200    802    387       C  
ATOM   2523  O   LEU A 345      41.387  73.102   9.423  1.00 38.39           O  
ANISOU 2523  O   LEU A 345     5097   4428   5063   -262    778    429       O  
ATOM   2524  CB  LEU A 345      38.757  71.317   9.317  1.00 41.68           C  
ANISOU 2524  CB  LEU A 345     5586   4918   5333    -87    657    279       C  
ATOM   2525  CG  LEU A 345      37.282  71.349   8.989  1.00 45.86           C  
ANISOU 2525  CG  LEU A 345     6188   5449   5789    -22    586    263       C  
ATOM   2526  CD1 LEU A 345      36.523  70.403   9.930  1.00 35.04           C  
ANISOU 2526  CD1 LEU A 345     4765   4094   4455     11    516    189       C  
ATOM   2527  CD2 LEU A 345      36.817  72.795   9.098  1.00 40.33           C  
ANISOU 2527  CD2 LEU A 345     5558   4676   5090    -28    553    321       C  
ATOM   2528  N   MET A 346      41.858  71.046   8.712  1.00 42.47           N  
ANISOU 2528  N   MET A 346     5534   5078   5525   -192    864    358       N  
ATOM   2529  CA  MET A 346      43.189  71.134   9.283  1.00 42.16           C  
ANISOU 2529  CA  MET A 346     5384   5035   5600   -262    905    388       C  
ATOM   2530  C   MET A 346      44.056  72.044   8.447  1.00 51.48           C  
ANISOU 2530  C   MET A 346     6561   6214   6783   -321   1000    496       C  
ATOM   2531  O   MET A 346      45.025  72.606   8.945  1.00 61.68           O  
ANISOU 2531  O   MET A 346     7775   7475   8186   -405   1011    547       O  
ATOM   2532  CB  MET A 346      43.835  69.764   9.404  1.00 48.86           C  
ANISOU 2532  CB  MET A 346     6138   5951   6477   -227    945    332       C  
ATOM   2533  CG  MET A 346      43.010  68.781  10.211  1.00 53.61           C  
ANISOU 2533  CG  MET A 346     6739   6551   7081   -175    855    236       C  
ATOM   2534  SD  MET A 346      42.327  69.446  11.745  1.00 54.99           S  
ANISOU 2534  SD  MET A 346     6926   6646   7322   -210    725    214       S  
ATOM   2535  CE  MET A 346      43.727  69.224  12.837  1.00 78.76           C  
ANISOU 2535  CE  MET A 346     9804   9650  10470   -272    719    215       C  
ATOM   2536  N   GLN A 347      43.724  72.205   7.174  1.00 47.29           N  
ANISOU 2536  N   GLN A 347     6117   5718   6133   -281   1066    538       N  
ATOM   2537  CA  GLN A 347      44.552  73.076   6.353  1.00 46.08           C  
ANISOU 2537  CA  GLN A 347     5964   5568   5977   -339   1170    657       C  
ATOM   2538  C   GLN A 347      44.218  74.519   6.670  1.00 52.59           C  
ANISOU 2538  C   GLN A 347     6854   6286   6842   -407   1102    723       C  
ATOM   2539  O   GLN A 347      45.104  75.342   6.892  1.00 48.99           O  
ANISOU 2539  O   GLN A 347     6346   5784   6486   -504   1126    805       O  
ATOM   2540  CB  GLN A 347      44.341  72.794   4.884  1.00 44.07           C  
ANISOU 2540  CB  GLN A 347     5793   5386   5565   -269   1266    685       C  
ATOM   2541  CG  GLN A 347      45.039  71.540   4.422  1.00 50.81           C  
ANISOU 2541  CG  GLN A 347     6579   6339   6386   -210   1367    642       C  
ATOM   2542  CD  GLN A 347      44.704  71.222   2.997  1.00 58.17           C  
ANISOU 2542  CD  GLN A 347     7624   7339   7139   -127   1446    651       C  
ATOM   2543  NE2 GLN A 347      45.185  70.087   2.515  1.00 70.41           N  
ANISOU 2543  NE2 GLN A 347     9145   8970   8638    -54   1530    598       N  
ATOM   2544  OE1 GLN A 347      44.014  71.989   2.329  1.00 63.23           O  
ANISOU 2544  OE1 GLN A 347     8386   7956   7683   -122   1427    704       O  
ATOM   2545  N   ALA A 348      42.922  74.814   6.694  1.00 49.81           N  
ANISOU 2545  N   ALA A 348     6616   5890   6418   -355   1013    687       N  
ATOM   2546  CA  ALA A 348      42.459  76.156   6.990  1.00 42.30           C  
ANISOU 2546  CA  ALA A 348     5746   4830   5497   -395    941    738       C  
ATOM   2547  C   ALA A 348      42.981  76.563   8.353  1.00 45.37           C  
ANISOU 2547  C   ALA A 348     6066   5140   6032   -471    870    716       C  
ATOM   2548  O   ALA A 348      43.531  77.651   8.503  1.00 45.27           O  
ANISOU 2548  O   ALA A 348     6063   5043   6095   -559    862    792       O  
ATOM   2549  CB  ALA A 348      40.947  76.236   6.948  1.00 40.61           C  
ANISOU 2549  CB  ALA A 348     5641   4593   5196   -308    851    689       C  
ATOM   2550  N   TRP A 349      42.847  75.674   9.336  1.00 34.66           N  
ANISOU 2550  N   TRP A 349     4646   3809   4716   -442    814    615       N  
ATOM   2551  CA  TRP A 349      43.270  76.006  10.690  1.00 39.93           C  
ANISOU 2551  CA  TRP A 349     5263   4405   5502   -503    732    583       C  
ATOM   2552  C   TRP A 349      44.787  76.138  10.777  1.00 45.72           C  
ANISOU 2552  C   TRP A 349     5880   5143   6350   -607    783    645       C  
ATOM   2553  O   TRP A 349      45.308  76.966  11.546  1.00 43.52           O  
ANISOU 2553  O   TRP A 349     5587   4773   6174   -695    717    667       O  
ATOM   2554  CB  TRP A 349      42.738  74.983  11.699  1.00 37.03           C  
ANISOU 2554  CB  TRP A 349     4861   4071   5138   -441    665    470       C  
ATOM   2555  CG  TRP A 349      41.231  74.954  11.720  1.00 32.60           C  
ANISOU 2555  CG  TRP A 349     4397   3503   4488   -348    609    421       C  
ATOM   2556  CD1 TRP A 349      40.394  75.867  11.136  1.00 35.92           C  
ANISOU 2556  CD1 TRP A 349     4928   3874   4847   -319    593    462       C  
ATOM   2557  CD2 TRP A 349      40.379  73.947  12.294  1.00 30.23           C  
ANISOU 2557  CD2 TRP A 349     4080   3247   4157   -272    564    335       C  
ATOM   2558  CE2 TRP A 349      39.044  74.330  12.041  1.00 33.59           C  
ANISOU 2558  CE2 TRP A 349     4598   3655   4509   -203    523    329       C  
ATOM   2559  CE3 TRP A 349      40.619  72.766  12.996  1.00 29.50           C  
ANISOU 2559  CE3 TRP A 349     3902   3208   4098   -258    553    270       C  
ATOM   2560  NE1 TRP A 349      39.076  75.505  11.339  1.00 40.00           N  
ANISOU 2560  NE1 TRP A 349     5488   4408   5301   -228    539    404       N  
ATOM   2561  CZ2 TRP A 349      37.961  73.582  12.462  1.00 33.18           C  
ANISOU 2561  CZ2 TRP A 349     4543   3640   4424   -128    477    266       C  
ATOM   2562  CZ3 TRP A 349      39.535  72.029  13.433  1.00 28.59           C  
ANISOU 2562  CZ3 TRP A 349     3798   3120   3944   -186    506    208       C  
ATOM   2563  CH2 TRP A 349      38.224  72.437  13.168  1.00 34.52           C  
ANISOU 2563  CH2 TRP A 349     4629   3858   4629   -126    471    208       C  
ATOM   2564  N   ALA A 350      45.496  75.375   9.952  1.00 48.42           N  
ANISOU 2564  N   ALA A 350     6140   5584   6672   -598    899    676       N  
ATOM   2565  CA  ALA A 350      46.950  75.511   9.896  1.00 46.77           C  
ANISOU 2565  CA  ALA A 350     5801   5394   6575   -692    967    754       C  
ATOM   2566  C   ALA A 350      47.326  76.943   9.517  1.00 55.10           C  
ANISOU 2566  C   ALA A 350     6896   6362   7676   -794    978    874       C  
ATOM   2567  O   ALA A 350      48.300  77.484  10.025  1.00 71.56           O  
ANISOU 2567  O   ALA A 350     8895   8398   9897   -905    954    927       O  
ATOM   2568  CB  ALA A 350      47.549  74.519   8.910  1.00 36.64           C  
ANISOU 2568  CB  ALA A 350     4441   4239   5243   -642   1111    774       C  
ATOM   2569  N   ILE A 351      46.534  77.562   8.644  1.00 52.04           N  
ANISOU 2569  N   ILE A 351     6642   5949   7182   -760   1002    919       N  
ATOM   2570  CA  ILE A 351      46.864  78.885   8.120  1.00 52.25           C  
ANISOU 2570  CA  ILE A 351     6719   5892   7242   -852   1025   1048       C  
ATOM   2571  C   ILE A 351      46.429  79.959   9.084  1.00 51.12           C  
ANISOU 2571  C   ILE A 351     6660   5594   7169   -902    879   1027       C  
ATOM   2572  O   ILE A 351      47.132  80.948   9.296  1.00 48.46           O  
ANISOU 2572  O   ILE A 351     6310   5160   6944  -1022    851   1108       O  
ATOM   2573  CB  ILE A 351      46.205  79.126   6.765  1.00 53.16           C  
ANISOU 2573  CB  ILE A 351     6954   6040   7205   -788   1106   1113       C  
ATOM   2574  CG1 ILE A 351      46.710  78.085   5.759  1.00 49.22           C  
ANISOU 2574  CG1 ILE A 351     6386   5693   6623   -733   1259   1132       C  
ATOM   2575  CG2 ILE A 351      46.444  80.591   6.287  1.00 43.40           C  
ANISOU 2575  CG2 ILE A 351     5789   4696   6004   -884   1117   1256       C  
ATOM   2576  CD1 ILE A 351      45.746  77.857   4.604  1.00 48.07           C  
ANISOU 2576  CD1 ILE A 351     6376   5602   6288   -624   1302   1131       C  
ATOM   2577  N   VAL A 352      45.256  79.741   9.665  1.00 56.30           N  
ANISOU 2577  N   VAL A 352     7405   6226   7760   -807    786    918       N  
ATOM   2578  CA  VAL A 352      44.736  80.587  10.725  1.00 60.29           C  
ANISOU 2578  CA  VAL A 352     7996   6595   8314   -821    647    868       C  
ATOM   2579  C   VAL A 352      45.749  80.777  11.864  1.00 58.88           C  
ANISOU 2579  C   VAL A 352     7729   6356   8285   -928    572    849       C  
ATOM   2580  O   VAL A 352      45.992  81.891  12.305  1.00 54.96           O  
ANISOU 2580  O   VAL A 352     7289   5725   7870  -1012    492    881       O  
ATOM   2581  CB  VAL A 352      43.425  80.001  11.283  1.00 54.29           C  
ANISOU 2581  CB  VAL A 352     7301   5860   7468   -691    580    745       C  
ATOM   2582  CG1 VAL A 352      42.952  80.804  12.487  1.00 50.64           C  
ANISOU 2582  CG1 VAL A 352     6922   5267   7051   -691    448    684       C  
ATOM   2583  CG2 VAL A 352      42.358  79.975  10.197  1.00 40.37           C  
ANISOU 2583  CG2 VAL A 352     5632   4137   5569   -594    624    768       C  
ATOM   2584  N   ARG A 353      46.365  79.694  12.318  1.00 62.19           N  
ANISOU 2584  N   ARG A 353     8014   6872   8744   -927    590    798       N  
ATOM   2585  CA  ARG A 353      47.293  79.791  13.439  1.00 59.04           C  
ANISOU 2585  CA  ARG A 353     7528   6424   8481  -1021    502    775       C  
ATOM   2586  C   ARG A 353      48.654  80.347  13.042  1.00 64.21           C  
ANISOU 2586  C   ARG A 353     8073   7058   9265  -1166    546    899       C  
ATOM   2587  O   ARG A 353      49.284  81.039  13.839  1.00 69.51           O  
ANISOU 2587  O   ARG A 353     8726   7627  10059  -1274    441    909       O  
ATOM   2588  CB  ARG A 353      47.457  78.426  14.104  1.00 59.35           C  
ANISOU 2588  CB  ARG A 353     7461   6569   8520   -963    496    682       C  
ATOM   2589  CG  ARG A 353      46.155  77.896  14.713  1.00 57.30           C  
ANISOU 2589  CG  ARG A 353     7295   6320   8155   -837    437    565       C  
ATOM   2590  CD  ARG A 353      46.292  77.737  16.196  1.00 58.62           C  
ANISOU 2590  CD  ARG A 353     7450   6447   8377   -847    314    479       C  
ATOM   2591  NE  ARG A 353      45.032  77.931  16.903  1.00 66.30           N  
ANISOU 2591  NE  ARG A 353     8555   7371   9266   -756    238    394       N  
ATOM   2592  CZ  ARG A 353      44.166  76.961  17.165  1.00 65.96           C  
ANISOU 2592  CZ  ARG A 353     8517   7405   9141   -647    248    323       C  
ATOM   2593  NH1 ARG A 353      44.419  75.718  16.760  1.00 73.31           N1+
ANISOU 2593  NH1 ARG A 353     9343   8453  10060   -617    321    318       N1+
ATOM   2594  NH2 ARG A 353      43.049  77.237  17.827  1.00 58.62           N  
ANISOU 2594  NH2 ARG A 353     7696   6431   8145   -568    187    259       N  
ATOM   2595  N   LYS A 354      49.107  80.055  11.821  1.00 60.53           N  
ANISOU 2595  N   LYS A 354     7538   6689   8773  -1169    699    995       N  
ATOM   2596  CA  LYS A 354      50.362  80.626  11.309  1.00 55.15           C  
ANISOU 2596  CA  LYS A 354     6745   5999   8212  -1306    768   1138       C  
ATOM   2597  C   LYS A 354      50.292  82.155  11.179  1.00 56.40           C  
ANISOU 2597  C   LYS A 354     7014   5995   8420  -1409    708   1227       C  
ATOM   2598  O   LYS A 354      51.280  82.849  11.409  1.00 55.65           O  
ANISOU 2598  O   LYS A 354     6841   5827   8476  -1556    673   1313       O  
ATOM   2599  CB  LYS A 354      50.726  80.010   9.953  1.00 45.76           C  
ANISOU 2599  CB  LYS A 354     5482   4953   6952  -1263    963   1224       C  
ATOM   2600  CG  LYS A 354      51.244  78.554  10.034  1.00 56.46           C  
ANISOU 2600  CG  LYS A 354     6687   6459   8308  -1193   1035   1164       C  
ATOM   2601  CD  LYS A 354      51.792  78.041   8.692  1.00 65.73           C  
ANISOU 2601  CD  LYS A 354     7785   7768   9421  -1156   1237   1257       C  
ATOM   2602  CE  LYS A 354      52.502  76.695   8.808  1.00 71.65           C  
ANISOU 2602  CE  LYS A 354     8373   8650  10200  -1095   1309   1209       C  
ATOM   2603  NZ  LYS A 354      53.152  76.281   7.507  1.00 80.99           N1+
ANISOU 2603  NZ  LYS A 354     9481   9963  11330  -1056   1518   1304       N1+
ATOM   2604  N   ALA A 355      49.114  82.661  10.820  1.00 48.49           N  
ANISOU 2604  N   ALA A 355     6192   4933   7298  -1330    690   1208       N  
ATOM   2605  CA  ALA A 355      48.878  84.077  10.666  1.00 51.00           C  
ANISOU 2605  CA  ALA A 355     6643   5088   7647  -1401    630   1284       C  
ATOM   2606  C   ALA A 355      48.536  84.740  11.995  1.00 59.70           C  
ANISOU 2606  C   ALA A 355     7839   6031   8812  -1424    441   1185       C  
ATOM   2607  O   ALA A 355      48.376  85.962  12.063  1.00 68.18           O  
ANISOU 2607  O   ALA A 355     9034   6941   9929  -1485    364   1230       O  
ATOM   2608  CB  ALA A 355      47.757  84.316   9.654  1.00 51.76           C  
ANISOU 2608  CB  ALA A 355     6890   5192   7583  -1293    691   1312       C  
ATOM   2609  N   GLY A 356      48.424  83.933  13.048  1.00 62.70           N  
ANISOU 2609  N   GLY A 356     8175   6456   9192  -1369    368   1051       N  
ATOM   2610  CA  GLY A 356      48.089  84.431  14.376  1.00 64.02           C  
ANISOU 2610  CA  GLY A 356     8437   6491   9395  -1371    196    942       C  
ATOM   2611  C   GLY A 356      46.714  85.082  14.461  1.00 63.71           C  
ANISOU 2611  C   GLY A 356     8602   6356   9248  -1260    141    884       C  
ATOM   2612  O   GLY A 356      46.531  86.107  15.115  1.00 63.98           O  
ANISOU 2612  O   GLY A 356     8761   6224   9326  -1292     18    857       O  
ATOM   2613  N   TYR A 357      45.739  84.484  13.792  1.00 65.32           N  
ANISOU 2613  N   TYR A 357     8841   6663   9315  -1125    228    865       N  
ATOM   2614  CA  TYR A 357      44.375  84.988  13.830  1.00 58.73           C  
ANISOU 2614  CA  TYR A 357     8175   5761   8379  -1003    185    815       C  
ATOM   2615  C   TYR A 357      43.644  84.493  15.065  1.00 55.34           C  
ANISOU 2615  C   TYR A 357     7780   5341   7906   -900     99    665       C  
ATOM   2616  O   TYR A 357      42.791  85.194  15.607  1.00 57.17           O  
ANISOU 2616  O   TYR A 357     8153   5466   8103   -828     19    607       O  
ATOM   2617  CB  TYR A 357      43.620  84.579  12.572  1.00 52.94           C  
ANISOU 2617  CB  TYR A 357     7460   5133   7522   -908    300    865       C  
ATOM   2618  CG  TYR A 357      44.014  85.382  11.364  1.00 53.28           C  
ANISOU 2618  CG  TYR A 357     7536   5133   7577   -982    372   1017       C  
ATOM   2619  CD1 TYR A 357      44.649  86.599  11.504  1.00 47.87           C  
ANISOU 2619  CD1 TYR A 357     6900   4286   7003  -1108    313   1095       C  
ATOM   2620  CD2 TYR A 357      43.754  84.914  10.079  1.00 51.42           C  
ANISOU 2620  CD2 TYR A 357     7287   5015   7235   -929    494   1087       C  
ATOM   2621  CE1 TYR A 357      45.018  87.330  10.401  1.00 67.64           C  
ANISOU 2621  CE1 TYR A 357     9432   6749   9519  -1182    385   1250       C  
ATOM   2622  CE2 TYR A 357      44.118  85.634   8.974  1.00 55.31           C  
ANISOU 2622  CE2 TYR A 357     7815   5475   7724   -993    568   1235       C  
ATOM   2623  CZ  TYR A 357      44.746  86.841   9.134  1.00 72.74           C  
ANISOU 2623  CZ  TYR A 357    10064   7524  10048  -1121    518   1323       C  
ATOM   2624  OH  TYR A 357      45.103  87.563   8.018  1.00 82.70           O  
ANISOU 2624  OH  TYR A 357    11363   8752  11306  -1189    598   1486       O  
ATOM   2625  N   VAL A 358      43.952  83.271  15.495  1.00 50.27           N  
ANISOU 2625  N   VAL A 358     7012   4830   7259   -881    124    605       N  
ATOM   2626  CA  VAL A 358      43.519  82.821  16.816  1.00 51.30           C  
ANISOU 2626  CA  VAL A 358     7162   4963   7366   -812     37    476       C  
ATOM   2627  C   VAL A 358      44.659  82.085  17.513  1.00 55.79           C  
ANISOU 2627  C   VAL A 358     7590   5587   8020   -894     10    452       C  
ATOM   2628  O   VAL A 358      45.457  81.409  16.871  1.00 57.04           O  
ANISOU 2628  O   VAL A 358     7608   5845   8217   -947     95    512       O  
ATOM   2629  CB  VAL A 358      42.214  81.941  16.763  1.00 53.23           C  
ANISOU 2629  CB  VAL A 358     7424   5318   7484   -651     83    409       C  
ATOM   2630  CG1 VAL A 358      41.443  82.161  15.466  1.00 51.13           C  
ANISOU 2630  CG1 VAL A 358     7209   5077   7142   -592    162    478       C  
ATOM   2631  CG2 VAL A 358      42.501  80.464  17.002  1.00 54.79           C  
ANISOU 2631  CG2 VAL A 358     7483   5664   7671   -630    127    366       C  
ATOM   2632  N   PRO A 359      44.769  82.269  18.836  1.00 66.67           N  
ANISOU 2632  N   PRO A 359     9011   6894   9425   -901   -113    365       N  
ATOM   2633  CA  PRO A 359      45.842  81.676  19.639  1.00 69.99           C  
ANISOU 2633  CA  PRO A 359     9313   7351   9930   -979   -169    338       C  
ATOM   2634  C   PRO A 359      45.614  80.203  19.877  1.00 60.29           C  
ANISOU 2634  C   PRO A 359     7986   6280   8643   -892   -115    285       C  
ATOM   2635  O   PRO A 359      44.574  79.690  19.475  1.00 65.74           O  
ANISOU 2635  O   PRO A 359     8707   7040   9229   -777    -43    264       O  
ATOM   2636  CB  PRO A 359      45.764  82.452  20.956  1.00 79.15           C  
ANISOU 2636  CB  PRO A 359    10600   8372  11100   -989   -328    252       C  
ATOM   2637  CG  PRO A 359      44.331  82.854  21.054  1.00 78.43           C  
ANISOU 2637  CG  PRO A 359    10672   8240  10889   -848   -323    195       C  
ATOM   2638  CD  PRO A 359      43.897  83.144  19.643  1.00 73.34           C  
ANISOU 2638  CD  PRO A 359    10034   7612  10221   -832   -211    288       C  
ATOM   2639  N   GLU A 360      46.566  79.550  20.540  1.00 64.55           N  
ANISOU 2639  N   GLU A 360     8409   6864   9253   -948   -159    268       N  
ATOM   2640  CA  GLU A 360      46.510  78.112  20.810  1.00 60.03           C  
ANISOU 2640  CA  GLU A 360     7736   6429   8643   -876   -117    226       C  
ATOM   2641  C   GLU A 360      45.516  77.757  21.908  1.00 52.18           C  
ANISOU 2641  C   GLU A 360     6838   5438   7549   -764   -178    121       C  
ATOM   2642  O   GLU A 360      44.710  76.843  21.764  1.00 54.16           O  
ANISOU 2642  O   GLU A 360     7076   5782   7718   -662   -110     94       O  
ATOM   2643  CB  GLU A 360      47.898  77.607  21.171  1.00 66.54           C  
ANISOU 2643  CB  GLU A 360     8403   7293   9587   -971   -152    251       C  
ATOM   2644  CG  GLU A 360      48.878  77.680  20.012  1.00 73.42           C  
ANISOU 2644  CG  GLU A 360     9142   8202  10553  -1062    -54    364       C  
ATOM   2645  CD  GLU A 360      48.407  76.895  18.804  1.00 80.64           C  
ANISOU 2645  CD  GLU A 360    10018   9232  11391   -979    106    396       C  
ATOM   2646  OE1 GLU A 360      47.587  75.958  18.967  1.00 89.40           O  
ANISOU 2646  OE1 GLU A 360    11150  10412  12405   -865    132    329       O  
ATOM   2647  OE2 GLU A 360      48.868  77.213  17.688  1.00 77.46           O1-
ANISOU 2647  OE2 GLU A 360     9564   8845  11020  -1030    204    490       O1-
ATOM   2648  N   SER A 361      45.567  78.478  23.015  1.00 51.01           N  
ANISOU 2648  N   SER A 361     6790   5187   7406   -783   -306     65       N  
ATOM   2649  CA  SER A 361      44.402  78.512  23.877  1.00 51.89           C  
ANISOU 2649  CA  SER A 361     7035   5281   7402   -662   -342    -22       C  
ATOM   2650  C   SER A 361      43.316  78.992  22.957  1.00 58.82           C  
ANISOU 2650  C   SER A 361     7989   6144   8214   -590   -258      4       C  
ATOM   2651  O   SER A 361      43.581  79.793  22.065  1.00 72.03           O  
ANISOU 2651  O   SER A 361     9678   7756   9936   -654   -234     70       O  
ATOM   2652  CB  SER A 361      44.587  79.443  25.059  1.00 50.24           C  
ANISOU 2652  CB  SER A 361     6955   4942   7194   -687   -488    -88       C  
ATOM   2653  OG  SER A 361      44.699  80.792  24.628  1.00 48.86           O  
ANISOU 2653  OG  SER A 361     6874   4626   7065   -751   -526    -58       O  
ATOM   2654  N   VAL A 362      42.108  78.507  23.172  1.00 63.43           N  
ANISOU 2654  N   VAL A 362     8618   6788   8694   -460   -216    -40       N  
ATOM   2655  CA  VAL A 362      41.059  78.478  22.143  1.00 58.55           C  
ANISOU 2655  CA  VAL A 362     8017   6211   8017   -382   -119     -6       C  
ATOM   2656  C   VAL A 362      41.340  77.359  21.162  1.00 52.64           C  
ANISOU 2656  C   VAL A 362     7129   5588   7285   -399    -23     45       C  
ATOM   2657  O   VAL A 362      42.054  77.514  20.168  1.00 47.28           O  
ANISOU 2657  O   VAL A 362     6393   4911   6659   -476     24    114       O  
ATOM   2658  CB  VAL A 362      40.887  79.774  21.383  1.00 39.93           C  
ANISOU 2658  CB  VAL A 362     5755   3744   5673   -405   -120     41       C  
ATOM   2659  CG1 VAL A 362      39.789  79.592  20.346  1.00 35.27           C  
ANISOU 2659  CG1 VAL A 362     5172   3215   5015   -316    -30     77       C  
ATOM   2660  CG2 VAL A 362      40.531  80.861  22.361  1.00 39.24           C  
ANISOU 2660  CG2 VAL A 362     5823   3523   5564   -369   -217    -20       C  
ATOM   2661  N   PRO A 363      40.789  76.200  21.491  1.00 52.68           N  
ANISOU 2661  N   PRO A 363     7082   5694   7240   -325      6      9       N  
ATOM   2662  CA  PRO A 363      40.887  74.903  20.831  1.00 57.56           C  
ANISOU 2662  CA  PRO A 363     7582   6429   7858   -316     82     30       C  
ATOM   2663  C   PRO A 363      40.654  74.886  19.314  1.00 66.23           C  
ANISOU 2663  C   PRO A 363     8663   7563   8939   -313    169     88       C  
ATOM   2664  O   PRO A 363      41.566  74.377  18.637  1.00 86.87           O  
ANISOU 2664  O   PRO A 363    11185  10224  11598   -370    220    126       O  
ATOM   2665  CB  PRO A 363      39.813  74.095  21.541  1.00 46.86           C  
ANISOU 2665  CB  PRO A 363     6238   5135   6433   -214     81    -20       C  
ATOM   2666  CG  PRO A 363      39.810  74.635  22.907  1.00 48.39           C  
ANISOU 2666  CG  PRO A 363     6507   5265   6613   -200     -2    -71       C  
ATOM   2667  CD  PRO A 363      40.176  76.087  22.827  1.00 41.81           C  
ANISOU 2667  CD  PRO A 363     5768   4309   5808   -251    -51    -62       C  
ATOM   2668  N   LEU A 364      39.520  75.369  18.793  1.00 34.21           N  
ANISOU 2668  N   LEU A 364     4688   3493   4818   -245    188     98       N  
ATOM   2669  CA  LEU A 364      39.185  75.028  17.389  1.00 35.05           C  
ANISOU 2669  CA  LEU A 364     4773   3658   4885   -226    263    144       C  
ATOM   2670  C   LEU A 364      39.220  73.510  17.131  1.00 44.28           C  
ANISOU 2670  C   LEU A 364     5844   4938   6043   -204    307    124       C  
ATOM   2671  O   LEU A 364      40.263  72.959  16.772  1.00 49.45           O  
ANISOU 2671  O   LEU A 364     6419   5629   6740   -257    346    141       O  
ATOM   2672  CB  LEU A 364      40.150  75.705  16.423  1.00 37.74           C  
ANISOU 2672  CB  LEU A 364     5109   3964   5265   -312    304    217       C  
ATOM   2673  CG  LEU A 364      39.734  76.934  15.655  1.00 39.83           C  
ANISOU 2673  CG  LEU A 364     5476   4155   5504   -311    309    274       C  
ATOM   2674  CD1 LEU A 364      38.947  77.865  16.527  1.00 40.21           C  
ANISOU 2674  CD1 LEU A 364     5631   4108   5540   -263    232    238       C  
ATOM   2675  CD2 LEU A 364      41.028  77.558  15.255  1.00 48.38           C  
ANISOU 2675  CD2 LEU A 364     6531   5190   6661   -427    332    343       C  
ATOM   2676  N   GLU A 365      38.079  72.845  17.300  1.00 47.95           N  
ANISOU 2676  N   GLU A 365     6313   5451   6456   -123    300     91       N  
ATOM   2677  CA  GLU A 365      38.033  71.386  17.404  1.00 39.64           C  
ANISOU 2677  CA  GLU A 365     5179   4480   5403   -102    316     61       C  
ATOM   2678  C   GLU A 365      37.166  70.756  16.318  1.00 37.05           C  
ANISOU 2678  C   GLU A 365     4851   4209   5018    -54    347     68       C  
ATOM   2679  O   GLU A 365      36.039  71.193  16.114  1.00 41.76           O  
ANISOU 2679  O   GLU A 365     5499   4798   5569     -1    329     76       O  
ATOM   2680  CB  GLU A 365      37.481  70.971  18.777  1.00 35.64           C  
ANISOU 2680  CB  GLU A 365     4665   3979   4896    -61    268     17       C  
ATOM   2681  CG  GLU A 365      38.289  71.439  19.977  1.00 38.39           C  
ANISOU 2681  CG  GLU A 365     5024   4277   5286   -101    219     -4       C  
ATOM   2682  CD  GLU A 365      37.604  71.118  21.318  1.00 60.71           C  
ANISOU 2682  CD  GLU A 365     7868   7115   8086    -43    179    -43       C  
ATOM   2683  OE1 GLU A 365      36.528  70.462  21.321  1.00 64.40           O  
ANISOU 2683  OE1 GLU A 365     8320   7634   8515     20    198    -45       O  
ATOM   2684  OE2 GLU A 365      38.139  71.525  22.376  1.00 64.11           O1-
ANISOU 2684  OE2 GLU A 365     8328   7502   8530    -63    127    -67       O1-
ATOM   2685  N   HIS A 366      37.664  69.728  15.638  1.00 26.49           N  
ANISOU 2685  N   HIS A 366     3459   2926   3682    -66    387     63       N  
ATOM   2686  CA  HIS A 366      36.855  69.091  14.620  1.00 34.98           C  
ANISOU 2686  CA  HIS A 366     4546   4046   4697    -22    399     59       C  
ATOM   2687  C   HIS A 366      36.192  67.914  15.271  1.00 42.68           C  
ANISOU 2687  C   HIS A 366     5475   5057   5685     10    364     19       C  
ATOM   2688  O   HIS A 366      36.841  66.909  15.595  1.00 40.24           O  
ANISOU 2688  O   HIS A 366     5107   4769   5414     -5    372     -7       O  
ATOM   2689  CB  HIS A 366      37.671  68.630  13.400  1.00 27.03           C  
ANISOU 2689  CB  HIS A 366     3529   3074   3668    -40    464     71       C  
ATOM   2690  CG  HIS A 366      36.831  68.010  12.313  1.00 36.24           C  
ANISOU 2690  CG  HIS A 366     4732   4281   4758      6    461     59       C  
ATOM   2691  CD2 HIS A 366      35.492  67.996  12.124  1.00 44.50           C  
ANISOU 2691  CD2 HIS A 366     5814   5333   5761     50    406     54       C  
ATOM   2692  ND1 HIS A 366      37.375  67.343  11.230  1.00 41.67           N  
ANISOU 2692  ND1 HIS A 366     5425   5007   5403     13    514     51       N  
ATOM   2693  CE1 HIS A 366      36.400  66.934  10.433  1.00 39.33           C  
ANISOU 2693  CE1 HIS A 366     5178   4732   5033     56    481     34       C  
ATOM   2694  NE2 HIS A 366      35.247  67.326  10.941  1.00 31.88           N  
ANISOU 2694  NE2 HIS A 366     4247   3772   4096     74    412     40       N  
ATOM   2695  N   HIS A 367      34.895  68.041  15.474  1.00 38.65           N  
ANISOU 2695  N   HIS A 367     4986   4551   5149     56    325     20       N  
ATOM   2696  CA  HIS A 367      34.148  66.949  16.039  1.00 28.39           C  
ANISOU 2696  CA  HIS A 367     3635   3285   3865     81    293     -2       C  
ATOM   2697  C   HIS A 367      33.523  66.164  14.898  1.00 28.07           C  
ANISOU 2697  C   HIS A 367     3596   3277   3790     96    279     -9       C  
ATOM   2698  O   HIS A 367      32.350  66.307  14.578  1.00 30.46           O  
ANISOU 2698  O   HIS A 367     3911   3594   4067    130    243      6       O  
ATOM   2699  CB  HIS A 367      33.117  67.483  17.012  1.00 32.67           C  
ANISOU 2699  CB  HIS A 367     4184   3821   4408    123    264      9       C  
ATOM   2700  CG  HIS A 367      33.723  68.006  18.274  1.00 37.87           C  
ANISOU 2700  CG  HIS A 367     4851   4447   5092    112    265      0       C  
ATOM   2701  CD2 HIS A 367      35.002  68.266  18.612  1.00 38.15           C  
ANISOU 2701  CD2 HIS A 367     4889   4451   5156     64    274    -10       C  
ATOM   2702  ND1 HIS A 367      32.968  68.315  19.393  1.00 48.32           N  
ANISOU 2702  ND1 HIS A 367     6182   5770   6409    158    249      1       N  
ATOM   2703  CE1 HIS A 367      33.760  68.756  20.345  1.00 47.43           C  
ANISOU 2703  CE1 HIS A 367     6093   5621   6308    140    242    -17       C  
ATOM   2704  NE2 HIS A 367      35.005  68.740  19.898  1.00 42.76           N  
ANISOU 2704  NE2 HIS A 367     5493   5008   5744     77    249    -22       N  
ATOM   2705  N   MET A 368      34.335  65.342  14.258  1.00 37.57           N  
ANISOU 2705  N   MET A 368     4790   4494   4993     76    305    -34       N  
ATOM   2706  CA  MET A 368      33.884  64.659  13.072  1.00 38.95           C  
ANISOU 2706  CA  MET A 368     4991   4690   5118     92    288    -51       C  
ATOM   2707  C   MET A 368      32.841  63.620  13.371  1.00 43.77           C  
ANISOU 2707  C   MET A 368     5563   5312   5754    103    223    -69       C  
ATOM   2708  O   MET A 368      32.759  63.063  14.470  1.00 45.81           O  
ANISOU 2708  O   MET A 368     5765   5569   6074     94    209    -71       O  
ATOM   2709  CB  MET A 368      35.061  64.009  12.357  1.00 48.16           C  
ANISOU 2709  CB  MET A 368     6163   5864   6273     82    341    -80       C  
ATOM   2710  CG  MET A 368      35.718  62.902  13.140  1.00 48.14           C  
ANISOU 2710  CG  MET A 368     6095   5857   6338     71    344   -113       C  
ATOM   2711  SD  MET A 368      37.480  62.977  12.801  1.00 55.86           S  
ANISOU 2711  SD  MET A 368     7052   6841   7330     56    436   -114       S  
ATOM   2712  CE  MET A 368      37.621  62.044  11.319  1.00 29.40           C  
ANISOU 2712  CE  MET A 368     3754   3511   3907     97    465   -157       C  
ATOM   2713  N   PHE A 369      32.037  63.381  12.355  1.00 48.51           N  
ANISOU 2713  N   PHE A 369     6199   5925   6307    120    178    -75       N  
ATOM   2714  CA  PHE A 369      31.157  62.238  12.321  1.00 36.69           C  
ANISOU 2714  CA  PHE A 369     4671   4433   4836    116    106    -95       C  
ATOM   2715  C   PHE A 369      31.245  61.533  10.976  1.00 44.07           C  
ANISOU 2715  C   PHE A 369     5669   5366   5709    122     78   -139       C  
ATOM   2716  O   PHE A 369      31.756  62.081   9.976  1.00 53.15           O  
ANISOU 2716  O   PHE A 369     6893   6524   6778    139    117   -143       O  
ATOM   2717  CB  PHE A 369      29.721  62.654  12.589  1.00 28.14           C  
ANISOU 2717  CB  PHE A 369     3554   3368   3769    132     47    -52       C  
ATOM   2718  CG  PHE A 369      29.206  63.709  11.667  1.00 32.94           C  
ANISOU 2718  CG  PHE A 369     4221   3986   4308    162     30    -25       C  
ATOM   2719  CD1 PHE A 369      28.669  63.372  10.429  1.00 37.30           C  
ANISOU 2719  CD1 PHE A 369     4820   4547   4804    168    -35    -40       C  
ATOM   2720  CD2 PHE A 369      29.229  65.057  12.050  1.00 43.99           C  
ANISOU 2720  CD2 PHE A 369     5637   5379   5697    186     70     15       C  
ATOM   2721  CE1 PHE A 369      28.175  64.359   9.580  1.00 50.23           C  
ANISOU 2721  CE1 PHE A 369     6517   6195   6373    201    -58     -7       C  
ATOM   2722  CE2 PHE A 369      28.740  66.062  11.210  1.00 45.24           C  
ANISOU 2722  CE2 PHE A 369     5854   5538   5796    219     52     48       C  
ATOM   2723  CZ  PHE A 369      28.210  65.712   9.974  1.00 56.32           C  
ANISOU 2723  CZ  PHE A 369     7299   6958   7141    227    -11     41       C  
ATOM   2724  N   GLY A 370      30.704  60.327  10.957  1.00 33.87           N  
ANISOU 2724  N   GLY A 370     4355   4060   4452    108      8   -170       N  
ATOM   2725  CA  GLY A 370      30.730  59.487   9.785  1.00 28.08           C  
ANISOU 2725  CA  GLY A 370     3694   3314   3663    116    -36   -227       C  
ATOM   2726  C   GLY A 370      29.410  59.501   9.069  1.00 29.71           C  
ANISOU 2726  C   GLY A 370     3922   3527   3839    115   -145   -219       C  
ATOM   2727  O   GLY A 370      28.457  60.151   9.487  1.00 41.53           O  
ANISOU 2727  O   GLY A 370     5367   5047   5368    113   -179   -162       O  
ATOM   2728  N   MET A 371      29.359  58.758   7.978  1.00 40.85           N  
ANISOU 2728  N   MET A 371     5414   4919   5186    123   -204   -278       N  
ATOM   2729  CA  MET A 371      28.238  58.792   7.047  1.00 47.09           C  
ANISOU 2729  CA  MET A 371     6249   5717   5926    124   -320   -279       C  
ATOM   2730  C   MET A 371      26.952  58.153   7.564  1.00 54.30           C  
ANISOU 2730  C   MET A 371     7072   6618   6943     79   -441   -255       C  
ATOM   2731  O   MET A 371      26.955  57.333   8.488  1.00 53.75           O  
ANISOU 2731  O   MET A 371     6926   6520   6975     42   -445   -254       O  
ATOM   2732  CB  MET A 371      28.666  58.108   5.756  1.00 43.85           C  
ANISOU 2732  CB  MET A 371     5969   5285   5406    150   -350   -361       C  
ATOM   2733  CG  MET A 371      29.720  58.876   5.008  1.00 48.08           C  
ANISOU 2733  CG  MET A 371     6596   5851   5822    200   -234   -366       C  
ATOM   2734  SD  MET A 371      30.305  57.919   3.621  1.00 88.78           S  
ANISOU 2734  SD  MET A 371    11907  10984  10843    246   -247   -470       S  
ATOM   2735  CE  MET A 371      31.216  56.644   4.489  1.00 97.95           C  
ANISOU 2735  CE  MET A 371    13013  12094  12111    238   -196   -528       C  
ATOM   2736  N   MET A 372      25.841  58.518   6.951  1.00 53.27           N  
ANISOU 2736  N   MET A 372     6945   6508   6788     79   -544   -228       N  
ATOM   2737  CA  MET A 372      24.595  57.862   7.293  1.00 49.90           C  
ANISOU 2737  CA  MET A 372     6423   6072   6465     29   -668   -200       C  
ATOM   2738  C   MET A 372      24.250  56.899   6.167  1.00 45.57           C  
ANISOU 2738  C   MET A 372     5962   5480   5871      7   -808   -272       C  
ATOM   2739  O   MET A 372      24.076  57.320   5.023  1.00 55.01           O  
ANISOU 2739  O   MET A 372     7259   6691   6953     39   -863   -294       O  
ATOM   2740  CB  MET A 372      23.491  58.889   7.520  1.00 56.70           C  
ANISOU 2740  CB  MET A 372     7200   6988   7357     45   -697   -112       C  
ATOM   2741  CG  MET A 372      22.268  58.331   8.193  1.00 59.98           C  
ANISOU 2741  CG  MET A 372     7472   7410   7907     -6   -786    -57       C  
ATOM   2742  SD  MET A 372      21.383  59.660   9.022  1.00 65.36           S  
ANISOU 2742  SD  MET A 372     8028   8164   8642     41   -733     54       S  
ATOM   2743  CE  MET A 372      19.733  58.944   9.049  1.00 55.21           C  
ANISOU 2743  CE  MET A 372     6597   6897   7485    -16   -891    115       C  
ATOM   2744  N   LEU A 373      24.184  55.606   6.490  1.00 50.19           N  
ANISOU 2744  N   LEU A 373     6524   6005   6541    -46   -870   -309       N  
ATOM   2745  CA  LEU A 373      23.931  54.548   5.504  1.00 52.44           C  
ANISOU 2745  CA  LEU A 373     6906   6226   6792    -72  -1014   -392       C  
ATOM   2746  C   LEU A 373      22.574  53.868   5.691  1.00 65.10           C  
ANISOU 2746  C   LEU A 373     8411   7804   8521   -154  -1182   -354       C  
ATOM   2747  O   LEU A 373      21.978  53.952   6.767  1.00 76.26           O  
ANISOU 2747  O   LEU A 373     9668   9243  10065   -194  -1162   -264       O  
ATOM   2748  CB  LEU A 373      25.034  53.490   5.559  1.00 48.49           C  
ANISOU 2748  CB  LEU A 373     6485   5655   6285    -65   -965   -479       C  
ATOM   2749  CG  LEU A 373      26.416  53.925   5.085  1.00 55.52           C  
ANISOU 2749  CG  LEU A 373     7487   6565   7045     16   -820   -532       C  
ATOM   2750  CD1 LEU A 373      26.278  55.018   4.010  1.00 62.71           C  
ANISOU 2750  CD1 LEU A 373     8484   7535   7807     67   -818   -524       C  
ATOM   2751  CD2 LEU A 373      27.277  54.376   6.219  1.00 56.70           C  
ANISOU 2751  CD2 LEU A 373     7549   6743   7252     30   -659   -483       C  
ATOM   2752  N   GLY A 374      22.099  53.200   4.639  1.00 61.80           N  
ANISOU 2752  N   GLY A 374     8085   7336   8061   -179  -1347   -421       N  
ATOM   2753  CA  GLY A 374      20.865  52.433   4.695  1.00 70.94           C  
ANISOU 2753  CA  GLY A 374     9155   8453   9344   -272  -1530   -392       C  
ATOM   2754  C   GLY A 374      21.161  51.049   5.261  1.00 73.95           C  
ANISOU 2754  C   GLY A 374     9530   8735   9834   -335  -1556   -430       C  
ATOM   2755  O   GLY A 374      22.310  50.777   5.623  1.00 64.77           O  
ANISOU 2755  O   GLY A 374     8424   7543   8642   -295  -1428   -475       O  
ATOM   2756  N   LYS A 375      20.137  50.177   5.301  1.00 81.93           N  
ANISOU 2756  N   LYS A 375    10471   9686  10971   -435  -1730   -408       N  
ATOM   2757  CA  LYS A 375      20.145  48.950   6.130  1.00 81.24           C  
ANISOU 2757  CA  LYS A 375    10324   9507  11036   -516  -1757   -395       C  
ATOM   2758  C   LYS A 375      21.385  48.066   5.911  1.00 79.72           C  
ANISOU 2758  C   LYS A 375    10295   9214  10781   -477  -1713   -517       C  
ATOM   2759  O   LYS A 375      21.840  47.409   6.857  1.00 70.68           O  
ANISOU 2759  O   LYS A 375     9102   8021   9734   -501  -1644   -494       O  
ATOM   2760  CB  LYS A 375      18.877  48.104   5.923  1.00 82.09           C  
ANISOU 2760  CB  LYS A 375    10361   9550  11279   -638  -1980   -366       C  
ATOM   2761  CG  LYS A 375      18.842  46.830   6.805  1.00 87.85           C  
ANISOU 2761  CG  LYS A 375    11026  10175  12177   -733  -2010   -336       C  
ATOM   2762  CD  LYS A 375      17.527  46.131   6.730  1.00 97.45           C  
ANISOU 2762  CD  LYS A 375    12137  11338  13551   -867  -2218   -277       C  
ATOM   2763  CE  LYS A 375      17.552  44.807   7.436  1.00 96.55           C  
ANISOU 2763  CE  LYS A 375    11992  11099  13594   -965  -2263   -255       C  
ATOM   2764  NZ  LYS A 375      18.311  43.740   6.703  1.00 91.22           N1+
ANISOU 2764  NZ  LYS A 375    11535  10266  12858   -956  -2356   -413       N1+
ATOM   2765  N   ASP A 376      21.925  48.067   4.689  1.00 86.57           N  
ANISOU 2765  N   ASP A 376    11354  10056  11484   -409  -1748   -640       N  
ATOM   2766  CA  ASP A 376      23.219  47.462   4.435  1.00 96.08           C  
ANISOU 2766  CA  ASP A 376    12710  11192  12604   -337  -1666   -753       C  
ATOM   2767  C   ASP A 376      24.091  48.338   3.515  1.00 87.20           C  
ANISOU 2767  C   ASP A 376    11724  10137  11271   -217  -1554   -819       C  
ATOM   2768  O   ASP A 376      24.368  47.978   2.361  1.00 80.40           O  
ANISOU 2768  O   ASP A 376    11044   9230  10274   -168  -1622   -935       O  
ATOM   2769  CB  ASP A 376      23.095  46.028   3.862  1.00110.85           C  
ANISOU 2769  CB  ASP A 376    14709  12908  14502   -380  -1840   -861       C  
ATOM   2770  CG  ASP A 376      22.503  45.033   4.848  1.00115.90           C  
ANISOU 2770  CG  ASP A 376    15224  13459  15355   -498  -1924   -794       C  
ATOM   2771  OD1 ASP A 376      22.987  45.038   6.003  1.00120.72           O  
ANISOU 2771  OD1 ASP A 376    15727  14090  16052   -497  -1781   -720       O  
ATOM   2772  OD2 ASP A 376      21.636  44.217   4.424  1.00113.57           O1-
ANISOU 2772  OD2 ASP A 376    14954  13066  15133   -590  -2134   -820       O1-
ATOM   2773  N   GLY A 377      24.566  49.463   4.069  1.00 76.94           N  
ANISOU 2773  N   GLY A 377    10342   8945   9947   -170  -1377   -743       N  
ATOM   2774  CA  GLY A 377      25.763  50.157   3.591  1.00 71.69           C  
ANISOU 2774  CA  GLY A 377     9777   8335   9127    -62  -1214   -787       C  
ATOM   2775  C   GLY A 377      25.679  51.079   2.382  1.00 82.86           C  
ANISOU 2775  C   GLY A 377    11304   9816  10363     -2  -1222   -809       C  
ATOM   2776  O   GLY A 377      26.615  51.843   2.112  1.00 81.39           O  
ANISOU 2776  O   GLY A 377    11170   9692  10064     76  -1067   -811       O  
ATOM   2777  N   LYS A 378      24.590  51.014   1.625  1.00 87.07           N  
ANISOU 2777  N   LYS A 378    11877  10338  10868    -39  -1404   -820       N  
ATOM   2778  CA  LYS A 378      24.434  51.958   0.528  1.00 84.98           C  
ANISOU 2778  CA  LYS A 378    11714  10142  10433     18  -1419   -824       C  
ATOM   2779  C   LYS A 378      24.044  53.312   1.125  1.00 79.43           C  
ANISOU 2779  C   LYS A 378    10867   9539   9772     15  -1338   -692       C  
ATOM   2780  O   LYS A 378      23.368  53.349   2.154  1.00 67.41           O  
ANISOU 2780  O   LYS A 378     9173   8026   8413    -49  -1356   -608       O  
ATOM   2781  CB  LYS A 378      23.402  51.441  -0.466  1.00 91.91           C  
ANISOU 2781  CB  LYS A 378    12683  10972  11266    -18  -1657   -879       C  
ATOM   2782  CG  LYS A 378      24.031  50.807  -1.675  1.00 91.57           C  
ANISOU 2782  CG  LYS A 378    12877  10874  11041     52  -1694  -1022       C  
ATOM   2783  CD  LYS A 378      22.980  50.214  -2.568  1.00 88.75           C  
ANISOU 2783  CD  LYS A 378    12615  10456  10651      5  -1955  -1084       C  
ATOM   2784  CE  LYS A 378      23.339  50.491  -4.013  1.00101.84           C  
ANISOU 2784  CE  LYS A 378    14507  12137  12051    103  -1973  -1173       C  
ATOM   2785  NZ  LYS A 378      22.457  49.745  -4.943  1.00 96.54           N1+
ANISOU 2785  NZ  LYS A 378    13967  11388  11328     65  -2242  -1262       N1+
ATOM   2786  N   PRO A 379      24.468  54.418   0.479  1.00 84.39           N  
ANISOU 2786  N   PRO A 379    11573  10241  10253     88  -1245   -673       N  
ATOM   2787  CA  PRO A 379      24.494  55.812   0.964  1.00 85.02           C  
ANISOU 2787  CA  PRO A 379    11560  10404  10341    111  -1125   -564       C  
ATOM   2788  C   PRO A 379      23.207  56.397   1.586  1.00 92.13           C  
ANISOU 2788  C   PRO A 379    12299  11341  11366     64  -1208   -458       C  
ATOM   2789  O   PRO A 379      23.200  57.584   1.944  1.00100.53           O  
ANISOU 2789  O   PRO A 379    13303  12465  12430     94  -1115   -375       O  
ATOM   2790  CB  PRO A 379      24.861  56.595  -0.302  1.00 76.93           C  
ANISOU 2790  CB  PRO A 379    10697   9424   9111    187  -1095   -581       C  
ATOM   2791  CG  PRO A 379      25.709  55.656  -1.073  1.00 75.07           C  
ANISOU 2791  CG  PRO A 379    10623   9141   8760    228  -1080   -701       C  
ATOM   2792  CD  PRO A 379      25.085  54.306  -0.858  1.00 78.67           C  
ANISOU 2792  CD  PRO A 379    11059   9510   9322    163  -1243   -767       C  
ATOM   2793  N   PHE A 380      22.165  55.582   1.716  1.00 69.41           N  
ANISOU 2793  N   PHE A 380     9350   8425   8597     -8  -1377   -459       N  
ATOM   2794  CA  PHE A 380      20.923  55.913   2.440  1.00 66.21           C  
ANISOU 2794  CA  PHE A 380     8760   8054   8341    -58  -1450   -354       C  
ATOM   2795  C   PHE A 380      20.004  56.821   1.653  1.00 68.40           C  
ANISOU 2795  C   PHE A 380     9046   8387   8555    -30  -1555   -304       C  
ATOM   2796  O   PHE A 380      20.217  58.025   1.549  1.00 61.70           O  
ANISOU 2796  O   PHE A 380     8215   7596   7633     36  -1459   -253       O  
ATOM   2797  CB  PHE A 380      21.181  56.551   3.818  1.00 54.63           C  
ANISOU 2797  CB  PHE A 380     7148   6631   6978    -50  -1281   -268       C  
ATOM   2798  CG  PHE A 380      19.909  56.871   4.583  1.00 58.40           C  
ANISOU 2798  CG  PHE A 380     7436   7151   7602    -86  -1337   -159       C  
ATOM   2799  CD1 PHE A 380      19.389  55.975   5.507  1.00 66.21           C  
ANISOU 2799  CD1 PHE A 380     8287   8115   8755   -162  -1374   -125       C  
ATOM   2800  CD2 PHE A 380      19.226  58.053   4.366  1.00 51.54           C  
ANISOU 2800  CD2 PHE A 380     6525   6349   6708    -37  -1350    -86       C  
ATOM   2801  CE1 PHE A 380      18.217  56.262   6.195  1.00 64.63           C  
ANISOU 2801  CE1 PHE A 380     7903   7965   8687   -189  -1411    -16       C  
ATOM   2802  CE2 PHE A 380      18.061  58.336   5.038  1.00 57.83           C  
ANISOU 2802  CE2 PHE A 380     7142   7191   7639    -55  -1392     14       C  
ATOM   2803  CZ  PHE A 380      17.557  57.442   5.957  1.00 66.71           C  
ANISOU 2803  CZ  PHE A 380     8123   8301   8924   -130  -1417     50       C  
ATOM   2804  N   LYS A 381      18.945  56.219   1.137  1.00 80.17           N  
ANISOU 2804  N   LYS A 381    10518   9854  10089    -85  -1764   -312       N  
ATOM   2805  CA  LYS A 381      17.961  56.921   0.347  1.00 69.96           C  
ANISOU 2805  CA  LYS A 381     9224   8608   8749    -64  -1903   -266       C  
ATOM   2806  C   LYS A 381      16.690  57.002   1.170  1.00 76.11           C  
ANISOU 2806  C   LYS A 381     9771   9423   9726   -119  -1978   -155       C  
ATOM   2807  O   LYS A 381      16.376  56.086   1.926  1.00 78.92           O  
ANISOU 2807  O   LYS A 381    10009   9741  10235   -201  -2010   -144       O  
ATOM   2808  CB  LYS A 381      17.733  56.196  -0.984  1.00 50.08           C  
ANISOU 2808  CB  LYS A 381     6874   6040   6115    -81  -2103   -364       C  
ATOM   2809  N   THR A 382      15.963  58.104   1.059  1.00 84.67           N  
ANISOU 2809  N   THR A 382    10783  10578  10809    -70  -1997    -65       N  
ATOM   2810  CA  THR A 382      14.697  58.186   1.762  1.00 90.11           C  
ANISOU 2810  CA  THR A 382    11242  11310  11684   -109  -2069     44       C  
ATOM   2811  C   THR A 382      13.709  57.273   1.058  1.00 93.73           C  
ANISOU 2811  C   THR A 382    11676  11735  12201   -195  -2328     25       C  
ATOM   2812  O   THR A 382      14.031  56.660   0.039  1.00 92.38           O  
ANISOU 2812  O   THR A 382    11684  11504  11911   -213  -2447    -81       O  
ATOM   2813  CB  THR A 382      14.132  59.634   1.830  1.00 82.34           C  
ANISOU 2813  CB  THR A 382    10183  10410  10694    -19  -2025    147       C  
ATOM   2814  CG2 THR A 382      15.006  60.531   2.717  1.00 68.11           C  
ANISOU 2814  CG2 THR A 382     8383   8631   8867     53  -1779    174       C  
ATOM   2815  OG1 THR A 382      14.034  60.185   0.510  1.00 86.24           O  
ANISOU 2815  OG1 THR A 382    10827  10911  11027     34  -2137    123       O  
ATOM   2816  N   ARG A 383      12.515  57.169   1.627  1.00 99.09           N  
ANISOU 2816  N   ARG A 383    12132  12451  13067   -248  -2413    127       N  
ATOM   2817  CA  ARG A 383      11.404  56.484   0.977  1.00107.28           C  
ANISOU 2817  CA  ARG A 383    13109  13468  14185   -335  -2678    135       C  
ATOM   2818  C   ARG A 383      11.177  57.067  -0.417  1.00102.00           C  
ANISOU 2818  C   ARG A 383    12591  12814  13349   -276  -2832     99       C  
ATOM   2819  O   ARG A 383      11.165  58.288  -0.585  1.00105.77           O  
ANISOU 2819  O   ARG A 383    13082  13360  13747   -172  -2756    152       O  
ATOM   2820  CB  ARG A 383      10.141  56.607   1.834  1.00108.69           C  
ANISOU 2820  CB  ARG A 383    12994  13713  14589   -376  -2711    281       C  
ATOM   2821  CG  ARG A 383       8.944  55.789   1.379  1.00107.31           C  
ANISOU 2821  CG  ARG A 383    12704  13518  14552   -491  -2983    311       C  
ATOM   2822  CD  ARG A 383       7.832  55.873   2.428  1.00110.45           C  
ANISOU 2822  CD  ARG A 383    12787  13991  15189   -530  -2960    470       C  
ATOM   2823  NE  ARG A 383       7.621  57.251   2.883  1.00108.60           N  
ANISOU 2823  NE  ARG A 383    12457  13865  14942   -397  -2802    564       N  
ATOM   2824  CZ  ARG A 383       6.695  57.622   3.763  1.00 97.64           C  
ANISOU 2824  CZ  ARG A 383    10807  12565  13727   -382  -2744    706       C  
ATOM   2825  NH1 ARG A 383       5.879  56.715   4.290  1.00101.28           N1+
ANISOU 2825  NH1 ARG A 383    11060  13026  14395   -503  -2826    784       N1+
ATOM   2826  NH2 ARG A 383       6.581  58.899   4.107  1.00 79.90           N  
ANISOU 2826  NH2 ARG A 383     8509  10402  11448   -245  -2602    773       N  
ATOM   2827  N   ALA A 384      11.029  56.187  -1.405  1.00 94.79           N  
ANISOU 2827  N   ALA A 384    11807  11831  12377   -340  -3048      6       N  
ATOM   2828  CA  ALA A 384      10.841  56.573  -2.809  1.00101.84           C  
ANISOU 2828  CA  ALA A 384    12875  12730  13088   -291  -3217    -42       C  
ATOM   2829  C   ALA A 384      12.036  57.348  -3.386  1.00 98.94           C  
ANISOU 2829  C   ALA A 384    12744  12375  12473   -170  -3051   -105       C  
ATOM   2830  O   ALA A 384      11.862  58.376  -4.060  1.00 79.81           O  
ANISOU 2830  O   ALA A 384    10388  10009   9929    -84  -3072    -65       O  
ATOM   2831  CB  ALA A 384       9.552  57.384  -2.978  1.00105.65           C  
ANISOU 2831  CB  ALA A 384    13188  13297  13656   -269  -3352     83       C  
ATOM   2832  N   GLY A 385      13.239  56.835  -3.121  1.00105.26           N  
ANISOU 2832  N   GLY A 385    13666  13122  13208   -167  -2890   -195       N  
ATOM   2833  CA  GLY A 385      14.462  57.318  -3.742  1.00112.42           C  
ANISOU 2833  CA  GLY A 385    14803  14029  13884    -71  -2741   -266       C  
ATOM   2834  C   GLY A 385      14.700  58.812  -3.648  1.00114.23           C  
ANISOU 2834  C   GLY A 385    15022  14339  14042     33  -2581   -175       C  
ATOM   2835  O   GLY A 385      14.966  59.345  -2.567  1.00119.98           O  
ANISOU 2835  O   GLY A 385    15618  15096  14871     50  -2394   -106       O  
ATOM   2836  N   GLY A 386      14.599  59.487  -4.791  1.00111.61           N  
ANISOU 2836  N   GLY A 386    14841  14035  13530    101  -2662   -175       N  
ATOM   2837  CA  GLY A 386      14.876  60.908  -4.868  1.00102.97           C  
ANISOU 2837  CA  GLY A 386    13774  13001  12348    200  -2523    -92       C  
ATOM   2838  C   GLY A 386      16.270  61.214  -4.361  1.00 96.46           C  
ANISOU 2838  C   GLY A 386    13018  12168  11464    239  -2251   -115       C  
ATOM   2839  O   GLY A 386      17.165  60.365  -4.410  1.00 96.27           O  
ANISOU 2839  O   GLY A 386    13094  12097  11386    216  -2184   -215       O  
ATOM   2840  N   THR A 387      16.458  62.419  -3.846  1.00 87.82           N  
ANISOU 2840  N   THR A 387    11863  11114  10390    299  -2097    -22       N  
ATOM   2841  CA  THR A 387      17.783  62.818  -3.407  1.00 90.59           C  
ANISOU 2841  CA  THR A 387    12277  11457  10686    331  -1852    -34       C  
ATOM   2842  C   THR A 387      17.809  63.047  -1.890  1.00 83.63           C  
ANISOU 2842  C   THR A 387    11198  10581   9997    311  -1711     22       C  
ATOM   2843  O   THR A 387      18.488  63.951  -1.394  1.00 93.07           O  
ANISOU 2843  O   THR A 387    12395  11785  11183    354  -1534     65       O  
ATOM   2844  CB  THR A 387      18.253  64.077  -4.175  1.00 96.88           C  
ANISOU 2844  CB  THR A 387    13219  12281  11310    418  -1772     18       C  
ATOM   2845  CG2 THR A 387      17.409  65.292  -3.813  1.00102.18           C  
ANISOU 2845  CG2 THR A 387    13774  12986  12063    465  -1789    142       C  
ATOM   2846  OG1 THR A 387      19.633  64.334  -3.898  1.00102.53           O  
ANISOU 2846  OG1 THR A 387    14008  12984  11964    436  -1547     -2       O  
ATOM   2847  N   VAL A 388      17.080  62.196  -1.169  1.00 64.45           N  
ANISOU 2847  N   VAL A 388     8608   8143   7739    241  -1794     20       N  
ATOM   2848  CA  VAL A 388      16.961  62.269   0.282  1.00 66.89           C  
ANISOU 2848  CA  VAL A 388     8726   8461   8227    220  -1679     75       C  
ATOM   2849  C   VAL A 388      16.256  63.554   0.691  1.00 79.65           C  
ANISOU 2849  C   VAL A 388    10236  10128   9901    288  -1648    188       C  
ATOM   2850  O   VAL A 388      16.855  64.635   0.726  1.00 81.83           O  
ANISOU 2850  O   VAL A 388    10581  10410  10102    356  -1518    219       O  
ATOM   2851  CB  VAL A 388      18.331  62.189   0.993  1.00 70.38           C  
ANISOU 2851  CB  VAL A 388     9212   8876   8652    220  -1466     32       C  
ATOM   2852  CG1 VAL A 388      18.150  62.308   2.488  1.00 65.75           C  
ANISOU 2852  CG1 VAL A 388     8444   8305   8235    205  -1360     90       C  
ATOM   2853  CG2 VAL A 388      19.058  60.897   0.636  1.00 75.27           C  
ANISOU 2853  CG2 VAL A 388     9933   9442   9223    168  -1486    -81       C  
ATOM   2854  N   LYS A 389      14.966  63.435   0.970  1.00 81.40           N  
ANISOU 2854  N   LYS A 389    10287  10383  10260    270  -1774    252       N  
ATOM   2855  CA  LYS A 389      14.171  64.570   1.409  1.00 70.07           C  
ANISOU 2855  CA  LYS A 389     8730   8997   8897    346  -1752    361       C  
ATOM   2856  C   LYS A 389      13.875  64.338   2.881  1.00 72.27           C  
ANISOU 2856  C   LYS A 389     8809   9295   9354    324  -1649    405       C  
ATOM   2857  O   LYS A 389      13.159  63.406   3.237  1.00 74.66           O  
ANISOU 2857  O   LYS A 389     8971   9609   9788    251  -1738    418       O  
ATOM   2858  CB  LYS A 389      12.884  64.716   0.575  1.00 53.35           C  
ANISOU 2858  CB  LYS A 389     6557   6915   6797    361  -1971    415       C  
ATOM   2859  N   LEU A 390      14.457  65.169   3.736  1.00 70.98           N  
ANISOU 2859  N   LEU A 390     8644   9133   9192    383  -1462    429       N  
ATOM   2860  CA  LEU A 390      14.375  64.961   5.178  1.00 64.51           C  
ANISOU 2860  CA  LEU A 390     7672   8331   8509    371  -1341    460       C  
ATOM   2861  C   LEU A 390      12.945  65.012   5.687  1.00 73.68           C  
ANISOU 2861  C   LEU A 390     8615   9555   9825    390  -1408    557       C  
ATOM   2862  O   LEU A 390      12.578  64.242   6.582  1.00 81.93           O  
ANISOU 2862  O   LEU A 390     9510  10620  11000    334  -1385    582       O  
ATOM   2863  CB  LEU A 390      15.234  65.984   5.919  1.00 50.46           C  
ANISOU 2863  CB  LEU A 390     5952   6535   6684    442  -1147    463       C  
ATOM   2864  CG  LEU A 390      16.725  65.815   5.609  1.00 49.74           C  
ANISOU 2864  CG  LEU A 390     6040   6389   6471    411  -1060    377       C  
ATOM   2865  CD1 LEU A 390      17.564  66.762   6.433  1.00 59.49           C  
ANISOU 2865  CD1 LEU A 390     7315   7603   7684    463   -884    383       C  
ATOM   2866  CD2 LEU A 390      17.166  64.387   5.847  1.00 38.51           C  
ANISOU 2866  CD2 LEU A 390     4604   4944   5085    313  -1071    310       C  
ATOM   2867  N   ALA A 391      12.133  65.896   5.112  1.00 70.61           N  
ANISOU 2867  N   ALA A 391     8202   9200   9427    468  -1492    620       N  
ATOM   2868  CA  ALA A 391      10.729  65.988   5.502  1.00 63.09           C  
ANISOU 2868  CA  ALA A 391     7028   8317   8628    497  -1562    721       C  
ATOM   2869  C   ALA A 391      10.045  64.646   5.300  1.00 64.05           C  
ANISOU 2869  C   ALA A 391     7030   8450   8857    376  -1720    723       C  
ATOM   2870  O   ALA A 391       9.095  64.315   5.999  1.00 70.43           O  
ANISOU 2870  O   ALA A 391     7621   9313   9827    357  -1734    803       O  
ATOM   2871  CB  ALA A 391      10.028  67.061   4.723  1.00 58.65           C  
ANISOU 2871  CB  ALA A 391     6476   7780   8028    599  -1654    780       C  
ATOM   2872  N   ASP A 392      10.552  63.865   4.355  1.00 63.05           N  
ANISOU 2872  N   ASP A 392     7049   8269   8640    293  -1835    635       N  
ATOM   2873  CA  ASP A 392      10.044  62.527   4.127  1.00 72.25           C  
ANISOU 2873  CA  ASP A 392     8136   9418   9897    166  -1995    618       C  
ATOM   2874  C   ASP A 392      10.454  61.613   5.283  1.00 68.09           C  
ANISOU 2874  C   ASP A 392     7531   8871   9469     89  -1875    606       C  
ATOM   2875  O   ASP A 392       9.633  60.896   5.849  1.00 70.63           O  
ANISOU 2875  O   ASP A 392     7662   9218   9957     18  -1925    670       O  
ATOM   2876  CB  ASP A 392      10.559  61.994   2.790  1.00 91.78           C  
ANISOU 2876  CB  ASP A 392    10821  11829  12223    117  -2143    512       C  
ATOM   2877  CG  ASP A 392      10.222  60.535   2.573  1.00113.56           C  
ANISOU 2877  CG  ASP A 392    13540  14544  15065    -19  -2307    470       C  
ATOM   2878  OD1 ASP A 392      10.940  59.663   3.126  1.00118.08           O  
ANISOU 2878  OD1 ASP A 392    14143  15064  15659    -86  -2224    412       O  
ATOM   2879  OD2 ASP A 392       9.245  60.262   1.838  1.00120.58           O1-
ANISOU 2879  OD2 ASP A 392    14370  15444  16000    -60  -2528    495       O1-
ATOM   2880  N   LEU A 393      11.730  61.655   5.635  1.00 61.06           N  
ANISOU 2880  N   LEU A 393     6784   7935   8479    103  -1715    532       N  
ATOM   2881  CA  LEU A 393      12.245  60.863   6.736  1.00 50.17           C  
ANISOU 2881  CA  LEU A 393     5354   6534   7175     42  -1594    519       C  
ATOM   2882  C   LEU A 393      11.435  61.094   7.989  1.00 56.96           C  
ANISOU 2882  C   LEU A 393     5991   7464   8186     68  -1500    634       C  
ATOM   2883  O   LEU A 393      11.103  60.156   8.712  1.00 61.82           O  
ANISOU 2883  O   LEU A 393     6477   8082   8930    -15  -1498    671       O  
ATOM   2884  CB  LEU A 393      13.700  61.208   6.993  1.00 42.02           C  
ANISOU 2884  CB  LEU A 393     4492   5460   6014     83  -1423    442       C  
ATOM   2885  CG  LEU A 393      14.339  60.455   8.142  1.00 52.98           C  
ANISOU 2885  CG  LEU A 393     5842   6823   7465     32  -1297    428       C  
ATOM   2886  CD1 LEU A 393      14.290  58.974   7.836  1.00 62.20           C  
ANISOU 2886  CD1 LEU A 393     7010   7933   8689    -88  -1423    382       C  
ATOM   2887  CD2 LEU A 393      15.756  60.912   8.256  1.00 52.42           C  
ANISOU 2887  CD2 LEU A 393     5936   6716   7266     77  -1151    355       C  
ATOM   2888  N   LEU A 394      11.097  62.357   8.220  1.00 58.65           N  
ANISOU 2888  N   LEU A 394     6168   7735   8383    187  -1421    692       N  
ATOM   2889  CA  LEU A 394      10.392  62.761   9.424  1.00 61.89           C  
ANISOU 2889  CA  LEU A 394     6388   8218   8910    245  -1303    795       C  
ATOM   2890  C   LEU A 394       8.921  62.405   9.352  1.00 69.61           C  
ANISOU 2890  C   LEU A 394     7136   9262  10049    213  -1433    901       C  
ATOM   2891  O   LEU A 394       8.285  62.125  10.377  1.00 71.36           O  
ANISOU 2891  O   LEU A 394     7167   9542  10405    205  -1357    991       O  
ATOM   2892  CB  LEU A 394      10.568  64.257   9.661  1.00 65.00           C  
ANISOU 2892  CB  LEU A 394     6837   8635   9225    396  -1179    811       C  
ATOM   2893  CG  LEU A 394      11.652  64.655  10.670  1.00 57.65           C  
ANISOU 2893  CG  LEU A 394     6001   7677   8226    439   -976    768       C  
ATOM   2894  CD1 LEU A 394      12.918  63.863  10.446  1.00 46.74           C  
ANISOU 2894  CD1 LEU A 394     4777   6219   6764    347   -966    665       C  
ATOM   2895  CD2 LEU A 394      11.925  66.147  10.547  1.00 62.10           C  
ANISOU 2895  CD2 LEU A 394     6671   8231   8693    572   -901    763       C  
ATOM   2896  N   ASP A 395       8.381  62.412   8.140  1.00 66.06           N  
ANISOU 2896  N   ASP A 395     6705   8807   9586    194  -1630    896       N  
ATOM   2897  CA  ASP A 395       7.016  61.961   7.938  1.00 74.36           C  
ANISOU 2897  CA  ASP A 395     7539   9914  10800    141  -1790    992       C  
ATOM   2898  C   ASP A 395       6.930  60.461   8.205  1.00 75.31           C  
ANISOU 2898  C   ASP A 395     7583   9996  11034    -22  -1862    989       C  
ATOM   2899  O   ASP A 395       6.036  59.997   8.919  1.00 80.47           O  
ANISOU 2899  O   ASP A 395     8005  10706  11864    -70  -1858   1098       O  
ATOM   2900  CB  ASP A 395       6.533  62.292   6.524  1.00 84.74           C  
ANISOU 2900  CB  ASP A 395     8915  11223  12060    155  -2007    978       C  
ATOM   2901  CG  ASP A 395       6.163  63.758   6.365  1.00 92.18           C  
ANISOU 2901  CG  ASP A 395     9851  12219  12954    318  -1962   1032       C  
ATOM   2902  OD1 ASP A 395       5.928  64.425   7.399  1.00 91.72           O  
ANISOU 2902  OD1 ASP A 395     9678  12217  12955    415  -1789   1101       O  
ATOM   2903  OD2 ASP A 395       6.104  64.241   5.210  1.00 96.82           O1-
ANISOU 2903  OD2 ASP A 395    10557  12789  13441    354  -2100   1004       O1-
ATOM   2904  N   GLU A 396       7.876  59.711   7.648  1.00 70.81           N  
ANISOU 2904  N   GLU A 396     7209   9330  10366   -104  -1918    869       N  
ATOM   2905  CA  GLU A 396       7.859  58.264   7.774  1.00 67.82           C  
ANISOU 2905  CA  GLU A 396     6792   8890  10086   -258  -2007    852       C  
ATOM   2906  C   GLU A 396       8.053  57.834   9.228  1.00 67.07           C  
ANISOU 2906  C   GLU A 396     6583   8813  10086   -283  -1820    911       C  
ATOM   2907  O   GLU A 396       7.446  56.863   9.678  1.00 65.61           O  
ANISOU 2907  O   GLU A 396     6242   8625  10062   -396  -1875    981       O  
ATOM   2908  CB  GLU A 396       8.926  57.630   6.881  1.00 73.34           C  
ANISOU 2908  CB  GLU A 396     7747   9479  10641   -312  -2087    700       C  
ATOM   2909  CG  GLU A 396       9.068  56.119   7.085  1.00 78.04           C  
ANISOU 2909  CG  GLU A 396     8334   9989  11329   -461  -2163    668       C  
ATOM   2910  CD  GLU A 396       9.798  55.419   5.954  1.00 83.31           C  
ANISOU 2910  CD  GLU A 396     9237  10547  11870   -512  -2303    520       C  
ATOM   2911  OE1 GLU A 396       9.137  54.648   5.232  1.00 90.17           O  
ANISOU 2911  OE1 GLU A 396    10087  11369  12803   -611  -2529    507       O  
ATOM   2912  OE2 GLU A 396      11.023  55.611   5.794  1.00 87.95           O1-
ANISOU 2912  OE2 GLU A 396    10025  11094  12298   -455  -2189    418       O1-
ATOM   2913  N   ALA A 397       8.893  58.554   9.965  1.00 61.34           N  
ANISOU 2913  N   ALA A 397     5941   8103   9264   -183  -1606    887       N  
ATOM   2914  CA  ALA A 397       9.050  58.267  11.387  1.00 59.40           C  
ANISOU 2914  CA  ALA A 397     5596   7885   9090   -188  -1425    948       C  
ATOM   2915  C   ALA A 397       7.701  58.356  12.095  1.00 68.33           C  
ANISOU 2915  C   ALA A 397     6449   9119  10393   -180  -1404   1107       C  
ATOM   2916  O   ALA A 397       7.289  57.431  12.798  1.00 71.83           O  
ANISOU 2916  O   ALA A 397     6747   9571  10974   -276  -1393   1185       O  
ATOM   2917  CB  ALA A 397      10.041  59.215  12.021  1.00 47.20           C  
ANISOU 2917  CB  ALA A 397     4177   6347   7410    -67  -1219    902       C  
ATOM   2918  N   LEU A 398       7.000  59.459  11.873  1.00 65.94           N  
ANISOU 2918  N   LEU A 398     6071   8896  10089    -64  -1401   1160       N  
ATOM   2919  CA  LEU A 398       5.749  59.692  12.566  1.00 66.74           C  
ANISOU 2919  CA  LEU A 398     5904   9110  10346    -25  -1355   1314       C  
ATOM   2920  C   LEU A 398       4.690  58.648  12.200  1.00 78.57           C  
ANISOU 2920  C   LEU A 398     7205  10617  12032   -173  -1545   1400       C  
ATOM   2921  O   LEU A 398       3.907  58.231  13.055  1.00 83.82           O  
ANISOU 2921  O   LEU A 398     7642  11352  12855   -210  -1484   1532       O  
ATOM   2922  CB  LEU A 398       5.246  61.104  12.274  1.00 64.32           C  
ANISOU 2922  CB  LEU A 398     5572   8873   9995    140  -1330   1344       C  
ATOM   2923  CG  LEU A 398       5.468  62.087  13.421  1.00 68.66           C  
ANISOU 2923  CG  LEU A 398     6118   9479  10489    297  -1084   1372       C  
ATOM   2924  CD1 LEU A 398       6.949  62.219  13.780  1.00 70.41           C  
ANISOU 2924  CD1 LEU A 398     6585   9621  10547    312   -956   1250       C  
ATOM   2925  CD2 LEU A 398       4.924  63.431  13.046  1.00 68.09           C  
ANISOU 2925  CD2 LEU A 398     6027   9459  10385    459  -1082   1400       C  
ATOM   2926  N   GLU A 399       4.669  58.212  10.945  1.00 75.20           N  
ANISOU 2926  N   GLU A 399     6867  10118  11586   -259  -1776   1329       N  
ATOM   2927  CA  GLU A 399       3.663  57.240  10.516  1.00 71.89           C  
ANISOU 2927  CA  GLU A 399     6273   9694  11347   -408  -1989   1401       C  
ATOM   2928  C   GLU A 399       3.903  55.917  11.211  1.00 68.79           C  
ANISOU 2928  C   GLU A 399     5842   9241  11054   -559  -1965   1421       C  
ATOM   2929  O   GLU A 399       2.977  55.270  11.679  1.00 74.48           O  
ANISOU 2929  O   GLU A 399     6327  10002  11971   -655  -2003   1553       O  
ATOM   2930  CB  GLU A 399       3.690  57.050   9.005  1.00 78.22           C  
ANISOU 2930  CB  GLU A 399     7220  10419  12079   -463  -2250   1300       C  
ATOM   2931  CG  GLU A 399       3.424  58.325   8.237  1.00 92.14           C  
ANISOU 2931  CG  GLU A 399     9029  12236  13743   -320  -2293   1290       C  
ATOM   2932  CD  GLU A 399       3.620  58.161   6.743  1.00104.45           C  
ANISOU 2932  CD  GLU A 399    10778  13717  15191   -363  -2535   1179       C  
ATOM   2933  OE1 GLU A 399       3.732  57.006   6.280  1.00107.19           O  
ANISOU 2933  OE1 GLU A 399    11184  13975  15569   -511  -2697   1119       O  
ATOM   2934  OE2 GLU A 399       3.664  59.189   6.032  1.00109.22           O1-
ANISOU 2934  OE2 GLU A 399    11484  14346  15670   -245  -2563   1150       O1-
ATOM   2935  N   ARG A 400       5.166  55.529  11.276  1.00 66.95           N  
ANISOU 2935  N   ARG A 400     5840   8910  10688   -576  -1901   1296       N  
ATOM   2936  CA  ARG A 400       5.567  54.346  12.005  1.00 68.37           C  
ANISOU 2936  CA  ARG A 400     6015   9021  10940   -697  -1856   1306       C  
ATOM   2937  C   ARG A 400       5.260  54.514  13.476  1.00 76.87           C  
ANISOU 2937  C   ARG A 400     6911  10195  12099   -653  -1629   1443       C  
ATOM   2938  O   ARG A 400       4.636  53.655  14.088  1.00 82.45           O  
ANISOU 2938  O   ARG A 400     7438  10913  12976   -764  -1636   1562       O  
ATOM   2939  CB  ARG A 400       7.045  54.089  11.811  1.00 58.58           C  
ANISOU 2939  CB  ARG A 400     5059   7672   9527   -689  -1808   1144       C  
ATOM   2940  CG  ARG A 400       7.380  53.648  10.433  1.00 56.23           C  
ANISOU 2940  CG  ARG A 400     4945   7269   9152   -749  -2026   1011       C  
ATOM   2941  CD  ARG A 400       8.863  53.625  10.284  1.00 64.43           C  
ANISOU 2941  CD  ARG A 400     6248   8224  10007   -703  -1937    861       C  
ATOM   2942  NE  ARG A 400       9.301  52.335   9.762  1.00 77.49           N  
ANISOU 2942  NE  ARG A 400     8026   9743  11674   -826  -2082    770       N  
ATOM   2943  CZ  ARG A 400       9.374  52.048   8.470  1.00 81.16           C  
ANISOU 2943  CZ  ARG A 400     8638  10134  12066   -859  -2280    661       C  
ATOM   2944  NH1 ARG A 400       9.031  52.959   7.572  1.00 78.55           N1+
ANISOU 2944  NH1 ARG A 400     8343   9857  11647   -783  -2358    641       N1+
ATOM   2945  NH2 ARG A 400       9.788  50.855   8.076  1.00 87.22           N  
ANISOU 2945  NH2 ARG A 400     9526  10770  12844   -961  -2402    573       N  
ATOM   2946  N   ALA A 401       5.706  55.636  14.030  1.00 76.09           N  
ANISOU 2946  N   ALA A 401     6872  10164  11875   -489  -1429   1428       N  
ATOM   2947  CA  ALA A 401       5.449  55.990  15.421  1.00 71.55           C  
ANISOU 2947  CA  ALA A 401     6156   9691  11340   -410  -1199   1544       C  
ATOM   2948  C   ALA A 401       3.962  55.957  15.780  1.00 74.18           C  
ANISOU 2948  C   ALA A 401     6175  10139  11869   -427  -1209   1727       C  
ATOM   2949  O   ALA A 401       3.585  55.447  16.833  1.00 72.36           O  
ANISOU 2949  O   ALA A 401     5787   9961  11746   -467  -1090   1851       O  
ATOM   2950  CB  ALA A 401       6.015  57.367  15.711  1.00 67.21           C  
ANISOU 2950  CB  ALA A 401     5728   9188  10623   -221  -1030   1486       C  
ATOM   2951  N   ARG A 402       3.128  56.521  14.911  1.00 76.82           N  
ANISOU 2951  N   ARG A 402     6417  10520  12250   -392  -1347   1751       N  
ATOM   2952  CA  ARG A 402       1.697  56.592  15.162  1.00 74.22           C  
ANISOU 2952  CA  ARG A 402     5775  10312  12115   -394  -1365   1928       C  
ATOM   2953  C   ARG A 402       1.096  55.187  15.178  1.00 86.37           C  
ANISOU 2953  C   ARG A 402     7175  11806  13837   -603  -1494   2010       C  
ATOM   2954  O   ARG A 402       0.411  54.800  16.131  1.00 89.15           O  
ANISOU 2954  O   ARG A 402     7384  12214  14276   -627  -1356   2133       O  
ATOM   2955  CB  ARG A 402       1.006  57.467  14.113  1.00 69.84           C  
ANISOU 2955  CB  ARG A 402     5174   9801  11563   -313  -1514   1922       C  
ATOM   2956  N   ARG A 403       1.368  54.412  14.134  1.00 88.61           N  
ANISOU 2956  N   ARG A 403     7572  11965  14131   -743  -1737   1917       N  
ATOM   2957  CA  ARG A 403       0.889  53.033  14.075  1.00 90.10           C  
ANISOU 2957  CA  ARG A 403     7725  12065  14443   -937  -1854   1951       C  
ATOM   2958  C   ARG A 403       1.443  52.194  15.241  1.00 83.54           C  
ANISOU 2958  C   ARG A 403     6905  11197  13638  -1004  -1693   1996       C  
ATOM   2959  O   ARG A 403       0.757  51.331  15.779  1.00 92.45           O  
ANISOU 2959  O   ARG A 403     7925  12315  14886  -1108  -1670   2102       O  
ATOM   2960  CB  ARG A 403       1.260  52.409  12.724  1.00 94.11           C  
ANISOU 2960  CB  ARG A 403     8403  12431  14922  -1054  -2139   1812       C  
ATOM   2961  CG  ARG A 403       0.668  53.159  11.521  1.00100.12           C  
ANISOU 2961  CG  ARG A 403     9167  13225  15649   -995  -2319   1772       C  
ATOM   2962  CD  ARG A 403       1.036  52.543  10.163  1.00 99.66           C  
ANISOU 2962  CD  ARG A 403     9305  13027  15534  -1100  -2601   1626       C  
ATOM   2963  NE  ARG A 403       2.468  52.606   9.876  1.00 94.04           N  
ANISOU 2963  NE  ARG A 403     8851  12230  14649  -1064  -2589   1470       N  
ATOM   2964  CZ  ARG A 403       3.321  51.620  10.139  1.00 92.68           C  
ANISOU 2964  CZ  ARG A 403     8825  11938  14451  -1155  -2567   1394       C  
ATOM   2965  NH1 ARG A 403       2.882  50.498  10.696  1.00 93.20           N1+
ANISOU 2965  NH1 ARG A 403     8760  11957  14694  -1308  -2601   1484       N1+
ATOM   2966  NH2 ARG A 403       4.609  51.754   9.852  1.00 92.24           N  
ANISOU 2966  NH2 ARG A 403     9053  11806  14187  -1087  -2500   1232       N  
ATOM   2967  N   LEU A 404       2.682  52.472  15.633  1.00 73.86           N  
ANISOU 2967  N   LEU A 404     5818   9951  12294   -939  -1578   1919       N  
ATOM   2968  CA  LEU A 404       3.341  51.788  16.741  1.00 76.83           C  
ANISOU 2968  CA  LEU A 404     6240  10292  12661   -979  -1415   1947       C  
ATOM   2969  C   LEU A 404       2.692  52.058  18.105  1.00 92.86           C  
ANISOU 2969  C   LEU A 404     8083  12457  14742   -907  -1170   2115       C  
ATOM   2970  O   LEU A 404       2.545  51.156  18.929  1.00100.11           O  
ANISOU 2970  O   LEU A 404     8960  13352  15726   -995  -1093   2203       O  
ATOM   2971  CB  LEU A 404       4.812  52.199  16.782  1.00 70.14           C  
ANISOU 2971  CB  LEU A 404     5692   9378  11581   -876  -1309   1774       C  
ATOM   2972  CG  LEU A 404       5.781  51.369  17.618  1.00 70.07           C  
ANISOU 2972  CG  LEU A 404     5803   9287  11532   -929  -1203   1750       C  
ATOM   2973  CD1 LEU A 404       5.713  49.912  17.213  1.00 60.12           C  
ANISOU 2973  CD1 LEU A 404     4546   7892  10406  -1130  -1394   1753       C  
ATOM   2974  CD2 LEU A 404       7.200  51.919  17.428  1.00 73.63           C  
ANISOU 2974  CD2 LEU A 404     6538   9679  11757   -820  -1131   1570       C  
ATOM   2975  N   VAL A 405       2.318  53.311  18.332  1.00 99.43           N  
ANISOU 2975  N   VAL A 405     8839  13422  15519   -732  -1041   2148       N  
ATOM   2976  CA  VAL A 405       1.675  53.750  19.570  1.00101.52           C  
ANISOU 2976  CA  VAL A 405     8967  13820  15787   -624   -795   2281       C  
ATOM   2977  C   VAL A 405       0.160  53.471  19.577  1.00108.68           C  
ANISOU 2977  C   VAL A 405     9674  14785  16833   -673   -829   2412       C  
ATOM   2978  O   VAL A 405      -0.519  53.623  20.601  1.00108.73           O  
ANISOU 2978  O   VAL A 405     9553  14895  16863   -608   -639   2538       O  
ATOM   2979  CB  VAL A 405       1.983  55.260  19.796  1.00 71.37           C  
ANISOU 2979  CB  VAL A 405     5178  10103  11837   -398   -642   2242       C  
ATOM   2980  CG1 VAL A 405       0.736  56.123  19.764  1.00 62.85           C  
ANISOU 2980  CG1 VAL A 405     3943   9142  10795   -279   -597   2321       C  
ATOM   2981  CG2 VAL A 405       2.763  55.456  21.086  1.00 72.84           C  
ANISOU 2981  CG2 VAL A 405     5446  10323  11907   -305   -394   2248       C  
ATOM   2982  N   ALA A 406      -0.351  53.025  18.431  1.00111.20           N  
ANISOU 2982  N   ALA A 406     9975  15035  17243   -790  -1075   2382       N  
ATOM   2983  CA  ALA A 406      -1.759  52.670  18.283  1.00111.53           C  
ANISOU 2983  CA  ALA A 406     9828  15115  17432   -859  -1146   2500       C  
ATOM   2984  C   ALA A 406      -2.183  51.625  19.298  1.00119.63           C  
ANISOU 2984  C   ALA A 406    10760  16137  18558   -966  -1045   2637       C  
ATOM   2985  O   ALA A 406      -3.295  51.668  19.821  1.00121.66           O  
ANISOU 2985  O   ALA A 406    10831  16490  18906   -947   -958   2778       O  
ATOM   2986  CB  ALA A 406      -2.032  52.162  16.880  1.00112.11           C  
ANISOU 2986  CB  ALA A 406     9941  15085  17572   -990  -1449   2425       C  
ATOM   2987  N   GLU A 407      -1.297  50.676  19.568  1.00128.91           N  
ANISOU 2987  N   GLU A 407    12064  17199  19718  -1075  -1060   2599       N  
ATOM   2988  CA  GLU A 407      -1.590  49.640  20.549  1.00138.22           C  
ANISOU 2988  CA  GLU A 407    13174  18360  20982  -1176   -969   2730       C  
ATOM   2989  C   GLU A 407      -1.430  50.252  21.945  1.00134.86           C  
ANISOU 2989  C   GLU A 407    12713  18064  20464  -1026   -666   2812       C  
ATOM   2990  O   GLU A 407      -0.500  51.029  22.180  1.00140.35           O  
ANISOU 2990  O   GLU A 407    13526  18787  21014   -898   -556   2724       O  
ATOM   2991  CB  GLU A 407      -0.678  48.421  20.357  1.00141.92           C  
ANISOU 2991  CB  GLU A 407    13806  18654  21462  -1334  -1092   2658       C  
ATOM   2992  CG  GLU A 407      -0.167  48.148  18.909  1.00159.27           C  
ANISOU 2992  CG  GLU A 407    16155  20710  23650  -1420  -1368   2489       C  
ATOM   2993  CD  GLU A 407      -1.193  48.370  17.783  1.00164.36           C  
ANISOU 2993  CD  GLU A 407    16709  21364  24375  -1451  -1569   2481       C  
ATOM   2994  OE1 GLU A 407      -2.413  48.216  18.009  1.00169.68           O  
ANISOU 2994  OE1 GLU A 407    17193  22104  25174  -1485  -1560   2619       O  
ATOM   2995  OE2 GLU A 407      -0.767  48.713  16.657  1.00164.08           O1-
ANISOU 2995  OE2 GLU A 407    16796  21274  24274  -1440  -1739   2337       O1-
ATOM   2996  N   LYS A 408      -2.339  49.894  22.853  1.00121.02           N  
ANISOU 2996  N   LYS A 408    10802  16386  18793  -1040   -539   2981       N  
ATOM   2997  CA  LYS A 408      -2.545  50.600  24.126  1.00108.39           C  
ANISOU 2997  CA  LYS A 408     9136  14936  17110   -877   -255   3076       C  
ATOM   2998  C   LYS A 408      -2.969  52.052  23.864  1.00110.27           C  
ANISOU 2998  C   LYS A 408     9317  15298  17284   -685   -188   3041       C  
ATOM   2999  O   LYS A 408      -2.339  53.004  24.335  1.00106.93           O  
ANISOU 2999  O   LYS A 408     8984  14936  16709   -516    -29   2980       O  
ATOM   3000  CB  LYS A 408      -1.297  50.548  25.014  1.00 97.49           C  
ANISOU 3000  CB  LYS A 408     7922  13535  15585   -825    -99   3031       C  
ATOM   3001  N   ASN A 409      -4.043  52.200  23.092  1.00115.46           N  
ANISOU 3001  N   ASN A 409     9829  15982  18059   -713   -320   3079       N  
ATOM   3002  CA  ASN A 409      -4.672  53.491  22.848  1.00120.07           C  
ANISOU 3002  CA  ASN A 409    10327  16684  18612   -538   -268   3072       C  
ATOM   3003  C   ASN A 409      -5.923  53.634  23.702  1.00129.61           C  
ANISOU 3003  C   ASN A 409    11324  18026  19895   -475   -103   3245       C  
ATOM   3004  O   ASN A 409      -6.550  52.634  24.053  1.00124.91           O  
ANISOU 3004  O   ASN A 409    10613  17420  19427   -611   -118   3374       O  
ATOM   3005  CB  ASN A 409      -5.048  53.649  21.373  1.00122.67           C  
ANISOU 3005  CB  ASN A 409    10634  16960  19014   -595   -531   2997       C  
ATOM   3006  CG  ASN A 409      -6.380  52.980  21.035  1.00127.52           C  
ANISOU 3006  CG  ASN A 409    11046  17585  19821   -724   -657   3121       C  
ATOM   3007  ND2 ASN A 409      -7.412  53.790  20.807  1.00124.83           N  
ANISOU 3007  ND2 ASN A 409    10547  17352  19530   -620   -645   3176       N  
ATOM   3008  OD1 ASN A 409      -6.478  51.753  20.987  1.00129.72           O  
ANISOU 3008  OD1 ASN A 409    11312  17772  20206   -911   -765   3169       O  
ATOM   3009  N   PRO A 410      -6.295  54.882  24.028  1.00139.57           N  
ANISOU 3009  N   PRO A 410    12538  19412  21080   -265     51   3249       N  
ATOM   3010  CA  PRO A 410      -7.517  55.283  24.738  1.00138.79           C  
ANISOU 3010  CA  PRO A 410    12240  19457  21038   -162    212   3396       C  
ATOM   3011  C   PRO A 410      -7.680  56.800  24.791  1.00128.97           C  
ANISOU 3011  C   PRO A 410    11003  18312  19686     84    333   3342       C  
ATOM   3012  O   PRO A 410      -8.804  57.287  24.656  1.00131.67           O  
ANISOU 3012  O   PRO A 410    11170  18746  20113    156    344   3418       O  
ATOM   3013  CB  PRO A 410      -7.317  54.708  26.144  1.00141.19           C  
ANISOU 3013  CB  PRO A 410    12556  19796  21293   -165    429   3498       C  
ATOM   3014  N   ASP A 411      -6.574  57.523  24.983  1.00113.53           N  
ANISOU 3014  N   ASP A 411     9248  16336  17553    211    417   3212       N  
ATOM   3015  CA  ASP A 411      -6.600  58.979  25.131  1.00 99.45           C  
ANISOU 3015  CA  ASP A 411     7507  14629  15650    456    544   3150       C  
ATOM   3016  C   ASP A 411      -6.525  59.675  23.779  1.00100.38           C  
ANISOU 3016  C   ASP A 411     7661  14699  15779    486    343   3038       C  
ATOM   3017  O   ASP A 411      -5.892  59.174  22.847  1.00 95.83           O  
ANISOU 3017  O   ASP A 411     7173  14014  15224    348    138   2954       O  
ATOM   3018  CB  ASP A 411      -5.453  59.449  26.027  1.00 95.08           C  
ANISOU 3018  CB  ASP A 411     7160  14070  14897    583    731   3067       C  
ATOM   3019  N   MET A 412      -7.168  60.836  23.682  1.00105.57           N  
ANISOU 3019  N   MET A 412     8259  15437  16417    674    401   3036       N  
ATOM   3020  CA  MET A 412      -7.310  61.541  22.408  1.00113.03           C  
ANISOU 3020  CA  MET A 412     9211  16350  17385    715    209   2955       C  
ATOM   3021  C   MET A 412      -5.957  61.915  21.834  1.00122.76           C  
ANISOU 3021  C   MET A 412    10679  17481  18485    736    129   2794       C  
ATOM   3022  O   MET A 412      -5.042  62.233  22.592  1.00130.09           O  
ANISOU 3022  O   MET A 412    11761  18398  19270    826    289   2736       O  
ATOM   3023  CB  MET A 412      -8.170  62.797  22.576  1.00107.49           C  
ANISOU 3023  CB  MET A 412     8421  15749  16669    940    318   2982       C  
ATOM   3024  N   PRO A 413      -5.820  61.857  20.496  1.00124.65           N  
ANISOU 3024  N   PRO A 413    10950  17644  18767    652   -123   2725       N  
ATOM   3025  CA  PRO A 413      -4.586  62.324  19.858  1.00123.39           C  
ANISOU 3025  CA  PRO A 413    11007  17395  18482    688   -205   2579       C  
ATOM   3026  C   PRO A 413      -4.299  63.742  20.310  1.00127.94           C  
ANISOU 3026  C   PRO A 413    11683  18011  18919    942    -34   2525       C  
ATOM   3027  O   PRO A 413      -3.345  63.946  21.068  1.00121.29           O  
ANISOU 3027  O   PRO A 413    10989  17149  17948   1009    120   2470       O  
ATOM   3028  CB  PRO A 413      -4.908  62.264  18.362  1.00119.57           C  
ANISOU 3028  CB  PRO A 413    10500  16858  18072    603   -491   2543       C  
ATOM   3029  CG  PRO A 413      -5.990  61.245  18.253  1.00119.72           C  
ANISOU 3029  CG  PRO A 413    10322  16901  18266    435   -588   2654       C  
ATOM   3030  CD  PRO A 413      -6.802  61.374  19.510  1.00122.74           C  
ANISOU 3030  CD  PRO A 413    10551  17398  18686    524   -347   2779       C  
ATOM   3031  N   ALA A 414      -5.143  64.673  19.859  1.00137.32           N  
ANISOU 3031  N   ALA A 414    12791  19248  20136   1076    -67   2542       N  
ATOM   3032  CA  ALA A 414      -5.164  66.079  20.279  1.00150.10           C  
ANISOU 3032  CA  ALA A 414    14480  20904  21646   1330     89   2505       C  
ATOM   3033  C   ALA A 414      -3.844  66.579  20.855  1.00161.07           C  
ANISOU 3033  C   ALA A 414    16102  22238  22858   1430    226   2400       C  
ATOM   3034  O   ALA A 414      -3.076  67.277  20.188  1.00165.57           O  
ANISOU 3034  O   ALA A 414    16834  22734  23341   1500    147   2300       O  
ATOM   3035  CB  ALA A 414      -6.282  66.291  21.293  1.00152.13           C  
ANISOU 3035  CB  ALA A 414    14570  21280  21951   1433    283   2616       C  
ATOM   3036  N   ASP A 415      -3.599  66.205  22.106  1.00161.95           N  
ANISOU 3036  N   ASP A 415    16231  22386  22917   1435    428   2429       N  
ATOM   3037  CA  ASP A 415      -2.342  66.496  22.780  1.00154.85           C  
ANISOU 3037  CA  ASP A 415    15545  21437  21854   1506    560   2336       C  
ATOM   3038  C   ASP A 415      -1.878  65.242  23.514  1.00146.97           C  
ANISOU 3038  C   ASP A 415    14540  20436  20865   1341    621   2377       C  
ATOM   3039  O   ASP A 415      -0.753  65.169  24.015  1.00152.18           O  
ANISOU 3039  O   ASP A 415    15365  21048  21408   1348    699   2306       O  
ATOM   3040  CB  ASP A 415      -2.497  67.685  23.741  1.00149.89           C  
ANISOU 3040  CB  ASP A 415    14993  20855  21103   1753    781   2313       C  
ATOM   3041  CG  ASP A 415      -3.551  67.455  24.819  1.00143.25           C  
ANISOU 3041  CG  ASP A 415    13994  20129  20303   1793    956   2431       C  
ATOM   3042  OD1 ASP A 415      -4.271  66.432  24.772  1.00141.53           O  
ANISOU 3042  OD1 ASP A 415    13590  19959  20226   1634    903   2544       O  
ATOM   3043  OD2 ASP A 415      -3.656  68.316  25.719  1.00139.28           O1-
ANISOU 3043  OD2 ASP A 415    13565  19666  19690   1987   1145   2411       O1-
ATOM   3044  N   GLU A 416      -2.762  64.252  23.559  1.00133.24           N  
ANISOU 3044  N   GLU A 416    12613  18744  19270   1192    577   2494       N  
ATOM   3045  CA  GLU A 416      -2.466  62.998  24.226  1.00115.63           C  
ANISOU 3045  CA  GLU A 416    10363  16504  17068   1027    621   2552       C  
ATOM   3046  C   GLU A 416      -1.622  62.125  23.317  1.00102.14           C  
ANISOU 3046  C   GLU A 416     8724  14683  15400    830    413   2489       C  
ATOM   3047  O   GLU A 416      -0.402  62.054  23.477  1.00 96.29           O  
ANISOU 3047  O   GLU A 416     8151  13877  14556    822    437   2401       O  
ATOM   3048  N   LEU A 417      -2.270  61.473  22.354  1.00 95.15           N  
ANISOU 3048  N   LEU A 417     7717  13773  14664    676    205   2529       N  
ATOM   3049  CA  LEU A 417      -1.580  60.490  21.527  1.00 94.94           C  
ANISOU 3049  CA  LEU A 417     7754  13634  14684    474     -1   2474       C  
ATOM   3050  C   LEU A 417      -0.639  61.113  20.528  1.00 86.88           C  
ANISOU 3050  C   LEU A 417     6896  12536  13578    517   -134   2338       C  
ATOM   3051  O   LEU A 417       0.445  60.575  20.278  1.00 79.24           O  
ANISOU 3051  O   LEU A 417     6058  11478  12571    419   -206   2261       O  
ATOM   3052  CB  LEU A 417      -2.567  59.608  20.774  1.00103.44           C  
ANISOU 3052  CB  LEU A 417     8672  14695  15935    297   -199   2547       C  
ATOM   3053  CG  LEU A 417      -3.008  58.333  21.480  1.00112.15           C  
ANISOU 3053  CG  LEU A 417     9668  15800  17144    135   -159   2663       C  
ATOM   3054  CD1 LEU A 417      -3.244  57.249  20.444  1.00112.13           C  
ANISOU 3054  CD1 LEU A 417     9629  15701  17274    -87   -425   2660       C  
ATOM   3055  CD2 LEU A 417      -1.987  57.889  22.523  1.00112.26           C  
ANISOU 3055  CD2 LEU A 417     9806  15788  17061    122      3   2650       C  
ATOM   3056  N   GLU A 418      -1.056  62.233  19.943  1.00 83.99           N  
ANISOU 3056  N   GLU A 418     6523  12202  13189    665   -171   2312       N  
ATOM   3057  CA  GLU A 418      -0.283  62.820  18.865  1.00 78.62           C  
ANISOU 3057  CA  GLU A 418     5989  11445  12437    702   -323   2200       C  
ATOM   3058  C   GLU A 418       1.051  63.328  19.380  1.00 84.22           C  
ANISOU 3058  C   GLU A 418     6961  12089  12951    788   -185   2074       C  
ATOM   3059  O   GLU A 418       2.077  63.149  18.723  1.00 88.90           O  
ANISOU 3059  O   GLU A 418     7785  12556  13434    705   -292   1936       O  
ATOM   3060  CB  GLU A 418      -1.047  63.942  18.176  1.00 81.56           C  
ANISOU 3060  CB  GLU A 418     6319  11856  12813    848   -386   2204       C  
ATOM   3061  CG  GLU A 418      -0.370  64.403  16.890  1.00 88.87           C  
ANISOU 3061  CG  GLU A 418     7412  12689  13664    852   -581   2095       C  
ATOM   3062  CD  GLU A 418      -0.194  63.285  15.857  1.00 87.74           C  
ANISOU 3062  CD  GLU A 418     7300  12460  13575    626   -831   2055       C  
ATOM   3063  OE1 GLU A 418       0.788  63.353  15.083  1.00 81.27           O  
ANISOU 3063  OE1 GLU A 418     6742  11524  12612    586   -929   1909       O  
ATOM   3064  OE2 GLU A 418      -1.038  62.359  15.804  1.00 87.66           O1-
ANISOU 3064  OE2 GLU A 418     7101  12483  13722    488   -920   2146       O1-
ATOM   3065  N   LYS A 419       1.050  63.948  20.554  1.00 83.34           N  
ANISOU 3065  N   LYS A 419     6845  12047  12773    947     51   2105       N  
ATOM   3066  CA  LYS A 419       2.312  64.367  21.156  1.00 83.15           C  
ANISOU 3066  CA  LYS A 419     7096  11945  12550   1009    179   1973       C  
ATOM   3067  C   LYS A 419       3.151  63.137  21.490  1.00 87.47           C  
ANISOU 3067  C   LYS A 419     7729  12424  13080    826    168   1941       C  
ATOM   3068  O   LYS A 419       4.379  63.166  21.407  1.00 88.41           O  
ANISOU 3068  O   LYS A 419     8097  12436  13059    797    159   1804       O  
ATOM   3069  CB  LYS A 419       2.074  65.217  22.401  1.00 81.74           C  
ANISOU 3069  CB  LYS A 419     6897  11856  12303   1217    427   2013       C  
ATOM   3070  CG  LYS A 419       1.733  66.667  22.099  1.00 80.44           C  
ANISOU 3070  CG  LYS A 419     6773  11706  12085   1430    451   1979       C  
ATOM   3071  CD  LYS A 419       1.455  67.440  23.371  1.00 83.58           C  
ANISOU 3071  CD  LYS A 419     7153  12189  12415   1642    698   2016       C  
ATOM   3072  CE  LYS A 419       0.885  68.811  23.063  1.00 84.33           C  
ANISOU 3072  CE  LYS A 419     7262  12296  12484   1851    712   1997       C  
ATOM   3073  NZ  LYS A 419       0.139  69.358  24.228  1.00 81.03           N1+
ANISOU 3073  NZ  LYS A 419     6810  11958  12018   2008    921   2035       N1+
ATOM   3074  N   LEU A 420       2.479  62.046  21.833  1.00 89.53           N  
ANISOU 3074  N   LEU A 420     7778  12745  13496    701    162   2074       N  
ATOM   3075  CA  LEU A 420       3.168  60.809  22.180  1.00 90.90           C  
ANISOU 3075  CA  LEU A 420     8014  12850  13673    527    147   2062       C  
ATOM   3076  C   LEU A 420       3.864  60.166  20.969  1.00 90.71           C  
ANISOU 3076  C   LEU A 420     8137  12687  13643    363    -83   1945       C  
ATOM   3077  O   LEU A 420       5.004  59.713  21.065  1.00 94.69           O  
ANISOU 3077  O   LEU A 420     8840  13092  14047    295    -85   1842       O  
ATOM   3078  CB  LEU A 420       2.185  59.830  22.824  1.00 83.40           C  
ANISOU 3078  CB  LEU A 420     6788  11995  12906    430    194   2252       C  
ATOM   3079  CG  LEU A 420       2.708  58.458  23.240  1.00 81.68           C  
ANISOU 3079  CG  LEU A 420     6599  11710  12725    244    177   2275       C  
ATOM   3080  CD1 LEU A 420       4.055  58.551  23.928  1.00 79.87           C  
ANISOU 3080  CD1 LEU A 420     6635  11410  12302    285    292   2155       C  
ATOM   3081  CD2 LEU A 420       1.707  57.802  24.175  1.00 87.39           C  
ANISOU 3081  CD2 LEU A 420     7145  12515  13543    198    291   2439       C  
ATOM   3082  N   ALA A 421       3.191  60.132  19.829  1.00 80.50           N  
ANISOU 3082  N   ALA A 421     6750  11388  12450    309   -277   1960       N  
ATOM   3083  CA  ALA A 421       3.794  59.545  18.646  1.00 62.96           C  
ANISOU 3083  CA  ALA A 421     4675   9038  10208    169   -495   1846       C  
ATOM   3084  C   ALA A 421       4.934  60.418  18.162  1.00 70.12           C  
ANISOU 3084  C   ALA A 421     5865   9863  10915    261   -490   1677       C  
ATOM   3085  O   ALA A 421       5.900  59.936  17.560  1.00 70.76           O  
ANISOU 3085  O   ALA A 421     6136   9830  10918    168   -586   1558       O  
ATOM   3086  CB  ALA A 421       2.765  59.365  17.567  1.00 60.84           C  
ANISOU 3086  CB  ALA A 421     4246   8788  10083    101   -710   1902       C  
ATOM   3087  N   ASN A 422       4.818  61.714  18.443  1.00 75.39           N  
ANISOU 3087  N   ASN A 422     6557  10585  11501    446   -371   1671       N  
ATOM   3088  CA  ASN A 422       5.814  62.687  18.014  1.00 73.36           C  
ANISOU 3088  CA  ASN A 422     6554  10253  11067    540   -359   1529       C  
ATOM   3089  C   ASN A 422       7.087  62.568  18.832  1.00 71.90           C  
ANISOU 3089  C   ASN A 422     6559  10009  10753    538   -225   1442       C  
ATOM   3090  O   ASN A 422       8.189  62.535  18.289  1.00 71.27           O  
ANISOU 3090  O   ASN A 422     6688   9827  10565    493   -280   1318       O  
ATOM   3091  CB  ASN A 422       5.263  64.104  18.122  1.00 72.28           C  
ANISOU 3091  CB  ASN A 422     6386  10181  10896    740   -277   1555       C  
ATOM   3092  CG  ASN A 422       6.231  65.143  17.590  1.00 69.93           C  
ANISOU 3092  CG  ASN A 422     6345   9795  10430    826   -282   1421       C  
ATOM   3093  ND2 ASN A 422       6.977  65.781  18.488  1.00 60.58           N  
ANISOU 3093  ND2 ASN A 422     5298   8592   9129    925   -115   1366       N  
ATOM   3094  OD1 ASN A 422       6.313  65.363  16.382  1.00 72.96           O  
ANISOU 3094  OD1 ASN A 422     6807  10127  10788    800   -440   1371       O  
ATOM   3095  N   ALA A 423       6.922  62.516  20.146  1.00 69.34           N  
ANISOU 3095  N   ALA A 423     6157   9753  10438    593    -45   1514       N  
ATOM   3096  CA  ALA A 423       8.038  62.277  21.044  1.00 64.90           C  
ANISOU 3096  CA  ALA A 423     5750   9144   9767    583     74   1450       C  
ATOM   3097  C   ALA A 423       8.769  61.017  20.626  1.00 73.04           C  
ANISOU 3097  C   ALA A 423     6852  10081  10817    400    -40   1399       C  
ATOM   3098  O   ALA A 423       9.978  61.036  20.422  1.00 82.73           O  
ANISOU 3098  O   ALA A 423     8285  11216  11931    378    -54   1278       O  
ATOM   3099  CB  ALA A 423       7.553  62.160  22.473  1.00 66.51           C  
ANISOU 3099  CB  ALA A 423     5828   9446   9995    646    262   1560       C  
ATOM   3100  N   VAL A 424       8.023  59.928  20.466  1.00 72.74           N  
ANISOU 3100  N   VAL A 424     6643  10062  10932    270   -129   1494       N  
ATOM   3101  CA  VAL A 424       8.617  58.638  20.123  1.00 68.81           C  
ANISOU 3101  CA  VAL A 424     6207   9469  10471     98   -241   1454       C  
ATOM   3102  C   VAL A 424       9.251  58.652  18.730  1.00 64.22           C  
ANISOU 3102  C   VAL A 424     5789   8783   9828     47   -415   1319       C  
ATOM   3103  O   VAL A 424      10.365  58.180  18.544  1.00 63.07           O  
ANISOU 3103  O   VAL A 424     5815   8543   9605    -11   -440   1216       O  
ATOM   3104  CB  VAL A 424       7.571  57.503  20.195  1.00 67.39           C  
ANISOU 3104  CB  VAL A 424     5800   9322  10484    -37   -317   1593       C  
ATOM   3105  CG1 VAL A 424       8.167  56.213  19.670  1.00 68.40           C  
ANISOU 3105  CG1 VAL A 424     6013   9326  10650   -211   -462   1535       C  
ATOM   3106  CG2 VAL A 424       7.083  57.320  21.623  1.00 54.86           C  
ANISOU 3106  CG2 VAL A 424     4063   7833   8947     -3   -129   1734       C  
ATOM   3107  N   GLY A 425       8.541  59.198  17.752  1.00 64.05           N  
ANISOU 3107  N   GLY A 425     5715   8785   9837     78   -531   1325       N  
ATOM   3108  CA  GLY A 425       9.067  59.269  16.401  1.00 58.58           C  
ANISOU 3108  CA  GLY A 425     5182   8006   9071     42   -692   1206       C  
ATOM   3109  C   GLY A 425      10.321  60.119  16.297  1.00 58.03           C  
ANISOU 3109  C   GLY A 425     5346   7882   8820    131   -612   1080       C  
ATOM   3110  O   GLY A 425      11.377  59.615  15.947  1.00 62.71           O  
ANISOU 3110  O   GLY A 425     6100   8386   9340     67   -646    980       O  
ATOM   3111  N   ILE A 426      10.209  61.408  16.605  1.00 62.91           N  
ANISOU 3111  N   ILE A 426     5980   8551   9373    280   -506   1089       N  
ATOM   3112  CA  ILE A 426      11.345  62.318  16.492  1.00 57.99           C  
ANISOU 3112  CA  ILE A 426     5571   7873   8591    359   -438    980       C  
ATOM   3113  C   ILE A 426      12.433  61.896  17.482  1.00 55.18           C  
ANISOU 3113  C   ILE A 426     5309   7479   8177    333   -316    935       C  
ATOM   3114  O   ILE A 426      13.625  61.950  17.170  1.00 60.04           O  
ANISOU 3114  O   ILE A 426     6102   8017   8691    314   -317    832       O  
ATOM   3115  CB  ILE A 426      10.941  63.805  16.741  1.00 44.93           C  
ANISOU 3115  CB  ILE A 426     3913   6270   6890    529   -349   1005       C  
ATOM   3116  CG1 ILE A 426       9.783  64.226  15.841  1.00 50.61           C  
ANISOU 3116  CG1 ILE A 426     4517   7035   7678    567   -470   1066       C  
ATOM   3117  CG2 ILE A 426      12.095  64.722  16.429  1.00 46.60           C  
ANISOU 3117  CG2 ILE A 426     4347   6406   6951    587   -313    897       C  
ATOM   3118  CD1 ILE A 426      10.101  64.104  14.362  1.00 54.61           C  
ANISOU 3118  CD1 ILE A 426     5141   7474   8135    500   -646    994       C  
ATOM   3119  N   GLY A 427      12.023  61.451  18.666  1.00 50.99           N  
ANISOU 3119  N   GLY A 427     4655   7006   7714    332   -213   1020       N  
ATOM   3120  CA  GLY A 427      12.968  60.947  19.648  1.00 46.06           C  
ANISOU 3120  CA  GLY A 427     4108   6350   7041    302   -111    992       C  
ATOM   3121  C   GLY A 427      13.829  59.835  19.081  1.00 53.47           C  
ANISOU 3121  C   GLY A 427     5141   7195   7981    168   -211    919       C  
ATOM   3122  O   GLY A 427      15.056  59.864  19.215  1.00 60.86           O  
ANISOU 3122  O   GLY A 427     6233   8069   8822    167   -173    830       O  
ATOM   3123  N   ALA A 428      13.185  58.860  18.439  1.00 49.36           N  
ANISOU 3123  N   ALA A 428     4524   6660   7570     58   -345    957       N  
ATOM   3124  CA  ALA A 428      13.898  57.778  17.767  1.00 46.16           C  
ANISOU 3124  CA  ALA A 428     4213   6155   7169    -61   -458    881       C  
ATOM   3125  C   ALA A 428      14.908  58.280  16.714  1.00 49.17           C  
ANISOU 3125  C   ALA A 428     4791   6468   7422    -35   -509    747       C  
ATOM   3126  O   ALA A 428      16.061  57.824  16.695  1.00 52.18           O  
ANISOU 3126  O   ALA A 428     5304   6778   7744    -68   -495    664       O  
ATOM   3127  CB  ALA A 428      12.924  56.843  17.149  1.00 39.17           C  
ANISOU 3127  CB  ALA A 428     3201   5261   6420   -172   -612    938       C  
ATOM   3128  N   VAL A 429      14.501  59.218  15.857  1.00 40.73           N  
ANISOU 3128  N   VAL A 429     3740   5423   6312     28   -562    733       N  
ATOM   3129  CA  VAL A 429      15.423  59.759  14.849  1.00 52.54           C  
ANISOU 3129  CA  VAL A 429     5421   6862   7681     56   -598    622       C  
ATOM   3130  C   VAL A 429      16.698  60.296  15.494  1.00 55.35           C  
ANISOU 3130  C   VAL A 429     5906   7191   7934    110   -459    561       C  
ATOM   3131  O   VAL A 429      17.812  59.909  15.129  1.00 61.15           O  
ANISOU 3131  O   VAL A 429     6769   7859   8604     73   -466    475       O  
ATOM   3132  CB  VAL A 429      14.784  60.896  14.011  1.00 59.98           C  
ANISOU 3132  CB  VAL A 429     6365   7840   8584    138   -650    635       C  
ATOM   3133  CG1 VAL A 429      15.827  61.537  13.071  1.00 52.15           C  
ANISOU 3133  CG1 VAL A 429     5572   6792   7449    171   -660    534       C  
ATOM   3134  CG2 VAL A 429      13.575  60.384  13.240  1.00 55.69           C  
ANISOU 3134  CG2 VAL A 429     5701   7320   8139     81   -815    688       C  
ATOM   3135  N   LYS A 430      16.520  61.175  16.470  1.00 57.27           N  
ANISOU 3135  N   LYS A 430     6110   7486   8164    200   -336    607       N  
ATOM   3136  CA  LYS A 430      17.640  61.801  17.150  1.00 47.24           C  
ANISOU 3136  CA  LYS A 430     4956   6191   6801    253   -218    555       C  
ATOM   3137  C   LYS A 430      18.433  60.776  17.947  1.00 44.75           C  
ANISOU 3137  C   LYS A 430     4657   5843   6501    185   -174    537       C  
ATOM   3138  O   LYS A 430      19.646  60.595  17.757  1.00 43.93           O  
ANISOU 3138  O   LYS A 430     4675   5680   6338    159   -166    458       O  
ATOM   3139  CB  LYS A 430      17.132  62.899  18.078  1.00 45.53           C  
ANISOU 3139  CB  LYS A 430     4696   6034   6571    368   -108    607       C  
ATOM   3140  CG  LYS A 430      16.332  63.985  17.379  1.00 36.54           C  
ANISOU 3140  CG  LYS A 430     3539   4922   5422    453   -145    631       C  
ATOM   3141  CD  LYS A 430      15.916  65.123  18.336  1.00 37.67           C  
ANISOU 3141  CD  LYS A 430     3660   5111   5543    587    -27    670       C  
ATOM   3142  CE  LYS A 430      17.080  66.101  18.597  1.00 43.69           C  
ANISOU 3142  CE  LYS A 430     4597   5810   6192    641     43    590       C  
ATOM   3143  NZ  LYS A 430      16.728  67.278  19.477  1.00 50.37           N1+
ANISOU 3143  NZ  LYS A 430     5455   6680   7004    779    146    610       N1+
ATOM   3144  N   TYR A 431      17.733  60.089  18.842  1.00 41.10           N  
ANISOU 3144  N   TYR A 431     4066   5425   6126    159   -145    621       N  
ATOM   3145  CA  TYR A 431      18.402  59.194  19.771  1.00 47.86           C  
ANISOU 3145  CA  TYR A 431     4933   6256   6995    108    -93    624       C  
ATOM   3146  C   TYR A 431      19.117  58.045  19.058  1.00 47.11           C  
ANISOU 3146  C   TYR A 431     4902   6077   6919      7   -188    560       C  
ATOM   3147  O   TYR A 431      20.177  57.606  19.503  1.00 51.75           O  
ANISOU 3147  O   TYR A 431     5566   6619   7476    -13   -151    516       O  
ATOM   3148  CB  TYR A 431      17.402  58.656  20.784  1.00 54.61           C  
ANISOU 3148  CB  TYR A 431     5631   7177   7942     96    -45    744       C  
ATOM   3149  CG  TYR A 431      18.033  58.058  22.014  1.00 51.52           C  
ANISOU 3149  CG  TYR A 431     5259   6779   7539     79     42    765       C  
ATOM   3150  CD1 TYR A 431      18.455  56.733  22.030  1.00 34.83           C  
ANISOU 3150  CD1 TYR A 431     3149   4603   5482    -26    -13    765       C  
ATOM   3151  CD2 TYR A 431      18.186  58.810  23.168  1.00 51.50           C  
ANISOU 3151  CD2 TYR A 431     5277   6826   7464    174    172    786       C  
ATOM   3152  CE1 TYR A 431      19.020  56.179  23.150  1.00 41.03           C  
ANISOU 3152  CE1 TYR A 431     3954   5380   6255    -37     58    792       C  
ATOM   3153  CE2 TYR A 431      18.759  58.262  24.298  1.00 55.49           C  
ANISOU 3153  CE2 TYR A 431     5808   7328   7947    161    241    808       C  
ATOM   3154  CZ  TYR A 431      19.173  56.946  24.283  1.00 52.85           C  
ANISOU 3154  CZ  TYR A 431     5471   6935   7673     55    184    816       C  
ATOM   3155  OH  TYR A 431      19.734  56.405  25.413  1.00 54.25           O  
ANISOU 3155  OH  TYR A 431     5677   7109   7827     48    248    847       O  
ATOM   3156  N   ALA A 432      18.558  57.564  17.950  1.00 40.51           N  
ANISOU 3156  N   ALA A 432     4041   5218   6133    -51   -315    552       N  
ATOM   3157  CA  ALA A 432      19.242  56.514  17.179  1.00 43.45           C  
ANISOU 3157  CA  ALA A 432     4498   5503   6510   -132   -409    476       C  
ATOM   3158  C   ALA A 432      20.579  57.010  16.664  1.00 46.79           C  
ANISOU 3158  C   ALA A 432     5081   5882   6815    -92   -377    367       C  
ATOM   3159  O   ALA A 432      21.528  56.248  16.546  1.00 53.53           O  
ANISOU 3159  O   ALA A 432     6013   6671   7656   -128   -386    306       O  
ATOM   3160  CB  ALA A 432      18.376  56.026  16.012  1.00 38.69           C  
ANISOU 3160  CB  ALA A 432     3859   4880   5963   -193   -566    474       C  
ATOM   3161  N   ASP A 433      20.649  58.298  16.358  1.00 50.76           N  
ANISOU 3161  N   ASP A 433     5630   6418   7238    -14   -336    351       N  
ATOM   3162  CA  ASP A 433      21.900  58.910  15.939  1.00 50.61           C  
ANISOU 3162  CA  ASP A 433     5749   6365   7113     22   -290    268       C  
ATOM   3163  C   ASP A 433      22.778  59.161  17.161  1.00 47.29           C  
ANISOU 3163  C   ASP A 433     5350   5947   6672     50   -175    267       C  
ATOM   3164  O   ASP A 433      23.881  58.615  17.253  1.00 49.29           O  
ANISOU 3164  O   ASP A 433     5667   6154   6909     24   -157    215       O  
ATOM   3165  CB  ASP A 433      21.627  60.213  15.182  1.00 60.56           C  
ANISOU 3165  CB  ASP A 433     7054   7651   8304     89   -295    262       C  
ATOM   3166  CG  ASP A 433      22.792  60.650  14.318  1.00 61.04           C  
ANISOU 3166  CG  ASP A 433     7257   7670   8264    102   -280    182       C  
ATOM   3167  OD1 ASP A 433      23.953  60.470  14.726  1.00 58.84           O  
ANISOU 3167  OD1 ASP A 433     7034   7362   7962     93   -216    141       O  
ATOM   3168  OD2 ASP A 433      22.539  61.183  13.224  1.00 70.86           O1-
ANISOU 3168  OD2 ASP A 433     8554   8917   9454    123   -334    169       O1-
ATOM   3169  N   LEU A 434      22.288  59.969  18.104  1.00 37.66           N  
ANISOU 3169  N   LEU A 434     4079   4780   5452    109   -101    324       N  
ATOM   3170  CA  LEU A 434      23.051  60.290  19.322  1.00 27.45           C  
ANISOU 3170  CA  LEU A 434     2815   3489   4126    142     -2    322       C  
ATOM   3171  C   LEU A 434      23.606  59.064  20.088  1.00 30.19           C  
ANISOU 3171  C   LEU A 434     3145   3810   4515     84      7    328       C  
ATOM   3172  O   LEU A 434      24.744  59.079  20.538  1.00 37.46           O  
ANISOU 3172  O   LEU A 434     4133   4701   5398     87     46    286       O  
ATOM   3173  CB  LEU A 434      22.178  61.120  20.260  1.00 36.27           C  
ANISOU 3173  CB  LEU A 434     3870   4670   5241    218     67    389       C  
ATOM   3174  CG  LEU A 434      21.710  62.512  19.790  1.00 39.98           C  
ANISOU 3174  CG  LEU A 434     4368   5159   5665    300     77    387       C  
ATOM   3175  CD1 LEU A 434      20.618  63.075  20.669  1.00 32.60           C  
ANISOU 3175  CD1 LEU A 434     3347   4293   4747    381    140    462       C  
ATOM   3176  CD2 LEU A 434      22.864  63.479  19.716  1.00 45.10           C  
ANISOU 3176  CD2 LEU A 434     5147   5759   6228    331    113    318       C  
ATOM   3177  N   SER A 435      22.824  57.998  20.229  1.00 34.50           N  
ANISOU 3177  N   SER A 435     3599   4362   5147     29    -37    385       N  
ATOM   3178  CA  SER A 435      23.271  56.821  20.989  1.00 39.08           C  
ANISOU 3178  CA  SER A 435     4165   4911   5774    -24    -32    405       C  
ATOM   3179  C   SER A 435      24.482  56.129  20.369  1.00 49.91           C  
ANISOU 3179  C   SER A 435     5627   6203   7134    -63    -75    318       C  
ATOM   3180  O   SER A 435      25.200  55.385  21.042  1.00 56.06           O  
ANISOU 3180  O   SER A 435     6422   6949   7931    -84    -59    318       O  
ATOM   3181  CB  SER A 435      22.139  55.820  21.120  1.00 45.39           C  
ANISOU 3181  CB  SER A 435     4846   5721   6680    -88    -81    491       C  
ATOM   3182  OG  SER A 435      21.730  55.377  19.835  1.00 59.62           O  
ANISOU 3182  OG  SER A 435     6646   7484   8523   -140   -196    458       O  
ATOM   3183  N   LYS A 436      24.701  56.357  19.081  1.00 52.62           N  
ANISOU 3183  N   LYS A 436     6032   6519   7444    -64   -129    249       N  
ATOM   3184  CA  LYS A 436      25.883  55.807  18.429  1.00 53.29           C  
ANISOU 3184  CA  LYS A 436     6206   6538   7505    -81   -151    163       C  
ATOM   3185  C   LYS A 436      27.028  56.816  18.351  1.00 53.96           C  
ANISOU 3185  C   LYS A 436     6370   6629   7505    -30    -82    110       C  
ATOM   3186  O   LYS A 436      26.830  58.003  18.103  1.00 52.02           O  
ANISOU 3186  O   LYS A 436     6143   6417   7205     12    -54    111       O  
ATOM   3187  CB  LYS A 436      25.546  55.311  17.041  1.00 34.18           C  
ANISOU 3187  CB  LYS A 436     3820   4080   5088   -113   -249    116       C  
ATOM   3188  CG  LYS A 436      24.572  54.183  17.011  1.00 34.09           C  
ANISOU 3188  CG  LYS A 436     3739   4040   5173   -181   -341    158       C  
ATOM   3189  CD  LYS A 436      24.209  53.893  15.565  1.00 42.51           C  
ANISOU 3189  CD  LYS A 436     4857   5071   6224   -204   -452     99       C  
ATOM   3190  CE  LYS A 436      23.187  52.789  15.465  1.00 43.30           C  
ANISOU 3190  CE  LYS A 436     4889   5132   6431   -285   -567    139       C  
ATOM   3191  NZ  LYS A 436      21.968  53.122  16.219  1.00 51.52           N1+
ANISOU 3191  NZ  LYS A 436     5788   6243   7545   -301   -555    255       N1+
ATOM   3192  N   ASN A 437      28.227  56.313  18.588  1.00 49.91           N  
ANISOU 3192  N   ASN A 437     5897   6076   6989    -35    -59     69       N  
ATOM   3193  CA  ASN A 437      29.412  57.128  18.600  1.00 46.58           C  
ANISOU 3193  CA  ASN A 437     5533   5656   6510     -1      1     27       C  
ATOM   3194  C   ASN A 437      29.493  57.881  17.290  1.00 50.71           C  
ANISOU 3194  C   ASN A 437     6116   6182   6970     17     -5    -15       C  
ATOM   3195  O   ASN A 437      29.304  57.311  16.214  1.00 49.70           O  
ANISOU 3195  O   ASN A 437     6018   6032   6835      3    -58    -51       O  
ATOM   3196  CB  ASN A 437      30.637  56.251  18.819  1.00 33.15           C  
ANISOU 3196  CB  ASN A 437     3852   3910   4833    -13      9    -10       C  
ATOM   3197  CG  ASN A 437      31.925  57.033  18.884  1.00 40.80           C  
ANISOU 3197  CG  ASN A 437     4858   4883   5760     13     67    -44       C  
ATOM   3198  ND2 ASN A 437      32.945  56.420  19.468  1.00 38.06           N  
ANISOU 3198  ND2 ASN A 437     4504   4512   5446     11     79    -55       N  
ATOM   3199  OD1 ASN A 437      32.020  58.163  18.399  1.00 56.17           O  
ANISOU 3199  OD1 ASN A 437     6837   6850   7653     32     96    -54       O  
ATOM   3200  N   ARG A 438      29.760  59.170  17.382  1.00 43.38           N  
ANISOU 3200  N   ARG A 438     5214   5278   5990     49     45    -10       N  
ATOM   3201  CA  ARG A 438      29.648  60.001  16.206  1.00 38.25           C  
ANISOU 3201  CA  ARG A 438     4619   4635   5279     68     41    -29       C  
ATOM   3202  C   ARG A 438      30.696  59.655  15.129  1.00 38.26           C  
ANISOU 3202  C   ARG A 438     4686   4610   5243     62     51    -89       C  
ATOM   3203  O   ARG A 438      30.466  59.860  13.958  1.00 28.05           O  
ANISOU 3203  O   ARG A 438     3443   3319   3895     72     28   -108       O  
ATOM   3204  CB  ARG A 438      29.735  61.472  16.604  1.00 25.03           C  
ANISOU 3204  CB  ARG A 438     2966   2976   3566    102     90     -5       C  
ATOM   3205  CG  ARG A 438      31.038  61.946  17.183  1.00 29.98           C  
ANISOU 3205  CG  ARG A 438     3619   3585   4185     99    147    -23       C  
ATOM   3206  CD  ARG A 438      31.050  63.517  17.370  1.00 36.10           C  
ANISOU 3206  CD  ARG A 438     4437   4359   4921    128    178     -4       C  
ATOM   3207  NE  ARG A 438      32.107  63.932  18.289  1.00 35.03           N  
ANISOU 3207  NE  ARG A 438     4312   4202   4795    117    212    -13       N  
ATOM   3208  CZ  ARG A 438      33.409  63.857  18.006  1.00 39.54           C  
ANISOU 3208  CZ  ARG A 438     4896   4753   5373     86    235    -38       C  
ATOM   3209  NH1 ARG A 438      33.824  63.397  16.814  1.00 28.36           N1+
ANISOU 3209  NH1 ARG A 438     3492   3338   3944     73    244    -58       N1+
ATOM   3210  NH2 ARG A 438      34.305  64.233  18.922  1.00 37.05           N  
ANISOU 3210  NH2 ARG A 438     4580   4419   5077     71    248    -42       N  
ATOM   3211  N   THR A 439      31.829  59.090  15.513  1.00 44.15           N  
ANISOU 3211  N   THR A 439     5428   5334   6013     53     85   -115       N  
ATOM   3212  CA  THR A 439      32.865  58.788  14.531  1.00 30.43           C  
ANISOU 3212  CA  THR A 439     3741   3580   4240     62    114   -168       C  
ATOM   3213  C   THR A 439      32.528  57.558  13.718  1.00 26.89           C  
ANISOU 3213  C   THR A 439     3321   3103   3792     60     54   -213       C  
ATOM   3214  O   THR A 439      33.232  57.210  12.794  1.00 47.36           O  
ANISOU 3214  O   THR A 439     5969   5683   6342     80     75   -263       O  
ATOM   3215  CB  THR A 439      34.241  58.598  15.205  1.00 34.24           C  
ANISOU 3215  CB  THR A 439     4198   4052   4760     62    170   -178       C  
ATOM   3216  CG2 THR A 439      34.903  59.932  15.466  1.00 30.25           C  
ANISOU 3216  CG2 THR A 439     3696   3564   4233     61    227   -153       C  
ATOM   3217  OG1 THR A 439      34.054  57.978  16.476  1.00 50.41           O  
ANISOU 3217  OG1 THR A 439     6190   6089   6876     47    144   -154       O  
ATOM   3218  N   THR A 440      31.431  56.901  14.037  1.00 39.58           N  
ANISOU 3218  N   THR A 440     4893   4698   5447     35    -21   -194       N  
ATOM   3219  CA  THR A 440      31.106  55.637  13.389  1.00 38.44           C  
ANISOU 3219  CA  THR A 440     4777   4507   5320     21    -97   -238       C  
ATOM   3220  C   THR A 440      30.086  55.846  12.285  1.00 50.37           C  
ANISOU 3220  C   THR A 440     6332   6027   6779     18   -171   -249       C  
ATOM   3221  O   THR A 440      29.204  56.705  12.385  1.00 61.84           O  
ANISOU 3221  O   THR A 440     7752   7520   8223     15   -187   -197       O  
ATOM   3222  CB  THR A 440      30.566  54.595  14.409  1.00 44.87           C  
ANISOU 3222  CB  THR A 440     5523   5288   6237    -20   -148   -205       C  
ATOM   3223  CG2 THR A 440      30.581  53.218  13.810  1.00 52.10           C  
ANISOU 3223  CG2 THR A 440     6482   6132   7181    -35   -221   -262       C  
ATOM   3224  OG1 THR A 440      31.406  54.575  15.570  1.00 51.11           O  
ANISOU 3224  OG1 THR A 440     6270   6080   7067    -14    -85   -180       O  
ATOM   3225  N   ASP A 441      30.215  55.076  11.213  1.00 47.97           N  
ANISOU 3225  N   ASP A 441     6108   5685   6434     26   -221   -318       N  
ATOM   3226  CA  ASP A 441      29.225  55.146  10.157  1.00 51.27           C  
ANISOU 3226  CA  ASP A 441     6575   6105   6799     20   -317   -333       C  
ATOM   3227  C   ASP A 441      27.943  54.568  10.740  1.00 43.35           C  
ANISOU 3227  C   ASP A 441     5488   5086   5899    -39   -420   -285       C  
ATOM   3228  O   ASP A 441      27.967  53.552  11.408  1.00 48.96           O  
ANISOU 3228  O   ASP A 441     6158   5749   6697    -73   -445   -283       O  
ATOM   3229  CB  ASP A 441      29.684  54.402   8.894  1.00 46.52           C  
ANISOU 3229  CB  ASP A 441     6097   5460   6117     48   -352   -427       C  
ATOM   3230  CG  ASP A 441      30.911  55.046   8.232  1.00 48.90           C  
ANISOU 3230  CG  ASP A 441     6474   5795   6312    111   -233   -459       C  
ATOM   3231  OD1 ASP A 441      31.174  56.272   8.389  1.00 44.74           O  
ANISOU 3231  OD1 ASP A 441     5924   5322   5753    124   -153   -406       O  
ATOM   3232  OD2 ASP A 441      31.642  54.301   7.554  1.00 56.87           O1-
ANISOU 3232  OD2 ASP A 441     7566   6769   7272    149   -218   -536       O1-
ATOM   3233  N   TYR A 442      26.835  55.257  10.511  1.00 50.11           N  
ANISOU 3233  N   TYR A 442     6308   5984   6748    -48   -474   -236       N  
ATOM   3234  CA  TYR A 442      25.598  54.995  11.224  1.00 47.39           C  
ANISOU 3234  CA  TYR A 442     5847   5648   6509    -98   -543   -163       C  
ATOM   3235  C   TYR A 442      24.636  54.316  10.302  1.00 50.40           C  
ANISOU 3235  C   TYR A 442     6248   5997   6904   -140   -696   -186       C  
ATOM   3236  O   TYR A 442      24.116  54.897   9.361  1.00 57.55           O  
ANISOU 3236  O   TYR A 442     7196   6930   7742   -121   -756   -194       O  
ATOM   3237  CB  TYR A 442      25.025  56.304  11.787  1.00 29.26           C  
ANISOU 3237  CB  TYR A 442     3476   3428   4212    -69   -487    -82       C  
ATOM   3238  CG  TYR A 442      23.552  56.318  12.119  1.00 47.07           C  
ANISOU 3238  CG  TYR A 442     5615   5717   6552   -100   -562     -3       C  
ATOM   3239  CD1 TYR A 442      22.918  55.218  12.685  1.00 46.26           C  
ANISOU 3239  CD1 TYR A 442     5425   5587   6564   -167   -624     34       C  
ATOM   3240  CD2 TYR A 442      22.799  57.471  11.918  1.00 48.26           C  
ANISOU 3240  CD2 TYR A 442     5734   5928   6675    -59   -563     47       C  
ATOM   3241  CE1 TYR A 442      21.573  55.255  12.999  1.00 53.11           C  
ANISOU 3241  CE1 TYR A 442     6166   6495   7518   -197   -682    121       C  
ATOM   3242  CE2 TYR A 442      21.455  57.510  12.234  1.00 49.58           C  
ANISOU 3242  CE2 TYR A 442     5777   6136   6927    -77   -622    127       C  
ATOM   3243  CZ  TYR A 442      20.854  56.407  12.771  1.00 54.73           C  
ANISOU 3243  CZ  TYR A 442     6332   6768   7693   -148   -678    166       C  
ATOM   3244  OH  TYR A 442      19.526  56.468  13.075  1.00 71.75           O  
ANISOU 3244  OH  TYR A 442     8347   8973   9941   -167   -728    257       O  
ATOM   3245  N   ILE A 443      24.401  53.052  10.576  1.00 59.43           N  
ANISOU 3245  N   ILE A 443     7366   7074   8139   -200   -772   -195       N  
ATOM   3246  CA  ILE A 443      23.516  52.306   9.733  1.00 56.80           C  
ANISOU 3246  CA  ILE A 443     7056   6694   7831   -253   -937   -222       C  
ATOM   3247  C   ILE A 443      22.114  52.424  10.289  1.00 62.61           C  
ANISOU 3247  C   ILE A 443     7636   7470   8681   -310  -1004   -115       C  
ATOM   3248  O   ILE A 443      21.762  51.768  11.267  1.00 63.88           O  
ANISOU 3248  O   ILE A 443     7694   7613   8966   -367  -1003    -50       O  
ATOM   3249  CB  ILE A 443      23.979  50.862   9.613  1.00 55.85           C  
ANISOU 3249  CB  ILE A 443     7004   6464   7753   -289   -999   -294       C  
ATOM   3250  CG1 ILE A 443      25.315  50.857   8.851  1.00 49.89           C  
ANISOU 3250  CG1 ILE A 443     6405   5685   6868   -211   -929   -404       C  
ATOM   3251  CG2 ILE A 443      22.912  49.997   8.908  1.00 47.74           C  
ANISOU 3251  CG2 ILE A 443     5987   5372   6782   -366  -1196   -313       C  
ATOM   3252  CD1 ILE A 443      25.937  49.499   8.699  1.00 56.69           C  
ANISOU 3252  CD1 ILE A 443     7351   6435   7756   -219   -971   -488       C  
ATOM   3253  N   PHE A 444      21.348  53.321   9.666  1.00 58.89           N  
ANISOU 3253  N   PHE A 444     7149   7060   8166   -288  -1051    -88       N  
ATOM   3254  CA  PHE A 444      19.927  53.483   9.921  1.00 55.01           C  
ANISOU 3254  CA  PHE A 444     6508   6614   7778   -332  -1133     10       C  
ATOM   3255  C   PHE A 444      19.184  52.159   9.877  1.00 57.01           C  
ANISOU 3255  C   PHE A 444     6707   6796   8157   -438  -1286     21       C  
ATOM   3256  O   PHE A 444      19.535  51.277   9.103  1.00 50.71           O  
ANISOU 3256  O   PHE A 444     6030   5908   7330   -468  -1385    -73       O  
ATOM   3257  CB  PHE A 444      19.307  54.424   8.904  1.00 56.09           C  
ANISOU 3257  CB  PHE A 444     6672   6802   7835   -290  -1205     11       C  
ATOM   3258  CG  PHE A 444      17.987  54.971   9.335  1.00 64.57           C  
ANISOU 3258  CG  PHE A 444     7574   7951   9007   -299  -1239    127       C  
ATOM   3259  CD1 PHE A 444      16.814  54.277   9.079  1.00 65.54           C  
ANISOU 3259  CD1 PHE A 444     7597   8061   9243   -382  -1404    171       C  
ATOM   3260  CD2 PHE A 444      17.916  56.170  10.013  1.00 63.94           C  
ANISOU 3260  CD2 PHE A 444     7429   7952   8912   -224  -1107    195       C  
ATOM   3261  CE1 PHE A 444      15.603  54.773   9.485  1.00 64.58           C  
ANISOU 3261  CE1 PHE A 444     7298   8018   9223   -385  -1426    287       C  
ATOM   3262  CE2 PHE A 444      16.704  56.673  10.420  1.00 64.25           C  
ANISOU 3262  CE2 PHE A 444     7307   8064   9041   -215  -1127    302       C  
ATOM   3263  CZ  PHE A 444      15.544  55.978  10.156  1.00 62.52           C  
ANISOU 3263  CZ  PHE A 444     6972   7844   8938   -294  -1281    352       C  
ATOM   3264  N   ASP A 445      18.135  52.058  10.693  1.00 56.38           N  
ANISOU 3264  N   ASP A 445     6448   6756   8218   -493  -1302    140       N  
ATOM   3265  CA  ASP A 445      17.403  50.822  10.925  1.00 51.78           C  
ANISOU 3265  CA  ASP A 445     5779   6109   7787   -609  -1426    183       C  
ATOM   3266  C   ASP A 445      16.117  51.150  11.665  1.00 58.85           C  
ANISOU 3266  C   ASP A 445     6455   7090   8814   -644  -1423    334       C  
ATOM   3267  O   ASP A 445      16.147  51.409  12.862  1.00 70.39           O  
ANISOU 3267  O   ASP A 445     7817   8608  10319   -622  -1278    420       O  
ATOM   3268  CB  ASP A 445      18.242  49.844  11.747  1.00 60.82           C  
ANISOU 3268  CB  ASP A 445     6955   7175   8977   -641  -1357    169       C  
ATOM   3269  CG  ASP A 445      17.693  48.429  11.722  1.00 64.70           C  
ANISOU 3269  CG  ASP A 445     7413   7560   9610   -766  -1509    185       C  
ATOM   3270  OD1 ASP A 445      16.502  48.242  11.407  1.00 71.46           O  
ANISOU 3270  OD1 ASP A 445     8164   8423  10564   -844  -1647    245       O  
ATOM   3271  OD2 ASP A 445      18.459  47.495  12.031  1.00 65.83           O1-
ANISOU 3271  OD2 ASP A 445     7632   7607   9773   -789  -1494    141       O1-
ATOM   3272  N   TRP A 446      14.995  51.128  10.957  1.00 57.26           N  
ANISOU 3272  N   TRP A 446     6180   6903   8675   -694  -1583    366       N  
ATOM   3273  CA  TRP A 446      13.715  51.523  11.528  1.00 58.91           C  
ANISOU 3273  CA  TRP A 446     6165   7207   9010   -715  -1583    514       C  
ATOM   3274  C   TRP A 446      13.316  50.713  12.753  1.00 63.73           C  
ANISOU 3274  C   TRP A 446     6619   7814   9782   -798  -1530    632       C  
ATOM   3275  O   TRP A 446      12.749  51.235  13.719  1.00 69.07           O  
ANISOU 3275  O   TRP A 446     7133   8592  10520   -766  -1409    755       O  
ATOM   3276  CB  TRP A 446      12.622  51.383  10.486  1.00 60.91           C  
ANISOU 3276  CB  TRP A 446     6365   7456   9323   -776  -1801    524       C  
ATOM   3277  CG  TRP A 446      12.530  52.519   9.544  1.00 68.40           C  
ANISOU 3277  CG  TRP A 446     7384   8462  10142   -680  -1833    480       C  
ATOM   3278  CD1 TRP A 446      12.595  52.467   8.182  1.00 77.88           C  
ANISOU 3278  CD1 TRP A 446     8732   9613  11245   -681  -1997    377       C  
ATOM   3279  CD2 TRP A 446      12.325  53.888   9.883  1.00 64.71           C  
ANISOU 3279  CD2 TRP A 446     6851   8110   9626   -563  -1702    541       C  
ATOM   3280  CE2 TRP A 446      12.272  54.616   8.679  1.00 68.85           C  
ANISOU 3280  CE2 TRP A 446     7483   8647  10030   -503  -1797    479       C  
ATOM   3281  CE3 TRP A 446      12.162  54.568  11.090  1.00 62.11           C  
ANISOU 3281  CE3 TRP A 446     6391   7871   9338   -498  -1517    641       C  
ATOM   3282  NE1 TRP A 446      12.440  53.728   7.650  1.00 78.62           N  
ANISOU 3282  NE1 TRP A 446     8851   9788  11233   -576  -1975    380       N  
ATOM   3283  CZ2 TRP A 446      12.089  55.985   8.651  1.00 64.88           C  
ANISOU 3283  CZ2 TRP A 446     6960   8233   9458   -385  -1714    517       C  
ATOM   3284  CZ3 TRP A 446      11.973  55.923  11.055  1.00 61.15           C  
ANISOU 3284  CZ3 TRP A 446     6254   7835   9144   -376  -1438    668       C  
ATOM   3285  CH2 TRP A 446      11.936  56.619   9.847  1.00 64.88           C  
ANISOU 3285  CH2 TRP A 446     6833   8310   9510   -323  -1537    609       C  
ATOM   3286  N   ASP A 447      13.602  49.424  12.689  1.00 51.48           N  
ANISOU 3286  N   ASP A 447     5124   6141   8294   -900  -1621    595       N  
ATOM   3287  CA  ASP A 447      13.025  48.487  13.615  1.00 58.46           C  
ANISOU 3287  CA  ASP A 447     5856   7001   9353  -1009  -1625    718       C  
ATOM   3288  C   ASP A 447      13.861  48.441  14.873  1.00 64.00           C  
ANISOU 3288  C   ASP A 447     6573   7717  10028   -964  -1424    750       C  
ATOM   3289  O   ASP A 447      13.333  48.298  15.973  1.00 75.38           O  
ANISOU 3289  O   ASP A 447     7855   9214  11571   -994  -1332    891       O  
ATOM   3290  CB  ASP A 447      12.900  47.103  12.962  1.00 67.78           C  
ANISOU 3290  CB  ASP A 447     7097   8029  10627  -1146  -1833    667       C  
ATOM   3291  CG  ASP A 447      11.826  47.064  11.863  1.00 81.87           C  
ANISOU 3291  CG  ASP A 447     8828   9806  12473  -1216  -2058    665       C  
ATOM   3292  OD1 ASP A 447      10.710  47.594  12.084  1.00 84.12           O  
ANISOU 3292  OD1 ASP A 447     8909  10198  12853  -1229  -2065    792       O  
ATOM   3293  OD2 ASP A 447      12.098  46.514  10.772  1.00 88.97           O1-
ANISOU 3293  OD2 ASP A 447     9890  10592  13321  -1250  -2229    534       O1-
ATOM   3294  N   ASN A 448      15.169  48.582  14.724  1.00 55.80           N  
ANISOU 3294  N   ASN A 448     5722   6634   8847   -888  -1352    626       N  
ATOM   3295  CA  ASN A 448      16.007  48.642  15.898  1.00 55.56           C  
ANISOU 3295  CA  ASN A 448     5709   6623   8780   -836  -1172    653       C  
ATOM   3296  C   ASN A 448      15.697  49.912  16.693  1.00 66.29           C  
ANISOU 3296  C   ASN A 448     6965   8129  10094   -737  -1008    736       C  
ATOM   3297  O   ASN A 448      15.582  49.870  17.920  1.00 75.12           O  
ANISOU 3297  O   ASN A 448     7991   9298  11255   -731   -883    840       O  
ATOM   3298  CB  ASN A 448      17.488  48.577  15.522  1.00 59.20           C  
ANISOU 3298  CB  ASN A 448     6377   7010   9105   -772  -1135    504       C  
ATOM   3299  CG  ASN A 448      17.896  47.216  14.954  1.00 73.54           C  
ANISOU 3299  CG  ASN A 448     8303   8672  10967   -852  -1271    424       C  
ATOM   3300  ND2 ASN A 448      19.202  46.984  14.848  1.00 78.13           N  
ANISOU 3300  ND2 ASN A 448     9041   9190  11455   -795  -1219    316       N  
ATOM   3301  OD1 ASN A 448      17.050  46.394  14.611  1.00 79.25           O  
ANISOU 3301  OD1 ASN A 448     8970   9331  11811   -961  -1423    458       O  
ATOM   3302  N   MET A 449      15.515  51.028  15.995  1.00 62.34           N  
ANISOU 3302  N   MET A 449     6486   7693   9506   -657  -1011    693       N  
ATOM   3303  CA  MET A 449      15.417  52.321  16.654  1.00 66.51           C  
ANISOU 3303  CA  MET A 449     6962   8340   9968   -543   -856    741       C  
ATOM   3304  C   MET A 449      14.047  52.580  17.285  1.00 73.65           C  
ANISOU 3304  C   MET A 449     7649   9348  10988   -551   -827    896       C  
ATOM   3305  O   MET A 449      13.946  53.255  18.320  1.00 78.95           O  
ANISOU 3305  O   MET A 449     8254  10107  11635   -471   -668    967       O  
ATOM   3306  CB  MET A 449      15.759  53.426  15.662  1.00 71.04           C  
ANISOU 3306  CB  MET A 449     7649   8934  10410   -453   -871    645       C  
ATOM   3307  CG  MET A 449      14.792  53.536  14.498  1.00 72.62           C  
ANISOU 3307  CG  MET A 449     7806   9142  10646   -483  -1036    645       C  
ATOM   3308  SD  MET A 449      15.289  54.832  13.361  1.00 46.74           S  
ANISOU 3308  SD  MET A 449     4681   5883   7195   -373  -1043    541       S  
ATOM   3309  CE  MET A 449      17.006  54.418  13.017  1.00 36.83           C  
ANISOU 3309  CE  MET A 449     3652   4529   5811   -364  -1003    394       C  
ATOM   3310  N   LEU A 450      12.998  52.033  16.680  1.00 64.33           N  
ANISOU 3310  N   LEU A 450     6354   8155   9931   -644   -979    949       N  
ATOM   3311  CA  LEU A 450      11.650  52.197  17.216  1.00 61.61           C  
ANISOU 3311  CA  LEU A 450     5777   7913   9718   -659   -959   1108       C  
ATOM   3312  C   LEU A 450      11.275  51.100  18.216  1.00 60.84           C  
ANISOU 3312  C   LEU A 450     5551   7802   9763   -764   -926   1234       C  
ATOM   3313  O   LEU A 450      10.118  50.971  18.597  1.00 61.89           O  
ANISOU 3313  O   LEU A 450     5474   8008  10033   -808   -926   1380       O  
ATOM   3314  CB  LEU A 450      10.634  52.237  16.073  1.00 62.65           C  
ANISOU 3314  CB  LEU A 450     5827   8051   9927   -708  -1148   1118       C  
ATOM   3315  CG  LEU A 450      10.534  53.603  15.390  1.00 62.55           C  
ANISOU 3315  CG  LEU A 450     5858   8105   9802   -580  -1142   1067       C  
ATOM   3316  CD1 LEU A 450       9.618  53.563  14.195  1.00 60.09           C  
ANISOU 3316  CD1 LEU A 450     5486   7789   9555   -631  -1352   1068       C  
ATOM   3317  CD2 LEU A 450      10.045  54.627  16.390  1.00 63.97           C  
ANISOU 3317  CD2 LEU A 450     5907   8416   9980   -461   -959   1171       C  
ATOM   3318  N   ALA A 451      12.264  50.316  18.636  1.00 64.87           N  
ANISOU 3318  N   ALA A 451     6184   8221  10242   -802   -894   1186       N  
ATOM   3319  CA  ALA A 451      12.052  49.218  19.572  1.00 66.60           C  
ANISOU 3319  CA  ALA A 451     6312   8409  10584   -903   -865   1303       C  
ATOM   3320  C   ALA A 451      11.916  49.709  21.019  1.00 76.80           C  
ANISOU 3320  C   ALA A 451     7508   9819  11852   -824   -647   1424       C  
ATOM   3321  O   ALA A 451      12.074  50.898  21.299  1.00 84.42           O  
ANISOU 3321  O   ALA A 451     8497  10878  12701   -686   -523   1400       O  
ATOM   3322  CB  ALA A 451      13.190  48.220  19.462  1.00 57.46           C  
ANISOU 3322  CB  ALA A 451     5332   7104   9396   -959   -918   1204       C  
ATOM   3323  N   PHE A 452      11.612  48.792  21.932  1.00 76.23           N  
ANISOU 3323  N   PHE A 452     7339   9738  11888   -909   -604   1556       N  
ATOM   3324  CA  PHE A 452      11.555  49.118  23.352  1.00 72.79           C  
ANISOU 3324  CA  PHE A 452     6834   9408  11414   -835   -395   1672       C  
ATOM   3325  C   PHE A 452      12.482  48.234  24.135  1.00 87.08           C  
ANISOU 3325  C   PHE A 452     8752  11134  13199   -875   -349   1675       C  
ATOM   3326  O   PHE A 452      12.416  48.197  25.358  1.00 91.63           O  
ANISOU 3326  O   PHE A 452     9277  11780  13759   -843   -197   1789       O  
ATOM   3327  CB  PHE A 452      10.144  48.960  23.898  1.00 64.37           C  
ANISOU 3327  CB  PHE A 452     5512   8447  10500   -884   -349   1874       C  
ATOM   3328  CG  PHE A 452       9.194  50.008  23.423  1.00 75.05           C  
ANISOU 3328  CG  PHE A 452     6733   9914  11867   -806   -347   1897       C  
ATOM   3329  CD1 PHE A 452       8.735  49.994  22.119  1.00 84.31           C  
ANISOU 3329  CD1 PHE A 452     7881  11043  13111   -867   -542   1838       C  
ATOM   3330  CD2 PHE A 452       8.740  50.997  24.284  1.00 72.23           C  
ANISOU 3330  CD2 PHE A 452     6283   9710  11451   -666   -156   1979       C  
ATOM   3331  CE1 PHE A 452       7.849  50.951  21.672  1.00 87.03           C  
ANISOU 3331  CE1 PHE A 452     8100  11492  13474   -791   -551   1867       C  
ATOM   3332  CE2 PHE A 452       7.846  51.957  23.849  1.00 73.38           C  
ANISOU 3332  CE2 PHE A 452     6303   9958  11619   -584   -155   2004       C  
ATOM   3333  CZ  PHE A 452       7.399  51.937  22.542  1.00 79.47           C  
ANISOU 3333  CZ  PHE A 452     7042  10685  12469   -648   -355   1952       C  
ATOM   3334  N   GLU A 453      13.345  47.519  23.429  1.00101.79           N  
ANISOU 3334  N   GLU A 453    10771  12851  15054   -936   -479   1551       N  
ATOM   3335  CA  GLU A 453      14.104  46.440  24.037  1.00107.14           C  
ANISOU 3335  CA  GLU A 453    11534  13425  15750   -997   -475   1566       C  
ATOM   3336  C   GLU A 453      15.519  46.861  24.435  1.00 95.32           C  
ANISOU 3336  C   GLU A 453    10223  11912  14081   -884   -383   1449       C  
ATOM   3337  O   GLU A 453      16.007  46.509  25.516  1.00 99.71           O  
ANISOU 3337  O   GLU A 453    10809  12469  14607   -870   -284   1510       O  
ATOM   3338  CB  GLU A 453      14.149  45.253  23.074  1.00123.54           C  
ANISOU 3338  CB  GLU A 453    13661  15336  17942  -1134   -682   1510       C  
ATOM   3339  CG  GLU A 453      12.923  45.151  22.182  1.00132.94           C  
ANISOU 3339  CG  GLU A 453    14712  16531  19268  -1228   -828   1551       C  
ATOM   3340  CD  GLU A 453      13.217  44.430  20.888  1.00140.98           C  
ANISOU 3340  CD  GLU A 453    15854  17390  20322  -1309  -1044   1413       C  
ATOM   3341  OE1 GLU A 453      14.366  43.979  20.716  1.00141.41           O  
ANISOU 3341  OE1 GLU A 453    16094  17334  20301  -1287  -1065   1292       O  
ATOM   3342  OE2 GLU A 453      12.313  44.337  20.034  1.00147.15           O1-
ANISOU 3342  OE2 GLU A 453    16550  18160  21200  -1385  -1194   1422       O1-
ATOM   3343  N   GLY A 454      16.175  47.624  23.570  1.00 69.74           N  
ANISOU 3343  N   GLY A 454     7105   8661  10731   -807   -416   1289       N  
ATOM   3344  CA  GLY A 454      17.541  48.040  23.846  1.00 65.96           C  
ANISOU 3344  CA  GLY A 454     6792   8165  10105   -711   -342   1177       C  
ATOM   3345  C   GLY A 454      17.669  49.500  24.261  1.00 67.14           C  
ANISOU 3345  C   GLY A 454     6954   8438  10120   -574   -207   1155       C  
ATOM   3346  O   GLY A 454      16.813  50.016  24.984  1.00 77.25           O  
ANISOU 3346  O   GLY A 454     8113   9830  11408   -536   -107   1268       O  
ATOM   3347  N   ASN A 455      18.744  50.150  23.805  1.00 48.87           N  
ANISOU 3347  N   ASN A 455     4785   6099   7685   -498   -202   1013       N  
ATOM   3348  CA  ASN A 455      19.017  51.562  24.070  1.00 48.42           C  
ANISOU 3348  CA  ASN A 455     4769   6130   7499   -374    -96    970       C  
ATOM   3349  C   ASN A 455      18.330  52.461  23.047  1.00 49.63           C  
ANISOU 3349  C   ASN A 455     4887   6327   7645   -341   -142    933       C  
ATOM   3350  O   ASN A 455      18.958  52.977  22.136  1.00 52.76           O  
ANISOU 3350  O   ASN A 455     5389   6688   7971   -309   -187    814       O  
ATOM   3351  CB  ASN A 455      20.526  51.832  24.063  1.00 50.35           C  
ANISOU 3351  CB  ASN A 455     5177   6323   7632   -321    -75    847       C  
ATOM   3352  CG  ASN A 455      20.887  53.175  24.711  1.00 58.32           C  
ANISOU 3352  CG  ASN A 455     6232   7413   8516   -203     43    823       C  
ATOM   3353  ND2 ASN A 455      22.183  53.405  24.937  1.00 56.42           N  
ANISOU 3353  ND2 ASN A 455     6114   7135   8189   -164     68    739       N  
ATOM   3354  OD1 ASN A 455      20.010  53.985  25.009  1.00 51.87           O  
ANISOU 3354  OD1 ASN A 455     5340   6685   7684   -147    107    881       O  
ATOM   3355  N   THR A 456      17.030  52.636  23.206  1.00 46.85           N  
ANISOU 3355  N   THR A 456     4379   6053   7368   -348   -128   1043       N  
ATOM   3356  CA  THR A 456      16.256  53.396  22.262  1.00 47.58           C  
ANISOU 3356  CA  THR A 456     4419   6188   7473   -320   -186   1026       C  
ATOM   3357  C   THR A 456      15.540  54.551  22.939  1.00 55.64           C  
ANISOU 3357  C   THR A 456     5354   7333   8455   -207    -59   1097       C  
ATOM   3358  O   THR A 456      15.283  54.524  24.145  1.00 52.86           O  
ANISOU 3358  O   THR A 456     4937   7046   8102   -175     64   1193       O  
ATOM   3359  CB  THR A 456      15.206  52.520  21.564  1.00 54.27           C  
ANISOU 3359  CB  THR A 456     5140   7009   8472   -438   -326   1091       C  
ATOM   3360  CG2 THR A 456      15.848  51.327  20.921  1.00 53.72           C  
ANISOU 3360  CG2 THR A 456     5164   6804   8441   -544   -456   1018       C  
ATOM   3361  OG1 THR A 456      14.234  52.087  22.527  1.00 54.18           O  
ANISOU 3361  OG1 THR A 456     4953   7066   8568   -475   -261   1255       O  
ATOM   3362  N   ALA A 457      15.199  55.556  22.142  1.00 55.12           N  
ANISOU 3362  N   ALA A 457     5292   7298   8352   -141    -90   1052       N  
ATOM   3363  CA  ALA A 457      14.345  56.629  22.604  1.00 49.82           C  
ANISOU 3363  CA  ALA A 457     4526   6737   7665    -29      9   1121       C  
ATOM   3364  C   ALA A 457      13.027  56.099  23.187  1.00 57.07           C  
ANISOU 3364  C   ALA A 457     5226   7739   8719    -67     40   1285       C  
ATOM   3365  O   ALA A 457      12.582  56.569  24.230  1.00 66.13           O  
ANISOU 3365  O   ALA A 457     6301   8980   9845     21    186   1369       O  
ATOM   3366  CB  ALA A 457      14.083  57.589  21.483  1.00 55.16           C  
ANISOU 3366  CB  ALA A 457     5230   7418   8311     27    -64   1058       C  
ATOM   3367  N   PRO A 458      12.393  55.108  22.537  1.00 59.65           N  
ANISOU 3367  N   PRO A 458     5447   8031   9186   -198    -95   1335       N  
ATOM   3368  CA  PRO A 458      11.154  54.733  23.214  1.00 54.74           C  
ANISOU 3368  CA  PRO A 458     4602   7500   8695   -226    -42   1508       C  
ATOM   3369  C   PRO A 458      11.380  53.966  24.523  1.00 59.78           C  
ANISOU 3369  C   PRO A 458     5219   8152   9344   -260     77   1601       C  
ATOM   3370  O   PRO A 458      10.615  54.159  25.472  1.00 61.55           O  
ANISOU 3370  O   PRO A 458     5304   8487   9596   -207    213   1734       O  
ATOM   3371  CB  PRO A 458      10.454  53.860  22.176  1.00 51.70           C  
ANISOU 3371  CB  PRO A 458     4115   7063   8465   -371   -236   1537       C  
ATOM   3372  CG  PRO A 458      11.040  54.263  20.875  1.00 51.71           C  
ANISOU 3372  CG  PRO A 458     4271   6987   8389   -360   -370   1381       C  
ATOM   3373  CD  PRO A 458      12.470  54.505  21.195  1.00 56.25           C  
ANISOU 3373  CD  PRO A 458     5058   7504   8809   -303   -291   1261       C  
ATOM   3374  N   TYR A 459      12.411  53.128  24.585  1.00 60.03           N  
ANISOU 3374  N   TYR A 459     5386   8074   9347   -336     34   1536       N  
ATOM   3375  CA  TYR A 459      12.681  52.388  25.815  1.00 61.66           C  
ANISOU 3375  CA  TYR A 459     5587   8285   9556   -366    137   1625       C  
ATOM   3376  C   TYR A 459      12.921  53.333  26.965  1.00 65.35           C  
ANISOU 3376  C   TYR A 459     6099   8849   9882   -214    328   1640       C  
ATOM   3377  O   TYR A 459      12.444  53.103  28.073  1.00 70.91           O  
ANISOU 3377  O   TYR A 459     6711   9633  10600   -197    455   1774       O  
ATOM   3378  CB  TYR A 459      13.887  51.464  25.677  1.00 63.44           C  
ANISOU 3378  CB  TYR A 459     5974   8373   9758   -446     58   1535       C  
ATOM   3379  CG  TYR A 459      14.277  50.847  27.002  1.00 68.09           C  
ANISOU 3379  CG  TYR A 459     6580   8968  10323   -454    170   1622       C  
ATOM   3380  CD1 TYR A 459      13.427  49.957  27.647  1.00 73.46           C  
ANISOU 3380  CD1 TYR A 459     7106   9677  11130   -542    200   1797       C  
ATOM   3381  CD2 TYR A 459      15.479  51.170  27.621  1.00 64.92           C  
ANISOU 3381  CD2 TYR A 459     6346   8546   9773   -375    244   1538       C  
ATOM   3382  CE1 TYR A 459      13.768  49.396  28.863  1.00 79.94           C  
ANISOU 3382  CE1 TYR A 459     7950  10506  11919   -546    304   1888       C  
ATOM   3383  CE2 TYR A 459      15.826  50.622  28.843  1.00 70.97           C  
ANISOU 3383  CE2 TYR A 459     7136   9322  10508   -376    337   1621       C  
ATOM   3384  CZ  TYR A 459      14.972  49.725  29.454  1.00 82.29           C  
ANISOU 3384  CZ  TYR A 459     8426  10783  12058   -460    369   1796       C  
ATOM   3385  OH  TYR A 459      15.307  49.163  30.667  1.00 85.57           O  
ANISOU 3385  OH  TYR A 459     8871  11208  12433   -461    462   1889       O  
ATOM   3386  N   MET A 460      13.652  54.405  26.681  1.00 66.81           N  
ANISOU 3386  N   MET A 460     6431   9025   9930   -106    344   1502       N  
ATOM   3387  CA  MET A 460      14.010  55.390  27.686  1.00 56.46           C  
ANISOU 3387  CA  MET A 460     5199   7783   8471     41    502   1485       C  
ATOM   3388  C   MET A 460      12.816  56.169  28.157  1.00 60.86           C  
ANISOU 3388  C   MET A 460     5611   8475   9040    148    620   1588       C  
ATOM   3389  O   MET A 460      12.591  56.320  29.362  1.00 74.91           O  
ANISOU 3389  O   MET A 460     7365  10338  10761    226    774   1671       O  
ATOM   3390  CB  MET A 460      15.051  56.324  27.133  1.00 44.95           C  
ANISOU 3390  CB  MET A 460     3924   6265   6887    112    467   1316       C  
ATOM   3391  CG  MET A 460      16.387  55.631  26.945  1.00 49.68           C  
ANISOU 3391  CG  MET A 460     4674   6750   7453     36    392   1219       C  
ATOM   3392  SD  MET A 460      17.288  55.551  28.485  1.00 71.42           S  
ANISOU 3392  SD  MET A 460     7535   9516  10088     90    516   1231       S  
ATOM   3393  CE  MET A 460      16.921  53.906  29.002  1.00 58.19           C  
ANISOU 3393  CE  MET A 460     5754   7820   8535    -42    500   1371       C  
ATOM   3394  N   GLN A 461      12.043  56.645  27.194  1.00 47.45           N  
ANISOU 3394  N   GLN A 461     3819   6798   7413    159    547   1584       N  
ATOM   3395  CA  GLN A 461      10.764  57.279  27.478  1.00 52.47           C  
ANISOU 3395  CA  GLN A 461     4278   7561   8096    253    640   1696       C  
ATOM   3396  C   GLN A 461       9.857  56.388  28.318  1.00 60.87           C  
ANISOU 3396  C   GLN A 461     5147   8709   9273    195    724   1885       C  
ATOM   3397  O   GLN A 461       9.235  56.850  29.276  1.00 65.23           O  
ANISOU 3397  O   GLN A 461     5614   9380   9790    309    893   1982       O  
ATOM   3398  CB  GLN A 461      10.081  57.652  26.172  1.00 51.40           C  
ANISOU 3398  CB  GLN A 461     4058   7421   8052    238    505   1674       C  
ATOM   3399  CG  GLN A 461      10.776  58.802  25.477  1.00 55.98           C  
ANISOU 3399  CG  GLN A 461     4813   7949   8509    333    465   1517       C  
ATOM   3400  CD  GLN A 461      10.464  58.859  23.992  1.00 66.64           C  
ANISOU 3400  CD  GLN A 461     6137   9252   9932    274    286   1470       C  
ATOM   3401  NE2 GLN A 461      10.408  60.069  23.443  1.00 64.95           N  
ANISOU 3401  NE2 GLN A 461     5982   9047   9652    390    278   1404       N  
ATOM   3402  OE1 GLN A 461      10.253  57.832  23.352  1.00 74.76           O  
ANISOU 3402  OE1 GLN A 461     7100  10233  11073    129    151   1495       O  
ATOM   3403  N   TYR A 462       9.799  55.110  27.962  1.00 66.06           N  
ANISOU 3403  N   TYR A 462     5739   9298  10061     19    608   1937       N  
ATOM   3404  CA  TYR A 462       9.026  54.139  28.721  1.00 69.86           C  
ANISOU 3404  CA  TYR A 462     6042   9838  10664    -66    673   2126       C  
ATOM   3405  C   TYR A 462       9.510  54.060  30.152  1.00 70.27           C  
ANISOU 3405  C   TYR A 462     6172   9934  10592      2    852   2175       C  
ATOM   3406  O   TYR A 462       8.715  54.055  31.095  1.00 73.68           O  
ANISOU 3406  O   TYR A 462     6465  10488  11041     53   1009   2331       O  
ATOM   3407  CB  TYR A 462       9.120  52.757  28.083  1.00 76.24           C  
ANISOU 3407  CB  TYR A 462     6821  10528  11620   -273    499   2147       C  
ATOM   3408  CG  TYR A 462       8.499  51.658  28.925  1.00 80.35           C  
ANISOU 3408  CG  TYR A 462     7184  11082  12264   -380    560   2343       C  
ATOM   3409  CD1 TYR A 462       7.123  51.454  28.926  1.00 78.95           C  
ANISOU 3409  CD1 TYR A 462     6741  10999  12256   -428    576   2517       C  
ATOM   3410  CD2 TYR A 462       9.288  50.826  29.719  1.00 80.65           C  
ANISOU 3410  CD2 TYR A 462     7332  11057  12256   -435    601   2365       C  
ATOM   3411  CE1 TYR A 462       6.547  50.459  29.690  1.00 78.91           C  
ANISOU 3411  CE1 TYR A 462     6585  11025  12372   -535    638   2712       C  
ATOM   3412  CE2 TYR A 462       8.719  49.828  30.487  1.00 77.52           C  
ANISOU 3412  CE2 TYR A 462     6796  10686  11971   -535    660   2556       C  
ATOM   3413  CZ  TYR A 462       7.345  49.652  30.468  1.00 77.54           C  
ANISOU 3413  CZ  TYR A 462     6535  10784  12144   -588    682   2733       C  
ATOM   3414  OH  TYR A 462       6.764  48.660  31.221  1.00 82.59           O  
ANISOU 3414  OH  TYR A 462     7090  11427  12862   -680    726   2898       O  
ATOM   3415  N   ALA A 463      10.826  53.978  30.299  1.00 68.24           N  
ANISOU 3415  N   ALA A 463     6138   9581  10210      3    825   2046       N  
ATOM   3416  CA  ALA A 463      11.427  53.774  31.604  1.00 63.99           C  
ANISOU 3416  CA  ALA A 463     5698   9065   9550     50    959   2083       C  
ATOM   3417  C   ALA A 463      11.148  54.988  32.451  1.00 68.50           C  
ANISOU 3417  C   ALA A 463     6290   9761   9978    246   1140   2088       C  
ATOM   3418  O   ALA A 463      10.761  54.871  33.614  1.00 68.16           O  
ANISOU 3418  O   ALA A 463     6197   9816   9887    303   1301   2213       O  
ATOM   3419  CB  ALA A 463      12.913  53.531  31.488  1.00 60.53           C  
ANISOU 3419  CB  ALA A 463     5485   8497   9015     19    875   1934       C  
ATOM   3420  N   TYR A 464      11.318  56.164  31.857  1.00 71.09           N  
ANISOU 3420  N   TYR A 464     6696  10083  10233    353   1114   1955       N  
ATOM   3421  CA  TYR A 464      11.054  57.389  32.598  1.00 66.87           C  
ANISOU 3421  CA  TYR A 464     6197   9649   9561    551   1274   1943       C  
ATOM   3422  C   TYR A 464       9.660  57.370  33.187  1.00 76.00           C  
ANISOU 3422  C   TYR A 464     7129  10957  10791    608   1420   2128       C  
ATOM   3423  O   TYR A 464       9.468  57.728  34.349  1.00 86.76           O  
ANISOU 3423  O   TYR A 464     8510  12416  12038    736   1600   2188       O  
ATOM   3424  CB  TYR A 464      11.210  58.620  31.729  1.00 54.60           C  
ANISOU 3424  CB  TYR A 464     4724   8062   7960    645   1212   1799       C  
ATOM   3425  CG  TYR A 464      10.842  59.878  32.472  1.00 61.10           C  
ANISOU 3425  CG  TYR A 464     5583   8979   8655    855   1371   1789       C  
ATOM   3426  CD1 TYR A 464      11.685  60.397  33.451  1.00 65.14           C  
ANISOU 3426  CD1 TYR A 464     6293   9480   8978    959   1461   1711       C  
ATOM   3427  CD2 TYR A 464       9.651  60.551  32.201  1.00 64.29           C  
ANISOU 3427  CD2 TYR A 464     5825   9476   9125    955   1426   1855       C  
ATOM   3428  CE1 TYR A 464      11.355  61.551  34.136  1.00 68.38           C  
ANISOU 3428  CE1 TYR A 464     6756   9963   9262   1158   1600   1690       C  
ATOM   3429  CE2 TYR A 464       9.314  61.708  32.882  1.00 65.27           C  
ANISOU 3429  CE2 TYR A 464     5991   9678   9129   1162   1575   1839       C  
ATOM   3430  CZ  TYR A 464      10.170  62.204  33.848  1.00 67.28           C  
ANISOU 3430  CZ  TYR A 464     6461   9913   9190   1264   1661   1752       C  
ATOM   3431  OH  TYR A 464       9.842  63.347  34.536  1.00 64.47           O  
ANISOU 3431  OH  TYR A 464     6167   9622   8707   1476   1803   1725       O  
ATOM   3432  N   THR A 465       8.694  56.938  32.385  1.00 74.76           N  
ANISOU 3432  N   THR A 465     6760  10821  10826    513   1341   2220       N  
ATOM   3433  CA  THR A 465       7.313  56.884  32.833  1.00 72.50           C  
ANISOU 3433  CA  THR A 465     6222  10682  10641    554   1469   2410       C  
ATOM   3434  C   THR A 465       7.170  55.895  33.976  1.00 75.10           C  
ANISOU 3434  C   THR A 465     6489  11066  10978    494   1593   2574       C  
ATOM   3435  O   THR A 465       6.470  56.166  34.943  1.00 81.22           O  
ANISOU 3435  O   THR A 465     7190  11970  11701    608   1777   2687       O  
ATOM   3436  CB  THR A 465       6.363  56.518  31.689  1.00 72.01           C  
ANISOU 3436  CB  THR A 465     5940  10618  10801    438   1326   2478       C  
ATOM   3437  CG2 THR A 465       6.313  57.642  30.702  1.00 72.29           C  
ANISOU 3437  CG2 THR A 465     6020  10632  10813    534   1240   2345       C  
ATOM   3438  OG1 THR A 465       6.842  55.347  31.020  1.00 79.88           O  
ANISOU 3438  OG1 THR A 465     6961  11484  11904    226   1141   2458       O  
ATOM   3439  N   ARG A 466       7.864  54.765  33.876  1.00 73.26           N  
ANISOU 3439  N   ARG A 466     6323  10721  10791    323   1482   2572       N  
ATOM   3440  CA  ARG A 466       7.811  53.745  34.918  1.00 68.10           C  
ANISOU 3440  CA  ARG A 466     5628  10099  10149    251   1581   2731       C  
ATOM   3441  C   ARG A 466       8.321  54.272  36.264  1.00 74.52           C  
ANISOU 3441  C   ARG A 466     6600  10982  10731    415   1771   2721       C  
ATOM   3442  O   ARG A 466       7.739  53.995  37.307  1.00 82.78           O  
ANISOU 3442  O   ARG A 466     7573  12133  11746    455   1933   2875       O  
ATOM   3443  CB  ARG A 466       8.616  52.515  34.499  1.00 63.55           C  
ANISOU 3443  CB  ARG A 466     5134   9363   9651     54   1408   2700       C  
ATOM   3444  CG  ARG A 466       7.953  51.678  33.419  1.00 67.33           C  
ANISOU 3444  CG  ARG A 466     5434   9776  10370   -132   1235   2761       C  
ATOM   3445  CD  ARG A 466       6.744  50.925  33.952  1.00 71.11           C  
ANISOU 3445  CD  ARG A 466     5719  10323  10975   -205   1295   2969       C  
ATOM   3446  NE  ARG A 466       7.091  50.006  35.033  1.00 76.21           N  
ANISOU 3446  NE  ARG A 466     6427  10952  11578   -258   1374   3074       N  
ATOM   3447  CZ  ARG A 466       6.217  49.569  35.934  1.00 84.68           C  
ANISOU 3447  CZ  ARG A 466     7411  12099  12663   -255   1484   3234       C  
ATOM   3448  NH1 ARG A 466       4.959  49.978  35.872  1.00 83.52           N1+
ANISOU 3448  NH1 ARG A 466     7107  12050  12578   -202   1529   3304       N1+
ATOM   3449  NH2 ARG A 466       6.596  48.735  36.898  1.00 91.02           N  
ANISOU 3449  NH2 ARG A 466     8283  12881  13419   -300   1548   3328       N  
ATOM   3450  N   VAL A 467       9.417  55.019  36.230  1.00 72.22           N  
ANISOU 3450  N   VAL A 467     6553  10620  10269    505   1732   2525       N  
ATOM   3451  CA  VAL A 467       9.978  55.657  37.414  1.00 61.23           C  
ANISOU 3451  CA  VAL A 467     5342   9279   8646    668   1880   2481       C  
ATOM   3452  C   VAL A 467       8.998  56.641  38.032  1.00 72.81           C  
ANISOU 3452  C   VAL A 467     6721  10907  10038    865   2080   2546       C  
ATOM   3453  O   VAL A 467       8.783  56.641  39.257  1.00 65.55           O  
ANISOU 3453  O   VAL A 467     5819  10093   8996    965   2264   2646       O  
ATOM   3454  CB  VAL A 467      11.255  56.426  37.075  1.00 66.34           C  
ANISOU 3454  CB  VAL A 467     6242   9812   9150    723   1777   2249       C  
ATOM   3455  CG1 VAL A 467      11.807  57.094  38.318  1.00 73.63           C  
ANISOU 3455  CG1 VAL A 467     7356  10784   9837    886   1912   2202       C  
ATOM   3456  CG2 VAL A 467      12.284  55.511  36.404  1.00 59.46           C  
ANISOU 3456  CG2 VAL A 467     5460   8784   8348    546   1585   2172       C  
ATOM   3457  N   LEU A 468       8.432  57.503  37.180  1.00 81.54           N  
ANISOU 3457  N   LEU A 468     7745  12029  11208    932   2042   2486       N  
ATOM   3458  CA  LEU A 468       7.459  58.507  37.616  1.00 90.24           C  
ANISOU 3458  CA  LEU A 468     8760  13271  12258   1132   2214   2534       C  
ATOM   3459  C   LEU A 468       6.189  57.876  38.184  1.00 89.24           C  
ANISOU 3459  C   LEU A 468     8463  13229  12215   1095   2289   2714       C  
ATOM   3460  O   LEU A 468       5.621  58.393  39.141  1.00100.72           O  
ANISOU 3460  O   LEU A 468     9943  14777  13549   1250   2447   2753       O  
ATOM   3461  CB  LEU A 468       7.084  59.451  36.469  1.00 98.46           C  
ANISOU 3461  CB  LEU A 468     9744  14290  13374   1190   2123   2437       C  
ATOM   3462  CG  LEU A 468       7.830  60.788  36.358  1.00108.23           C  
ANISOU 3462  CG  LEU A 468    11221  15462  14439   1348   2103   2229       C  
ATOM   3463  CD1 LEU A 468       7.015  61.796  35.556  1.00109.72           C  
ANISOU 3463  CD1 LEU A 468    11305  15685  14700   1459   2087   2201       C  
ATOM   3464  CD2 LEU A 468       8.179  61.356  37.728  1.00112.48           C  
ANISOU 3464  CD2 LEU A 468    11935  16058  14745   1526   2281   2201       C  
ATOM   3465  N   SER A 469       5.740  56.769  37.598  1.00 81.80           N  
ANISOU 3465  N   SER A 469     7353  12248  11477    893   2173   2821       N  
ATOM   3466  CA  SER A 469       4.557  56.090  38.106  1.00 83.90           C  
ANISOU 3466  CA  SER A 469     7452  12586  11840    842   2235   3000       C  
ATOM   3467  C   SER A 469       4.855  55.435  39.459  1.00 89.87           C  
ANISOU 3467  C   SER A 469     8295  13377  12473    847   2366   3095       C  
ATOM   3468  O   SER A 469       4.021  55.451  40.358  1.00 89.85           O  
ANISOU 3468  O   SER A 469     8235  13476  12428    928   2510   3208       O  
ATOM   3469  CB  SER A 469       4.055  55.049  37.108  1.00 85.20           C  
ANISOU 3469  CB  SER A 469     7436  12682  12254    618   2056   3078       C  
ATOM   3470  OG  SER A 469       4.679  53.794  37.309  1.00 89.14           O  
ANISOU 3470  OG  SER A 469     7971  13098  12800    445   1993   3136       O  
ATOM   3471  N   VAL A 470       6.049  54.867  39.598  1.00 95.01           N  
ANISOU 3471  N   VAL A 470     9086  13945  13067    765   2316   3052       N  
ATOM   3472  CA  VAL A 470       6.490  54.291  40.869  1.00102.51           C  
ANISOU 3472  CA  VAL A 470    10150  14920  13880    777   2428   3129       C  
ATOM   3473  C   VAL A 470       6.475  55.349  41.968  1.00104.13           C  
ANISOU 3473  C   VAL A 470    10495  15228  13840   1017   2614   3084       C  
ATOM   3474  O   VAL A 470       6.031  55.102  43.086  1.00110.15           O  
ANISOU 3474  O   VAL A 470    11266  16073  14515   1076   2751   3194       O  
ATOM   3475  CB  VAL A 470       7.914  53.673  40.748  1.00 90.16           C  
ANISOU 3475  CB  VAL A 470     8735  13241  12279    667   2332   3066       C  
ATOM   3476  CG1 VAL A 470       8.583  53.539  42.109  1.00 84.47           C  
ANISOU 3476  CG1 VAL A 470     8197  12557  11342    749   2459   3094       C  
ATOM   3477  CG2 VAL A 470       7.850  52.322  40.036  1.00 92.13           C  
ANISOU 3477  CG2 VAL A 470     8863  13385  12758    422   2170   3153       C  
ATOM   3478  N   PHE A 471       6.943  56.538  41.624  1.00 97.24           N  
ANISOU 3478  N   PHE A 471     9739  14346  12860   1156   2612   2916       N  
ATOM   3479  CA  PHE A 471       7.073  57.630  42.571  1.00 84.96           C  
ANISOU 3479  CA  PHE A 471     8357  12859  11063   1388   2760   2835       C  
ATOM   3480  C   PHE A 471       5.730  58.231  42.915  1.00 87.39           C  
ANISOU 3480  C   PHE A 471     8549  13277  11379   1522   2879   2902       C  
ATOM   3481  O   PHE A 471       5.276  58.160  44.058  1.00 99.96           O  
ANISOU 3481  O   PHE A 471    10165  14956  12859   1612   3026   2990       O  
ATOM   3482  CB  PHE A 471       7.989  58.696  41.986  1.00 84.63           C  
ANISOU 3482  CB  PHE A 471     8476  12753  10927   1482   2698   2631       C  
ATOM   3483  CG  PHE A 471       8.215  59.873  42.879  1.00 84.15           C  
ANISOU 3483  CG  PHE A 471     8622  12733  10616   1716   2819   2519       C  
ATOM   3484  CD1 PHE A 471       9.206  59.846  43.838  1.00 81.89           C  
ANISOU 3484  CD1 PHE A 471     8563  12434  10117   1771   2866   2467       C  
ATOM   3485  CD2 PHE A 471       7.465  61.030  42.725  1.00 90.45           C  
ANISOU 3485  CD2 PHE A 471     9404  13571  11393   1882   2870   2457       C  
ATOM   3486  CE1 PHE A 471       9.434  60.944  44.644  1.00 88.45           C  
ANISOU 3486  CE1 PHE A 471     9605  13287  10714   1983   2954   2348       C  
ATOM   3487  CE2 PHE A 471       7.688  62.135  43.529  1.00 92.12           C  
ANISOU 3487  CE2 PHE A 471     9825  13800  11377   2096   2965   2341       C  
ATOM   3488  CZ  PHE A 471       8.674  62.090  44.489  1.00 92.56           C  
ANISOU 3488  CZ  PHE A 471    10112  13838  11220   2145   3003   2283       C  
ATOM   3489  N   ARG A 472       5.095  58.828  41.916  1.00 83.34           N  
ANISOU 3489  N   ARG A 472     7910  12759  10996   1538   2814   2861       N  
ATOM   3490  CA  ARG A 472       3.861  59.556  42.145  1.00 85.25           C  
ANISOU 3490  CA  ARG A 472     8049  13100  11244   1683   2921   2908       C  
ATOM   3491  C   ARG A 472       2.792  58.644  42.737  1.00 91.79           C  
ANISOU 3491  C   ARG A 472     8691  14015  12170   1613   3005   3118       C  
ATOM   3492  O   ARG A 472       2.327  58.882  43.849  1.00 96.41           O  
ANISOU 3492  O   ARG A 472     9312  14695  12624   1750   3173   3179       O  
ATOM   3493  CB  ARG A 472       3.383  60.210  40.850  1.00 83.18           C  
ANISOU 3493  CB  ARG A 472     7668  12807  11130   1683   2810   2842       C  
ATOM   3494  CG  ARG A 472       4.332  61.300  40.375  1.00 88.61           C  
ANISOU 3494  CG  ARG A 472     8547  13418  11702   1792   2754   2637       C  
ATOM   3495  CD  ARG A 472       3.753  62.120  39.244  1.00 95.21           C  
ANISOU 3495  CD  ARG A 472     9282  14237  12655   1835   2668   2576       C  
ATOM   3496  NE  ARG A 472       3.170  61.273  38.213  1.00 99.27           N  
ANISOU 3496  NE  ARG A 472     9568  14735  13417   1639   2531   2673       N  
ATOM   3497  CZ  ARG A 472       3.024  61.636  36.944  1.00 97.92           C  
ANISOU 3497  CZ  ARG A 472     9318  14512  13374   1600   2387   2613       C  
ATOM   3498  NH1 ARG A 472       3.451  62.826  36.536  1.00 89.28           N1+
ANISOU 3498  NH1 ARG A 472     8355  13377  12191   1742   2367   2460       N1+
ATOM   3499  NH2 ARG A 472       2.475  60.792  36.082  1.00102.67           N  
ANISOU 3499  NH2 ARG A 472     9724  15096  14190   1417   2254   2703       N  
ATOM   3500  N   LYS A 473       2.427  57.589  42.018  1.00 92.82           N  
ANISOU 3500  N   LYS A 473     8634  14109  12526   1400   2887   3226       N  
ATOM   3501  CA  LYS A 473       1.462  56.631  42.543  1.00 97.57           C  
ANISOU 3501  CA  LYS A 473     9059  14778  13235   1312   2951   3431       C  
ATOM   3502  C   LYS A 473       1.998  55.954  43.811  1.00103.04           C  
ANISOU 3502  C   LYS A 473     9879  15492  13781   1310   3059   3503       C  
ATOM   3503  O   LYS A 473       2.485  54.825  43.752  1.00 98.16           O  
ANISOU 3503  O   LYS A 473     9256  14803  13239   1130   2974   3566       O  
ATOM   3504  CB  LYS A 473       1.113  55.582  41.484  1.00 95.48           C  
ANISOU 3504  CB  LYS A 473     8601  14441  13238   1068   2772   3514       C  
ATOM   3505  N   ALA A 474       1.905  56.660  44.942  1.00105.97           N  
ANISOU 3505  N   ALA A 474    10372  15954  13937   1516   3238   3490       N  
ATOM   3506  CA  ALA A 474       2.323  56.161  46.257  1.00102.68           C  
ANISOU 3506  CA  ALA A 474    10089  15575  13349   1549   3358   3557       C  
ATOM   3507  C   ALA A 474       1.829  57.101  47.353  1.00112.34           C  
ANISOU 3507  C   ALA A 474    11399  16916  14368   1796   3557   3549       C  
ATOM   3508  O   ALA A 474       0.842  56.822  48.032  1.00121.32           O  
ANISOU 3508  O   ALA A 474    12413  18159  15526   1832   3690   3705       O  
ATOM   3509  CB  ALA A 474       3.843  56.019  46.330  1.00 93.43           C  
ANISOU 3509  CB  ALA A 474     9150  14304  12046   1512   3277   3432       C  
ATOM   3510  N   GLU A 475       2.536  58.216  47.511  1.00114.32           N  
ANISOU 3510  N   GLU A 475    11869  17144  14422   1966   3573   3364       N  
ATOM   3511  CA  GLU A 475       2.187  59.273  48.458  1.00115.04           C  
ANISOU 3511  CA  GLU A 475    12083  17322  14304   2216   3739   3313       C  
ATOM   3512  C   GLU A 475       2.922  60.542  48.042  1.00120.80           C  
ANISOU 3512  C   GLU A 475    13009  17980  14910   2352   3678   3083       C  
ATOM   3513  O   GLU A 475       3.546  60.577  46.978  1.00121.76           O  
ANISOU 3513  O   GLU A 475    13132  18001  15128   2249   3522   2987       O  
ATOM   3514  CB  GLU A 475       2.557  58.884  49.892  1.00109.33           C  
ANISOU 3514  CB  GLU A 475    11521  16651  13368   2280   3865   3368       C  
ATOM   3515  N   ILE A 476       2.858  61.576  48.875  1.00121.57           N  
ANISOU 3515  N   ILE A 476    13277  18122  14793   2581   3797   2995       N  
ATOM   3516  CA  ILE A 476       3.621  62.799  48.626  1.00118.80           C  
ANISOU 3516  CA  ILE A 476    13147  17689  14301   2717   3739   2771       C  
ATOM   3517  C   ILE A 476       3.746  63.669  49.870  1.00117.46           C  
ANISOU 3517  C   ILE A 476    13217  17558  13855   2950   3868   2685       C  
ATOM   3518  O   ILE A 476       2.799  63.826  50.644  1.00125.36           O  
ANISOU 3518  O   ILE A 476    14160  18666  14805   3073   4024   2780       O  
ATOM   3519  CB  ILE A 476       2.994  63.655  47.504  1.00118.53           C  
ANISOU 3519  CB  ILE A 476    12989  17633  14414   2760   3680   2709       C  
ATOM   3520  N   ASP A 477       4.928  64.235  50.048  1.00105.96           N  
ANISOU 3520  N   ASP A 477    12032  16008  12220   3008   3797   2503       N  
ATOM   3521  CA  ASP A 477       5.159  65.225  51.079  1.00100.51           C  
ANISOU 3521  CA  ASP A 477    11602  15321  11266   3230   3878   2379       C  
ATOM   3522  C   ASP A 477       6.484  65.864  50.764  1.00110.12           C  
ANISOU 3522  C   ASP A 477    13069  16401  12370   3241   3736   2164       C  
ATOM   3523  O   ASP A 477       7.477  65.564  51.422  1.00122.95           O  
ANISOU 3523  O   ASP A 477    14893  17990  13833   3221   3702   2112       O  
ATOM   3524  CB  ASP A 477       5.171  64.604  52.469  1.00 93.47           C  
ANISOU 3524  CB  ASP A 477    10798  14513  10205   3269   4001   2479       C  
ATOM   3525  N   GLU A 478       6.490  66.711  49.734  1.00 98.72           N  
ANISOU 3525  N   GLU A 478    11610  14881  11019   3266   3646   2047       N  
ATOM   3526  CA  GLU A 478       7.703  67.349  49.241  1.00 95.80           C  
ANISOU 3526  CA  GLU A 478    11451  14371  10578   3262   3499   1845       C  
ATOM   3527  C   GLU A 478       8.598  67.847  50.372  1.00101.94           C  
ANISOU 3527  C   GLU A 478    12556  15103  11073   3384   3502   1709       C  
ATOM   3528  O   GLU A 478       9.740  67.400  50.497  1.00107.09           O  
ANISOU 3528  O   GLU A 478    13347  15694  11649   3291   3411   1654       O  
ATOM   3529  CB  GLU A 478       7.354  68.513  48.303  1.00 94.61           C  
ANISOU 3529  CB  GLU A 478    11280  14155  10511   3350   3445   1732       C  
ATOM   3530  N   GLU A 479       8.069  68.742  51.207  1.00100.77           N  
ANISOU 3530  N   GLU A 479    12530  14986  10772   3591   3603   1660       N  
ATOM   3531  CA  GLU A 479       8.857  69.352  52.277  1.00 98.38           C  
ANISOU 3531  CA  GLU A 479    12554  14629  10197   3720   3590   1515       C  
ATOM   3532  C   GLU A 479       9.280  68.307  53.294  1.00105.39           C  
ANISOU 3532  C   GLU A 479    13502  15580  10962   3658   3634   1611       C  
ATOM   3533  O   GLU A 479      10.359  68.413  53.883  1.00108.66           O  
ANISOU 3533  O   GLU A 479    14169  15924  11191   3668   3553   1495       O  
ATOM   3534  CB  GLU A 479       8.075  70.471  52.966  1.00 94.33           C  
ANISOU 3534  CB  GLU A 479    12142  14143   9557   3957   3699   1459       C  
ATOM   3535  N   GLN A 480       8.431  67.297  53.485  1.00103.63           N  
ANISOU 3535  N   GLN A 480    13044  15484  10846   3587   3753   1825       N  
ATOM   3536  CA  GLN A 480       8.722  66.207  54.412  1.00103.39           C  
ANISOU 3536  CA  GLN A 480    13041  15518  10723   3515   3802   1945       C  
ATOM   3537  C   GLN A 480       9.670  65.174  53.774  1.00 97.07           C  
ANISOU 3537  C   GLN A 480    12194  14660  10029   3287   3669   1978       C  
ATOM   3538  O   GLN A 480      10.654  64.762  54.401  1.00 94.06           O  
ANISOU 3538  O   GLN A 480    11996  14247   9498   3248   3612   1944       O  
ATOM   3539  CB  GLN A 480       7.420  65.547  54.887  1.00102.87           C  
ANISOU 3539  CB  GLN A 480    12746  15605  10735   3527   3981   2168       C  
ATOM   3540  N   LEU A 481       9.385  64.773  52.533  1.00 90.37           N  
ANISOU 3540  N   LEU A 481    11106  13796   9436   3141   3613   2041       N  
ATOM   3541  CA  LEU A 481      10.262  63.869  51.788  1.00 79.30           C  
ANISOU 3541  CA  LEU A 481     9652  12329   8151   2930   3482   2062       C  
ATOM   3542  C   LEU A 481      11.663  64.454  51.705  1.00 78.11           C  
ANISOU 3542  C   LEU A 481     9772  12054   7852   2947   3342   1856       C  
ATOM   3543  O   LEU A 481      12.644  63.718  51.643  1.00 74.97           O  
ANISOU 3543  O   LEU A 481     9435  11612   7440   2816   3250   1861       O  
ATOM   3544  CB  LEU A 481       9.718  63.599  50.382  1.00 63.79           C  
ANISOU 3544  CB  LEU A 481     7411  10351   6475   2796   3429   2125       C  
ATOM   3545  N   ALA A 482      11.756  65.781  51.722  1.00 78.80           N  
ANISOU 3545  N   ALA A 482    10027  12082   7830   3109   3319   1678       N  
ATOM   3546  CA  ALA A 482      13.050  66.457  51.649  1.00 82.10           C  
ANISOU 3546  CA  ALA A 482    10713  12371   8111   3131   3175   1470       C  
ATOM   3547  C   ALA A 482      13.778  66.436  52.988  1.00 87.91           C  
ANISOU 3547  C   ALA A 482    11720  13102   8579   3202   3167   1416       C  
ATOM   3548  O   ALA A 482      14.976  66.745  53.049  1.00 85.96           O  
ANISOU 3548  O   ALA A 482    11697  12752   8212   3188   3028   1265       O  
ATOM   3549  CB  ALA A 482      12.879  67.882  51.172  1.00 83.20           C  
ANISOU 3549  CB  ALA A 482    10939  12430   8243   3267   3138   1301       C  
ATOM   3550  N   ALA A 483      13.051  66.084  54.053  1.00 82.98           N  
ANISOU 3550  N   ALA A 483    11074  12589   7864   3279   3310   1539       N  
ATOM   3551  CA  ALA A 483      13.666  65.832  55.363  1.00 82.44           C  
ANISOU 3551  CA  ALA A 483    11234  12536   7554   3327   3310   1525       C  
ATOM   3552  C   ALA A 483      13.835  64.331  55.631  1.00 87.85           C  
ANISOU 3552  C   ALA A 483    11805  13287   8286   3166   3332   1716       C  
ATOM   3553  O   ALA A 483      14.489  63.951  56.618  1.00 99.92           O  
ANISOU 3553  O   ALA A 483    13515  14821   9629   3174   3307   1717       O  
ATOM   3554  CB  ALA A 483      12.863  66.476  56.481  1.00 85.64           C  
ANISOU 3554  CB  ALA A 483    11733  13013   7792   3533   3451   1523       C  
ATOM   3555  N   ALA A 484      13.267  63.492  54.763  1.00 91.61           N  
ANISOU 3555  N   ALA A 484    11991  13804   9012   3018   3364   1873       N  
ATOM   3556  CA  ALA A 484      13.553  62.085  54.814  1.00 94.20           C  
ANISOU 3556  CA  ALA A 484    12216  14160   9418   2840   3348   2039       C  
ATOM   3557  C   ALA A 484      15.065  61.912  54.753  1.00103.83           C  
ANISOU 3557  C   ALA A 484    13639  15276  10535   2761   3177   1929       C  
ATOM   3558  O   ALA A 484      15.811  62.818  54.305  1.00109.92           O  
ANISOU 3558  O   ALA A 484    14566  15950  11249   2805   3061   1734       O  
ATOM   3559  CB  ALA A 484      12.875  61.352  53.682  1.00 90.73           C  
ANISOU 3559  CB  ALA A 484    11455  13740   9279   2678   3359   2182       C  
ATOM   3560  N   PRO A 485      15.562  60.776  55.262  1.00110.59           N  
ANISOU 3560  N   PRO A 485    14514  16148  11358   2649   3153   2051       N  
ATOM   3561  CA  PRO A 485      17.017  60.881  55.440  1.00106.37           C  
ANISOU 3561  CA  PRO A 485    14231  15517  10666   2627   2986   1917       C  
ATOM   3562  C   PRO A 485      17.920  60.111  54.448  1.00 99.56           C  
ANISOU 3562  C   PRO A 485    13300  14576   9951   2434   2844   1943       C  
ATOM   3563  O   PRO A 485      19.148  60.319  54.561  1.00107.86           O  
ANISOU 3563  O   PRO A 485    14552  15512  10920   2399   2648   1793       O  
ATOM   3564  CB  PRO A 485      17.236  60.348  56.862  1.00110.94           C  
ANISOU 3564  CB  PRO A 485    14965  16148  11038   2669   3018   1991       C  
ATOM   3565  CG  PRO A 485      15.996  59.434  57.109  1.00111.59           C  
ANISOU 3565  CG  PRO A 485    14798  16346  11254   2623   3192   2229       C  
ATOM   3566  CD  PRO A 485      14.966  59.710  56.084  1.00111.88           C  
ANISOU 3566  CD  PRO A 485    14578  16407  11524   2606   3266   2263       C  
ATOM   3567  N   VAL A 486      17.386  59.457  53.412  1.00 85.36           N  
ANISOU 3567  N   VAL A 486    11226  12771   8437   2283   2848   2053       N  
ATOM   3568  CA  VAL A 486      18.140  58.516  52.555  1.00 74.55           C  
ANISOU 3568  CA  VAL A 486     9758  11273   7295   2046   2646   2062       C  
ATOM   3569  C   VAL A 486      19.240  57.729  53.234  1.00 67.29           C  
ANISOU 3569  C   VAL A 486     8994  10297   6278   1969   2519   2081       C  
ATOM   3570  O   VAL A 486      20.320  58.215  53.422  1.00 64.86           O  
ANISOU 3570  O   VAL A 486     8889   9896   5858   1987   2361   1914       O  
ATOM   3571  CB  VAL A 486      18.777  59.188  51.282  1.00 89.03           C  
ANISOU 3571  CB  VAL A 486    11584  12954   9289   1968   2446   1857       C  
ATOM   3572  CG1 VAL A 486      17.731  59.535  50.257  1.00 85.52           C  
ANISOU 3572  CG1 VAL A 486    10916  12539   9040   1963   2521   1879       C  
ATOM   3573  CG2 VAL A 486      19.649  60.380  51.525  1.00 96.08           C  
ANISOU 3573  CG2 VAL A 486    12730  13767  10008   2075   2336   1628       C  
ATOM   3574  N   ILE A 487      18.958  56.468  53.525  1.00 70.89           N  
ANISOU 3574  N   ILE A 487     9334  10798   6802   1867   2577   2293       N  
ATOM   3575  CA  ILE A 487      19.957  55.576  54.080  1.00 69.59           C  
ANISOU 3575  CA  ILE A 487     9288  10572   6580   1780   2451   2335       C  
ATOM   3576  C   ILE A 487      20.297  54.441  53.100  1.00 71.69           C  
ANISOU 3576  C   ILE A 487     9380  10724   7134   1553   2307   2398       C  
ATOM   3577  O   ILE A 487      19.418  53.766  52.554  1.00 66.02           O  
ANISOU 3577  O   ILE A 487     8433  10036   6616   1457   2387   2548       O  
ATOM   3578  CB  ILE A 487      19.492  54.984  55.402  1.00 71.28           C  
ANISOU 3578  CB  ILE A 487     9563  10923   6599   1859   2627   2536       C  
ATOM   3579  N   ILE A 488      21.584  54.276  52.830  1.00 76.55           N  
ANISOU 3579  N   ILE A 488    10103  11203   7779   1469   2085   2272       N  
ATOM   3580  CA  ILE A 488      22.033  53.248  51.914  1.00 66.33           C  
ANISOU 3580  CA  ILE A 488     8674   9788   6739   1275   1939   2307       C  
ATOM   3581  C   ILE A 488      22.362  52.008  52.724  1.00 65.58           C  
ANISOU 3581  C   ILE A 488     8619   9692   6605   1213   1926   2478       C  
ATOM   3582  O   ILE A 488      23.256  52.042  53.567  1.00 67.85           O  
ANISOU 3582  O   ILE A 488     9106   9965   6710   1268   1847   2436       O  
ATOM   3583  CB  ILE A 488      23.280  53.707  51.103  1.00 69.84           C  
ANISOU 3583  CB  ILE A 488     9195  10086   7256   1218   1710   2084       C  
ATOM   3584  CG1 ILE A 488      23.086  55.114  50.507  1.00 65.76           C  
ANISOU 3584  CG1 ILE A 488     8697   9568   6723   1305   1718   1903       C  
ATOM   3585  CG2 ILE A 488      23.602  52.714  50.004  1.00 63.08           C  
ANISOU 3585  CG2 ILE A 488     8184   9111   6672   1033   1582   2109       C  
ATOM   3586  CD1 ILE A 488      21.990  55.208  49.471  1.00 59.88           C  
ANISOU 3586  CD1 ILE A 488     7731   8848   6173   1264   1805   1942       C  
ATOM   3587  N   ARG A 489      21.649  50.910  52.503  1.00 66.19           N  
ANISOU 3587  N   ARG A 489     8515   9782   6852   1100   1996   2677       N  
ATOM   3588  CA  ARG A 489      22.036  49.678  53.195  1.00 71.23           C  
ANISOU 3588  CA  ARG A 489     9196  10394   7476   1028   1963   2842       C  
ATOM   3589  C   ARG A 489      22.099  48.481  52.251  1.00 79.78           C  
ANISOU 3589  C   ARG A 489    10110  11352   8852    832   1855   2920       C  
ATOM   3590  O   ARG A 489      22.919  47.591  52.431  1.00 93.00           O  
ANISOU 3590  O   ARG A 489    11846  12931  10559    757   1728   2960       O  
ATOM   3591  CB  ARG A 489      21.099  49.379  54.372  1.00 64.91           C  
ANISOU 3591  CB  ARG A 489     8400   9750   6514   1110   2189   3067       C  
ATOM   3592  CG  ARG A 489      20.879  50.566  55.303  1.00 72.90           C  
ANISOU 3592  CG  ARG A 489     9577  10896   7226   1322   2322   2994       C  
ATOM   3593  CD  ARG A 489      20.424  50.146  56.698  1.00 95.25           C  
ANISOU 3593  CD  ARG A 489    12497  13863   9832   1414   2501   3202       C  
ATOM   3594  NE  ARG A 489      21.455  49.408  57.434  1.00108.86           N  
ANISOU 3594  NE  ARG A 489    14392  15524  11445   1383   2370   3245       N  
ATOM   3595  CZ  ARG A 489      22.121  49.893  58.482  1.00118.60           C  
ANISOU 3595  CZ  ARG A 489    15884  16796  12383   1520   2341   3173       C  
ATOM   3596  NH1 ARG A 489      21.879  51.125  58.914  1.00120.66           N1+
ANISOU 3596  NH1 ARG A 489    16267  17140  12438   1692   2422   3031       N1+
ATOM   3597  NH2 ARG A 489      23.039  49.153  59.095  1.00121.68           N  
ANISOU 3597  NH2 ARG A 489    16411  17126  12695   1483   2208   3226       N  
ATOM   3598  N   GLU A 490      21.262  48.466  51.226  1.00 71.00           N  
ANISOU 3598  N   GLU A 490     8793  10232   7951    754   1893   2934       N  
ATOM   3599  CA  GLU A 490      21.311  47.380  50.259  1.00 62.36           C  
ANISOU 3599  CA  GLU A 490     7553   9008   7133    572   1776   2986       C  
ATOM   3600  C   GLU A 490      22.444  47.649  49.232  1.00 78.77           C  
ANISOU 3600  C   GLU A 490     9682  10940   9308    525   1561   2755       C  
ATOM   3601  O   GLU A 490      22.991  48.756  49.175  1.00 81.60           O  
ANISOU 3601  O   GLU A 490    10150  11308   9545    623   1521   2570       O  
ATOM   3602  CB  GLU A 490      19.939  47.217  49.594  1.00 53.06           C  
ANISOU 3602  CB  GLU A 490     6136   7882   6142    502   1891   3101       C  
ATOM   3603  N   ASP A 491      22.823  46.643  48.445  1.00 69.66           N  
ANISOU 3603  N   ASP A 491     8454   9647   8366    379   1425   2769       N  
ATOM   3604  CA  ASP A 491      23.938  46.815  47.514  1.00 59.31           C  
ANISOU 3604  CA  ASP A 491     7191   8205   7140    342   1236   2566       C  
ATOM   3605  C   ASP A 491      23.454  47.444  46.218  1.00 60.50           C  
ANISOU 3605  C   ASP A 491     7216   8339   7431    310   1223   2446       C  
ATOM   3606  O   ASP A 491      24.201  48.157  45.558  1.00 64.78           O  
ANISOU 3606  O   ASP A 491     7812   8828   7972    334   1122   2254       O  
ATOM   3607  CB  ASP A 491      24.646  45.487  47.232  1.00 64.16           C  
ANISOU 3607  CB  ASP A 491     7801   8671   7905    222   1093   2616       C  
ATOM   3608  N   ARG A 492      22.194  47.214  45.867  1.00 57.89           N  
ANISOU 3608  N   ARG A 492     6715   8059   7220    257   1324   2565       N  
ATOM   3609  CA  ARG A 492      21.625  47.869  44.699  1.00 54.37           C  
ANISOU 3609  CA  ARG A 492     6150   7614   6892    239   1318   2464       C  
ATOM   3610  C   ARG A 492      21.366  49.359  44.943  1.00 63.45           C  
ANISOU 3610  C   ARG A 492     7354   8878   7876    391   1415   2358       C  
ATOM   3611  O   ARG A 492      21.467  50.168  44.020  1.00 63.12           O  
ANISOU 3611  O   ARG A 492     7297   8808   7878    406   1361   2203       O  
ATOM   3612  CB  ARG A 492      20.325  47.184  44.275  1.00 56.13           C  
ANISOU 3612  CB  ARG A 492     6166   7861   7300    135   1385   2630       C  
ATOM   3613  CG  ARG A 492      20.503  45.775  43.785  1.00 58.31           C  
ANISOU 3613  CG  ARG A 492     6384   7999   7774    -27   1266   2709       C  
ATOM   3614  CD  ARG A 492      19.198  45.215  43.236  1.00 59.40           C  
ANISOU 3614  CD  ARG A 492     6309   8150   8110   -141   1309   2853       C  
ATOM   3615  NE  ARG A 492      19.355  43.804  42.906  1.00 62.55           N  
ANISOU 3615  NE  ARG A 492     6672   8406   8691   -297   1194   2942       N  
ATOM   3616  CZ  ARG A 492      19.568  43.342  41.683  1.00 62.58           C  
ANISOU 3616  CZ  ARG A 492     6635   8270   8873   -403   1037   2845       C  
ATOM   3617  NH1 ARG A 492      19.615  44.176  40.655  1.00 62.00           N1+
ANISOU 3617  NH1 ARG A 492     6543   8192   8822   -375    982   2669       N1+
ATOM   3618  NH2 ARG A 492      19.709  42.040  41.494  1.00 63.88           N  
ANISOU 3618  NH2 ARG A 492     6786   8297   9191   -533    936   2929       N  
ATOM   3619  N   GLU A 493      21.002  49.718  46.174  1.00 69.65           N  
ANISOU 3619  N   GLU A 493     8207   9788   8469    507   1563   2446       N  
ATOM   3620  CA  GLU A 493      20.788  51.122  46.508  1.00 64.69           C  
ANISOU 3620  CA  GLU A 493     7656   9257   7665    667   1655   2341       C  
ATOM   3621  C   GLU A 493      22.076  51.892  46.280  1.00 62.39           C  
ANISOU 3621  C   GLU A 493     7535   8882   7290    711   1510   2120       C  
ATOM   3622  O   GLU A 493      22.044  53.005  45.748  1.00 55.22           O  
ANISOU 3622  O   GLU A 493     6645   7977   6360    775   1503   1976       O  
ATOM   3623  CB  GLU A 493      20.329  51.300  47.960  1.00 62.97           C  
ANISOU 3623  CB  GLU A 493     7519   9180   7228    797   1831   2465       C  
ATOM   3624  CG  GLU A 493      18.915  50.815  48.230  1.00 76.21           C  
ANISOU 3624  CG  GLU A 493     9012  10973   8972    782   2015   2687       C  
ATOM   3625  CD  GLU A 493      18.620  50.659  49.716  1.00 90.23           C  
ANISOU 3625  CD  GLU A 493    10876  12875  10533    887   2182   2842       C  
ATOM   3626  OE1 GLU A 493      17.635  49.971  50.053  1.00101.65           O  
ANISOU 3626  OE1 GLU A 493    12175  14404  12042    847   2323   3061       O  
ATOM   3627  OE2 GLU A 493      19.371  51.216  50.547  1.00 87.76           O1-
ANISOU 3627  OE2 GLU A 493    10779  12578   9988   1006   2170   2750       O1-
ATOM   3628  N   ALA A 494      23.199  51.285  46.684  1.00 52.93           N  
ANISOU 3628  N   ALA A 494     6455   7605   6052    672   1393   2104       N  
ATOM   3629  CA  ALA A 494      24.507  51.943  46.654  1.00 48.86           C  
ANISOU 3629  CA  ALA A 494     6101   7016   5448    711   1253   1916       C  
ATOM   3630  C   ALA A 494      24.953  52.125  45.238  1.00 53.20           C  
ANISOU 3630  C   ALA A 494     6581   7459   6174    627   1126   1775       C  
ATOM   3631  O   ALA A 494      25.557  53.137  44.899  1.00 56.84           O  
ANISOU 3631  O   ALA A 494     7122   7890   6584    675   1061   1609       O  
ATOM   3632  CB  ALA A 494      25.544  51.150  47.425  1.00 43.45           C  
ANISOU 3632  CB  ALA A 494     5534   6279   4697    687   1156   1954       C  
ATOM   3633  N   GLN A 495      24.647  51.115  44.430  1.00 53.78           N  
ANISOU 3633  N   GLN A 495     6511   7472   6451    501   1090   1850       N  
ATOM   3634  CA  GLN A 495      24.857  51.126  43.001  1.00 45.82           C  
ANISOU 3634  CA  GLN A 495     5419   6371   5620    416    987   1743       C  
ATOM   3635  C   GLN A 495      24.013  52.181  42.269  1.00 43.62           C  
ANISOU 3635  C   GLN A 495     5065   6145   5365    459   1052   1675       C  
ATOM   3636  O   GLN A 495      24.522  52.929  41.440  1.00 46.52           O  
ANISOU 3636  O   GLN A 495     5460   6459   5755    465    975   1521       O  
ATOM   3637  CB  GLN A 495      24.545  49.755  42.454  1.00 58.52           C  
ANISOU 3637  CB  GLN A 495     6904   7909   7422    281    946   1855       C  
ATOM   3638  CG  GLN A 495      25.193  49.460  41.143  1.00 71.45           C  
ANISOU 3638  CG  GLN A 495     8508   9421   9217    193    803   1737       C  
ATOM   3639  CD  GLN A 495      25.117  48.002  40.840  1.00 78.51           C  
ANISOU 3639  CD  GLN A 495     9330  10227  10275     72    743   1842       C  
ATOM   3640  NE2 GLN A 495      26.042  47.520  40.023  1.00 73.80           N  
ANISOU 3640  NE2 GLN A 495     8755   9506   9779     15    607   1744       N  
ATOM   3641  OE1 GLN A 495      24.245  47.295  41.363  1.00 83.81           O  
ANISOU 3641  OE1 GLN A 495     9927  10935  10981     34    819   2015       O  
ATOM   3642  N   LEU A 496      22.726  52.239  42.567  1.00 40.93           N  
ANISOU 3642  N   LEU A 496     4623   5907   5022    492   1195   1799       N  
ATOM   3643  CA  LEU A 496      21.877  53.237  41.924  1.00 46.18           C  
ANISOU 3643  CA  LEU A 496     5210   6627   5710    546   1258   1746       C  
ATOM   3644  C   LEU A 496      22.400  54.605  42.301  1.00 52.73           C  
ANISOU 3644  C   LEU A 496     6195   7477   6361    680   1267   1599       C  
ATOM   3645  O   LEU A 496      22.660  55.445  41.422  1.00 55.88           O  
ANISOU 3645  O   LEU A 496     6610   7830   6794    690   1203   1458       O  
ATOM   3646  CB  LEU A 496      20.403  53.088  42.337  1.00 41.52           C  
ANISOU 3646  CB  LEU A 496     4476   6160   5138    575   1424   1919       C  
ATOM   3647  CG  LEU A 496      19.420  53.997  41.583  1.00 49.03           C  
ANISOU 3647  CG  LEU A 496     5315   7168   6148    625   1483   1883       C  
ATOM   3648  CD1 LEU A 496      19.429  53.706  40.081  1.00 47.96           C  
ANISOU 3648  CD1 LEU A 496     5074   6935   6214    501   1348   1821       C  
ATOM   3649  CD2 LEU A 496      17.997  53.900  42.124  1.00 43.43           C  
ANISOU 3649  CD2 LEU A 496     4456   6598   5448    672   1661   2063       C  
ATOM   3650  N   ALA A 497      22.580  54.794  43.611  1.00 48.21           N  
ANISOU 3650  N   ALA A 497     5750   6969   5600    778   1339   1634       N  
ATOM   3651  CA  ALA A 497      22.972  56.069  44.197  1.00 46.82           C  
ANISOU 3651  CA  ALA A 497     5741   6818   5230    917   1356   1507       C  
ATOM   3652  C   ALA A 497      24.249  56.589  43.544  1.00 52.66           C  
ANISOU 3652  C   ALA A 497     6581   7439   5989    881   1187   1324       C  
ATOM   3653  O   ALA A 497      24.339  57.751  43.151  1.00 52.81           O  
ANISOU 3653  O   ALA A 497     6654   7440   5972    943   1171   1195       O  
ATOM   3654  CB  ALA A 497      23.166  55.922  45.696  1.00 44.59           C  
ANISOU 3654  CB  ALA A 497     5597   6602   4741   1005   1423   1575       C  
ATOM   3655  N   ALA A 498      25.222  55.698  43.414  1.00 49.68           N  
ANISOU 3655  N   ALA A 498     6219   6979   5680    778   1065   1323       N  
ATOM   3656  CA  ALA A 498      26.485  56.021  42.800  1.00 47.79           C  
ANISOU 3656  CA  ALA A 498     6050   6632   5478    733    909   1173       C  
ATOM   3657  C   ALA A 498      26.324  56.374  41.302  1.00 50.86           C  
ANISOU 3657  C   ALA A 498     6333   6965   6025    672    866   1092       C  
ATOM   3658  O   ALA A 498      26.972  57.292  40.788  1.00 47.37           O  
ANISOU 3658  O   ALA A 498     5956   6470   5572    686    795    953       O  
ATOM   3659  CB  ALA A 498      27.439  54.860  42.983  1.00 46.06           C  
ANISOU 3659  CB  ALA A 498     5844   6347   5312    645    804   1213       C  
ATOM   3660  N   ARG A 499      25.464  55.642  40.602  1.00 40.14           N  
ANISOU 3660  N   ARG A 499     4819   5617   4814    601    902   1183       N  
ATOM   3661  CA  ARG A 499      25.261  55.933  39.199  1.00 48.08           C  
ANISOU 3661  CA  ARG A 499     5736   6575   5956    548    857   1113       C  
ATOM   3662  C   ARG A 499      24.698  57.358  39.033  1.00 42.78           C  
ANISOU 3662  C   ARG A 499     5092   5951   5214    651    920   1039       C  
ATOM   3663  O   ARG A 499      25.269  58.169  38.322  1.00 41.01           O  
ANISOU 3663  O   ARG A 499     4917   5667   4998    653    851    912       O  
ATOM   3664  CB  ARG A 499      24.338  54.892  38.541  1.00 43.00           C  
ANISOU 3664  CB  ARG A 499     4924   5936   5478    454    875   1228       C  
ATOM   3665  CG  ARG A 499      24.295  55.039  37.014  1.00 46.20           C  
ANISOU 3665  CG  ARG A 499     5255   6278   6022    387    797   1146       C  
ATOM   3666  CD  ARG A 499      25.634  54.646  36.397  1.00 42.94           C  
ANISOU 3666  CD  ARG A 499     4902   5753   5660    317    664   1046       C  
ATOM   3667  NE  ARG A 499      25.961  53.276  36.786  1.00 55.91           N  
ANISOU 3667  NE  ARG A 499     6528   7355   7360    245    627   1133       N  
ATOM   3668  CZ  ARG A 499      27.187  52.811  36.993  1.00 71.40           C  
ANISOU 3668  CZ  ARG A 499     8568   9248   9313    222    543   1089       C  
ATOM   3669  NH1 ARG A 499      28.241  53.600  36.821  1.00 79.64           N1+
ANISOU 3669  NH1 ARG A 499     9702  10259  10301    255    485    960       N1+
ATOM   3670  NH2 ARG A 499      27.357  51.546  37.360  1.00 76.43           N  
ANISOU 3670  NH2 ARG A 499     9186   9845  10007    164    513   1181       N  
ATOM   3671  N   LEU A 500      23.582  57.631  39.699  1.00 40.81           N  
ANISOU 3671  N   LEU A 500     4806   5805   4896    739   1057   1127       N  
ATOM   3672  CA  LEU A 500      23.005  58.969  39.808  1.00 41.42           C  
ANISOU 3672  CA  LEU A 500     4926   5932   4880    868   1135   1069       C  
ATOM   3673  C   LEU A 500      24.057  60.059  40.021  1.00 51.54           C  
ANISOU 3673  C   LEU A 500     6391   7151   6041    928   1062    910       C  
ATOM   3674  O   LEU A 500      24.080  61.056  39.315  1.00 53.91           O  
ANISOU 3674  O   LEU A 500     6715   7412   6357    958   1033    810       O  
ATOM   3675  CB  LEU A 500      21.999  58.988  40.952  1.00 38.03           C  
ANISOU 3675  CB  LEU A 500     4481   5627   4340    977   1299   1187       C  
ATOM   3676  CG  LEU A 500      20.775  58.146  40.606  1.00 55.03           C  
ANISOU 3676  CG  LEU A 500     6426   7849   6636    920   1379   1347       C  
ATOM   3677  CD1 LEU A 500      19.879  57.858  41.823  1.00 40.71           C  
ANISOU 3677  CD1 LEU A 500     4578   6165   4726   1004   1550   1502       C  
ATOM   3678  CD2 LEU A 500      19.994  58.799  39.442  1.00 57.19           C  
ANISOU 3678  CD2 LEU A 500     6582   8124   7024    927   1378   1311       C  
ATOM   3679  N   LEU A 501      24.952  59.854  40.979  1.00 55.97           N  
ANISOU 3679  N   LEU A 501     7081   7696   6489    939   1021    892       N  
ATOM   3680  CA  LEU A 501      25.961  60.862  41.288  1.00 49.90           C  
ANISOU 3680  CA  LEU A 501     6488   6866   5607    988    939    749       C  
ATOM   3681  C   LEU A 501      26.952  61.058  40.152  1.00 50.29           C  
ANISOU 3681  C   LEU A 501     6531   6805   5774    888    800    641       C  
ATOM   3682  O   LEU A 501      27.631  62.076  40.108  1.00 64.47           O  
ANISOU 3682  O   LEU A 501     8440   8541   7513    918    734    521       O  
ATOM   3683  CB  LEU A 501      26.716  60.490  42.571  1.00 48.70           C  
ANISOU 3683  CB  LEU A 501     6469   6723   5313   1012    908    763       C  
ATOM   3684  CG  LEU A 501      25.797  60.455  43.789  1.00 51.54           C  
ANISOU 3684  CG  LEU A 501     6867   7197   5517   1132   1057    862       C  
ATOM   3685  CD1 LEU A 501      26.517  59.996  45.045  1.00 49.85           C  
ANISOU 3685  CD1 LEU A 501     6790   6997   5155   1154   1021    889       C  
ATOM   3686  CD2 LEU A 501      25.160  61.819  44.000  1.00 53.04           C  
ANISOU 3686  CD2 LEU A 501     7140   7421   5592   1279   1141    787       C  
ATOM   3687  N   GLN A 502      27.062  60.080  39.253  1.00 44.54           N  
ANISOU 3687  N   GLN A 502     5674   6045   5205    771    754    685       N  
ATOM   3688  CA  GLN A 502      27.973  60.212  38.120  1.00 41.93           C  
ANISOU 3688  CA  GLN A 502     5329   5619   4981    684    640    591       C  
ATOM   3689  C   GLN A 502      27.378  60.990  36.945  1.00 35.54           C  
ANISOU 3689  C   GLN A 502     4461   4795   4245    689    656    544       C  
ATOM   3690  O   GLN A 502      27.904  60.953  35.840  1.00 45.89           O  
ANISOU 3690  O   GLN A 502     5735   6042   5658    612    582    491       O  
ATOM   3691  CB  GLN A 502      28.404  58.854  37.639  1.00 39.15           C  
ANISOU 3691  CB  GLN A 502     4887   5232   4757    571    581    643       C  
ATOM   3692  CG  GLN A 502      29.176  58.110  38.619  1.00 46.98           C  
ANISOU 3692  CG  GLN A 502     5939   6217   5696    558    538    679       C  
ATOM   3693  CD  GLN A 502      29.254  56.654  38.279  1.00 48.75           C  
ANISOU 3693  CD  GLN A 502     6065   6415   6045    465    509    762       C  
ATOM   3694  NE2 GLN A 502      30.270  55.989  38.814  1.00 46.21           N  
ANISOU 3694  NE2 GLN A 502     5791   6054   5712    437    432    768       N  
ATOM   3695  OE1 GLN A 502      28.420  56.124  37.530  1.00 39.85           O  
ANISOU 3695  OE1 GLN A 502     4821   5294   5026    419    543    818       O  
ATOM   3696  N   PHE A 503      26.287  61.698  37.193  1.00 41.87           N  
ANISOU 3696  N   PHE A 503     5259   5661   4990    787    756    567       N  
ATOM   3697  CA  PHE A 503      25.632  62.461  36.142  1.00 50.10           C  
ANISOU 3697  CA  PHE A 503     6245   6694   6095    806    771    534       C  
ATOM   3698  C   PHE A 503      26.458  63.638  35.671  1.00 49.18           C  
ANISOU 3698  C   PHE A 503     6240   6492   5953    816    696    405       C  
ATOM   3699  O   PHE A 503      26.505  63.909  34.473  1.00 59.23           O  
ANISOU 3699  O   PHE A 503     7467   7721   7317    768    653    368       O  
ATOM   3700  CB  PHE A 503      24.265  62.946  36.610  1.00 45.22           C  
ANISOU 3700  CB  PHE A 503     5591   6169   5423    925    901    597       C  
ATOM   3701  CG  PHE A 503      23.529  63.761  35.597  1.00 43.86           C  
ANISOU 3701  CG  PHE A 503     5360   5991   5314    959    915    571       C  
ATOM   3702  CD1 PHE A 503      23.206  63.235  34.369  1.00 42.37           C  
ANISOU 3702  CD1 PHE A 503     5041   5789   5271    867    871    601       C  
ATOM   3703  CD2 PHE A 503      23.131  65.055  35.886  1.00 53.17           C  
ANISOU 3703  CD2 PHE A 503     6625   7176   6401   1092    967    517       C  
ATOM   3704  CE1 PHE A 503      22.519  64.000  33.436  1.00 48.75           C  
ANISOU 3704  CE1 PHE A 503     5799   6593   6128    903    874    582       C  
ATOM   3705  CE2 PHE A 503      22.432  65.817  34.958  1.00 48.41           C  
ANISOU 3705  CE2 PHE A 503     5969   6566   5857   1132    975    501       C  
ATOM   3706  CZ  PHE A 503      22.127  65.283  33.739  1.00 43.77           C  
ANISOU 3706  CZ  PHE A 503     5247   5971   5413   1036    928    537       C  
ATOM   3707  N   GLU A 504      27.113  64.326  36.602  1.00 47.32           N  
ANISOU 3707  N   GLU A 504     6155   6232   5593    875    675    338       N  
ATOM   3708  CA  GLU A 504      27.922  65.495  36.256  1.00 56.24           C  
ANISOU 3708  CA  GLU A 504     7397   7270   6700    878    596    220       C  
ATOM   3709  C   GLU A 504      29.133  65.067  35.443  1.00 54.25           C  
ANISOU 3709  C   GLU A 504     7117   6946   6551    748    485    181       C  
ATOM   3710  O   GLU A 504      29.504  65.735  34.459  1.00 50.21           O  
ANISOU 3710  O   GLU A 504     6610   6369   6098    710    438    122       O  
ATOM   3711  CB  GLU A 504      28.371  66.274  37.507  1.00 56.28           C  
ANISOU 3711  CB  GLU A 504     7578   7257   6548    964    580    154       C  
ATOM   3712  CG  GLU A 504      29.119  67.587  37.214  1.00 57.08           C  
ANISOU 3712  CG  GLU A 504     7805   7253   6631    968    494     34       C  
ATOM   3713  CD  GLU A 504      29.538  68.374  38.472  1.00 70.75           C  
ANISOU 3713  CD  GLU A 504     9727   8954   8202   1052    461    -41       C  
ATOM   3714  OE1 GLU A 504      28.705  68.615  39.375  1.00 75.34           O  
ANISOU 3714  OE1 GLU A 504    10372   9595   8657   1182    553    -24       O  
ATOM   3715  OE2 GLU A 504      30.723  68.746  38.567  1.00 77.71           O1-
ANISOU 3715  OE2 GLU A 504    10695   9749   9081    989    339   -117       O1-
ATOM   3716  N   GLU A 505      29.739  63.946  35.826  1.00 47.58           N  
ANISOU 3716  N   GLU A 505     6239   6111   5728    683    450    222       N  
ATOM   3717  CA  GLU A 505      30.986  63.580  35.190  1.00 40.53           C  
ANISOU 3717  CA  GLU A 505     5328   5151   4922    578    350    181       C  
ATOM   3718  C   GLU A 505      30.701  63.067  33.781  1.00 43.20           C  
ANISOU 3718  C   GLU A 505     5542   5480   5392    509    355    203       C  
ATOM   3719  O   GLU A 505      31.590  63.081  32.916  1.00 43.21           O  
ANISOU 3719  O   GLU A 505     5527   5425   5467    438    292    157       O  
ATOM   3720  CB  GLU A 505      31.775  62.573  36.038  1.00 55.30           C  
ANISOU 3720  CB  GLU A 505     7208   7028   6776    543    301    213       C  
ATOM   3721  CG  GLU A 505      31.278  61.126  36.030  1.00 68.77           C  
ANISOU 3721  CG  GLU A 505     8805   8780   8545    507    340    317       C  
ATOM   3722  CD  GLU A 505      32.180  60.182  36.831  1.00 65.46           C  
ANISOU 3722  CD  GLU A 505     8407   8352   8115    474    278    347       C  
ATOM   3723  OE1 GLU A 505      32.191  60.258  38.087  1.00 64.62           O  
ANISOU 3723  OE1 GLU A 505     8388   8279   7886    533    286    368       O  
ATOM   3724  OE2 GLU A 505      32.873  59.361  36.200  1.00 61.57           O1-
ANISOU 3724  OE2 GLU A 505     7847   7818   7730    397    222    350       O1-
ATOM   3725  N   THR A 506      29.454  62.662  33.546  1.00 37.85           N  
ANISOU 3725  N   THR A 506     4778   4861   4741    533    430    275       N  
ATOM   3726  CA  THR A 506      29.012  62.227  32.214  1.00 42.47           C  
ANISOU 3726  CA  THR A 506     5256   5440   5441    475    427    294       C  
ATOM   3727  C   THR A 506      28.804  63.419  31.300  1.00 45.12           C  
ANISOU 3727  C   THR A 506     5617   5745   5781    500    425    237       C  
ATOM   3728  O   THR A 506      29.241  63.443  30.168  1.00 51.55           O  
ANISOU 3728  O   THR A 506     6408   6516   6662    441    380    202       O  
ATOM   3729  CB  THR A 506      27.707  61.434  32.280  1.00 41.91           C  
ANISOU 3729  CB  THR A 506     5078   5439   5408    485    494    395       C  
ATOM   3730  CG2 THR A 506      27.384  60.867  30.910  1.00 37.51           C  
ANISOU 3730  CG2 THR A 506     4422   4862   4969    412    461    406       C  
ATOM   3731  OG1 THR A 506      27.836  60.370  33.241  1.00 42.06           O  
ANISOU 3731  OG1 THR A 506     5083   5484   5414    467    504    464       O  
ATOM   3732  N   LEU A 507      28.089  64.394  31.825  1.00 50.05           N  
ANISOU 3732  N   LEU A 507     6294   6396   6329    597    479    232       N  
ATOM   3733  CA  LEU A 507      27.995  65.723  31.264  1.00 43.17           C  
ANISOU 3733  CA  LEU A 507     5484   5481   5438    641    473    172       C  
ATOM   3734  C   LEU A 507      29.356  66.307  30.877  1.00 48.52           C  
ANISOU 3734  C   LEU A 507     6244   6070   6123    582    391     90       C  
ATOM   3735  O   LEU A 507      29.547  66.885  29.802  1.00 43.98           O  
ANISOU 3735  O   LEU A 507     5670   5447   5592    553    364     59       O  
ATOM   3736  CB  LEU A 507      27.332  66.630  32.290  1.00 42.08           C  
ANISOU 3736  CB  LEU A 507     5427   5370   5190    768    536    165       C  
ATOM   3737  CG  LEU A 507      25.816  66.519  32.434  1.00 45.32           C  
ANISOU 3737  CG  LEU A 507     5750   5870   5599    853    634    244       C  
ATOM   3738  CD1 LEU A 507      25.362  67.311  33.642  1.00 43.79           C  
ANISOU 3738  CD1 LEU A 507     5654   5706   5277    990    706    231       C  
ATOM   3739  CD2 LEU A 507      25.165  67.058  31.197  1.00 42.89           C  
ANISOU 3739  CD2 LEU A 507     5384   5549   5362    859    630    245       C  
ATOM   3740  N   THR A 508      30.305  66.171  31.783  1.00 51.27           N  
ANISOU 3740  N   THR A 508     6658   6396   6426    565    349     62       N  
ATOM   3741  CA  THR A 508      31.609  66.778  31.599  1.00 45.66           C  
ANISOU 3741  CA  THR A 508     6019   5605   5726    509    268     -9       C  
ATOM   3742  C   THR A 508      32.340  66.139  30.414  1.00 51.14           C  
ANISOU 3742  C   THR A 508     6627   6275   6528    407    232     -5       C  
ATOM   3743  O   THR A 508      32.899  66.860  29.549  1.00 39.23           O  
ANISOU 3743  O   THR A 508     5139   4711   5057    367    201    -43       O  
ATOM   3744  CB  THR A 508      32.413  66.658  32.892  1.00 46.03           C  
ANISOU 3744  CB  THR A 508     6143   5642   5703    514    221    -32       C  
ATOM   3745  CG2 THR A 508      33.726  67.367  32.791  1.00 28.12           C  
ANISOU 3745  CG2 THR A 508     3941   3289   3453    453    127   -100       C  
ATOM   3746  OG1 THR A 508      31.648  67.249  33.952  1.00 45.88           O  
ANISOU 3746  OG1 THR A 508     6216   5650   5566    624    267    -38       O  
ATOM   3747  N   VAL A 509      32.297  64.799  30.362  1.00 45.43           N  
ANISOU 3747  N   VAL A 509     5815   5594   5854    369    240     43       N  
ATOM   3748  CA  VAL A 509      32.819  64.045  29.219  1.00 42.89           C  
ANISOU 3748  CA  VAL A 509     5414   5256   5627    291    217     46       C  
ATOM   3749  C   VAL A 509      32.194  64.507  27.891  1.00 39.84           C  
ANISOU 3749  C   VAL A 509     5001   4864   5274    289    240     43       C  
ATOM   3750  O   VAL A 509      32.897  64.841  26.942  1.00 41.55           O  
ANISOU 3750  O   VAL A 509     5221   5040   5526    244    218     11       O  
ATOM   3751  CB  VAL A 509      32.578  62.534  29.377  1.00 48.92           C  
ANISOU 3751  CB  VAL A 509     6096   6057   6434    266    225    102       C  
ATOM   3752  CG1 VAL A 509      32.815  61.822  28.056  1.00 52.75           C  
ANISOU 3752  CG1 VAL A 509     6512   6524   7007    206    211     97       C  
ATOM   3753  CG2 VAL A 509      33.492  61.963  30.425  1.00 48.31           C  
ANISOU 3753  CG2 VAL A 509     6040   5973   6341    252    185    105       C  
ATOM   3754  N   VAL A 510      30.871  64.530  27.846  1.00 30.25           N  
ANISOU 3754  N   VAL A 510     3755   3693   4044    340    286     83       N  
ATOM   3755  CA  VAL A 510      30.141  64.980  26.679  1.00 30.58           C  
ANISOU 3755  CA  VAL A 510     3773   3735   4111    349    298     87       C  
ATOM   3756  C   VAL A 510      30.579  66.374  26.288  1.00 38.78           C  
ANISOU 3756  C   VAL A 510     4897   4717   5120    364    285     39       C  
ATOM   3757  O   VAL A 510      30.737  66.657  25.119  1.00 46.25           O  
ANISOU 3757  O   VAL A 510     5840   5638   6096    333    271     29       O  
ATOM   3758  CB  VAL A 510      28.608  64.958  26.925  1.00 28.88           C  
ANISOU 3758  CB  VAL A 510     3507   3582   3884    417    348    144       C  
ATOM   3759  CG1 VAL A 510      27.886  65.589  25.786  1.00 31.98           C  
ANISOU 3759  CG1 VAL A 510     3884   3972   4296    437    347    147       C  
ATOM   3760  CG2 VAL A 510      28.127  63.527  27.083  1.00 34.32           C  
ANISOU 3760  CG2 VAL A 510     4098   4318   4624    381    354    205       C  
ATOM   3761  N   ALA A 511      30.834  67.232  27.271  1.00 48.46           N  
ANISOU 3761  N   ALA A 511     6210   5916   6285    409    283     10       N  
ATOM   3762  CA  ALA A 511      31.158  68.628  26.974  1.00 44.51           C  
ANISOU 3762  CA  ALA A 511     5801   5347   5762    424    263    -32       C  
ATOM   3763  C   ALA A 511      32.608  68.792  26.537  1.00 48.44           C  
ANISOU 3763  C   ALA A 511     6321   5784   6300    333    212    -66       C  
ATOM   3764  O   ALA A 511      32.933  69.670  25.733  1.00 46.10           O  
ANISOU 3764  O   ALA A 511     6063   5432   6019    310    198    -80       O  
ATOM   3765  CB  ALA A 511      30.861  69.525  28.182  1.00 33.73           C  
ANISOU 3765  CB  ALA A 511     4537   3963   4314    510    272    -60       C  
ATOM   3766  N   ARG A 512      33.485  67.942  27.059  1.00 45.78           N  
ANISOU 3766  N   ARG A 512     5952   5457   5984    283    185    -71       N  
ATOM   3767  CA  ARG A 512      34.884  68.002  26.667  1.00 38.87           C  
ANISOU 3767  CA  ARG A 512     5072   4537   5160    199    141    -93       C  
ATOM   3768  C   ARG A 512      35.072  67.300  25.308  1.00 42.82           C  
ANISOU 3768  C   ARG A 512     5490   5057   5723    150    164    -72       C  
ATOM   3769  O   ARG A 512      35.627  67.862  24.381  1.00 46.57           O  
ANISOU 3769  O   ARG A 512     5973   5498   6225    109    164    -78       O  
ATOM   3770  CB  ARG A 512      35.750  67.366  27.747  1.00 43.76           C  
ANISOU 3770  CB  ARG A 512     5684   5162   5781    174     97   -103       C  
ATOM   3771  CG  ARG A 512      37.200  67.286  27.419  1.00 49.36           C  
ANISOU 3771  CG  ARG A 512     6359   5837   6558     92     51   -117       C  
ATOM   3772  CD  ARG A 512      37.755  65.942  27.834  1.00 62.59           C  
ANISOU 3772  CD  ARG A 512     7961   7552   8269     71     35   -100       C  
ATOM   3773  NE  ARG A 512      38.415  65.951  29.131  1.00 83.97           N  
ANISOU 3773  NE  ARG A 512    10707  10248  10952     69    -33   -115       N  
ATOM   3774  CZ  ARG A 512      39.665  66.371  29.332  1.00101.00           C  
ANISOU 3774  CZ  ARG A 512    12865  12362  13149     12   -102   -137       C  
ATOM   3775  NH1 ARG A 512      40.384  66.842  28.319  1.00 99.16           N1+
ANISOU 3775  NH1 ARG A 512    12592  12097  12987    -49    -98   -138       N1+
ATOM   3776  NH2 ARG A 512      40.194  66.333  30.550  1.00108.11           N  
ANISOU 3776  NH2 ARG A 512    13805  13253  14017     14   -178   -151       N  
ATOM   3777  N   GLU A 513      34.557  66.089  25.174  1.00 43.60           N  
ANISOU 3777  N   GLU A 513     5519   5209   5839    157    184    -47       N  
ATOM   3778  CA  GLU A 513      34.825  65.307  23.972  1.00 48.14           C  
ANISOU 3778  CA  GLU A 513     6032   5795   6464    116    196    -40       C  
ATOM   3779  C   GLU A 513      33.797  65.462  22.835  1.00 51.20           C  
ANISOU 3779  C   GLU A 513     6414   6200   6841    137    220    -25       C  
ATOM   3780  O   GLU A 513      34.008  64.961  21.730  1.00 53.69           O  
ANISOU 3780  O   GLU A 513     6701   6519   7180    109    227    -27       O  
ATOM   3781  CB  GLU A 513      34.959  63.835  24.358  1.00 41.94           C  
ANISOU 3781  CB  GLU A 513     5182   5040   5713    103    188    -27       C  
ATOM   3782  CG  GLU A 513      36.074  63.601  25.358  1.00 61.09           C  
ANISOU 3782  CG  GLU A 513     7608   7451   8154     81    153    -38       C  
ATOM   3783  CD  GLU A 513      36.547  62.157  25.384  1.00 87.40           C  
ANISOU 3783  CD  GLU A 513    10874  10795  11538     61    142    -27       C  
ATOM   3784  OE1 GLU A 513      35.694  61.260  25.219  1.00102.99           O  
ANISOU 3784  OE1 GLU A 513    12818  12792  13523     74    155     -3       O  
ATOM   3785  OE2 GLU A 513      37.770  61.917  25.552  1.00 87.01           O1-
ANISOU 3785  OE2 GLU A 513    10801  10729  11530     32    116    -40       O1-
ATOM   3786  N   GLY A 514      32.696  66.156  23.085  1.00 44.95           N  
ANISOU 3786  N   GLY A 514     5652   5417   6010    193    232     -9       N  
ATOM   3787  CA  GLY A 514      31.660  66.262  22.071  1.00 37.91           C  
ANISOU 3787  CA  GLY A 514     4745   4545   5114    217    241     12       C  
ATOM   3788  C   GLY A 514      30.999  64.955  21.649  1.00 42.23           C  
ANISOU 3788  C   GLY A 514     5215   5136   5693    204    233     34       C  
ATOM   3789  O   GLY A 514      30.606  64.795  20.493  1.00 44.17           O  
ANISOU 3789  O   GLY A 514     5450   5388   5944    195    221     38       O  
ATOM   3790  N   THR A 515      30.839  64.024  22.584  1.00 41.18           N  
ANISOU 3790  N   THR A 515     5037   5029   5581    202    233     51       N  
ATOM   3791  CA  THR A 515      30.243  62.731  22.264  1.00 37.80           C  
ANISOU 3791  CA  THR A 515     4537   4626   5197    178    216     76       C  
ATOM   3792  C   THR A 515      28.962  62.424  23.032  1.00 37.14           C  
ANISOU 3792  C   THR A 515     4399   4591   5123    212    230    134       C  
ATOM   3793  O   THR A 515      29.016  61.806  24.092  1.00 48.02           O  
ANISOU 3793  O   THR A 515     5753   5984   6507    211    243    160       O  
ATOM   3794  CB  THR A 515      31.235  61.610  22.533  1.00 44.51           C  
ANISOU 3794  CB  THR A 515     5369   5458   6085    133    201     61       C  
ATOM   3795  CG2 THR A 515      32.455  61.770  21.607  1.00 29.98           C  
ANISOU 3795  CG2 THR A 515     3561   3582   4247    102    198     12       C  
ATOM   3796  OG1 THR A 515      31.624  61.629  23.923  1.00 41.01           O  
ANISOU 3796  OG1 THR A 515     4935   5019   5627    147    213     72       O  
ATOM   3797  N   PRO A 516      27.807  62.830  22.484  1.00 35.10           N  
ANISOU 3797  N   PRO A 516     4111   4360   4865    243    229    162       N  
ATOM   3798  CA  PRO A 516      26.518  62.626  23.156  1.00 41.16           C  
ANISOU 3798  CA  PRO A 516     4805   5184   5650    281    253    228       C  
ATOM   3799  C   PRO A 516      26.185  61.160  23.415  1.00 41.10           C  
ANISOU 3799  C   PRO A 516     4716   5193   5707    227    234    273       C  
ATOM   3800  O   PRO A 516      25.253  60.870  24.156  1.00 48.26           O  
ANISOU 3800  O   PRO A 516     5553   6149   6635    247    264    342       O  
ATOM   3801  CB  PRO A 516      25.499  63.228  22.172  1.00 38.23           C  
ANISOU 3801  CB  PRO A 516     4408   4831   5285    311    232    245       C  
ATOM   3802  CG  PRO A 516      26.266  64.225  21.361  1.00 29.62           C  
ANISOU 3802  CG  PRO A 516     3413   3693   4150    318    221    189       C  
ATOM   3803  CD  PRO A 516      27.667  63.635  21.253  1.00 38.64           C  
ANISOU 3803  CD  PRO A 516     4596   4792   5294    253    209    140       C  
ATOM   3804  N   HIS A 517      26.920  60.235  22.822  1.00 39.55           N  
ANISOU 3804  N   HIS A 517     4528   4954   5546    161    187    240       N  
ATOM   3805  CA  HIS A 517      26.557  58.840  23.021  1.00 40.02           C  
ANISOU 3805  CA  HIS A 517     4519   5011   5676    108    158    283       C  
ATOM   3806  C   HIS A 517      26.979  58.374  24.406  1.00 39.09           C  
ANISOU 3806  C   HIS A 517     4401   4901   5552    111    197    317       C  
ATOM   3807  O   HIS A 517      26.459  57.382  24.915  1.00 36.22           O  
ANISOU 3807  O   HIS A 517     3973   4547   5240     80    192    382       O  
ATOM   3808  CB  HIS A 517      27.180  57.962  21.957  1.00 44.80           C  
ANISOU 3808  CB  HIS A 517     5147   5559   6317     50     95    231       C  
ATOM   3809  CG  HIS A 517      28.645  57.776  22.132  1.00 39.45           C  
ANISOU 3809  CG  HIS A 517     4530   4839   5620     43    104    176       C  
ATOM   3810  CD2 HIS A 517      29.359  56.726  22.599  1.00 31.99           C  
ANISOU 3810  CD2 HIS A 517     3583   3859   4712     14     91    175       C  
ATOM   3811  ND1 HIS A 517      29.558  58.760  21.819  1.00 37.46           N  
ANISOU 3811  ND1 HIS A 517     4343   4577   5313     67    128    122       N  
ATOM   3812  CE1 HIS A 517      30.778  58.317  22.077  1.00 32.71           C  
ANISOU 3812  CE1 HIS A 517     3765   3942   4720     52    130     90       C  
ATOM   3813  NE2 HIS A 517      30.679  57.090  22.560  1.00 35.57           N  
ANISOU 3813  NE2 HIS A 517     4091   4290   5136     26    107    119       N  
ATOM   3814  N   VAL A 518      27.914  59.101  25.015  1.00 35.84           N  
ANISOU 3814  N   VAL A 518     4060   4481   5077    146    227    279       N  
ATOM   3815  CA  VAL A 518      28.288  58.830  26.387  1.00 33.42           C  
ANISOU 3815  CA  VAL A 518     3767   4188   4743    162    257    309       C  
ATOM   3816  C   VAL A 518      27.053  59.005  27.290  1.00 40.94           C  
ANISOU 3816  C   VAL A 518     4671   5209   5674    210    316    391       C  
ATOM   3817  O   VAL A 518      26.715  58.110  28.050  1.00 44.81           O  
ANISOU 3817  O   VAL A 518     5116   5721   6190    192    333    462       O  
ATOM   3818  CB  VAL A 518      29.441  59.721  26.845  1.00 35.56           C  
ANISOU 3818  CB  VAL A 518     4127   4437   4948    190    263    249       C  
ATOM   3819  CG1 VAL A 518      29.631  59.619  28.320  1.00 39.87           C  
ANISOU 3819  CG1 VAL A 518     4699   5006   5444    221    289    282       C  
ATOM   3820  CG2 VAL A 518      30.729  59.306  26.149  1.00 24.87           C  
ANISOU 3820  CG2 VAL A 518     2795   3027   3629    141    217    190       C  
ATOM   3821  N   MET A 519      26.347  60.119  27.162  1.00 43.98           N  
ANISOU 3821  N   MET A 519     5061   5629   6020    272    352    389       N  
ATOM   3822  CA  MET A 519      25.121  60.300  27.922  1.00 36.14           C  
ANISOU 3822  CA  MET A 519     4010   4710   5013    331    421    469       C  
ATOM   3823  C   MET A 519      24.072  59.226  27.648  1.00 36.11           C  
ANISOU 3823  C   MET A 519     3879   4738   5105    278    411    558       C  
ATOM   3824  O   MET A 519      23.371  58.793  28.552  1.00 51.02           O  
ANISOU 3824  O   MET A 519     5704   6682   6999    294    468    648       O  
ATOM   3825  CB  MET A 519      24.508  61.666  27.632  1.00 36.33           C  
ANISOU 3825  CB  MET A 519     4055   4757   4993    414    453    447       C  
ATOM   3826  CG  MET A 519      23.209  61.908  28.414  1.00 35.80           C  
ANISOU 3826  CG  MET A 519     3918   4776   4910    495    538    532       C  
ATOM   3827  SD  MET A 519      23.443  61.823  30.171  1.00 81.95           S  
ANISOU 3827  SD  MET A 519     9817  10662  10659    555    620    566       S  
ATOM   3828  CE  MET A 519      24.585  63.156  30.414  1.00 33.73           C  
ANISOU 3828  CE  MET A 519     3883   4490   4442    612    600    445       C  
ATOM   3829  N   CYS A 520      23.940  58.803  26.403  1.00 39.61           N  
ANISOU 3829  N   CYS A 520     4285   5144   5621    215    337    537       N  
ATOM   3830  CA  CYS A 520      22.927  57.813  26.079  1.00 34.51           C  
ANISOU 3830  CA  CYS A 520     3520   4516   5076    154    306    616       C  
ATOM   3831  C   CYS A 520      23.258  56.537  26.817  1.00 43.92           C  
ANISOU 3831  C   CYS A 520     4694   5685   6308     93    302    667       C  
ATOM   3832  O   CYS A 520      22.393  55.950  27.455  1.00 46.26           O  
ANISOU 3832  O   CYS A 520     4898   6026   6652     76    337    774       O  
ATOM   3833  CB  CYS A 520      22.851  57.572  24.573  1.00 39.48           C  
ANISOU 3833  CB  CYS A 520     4141   5097   5762     97    208    567       C  
ATOM   3834  SG  CYS A 520      22.310  59.041  23.628  1.00 58.25           S  
ANISOU 3834  SG  CYS A 520     6533   7502   8096    169    204    527       S  
ATOM   3835  N   ALA A 521      24.526  56.130  26.779  1.00 48.98           N  
ANISOU 3835  N   ALA A 521     5420   6258   6931     65    265    600       N  
ATOM   3836  CA  ALA A 521      24.948  54.909  27.496  1.00 45.82           C  
ANISOU 3836  CA  ALA A 521     5015   5825   6569     14    253    648       C  
ATOM   3837  C   ALA A 521      24.765  55.061  29.003  1.00 41.76           C  
ANISOU 3837  C   ALA A 521     4501   5374   5992     66    342    726       C  
ATOM   3838  O   ALA A 521      24.459  54.094  29.689  1.00 47.37           O  
ANISOU 3838  O   ALA A 521     5166   6090   6744     28    355    820       O  
ATOM   3839  CB  ALA A 521      26.395  54.552  27.172  1.00 29.50           C  
ANISOU 3839  CB  ALA A 521     3037   3679   4493     -7    200    558       C  
ATOM   3840  N   TYR A 522      24.936  56.282  29.513  1.00 41.19           N  
ANISOU 3840  N   TYR A 522     4491   5347   5814    154    401    690       N  
ATOM   3841  CA  TYR A 522      24.662  56.575  30.919  1.00 34.24           C  
ANISOU 3841  CA  TYR A 522     3626   4534   4849    223    491    755       C  
ATOM   3842  C   TYR A 522      23.181  56.419  31.268  1.00 43.15           C  
ANISOU 3842  C   TYR A 522     4636   5746   6012    240    565    876       C  
ATOM   3843  O   TYR A 522      22.831  55.736  32.230  1.00 45.95           O  
ANISOU 3843  O   TYR A 522     4954   6140   6365    234    619    980       O  
ATOM   3844  CB  TYR A 522      25.111  57.979  31.287  1.00 42.29           C  
ANISOU 3844  CB  TYR A 522     4749   5570   5749    317    526    676       C  
ATOM   3845  CG  TYR A 522      24.718  58.370  32.706  1.00 45.65           C  
ANISOU 3845  CG  TYR A 522     5208   6070   6067    406    622    733       C  
ATOM   3846  CD1 TYR A 522      25.550  58.063  33.785  1.00 43.64           C  
ANISOU 3846  CD1 TYR A 522     5038   5807   5736    417    621    736       C  
ATOM   3847  CD2 TYR A 522      23.527  59.048  32.965  1.00 34.45           C  
ANISOU 3847  CD2 TYR A 522     3739   4731   4618    489    712    783       C  
ATOM   3848  CE1 TYR A 522      25.224  58.422  35.074  1.00 44.96           C  
ANISOU 3848  CE1 TYR A 522     5256   6043   5785    506    707    782       C  
ATOM   3849  CE2 TYR A 522      23.180  59.389  34.256  1.00 47.57           C  
ANISOU 3849  CE2 TYR A 522     5441   6464   6169    583    811    832       C  
ATOM   3850  CZ  TYR A 522      24.033  59.079  35.302  1.00 51.74           C  
ANISOU 3850  CZ  TYR A 522     6069   6981   6607    591    808    828       C  
ATOM   3851  OH  TYR A 522      23.695  59.441  36.576  1.00 49.82           O  
ANISOU 3851  OH  TYR A 522     5884   6811   6233    694    905    871       O  
ATOM   3852  N   LEU A 523      22.309  57.063  30.500  1.00 47.96           N  
ANISOU 3852  N   LEU A 523     5181   6387   6655    263    572    872       N  
ATOM   3853  CA  LEU A 523      20.887  57.027  30.820  1.00 52.45           C  
ANISOU 3853  CA  LEU A 523     5619   7046   7265    290    647    990       C  
ATOM   3854  C   LEU A 523      20.282  55.637  30.623  1.00 52.40           C  
ANISOU 3854  C   LEU A 523     5488   7029   7394    176    608   1097       C  
ATOM   3855  O   LEU A 523      19.207  55.349  31.119  1.00 61.55           O  
ANISOU 3855  O   LEU A 523     6525   8262   8598    178    677   1224       O  
ATOM   3856  CB  LEU A 523      20.130  58.038  29.973  1.00 46.28           C  
ANISOU 3856  CB  LEU A 523     4792   6294   6498    343    647    960       C  
ATOM   3857  CG  LEU A 523      20.567  59.503  29.998  1.00 37.13           C  
ANISOU 3857  CG  LEU A 523     3751   5133   5224    454    675    858       C  
ATOM   3858  CD1 LEU A 523      19.736  60.221  29.021  1.00 32.33           C  
ANISOU 3858  CD1 LEU A 523     3079   4543   4661    486    655    850       C  
ATOM   3859  CD2 LEU A 523      20.445  60.160  31.371  1.00 41.18           C  
ANISOU 3859  CD2 LEU A 523     4321   5711   5615    572    794    883       C  
ATOM   3860  N   TYR A 524      20.974  54.776  29.897  1.00 51.57           N  
ANISOU 3860  N   TYR A 524     5412   6826   7358     77    498   1048       N  
ATOM   3861  CA  TYR A 524      20.472  53.431  29.631  1.00 45.12           C  
ANISOU 3861  CA  TYR A 524     4495   5971   6676    -39    439   1135       C  
ATOM   3862  C   TYR A 524      20.910  52.500  30.745  1.00 56.43           C  
ANISOU 3862  C   TYR A 524     5955   7388   8098    -68    472   1212       C  
ATOM   3863  O   TYR A 524      20.108  51.711  31.251  1.00 73.58           O  
ANISOU 3863  O   TYR A 524     8024   9589  10345   -120    504   1350       O  
ATOM   3864  CB  TYR A 524      20.968  52.920  28.281  1.00 43.90           C  
ANISOU 3864  CB  TYR A 524     4375   5711   6595   -120    301   1039       C  
ATOM   3865  CG  TYR A 524      20.500  51.535  27.931  1.00 54.95           C  
ANISOU 3865  CG  TYR A 524     5695   7048   8137   -242    218   1110       C  
ATOM   3866  CD1 TYR A 524      19.148  51.247  27.820  1.00 50.85           C  
ANISOU 3866  CD1 TYR A 524     5023   6576   7723   -293    215   1224       C  
ATOM   3867  CD2 TYR A 524      21.408  50.509  27.687  1.00 56.11           C  
ANISOU 3867  CD2 TYR A 524     5916   7083   8321   -308    135   1063       C  
ATOM   3868  CE1 TYR A 524      18.716  49.976  27.485  1.00 45.07           C  
ANISOU 3868  CE1 TYR A 524     4221   5773   7132   -418    123   1289       C  
ATOM   3869  CE2 TYR A 524      20.975  49.228  27.356  1.00 50.49           C  
ANISOU 3869  CE2 TYR A 524     5146   6295   7744   -422     47   1122       C  
ATOM   3870  CZ  TYR A 524      19.627  48.974  27.253  1.00 55.36           C  
ANISOU 3870  CZ  TYR A 524     5617   6952   8465   -482     37   1235       C  
ATOM   3871  OH  TYR A 524      19.172  47.711  26.924  1.00 77.53           O  
ANISOU 3871  OH  TYR A 524     8367   9673  11418   -607    -64   1296       O  
ATOM   3872  N   ASP A 525      22.175  52.600  31.144  1.00 44.41           N  
ANISOU 3872  N   ASP A 525     4565   5822   6487    -35    463   1132       N  
ATOM   3873  CA  ASP A 525      22.644  51.852  32.310  1.00 51.36           C  
ANISOU 3873  CA  ASP A 525     5485   6696   7334    -43    496   1206       C  
ATOM   3874  C   ASP A 525      21.849  52.275  33.548  1.00 61.38           C  
ANISOU 3874  C   ASP A 525     6716   8083   8522     32    633   1321       C  
ATOM   3875  O   ASP A 525      21.526  51.453  34.415  1.00 73.25           O  
ANISOU 3875  O   ASP A 525     8181   9609  10042      2    680   1452       O  
ATOM   3876  CB  ASP A 525      24.138  52.070  32.536  1.00 53.12           C  
ANISOU 3876  CB  ASP A 525     5852   6864   7469     -7    457   1096       C  
ATOM   3877  CG  ASP A 525      24.686  51.259  33.688  1.00 71.28           C  
ANISOU 3877  CG  ASP A 525     8199   9149   9735    -14    471   1170       C  
ATOM   3878  OD1 ASP A 525      24.345  50.063  33.809  1.00 85.14           O  
ANISOU 3878  OD1 ASP A 525     9897  10866  11586    -93    448   1271       O  
ATOM   3879  OD2 ASP A 525      25.479  51.822  34.475  1.00 77.46           O1-
ANISOU 3879  OD2 ASP A 525     9082   9953  10395     58    495   1128       O1-
ATOM   3880  N   LEU A 526      21.527  53.563  33.611  1.00 53.38           N  
ANISOU 3880  N   LEU A 526     5719   7144   7419    135    701   1274       N  
ATOM   3881  CA  LEU A 526      20.814  54.117  34.745  1.00 51.68           C  
ANISOU 3881  CA  LEU A 526     5486   7045   7106    234    842   1362       C  
ATOM   3882  C   LEU A 526      19.415  53.535  34.836  1.00 46.36           C  
ANISOU 3882  C   LEU A 526     4635   6442   6538    192    907   1525       C  
ATOM   3883  O   LEU A 526      18.997  53.091  35.898  1.00 46.24           O  
ANISOU 3883  O   LEU A 526     4587   6492   6491    207   1004   1657       O  
ATOM   3884  CB  LEU A 526      20.754  55.638  34.649  1.00 59.87           C  
ANISOU 3884  CB  LEU A 526     6583   8127   8037    356    888   1264       C  
ATOM   3885  CG  LEU A 526      20.178  56.347  35.876  1.00 54.85           C  
ANISOU 3885  CG  LEU A 526     5968   7603   7267    488   1037   1324       C  
ATOM   3886  CD1 LEU A 526      20.855  55.832  37.111  1.00 58.16           C  
ANISOU 3886  CD1 LEU A 526     6488   8028   7583    501   1068   1365       C  
ATOM   3887  CD2 LEU A 526      20.424  57.812  35.751  1.00 53.89           C  
ANISOU 3887  CD2 LEU A 526     5949   7486   7039    604   1051   1197       C  
ATOM   3888  N   ALA A 527      18.688  53.527  33.727  1.00 51.99           N  
ANISOU 3888  N   ALA A 527     5233   7144   7377    138    850   1523       N  
ATOM   3889  CA  ALA A 527      17.350  52.955  33.730  1.00 62.54           C  
ANISOU 3889  CA  ALA A 527     6381   8543   8840     83    893   1681       C  
ATOM   3890  C   ALA A 527      17.391  51.435  33.939  1.00 69.29           C  
ANISOU 3890  C   ALA A 527     7189   9334   9806    -54    843   1791       C  
ATOM   3891  O   ALA A 527      16.436  50.839  34.456  1.00 70.13           O  
ANISOU 3891  O   ALA A 527     7157   9501   9988    -97    912   1960       O  
ATOM   3892  CB  ALA A 527      16.633  53.289  32.452  1.00 63.02           C  
ANISOU 3892  CB  ALA A 527     6337   8598   9011     51    817   1646       C  
ATOM   3893  N   GLY A 528      18.495  50.813  33.538  1.00 63.94           N  
ANISOU 3893  N   GLY A 528     6622   8532   9143   -121    724   1699       N  
ATOM   3894  CA  GLY A 528      18.684  49.398  33.793  1.00 67.58           C  
ANISOU 3894  CA  GLY A 528     7068   8912   9697   -236    671   1790       C  
ATOM   3895  C   GLY A 528      18.838  49.134  35.281  1.00 65.46           C  
ANISOU 3895  C   GLY A 528     6840   8701   9329   -191    787   1905       C  
ATOM   3896  O   GLY A 528      18.337  48.141  35.826  1.00 71.15           O  
ANISOU 3896  O   GLY A 528     7484   9422  10128   -268    815   2066       O  
ATOM   3897  N   LEU A 529      19.529  50.048  35.944  1.00 54.12           N  
ANISOU 3897  N   LEU A 529     5534   7313   7717    -66    851   1826       N  
ATOM   3898  CA  LEU A 529      19.805  49.920  37.359  1.00 56.19           C  
ANISOU 3898  CA  LEU A 529     5869   7631   7849     -5    950   1911       C  
ATOM   3899  C   LEU A 529      18.571  50.229  38.201  1.00 62.68           C  
ANISOU 3899  C   LEU A 529     6584   8601   8631     58   1121   2066       C  
ATOM   3900  O   LEU A 529      18.487  49.810  39.348  1.00 64.38           O  
ANISOU 3900  O   LEU A 529     6819   8869   8772     80   1214   2193       O  
ATOM   3901  CB  LEU A 529      20.966  50.842  37.753  1.00 61.78           C  
ANISOU 3901  CB  LEU A 529     6757   8335   8381    105    943   1763       C  
ATOM   3902  CG  LEU A 529      22.357  50.230  37.907  1.00 62.41           C  
ANISOU 3902  CG  LEU A 529     6968   8308   8438     71    837   1697       C  
ATOM   3903  CD1 LEU A 529      22.708  49.428  36.677  1.00 67.74           C  
ANISOU 3903  CD1 LEU A 529     7606   8855   9278    -46    697   1639       C  
ATOM   3904  CD2 LEU A 529      23.381  51.334  38.123  1.00 59.58           C  
ANISOU 3904  CD2 LEU A 529     6759   7952   7927    173    821   1543       C  
ATOM   3905  N   PHE A 530      17.621  50.972  37.645  1.00 61.54           N  
ANISOU 3905  N   PHE A 530     6326   8528   8530     95   1165   2061       N  
ATOM   3906  CA  PHE A 530      16.406  51.257  38.389  1.00 61.98           C  
ANISOU 3906  CA  PHE A 530     6259   8731   8561    163   1336   2214       C  
ATOM   3907  C   PHE A 530      15.510  50.039  38.358  1.00 62.22           C  
ANISOU 3907  C   PHE A 530     6108   8762   8771     24   1341   2408       C  
ATOM   3908  O   PHE A 530      14.955  49.656  39.385  1.00 74.98           O  
ANISOU 3908  O   PHE A 530     7666  10467  10356     39   1475   2581       O  
ATOM   3909  CB  PHE A 530      15.668  52.468  37.828  1.00 65.15           C  
ANISOU 3909  CB  PHE A 530     6589   9209   8957    259   1383   2152       C  
ATOM   3910  CG  PHE A 530      14.422  52.820  38.588  1.00 70.41           C  
ANISOU 3910  CG  PHE A 530     7121  10036   9597    351   1571   2305       C  
ATOM   3911  CD1 PHE A 530      14.479  53.650  39.699  1.00 76.67           C  
ANISOU 3911  CD1 PHE A 530     8018  10928  10185    521   1723   2300       C  
ATOM   3912  CD2 PHE A 530      13.190  52.328  38.196  1.00 69.95           C  
ANISOU 3912  CD2 PHE A 530     6830  10029   9718    271   1595   2455       C  
ATOM   3913  CE1 PHE A 530      13.320  53.982  40.400  1.00 74.17           C  
ANISOU 3913  CE1 PHE A 530     7577  10768   9836    623   1913   2442       C  
ATOM   3914  CE2 PHE A 530      12.035  52.654  38.896  1.00 69.20           C  
ANISOU 3914  CE2 PHE A 530     6592  10094   9607    362   1781   2607       C  
ATOM   3915  CZ  PHE A 530      12.103  53.482  39.992  1.00 69.45           C  
ANISOU 3915  CZ  PHE A 530     6731  10230   9427    544   1947   2600       C  
ATOM   3916  N   SER A 531      15.370  49.425  37.189  1.00 53.01           N  
ANISOU 3916  N   SER A 531     4859   7495   7790   -113   1192   2382       N  
ATOM   3917  CA  SER A 531      14.536  48.237  37.081  1.00 65.50           C  
ANISOU 3917  CA  SER A 531     6272   9054   9562   -264   1168   2560       C  
ATOM   3918  C   SER A 531      14.999  47.141  38.040  1.00 75.23           C  
ANISOU 3918  C   SER A 531     7566  10240  10777   -325   1189   2680       C  
ATOM   3919  O   SER A 531      14.195  46.579  38.781  1.00 87.60           O  
ANISOU 3919  O   SER A 531     9014  11877  12391   -365   1296   2885       O  
ATOM   3920  CB  SER A 531      14.528  47.724  35.654  1.00 70.46           C  
ANISOU 3920  CB  SER A 531     6850   9552  10369   -399    974   2479       C  
ATOM   3921  OG  SER A 531      14.166  48.774  34.788  1.00 82.61           O  
ANISOU 3921  OG  SER A 531     8349  11134  11906   -334    952   2368       O  
ATOM   3922  N   GLY A 532      16.295  46.862  38.044  1.00 69.96           N  
ANISOU 3922  N   GLY A 532     7082   9460  10041   -328   1092   2561       N  
ATOM   3923  CA  GLY A 532      16.869  45.934  39.004  1.00 67.75           C  
ANISOU 3923  CA  GLY A 532     6887   9134   9719   -361   1106   2660       C  
ATOM   3924  C   GLY A 532      16.681  46.400  40.438  1.00 70.11           C  
ANISOU 3924  C   GLY A 532     7227   9580   9831   -235   1296   2768       C  
ATOM   3925  O   GLY A 532      16.573  45.585  41.344  1.00 84.89           O  
ANISOU 3925  O   GLY A 532     9096  11464  11695   -273   1358   2936       O  
ATOM   3926  N   PHE A 533      16.644  47.713  40.644  1.00 62.91           N  
ANISOU 3926  N   PHE A 533     6363   8775   8764    -81   1387   2671       N  
ATOM   3927  CA  PHE A 533      16.341  48.281  41.954  1.00 63.81           C  
ANISOU 3927  CA  PHE A 533     6519   9040   8688     59   1578   2760       C  
ATOM   3928  C   PHE A 533      14.859  48.142  42.247  1.00 77.66           C  
ANISOU 3928  C   PHE A 533     8060  10924  10523     47   1732   2966       C  
ATOM   3929  O   PHE A 533      14.459  48.103  43.399  1.00 80.62           O  
ANISOU 3929  O   PHE A 533     8433  11415  10785    118   1900   3114       O  
ATOM   3930  CB  PHE A 533      16.765  49.750  42.021  1.00 65.48           C  
ANISOU 3930  CB  PHE A 533     6857   9306   8714    229   1613   2578       C  
ATOM   3931  CG  PHE A 533      16.352  50.466  43.285  1.00 63.19           C  
ANISOU 3931  CG  PHE A 533     6618   9173   8219    393   1811   2648       C  
ATOM   3932  CD1 PHE A 533      16.951  50.160  44.506  1.00 56.80           C  
ANISOU 3932  CD1 PHE A 533     5958   8385   7239    444   1863   2704       C  
ATOM   3933  CD2 PHE A 533      15.390  51.483  43.237  1.00 61.85           C  
ANISOU 3933  CD2 PHE A 533     6358   9127   8016    510   1940   2648       C  
ATOM   3934  CE1 PHE A 533      16.573  50.832  45.664  1.00 58.90           C  
ANISOU 3934  CE1 PHE A 533     6289   8796   7294    607   2046   2759       C  
ATOM   3935  CE2 PHE A 533      15.013  52.165  44.379  1.00 64.92           C  
ANISOU 3935  CE2 PHE A 533     6805   9657   8205    679   2127   2700       C  
ATOM   3936  CZ  PHE A 533      15.602  51.837  45.603  1.00 66.19           C  
ANISOU 3936  CZ  PHE A 533     7124   9841   8185    728   2183   2754       C  
ATOM   3937  N   TYR A 534      14.038  48.059  41.206  1.00 81.02           N  
ANISOU 3937  N   TYR A 534     8302  11335  11146    -41   1677   2982       N  
ATOM   3938  CA  TYR A 534      12.605  47.949  41.429  1.00 79.12           C  
ANISOU 3938  CA  TYR A 534     7832  11223  11006    -57   1817   3183       C  
ATOM   3939  C   TYR A 534      12.229  46.533  41.811  1.00 81.34           C  
ANISOU 3939  C   TYR A 534     8010  11466  11429   -218   1819   3404       C  
ATOM   3940  O   TYR A 534      11.423  46.325  42.721  1.00 89.38           O  
ANISOU 3940  O   TYR A 534     8953  12592  12417   -185   1962   3567       O  
ATOM   3941  CB  TYR A 534      11.810  48.388  40.201  1.00 77.53           C  
ANISOU 3941  CB  TYR A 534     7460  11025  10971    -94   1747   3131       C  
ATOM   3942  CG  TYR A 534      10.343  48.592  40.499  1.00 84.84           C  
ANISOU 3942  CG  TYR A 534     8158  12109  11968    -61   1904   3308       C  
ATOM   3943  CD1 TYR A 534       9.944  49.347  41.595  1.00 90.60           C  
ANISOU 3943  CD1 TYR A 534     8928  12987  12509    123   2099   3343       C  
ATOM   3944  CD2 TYR A 534       9.357  48.054  39.682  1.00 88.39           C  
ANISOU 3944  CD2 TYR A 534     8420  12521  12643   -191   1795   3364       C  
ATOM   3945  CE1 TYR A 534       8.608  49.549  41.884  1.00 95.50           C  
ANISOU 3945  CE1 TYR A 534     9396  13718  13173    177   2194   3440       C  
ATOM   3946  CE2 TYR A 534       8.009  48.260  39.955  1.00 91.71           C  
ANISOU 3946  CE2 TYR A 534     8683  13055  13109   -143   1884   3466       C  
ATOM   3947  CZ  TYR A 534       7.640  49.010  41.062  1.00 92.41           C  
ANISOU 3947  CZ  TYR A 534     8805  13293  13015     43   2089   3507       C  
ATOM   3948  OH  TYR A 534       6.307  49.220  41.367  1.00 82.23           O  
ANISOU 3948  OH  TYR A 534     7357  12117  11771     98   2188   3614       O  
ATOM   3949  N   GLU A 535      12.811  45.558  41.123  1.00 82.05           N  
ANISOU 3949  N   GLU A 535     8136  11379  11660   -376   1627   3363       N  
ATOM   3950  CA  GLU A 535      12.419  44.172  41.348  1.00 93.69           C  
ANISOU 3950  CA  GLU A 535     9512  12788  13299   -546   1599   3567       C  
ATOM   3951  C   GLU A 535      13.057  43.597  42.600  1.00 93.12           C  
ANISOU 3951  C   GLU A 535     9585  12711  13085   -518   1672   3665       C  
ATOM   3952  O   GLU A 535      12.368  43.277  43.572  1.00 96.51           O  
ANISOU 3952  O   GLU A 535     9975  13227  13468   -490   1788   3807       O  
ATOM   3953  CB  GLU A 535      12.774  43.288  40.151  1.00 99.56           C  
ANISOU 3953  CB  GLU A 535    10250  13329  14248   -721   1362   3487       C  
ATOM   3954  CG  GLU A 535      12.686  43.961  38.809  1.00108.18           C  
ANISOU 3954  CG  GLU A 535    11305  14386  15413   -720   1236   3299       C  
ATOM   3955  CD  GLU A 535      13.234  43.086  37.703  1.00120.73           C  
ANISOU 3955  CD  GLU A 535    12945  15769  17159   -867   1002   3194       C  
ATOM   3956  OE1 GLU A 535      14.107  42.237  37.996  1.00123.39           O  
ANISOU 3956  OE1 GLU A 535    13416  15982  17485   -917    932   3190       O  
ATOM   3957  OE2 GLU A 535      12.796  43.247  36.544  1.00125.39           O1-
ANISOU 3957  OE2 GLU A 535    13447  16321  17876   -926    886   3113       O1-
ATOM   3958  N   HIS A 536      14.378  43.469  42.577  1.00 81.87           N  
ANISOU 3958  N   HIS A 536     8369  11168  11568   -498   1557   3519       N  
ATOM   3959  CA  HIS A 536      15.086  42.806  43.660  1.00 82.90           C  
ANISOU 3959  CA  HIS A 536     8645  11270  11583   -487   1588   3610       C  
ATOM   3960  C   HIS A 536      15.118  43.635  44.935  1.00 88.61           C  
ANISOU 3960  C   HIS A 536     9464  12164  12040   -304   1783   3648       C  
ATOM   3961  O   HIS A 536      15.650  43.204  45.952  1.00 97.95           O  
ANISOU 3961  O   HIS A 536    10775  13349  13091   -272   1826   3732       O  
ATOM   3962  CB  HIS A 536      16.503  42.467  43.219  1.00 83.53           C  
ANISOU 3962  CB  HIS A 536     8913  11175  11648   -508   1395   3428       C  
ATOM   3963  CG  HIS A 536      16.558  41.453  42.122  1.00 93.56           C  
ANISOU 3963  CG  HIS A 536    10123  12262  13162   -682   1206   3406       C  
ATOM   3964  CD2 HIS A 536      16.793  40.119  42.153  1.00 94.36           C  
ANISOU 3964  CD2 HIS A 536    10240  12214  13397   -818   1106   3510       C  
ATOM   3965  ND1 HIS A 536      16.345  41.773  40.797  1.00 94.40           N  
ANISOU 3965  ND1 HIS A 536    10156  12314  13396   -729   1092   3261       N  
ATOM   3966  CE1 HIS A 536      16.454  40.683  40.060  1.00 96.86           C  
ANISOU 3966  CE1 HIS A 536    10447  12454  13903   -882    930   3268       C  
ATOM   3967  NE2 HIS A 536      16.730  39.664  40.858  1.00 95.22           N  
ANISOU 3967  NE2 HIS A 536    10292  12181  13708   -939    934   3415       N  
ATOM   3968  N   CYS A 537      14.525  44.817  44.881  1.00 88.74           N  
ANISOU 3968  N   CYS A 537     9422  12321  11973   -178   1900   3588       N  
ATOM   3969  CA  CYS A 537      14.573  45.742  45.998  1.00 90.46           C  
ANISOU 3969  CA  CYS A 537     9753  12695  11925     17   2076   3586       C  
ATOM   3970  C   CYS A 537      13.183  46.387  46.158  1.00 99.90           C  
ANISOU 3970  C   CYS A 537    10771  14057  13129     96   2250   3669       C  
ATOM   3971  O   CYS A 537      12.723  47.134  45.294  1.00107.92           O  
ANISOU 3971  O   CYS A 537    11682  15100  14222    121   2237   3578       O  
ATOM   3972  CB  CYS A 537      15.683  46.769  45.749  1.00 84.71           C  
ANISOU 3972  CB  CYS A 537     9227  11923  11037    138   1982   3314       C  
ATOM   3973  SG  CYS A 537      16.442  47.516  47.180  1.00112.88           S  
ANISOU 3973  SG  CYS A 537    13045  15584  14262    337   2088   3264       S  
ATOM   3974  N   PRO A 538      12.490  46.069  47.258  1.00 96.90           N  
ANISOU 3974  N   PRO A 538    10372  13771  12675    142   2380   3809       N  
ATOM   3975  CA  PRO A 538      11.054  46.369  47.367  1.00 89.57           C  
ANISOU 3975  CA  PRO A 538     9260  12963  11809    187   2494   3884       C  
ATOM   3976  C   PRO A 538      10.700  47.840  47.650  1.00 84.98           C  
ANISOU 3976  C   PRO A 538     8713  12526  11052    405   2636   3781       C  
ATOM   3977  O   PRO A 538      11.222  48.448  48.583  1.00 72.41           O  
ANISOU 3977  O   PRO A 538     7305  11000   9207    562   2734   3731       O  
ATOM   3978  CB  PRO A 538      10.605  45.471  48.523  1.00 86.83           C  
ANISOU 3978  CB  PRO A 538     8905  12658  11427    162   2586   4072       C  
ATOM   3979  CG  PRO A 538      11.825  45.268  49.353  1.00 93.51           C  
ANISOU 3979  CG  PRO A 538     9990  13468  12071    208   2582   4055       C  
ATOM   3980  CD  PRO A 538      13.006  45.330  48.423  1.00 99.11           C  
ANISOU 3980  CD  PRO A 538    10793  14041  12822    145   2415   3915       C  
ATOM   3981  N   ILE A 539       9.800  48.393  46.840  1.00 90.52           N  
ANISOU 3981  N   ILE A 539     9243  13264  11885    414   2633   3747       N  
ATOM   3982  CA  ILE A 539       9.340  49.766  47.018  1.00 98.59           C  
ANISOU 3982  CA  ILE A 539    10281  14409  12771    618   2757   3653       C  
ATOM   3983  C   ILE A 539       8.027  49.792  47.790  1.00111.55           C  
ANISOU 3983  C   ILE A 539    11796  16181  14406    693   2916   3792       C  
ATOM   3984  O   ILE A 539       6.961  49.566  47.211  1.00118.84           O  
ANISOU 3984  O   ILE A 539    12502  17121  15531    619   2896   3872       O  
ATOM   3985  CB  ILE A 539       9.154  50.481  45.670  1.00 89.24           C  
ANISOU 3985  CB  ILE A 539     8996  13190  11722    606   2662   3525       C  
ATOM   3986  N   LEU A 540       8.131  50.078  49.092  1.00111.23           N  
ANISOU 3986  N   LEU A 540    11898  16232  14130    843   3066   3819       N  
ATOM   3987  CA  LEU A 540       7.030  49.997  50.069  1.00103.96           C  
ANISOU 3987  CA  LEU A 540    10893  15442  13167    924   3238   3968       C  
ATOM   3988  C   LEU A 540       6.632  48.542  50.377  1.00 97.74           C  
ANISOU 3988  C   LEU A 540     9986  14624  12525    745   3223   4176       C  
ATOM   3989  O   LEU A 540       5.943  47.915  49.581  1.00102.66           O  
ANISOU 3989  O   LEU A 540    10402  15202  13400    590   3139   4259       O  
ATOM   3990  CB  LEU A 540       5.809  50.781  49.579  1.00 96.18           C  
ANISOU 3990  CB  LEU A 540     9722  14540  12280   1003   3300   3964       C  
ATOM   3991  N   SER A 541       7.019  48.006  51.534  1.00 92.06           N  
ANISOU 3991  N   SER A 541     9400  13928  11651    767   3299   4263       N  
ATOM   3992  CA  SER A 541       7.662  48.740  52.621  1.00 97.73           C  
ANISOU 3992  CA  SER A 541    10362  14716  12057    963   3408   4180       C  
ATOM   3993  C   SER A 541       8.502  47.795  53.467  1.00103.77           C  
ANISOU 3993  C   SER A 541    11284  15431  12714    898   3386   4260       C  
ATOM   3994  O   SER A 541       8.543  46.593  53.204  1.00102.41           O  
ANISOU 3994  O   SER A 541    11026  15168  12716    707   3294   4380       O  
ATOM   3995  CB  SER A 541       6.623  49.423  53.516  1.00 97.70           C  
ANISOU 3995  CB  SER A 541    10320  14874  11926   1147   3616   4236       C  
ATOM   3996  N   ALA A 542       9.144  48.340  54.498  1.00105.53           N  
ANISOU 3996  N   ALA A 542    11744  15708  12646   1061   3464   4191       N  
ATOM   3997  CA  ALA A 542      10.001  47.561  55.392  1.00107.42           C  
ANISOU 3997  CA  ALA A 542    12162  15907  12745   1025   3441   4255       C  
ATOM   3998  C   ALA A 542      10.128  48.266  56.736  1.00113.77           C  
ANISOU 3998  C   ALA A 542    13174  16826  13227   1239   3586   4219       C  
ATOM   3999  O   ALA A 542       9.497  47.867  57.713  1.00120.65           O  
ANISOU 3999  O   ALA A 542    14026  17787  14030   1274   3722   4367       O  
ATOM   4000  CB  ALA A 542      11.380  47.344  54.773  1.00104.90           C  
ANISOU 4000  CB  ALA A 542    11981  15442  12433    937   3251   4142       C  
ATOM   4001  N   GLU A 543      10.955  49.309  56.783  1.00117.63           N  
ANISOU 4001  N   GLU A 543    13869  17307  13517   1380   3551   4019       N  
ATOM   4002  CA  GLU A 543      11.034  50.168  57.961  1.00120.51           C  
ANISOU 4002  CA  GLU A 543    14442  17772  13574   1600   3673   3947       C  
ATOM   4003  C   GLU A 543      10.010  51.276  57.826  1.00136.64           C  
ANISOU 4003  C   GLU A 543    16389  19915  15613   1755   3801   3884       C  
ATOM   4004  O   GLU A 543      10.351  52.460  57.874  1.00134.45           O  
ANISOU 4004  O   GLU A 543    16265  19647  15171   1918   3803   3698       O  
ATOM   4005  CB  GLU A 543      12.430  50.761  58.142  1.00109.21           C  
ANISOU 4005  CB  GLU A 543    13298  16275  11922   1679   3557   3757       C  
ATOM   4006  N   ASN A 544       8.756  50.864  57.645  1.00147.71           N  
ANISOU 4006  N   ASN A 544    17536  21382  17206   1699   3898   4043       N  
ATOM   4007  CA  ASN A 544       7.621  51.769  57.527  1.00149.27           C  
ANISOU 4007  CA  ASN A 544    17604  21681  17432   1835   4027   4025       C  
ATOM   4008  C   ASN A 544       7.892  52.889  56.542  1.00140.61           C  
ANISOU 4008  C   ASN A 544    16531  20533  16363   1902   3941   3818       C  
ATOM   4009  O   ASN A 544       7.978  52.664  55.336  1.00144.69           O  
ANISOU 4009  O   ASN A 544    16909  20966  17100   1760   3813   3795       O  
ATOM   4010  CB  ASN A 544       7.258  52.351  58.897  1.00154.97           C  
ANISOU 4010  CB  ASN A 544    18469  22528  17883   2051   4210   4034       C  
ATOM   4011  N   GLU A 545       8.046  54.096  57.071  1.00125.94           N  
ANISOU 4011  N   GLU A 545    14859  18720  14274   2119   4007   3664       N  
ATOM   4012  CA  GLU A 545       8.365  55.244  56.248  1.00109.93           C  
ANISOU 4012  CA  GLU A 545    12888  16639  12243   2201   3929   3457       C  
ATOM   4013  C   GLU A 545       9.882  55.443  56.122  1.00 97.77           C  
ANISOU 4013  C   GLU A 545    11593  14987  10566   2185   3775   3289       C  
ATOM   4014  O   GLU A 545      10.341  56.042  55.159  1.00 91.59           O  
ANISOU 4014  O   GLU A 545    10825  14127   9847   2172   3665   3142       O  
ATOM   4015  CB  GLU A 545       7.703  56.505  56.813  1.00105.58           C  
ANISOU 4015  CB  GLU A 545    12410  16177  11530   2446   4068   3370       C  
ATOM   4016  N   GLU A 546      10.657  54.935  57.076  1.00 90.20           N  
ANISOU 4016  N   GLU A 546    10826  14020   9425   2182   3762   3314       N  
ATOM   4017  CA  GLU A 546      12.096  55.205  57.102  1.00 85.26           C  
ANISOU 4017  CA  GLU A 546    10456  13299   8641   2190   3617   3152       C  
ATOM   4018  C   GLU A 546      12.774  54.848  55.781  1.00 95.73           C  
ANISOU 4018  C   GLU A 546    11698  14508  10169   2015   3448   3110       C  
ATOM   4019  O   GLU A 546      13.337  55.699  55.090  1.00 95.98           O  
ANISOU 4019  O   GLU A 546    11808  14476  10183   2057   3359   2932       O  
ATOM   4020  CB  GLU A 546      12.764  54.436  58.240  1.00 87.18           C  
ANISOU 4020  CB  GLU A 546    10873  13547   8704   2172   3609   3230       C  
ATOM   4021  N   VAL A 547      12.694  53.571  55.439  1.00 96.38           N  
ANISOU 4021  N   VAL A 547    11619  14556  10446   1818   3404   3277       N  
ATOM   4022  CA  VAL A 547      13.315  53.035  54.242  1.00 78.07           C  
ANISOU 4022  CA  VAL A 547     9213  12120   8329   1636   3244   3263       C  
ATOM   4023  C   VAL A 547      12.492  53.401  53.002  1.00 76.26           C  
ANISOU 4023  C   VAL A 547     8748  11886   8340   1591   3239   3242       C  
ATOM   4024  O   VAL A 547      13.047  53.596  51.913  1.00 80.63           O  
ANISOU 4024  O   VAL A 547     9280  12353   9003   1517   3116   3142       O  
ATOM   4025  CB  VAL A 547      13.489  51.478  54.387  1.00 74.38           C  
ANISOU 4025  CB  VAL A 547     8671  11603   7989   1441   3191   3455       C  
ATOM   4026  CG1 VAL A 547      13.940  50.828  53.100  1.00 63.24           C  
ANISOU 4026  CG1 VAL A 547     7138  10066   6825   1243   3032   3460       C  
ATOM   4027  CG2 VAL A 547      14.485  51.149  55.507  1.00 65.87           C  
ANISOU 4027  CG2 VAL A 547     7846  10511   6670   1483   3162   3459       C  
ATOM   4028  N   ARG A 548      11.173  53.507  53.171  1.00 73.30           N  
ANISOU 4028  N   ARG A 548     8200  11608   8044   1638   3369   3339       N  
ATOM   4029  CA  ARG A 548      10.269  53.815  52.065  1.00 72.40           C  
ANISOU 4029  CA  ARG A 548     7850  11499   8158   1598   3361   3338       C  
ATOM   4030  C   ARG A 548      10.638  55.152  51.473  1.00 75.91           C  
ANISOU 4030  C   ARG A 548     8395  11917   8529   1726   3322   3124       C  
ATOM   4031  O   ARG A 548      10.677  55.322  50.254  1.00 82.33           O  
ANISOU 4031  O   ARG A 548     9098  12668   9517   1645   3222   3062       O  
ATOM   4032  CB  ARG A 548       8.811  53.842  52.524  1.00 79.66           C  
ANISOU 4032  CB  ARG A 548     8597  12540   9132   1664   3518   3473       C  
ATOM   4033  CG  ARG A 548       7.875  54.526  51.532  1.00 89.48           C  
ANISOU 4033  CG  ARG A 548     9645  13804  10548   1688   3519   3436       C  
ATOM   4034  CD  ARG A 548       6.712  55.194  52.260  1.00101.63           C  
ANISOU 4034  CD  ARG A 548    11131  15477  12009   1868   3700   3486       C  
ATOM   4035  NE  ARG A 548       5.591  55.579  51.399  1.00103.85           N  
ANISOU 4035  NE  ARG A 548    11177  15791  12489   1867   3710   3514       N  
ATOM   4036  CZ  ARG A 548       4.787  54.720  50.779  1.00108.21           C  
ANISOU 4036  CZ  ARG A 548    11471  16343  13299   1699   3672   3667       C  
ATOM   4037  NH1 ARG A 548       4.982  53.415  50.901  1.00110.94           N1+
ANISOU 4037  NH1 ARG A 548    11761  16649  13744   1515   3622   3804       N1+
ATOM   4038  NH2 ARG A 548       3.784  55.166  50.036  1.00112.24           N  
ANISOU 4038  NH2 ARG A 548    11787  16889  13971   1714   3675   3681       N  
ATOM   4039  N   ASN A 549      10.923  56.104  52.349  1.00 66.88           N  
ANISOU 4039  N   ASN A 549     7472  10816   7124   1926   3393   3007       N  
ATOM   4040  CA  ASN A 549      11.250  57.438  51.899  1.00 71.38           C  
ANISOU 4040  CA  ASN A 549     8161  11353   7609   2061   3358   2799       C  
ATOM   4041  C   ASN A 549      12.596  57.458  51.179  1.00 69.18           C  
ANISOU 4041  C   ASN A 549     8006  10955   7324   1976   3194   2668       C  
ATOM   4042  O   ASN A 549      12.756  58.147  50.165  1.00 63.16           O  
ANISOU 4042  O   ASN A 549     7216  10139   6644   1980   3123   2544       O  
ATOM   4043  CB  ASN A 549      11.237  58.402  53.074  1.00 65.36           C  
ANISOU 4043  CB  ASN A 549     7620  10647   6565   2290   3461   2704       C  
ATOM   4044  CG  ASN A 549       9.869  58.495  53.726  1.00 68.44           C  
ANISOU 4044  CG  ASN A 549     7881  11161   6960   2393   3636   2828       C  
ATOM   4045  ND2 ASN A 549       9.846  58.825  55.007  1.00 70.57           N  
ANISOU 4045  ND2 ASN A 549     8330  11493   6990   2550   3740   2816       N  
ATOM   4046  OD1 ASN A 549       8.841  58.257  53.082  1.00 73.30           O  
ANISOU 4046  OD1 ASN A 549     8240  11816   7796   2329   3672   2936       O  
ATOM   4047  N   SER A 550      13.549  56.686  51.692  1.00 64.89           N  
ANISOU 4047  N   SER A 550     7595  10372   6690   1898   3134   2704       N  
ATOM   4048  CA  SER A 550      14.873  56.634  51.094  1.00 62.90           C  
ANISOU 4048  CA  SER A 550     7467  10011   6422   1819   2980   2597       C  
ATOM   4049  C   SER A 550      14.738  56.160  49.652  1.00 67.06           C  
ANISOU 4049  C   SER A 550     7777  10442   7261   1627   2843   2598       C  
ATOM   4050  O   SER A 550      15.130  56.879  48.733  1.00 66.47           O  
ANISOU 4050  O   SER A 550     7730  10270   7256   1618   2708   2415       O  
ATOM   4051  CB  SER A 550      15.804  55.724  51.892  1.00 57.73           C  
ANISOU 4051  CB  SER A 550     6963   9315   5656   1746   2910   2656       C  
ATOM   4052  OG  SER A 550      16.903  55.303  51.108  1.00 62.37           O  
ANISOU 4052  OG  SER A 550     7589   9730   6377   1582   2662   2542       O  
ATOM   4053  N   ARG A 551      14.134  54.983  49.463  1.00 70.53           N  
ANISOU 4053  N   ARG A 551     8005  10907   7885   1478   2878   2806       N  
ATOM   4054  CA  ARG A 551      13.895  54.420  48.128  1.00 72.60           C  
ANISOU 4054  CA  ARG A 551     8058  11079   8447   1290   2746   2821       C  
ATOM   4055  C   ARG A 551      13.127  55.370  47.239  1.00 70.10           C  
ANISOU 4055  C   ARG A 551     7610  10793   8232   1356   2770   2744       C  
ATOM   4056  O   ARG A 551      13.393  55.460  46.049  1.00 75.73           O  
ANISOU 4056  O   ARG A 551     8272  11396   9108   1255   2604   2631       O  
ATOM   4057  CB  ARG A 551      13.129  53.098  48.211  1.00 81.47           C  
ANISOU 4057  CB  ARG A 551     8969  12242   9745   1141   2805   3072       C  
ATOM   4058  CG  ARG A 551      13.836  52.079  49.026  1.00 81.66           C  
ANISOU 4058  CG  ARG A 551     9109  12229   9690   1067   2780   3172       C  
ATOM   4059  CD  ARG A 551      13.622  50.690  48.480  1.00 81.24           C  
ANISOU 4059  CD  ARG A 551     8881  12092   9893    841   2687   3322       C  
ATOM   4060  NE  ARG A 551      14.638  49.811  49.046  1.00 65.03           N  
ANISOU 4060  NE  ARG A 551     6984   9955   7771    768   2601   3359       N  
ATOM   4061  CZ  ARG A 551      14.398  48.876  49.950  1.00 63.38           C  
ANISOU 4061  CZ  ARG A 551     6771   9773   7538    725   2663   3536       C  
ATOM   4062  NH1 ARG A 551      13.159  48.662  50.363  1.00 60.74           N1+
ANISOU 4062  NH1 ARG A 551     6286   9527   7264    734   2779   3659       N1+
ATOM   4063  NH2 ARG A 551      15.393  48.137  50.407  1.00 58.12           N  
ANISOU 4063  NH2 ARG A 551     6252   9028   6802    668   2584   3576       N  
ATOM   4064  N   LEU A 552      12.161  56.066  47.824  1.00 73.50           N  
ANISOU 4064  N   LEU A 552     8002  11351   8573   1521   2942   2782       N  
ATOM   4065  CA  LEU A 552      11.411  57.072  47.091  1.00 78.96           C  
ANISOU 4065  CA  LEU A 552     8591  12067   9342   1610   2959   2699       C  
ATOM   4066  C   LEU A 552      12.332  58.193  46.649  1.00 72.64           C  
ANISOU 4066  C   LEU A 552     7981  11192   8429   1704   2877   2471       C  
ATOM   4067  O   LEU A 552      12.288  58.616  45.495  1.00 68.94           O  
ANISOU 4067  O   LEU A 552     7439  10648   8108   1656   2758   2370       O  
ATOM   4068  CB  LEU A 552      10.267  57.607  47.942  1.00 77.61           C  
ANISOU 4068  CB  LEU A 552     8387  12011   9088   1772   3117   2752       C  
ATOM   4069  CG  LEU A 552       9.069  56.671  47.844  1.00 77.88           C  
ANISOU 4069  CG  LEU A 552     8157  12102   9332   1654   3158   2957       C  
ATOM   4070  CD1 LEU A 552       7.871  57.180  48.642  1.00 79.01           C  
ANISOU 4070  CD1 LEU A 552     8243  12368   9408   1814   3325   3026       C  
ATOM   4071  CD2 LEU A 552       8.718  56.479  46.373  1.00 76.44           C  
ANISOU 4071  CD2 LEU A 552     7764  11860   9419   1510   3032   2958       C  
ATOM   4072  N   LYS A 553      13.183  58.645  47.565  1.00 67.73           N  
ANISOU 4072  N   LYS A 553     7623  10551   7559   1814   2881   2364       N  
ATOM   4073  CA  LYS A 553      14.148  59.692  47.265  1.00 76.18           C  
ANISOU 4073  CA  LYS A 553     8913  11504   8529   1878   2741   2118       C  
ATOM   4074  C   LYS A 553      15.113  59.279  46.133  1.00 85.04           C  
ANISOU 4074  C   LYS A 553    10036  12457   9820   1680   2493   2012       C  
ATOM   4075  O   LYS A 553      15.636  60.134  45.415  1.00 79.85           O  
ANISOU 4075  O   LYS A 553     9464  11701   9174   1696   2372   1832       O  
ATOM   4076  CB  LYS A 553      14.931  60.057  48.529  1.00 71.33           C  
ANISOU 4076  CB  LYS A 553     8580  10897   7626   2005   2769   2042       C  
ATOM   4077  CG  LYS A 553      14.135  60.814  49.597  1.00 75.29           C  
ANISOU 4077  CG  LYS A 553     9150  11547   7911   2248   3001   2079       C  
ATOM   4078  CD  LYS A 553      14.604  62.256  49.743  1.00 75.96           C  
ANISOU 4078  CD  LYS A 553     9471  11571   7819   2421   2961   1851       C  
ATOM   4079  CE  LYS A 553      15.525  62.444  50.946  1.00 72.92           C  
ANISOU 4079  CE  LYS A 553     9386  11168   7151   2509   2938   1768       C  
ATOM   4080  NZ  LYS A 553      16.045  63.845  51.050  1.00 70.77           N1+
ANISOU 4080  NZ  LYS A 553     9355  10812   6721   2658   2868   1535       N1+
ATOM   4081  N   LEU A 554      15.338  57.974  45.972  1.00 79.96           N  
ANISOU 4081  N   LEU A 554     9300  11777   9305   1499   2424   2126       N  
ATOM   4082  CA  LEU A 554      16.206  57.471  44.908  1.00 64.25           C  
ANISOU 4082  CA  LEU A 554     7302   9633   7476   1318   2205   2038       C  
ATOM   4083  C   LEU A 554      15.444  57.326  43.617  1.00 62.29           C  
ANISOU 4083  C   LEU A 554     6830   9368   7469   1222   2160   2068       C  
ATOM   4084  O   LEU A 554      16.004  57.501  42.541  1.00 68.97           O  
ANISOU 4084  O   LEU A 554     7689  10099   8417   1140   1999   1939       O  
ATOM   4085  CB  LEU A 554      16.811  56.122  45.273  1.00 63.53           C  
ANISOU 4085  CB  LEU A 554     7224   9495   7421   1175   2139   2137       C  
ATOM   4086  CG  LEU A 554      17.882  56.124  46.350  1.00 55.87           C  
ANISOU 4086  CG  LEU A 554     6492   8501   6235   1231   2110   2083       C  
ATOM   4087  CD1 LEU A 554      18.161  54.710  46.784  1.00 53.91           C  
ANISOU 4087  CD1 LEU A 554     6216   8232   6036   1103   2083   2234       C  
ATOM   4088  CD2 LEU A 554      19.131  56.782  45.845  1.00 45.92           C  
ANISOU 4088  CD2 LEU A 554     5396   7110   4942   1221   1929   1862       C  
ATOM   4089  N   ALA A 555      14.170  56.971  43.713  1.00 60.58           N  
ANISOU 4089  N   ALA A 555     6404   9268   7346   1226   2300   2247       N  
ATOM   4090  CA  ALA A 555      13.334  56.959  42.521  1.00 66.18           C  
ANISOU 4090  CA  ALA A 555     6896   9975   8276   1153   2257   2276       C  
ATOM   4091  C   ALA A 555      13.101  58.405  42.053  1.00 71.41           C  
ANISOU 4091  C   ALA A 555     7599  10647   8886   1303   2270   2132       C  
ATOM   4092  O   ALA A 555      13.067  58.683  40.854  1.00 73.46           O  
ANISOU 4092  O   ALA A 555     7794  10835   9282   1243   2147   2050       O  
ATOM   4093  CB  ALA A 555      12.030  56.252  42.790  1.00 63.11           C  
ANISOU 4093  CB  ALA A 555     6261   9712   8006   1119   2400   2511       C  
ATOM   4094  N   GLN A 556      12.971  59.318  43.018  1.00 69.43           N  
ANISOU 4094  N   GLN A 556     7471  10478   8430   1503   2415   2099       N  
ATOM   4095  CA  GLN A 556      12.825  60.760  42.766  1.00 63.93           C  
ANISOU 4095  CA  GLN A 556     6855   9780   7654   1672   2436   1955       C  
ATOM   4096  C   GLN A 556      13.982  61.325  41.955  1.00 60.09           C  
ANISOU 4096  C   GLN A 556     6535   9132   7165   1620   2236   1744       C  
ATOM   4097  O   GLN A 556      13.771  61.964  40.941  1.00 60.16           O  
ANISOU 4097  O   GLN A 556     6493   9095   7270   1624   2165   1667       O  
ATOM   4098  CB  GLN A 556      12.722  61.505  44.095  1.00 67.40           C  
ANISOU 4098  CB  GLN A 556     7454  10312   7844   1890   2610   1940       C  
ATOM   4099  CG  GLN A 556      12.421  62.992  44.029  1.00 66.32           C  
ANISOU 4099  CG  GLN A 556     7405  10183   7610   2093   2663   1810       C  
ATOM   4100  CD  GLN A 556      12.080  63.554  45.421  1.00 78.70           C  
ANISOU 4100  CD  GLN A 556     9102  11867   8935   2319   2868   1830       C  
ATOM   4101  NE2 GLN A 556      11.028  64.358  45.485  1.00 80.61           N  
ANISOU 4101  NE2 GLN A 556     9277  12171   9181   2469   2967   1838       N  
ATOM   4102  OE1 GLN A 556      12.733  63.236  46.426  1.00 75.55           O  
ANISOU 4102  OE1 GLN A 556     8873  11472   8360   2334   2890   1828       O  
ATOM   4103  N   LEU A 557      15.206  61.082  42.413  1.00 62.73           N  
ANISOU 4103  N   LEU A 557     7063   9382   7389   1572   2147   1661       N  
ATOM   4104  CA  LEU A 557      16.396  61.609  41.756  1.00 61.18           C  
ANISOU 4104  CA  LEU A 557     7025   9038   7181   1524   1967   1471       C  
ATOM   4105  C   LEU A 557      16.634  60.923  40.404  1.00 64.56           C  
ANISOU 4105  C   LEU A 557     7330   9376   7826   1333   1809   1465       C  
ATOM   4106  O   LEU A 557      17.157  61.535  39.464  1.00 60.72           O  
ANISOU 4106  O   LEU A 557     6896   8791   7384   1306   1687   1330       O  
ATOM   4107  CB  LEU A 557      17.622  61.461  42.669  1.00 52.51           C  
ANISOU 4107  CB  LEU A 557     6148   7887   5917   1522   1912   1401       C  
ATOM   4108  CG  LEU A 557      18.974  61.916  42.090  1.00 54.44           C  
ANISOU 4108  CG  LEU A 557     6549   7980   6155   1457   1724   1218       C  
ATOM   4109  CD1 LEU A 557      18.902  63.362  41.678  1.00 51.51           C  
ANISOU 4109  CD1 LEU A 557     6263   7570   5738   1574   1714   1079       C  
ATOM   4110  CD2 LEU A 557      20.124  61.716  43.079  1.00 53.41           C  
ANISOU 4110  CD2 LEU A 557     6616   7810   5867   1457   1668   1166       C  
ATOM   4111  N   THR A 558      16.231  59.660  40.306  1.00 63.82           N  
ANISOU 4111  N   THR A 558     7075   9310   7862   1204   1813   1613       N  
ATOM   4112  CA  THR A 558      16.331  58.911  39.051  1.00 56.65           C  
ANISOU 4112  CA  THR A 558     6048   8320   7158   1028   1669   1616       C  
ATOM   4113  C   THR A 558      15.393  59.538  38.029  1.00 57.01           C  
ANISOU 4113  C   THR A 558     5952   8390   7321   1055   1666   1609       C  
ATOM   4114  O   THR A 558      15.759  59.749  36.887  1.00 68.15           O  
ANISOU 4114  O   THR A 558     7369   9710   8816    988   1532   1509       O  
ATOM   4115  CB  THR A 558      15.980  57.402  39.241  1.00 61.33           C  
ANISOU 4115  CB  THR A 558     6499   8934   7871    888   1677   1788       C  
ATOM   4116  CG2 THR A 558      15.944  56.671  37.910  1.00 57.68           C  
ANISOU 4116  CG2 THR A 558     5915   8383   7618    719   1527   1785       C  
ATOM   4117  OG1 THR A 558      16.936  56.772  40.103  1.00 51.49           O  
ANISOU 4117  OG1 THR A 558     5391   7650   6524    856   1658   1793       O  
ATOM   4118  N   ALA A 559      14.175  59.831  38.457  1.00 66.20           N  
ANISOU 4118  N   ALA A 559     6986   9681   8486   1161   1819   1722       N  
ATOM   4119  CA  ALA A 559      13.213  60.518  37.611  1.00 68.68           C  
ANISOU 4119  CA  ALA A 559     7162  10032   8900   1214   1827   1724       C  
ATOM   4120  C   ALA A 559      13.786  61.850  37.113  1.00 60.53           C  
ANISOU 4120  C   ALA A 559     6293   8923   7783   1312   1762   1538       C  
ATOM   4121  O   ALA A 559      13.721  62.167  35.933  1.00 67.19           O  
ANISOU 4121  O   ALA A 559     7092   9706   8730   1267   1652   1478       O  
ATOM   4122  CB  ALA A 559      11.906  60.745  38.373  1.00 60.09           C  
ANISOU 4122  CB  ALA A 559     5928   9107   7796   1349   2029   1872       C  
ATOM   4123  N   LYS A 560      14.368  62.603  38.035  1.00 54.54           N  
ANISOU 4123  N   LYS A 560     5732   8159   6831   1443   1824   1451       N  
ATOM   4124  CA  LYS A 560      14.864  63.944  37.765  1.00 47.72           C  
ANISOU 4124  CA  LYS A 560     5037   7221   5874   1551   1780   1285       C  
ATOM   4125  C   LYS A 560      16.100  63.819  36.872  1.00 49.46           C  
ANISOU 4125  C   LYS A 560     5360   7294   6137   1409   1590   1160       C  
ATOM   4126  O   LYS A 560      16.346  64.658  36.013  1.00 52.13           O  
ANISOU 4126  O   LYS A 560     5752   7557   6498   1424   1507   1054       O  
ATOM   4127  CB  LYS A 560      15.190  64.692  39.080  1.00 50.64           C  
ANISOU 4127  CB  LYS A 560     5605   7616   6019   1719   1885   1226       C  
ATOM   4128  CG  LYS A 560      13.983  64.991  40.064  1.00 51.77           C  
ANISOU 4128  CG  LYS A 560     5676   7914   6080   1904   2103   1336       C  
ATOM   4129  CD  LYS A 560      12.646  65.272  39.338  1.00 71.56           C  
ANISOU 4129  CD  LYS A 560     7956  10499   8733   1957   2165   1423       C  
ATOM   4130  CE  LYS A 560      11.406  65.193  40.269  1.00 81.77           C  
ANISOU 4130  CE  LYS A 560     9112  11967   9989   2102   2390   1581       C  
ATOM   4131  NZ  LYS A 560      10.141  64.879  39.517  1.00 73.97           N1+
ANISOU 4131  NZ  LYS A 560     7829  11067   9208   2070   2424   1723       N1+
ATOM   4132  N   THR A 561      16.859  62.744  37.038  1.00 57.50           N  
ANISOU 4132  N   THR A 561     6398   8274   7177   1272   1524   1182       N  
ATOM   4133  CA  THR A 561      18.093  62.596  36.274  1.00 51.04           C  
ANISOU 4133  CA  THR A 561     5676   7324   6392   1150   1360   1066       C  
ATOM   4134  C   THR A 561      17.827  62.169  34.836  1.00 50.08           C  
ANISOU 4134  C   THR A 561     5419   7160   6449   1028   1255   1076       C  
ATOM   4135  O   THR A 561      18.400  62.734  33.900  1.00 53.63           O  
ANISOU 4135  O   THR A 561     5935   7524   6920   1001   1152    966       O  
ATOM   4136  CB  THR A 561      19.056  61.600  36.947  1.00 48.36           C  
ANISOU 4136  CB  THR A 561     5410   6952   6013   1059   1320   1081       C  
ATOM   4137  CG2 THR A 561      20.282  61.369  36.083  1.00 42.80           C  
ANISOU 4137  CG2 THR A 561     4775   6122   5364    936   1159    974       C  
ATOM   4138  OG1 THR A 561      19.474  62.128  38.215  1.00 44.53           O  
ANISOU 4138  OG1 THR A 561     5088   6491   5341   1175   1388   1044       O  
ATOM   4139  N   LEU A 562      16.960  61.182  34.645  1.00 51.72           N  
ANISOU 4139  N   LEU A 562     5442   7427   6783    952   1276   1211       N  
ATOM   4140  CA  LEU A 562      16.535  60.814  33.295  1.00 42.45           C  
ANISOU 4140  CA  LEU A 562     4137   6220   5773    847   1172   1223       C  
ATOM   4141  C   LEU A 562      15.961  62.022  32.554  1.00 53.74           C  
ANISOU 4141  C   LEU A 562     5549   7659   7211    944   1169   1170       C  
ATOM   4142  O   LEU A 562      16.418  62.376  31.466  1.00 48.78           O  
ANISOU 4142  O   LEU A 562     4969   6948   6617    900   1055   1076       O  
ATOM   4143  CB  LEU A 562      15.497  59.714  33.348  1.00 42.43           C  
ANISOU 4143  CB  LEU A 562     3928   6290   5904    767   1206   1389       C  
ATOM   4144  CG  LEU A 562      16.031  58.402  33.906  1.00 46.76           C  
ANISOU 4144  CG  LEU A 562     4485   6809   6472    651   1188   1452       C  
ATOM   4145  CD1 LEU A 562      15.077  57.269  33.539  1.00 42.28           C  
ANISOU 4145  CD1 LEU A 562     3712   6271   6082    529   1166   1599       C  
ATOM   4146  CD2 LEU A 562      17.433  58.145  33.390  1.00 48.23           C  
ANISOU 4146  CD2 LEU A 562     4820   6866   6640    567   1052   1321       C  
ATOM   4147  N   LYS A 563      14.950  62.644  33.149  1.00 54.78           N  
ANISOU 4147  N   LYS A 563     5612   7893   7309   1083   1300   1237       N  
ATOM   4148  CA  LYS A 563      14.393  63.857  32.582  1.00 54.00           C  
ANISOU 4148  CA  LYS A 563     5507   7802   7208   1201   1307   1191       C  
ATOM   4149  C   LYS A 563      15.493  64.790  32.092  1.00 55.81           C  
ANISOU 4149  C   LYS A 563     5939   7912   7355   1219   1217   1025       C  
ATOM   4150  O   LYS A 563      15.589  65.068  30.898  1.00 60.56           O  
ANISOU 4150  O   LYS A 563     6533   8451   8025   1169   1108    974       O  
ATOM   4151  CB  LYS A 563      13.526  64.588  33.594  1.00 46.20           C  
ANISOU 4151  CB  LYS A 563     4494   6923   6136   1389   1480   1247       C  
ATOM   4152  CG  LYS A 563      12.787  65.734  32.946  1.00 62.44           C  
ANISOU 4152  CG  LYS A 563     6513   8992   8220   1513   1485   1220       C  
ATOM   4153  CD  LYS A 563      11.751  65.219  31.952  1.00 72.36           C  
ANISOU 4153  CD  LYS A 563     7533  10296   9663   1436   1429   1325       C  
ATOM   4154  CE  LYS A 563      11.641  66.105  30.718  1.00 74.24           C  
ANISOU 4154  CE  LYS A 563     7789  10472   9949   1463   1320   1248       C  
ATOM   4155  NZ  LYS A 563      12.533  65.584  29.609  1.00 75.44           N1+
ANISOU 4155  NZ  LYS A 563     8002  10508  10152   1288   1142   1173       N1+
ATOM   4156  N   LEU A 564      16.351  65.226  33.010  1.00 48.85           N  
ANISOU 4156  N   LEU A 564     5238   6997   6328   1280   1254    948       N  
ATOM   4157  CA  LEU A 564      17.392  66.191  32.685  1.00 50.10           C  
ANISOU 4157  CA  LEU A 564     5587   7041   6408   1300   1176    800       C  
ATOM   4158  C   LEU A 564      18.328  65.700  31.607  1.00 60.40           C  
ANISOU 4158  C   LEU A 564     6913   8248   7786   1140   1029    741       C  
ATOM   4159  O   LEU A 564      18.605  66.422  30.644  1.00 64.47           O  
ANISOU 4159  O   LEU A 564     7481   8693   8322   1135    953    667       O  
ATOM   4160  CB  LEU A 564      18.203  66.553  33.927  1.00 54.02           C  
ANISOU 4160  CB  LEU A 564     6265   7516   6743   1369   1222    735       C  
ATOM   4161  CG  LEU A 564      17.709  67.833  34.610  1.00 62.28           C  
ANISOU 4161  CG  LEU A 564     7405   8585   7672   1566   1321    695       C  
ATOM   4162  CD1 LEU A 564      18.697  68.350  35.665  1.00 56.92           C  
ANISOU 4162  CD1 LEU A 564     6949   7852   6827   1623   1322    595       C  
ATOM   4163  CD2 LEU A 564      17.407  68.901  33.553  1.00 63.39           C  
ANISOU 4163  CD2 LEU A 564     7553   8669   7865   1617   1269    639       C  
ATOM   4164  N   GLY A 565      18.816  64.476  31.781  1.00 59.92           N  
ANISOU 4164  N   GLY A 565     6820   8183   7763   1017    996    778       N  
ATOM   4165  CA  GLY A 565      19.739  63.869  30.839  1.00 48.37           C  
ANISOU 4165  CA  GLY A 565     5379   6634   6367    874    869    724       C  
ATOM   4166  C   GLY A 565      19.187  63.805  29.430  1.00 40.84           C  
ANISOU 4166  C   GLY A 565     4324   5666   5528    818    793    735       C  
ATOM   4167  O   GLY A 565      19.924  63.960  28.468  1.00 40.17           O  
ANISOU 4167  O   GLY A 565     4302   5501   5460    756    698    656       O  
ATOM   4168  N   LEU A 566      17.882  63.593  29.309  1.00 47.95           N  
ANISOU 4168  N   LEU A 566     5065   6649   6506    844    833    836       N  
ATOM   4169  CA  LEU A 566      17.255  63.476  28.006  1.00 46.49           C  
ANISOU 4169  CA  LEU A 566     4775   6457   6432    790    747    855       C  
ATOM   4170  C   LEU A 566      17.027  64.845  27.409  1.00 66.66           C  
ANISOU 4170  C   LEU A 566     7384   8992   8950    893    738    797       C  
ATOM   4171  O   LEU A 566      16.983  64.998  26.189  1.00 71.14           O  
ANISOU 4171  O   LEU A 566     7942   9520   9569    850    641    768       O  
ATOM   4172  CB  LEU A 566      15.930  62.723  28.112  1.00 48.95           C  
ANISOU 4172  CB  LEU A 566     4880   6863   6854    769    781    994       C  
ATOM   4173  CG  LEU A 566      15.964  61.208  28.318  1.00 46.85           C  
ANISOU 4173  CG  LEU A 566     4529   6599   6672    632    752   1069       C  
ATOM   4174  CD1 LEU A 566      14.581  60.639  28.162  1.00 52.22           C  
ANISOU 4174  CD1 LEU A 566     4994   7363   7486    601    762   1206       C  
ATOM   4175  CD2 LEU A 566      16.851  60.594  27.280  1.00 43.67           C  
ANISOU 4175  CD2 LEU A 566     4193   6092   6308    504    612    988       C  
ATOM   4176  N   ASP A 567      16.859  65.841  28.276  1.00 70.93           N  
ANISOU 4176  N   ASP A 567     7991   9560   9398   1037    838    783       N  
ATOM   4177  CA  ASP A 567      16.693  67.209  27.813  1.00 62.59           C  
ANISOU 4177  CA  ASP A 567     7009   8470   8303   1147    832    725       C  
ATOM   4178  C   ASP A 567      18.010  67.821  27.350  1.00 59.58           C  
ANISOU 4178  C   ASP A 567     6813   7968   7857   1109    755    603       C  
ATOM   4179  O   ASP A 567      18.006  68.871  26.717  1.00 58.61           O  
ANISOU 4179  O   ASP A 567     6758   7793   7716   1168    723    556       O  
ATOM   4180  CB  ASP A 567      16.086  68.082  28.895  1.00 68.51           C  
ANISOU 4180  CB  ASP A 567     7783   9275   8972   1324    962    742       C  
ATOM   4181  CG  ASP A 567      14.596  67.942  28.968  1.00 93.10           C  
ANISOU 4181  CG  ASP A 567    10700  12507  12166   1398   1034    863       C  
ATOM   4182  OD1 ASP A 567      14.021  67.303  28.053  1.00 99.50           O  
ANISOU 4182  OD1 ASP A 567    11360  13343  13102   1308    960    927       O  
ATOM   4183  OD2 ASP A 567      14.001  68.479  29.933  1.00101.62           O1-
ANISOU 4183  OD2 ASP A 567    11775  13654  13184   1549   1163    894       O1-
ATOM   4184  N   THR A 568      19.138  67.186  27.662  1.00 49.87           N  
ANISOU 4184  N   THR A 568     5659   6692   6597   1013    726    558       N  
ATOM   4185  CA  THR A 568      20.385  67.656  27.075  1.00 48.85           C  
ANISOU 4185  CA  THR A 568     5673   6456   6432    958    648    458       C  
ATOM   4186  C   THR A 568      20.587  67.013  25.692  1.00 45.81           C  
ANISOU 4186  C   THR A 568     5235   6041   6129    837    548    456       C  
ATOM   4187  O   THR A 568      21.329  67.534  24.879  1.00 58.36           O  
ANISOU 4187  O   THR A 568     6914   7556   7703    804    488    392       O  
ATOM   4188  CB  THR A 568      21.621  67.361  27.974  1.00 59.10           C  
ANISOU 4188  CB  THR A 568     7080   7713   7661    914    652    404       C  
ATOM   4189  CG2 THR A 568      21.318  67.643  29.419  1.00 54.67           C  
ANISOU 4189  CG2 THR A 568     6559   7202   7014   1023    749    419       C  
ATOM   4190  OG1 THR A 568      22.010  65.987  27.846  1.00 71.10           O  
ANISOU 4190  OG1 THR A 568     8531   9244   9240    792    615    434       O  
ATOM   4191  N   LEU A 569      19.947  65.872  25.443  1.00 43.13           N  
ANISOU 4191  N   LEU A 569     4756   5756   5875    769    529    528       N  
ATOM   4192  CA  LEU A 569      20.112  65.159  24.177  1.00 43.84           C  
ANISOU 4192  CA  LEU A 569     4808   5815   6033    658    428    519       C  
ATOM   4193  C   LEU A 569      19.045  65.654  23.224  1.00 41.48           C  
ANISOU 4193  C   LEU A 569     4436   5543   5781    698    388    555       C  
ATOM   4194  O   LEU A 569      19.078  65.384  22.047  1.00 47.33           O  
ANISOU 4194  O   LEU A 569     5169   6255   6558    633    296    540       O  
ATOM   4195  CB  LEU A 569      19.996  63.650  24.348  1.00 38.20           C  
ANISOU 4195  CB  LEU A 569     3996   5125   5392    556    406    572       C  
ATOM   4196  CG  LEU A 569      21.056  62.941  25.168  1.00 41.40           C  
ANISOU 4196  CG  LEU A 569     4463   5500   5767    504    426    546       C  
ATOM   4197  CD1 LEU A 569      20.541  61.577  25.499  1.00 38.65           C  
ANISOU 4197  CD1 LEU A 569     3997   5188   5500    431    421    629       C  
ATOM   4198  CD2 LEU A 569      22.347  62.833  24.376  1.00 43.00           C  
ANISOU 4198  CD2 LEU A 569     4769   5619   5953    433    355    455       C  
ATOM   4199  N   GLY A 570      18.100  66.400  23.757  1.00 44.41           N  
ANISOU 4199  N   GLY A 570     4757   5970   6146    817    456    603       N  
ATOM   4200  CA  GLY A 570      17.065  66.993  22.934  1.00 44.33           C  
ANISOU 4200  CA  GLY A 570     4674   5988   6180    875    419    641       C  
ATOM   4201  C   GLY A 570      15.884  66.088  22.751  1.00 41.88           C  
ANISOU 4201  C   GLY A 570     4171   5760   5983    836    394    742       C  
ATOM   4202  O   GLY A 570      15.133  66.261  21.816  1.00 49.11           O  
ANISOU 4202  O   GLY A 570     5013   6692   6955    841    320    773       O  
ATOM   4203  N   ILE A 571      15.712  65.132  23.657  1.00 58.11           N  
ANISOU 4203  N   ILE A 571     6141   7866   8073    794    450    801       N  
ATOM   4204  CA  ILE A 571      14.666  64.121  23.530  1.00 60.31           C  
ANISOU 4204  CA  ILE A 571     6227   8212   8475    728    420    907       C  
ATOM   4205  C   ILE A 571      13.512  64.392  24.527  1.00 60.09           C  
ANISOU 4205  C   ILE A 571     6058   8296   8477    838    544   1015       C  
ATOM   4206  O   ILE A 571      13.723  64.462  25.743  1.00 55.69           O  
ANISOU 4206  O   ILE A 571     5535   7771   7854    898    666   1028       O  
ATOM   4207  CB  ILE A 571      15.253  62.675  23.734  1.00 46.76           C  
ANISOU 4207  CB  ILE A 571     4502   6465   6798    582    384    913       C  
ATOM   4208  CG1 ILE A 571      15.966  62.179  22.470  1.00 42.62           C  
ANISOU 4208  CG1 ILE A 571     4055   5852   6288    470    244    834       C  
ATOM   4209  CG2 ILE A 571      14.133  61.669  24.049  1.00 37.86           C  
ANISOU 4209  CG2 ILE A 571     3172   5414   5799    524    390   1046       C  
ATOM   4210  CD1 ILE A 571      17.263  62.811  22.159  1.00 48.15           C  
ANISOU 4210  CD1 ILE A 571     4942   6471   6880    484    236    716       C  
ATOM   4211  N   GLU A 572      12.298  64.566  24.002  1.00 63.24           N  
ANISOU 4211  N   GLU A 572     6298   8759   8970    872    513   1094       N  
ATOM   4212  CA  GLU A 572      11.143  64.899  24.838  1.00 62.13           C  
ANISOU 4212  CA  GLU A 572     6006   8735   8866    993    637   1204       C  
ATOM   4213  C   GLU A 572      10.708  63.739  25.715  1.00 60.18           C  
ANISOU 4213  C   GLU A 572     5614   8562   8691    921    707   1318       C  
ATOM   4214  O   GLU A 572      11.120  62.599  25.509  1.00 64.57           O  
ANISOU 4214  O   GLU A 572     6163   9075   9298    766    631   1323       O  
ATOM   4215  CB  GLU A 572       9.944  65.325  23.989  1.00 69.75           C  
ANISOU 4215  CB  GLU A 572     6816   9753   9933   1041    573   1269       C  
ATOM   4216  CG  GLU A 572      10.065  66.641  23.287  1.00 84.17           C  
ANISOU 4216  CG  GLU A 572     8757  11529  11695   1153    533   1192       C  
ATOM   4217  CD  GLU A 572       8.820  66.961  22.469  1.00100.12           C  
ANISOU 4217  CD  GLU A 572    10608  13609  13826   1200    459   1271       C  
ATOM   4218  OE1 GLU A 572       8.439  66.124  21.616  1.00 98.71           O  
ANISOU 4218  OE1 GLU A 572    10319  13433  13753   1069    321   1312       O  
ATOM   4219  OE2 GLU A 572       8.236  68.054  22.668  1.00106.63           O1-
ANISOU 4219  OE2 GLU A 572    11414  14471  14631   1370    528   1289       O1-
ATOM   4220  N   THR A 573       9.847  64.030  26.682  1.00 62.63           N  
ANISOU 4220  N   THR A 573     5809   8983   9007   1040    856   1416       N  
ATOM   4221  CA  THR A 573       9.225  62.976  27.471  1.00 66.75           C  
ANISOU 4221  CA  THR A 573     6159   9591   9611    977    933   1557       C  
ATOM   4222  C   THR A 573       7.726  63.135  27.532  1.00 68.86           C  
ANISOU 4222  C   THR A 573     6177   9987   9998   1050    994   1702       C  
ATOM   4223  O   THR A 573       7.193  64.236  27.479  1.00 71.57           O  
ANISOU 4223  O   THR A 573     6503  10374  10315   1212   1047   1695       O  
ATOM   4224  CB  THR A 573       9.740  62.935  28.927  1.00 64.95           C  
ANISOU 4224  CB  THR A 573     6028   9393   9256   1043   1098   1562       C  
ATOM   4225  CG2 THR A 573      11.235  62.641  28.987  1.00 50.29           C  
ANISOU 4225  CG2 THR A 573     4393   7418   7297    961   1038   1436       C  
ATOM   4226  OG1 THR A 573       9.444  64.184  29.565  1.00 70.02           O  
ANISOU 4226  OG1 THR A 573     6721  10090   9792   1252   1233   1541       O  
ATOM   4227  N   VAL A 574       7.057  62.002  27.658  1.00 74.50           N  
ANISOU 4227  N   VAL A 574     6695  10758  10854    927    983   1839       N  
ATOM   4228  CA  VAL A 574       5.658  61.964  28.024  1.00 75.83           C  
ANISOU 4228  CA  VAL A 574     6598  11069  11144    985   1078   2009       C  
ATOM   4229  C   VAL A 574       5.481  61.549  29.491  1.00 72.55           C  
ANISOU 4229  C   VAL A 574     6130  10750  10685   1028   1283   2121       C  
ATOM   4230  O   VAL A 574       6.421  61.561  30.289  1.00 68.73           O  
ANISOU 4230  O   VAL A 574     5838  10226  10049   1056   1362   2051       O  
ATOM   4231  CB  VAL A 574       4.912  60.985  27.135  1.00 75.69           C  
ANISOU 4231  CB  VAL A 574     6371  11054  11335    808    918   2107       C  
ATOM   4232  CG1 VAL A 574       4.833  61.538  25.719  1.00 74.61           C  
ANISOU 4232  CG1 VAL A 574     6262  10853  11233    802    731   2018       C  
ATOM   4233  CG2 VAL A 574       5.606  59.614  27.174  1.00 65.50           C  
ANISOU 4233  CG2 VAL A 574     5133   9676  10079    602    836   2107       C  
ATOM   4234  N   GLU A 575       4.264  61.168  29.840  1.00 75.34           N  
ANISOU 4234  N   GLU A 575     6218  11234  11176   1031   1367   2304       N  
ATOM   4235  CA  GLU A 575       4.020  60.598  31.144  1.00 71.30           C  
ANISOU 4235  CA  GLU A 575     5689  10788  10615   1030   1530   2408       C  
ATOM   4236  C   GLU A 575       3.121  59.389  30.988  1.00 69.56           C  
ANISOU 4236  C   GLU A 575     5275  10581  10575    843   1455   2555       C  
ATOM   4237  O   GLU A 575       2.973  58.590  31.904  1.00 73.93           O  
ANISOU 4237  O   GLU A 575     5801  11165  11123    784   1547   2659       O  
ATOM   4238  CB  GLU A 575       3.428  61.643  32.080  1.00 79.65           C  
ANISOU 4238  CB  GLU A 575     6781  11941  11542   1255   1723   2417       C  
ATOM   4239  CG  GLU A 575       4.444  62.719  32.452  1.00 87.14           C  
ANISOU 4239  CG  GLU A 575     7962  12858  12291   1431   1804   2267       C  
ATOM   4240  CD  GLU A 575       3.978  63.616  33.581  1.00100.16           C  
ANISOU 4240  CD  GLU A 575     9683  14586  13786   1646   2000   2269       C  
ATOM   4241  OE1 GLU A 575       2.786  63.548  33.954  1.00101.73           O  
ANISOU 4241  OE1 GLU A 575     9734  14876  14044   1678   2074   2385       O  
ATOM   4242  OE2 GLU A 575       4.817  64.381  34.104  1.00102.72           O1-
ANISOU 4242  OE2 GLU A 575    10220  14879  13931   1784   2075   2150       O1-
ATOM   4243  N   ARG A 576       2.553  59.243  29.798  1.00 72.90           N  
ANISOU 4243  N   ARG A 576     5573  10972  11154    748   1276   2561       N  
ATOM   4244  CA  ARG A 576       1.855  58.019  29.424  1.00 82.63           C  
ANISOU 4244  CA  ARG A 576     6644  12181  12569    542   1153   2674       C  
ATOM   4245  C   ARG A 576       2.778  57.092  28.621  1.00 76.34           C  
ANISOU 4245  C   ARG A 576     5912  11254  11841    348    962   2611       C  
ATOM   4246  O   ARG A 576       2.565  56.844  27.431  1.00 69.36           O  
ANISOU 4246  O   ARG A 576     4970  10308  11077    239    760   2580       O  
ATOM   4247  CB  ARG A 576       0.593  58.345  28.622  1.00 90.25           C  
ANISOU 4247  CB  ARG A 576     7432  13189  13668    546   1057   2723       C  
TER   
HETATM 4248  N   ARG A 601      27.597  73.840   4.290  1.00 56.28           N  
ANISOU 4248  N   ARG A 601     7933   6810   6640    444    -14    447       N  
HETATM 4249  CA  ARG A 601      28.785  73.025   4.039  1.00 53.55           C  
ANISOU 4249  CA  ARG A 601     7594   6491   6263    383     66    404       C  
HETATM 4250  C   ARG A 601      28.391  71.715   3.344  1.00 50.63           C  
ANISOU 4250  C   ARG A 601     7218   6186   5831    390      5    345       C  
HETATM 4251  O   ARG A 601      29.238  70.850   3.082  1.00 47.98           O  
ANISOU 4251  O   ARG A 601     6888   5877   5463    357     61    296       O  
HETATM 4252  CB  ARG A 601      29.535  72.743   5.352  1.00 42.63           C  
ANISOU 4252  CB  ARG A 601     6119   5087   4990    336    133    360       C  
HETATM 4253  CG  ARG A 601      30.079  73.987   6.083  1.00 40.22           C  
ANISOU 4253  CG  ARG A 601     5830   4705   4747    318    186    405       C  
HETATM 4254  CD  ARG A 601      30.647  73.552   7.406  1.00 45.42           C  
ANISOU 4254  CD  ARG A 601     6399   5353   5506    278    223    351       C  
HETATM 4255  NE  ARG A 601      31.223  74.570   8.295  1.00 40.74           N  
ANISOU 4255  NE  ARG A 601     5815   4683   4981    253    258    373       N  
HETATM 4256  CZ  ARG A 601      32.442  75.089   8.140  1.00 43.63           C  
ANISOU 4256  CZ  ARG A 601     6212   5009   5355    189    326    406       C  
HETATM 4257  NH1 ARG A 601      33.187  74.762   7.074  1.00 31.31           N  
ANISOU 4257  NH1 ARG A 601     4679   3488   3730    155    385    431       N  
HETATM 4258  NH2 ARG A 601      32.910  75.962   9.024  1.00 30.80           N  
ANISOU 4258  NH2 ARG A 601     4596   3306   3802    159    336    417       N  
HETATM 4259  OXT ARG A 601      27.206  71.498   3.017  1.00 39.21           O  
ANISOU 4259  OXT ARG A 601     5765   4765   4370    430   -109    344       O  
CONECT 4248 4249
CONECT 4249 4248 4250 4252
CONECT 4250 4249 4251 4259
CONECT 4251 4250
CONECT 4252 4249 4253
CONECT 4253 4252 4254
CONECT 4254 4253 4255
CONECT 4255 4254 4256
CONECT 4256 4255 4257 4258
CONECT 4257 4256
CONECT 4258 4256
CONECT 4259 4250
END


A second structure was input as follows:


CRYST1  102.241  102.241  480.567  90.00  90.00 120.00 P 65          1
ATOM      1  N   MET A   1      56.165 -11.610  36.196  1.00106.53           N  
ANISOU    1  N   MET A   1    13083  13636  13756   2223   1372   -296       N  
ATOM      2  CA  MET A   1      55.678 -11.743  34.830  1.00107.26           C  
ANISOU    2  CA  MET A   1    13295  13703  13757   2267   1407   -386       C  
ATOM      3  C   MET A   1      55.531 -10.380  34.168  1.00105.24           C  
ANISOU    3  C   MET A   1    13095  13507  13385   2255   1440   -392       C  
ATOM      4  O   MET A   1      54.634  -9.611  34.506  1.00 90.97           O  
ANISOU    4  O   MET A   1    11303  11739  11524   2208   1367   -386       O  
ATOM      5  CB  MET A   1      54.340 -12.478  34.803  1.00111.00           C  
ANISOU    5  CB  MET A   1    13835  14138  14202   2240   1315   -444       C  
ATOM      6  CG  MET A   1      53.801 -12.692  33.404  1.00105.03           C  
ANISOU    6  CG  MET A   1    13203  13353  13348   2283   1336   -540       C  
ATOM      7  SD  MET A   1      55.000 -13.547  32.366  1.00152.63           S  
ANISOU    7  SD  MET A   1    19267  19316  19409   2376   1461   -586       S  
ATOM      8  CE  MET A   1      54.123 -13.597  30.811  1.00159.28           C  
ANISOU    8  CE  MET A   1    20274  20143  20101   2398   1466   -699       C  
ATOM      9  N   ASN A   2      56.417 -10.091  33.224  1.00112.04           N  
ANISOU    9  N   ASN A   2    13991  14371  14207   2296   1552   -408       N  
ATOM     10  CA  ASN A   2      56.384  -8.827  32.502  1.00101.70           C  
ANISOU   10  CA  ASN A   2    12762  13103  12775   2278   1590   -406       C  
ATOM     11  C   ASN A   2      55.829  -9.030  31.098  1.00 92.81           C  
ANISOU   11  C   ASN A   2    11791  11945  11528   2314   1605   -489       C  
ATOM     12  O   ASN A   2      56.583  -9.112  30.126  1.00 98.32           O  
ANISOU   12  O   ASN A   2    12543  12635  12179   2341   1718   -521       O  
ATOM     13  CB  ASN A   2      57.787  -8.227  32.431  1.00 90.37           C  
ANISOU   13  CB  ASN A   2    11269  11706  11363   2271   1713   -363       C  
ATOM     14  CG  ASN A   2      57.772  -6.740  32.143  1.00 88.09           C  
ANISOU   14  CG  ASN A   2    11047  11458  10965   2222   1732   -328       C  
ATOM     15  ND2 ASN A   2      58.735  -6.023  32.705  1.00 94.91           N  
ANISOU   15  ND2 ASN A   2    11821  12368  11873   2180   1792   -266       N  
ATOM     16  OD1 ASN A   2      56.906  -6.241  31.427  1.00 73.96           O  
ANISOU   16  OD1 ASN A   2     9392   9654   9056   2222   1686   -357       O  
ATOM     17  N   ILE A   3      54.505  -9.111  31.006  1.00 95.92           N  
ANISOU   17  N   ILE A   3    12250  12327  11869   2308   1491   -529       N  
ATOM     18  CA  ILE A   3      53.816  -9.390  29.750  1.00101.94           C  
ANISOU   18  CA  ILE A   3    13157  13060  12516   2339   1475   -612       C  
ATOM     19  C   ILE A   3      54.150  -8.365  28.671  1.00 99.13           C  
ANISOU   19  C   ILE A   3    12927  12719  12017   2340   1537   -608       C  
ATOM     20  O   ILE A   3      54.197  -8.693  27.484  1.00 95.05           O  
ANISOU   20  O   ILE A   3    12532  12179  11406   2365   1587   -669       O  
ATOM     21  CB  ILE A   3      52.290  -9.453  29.962  1.00106.79           C  
ANISOU   21  CB  ILE A   3    13795  13676  13102   2324   1326   -655       C  
ATOM     22  CG1 ILE A   3      51.958 -10.455  31.067  1.00107.39           C  
ANISOU   22  CG1 ILE A   3    13759  13738  13306   2297   1273   -655       C  
ATOM     23  CG2 ILE A   3      51.575  -9.836  28.676  1.00115.27           C  
ANISOU   23  CG2 ILE A   3    15014  14723  14062   2355   1295   -747       C  
ATOM     24  CD1 ILE A   3      50.481 -10.648  31.294  1.00107.37           C  
ANISOU   24  CD1 ILE A   3    13763  13748  13285   2267   1143   -714       C  
ATOM     25  N   GLN A   4      54.398  -7.129  29.091  1.00 93.54           N  
ANISOU   25  N   GLN A   4    12203  12048  11292   2305   1536   -536       N  
ATOM     26  CA  GLN A   4      54.761  -6.065  28.165  1.00 93.00           C  
ANISOU   26  CA  GLN A   4    12266  11985  11085   2288   1593   -516       C  
ATOM     27  C   GLN A   4      56.030  -6.425  27.402  1.00 99.78           C  
ANISOU   27  C   GLN A   4    13144  12844  11922   2287   1766   -532       C  
ATOM     28  O   GLN A   4      56.045  -6.429  26.172  1.00109.66           O  
ANISOU   28  O   GLN A   4    14545  14080  13042   2292   1817   -578       O  
ATOM     29  CB  GLN A   4      54.949  -4.745  28.915  1.00 86.08           C  
ANISOU   29  CB  GLN A   4    11351  11137  10217   2243   1572   -433       C  
ATOM     30  CG  GLN A   4      55.163  -3.534  28.018  1.00 96.83           C  
ANISOU   30  CG  GLN A   4    12876  12488  11428   2215   1605   -402       C  
ATOM     31  CD  GLN A   4      56.626  -3.280  27.708  1.00104.67           C  
ANISOU   31  CD  GLN A   4    13859  13503  12408   2166   1783   -369       C  
ATOM     32  NE2 GLN A   4      56.885  -2.302  26.849  1.00 90.04           N  
ANISOU   32  NE2 GLN A   4    12167  11636  10408   2123   1830   -342       N  
ATOM     33  OE1 GLN A   4      57.512  -3.951  28.238  1.00121.53           O  
ANISOU   33  OE1 GLN A   4    15844  15667  14665   2165   1873   -368       O  
ATOM     34  N   ALA A   5      57.089  -6.733  28.144  1.00 88.60           N  
ANISOU   34  N   ALA A   5    11573  11452  10638   2280   1854   -501       N  
ATOM     35  CA  ALA A   5      58.376  -7.088  27.557  1.00 91.00           C  
ANISOU   35  CA  ALA A   5    11853  11771  10953   2283   2025   -530       C  
ATOM     36  C   ALA A   5      58.272  -8.344  26.703  1.00 98.81           C  
ANISOU   36  C   ALA A   5    12895  12718  11930   2341   2064   -630       C  
ATOM     37  O   ALA A   5      59.013  -8.511  25.733  1.00 96.79           O  
ANISOU   37  O   ALA A   5    12695  12471  11611   2342   2203   -685       O  
ATOM     38  CB  ALA A   5      59.412  -7.279  28.646  1.00 89.05           C  
ANISOU   38  CB  ALA A   5    11406  11557  10873   2280   2076   -485       C  
ATOM     39  N   LEU A   6      57.354  -9.229  27.078  1.00100.47           N  
ANISOU   39  N   LEU A   6    13088  12885  12199   2380   1947   -661       N  
ATOM     40  CA  LEU A   6      57.111 -10.452  26.326  1.00105.34           C  
ANISOU   40  CA  LEU A   6    13766  13451  12807   2431   1964   -761       C  
ATOM     41  C   LEU A   6      56.601 -10.120  24.932  1.00112.24           C  
ANISOU   41  C   LEU A   6    14840  14320  13485   2419   1976   -818       C  
ATOM     42  O   LEU A   6      57.202 -10.504  23.929  1.00123.62           O  
ANISOU   42  O   LEU A   6    16352  15757  14862   2431   2101   -888       O  
ATOM     43  CB  LEU A   6      56.089 -11.327  27.051  1.00 97.13           C  
ANISOU   43  CB  LEU A   6    12685  12366  11854   2451   1822   -775       C  
ATOM     44  CG  LEU A   6      55.687 -12.624  26.348  1.00 95.14           C  
ANISOU   44  CG  LEU A   6    12504  12049  11596   2494   1819   -880       C  
ATOM     45  CD1 LEU A   6      56.784 -13.664  26.477  1.00 93.33           C  
ANISOU   45  CD1 LEU A   6    12182  11777  11501   2549   1924   -914       C  
ATOM     46  CD2 LEU A   6      54.379 -13.151  26.906  1.00 89.01           C  
ANISOU   46  CD2 LEU A   6    11728  11241  10850   2479   1661   -893       C  
ATOM     47  N   LEU A   7      55.487  -9.395  24.880  1.00101.76           N  
ANISOU   47  N   LEU A   7    13605  12998  12062   2397   1841   -792       N  
ATOM     48  CA  LEU A   7      54.885  -8.988  23.617  1.00100.99           C  
ANISOU   48  CA  LEU A   7    13710  12892  11769   2388   1815   -833       C  
ATOM     49  C   LEU A   7      55.770  -7.987  22.889  1.00112.32           C  
ANISOU   49  C   LEU A   7    15243  14356  13077   2339   1940   -796       C  
ATOM     50  O   LEU A   7      55.668  -7.824  21.675  1.00118.03           O  
ANISOU   50  O   LEU A   7    16146  15071  13629   2323   1974   -837       O  
ATOM     51  CB  LEU A   7      53.507  -8.373  23.863  1.00 96.86           C  
ANISOU   51  CB  LEU A   7    13237  12368  11197   2387   1623   -812       C  
ATOM     52  CG  LEU A   7      52.497  -9.260  24.589  1.00 94.40           C  
ANISOU   52  CG  LEU A   7    12834  12041  10995   2411   1496   -854       C  
ATOM     53  CD1 LEU A   7      51.262  -8.461  24.965  1.00 89.56           C  
ANISOU   53  CD1 LEU A   7    12232  11446  10350   2407   1322   -836       C  
ATOM     54  CD2 LEU A   7      52.125 -10.446  23.719  1.00 85.95           C  
ANISOU   54  CD2 LEU A   7    11843  10931   9882   2436   1499   -962       C  
ATOM     55  N   SER A   8      56.636  -7.314  23.641  1.00113.43           N  
ANISOU   55  N   SER A   8    15272  14531  13296   2306   2009   -719       N  
ATOM     56  CA  SER A   8      57.555  -6.343  23.065  1.00115.46           C  
ANISOU   56  CA  SER A   8    15607  14819  13444   2239   2141   -680       C  
ATOM     57  C   SER A   8      58.529  -7.032  22.121  1.00118.01           C  
ANISOU   57  C   SER A   8    15955  15156  13726   2234   2329   -764       C  
ATOM     58  O   SER A   8      58.917  -6.475  21.094  1.00110.10           O  
ANISOU   58  O   SER A   8    15107  14170  12557   2174   2430   -774       O  
ATOM     59  CB  SER A   8      58.323  -5.611  24.168  1.00108.43           C  
ANISOU   59  CB  SER A   8    14563  13967  12670   2200   2178   -592       C  
ATOM     60  OG  SER A   8      58.900  -4.410  23.683  1.00101.83           O  
ANISOU   60  OG  SER A   8    13833  13151  11707   2118   2262   -539       O  
ATOM     61  N   GLU A   9      58.913  -8.252  22.476  1.00122.15           N  
ANISOU   61  N   GLU A   9    16336  15673  14404   2295   2376   -828       N  
ATOM     62  CA  GLU A   9      59.862  -9.015  21.680  1.00122.61           C  
ANISOU   62  CA  GLU A   9    16386  15744  14457   2307   2556   -927       C  
ATOM     63  C   GLU A   9      59.177  -9.692  20.503  1.00116.66           C  
ANISOU   63  C   GLU A   9    15810  14951  13566   2328   2542  -1027       C  
ATOM     64  O   GLU A   9      59.636  -9.594  19.366  1.00120.91           O  
ANISOU   64  O   GLU A   9    16475  15510  13956   2286   2676  -1087       O  
ATOM     65  CB  GLU A   9      60.561 -10.064  22.545  1.00127.62           C  
ANISOU   65  CB  GLU A   9    16798  16370  15322   2379   2596   -959       C  
ATOM     66  CG  GLU A   9      61.680 -10.806  21.836  1.00139.07           C  
ANISOU   66  CG  GLU A   9    18203  17838  16801   2405   2792  -1072       C  
ATOM     67  CD  GLU A   9      62.926  -9.959  21.659  1.00142.48           C  
ANISOU   67  CD  GLU A   9    18577  18354  17206   2333   2967  -1056       C  
ATOM     68  OE1 GLU A   9      62.962  -8.829  22.191  1.00143.43           O  
ANISOU   68  OE1 GLU A   9    18686  18509  17301   2264   2931   -947       O  
ATOM     69  OE2 GLU A   9      63.873 -10.426  20.992  1.00138.49           O1-
ANISOU   69  OE2 GLU A   9    18032  17880  16706   2341   3147  -1160       O1-
ATOM     70  N   LYS A  10      58.070 -10.374  20.781  1.00111.26           N  
ANISOU   70  N   LYS A  10    15136  14214  12925   2382   2383  -1048       N  
ATOM     71  CA  LYS A  10      57.354 -11.127  19.757  1.00111.40           C  
ANISOU   71  CA  LYS A  10    15306  14191  12829   2403   2352  -1150       C  
ATOM     72  C   LYS A  10      56.787 -10.236  18.657  1.00115.57           C  
ANISOU   72  C   LYS A  10    16070  14733  13110   2344   2315  -1140       C  
ATOM     73  O   LYS A  10      56.456 -10.715  17.574  1.00119.79           O  
ANISOU   73  O   LYS A  10    16757  15250  13508   2342   2330  -1229       O  
ATOM     74  CB  LYS A  10      56.241 -11.968  20.382  1.00 94.89           C  
ANISOU   74  CB  LYS A  10    13166  12046  10841   2455   2179  -1170       C  
ATOM     75  CG  LYS A  10      56.743 -13.051  21.318  1.00 93.98           C  
ANISOU   75  CG  LYS A  10    12862  11895  10951   2513   2207  -1190       C  
ATOM     76  CD  LYS A  10      55.685 -14.112  21.550  1.00109.53           C  
ANISOU   76  CD  LYS A  10    14838  13798  12979   2546   2072  -1244       C  
ATOM     77  CE  LYS A  10      55.355 -14.848  20.261  1.00122.44           C  
ANISOU   77  CE  LYS A  10    16634  15399  14490   2556   2105  -1371       C  
ATOM     78  NZ  LYS A  10      54.348 -15.924  20.470  1.00128.50           N1+
ANISOU   78  NZ  LYS A  10    17409  16098  15316   2577   1980  -1432       N1+
ATOM     79  N   VAL A  11      56.665  -8.944  18.942  1.00104.31           N  
ANISOU   79  N   VAL A  11    14682  13330  11622   2297   2258  -1031       N  
ATOM     80  CA  VAL A  11      56.276  -7.983  17.921  1.00103.27           C  
ANISOU   80  CA  VAL A  11    14785  13199  11252   2239   2225  -1004       C  
ATOM     81  C   VAL A  11      57.530  -7.460  17.230  1.00108.44           C  
ANISOU   81  C   VAL A  11    15508  13896  11799   2156   2440  -1000       C  
ATOM     82  O   VAL A  11      57.544  -7.260  16.017  1.00115.01           O  
ANISOU   82  O   VAL A  11    16549  14730  12419   2102   2496  -1036       O  
ATOM     83  CB  VAL A  11      55.441  -6.820  18.506  1.00 99.29           C  
ANISOU   83  CB  VAL A  11    14314  12684  10729   2233   2042   -894       C  
ATOM     84  CG1 VAL A  11      55.254  -5.719  17.475  1.00 91.77           C  
ANISOU   84  CG1 VAL A  11    13615  11720   9533   2171   2017   -849       C  
ATOM     85  CG2 VAL A  11      54.089  -7.328  18.982  1.00 95.43           C  
ANISOU   85  CG2 VAL A  11    13780  12167  10313   2302   1834   -922       C  
ATOM     86  N   ARG A  12      58.596  -7.267  18.000  1.00110.13           N  
ANISOU   86  N   ARG A  12    15542  14148  12154   2138   2563   -963       N  
ATOM     87  CA  ARG A  12      59.859  -6.837  17.416  1.00114.36           C  
ANISOU   87  CA  ARG A  12    16104  14737  12608   2050   2785   -975       C  
ATOM     88  C   ARG A  12      60.460  -7.941  16.556  1.00126.31           C  
ANISOU   88  C   ARG A  12    17620  16269  14102   2065   2955  -1120       C  
ATOM     89  O   ARG A  12      60.910  -7.692  15.438  1.00126.14           O  
ANISOU   89  O   ARG A  12    17758  16276  13891   1984   3096  -1166       O  
ATOM     90  CB  ARG A  12      60.856  -6.414  18.492  1.00118.15           C  
ANISOU   90  CB  ARG A  12    16367  15263  13261   2030   2868   -912       C  
ATOM     91  CG  ARG A  12      62.125  -5.820  17.913  1.00121.38           C  
ANISOU   91  CG  ARG A  12    16800  15738  13580   1919   3095   -923       C  
ATOM     92  CD  ARG A  12      63.120  -5.435  18.992  1.00131.61           C  
ANISOU   92  CD  ARG A  12    17864  17087  15055   1897   3171   -870       C  
ATOM     93  NE  ARG A  12      63.766  -6.596  19.594  1.00142.89           N  
ANISOU   93  NE  ARG A  12    19044  18538  16710   1989   3235   -950       N  
ATOM     94  CZ  ARG A  12      64.929  -6.546  20.234  1.00147.66           C  
ANISOU   94  CZ  ARG A  12    19433  19207  17465   1975   3355   -953       C  
ATOM     95  NH1 ARG A  12      65.574  -5.393  20.345  1.00150.32           N1+
ANISOU   95  NH1 ARG A  12    19773  19598  17746   1859   3437   -883       N1+
ATOM     96  NH2 ARG A  12      65.452  -7.646  20.756  1.00144.61           N  
ANISOU   96  NH2 ARG A  12    18833  18826  17286   2077   3388  -1026       N  
ATOM     97  N   GLN A  13      60.463  -9.163  17.084  1.00139.35           N  
ANISOU   97  N   GLN A  13    19103  17898  15946   2166   2941  -1194       N  
ATOM     98  CA  GLN A  13      60.979 -10.314  16.349  1.00141.43           C  
ANISOU   98  CA  GLN A  13    19355  18162  16219   2201   3087  -1345       C  
ATOM     99  C   GLN A  13      60.073 -10.649  15.173  1.00144.30           C  
ANISOU   99  C   GLN A  13    19960  18490  16379   2191   3030  -1416       C  
ATOM    100  O   GLN A  13      60.473 -11.352  14.245  1.00153.47           O  
ANISOU  100  O   GLN A  13    21185  19660  17468   2187   3170  -1546       O  
ATOM    101  CB  GLN A  13      61.151 -11.520  17.270  1.00138.15           C  
ANISOU  101  CB  GLN A  13    18716  17709  16067   2318   3060  -1395       C  
ATOM    102  CG  GLN A  13      62.224 -11.326  18.329  1.00142.27           C  
ANISOU  102  CG  GLN A  13    18994  18274  16790   2333   3136  -1345       C  
ATOM    103  CD  GLN A  13      63.613 -11.160  17.737  1.00142.35           C  
ANISOU  103  CD  GLN A  13    18949  18362  16774   2282   3386  -1419       C  
ATOM    104  NE2 GLN A  13      64.005  -9.917  17.478  1.00132.56           N  
ANISOU  104  NE2 GLN A  13    17783  17187  15398   2163   3462  -1348       N  
ATOM    105  OE1 GLN A  13      64.327 -12.138  17.520  1.00148.03           O  
ANISOU  105  OE1 GLN A  13    19562  19083  17600   2346   3511  -1545       O  
ATOM    106  N   ALA A  14      58.847 -10.138  15.222  1.00134.96           N  
ANISOU  106  N   ALA A  14    18905  17271  15105   2188   2820  -1339       N  
ATOM    107  CA  ALA A  14      58.010 -10.059  14.037  1.00132.00           C  
ANISOU  107  CA  ALA A  14    18790  16876  14490   2153   2749  -1378       C  
ATOM    108  C   ALA A  14      58.548  -8.879  13.244  1.00139.22           C  
ANISOU  108  C   ALA A  14    19883  17833  15183   2034   2855  -1323       C  
ATOM    109  O   ALA A  14      59.751  -8.792  13.038  1.00151.80           O  
ANISOU  109  O   ALA A  14    21421  19479  16776   1977   3075  -1356       O  
ATOM    110  CB  ALA A  14      56.565  -9.840  14.421  1.00128.22           C  
ANISOU  110  CB  ALA A  14    18362  16351  14005   2196   2482  -1317       C  
ATOM    111  N   MET A  15      57.668  -7.969  12.824  1.00132.14           N  
ANISOU  111  N   MET A  15    19197  16911  14101   1994   2696  -1241       N  
ATOM    112  CA  MET A  15      58.053  -6.717  12.147  1.00133.27           C  
ANISOU  112  CA  MET A  15    19542  17072  14023   1874   2759  -1160       C  
ATOM    113  C   MET A  15      59.255  -6.812  11.194  1.00140.61           C  
ANISOU  113  C   MET A  15    20547  18061  14817   1767   3037  -1239       C  
ATOM    114  O   MET A  15      59.125  -6.556   9.998  1.00145.51           O  
ANISOU  114  O   MET A  15    21427  18683  15176   1683   3070  -1261       O  
ATOM    115  CB  MET A  15      58.271  -5.595  13.170  1.00133.58           C  
ANISOU  115  CB  MET A  15    19484  17110  14159   1853   2711  -1017       C  
ATOM    116  CG  MET A  15      56.990  -5.101  13.828  1.00139.93           C  
ANISOU  116  CG  MET A  15    20301  17859  15009   1926   2432   -929       C  
ATOM    117  SD  MET A  15      57.280  -3.911  15.152  1.00132.22           S  
ANISOU  117  SD  MET A  15    19181  16880  14178   1911   2386   -784       S  
ATOM    118  CE  MET A  15      57.577  -2.413  14.223  1.00 87.41           C  
ANISOU  118  CE  MET A  15    13807  11182   8224   1774   2422   -685       C  
ATOM    119  N   ILE A  16      60.419  -7.153  11.747  1.00139.91           N  
ANISOU  119  N   ILE A  16    20228  18026  14906   1767   3232  -1282       N  
ATOM    120  CA  ILE A  16      61.610  -7.490  10.971  1.00136.77           C  
ANISOU  120  CA  ILE A  16    19830  17699  14438   1688   3514  -1396       C  
ATOM    121  C   ILE A  16      61.265  -8.485   9.873  1.00143.38           C  
ANISOU  121  C   ILE A  16    20807  18525  15145   1705   3550  -1543       C  
ATOM    122  O   ILE A  16      61.665  -8.323   8.720  1.00147.94           O  
ANISOU  122  O   ILE A  16    21577  19142  15492   1593   3703  -1604       O  
ATOM    123  CB  ILE A  16      62.674  -8.160  11.863  1.00123.36           C  
ANISOU  123  CB  ILE A  16    17803  16046  13023   1752   3663  -1461       C  
ATOM    124  CG1 ILE A  16      63.058  -7.249  13.028  1.00115.42           C  
ANISOU  124  CG1 ILE A  16    16638  15057  12161   1735   3626  -1324       C  
ATOM    125  CG2 ILE A  16      63.898  -8.534  11.045  1.00128.87           C  
ANISOU  125  CG2 ILE A  16    18479  16825  13662   1679   3959  -1602       C  
ATOM    126  CD1 ILE A  16      63.859  -6.043  12.615  1.00115.06           C  
ANISOU  126  CD1 ILE A  16    16695  15068  11953   1570   3778  -1262       C  
ATOM    127  N   ALA A  17      60.505  -9.513  10.240  1.00141.21           N  
ANISOU  127  N   ALA A  17    20445  18197  15013   1835   3410  -1600       N  
ATOM    128  CA  ALA A  17      60.100 -10.549   9.297  1.00150.36           C  
ANISOU  128  CA  ALA A  17    21722  19335  16074   1861   3425  -1747       C  
ATOM    129  C   ALA A  17      59.038 -10.045   8.324  1.00156.73           C  
ANISOU  129  C   ALA A  17    22844  20112  16593   1801   3268  -1709       C  
ATOM    130  O   ALA A  17      58.486 -10.814   7.538  1.00161.08           O  
ANISOU  130  O   ALA A  17    23522  20642  17039   1818   3233  -1816       O  
ATOM    131  CB  ALA A  17      59.603 -11.778  10.044  1.00144.80           C  
ANISOU  131  CB  ALA A  17    20832  18572  15614   2007   3315  -1813       C  
ATOM    132  N   ALA A  18      58.754  -8.749   8.387  1.00148.11           N  
ANISOU  132  N   ALA A  18    21882  19015  15379   1734   3165  -1556       N  
ATOM    133  CA  ALA A  18      57.822  -8.114   7.469  1.00140.57           C  
ANISOU  133  CA  ALA A  18    21238  18028  14144   1677   3004  -1502       C  
ATOM    134  C   ALA A  18      58.478  -6.892   6.842  1.00140.73           C  
ANISOU  134  C   ALA A  18    21460  18077  13933   1521   3121  -1414       C  
ATOM    135  O   ALA A  18      57.805  -6.039   6.266  1.00147.74           O  
ANISOU  135  O   ALA A  18    22611  18926  14598   1467   2970  -1321       O  
ATOM    136  CB  ALA A  18      56.551  -7.720   8.196  1.00128.87           C  
ANISOU  136  CB  ALA A  18    19740  16484  12742   1769   2696  -1395       C  
ATOM    137  N   GLY A  19      59.798  -6.812   6.967  1.00133.07           N  
ANISOU  137  N   GLY A  19    20366  17174  13021   1448   3387  -1446       N  
ATOM    138  CA  GLY A  19      60.553  -5.709   6.402  1.00134.50           C  
ANISOU  138  CA  GLY A  19    20722  17391  12992   1276   3536  -1375       C  
ATOM    139  C   GLY A  19      60.700  -4.556   7.375  1.00133.42           C  
ANISOU  139  C   GLY A  19    20505  17232  12955   1259   3463  -1209       C  
ATOM    140  O   GLY A  19      59.874  -3.645   7.401  1.00137.58           O  
ANISOU  140  O   GLY A  19    21209  17690  13377   1254   3247  -1075       O  
ATOM    141  N   ALA A  20      61.758  -4.595   8.177  1.00138.19           N  
ANISOU  141  N   ALA A  20    20843  17895  13767   1252   3637  -1223       N  
ATOM    142  CA  ALA A  20      61.993  -3.558   9.174  1.00143.18           C  
ANISOU  142  CA  ALA A  20    21375  18514  14513   1231   3585  -1079       C  
ATOM    143  C   ALA A  20      63.480  -3.424   9.485  1.00161.33           C  
ANISOU  143  C   ALA A  20    23478  20906  16912   1139   3864  -1117       C  
ATOM    144  O   ALA A  20      64.230  -4.392   9.362  1.00175.11           O  
ANISOU  144  O   ALA A  20    25052  22722  18761   1164   4055  -1265       O  
ATOM    145  CB  ALA A  20      61.205  -3.861  10.439  1.00116.16           C  
ANISOU  145  CB  ALA A  20    17739  15041  11356   1402   3359  -1032       C  
ATOM    146  N   PRO A  21      63.914  -2.218   9.886  1.00153.51           N  
ANISOU  146  N   PRO A  21    22512  19917  15896   1033   3886   -991       N  
ATOM    147  CA  PRO A  21      65.324  -1.979  10.209  1.00156.70           C  
ANISOU  147  CA  PRO A  21    22727  20418  16393    929   4144  -1023       C  
ATOM    148  C   PRO A  21      65.716  -2.563  11.558  1.00159.21           C  
ANISOU  148  C   PRO A  21    22662  20769  17063   1064   4133  -1049       C  
ATOM    149  O   PRO A  21      64.855  -3.018  12.310  1.00158.21           O  
ANISOU  149  O   PRO A  21    22435  20580  17097   1222   3919  -1021       O  
ATOM    150  CB  PRO A  21      65.406  -0.455  10.271  1.00148.57           C  
ANISOU  150  CB  PRO A  21    21877  19351  15220    781   4110   -861       C  
ATOM    151  CG  PRO A  21      64.044  -0.033  10.682  1.00137.86           C  
ANISOU  151  CG  PRO A  21    20642  17874  13864    891   3785   -737       C  
ATOM    152  CD  PRO A  21      63.113  -0.986   9.992  1.00138.72           C  
ANISOU  152  CD  PRO A  21    20860  17951  13897    998   3671   -820       C  
ATOM    153  N   ALA A  22      67.011  -2.536  11.854  1.00169.20           N  
ANISOU  153  N   ALA A  22    23716  22133  18440    994   4362  -1105       N  
ATOM    154  CA  ALA A  22      67.531  -3.045  13.118  1.00174.94           C  
ANISOU  154  CA  ALA A  22    24079  22897  19492   1109   4362  -1129       C  
ATOM    155  C   ALA A  22      67.055  -2.198  14.291  1.00175.61           C  
ANISOU  155  C   ALA A  22    24111  22925  19689   1138   4157   -965       C  
ATOM    156  O   ALA A  22      66.399  -2.701  15.204  1.00164.80           O  
ANISOU  156  O   ALA A  22    22601  21507  18510   1292   3970   -938       O  
ATOM    157  CB  ALA A  22      69.048  -3.098  13.082  1.00176.59           C  
ANISOU  157  CB  ALA A  22    24086  23235  19776   1015   4651  -1230       C  
ATOM    158  N   ASP A  23      67.387  -0.910  14.266  1.00179.49           N  
ANISOU  158  N   ASP A  23    24721  23420  20058    982   4198   -859       N  
ATOM    159  CA  ASP A  23      66.925   0.016  15.293  1.00167.66           C  
ANISOU  159  CA  ASP A  23    23205  21860  18639    995   4010   -707       C  
ATOM    160  C   ASP A  23      65.418   0.199  15.194  1.00164.84           C  
ANISOU  160  C   ASP A  23    23063  21381  18189   1085   3735   -625       C  
ATOM    161  O   ASP A  23      64.931   1.247  14.771  1.00169.51           O  
ANISOU  161  O   ASP A  23    23919  21902  18585   1001   3647   -521       O  
ATOM    162  CB  ASP A  23      67.640   1.361  15.168  1.00161.25           C  
ANISOU  162  CB  ASP A  23    22503  21067  17696    793   4126   -621       C  
ATOM    163  CG  ASP A  23      69.064   1.311  15.682  1.00159.22           C  
ANISOU  163  CG  ASP A  23    21963  20935  17600    719   4350   -685       C  
ATOM    164  OD1 ASP A  23      69.584   0.193  15.879  1.00157.31           O  
ANISOU  164  OD1 ASP A  23    21469  20768  17534    817   4444   -812       O  
ATOM    165  OD2 ASP A  23      69.662   2.387  15.890  1.00160.20           O1-
ANISOU  165  OD2 ASP A  23    22114  21078  17676    563   4425   -611       O1-
ATOM    166  N   CYS A  24      64.686  -0.836  15.588  1.00156.17           N  
ANISOU  166  N   CYS A  24    21845  20257  17235   1257   3596   -676       N  
ATOM    167  CA  CYS A  24      63.237  -0.838  15.479  1.00152.06           C  
ANISOU  167  CA  CYS A  24    21491  19639  16647   1353   3341   -628       C  
ATOM    168  C   CYS A  24      62.588  -0.740  16.850  1.00153.90           C  
ANISOU  168  C   CYS A  24    21550  19833  17094   1466   3137   -556       C  
ATOM    169  O   CYS A  24      63.100  -1.278  17.832  1.00154.08           O  
ANISOU  169  O   CYS A  24    21295  19902  17347   1524   3177   -583       O  
ATOM    170  CB  CYS A  24      62.763  -2.102  14.767  1.00149.12           C  
ANISOU  170  CB  CYS A  24    21150  19264  16245   1444   3333   -752       C  
ATOM    171  SG  CYS A  24      60.987  -2.357  14.865  1.00178.09           S  
ANISOU  171  SG  CYS A  24    24931  22834  19899   1583   3012   -720       S  
ATOM    172  N   GLU A  25      61.455  -0.051  16.908  1.00153.17           N  
ANISOU  172  N   GLU A  25    21622  19655  16920   1498   2916   -469       N  
ATOM    173  CA  GLU A  25      60.759   0.164  18.168  1.00137.14           C  
ANISOU  173  CA  GLU A  25    19447  17590  15069   1592   2723   -406       C  
ATOM    174  C   GLU A  25      59.260  -0.053  18.049  1.00120.39           C  
ANISOU  174  C   GLU A  25    17432  15399  12913   1704   2478   -408       C  
ATOM    175  O   GLU A  25      58.543   0.803  17.535  1.00125.14           O  
ANISOU  175  O   GLU A  25    18266  15932  13351   1686   2346   -346       O  
ATOM    176  CB  GLU A  25      61.014   1.581  18.687  1.00134.49           C  
ANISOU  176  CB  GLU A  25    19159  17226  14713   1503   2699   -287       C  
ATOM    177  CG  GLU A  25      62.421   1.833  19.192  1.00139.24           C  
ANISOU  177  CG  GLU A  25    19588  17907  15411   1402   2907   -280       C  
ATOM    178  CD  GLU A  25      62.622   3.269  19.636  1.00143.96           C  
ANISOU  178  CD  GLU A  25    20262  18466  15970   1301   2879   -165       C  
ATOM    179  OE1 GLU A  25      61.652   4.054  19.566  1.00133.84           O  
ANISOU  179  OE1 GLU A  25    19168  17088  14595   1324   2692    -91       O  
ATOM    180  OE2 GLU A  25      63.747   3.615  20.053  1.00155.15           O1-
ANISOU  180  OE2 GLU A  25    21549  19947  17455   1200   3038   -154       O1-
ATOM    181  N   PRO A  26      58.778  -1.208  18.520  1.00106.38           N  
ANISOU  181  N   PRO A  26    15488  13637  11293   1818   2412   -481       N  
ATOM    182  CA  PRO A  26      57.337  -1.336  18.720  1.00 96.18           C  
ANISOU  182  CA  PRO A  26    14237  12292  10015   1920   2169   -481       C  
ATOM    183  C   PRO A  26      56.971  -0.600  19.999  1.00121.49           C  
ANISOU  183  C   PRO A  26    17316  15481  13363   1948   2041   -400       C  
ATOM    184  O   PRO A  26      57.773  -0.555  20.931  1.00139.05           O  
ANISOU  184  O   PRO A  26    19346  17746  15738   1923   2133   -374       O  
ATOM    185  CB  PRO A  26      57.147  -2.840  18.901  1.00 77.76           C  
ANISOU  185  CB  PRO A  26    11745   9985   7816   2006   2179   -587       C  
ATOM    186  CG  PRO A  26      58.434  -3.308  19.475  1.00 83.76           C  
ANISOU  186  CG  PRO A  26    12292  10804   8729   1982   2372   -608       C  
ATOM    187  CD  PRO A  26      59.502  -2.444  18.860  1.00106.43           C  
ANISOU  187  CD  PRO A  26    15269  13704  11467   1859   2550   -572       C  
ATOM    188  N   GLN A  27      55.784  -0.014  20.044  1.00118.02           N  
ANISOU  188  N   GLN A  27    16982  14984  12875   2000   1827   -368       N  
ATOM    189  CA  GLN A  27      55.362   0.700  21.240  1.00109.14           C  
ANISOU  189  CA  GLN A  27    15743  13845  11882   2030   1704   -307       C  
ATOM    190  C   GLN A  27      54.249  -0.050  21.949  1.00102.77           C  
ANISOU  190  C   GLN A  27    14788  13046  11214   2136   1543   -365       C  
ATOM    191  O   GLN A  27      53.079   0.305  21.856  1.00104.95           O  
ANISOU  191  O   GLN A  27    15143  13282  11450   2197   1351   -372       O  
ATOM    192  CB  GLN A  27      54.946   2.131  20.904  1.00113.42           C  
ANISOU  192  CB  GLN A  27    16500  14312  12284   2004   1589   -225       C  
ATOM    193  CG  GLN A  27      56.005   2.923  20.144  1.00121.61           C  
ANISOU  193  CG  GLN A  27    17716  15333  13159   1875   1748   -162       C  
ATOM    194  CD  GLN A  27      57.243   3.242  20.978  1.00127.57           C  
ANISOU  194  CD  GLN A  27    18303  16136  14030   1787   1921   -121       C  
ATOM    195  NE2 GLN A  27      57.608   4.517  21.019  1.00136.97           N  
ANISOU  195  NE2 GLN A  27    19617  17280  15147   1700   1932    -32       N  
ATOM    196  OE1 GLN A  27      57.864   2.358  21.571  1.00123.47           O  
ANISOU  196  OE1 GLN A  27    17554  15693  13665   1797   2035   -168       O  
ATOM    197  N   VAL A  28      54.641  -1.102  22.655  1.00 92.13           N  
ANISOU  197  N   VAL A  28    13224  11749  10031   2154   1622   -409       N  
ATOM    198  CA  VAL A  28      53.704  -1.959  23.359  1.00 96.69           C  
ANISOU  198  CA  VAL A  28    13657  12339  10743   2231   1498   -466       C  
ATOM    199  C   VAL A  28      53.294  -1.373  24.696  1.00 93.62           C  
ANISOU  199  C   VAL A  28    13122  11959  10489   2243   1397   -422       C  
ATOM    200  O   VAL A  28      54.012  -1.492  25.686  1.00 84.44           O  
ANISOU  200  O   VAL A  28    11788  10833   9463   2214   1478   -390       O  
ATOM    201  CB  VAL A  28      54.304  -3.345  23.588  1.00103.38           C  
ANISOU  201  CB  VAL A  28    14351  13221  11708   2242   1618   -526       C  
ATOM    202  CG1 VAL A  28      53.580  -4.378  22.740  1.00102.11           C  
ANISOU  202  CG1 VAL A  28    14270  13043  11486   2289   1568   -622       C  
ATOM    203  CG2 VAL A  28      55.780  -3.316  23.273  1.00104.26           C  
ANISOU  203  CG2 VAL A  28    14451  13359  11804   2180   1830   -507       C  
ATOM    204  N   ARG A  29      52.132  -0.734  24.718  1.00 93.27           N  
ANISOU  204  N   ARG A  29    13147  11885  10406   2288   1216   -426       N  
ATOM    205  CA  ARG A  29      51.596  -0.185  25.950  1.00 81.09           C  
ANISOU  205  CA  ARG A  29    11470  10353   8986   2304   1113   -406       C  
ATOM    206  C   ARG A  29      50.381  -0.991  26.368  1.00 93.38           C  
ANISOU  206  C   ARG A  29    12920  11935  10626   2364    979   -491       C  
ATOM    207  O   ARG A  29      49.975  -1.929  25.681  1.00 88.14           O  
ANISOU  207  O   ARG A  29    12296  11272   9922   2392    962   -559       O  
ATOM    208  CB  ARG A  29      51.191   1.275  25.756  1.00 88.80           C  
ANISOU  208  CB  ARG A  29    12591  11275   9873   2313   1006   -356       C  
ATOM    209  CG  ARG A  29      52.280   2.164  25.185  1.00 96.92           C  
ANISOU  209  CG  ARG A  29    13771  12267  10788   2237   1126   -271       C  
ATOM    210  CD  ARG A  29      53.456   2.291  26.137  1.00101.62           C  
ANISOU  210  CD  ARG A  29    14209  12905  11497   2160   1278   -219       C  
ATOM    211  NE  ARG A  29      54.559   1.400  25.787  1.00103.00           N  
ANISOU  211  NE  ARG A  29    14332  13124  11678   2114   1465   -230       N  
ATOM    212  CZ  ARG A  29      55.622   1.773  25.081  1.00 99.71           C  
ANISOU  212  CZ  ARG A  29    14020  12704  11160   2034   1617   -192       C  
ATOM    213  NH1 ARG A  29      55.727   3.022  24.650  1.00 90.27           N1+
ANISOU  213  NH1 ARG A  29    13006  11454   9839   1982   1602   -127       N1+
ATOM    214  NH2 ARG A  29      56.582   0.899  24.809  1.00 97.85           N  
ANISOU  214  NH2 ARG A  29    13710  12519  10951   2004   1785   -224       N  
ATOM    215  N   GLN A  30      49.805  -0.617  27.502  1.00103.19           N  
ANISOU  215  N   GLN A  30    14027  13200  11981   2374    891   -493       N  
ATOM    216  CA  GLN A  30      48.543  -1.182  27.941  1.00 99.25           C  
ANISOU  216  CA  GLN A  30    13428  12731  11553   2418    757   -579       C  
ATOM    217  C   GLN A  30      47.434  -0.355  27.314  1.00 98.08           C  
ANISOU  217  C   GLN A  30    13404  12549  11313   2487    581   -617       C  
ATOM    218  O   GLN A  30      47.492   0.874  27.333  1.00 98.75           O  
ANISOU  218  O   GLN A  30    13568  12594  11357   2498    537   -566       O  
ATOM    219  CB  GLN A  30      48.446  -1.131  29.464  1.00106.96           C  
ANISOU  219  CB  GLN A  30    14202  13756  12683   2386    752   -573       C  
ATOM    220  CG  GLN A  30      49.608  -1.799  30.174  1.00119.67           C  
ANISOU  220  CG  GLN A  30    15692  15391  14384   2323    904   -521       C  
ATOM    221  CD  GLN A  30      49.545  -1.630  31.679  1.00117.81           C  
ANISOU  221  CD  GLN A  30    15281  15203  14279   2281    892   -503       C  
ATOM    222  NE2 GLN A  30      50.545  -2.158  32.375  1.00106.74           N  
ANISOU  222  NE2 GLN A  30    13773  13822  12960   2229   1003   -452       N  
ATOM    223  OE1 GLN A  30      48.610  -1.031  32.210  1.00114.46           O  
ANISOU  223  OE1 GLN A  30    14814  14796  13879   2296    781   -541       O  
ATOM    224  N   SER A  31      46.434  -1.025  26.747  1.00101.57           N  
ANISOU  224  N   SER A  31    13867  13001  11723   2534    475   -707       N  
ATOM    225  CA  SER A  31      45.359  -0.334  26.042  1.00107.46           C  
ANISOU  225  CA  SER A  31    14734  13718  12380   2611    290   -752       C  
ATOM    226  C   SER A  31      44.611   0.633  26.949  1.00104.33           C  
ANISOU  226  C   SER A  31    14240  13330  12071   2652    166   -771       C  
ATOM    227  O   SER A  31      44.280   0.303  28.088  1.00110.63           O  
ANISOU  227  O   SER A  31    14838  14190  13007   2629    172   -814       O  
ATOM    228  CB  SER A  31      44.375  -1.334  25.433  1.00109.83           C  
ANISOU  228  CB  SER A  31    15031  14045  12654   2646    194   -861       C  
ATOM    229  OG  SER A  31      44.865  -2.658  25.531  1.00105.36           O  
ANISOU  229  OG  SER A  31    14389  13507  12134   2591    325   -882       O  
ATOM    230  N   ALA A  32      44.353   1.829  26.430  1.00102.83           N  
ANISOU  230  N   ALA A  32    14202  13074  11795   2711     54   -741       N  
ATOM    231  CA  ALA A  32      43.626   2.854  27.167  1.00116.07           C  
ANISOU  231  CA  ALA A  32    15809  14743  13549   2768    -76   -769       C  
ATOM    232  C   ALA A  32      42.240   2.358  27.544  1.00125.29           C  
ANISOU  232  C   ALA A  32    16814  15982  14808   2825   -217   -909       C  
ATOM    233  O   ALA A  32      41.962   2.080  28.709  1.00134.27           O  
ANISOU  233  O   ALA A  32    17742  17192  16083   2792   -189   -961       O  
ATOM    234  CB  ALA A  32      43.522   4.121  26.337  1.00120.87           C  
ANISOU  234  CB  ALA A  32    16644  15246  14034   2835   -194   -717       C  
ATOM    235  N   LYS A  33      41.372   2.246  26.547  1.00130.62           N  
ANISOU  235  N   LYS A  33    17588  16642  15400   2903   -370   -974       N  
ATOM    236  CA  LYS A  33      40.040   1.707  26.765  1.00137.67           C  
ANISOU  236  CA  LYS A  33    18325  17612  16370   2951   -506  -1121       C  
ATOM    237  C   LYS A  33      40.077   0.196  26.568  1.00131.98           C  
ANISOU  237  C   LYS A  33    17544  16952  15652   2880   -418  -1166       C  
ATOM    238  O   LYS A  33      40.995  -0.332  25.941  1.00127.40           O  
ANISOU  238  O   LYS A  33    17084  16338  14985   2829   -293  -1094       O  
ATOM    239  CB  LYS A  33      39.034   2.359  25.814  1.00149.13           C  
ANISOU  239  CB  LYS A  33    19902  19020  17741   3077   -738  -1178       C  
ATOM    240  CG  LYS A  33      37.583   2.130  26.200  1.00164.85           C  
ANISOU  240  CG  LYS A  33    21700  21097  19839   3141   -900  -1344       C  
ATOM    241  CD  LYS A  33      36.631   2.924  25.325  1.00178.04           C  
ANISOU  241  CD  LYS A  33    23486  22717  21443   3285  -1150  -1397       C  
ATOM    242  CE  LYS A  33      36.738   4.416  25.594  1.00183.22           C  
ANISOU  242  CE  LYS A  33    24219  23282  22114   3367  -1229  -1342       C  
ATOM    243  NZ  LYS A  33      35.673   5.173  24.882  1.00186.49           N1+
ANISOU  243  NZ  LYS A  33    24716  23647  22494   3525  -1501  -1412       N1+
ATOM    244  N   VAL A  34      39.083  -0.497  27.113  1.00133.34           N  
ANISOU  244  N   VAL A  34    17527  17212  15924   2872   -477  -1291       N  
ATOM    245  CA  VAL A  34      39.025  -1.949  27.024  1.00132.54           C  
ANISOU  245  CA  VAL A  34    17363  17160  15837   2797   -403  -1343       C  
ATOM    246  C   VAL A  34      38.625  -2.404  25.620  1.00129.11           C  
ANISOU  246  C   VAL A  34    17085  16701  15270   2840   -496  -1386       C  
ATOM    247  O   VAL A  34      38.706  -3.588  25.294  1.00120.08           O  
ANISOU  247  O   VAL A  34    15942  15574  14108   2782   -430  -1420       O  
ATOM    248  CB  VAL A  34      38.047  -2.534  28.063  1.00135.99           C  
ANISOU  248  CB  VAL A  34    17556  17699  16413   2753   -435  -1467       C  
ATOM    249  CG1 VAL A  34      36.618  -2.428  27.565  1.00137.79           C  
ANISOU  249  CG1 VAL A  34    17743  17974  16637   2832   -640  -1612       C  
ATOM    250  CG2 VAL A  34      38.400  -3.982  28.374  1.00137.85           C  
ANISOU  250  CG2 VAL A  34    17725  17963  16687   2640   -298  -1472       C  
ATOM    251  N   GLN A  35      38.199  -1.456  24.790  1.00134.55           N  
ANISOU  251  N   GLN A  35    17918  17342  15862   2941   -656  -1385       N  
ATOM    252  CA  GLN A  35      37.866  -1.748  23.399  1.00134.71           C  
ANISOU  252  CA  GLN A  35    18118  17333  15732   2983   -758  -1414       C  
ATOM    253  C   GLN A  35      39.079  -2.281  22.651  1.00125.66           C  
ANISOU  253  C   GLN A  35    17148  16132  14465   2916   -587  -1318       C  
ATOM    254  O   GLN A  35      38.952  -3.075  21.720  1.00127.14           O  
ANISOU  254  O   GLN A  35    17433  16319  14554   2902   -598  -1362       O  
ATOM    255  CB  GLN A  35      37.371  -0.488  22.692  1.00144.47           C  
ANISOU  255  CB  GLN A  35    19508  18507  16876   3103   -959  -1399       C  
ATOM    256  CG  GLN A  35      36.028   0.029  23.160  1.00153.06           C  
ANISOU  256  CG  GLN A  35    20436  19647  18072   3199  -1166  -1523       C  
ATOM    257  CD  GLN A  35      35.615   1.276  22.409  1.00165.46           C  
ANISOU  257  CD  GLN A  35    22183  21134  19550   3331  -1377  -1498       C  
ATOM    258  NE2 GLN A  35      34.349   1.657  22.538  1.00169.46           N  
ANISOU  258  NE2 GLN A  35    22570  21684  20134   3440  -1593  -1625       N  
ATOM    259  OE1 GLN A  35      36.425   1.889  21.715  1.00167.57           O  
ANISOU  259  OE1 GLN A  35    22693  21298  19677   3335  -1348  -1367       O  
ATOM    260  N   PHE A  36      40.257  -1.839  23.073  1.00112.15           N  
ANISOU  260  N   PHE A  36    15469  14380  12764   2872   -427  -1198       N  
ATOM    261  CA  PHE A  36      41.489  -2.137  22.360  1.00101.07           C  
ANISOU  261  CA  PHE A  36    14230  12927  11246   2814   -259  -1108       C  
ATOM    262  C   PHE A  36      42.258  -3.284  23.007  1.00109.42           C  
ANISOU  262  C   PHE A  36    15153  14018  12403   2726    -60  -1105       C  
ATOM    263  O   PHE A  36      43.477  -3.376  22.876  1.00106.20           O  
ANISOU  263  O   PHE A  36    14810  13580  11962   2676    113  -1023       O  
ATOM    264  CB  PHE A  36      42.365  -0.886  22.293  1.00 98.25           C  
ANISOU  264  CB  PHE A  36    14009  12500  10823   2815   -208   -980       C  
ATOM    265  CG  PHE A  36      41.632   0.342  21.829  1.00105.90           C  
ANISOU  265  CG  PHE A  36    15109  13415  11713   2908   -415   -971       C  
ATOM    266  CD1 PHE A  36      40.668   0.260  20.836  1.00114.14           C  
ANISOU  266  CD1 PHE A  36    16267  14451  12651   2978   -603  -1041       C  
ATOM    267  CD2 PHE A  36      41.899   1.577  22.394  1.00 99.65           C  
ANISOU  267  CD2 PHE A  36    14331  12575  10957   2929   -432   -895       C  
ATOM    268  CE1 PHE A  36      39.991   1.387  20.414  1.00108.94           C  
ANISOU  268  CE1 PHE A  36    15734  13733  11927   3077   -813  -1031       C  
ATOM    269  CE2 PHE A  36      41.227   2.708  21.974  1.00102.79           C  
ANISOU  269  CE2 PHE A  36    14861  12905  11291   3025   -634   -887       C  
ATOM    270  CZ  PHE A  36      40.272   2.613  20.982  1.00106.28           C  
ANISOU  270  CZ  PHE A  36    15415  13336  11630   3104   -829   -953       C  
ATOM    271  N   GLY A  37      41.540  -4.155  23.708  1.00119.11           N  
ANISOU  271  N   GLY A  37    16194  15307  13754   2705    -88  -1198       N  
ATOM    272  CA  GLY A  37      42.145  -5.330  24.308  1.00115.76           C  
ANISOU  272  CA  GLY A  37    15656  14901  13424   2627     72  -1200       C  
ATOM    273  C   GLY A  37      42.928  -5.045  25.573  1.00110.71           C  
ANISOU  273  C   GLY A  37    14883  14273  12911   2582    191  -1118       C  
ATOM    274  O   GLY A  37      42.644  -4.089  26.293  1.00113.10           O  
ANISOU  274  O   GLY A  37    15113  14592  13267   2602    130  -1097       O  
ATOM    275  N   ASP A  38      43.922  -5.884  25.841  1.00106.42           N  
ANISOU  275  N   ASP A  38    14305  13716  12413   2525    356  -1076       N  
ATOM    276  CA  ASP A  38      44.735  -5.760  27.044  1.00 99.20           C  
ANISOU  276  CA  ASP A  38    13260  12813  11617   2478    467   -999       C  
ATOM    277  C   ASP A  38      46.055  -5.047  26.763  1.00 91.17           C  
ANISOU  277  C   ASP A  38    12338  11757  10546   2474    591   -889       C  
ATOM    278  O   ASP A  38      46.678  -4.500  27.673  1.00102.85           O  
ANISOU  278  O   ASP A  38    13732  13248  12100   2446    652   -816       O  
ATOM    279  CB  ASP A  38      44.999  -7.139  27.655  1.00102.54           C  
ANISOU  279  CB  ASP A  38    13571  13243  12145   2420    555  -1020       C  
ATOM    280  CG  ASP A  38      43.733  -7.803  28.163  1.00115.50           C  
ANISOU  280  CG  ASP A  38    15100  14930  13853   2392    448  -1122       C  
ATOM    281  OD1 ASP A  38      42.926  -7.118  28.826  1.00123.13           O  
ANISOU  281  OD1 ASP A  38    15974  15947  14863   2395    351  -1151       O  
ATOM    282  OD2 ASP A  38      43.540  -9.007  27.892  1.00113.01           O1-
ANISOU  282  OD2 ASP A  38    14790  14599  13548   2364    466  -1182       O1-
ATOM    283  N   TYR A  39      46.471  -5.048  25.500  1.00101.99           N  
ANISOU  283  N   TYR A  39    13886  13088  11779   2493    630   -883       N  
ATOM    284  CA  TYR A  39      47.708  -4.384  25.100  1.00111.46           C  
ANISOU  284  CA  TYR A  39    15186  14256  12907   2473    759   -791       C  
ATOM    285  C   TYR A  39      47.627  -3.784  23.698  1.00112.05           C  
ANISOU  285  C   TYR A  39    15495  14290  12789   2498    719   -787       C  
ATOM    286  O   TYR A  39      46.890  -4.275  22.844  1.00111.97           O  
ANISOU  286  O   TYR A  39    15576  14273  12694   2528    633   -861       O  
ATOM    287  CB  TYR A  39      48.885  -5.357  25.182  1.00108.93           C  
ANISOU  287  CB  TYR A  39    14811  13934  12643   2434    942   -776       C  
ATOM    288  CG  TYR A  39      49.330  -5.662  26.591  1.00104.93           C  
ANISOU  288  CG  TYR A  39    14103  13455  12310   2401    998   -738       C  
ATOM    289  CD1 TYR A  39      50.214  -4.824  27.252  1.00106.60           C  
ANISOU  289  CD1 TYR A  39    14261  13678  12564   2370   1073   -648       C  
ATOM    290  CD2 TYR A  39      48.868  -6.788  27.258  1.00110.49           C  
ANISOU  290  CD2 TYR A  39    14682  14173  13127   2392    972   -790       C  
ATOM    291  CE1 TYR A  39      50.627  -5.094  28.538  1.00115.66           C  
ANISOU  291  CE1 TYR A  39    15232  14853  13859   2337   1113   -611       C  
ATOM    292  CE2 TYR A  39      49.274  -7.069  28.547  1.00118.63           C  
ANISOU  292  CE2 TYR A  39    15548  15224  14301   2355   1013   -748       C  
ATOM    293  CZ  TYR A  39      50.154  -6.218  29.182  1.00122.61           C  
ANISOU  293  CZ  TYR A  39    16000  15744  14843   2331   1080   -658       C  
ATOM    294  OH  TYR A  39      50.564  -6.493  30.466  1.00125.73           O  
ANISOU  294  OH  TYR A  39    16238  16162  15370   2291   1110   -613       O  
ATOM    295  N   GLN A  40      48.398  -2.724  23.473  1.00106.19           N  
ANISOU  295  N   GLN A  40    14856  13520  11972   2475    780   -698       N  
ATOM    296  CA  GLN A  40      48.444  -2.048  22.180  1.00 98.13           C  
ANISOU  296  CA  GLN A  40    14083  12452  10752   2479    752   -673       C  
ATOM    297  C   GLN A  40      49.856  -2.056  21.615  1.00110.03           C  
ANISOU  297  C   GLN A  40    15678  13949  12178   2408    962   -620       C  
ATOM    298  O   GLN A  40      50.822  -1.948  22.359  1.00113.04           O  
ANISOU  298  O   GLN A  40    15942  14351  12658   2363   1097   -568       O  
ATOM    299  CB  GLN A  40      48.007  -0.591  22.322  1.00 88.24           C  
ANISOU  299  CB  GLN A  40    12913  11158   9456   2508    619   -613       C  
ATOM    300  CG  GLN A  40      46.542  -0.377  22.612  1.00 96.44           C  
ANISOU  300  CG  GLN A  40    13900  12202  10541   2591    394   -679       C  
ATOM    301  CD  GLN A  40      46.200   1.094  22.743  1.00104.55           C  
ANISOU  301  CD  GLN A  40    15015  13174  11534   2631    266   -622       C  
ATOM    302  NE2 GLN A  40      44.957   1.384  23.103  1.00114.02           N  
ANISOU  302  NE2 GLN A  40    16144  14383  12797   2714     70   -688       N  
ATOM    303  OE1 GLN A  40      47.046   1.960  22.525  1.00103.80           O  
ANISOU  303  OE1 GLN A  40    15048  13028  11362   2586    343   -526       O  
ATOM    304  N   ALA A  41      49.973  -2.175  20.297  1.00104.50           N  
ANISOU  304  N   ALA A  41    15184  13226  11297   2393    989   -639       N  
ATOM    305  CA  ALA A  41      51.253  -1.975  19.629  1.00 88.93           C  
ANISOU  305  CA  ALA A  41    13324  11247   9216   2314   1186   -595       C  
ATOM    306  C   ALA A  41      51.158  -0.725  18.768  1.00105.26           C  
ANISOU  306  C   ALA A  41    15652  13259  11082   2286   1120   -524       C  
ATOM    307  O   ALA A  41      50.540  -0.741  17.705  1.00124.46           O  
ANISOU  307  O   ALA A  41    18280  15662  13347   2305   1021   -554       O  
ATOM    308  CB  ALA A  41      51.614  -3.179  18.781  1.00 94.95           C  
ANISOU  308  CB  ALA A  41    14125  12030   9921   2300   1305   -680       C  
ATOM    309  N   ASN A  42      51.765   0.360  19.238  1.00108.35           N  
ANISOU  309  N   ASN A  42    16053  13629  11485   2238   1166   -429       N  
ATOM    310  CA  ASN A  42      51.661   1.651  18.568  1.00119.36           C  
ANISOU  310  CA  ASN A  42    17700  14950  12700   2209   1088   -347       C  
ATOM    311  C   ASN A  42      52.784   1.906  17.569  1.00125.40           C  
ANISOU  311  C   ASN A  42    18657  15708  13281   2089   1279   -306       C  
ATOM    312  O   ASN A  42      52.741   2.872  16.807  1.00117.57           O  
ANISOU  312  O   ASN A  42    17922  14648  12101   2045   1227   -237       O  
ATOM    313  CB  ASN A  42      51.648   2.776  19.603  1.00120.05           C  
ANISOU  313  CB  ASN A  42    17717  15005  12891   2213   1025   -269       C  
ATOM    314  CG  ASN A  42      50.537   2.624  20.621  1.00112.86           C  
ANISOU  314  CG  ASN A  42    16616  14109  12156   2320    846   -317       C  
ATOM    315  ND2 ASN A  42      50.464   3.561  21.558  1.00 88.91           N  
ANISOU  315  ND2 ASN A  42    13512  11051   9218   2328    789   -266       N  
ATOM    316  OD1 ASN A  42      49.760   1.672  20.573  1.00120.28           O  
ANISOU  316  OD1 ASN A  42    17473  15086  13144   2384    768   -406       O  
ATOM    317  N   GLY A  43      53.784   1.031  17.570  1.00130.68           N  
ANISOU  317  N   GLY A  43    19205  16445  14002   2035   1499   -352       N  
ATOM    318  CA  GLY A  43      55.005   1.257  16.815  1.00132.72           C  
ANISOU  318  CA  GLY A  43    19587  16720  14122   1907   1719   -327       C  
ATOM    319  C   GLY A  43      54.887   1.257  15.302  1.00141.24           C  
ANISOU  319  C   GLY A  43    20960  17772  14934   1857   1729   -345       C  
ATOM    320  O   GLY A  43      55.868   1.516  14.606  1.00150.12           O  
ANISOU  320  O   GLY A  43    22210  18911  15916   1734   1918   -327       O  
ATOM    321  N   MET A  44      53.695   0.973  14.786  1.00134.96           N  
ANISOU  321  N   MET A  44    20273  16941  14063   1943   1529   -385       N  
ATOM    322  CA  MET A  44      53.493   0.888  13.340  1.00121.31           C  
ANISOU  322  CA  MET A  44    18830  15190  12073   1899   1516   -409       C  
ATOM    323  C   MET A  44      53.708   2.215  12.619  1.00117.57           C  
ANISOU  323  C   MET A  44    18662  14641  11368   1802   1493   -294       C  
ATOM    324  O   MET A  44      54.661   2.358  11.852  1.00123.31           O  
ANISOU  324  O   MET A  44    19537  15385  11929   1667   1691   -281       O  
ATOM    325  CB  MET A  44      52.096   0.355  13.015  1.00115.22           C  
ANISOU  325  CB  MET A  44    18099  14398  11280   2016   1276   -475       C  
ATOM    326  CG  MET A  44      51.853  -1.074  13.460  1.00120.79           C  
ANISOU  326  CG  MET A  44    18562  15168  12165   2088   1306   -598       C  
ATOM    327  SD  MET A  44      53.140  -2.210  12.913  1.00133.28           S  
ANISOU  327  SD  MET A  44    20096  16820  13726   2003   1620   -691       S  
ATOM    328  CE  MET A  44      53.952  -2.572  14.467  1.00117.16           C  
ANISOU  328  CE  MET A  44    17691  14826  11998   2025   1757   -685       C  
ATOM    329  N   MET A  45      52.814   3.169  12.878  1.00115.67           N  
ANISOU  329  N   MET A  45    18515  14316  11119   1870   1252   -218       N  
ATOM    330  CA  MET A  45      52.758   4.446  12.163  1.00115.22           C  
ANISOU  330  CA  MET A  45    18786  14157  10837   1804   1163   -104       C  
ATOM    331  C   MET A  45      54.117   5.098  11.934  1.00121.63           C  
ANISOU  331  C   MET A  45    19704  14969  11541   1624   1409    -29       C  
ATOM    332  O   MET A  45      54.448   5.479  10.812  1.00123.50           O  
ANISOU  332  O   MET A  45    20238  15172  11515   1507   1467     12       O  
ATOM    333  CB  MET A  45      51.851   5.432  12.902  1.00112.50           C  
ANISOU  333  CB  MET A  45    18433  13722  10588   1912    907    -36       C  
ATOM    334  CG  MET A  45      50.420   4.966  13.079  1.00103.90           C  
ANISOU  334  CG  MET A  45    17255  12631   9590   2083    643   -111       C  
ATOM    335  SD  MET A  45      50.303   3.465  14.063  1.00146.32           S  
ANISOU  335  SD  MET A  45    22223  18132  15241   2158    728   -247       S  
ATOM    336  CE  MET A  45      48.587   3.535  14.562  1.00107.56           C  
ANISOU  336  CE  MET A  45    17219  13196  10454   2339    390   -299       C  
ATOM    337  N   ALA A  46      54.893   5.226  13.005  1.00130.06           N  
ANISOU  337  N   ALA A  46    20530  16080  12806   1594   1551    -14       N  
ATOM    338  CA  ALA A  46      56.209   5.845  12.927  1.00131.74           C  
ANISOU  338  CA  ALA A  46    20798  16307  12950   1419   1790     47       C  
ATOM    339  C   ALA A  46      57.122   5.069  11.987  1.00125.07           C  
ANISOU  339  C   ALA A  46    20001  15550  11969   1300   2046    -29       C  
ATOM    340  O   ALA A  46      57.816   5.654  11.155  1.00126.52           O  
ANISOU  340  O   ALA A  46    20421  15718  11933   1136   2183     19       O  
ATOM    341  CB  ALA A  46      56.828   5.934  14.307  1.00135.18           C  
ANISOU  341  CB  ALA A  46    20923  16791  13647   1425   1885     54       C  
ATOM    342  N   VAL A  47      57.117   3.748  12.128  1.00123.53           N  
ANISOU  342  N   VAL A  47    19586  15445  11905   1377   2115   -154       N  
ATOM    343  CA  VAL A  47      57.885   2.886  11.243  1.00129.42           C  
ANISOU  343  CA  VAL A  47    20357  16274  12541   1290   2348   -253       C  
ATOM    344  C   VAL A  47      57.321   2.971   9.831  1.00135.02           C  
ANISOU  344  C   VAL A  47    21420  16935  12947   1248   2266   -252       C  
ATOM    345  O   VAL A  47      58.065   3.141   8.864  1.00135.16           O  
ANISOU  345  O   VAL A  47    21635  16976  12744   1090   2449   -256       O  
ATOM    346  CB  VAL A  47      57.874   1.425  11.728  1.00122.85           C  
ANISOU  346  CB  VAL A  47    19225  15525  11928   1404   2404   -388       C  
ATOM    347  CG1 VAL A  47      58.386   0.496  10.641  1.00115.83           C  
ANISOU  347  CG1 VAL A  47    18409  14701  10902   1342   2595   -507       C  
ATOM    348  CG2 VAL A  47      58.706   1.282  12.992  1.00120.71           C  
ANISOU  348  CG2 VAL A  47    18623  15314  11926   1415   2532   -391       C  
ATOM    349  N   ALA A  48      55.999   2.882   9.721  1.00142.99           N  
ANISOU  349  N   ALA A  48    22508  17881  13940   1381   1986   -249       N  
ATOM    350  CA  ALA A  48      55.317   3.009   8.436  1.00150.69           C  
ANISOU  350  CA  ALA A  48    23823  18802  14630   1359   1855   -241       C  
ATOM    351  C   ALA A  48      55.436   4.423   7.873  1.00161.98           C  
ANISOU  351  C   ALA A  48    25592  20132  15822   1240   1800    -95       C  
ATOM    352  O   ALA A  48      54.434   5.082   7.600  1.00170.20           O  
ANISOU  352  O   ALA A  48    26840  21069  16761   1309   1526    -21       O  
ATOM    353  CB  ALA A  48      53.860   2.620   8.574  1.00144.41           C  
ANISOU  353  CB  ALA A  48    22996  17969  13904   1538   1553   -277       C  
ATOM    354  N   LYS A  49      56.674   4.874   7.704  1.00160.15           N  
ANISOU  354  N   LYS A  49    25413  19930  15507   1061   2058    -59       N  
ATOM    355  CA  LYS A  49      56.965   6.200   7.185  1.00154.64           C  
ANISOU  355  CA  LYS A  49    25042  19136  14578    912   2050     82       C  
ATOM    356  C   LYS A  49      58.418   6.254   6.737  1.00164.90           C  
ANISOU  356  C   LYS A  49    26379  20518  15760    687   2403     63       C  
ATOM    357  O   LYS A  49      58.738   6.822   5.692  1.00170.82           O  
ANISOU  357  O   LYS A  49    27465  21230  16208    517   2472    120       O  
ATOM    358  CB  LYS A  49      56.703   7.268   8.245  1.00135.62           C  
ANISOU  358  CB  LYS A  49    22568  16633  12327    972   1894    197       C  
ATOM    359  CG  LYS A  49      57.437   8.569   7.989  1.00123.70           C  
ANISOU  359  CG  LYS A  49    21311  15044  10645    783   1982    330       C  
ATOM    360  CD  LYS A  49      56.883   9.697   8.829  1.00112.32           C  
ANISOU  360  CD  LYS A  49    19891  13472   9315    864   1757    448       C  
ATOM    361  CE  LYS A  49      57.629  10.988   8.548  1.00110.84           C  
ANISOU  361  CE  LYS A  49    19975  13191   8948    663   1846    581       C  
ATOM    362  NZ  LYS A  49      56.962  12.153   9.186  1.00104.41           N1+
ANISOU  362  NZ  LYS A  49    19251  12218   8204    750   1591    697       N1+
ATOM    363  N   LYS A  50      59.297   5.651   7.532  1.00164.71           N  
ANISOU  363  N   LYS A  50    26004  20607  15970    685   2625    -21       N  
ATOM    364  CA  LYS A  50      60.708   5.566   7.181  1.00161.10           C  
ANISOU  364  CA  LYS A  50    25515  20253  15443    487   2974    -71       C  
ATOM    365  C   LYS A  50      60.911   4.657   5.973  1.00156.40           C  
ANISOU  365  C   LYS A  50    25040  19734  14650    421   3126   -194       C  
ATOM    366  O   LYS A  50      61.938   4.726   5.300  1.00159.36           O  
ANISOU  366  O   LYS A  50    25505  20181  14864    227   3400   -233       O  
ATOM    367  CB  LYS A  50      61.538   5.071   8.367  1.00149.66           C  
ANISOU  367  CB  LYS A  50    23639  18908  14317    529   3144   -141       C  
ATOM    368  CG  LYS A  50      61.614   6.052   9.523  1.00138.91           C  
ANISOU  368  CG  LYS A  50    22167  17489  13124    542   3058    -25       C  
ATOM    369  CD  LYS A  50      62.606   5.585  10.573  1.00143.90           C  
ANISOU  369  CD  LYS A  50    22402  18237  14038    549   3254    -95       C  
ATOM    370  CE  LYS A  50      62.561   6.472  11.806  1.00139.85           C  
ANISOU  370  CE  LYS A  50    21762  17669  13706    579   3142     10       C  
ATOM    371  NZ  LYS A  50      61.223   6.435  12.459  1.00128.99           N1+
ANISOU  371  NZ  LYS A  50    20344  16205  12459    786   2828     46       N1+
ATOM    372  N   LEU A  51      59.925   3.804   5.710  1.00149.66           N  
ANISOU  372  N   LEU A  51    24184  18870  13810    578   2952   -265       N  
ATOM    373  CA  LEU A  51      59.919   2.977   4.509  1.00157.60           C  
ANISOU  373  CA  LEU A  51    25344  19930  14607    527   3049   -379       C  
ATOM    374  C   LEU A  51      58.860   3.500   3.547  1.00174.66           C  
ANISOU  374  C   LEU A  51    27904  21980  16477    523   2793   -294       C  
ATOM    375  O   LEU A  51      58.756   3.042   2.409  1.00182.90           O  
ANISOU  375  O   LEU A  51    29164  23050  17281    455   2837   -361       O  
ATOM    376  CB  LEU A  51      59.636   1.515   4.851  1.00139.91           C  
ANISOU  376  CB  LEU A  51    22810  17762  12588    695   3053   -540       C  
ATOM    377  CG  LEU A  51      60.192   0.989   6.172  1.00120.69           C  
ANISOU  377  CG  LEU A  51    19944  15392  10520    794   3154   -593       C  
ATOM    378  CD1 LEU A  51      59.037   0.661   7.091  1.00125.65           C  
ANISOU  378  CD1 LEU A  51    20403  15964  11375   1009   2868   -576       C  
ATOM    379  CD2 LEU A  51      61.080  -0.230   5.966  1.00111.85           C  
ANISOU  379  CD2 LEU A  51    18618  14393   9486    780   3430   -773       C  
ATOM    380  N   GLY A  52      58.066   4.452   4.026  1.00179.33           N  
ANISOU  380  N   GLY A  52    28589  22449  17098    602   2516   -151       N  
ATOM    381  CA  GLY A  52      57.105   5.157   3.197  1.00180.96           C  
ANISOU  381  CA  GLY A  52    29185  22533  17041    603   2247    -47       C  
ATOM    382  C   GLY A  52      55.983   4.319   2.613  1.00182.27           C  
ANISOU  382  C   GLY A  52    29415  22697  17145    739   2038   -129       C  
ATOM    383  O   GLY A  52      55.603   4.507   1.460  1.00183.01           O  
ANISOU  383  O   GLY A  52    29859  22747  16931    667   1947   -102       O  
ATOM    384  N   MET A  53      55.446   3.399   3.406  1.00179.85           N  
ANISOU  384  N   MET A  53    28777  22436  17120    926   1956   -229       N  
ATOM    385  CA  MET A  53      54.315   2.587   2.967  1.00174.93           C  
ANISOU  385  CA  MET A  53    28182  21812  16469   1060   1742   -314       C  
ATOM    386  C   MET A  53      53.013   3.074   3.598  1.00168.42           C  
ANISOU  386  C   MET A  53    27323  20894  15775   1246   1375   -243       C  
ATOM    387  O   MET A  53      52.819   4.274   3.787  1.00172.54           O  
ANISOU  387  O   MET A  53    27996  21311  16248   1241   1230   -101       O  
ATOM    388  CB  MET A  53      54.557   1.111   3.286  1.00168.59           C  
ANISOU  388  CB  MET A  53    27060  21126  15871   1128   1905   -492       C  
ATOM    389  CG  MET A  53      55.042   0.853   4.702  1.00162.16           C  
ANISOU  389  CG  MET A  53    25844  20355  15415   1206   2011   -512       C  
ATOM    390  SD  MET A  53      55.675  -0.820   4.912  1.00138.05           S  
ANISOU  390  SD  MET A  53    22469  17425  12556   1242   2263   -712       S  
ATOM    391  CE  MET A  53      57.040  -0.810   3.753  1.00241.07           C  
ANISOU  391  CE  MET A  53    35712  30545  25338   1013   2618   -764       C  
ATOM    392  N   ALA A  54      52.122   2.140   3.916  1.00157.92           N  
ANISOU  392  N   ALA A  54    25794  19598  14609   1408   1227   -349       N  
ATOM    393  CA  ALA A  54      50.855   2.479   4.555  1.00152.76           C  
ANISOU  393  CA  ALA A  54    25061  18878  14102   1589    892   -313       C  
ATOM    394  C   ALA A  54      50.694   1.703   5.857  1.00154.14           C  
ANISOU  394  C   ALA A  54    24810  19118  14639   1717    915   -399       C  
ATOM    395  O   ALA A  54      50.779   0.475   5.862  1.00158.50           O  
ANISOU  395  O   ALA A  54    25188  19753  15281   1739   1028   -531       O  
ATOM    396  CB  ALA A  54      49.693   2.196   3.616  1.00152.53           C  
ANISOU  396  CB  ALA A  54    25238  18822  13894   1657    630   -354       C  
ATOM    397  N   PRO A  55      50.464   2.424   6.966  1.00147.08           N  
ANISOU  397  N   PRO A  55    23758  18179  13947   1798    808   -324       N  
ATOM    398  CA  PRO A  55      50.377   1.867   8.322  1.00124.78           C  
ANISOU  398  CA  PRO A  55    20543  15409  11460   1902    834   -382       C  
ATOM    399  C   PRO A  55      49.398   0.708   8.439  1.00115.26           C  
ANISOU  399  C   PRO A  55    19167  14254  10373   2024    704   -514       C  
ATOM    400  O   PRO A  55      49.763  -0.350   8.949  1.00 98.13           O  
ANISOU  400  O   PRO A  55    16749  12161   8377   2034    860   -610       O  
ATOM    401  CB  PRO A  55      49.880   3.053   9.149  1.00119.82           C  
ANISOU  401  CB  PRO A  55    19892  14698  10938   1978    639   -274       C  
ATOM    402  CG  PRO A  55      50.381   4.240   8.423  1.00132.88           C  
ANISOU  402  CG  PRO A  55    21879  16262  12346   1860    656   -144       C  
ATOM    403  CD  PRO A  55      50.294   3.888   6.967  1.00147.57           C  
ANISOU  403  CD  PRO A  55    24035  18124  13910   1786    655   -173       C  
ATOM    404  N   ARG A  56      48.174   0.900   7.961  1.00120.64           N  
ANISOU  404  N   ARG A  56    19985  14892  10962   2113    416   -522       N  
ATOM    405  CA  ARG A  56      47.146  -0.126   8.083  1.00119.22           C  
ANISOU  405  CA  ARG A  56    19644  14760  10894   2222    271   -650       C  
ATOM    406  C   ARG A  56      47.409  -1.317   7.165  1.00126.80           C  
ANISOU  406  C   ARG A  56    20669  15780  11729   2157    410   -765       C  
ATOM    407  O   ARG A  56      46.646  -2.281   7.156  1.00119.18           O  
ANISOU  407  O   ARG A  56    19589  14856  10838   2224    317   -882       O  
ATOM    408  CB  ARG A  56      45.764   0.460   7.804  1.00115.00           C  
ANISOU  408  CB  ARG A  56    19229  14169  10297   2337    -84   -635       C  
ATOM    409  CG  ARG A  56      44.658  -0.191   8.607  1.00114.52           C  
ANISOU  409  CG  ARG A  56    18886  14157  10472   2471   -253   -741       C  
ATOM    410  CD  ARG A  56      43.319   0.422   8.268  1.00130.60           C  
ANISOU  410  CD  ARG A  56    21034  16144  12444   2588   -606   -739       C  
ATOM    411  NE  ARG A  56      42.543   0.723   9.466  1.00145.82           N  
ANISOU  411  NE  ARG A  56    22697  18079  14629   2711   -758   -760       N  
ATOM    412  CZ  ARG A  56      41.712  -0.132  10.050  1.00152.62           C  
ANISOU  412  CZ  ARG A  56    23296  19015  15677   2784   -837   -886       C  
ATOM    413  NH1 ARG A  56      41.547  -1.347   9.545  1.00154.13           N1+
ANISOU  413  NH1 ARG A  56    23461  19271  15831   2749   -787   -999       N1+
ATOM    414  NH2 ARG A  56      41.047   0.227  11.139  1.00149.13           N  
ANISOU  414  NH2 ARG A  56    22624  18583  15455   2881   -961   -905       N  
ATOM    415  N   GLN A  57      48.487  -1.239   6.390  1.00143.88           N  
ANISOU  415  N   GLN A  57    23017  17950  13703   2018    637   -740       N  
ATOM    416  CA  GLN A  57      48.902  -2.345   5.534  1.00153.97           C  
ANISOU  416  CA  GLN A  57    24352  19286  14864   1946    810   -859       C  
ATOM    417  C   GLN A  57      50.166  -3.013   6.070  1.00148.57           C  
ANISOU  417  C   GLN A  57    23450  18664  14336   1885   1140   -911       C  
ATOM    418  O   GLN A  57      50.343  -4.225   5.936  1.00140.89           O  
ANISOU  418  O   GLN A  57    22364  17744  13426   1889   1262  -1042       O  
ATOM    419  CB  GLN A  57      49.102  -1.874   4.094  1.00164.08           C  
ANISOU  419  CB  GLN A  57    26023  20538  15781   1828    819   -821       C  
ATOM    420  CG  GLN A  57      47.807  -1.485   3.405  1.00170.89           C  
ANISOU  420  CG  GLN A  57    27109  21347  16476   1896    480   -799       C  
ATOM    421  CD  GLN A  57      46.783  -2.606   3.421  1.00174.62           C  
ANISOU  421  CD  GLN A  57    27434  21865  17050   2001    331   -943       C  
ATOM    422  NE2 GLN A  57      45.526  -2.255   3.664  1.00170.75           N  
ANISOU  422  NE2 GLN A  57    26918  21340  16617   2127     10   -930       N  
ATOM    423  OE1 GLN A  57      47.119  -3.774   3.224  1.00178.75           O  
ANISOU  423  OE1 GLN A  57    27862  22450  17605   1967    503  -1071       O  
ATOM    424  N   LEU A  58      51.039  -2.218   6.681  1.00152.34           N  
ANISOU  424  N   LEU A  58    23869  19132  14882   1833   1274   -810       N  
ATOM    425  CA  LEU A  58      52.194  -2.755   7.390  1.00150.17           C  
ANISOU  425  CA  LEU A  58    23343  18915  14798   1798   1552   -851       C  
ATOM    426  C   LEU A  58      51.695  -3.526   8.603  1.00145.21           C  
ANISOU  426  C   LEU A  58    22382  18308  14484   1929   1476   -908       C  
ATOM    427  O   LEU A  58      52.358  -4.439   9.097  1.00140.31           O  
ANISOU  427  O   LEU A  58    21541  17734  14035   1935   1658   -987       O  
ATOM    428  CB  LEU A  58      53.128  -1.625   7.831  1.00141.40           C  
ANISOU  428  CB  LEU A  58    22242  17789  13694   1713   1676   -725       C  
ATOM    429  CG  LEU A  58      54.275  -1.983   8.782  1.00131.81           C  
ANISOU  429  CG  LEU A  58    20735  16635  12712   1692   1923   -748       C  
ATOM    430  CD1 LEU A  58      55.177  -3.041   8.169  1.00128.60           C  
ANISOU  430  CD1 LEU A  58    20292  16302  12270   1627   2188   -879       C  
ATOM    431  CD2 LEU A  58      55.075  -0.748   9.159  1.00131.49           C  
ANISOU  431  CD2 LEU A  58    20731  16576  12655   1598   2013   -619       C  
ATOM    432  N   ALA A  59      50.507  -3.151   9.066  1.00139.45           N  
ANISOU  432  N   ALA A  59    21623  17539  13822   2031   1201   -872       N  
ATOM    433  CA  ALA A  59      49.878  -3.774  10.223  1.00144.01           C  
ANISOU  433  CA  ALA A  59    21907  18135  14677   2142   1104   -921       C  
ATOM    434  C   ALA A  59      49.761  -5.290  10.086  1.00153.69           C  
ANISOU  434  C   ALA A  59    23013  19402  15981   2167   1173  -1069       C  
ATOM    435  O   ALA A  59      50.483  -6.032  10.750  1.00149.12           O  
ANISOU  435  O   ALA A  59    22221  18853  15583   2166   1349  -1112       O  
ATOM    436  CB  ALA A  59      48.513  -3.155  10.471  1.00145.41           C  
ANISOU  436  CB  ALA A  59    22109  18273  14869   2239    792   -887       C  
ATOM    437  N   GLU A  60      48.862  -5.749   9.220  1.00163.49           N  
ANISOU  437  N   GLU A  60    24397  20638  17084   2188   1028  -1146       N  
ATOM    438  CA  GLU A  60      48.625  -7.184   9.067  1.00154.17           C  
ANISOU  438  CA  GLU A  60    23120  19484  15972   2210   1069  -1292       C  
ATOM    439  C   GLU A  60      49.723  -7.887   8.272  1.00133.96           C  
ANISOU  439  C   GLU A  60    20641  16947  13309   2126   1336  -1369       C  
ATOM    440  O   GLU A  60      49.679  -9.102   8.086  1.00128.27           O  
ANISOU  440  O   GLU A  60    19855  16239  12642   2140   1399  -1498       O  
ATOM    441  CB  GLU A  60      47.251  -7.466   8.445  1.00150.59           C  
ANISOU  441  CB  GLU A  60    22776  19024  15415   2257    815  -1361       C  
ATOM    442  CG  GLU A  60      47.099  -7.034   6.996  1.00153.34           C  
ANISOU  442  CG  GLU A  60    23461  19358  15442   2198    755  -1356       C  
ATOM    443  CD  GLU A  60      46.867  -5.545   6.855  1.00155.92           C  
ANISOU  443  CD  GLU A  60    23960  19642  15639   2200    603  -1212       C  
ATOM    444  OE1 GLU A  60      47.763  -4.769   7.243  1.00146.83           O  
ANISOU  444  OE1 GLU A  60    22803  18475  14509   2155    739  -1108       O  
ATOM    445  OE2 GLU A  60      45.786  -5.154   6.365  1.00164.54           O1-
ANISOU  445  OE2 GLU A  60    25192  20711  16614   2249    339  -1206       O1-
ATOM    446  N   GLN A  61      50.707  -7.127   7.804  1.00120.98           N  
ANISOU  446  N   GLN A  61    19138  15308  11520   2036   1497  -1299       N  
ATOM    447  CA  GLN A  61      51.888  -7.729   7.200  1.00133.37           C  
ANISOU  447  CA  GLN A  61    20738  16913  13023   1954   1784  -1379       C  
ATOM    448  C   GLN A  61      52.747  -8.322   8.312  1.00133.83           C  
ANISOU  448  C   GLN A  61    20489  16993  13368   1990   1961  -1404       C  
ATOM    449  O   GLN A  61      53.557  -9.220   8.082  1.00128.51           O  
ANISOU  449  O   GLN A  61    19746  16346  12737   1971   2172  -1512       O  
ATOM    450  CB  GLN A  61      52.683  -6.694   6.404  1.00149.27           C  
ANISOU  450  CB  GLN A  61    22990  18934  14794   1828   1911  -1298       C  
ATOM    451  CG  GLN A  61      53.851  -7.278   5.627  1.00156.81           C  
ANISOU  451  CG  GLN A  61    23996  19938  15645   1729   2213  -1400       C  
ATOM    452  CD  GLN A  61      54.610  -6.230   4.841  1.00151.14           C  
ANISOU  452  CD  GLN A  61    23521  19233  14671   1581   2345  -1321       C  
ATOM    453  NE2 GLN A  61      55.762  -6.613   4.301  1.00143.01           N  
ANISOU  453  NE2 GLN A  61    22500  18262  13574   1482   2640  -1408       N  
ATOM    454  OE1 GLN A  61      54.168  -5.088   4.721  1.00149.95           O  
ANISOU  454  OE1 GLN A  61    23549  19037  14387   1553   2185  -1186       O  
ATOM    455  N   VAL A  62      52.547  -7.813   9.523  1.00142.72           N  
ANISOU  455  N   VAL A  62    21431  18106  14689   2047   1864  -1309       N  
ATOM    456  CA  VAL A  62      53.273  -8.280  10.696  1.00137.67           C  
ANISOU  456  CA  VAL A  62    20501  17483  14324   2086   1991  -1312       C  
ATOM    457  C   VAL A  62      52.561  -9.467  11.337  1.00139.45           C  
ANISOU  457  C   VAL A  62    20544  17691  14747   2179   1892  -1399       C  
ATOM    458  O   VAL A  62      53.202 -10.412  11.799  1.00150.73           O  
ANISOU  458  O   VAL A  62    21798  19125  16348   2206   2032  -1467       O  
ATOM    459  CB  VAL A  62      53.429  -7.149  11.733  1.00129.31           C  
ANISOU  459  CB  VAL A  62    19337  16420  13373   2090   1939  -1168       C  
ATOM    460  CG1 VAL A  62      54.073  -7.667  13.006  1.00132.98           C  
ANISOU  460  CG1 VAL A  62    19501  16903  14121   2133   2038  -1170       C  
ATOM    461  CG2 VAL A  62      54.245  -6.010  11.152  1.00123.14           C  
ANISOU  461  CG2 VAL A  62    18731  15649  12407   1981   2059  -1083       C  
ATOM    462  N   LEU A  63      51.232  -9.416  11.352  1.00132.83           N  
ANISOU  462  N   LEU A  63    19752  16832  13884   2225   1648  -1399       N  
ATOM    463  CA  LEU A  63      50.420 -10.483  11.932  1.00142.33           C  
ANISOU  463  CA  LEU A  63    20802  18021  15258   2293   1539  -1480       C  
ATOM    464  C   LEU A  63      50.673 -11.826  11.257  1.00158.28           C  
ANISOU  464  C   LEU A  63    22849  20030  17259   2287   1658  -1628       C  
ATOM    465  O   LEU A  63      50.457 -12.881  11.855  1.00163.26           O  
ANISOU  465  O   LEU A  63    23324  20638  18070   2330   1650  -1697       O  
ATOM    466  CB  LEU A  63      48.929 -10.144  11.850  1.00138.77           C  
ANISOU  466  CB  LEU A  63    20417  17562  14747   2330   1260  -1474       C  
ATOM    467  CG  LEU A  63      48.318  -9.275  12.952  1.00137.41           C  
ANISOU  467  CG  LEU A  63    20112  17392  14703   2374   1098  -1375       C  
ATOM    468  CD1 LEU A  63      48.906  -7.871  12.947  1.00145.08           C  
ANISOU  468  CD1 LEU A  63    21175  18360  15588   2344   1130  -1243       C  
ATOM    469  CD2 LEU A  63      46.803  -9.230  12.805  1.00126.96           C  
ANISOU  469  CD2 LEU A  63    18824  16070  13344   2420    831  -1416       C  
ATOM    470  N   THR A  64      51.125 -11.778  10.008  1.00162.32           N  
ANISOU  470  N   THR A  64    23572  20554  17550   2226   1769  -1677       N  
ATOM    471  CA  THR A  64      51.443 -12.984   9.255  1.00162.04           C  
ANISOU  471  CA  THR A  64    23584  20510  17476   2215   1901  -1829       C  
ATOM    472  C   THR A  64      52.569 -13.773   9.912  1.00161.99           C  
ANISOU  472  C   THR A  64    23369  20495  17686   2244   2115  -1876       C  
ATOM    473  O   THR A  64      52.625 -14.997   9.806  1.00162.35           O  
ANISOU  473  O   THR A  64    23363  20507  17815   2275   2174  -2002       O  
ATOM    474  CB  THR A  64      51.854 -12.651   7.809  1.00161.74           C  
ANISOU  474  CB  THR A  64    23815  20497  17142   2128   2008  -1868       C  
ATOM    475  CG2 THR A  64      50.700 -12.008   7.060  1.00157.36           C  
ANISOU  475  CG2 THR A  64    23489  19940  16362   2107   1775  -1833       C  
ATOM    476  OG1 THR A  64      52.970 -11.753   7.822  1.00164.97           O  
ANISOU  476  OG1 THR A  64    24238  20938  17504   2068   2182  -1782       O  
ATOM    477  N   HIS A  65      53.465 -13.067  10.593  1.00162.05           N  
ANISOU  477  N   HIS A  65    23259  20528  17787   2236   2222  -1777       N  
ATOM    478  CA  HIS A  65      54.604 -13.707  11.237  1.00167.90           C  
ANISOU  478  CA  HIS A  65    23793  21267  18735   2269   2415  -1814       C  
ATOM    479  C   HIS A  65      54.532 -13.555  12.750  1.00164.91           C  
ANISOU  479  C   HIS A  65    23178  20875  18604   2325   2328  -1713       C  
ATOM    480  O   HIS A  65      55.351 -14.110  13.483  1.00167.49           O  
ANISOU  480  O   HIS A  65    23314  21193  19133   2368   2441  -1729       O  
ATOM    481  CB  HIS A  65      55.910 -13.134  10.692  1.00175.45           C  
ANISOU  481  CB  HIS A  65    24795  22279  19591   2199   2652  -1811       C  
ATOM    482  CG  HIS A  65      56.010 -13.195   9.200  1.00184.79           C  
ANISOU  482  CG  HIS A  65    26224  23483  20503   2123   2749  -1906       C  
ATOM    483  CD2 HIS A  65      56.333 -14.215   8.371  1.00188.87           C  
ANISOU  483  CD2 HIS A  65    26798  23995  20969   2122   2886  -2070       C  
ATOM    484  ND1 HIS A  65      55.730 -12.116   8.390  1.00188.25           N  
ANISOU  484  ND1 HIS A  65    26902  23948  20677   2033   2701  -1833       N  
ATOM    485  CE1 HIS A  65      55.891 -12.465   7.125  1.00190.87           C  
ANISOU  485  CE1 HIS A  65    27430  24297  20794   1969   2808  -1944       C  
ATOM    486  NE2 HIS A  65      56.256 -13.733   7.087  1.00192.44           N  
ANISOU  486  NE2 HIS A  65    27519  24481  21119   2022   2926  -2095       N  
ATOM    487  N   LEU A  66      53.541 -12.798  13.207  1.00154.60           N  
ANISOU  487  N   LEU A  66    21891  19570  17282   2328   2122  -1614       N  
ATOM    488  CA  LEU A  66      53.272 -12.665  14.629  1.00139.88           C  
ANISOU  488  CA  LEU A  66    19819  17695  15633   2372   2019  -1529       C  
ATOM    489  C   LEU A  66      52.444 -13.851  15.097  1.00134.45           C  
ANISOU  489  C   LEU A  66    19043  16960  15083   2422   1906  -1604       C  
ATOM    490  O   LEU A  66      51.280 -13.990  14.723  1.00136.21           O  
ANISOU  490  O   LEU A  66    19360  17173  15222   2421   1743  -1643       O  
ATOM    491  CB  LEU A  66      52.517 -11.367  14.911  1.00136.13           C  
ANISOU  491  CB  LEU A  66    19399  17240  15085   2355   1847  -1410       C  
ATOM    492  CG  LEU A  66      52.066 -11.141  16.357  1.00124.14           C  
ANISOU  492  CG  LEU A  66    17681  15719  13766   2392   1724  -1330       C  
ATOM    493  CD1 LEU A  66      53.212 -10.625  17.215  1.00108.15           C  
ANISOU  493  CD1 LEU A  66    15508  13717  11867   2379   1856  -1242       C  
ATOM    494  CD2 LEU A  66      50.880 -10.193  16.405  1.00125.08           C  
ANISOU  494  CD2 LEU A  66    17877  15846  13803   2396   1507  -1272       C  
ATOM    495  N   ASP A  67      53.046 -14.710  15.910  1.00129.79           N  
ANISOU  495  N   ASP A  67    18273  16338  14703   2463   1988  -1625       N  
ATOM    496  CA  ASP A  67      52.339 -15.876  16.420  1.00135.79           C  
ANISOU  496  CA  ASP A  67    18955  17039  15599   2498   1892  -1689       C  
ATOM    497  C   ASP A  67      52.134 -15.803  17.927  1.00137.45           C  
ANISOU  497  C   ASP A  67    18970  17243  16011   2515   1803  -1595       C  
ATOM    498  O   ASP A  67      52.893 -16.390  18.698  1.00143.31           O  
ANISOU  498  O   ASP A  67    19567  17952  16930   2548   1883  -1583       O  
ATOM    499  CB  ASP A  67      53.077 -17.162  16.051  1.00135.99           C  
ANISOU  499  CB  ASP A  67    18966  17007  15696   2532   2040  -1810       C  
ATOM    500  CG  ASP A  67      52.303 -18.403  16.438  1.00135.69           C  
ANISOU  500  CG  ASP A  67    18889  16891  15775   2555   1938  -1882       C  
ATOM    501  OD1 ASP A  67      51.066 -18.409  16.265  1.00136.87           O  
ANISOU  501  OD1 ASP A  67    19112  17044  15849   2525   1775  -1902       O  
ATOM    502  OD2 ASP A  67      52.930 -19.366  16.925  1.00132.26           O1-
ANISOU  502  OD2 ASP A  67    18351  16390  15512   2602   2016  -1920       O1-
ATOM    503  N   LEU A  68      51.100 -15.080  18.342  1.00125.67           N  
ANISOU  503  N   LEU A  68    17476  15782  14490   2495   1632  -1533       N  
ATOM    504  CA  LEU A  68      50.767 -14.975  19.755  1.00115.13           C  
ANISOU  504  CA  LEU A  68    15968  14451  13325   2497   1541  -1454       C  
ATOM    505  C   LEU A  68      49.795 -16.077  20.152  1.00121.74           C  
ANISOU  505  C   LEU A  68    16763  15243  14251   2491   1429  -1524       C  
ATOM    506  O   LEU A  68      48.859 -15.849  20.918  1.00116.45           O  
ANISOU  506  O   LEU A  68    16019  14596  13632   2468   1289  -1493       O  
ATOM    507  CB  LEU A  68      50.176 -13.601  20.066  1.00103.50           C  
ANISOU  507  CB  LEU A  68    14499  13037  11788   2478   1423  -1362       C  
ATOM    508  CG  LEU A  68      51.101 -12.410  19.811  1.00 97.79           C  
ANISOU  508  CG  LEU A  68    13821  12351  10984   2466   1522  -1277       C  
ATOM    509  CD1 LEU A  68      50.409 -11.120  20.208  1.00 98.66           C  
ANISOU  509  CD1 LEU A  68    13937  12499  11050   2455   1384  -1192       C  
ATOM    510  CD2 LEU A  68      52.414 -12.578  20.561  1.00 84.76           C  
ANISOU  510  CD2 LEU A  68    12023  10699   9483   2474   1677  -1228       C  
ATOM    511  N   ASN A  69      50.023 -17.270  19.614  1.00132.11           N  
ANISOU  511  N   ASN A  69    18125  16491  15579   2506   1498  -1626       N  
ATOM    512  CA  ASN A  69      49.206 -18.430  19.930  1.00131.34           C  
ANISOU  512  CA  ASN A  69    18004  16334  15564   2489   1411  -1699       C  
ATOM    513  C   ASN A  69      49.664 -19.036  21.245  1.00117.65           C  
ANISOU  513  C   ASN A  69    16111  14548  14041   2498   1434  -1642       C  
ATOM    514  O   ASN A  69      50.852 -19.289  21.437  1.00105.71           O  
ANISOU  514  O   ASN A  69    14544  13001  12618   2543   1563  -1619       O  
ATOM    515  CB  ASN A  69      49.301 -19.468  18.814  1.00139.21           C  
ANISOU  515  CB  ASN A  69    19133  17269  16492   2500   1477  -1836       C  
ATOM    516  CG  ASN A  69      48.051 -20.314  18.700  1.00140.37           C  
ANISOU  516  CG  ASN A  69    19324  17381  16631   2457   1343  -1928       C  
ATOM    517  ND2 ASN A  69      47.048 -19.789  18.008  1.00140.91           N  
ANISOU  517  ND2 ASN A  69    19487  17509  16542   2426   1224  -1965       N  
ATOM    518  OD1 ASN A  69      47.983 -21.422  19.229  1.00139.67           O  
ANISOU  518  OD1 ASN A  69    19186  17209  16674   2449   1342  -1967       O  
ATOM    519  N   GLY A  70      48.719 -19.270  22.148  1.00122.31           N  
ANISOU  519  N   GLY A  70    16626  15137  14710   2451   1305  -1622       N  
ATOM    520  CA  GLY A  70      49.051 -19.701  23.491  1.00130.84           C  
ANISOU  520  CA  GLY A  70    17568  16177  15971   2442   1305  -1548       C  
ATOM    521  C   GLY A  70      49.233 -18.485  24.376  1.00124.88           C  
ANISOU  521  C   GLY A  70    16703  15505  15243   2432   1283  -1424       C  
ATOM    522  O   GLY A  70      49.561 -18.595  25.557  1.00124.91           O  
ANISOU  522  O   GLY A  70    16587  15494  15379   2419   1279  -1344       O  
ATOM    523  N   ILE A  71      49.015 -17.313  23.787  1.00110.20           N  
ANISOU  523  N   ILE A  71    14895  13725  13250   2436   1263  -1408       N  
ATOM    524  CA  ILE A  71      49.146 -16.051  24.500  1.00 91.20           C  
ANISOU  524  CA  ILE A  71    12406  11393  10854   2427   1239  -1300       C  
ATOM    525  C   ILE A  71      47.904 -15.194  24.308  1.00105.42           C  
ANISOU  525  C   ILE A  71    14242  13262  12552   2401   1097  -1316       C  
ATOM    526  O   ILE A  71      47.214 -14.860  25.268  1.00115.41           O  
ANISOU  526  O   ILE A  71    15404  14566  13879   2365   1003  -1283       O  
ATOM    527  CB  ILE A  71      50.372 -15.266  24.019  1.00 83.69           C  
ANISOU  527  CB  ILE A  71    11483  10464   9851   2466   1371  -1248       C  
ATOM    528  CG1 ILE A  71      51.651 -16.018  24.384  1.00 92.16           C  
ANISOU  528  CG1 ILE A  71    12478  11484  11054   2501   1504  -1233       C  
ATOM    529  CG2 ILE A  71      50.380 -13.871  24.622  1.00 74.56           C  
ANISOU  529  CG2 ILE A  71    10270   9379   8681   2449   1334  -1146       C  
ATOM    530  CD1 ILE A  71      52.909 -15.326  23.941  1.00 94.62           C  
ANISOU  530  CD1 ILE A  71    12795  11829  11329   2528   1650  -1197       C  
ATOM    531  N   ALA A  72      47.622 -14.845  23.058  1.00111.46           N  
ANISOU  531  N   ALA A  72    15152  14040  13157   2422   1079  -1371       N  
ATOM    532  CA  ALA A  72      46.457 -14.035  22.738  1.00105.47           C  
ANISOU  532  CA  ALA A  72    14439  13338  12296   2416    928  -1393       C  
ATOM    533  C   ALA A  72      45.358 -14.893  22.134  1.00111.62           C  
ANISOU  533  C   ALA A  72    15278  14106  13027   2395    828  -1517       C  
ATOM    534  O   ALA A  72      45.621 -15.965  21.592  1.00112.15           O  
ANISOU  534  O   ALA A  72    15408  14115  13088   2392    894  -1587       O  
ATOM    535  CB  ALA A  72      46.836 -12.916  21.788  1.00 94.68           C  
ANISOU  535  CB  ALA A  72    13207  11994  10771   2447    949  -1357       C  
ATOM    536  N   SER A  73      44.123 -14.418  22.230  1.00112.05           N  
ANISOU  536  N   SER A  73    15307  14216  13050   2383    666  -1552       N  
ATOM    537  CA  SER A  73      42.990 -15.147  21.686  1.00122.28           C  
ANISOU  537  CA  SER A  73    16643  15518  14300   2356    554  -1676       C  
ATOM    538  C   SER A  73      42.311 -14.318  20.607  1.00124.02           C  
ANISOU  538  C   SER A  73    16989  15781  14352   2395    430  -1713       C  
ATOM    539  O   SER A  73      41.369 -14.774  19.957  1.00128.54           O  
ANISOU  539  O   SER A  73    17614  16367  14857   2381    321  -1821       O  
ATOM    540  CB  SER A  73      41.991 -15.483  22.792  1.00120.23           C  
ANISOU  540  CB  SER A  73    16221  15296  14165   2296    459  -1710       C  
ATOM    541  OG  SER A  73      41.446 -14.305  23.357  1.00119.60           O  
ANISOU  541  OG  SER A  73    16053  15292  14098   2313    361  -1670       O  
ATOM    542  N   LYS A  74      42.807 -13.100  20.415  1.00111.40           N  
ANISOU  542  N   LYS A  74    15447  14199  12683   2441    441  -1623       N  
ATOM    543  CA  LYS A  74      42.191 -12.164  19.486  1.00105.54           C  
ANISOU  543  CA  LYS A  74    14836  13486  11781   2484    306  -1636       C  
ATOM    544  C   LYS A  74      43.106 -10.980  19.182  1.00104.87           C  
ANISOU  544  C   LYS A  74    14854  13386  11606   2518    373  -1521       C  
ATOM    545  O   LYS A  74      43.261 -10.076  20.002  1.00113.29           O  
ANISOU  545  O   LYS A  74    15833  14470  12743   2532    363  -1437       O  
ATOM    546  CB  LYS A  74      40.863 -11.672  20.062  1.00108.85           C  
ANISOU  546  CB  LYS A  74    15135  13969  12256   2497    112  -1678       C  
ATOM    547  CG  LYS A  74      40.182 -10.579  19.270  1.00109.94           C  
ANISOU  547  CG  LYS A  74    15386  14130  12254   2561    -59  -1682       C  
ATOM    548  CD  LYS A  74      38.943 -10.104  20.004  1.00107.07           C  
ANISOU  548  CD  LYS A  74    14863  13835  11985   2583   -237  -1734       C  
ATOM    549  CE  LYS A  74      38.320  -8.898  19.332  1.00110.17           C  
ANISOU  549  CE  LYS A  74    15360  14239  12262   2669   -421  -1727       C  
ATOM    550  NZ  LYS A  74      37.177  -8.378  20.127  1.00109.87           N1+
ANISOU  550  NZ  LYS A  74    15140  14269  12336   2704   -584  -1787       N1+
ATOM    551  N   VAL A  75      43.714 -10.992  18.000  1.00108.72           N  
ANISOU  551  N   VAL A  75    15533  13842  11933   2519    447  -1522       N  
ATOM    552  CA  VAL A  75      44.543  -9.877  17.560  1.00110.74           C  
ANISOU  552  CA  VAL A  75    15917  14084  12074   2530    512  -1420       C  
ATOM    553  C   VAL A  75      43.930  -9.223  16.331  1.00113.62           C  
ANISOU  553  C   VAL A  75    16498  14447  12224   2553    371  -1436       C  
ATOM    554  O   VAL A  75      43.689  -9.886  15.324  1.00121.41           O  
ANISOU  554  O   VAL A  75    17614  15427  13090   2540    356  -1520       O  
ATOM    555  CB  VAL A  75      45.966 -10.334  17.217  1.00109.87           C  
ANISOU  555  CB  VAL A  75    15860  13944  11943   2497    748  -1397       C  
ATOM    556  CG1 VAL A  75      46.809  -9.144  16.791  1.00109.73           C  
ANISOU  556  CG1 VAL A  75    15970  13919  11802   2486    823  -1293       C  
ATOM    557  CG2 VAL A  75      46.591 -11.045  18.403  1.00106.49           C  
ANISOU  557  CG2 VAL A  75    15225  13509  11728   2484    869  -1381       C  
ATOM    558  N   GLU A  76      43.678  -7.922  16.413  1.00106.92           N  
ANISOU  558  N   GLU A  76    15698  13599  11328   2588    260  -1357       N  
ATOM    559  CA  GLU A  76      43.028  -7.216  15.317  1.00116.50           C  
ANISOU  559  CA  GLU A  76    17123  14800  12342   2621     92  -1360       C  
ATOM    560  C   GLU A  76      43.581  -5.812  15.133  1.00121.31           C  
ANISOU  560  C   GLU A  76    17871  15370  12849   2628     95  -1232       C  
ATOM    561  O   GLU A  76      44.195  -5.251  16.038  1.00117.33           O  
ANISOU  561  O   GLU A  76    17260  14861  12457   2620    182  -1149       O  
ATOM    562  CB  GLU A  76      41.519  -7.151  15.549  1.00119.14           C  
ANISOU  562  CB  GLU A  76    17368  15170  12730   2681   -159  -1439       C  
ATOM    563  CG  GLU A  76      41.121  -6.402  16.809  1.00124.07           C  
ANISOU  563  CG  GLU A  76    17799  15816  13526   2723   -237  -1399       C  
ATOM    564  CD  GLU A  76      39.648  -6.554  17.126  1.00136.77           C  
ANISOU  564  CD  GLU A  76    19272  17478  15216   2771   -454  -1508       C  
ATOM    565  OE1 GLU A  76      38.999  -7.430  16.517  1.00145.30           O  
ANISOU  565  OE1 GLU A  76    20374  18583  16249   2759   -523  -1617       O  
ATOM    566  OE2 GLU A  76      39.138  -5.801  17.983  1.00133.71           O1-
ANISOU  566  OE2 GLU A  76    18750  17112  14941   2818   -552  -1495       O1-
ATOM    567  N   ILE A  77      43.353  -5.251  13.951  1.00130.85           N  
ANISOU  567  N   ILE A  77    19331  16548  13837   2636     -7  -1215       N  
ATOM    568  CA  ILE A  77      43.816  -3.909  13.638  1.00124.45           C  
ANISOU  568  CA  ILE A  77    18699  15685  12900   2632    -20  -1090       C  
ATOM    569  C   ILE A  77      42.685  -2.912  13.824  1.00120.61           C  
ANISOU  569  C   ILE A  77    18226  15179  12423   2726   -294  -1072       C  
ATOM    570  O   ILE A  77      41.531  -3.204  13.520  1.00123.18           O  
ANISOU  570  O   ILE A  77    18539  15527  12737   2787   -496  -1163       O  
ATOM    571  CB  ILE A  77      44.312  -3.808  12.187  1.00122.48           C  
ANISOU  571  CB  ILE A  77    18755  15403  12378   2572     34  -1069       C  
ATOM    572  CG1 ILE A  77      45.074  -5.073  11.789  1.00127.74           C  
ANISOU  572  CG1 ILE A  77    19406  16101  13028   2500    259  -1147       C  
ATOM    573  CG2 ILE A  77      45.177  -2.572  12.008  1.00119.45           C  
ANISOU  573  CG2 ILE A  77    18541  14965  11882   2526    110   -929       C  
ATOM    574  CD1 ILE A  77      46.354  -5.278  12.560  1.00132.78           C  
ANISOU  574  CD1 ILE A  77    19894  16751  13805   2448    521  -1106       C  
ATOM    575  N   ALA A  78      43.026  -1.732  14.325  1.00116.18           N  
ANISOU  575  N   ALA A  78    17683  14572  11888   2741   -301   -964       N  
ATOM    576  CA  ALA A  78      42.053  -0.669  14.507  1.00121.92           C  
ANISOU  576  CA  ALA A  78    18433  15263  12629   2840   -556   -943       C  
ATOM    577  C   ALA A  78      42.711   0.682  14.285  1.00119.86           C  
ANISOU  577  C   ALA A  78    18376  14911  12252   2822   -544   -800       C  
ATOM    578  O   ALA A  78      43.932   0.810  14.379  1.00110.07           O  
ANISOU  578  O   ALA A  78    17176  13657  10987   2728   -318   -721       O  
ATOM    579  CB  ALA A  78      41.442  -0.743  15.894  1.00115.91           C  
ANISOU  579  CB  ALA A  78    17364  14553  12125   2897   -609   -997       C  
ATOM    580  N   GLY A  79      41.893   1.685  13.988  1.00119.24           N  
ANISOU  580  N   GLY A  79    18429  14769  12109   2913   -793   -772       N  
ATOM    581  CA  GLY A  79      42.378   3.033  13.769  1.00119.08           C  
ANISOU  581  CA  GLY A  79    18627  14643  11977   2902   -819   -636       C  
ATOM    582  C   GLY A  79      43.368   3.115  12.626  1.00128.00           C  
ANISOU  582  C   GLY A  79    20054  15727  12852   2782   -672   -551       C  
ATOM    583  O   GLY A  79      43.259   2.376  11.647  1.00136.90           O  
ANISOU  583  O   GLY A  79    21303  16883  13828   2749   -668   -604       O  
ATOM    584  N   PRO A  80      44.350   4.018  12.748  1.00126.72           N  
ANISOU  584  N   PRO A  80    20011  15500  12638   2703   -541   -427       N  
ATOM    585  CA  PRO A  80      45.386   4.201  11.727  1.00129.11           C  
ANISOU  585  CA  PRO A  80    20595  15765  12697   2564   -374   -343       C  
ATOM    586  C   PRO A  80      46.463   3.124  11.772  1.00133.94           C  
ANISOU  586  C   PRO A  80    21082  16470  13339   2449    -60   -390       C  
ATOM    587  O   PRO A  80      47.577   3.374  11.322  1.00133.53           O  
ANISOU  587  O   PRO A  80    21177  16404  13154   2319    145   -321       O  
ATOM    588  CB  PRO A  80      45.994   5.556  12.091  1.00122.88           C  
ANISOU  588  CB  PRO A  80    19919  14878  11891   2522   -346   -206       C  
ATOM    589  CG  PRO A  80      45.768   5.685  13.550  1.00117.10           C  
ANISOU  589  CG  PRO A  80    18872  14176  11445   2598   -360   -234       C  
ATOM    590  CD  PRO A  80      44.451   5.019  13.823  1.00120.35           C  
ANISOU  590  CD  PRO A  80    19097  14643  11986   2739   -565   -361       C  
ATOM    591  N   GLY A  81      46.144   1.953  12.313  1.00140.91           N  
ANISOU  591  N   GLY A  81    21698  17445  14397   2493    -23   -507       N  
ATOM    592  CA  GLY A  81      47.070   0.837  12.275  1.00138.88           C  
ANISOU  592  CA  GLY A  81    21333  17264  14170   2406    245   -565       C  
ATOM    593  C   GLY A  81      47.608   0.380  13.616  1.00125.37           C  
ANISOU  593  C   GLY A  81    19299  15611  12725   2405    402   -585       C  
ATOM    594  O   GLY A  81      48.751  -0.064  13.707  1.00128.61           O  
ANISOU  594  O   GLY A  81    19647  16059  13160   2318    652   -583       O  
ATOM    595  N   PHE A  82      46.794   0.493  14.659  1.00103.27           N  
ANISOU  595  N   PHE A  82    16293  12822  10123   2500    254   -608       N  
ATOM    596  CA  PHE A  82      47.161  -0.048  15.958  1.00105.10           C  
ANISOU  596  CA  PHE A  82    16220  13113  10602   2500    377   -634       C  
ATOM    597  C   PHE A  82      47.023  -1.558  15.916  1.00109.46           C  
ANISOU  597  C   PHE A  82    16634  13730  11226   2503    446   -751       C  
ATOM    598  O   PHE A  82      46.117  -2.083  15.272  1.00118.97           O  
ANISOU  598  O   PHE A  82    17901  14942  12361   2546    308   -832       O  
ATOM    599  CB  PHE A  82      46.256   0.508  17.057  1.00110.37           C  
ANISOU  599  CB  PHE A  82    16717  13776  11442   2590    198   -636       C  
ATOM    600  CG  PHE A  82      46.449   1.970  17.319  1.00111.02           C  
ANISOU  600  CG  PHE A  82    16900  13786  11497   2593    142   -526       C  
ATOM    601  CD1 PHE A  82      47.559   2.418  18.011  1.00100.87           C  
ANISOU  601  CD1 PHE A  82    15546  12498  10281   2516    324   -447       C  
ATOM    602  CD2 PHE A  82      45.518   2.894  16.882  1.00114.69           C  
ANISOU  602  CD2 PHE A  82    17527  14180  11871   2673   -101   -507       C  
ATOM    603  CE1 PHE A  82      47.742   3.760  18.255  1.00 94.66           C  
ANISOU  603  CE1 PHE A  82    14860  11637   9469   2509    275   -349       C  
ATOM    604  CE2 PHE A  82      45.693   4.241  17.126  1.00110.63           C  
ANISOU  604  CE2 PHE A  82    17119  13581  11336   2679   -158   -407       C  
ATOM    605  CZ  PHE A  82      46.808   4.674  17.815  1.00 98.35           C  
ANISOU  605  CZ  PHE A  82    15502  12021   9846   2590     35   -329       C  
ATOM    606  N   ILE A  83      47.922  -2.255  16.599  1.00105.79           N  
ANISOU  606  N   ILE A  83    15987  13307  10901   2458    651   -761       N  
ATOM    607  CA  ILE A  83      47.805  -3.699  16.737  1.00108.17           C  
ANISOU  607  CA  ILE A  83    16143  13655  11303   2466    711   -868       C  
ATOM    608  C   ILE A  83      47.305  -4.034  18.134  1.00107.33           C  
ANISOU  608  C   ILE A  83    15766  13581  11435   2509    653   -892       C  
ATOM    609  O   ILE A  83      48.067  -4.013  19.100  1.00109.07           O  
ANISOU  609  O   ILE A  83    15827  13817  11796   2482    778   -846       O  
ATOM    610  CB  ILE A  83      49.141  -4.410  16.487  1.00107.05           C  
ANISOU  610  CB  ILE A  83    15987  13530  11157   2395    974   -879       C  
ATOM    611  CG1 ILE A  83      49.736  -3.966  15.151  1.00109.02           C  
ANISOU  611  CG1 ILE A  83    16507  13757  11159   2329   1060   -853       C  
ATOM    612  CG2 ILE A  83      48.953  -5.918  16.521  1.00107.57           C  
ANISOU  612  CG2 ILE A  83    15935  13621  11314   2413   1016   -995       C  
ATOM    613  CD1 ILE A  83      50.999  -4.705  14.777  1.00109.10           C  
ANISOU  613  CD1 ILE A  83    16503  13795  11155   2261   1323   -891       C  
ATOM    614  N   ASN A  84      46.016  -4.337  18.232  1.00100.79           N  
ANISOU  614  N   ASN A  84    14885  12768  10644   2568    462   -969       N  
ATOM    615  CA  ASN A  84      45.386  -4.609  19.517  1.00 95.91           C  
ANISOU  615  CA  ASN A  84    14022  12188  10232   2596    394  -1002       C  
ATOM    616  C   ASN A  84      45.413  -6.085  19.890  1.00106.35           C  
ANISOU  616  C   ASN A  84    15197  13540  11672   2571    478  -1085       C  
ATOM    617  O   ASN A  84      45.032  -6.946  19.097  1.00114.24           O  
ANISOU  617  O   ASN A  84    16268  14539  12600   2570    455  -1171       O  
ATOM    618  CB  ASN A  84      43.956  -4.074  19.522  1.00 91.63           C  
ANISOU  618  CB  ASN A  84    13478  11655   9683   2668    144  -1051       C  
ATOM    619  CG  ASN A  84      43.898  -2.591  19.227  1.00103.19           C  
ANISOU  619  CG  ASN A  84    15092  13070  11047   2706     41   -966       C  
ATOM    620  ND2 ASN A  84      42.756  -2.124  18.737  1.00104.72           N  
ANISOU  620  ND2 ASN A  84    15364  13252  11172   2781   -186  -1011       N  
ATOM    621  OD1 ASN A  84      44.873  -1.871  19.435  1.00106.39           O  
ANISOU  621  OD1 ASN A  84    15543  13443  11438   2668    159   -864       O  
ATOM    622  N   ILE A  85      45.866  -6.369  21.106  1.00106.14           N  
ANISOU  622  N   ILE A  85    14974  13533  11822   2547    570  -1057       N  
ATOM    623  CA  ILE A  85      46.052  -7.744  21.552  1.00105.39           C  
ANISOU  623  CA  ILE A  85    14750  13447  11846   2519    659  -1115       C  
ATOM    624  C   ILE A  85      45.139  -8.103  22.721  1.00109.35           C  
ANISOU  624  C   ILE A  85    15055  13986  12507   2515    559  -1156       C  
ATOM    625  O   ILE A  85      45.286  -7.575  23.822  1.00105.49           O  
ANISOU  625  O   ILE A  85    14436  13518  12128   2505    566  -1098       O  
ATOM    626  CB  ILE A  85      47.511  -7.989  21.961  1.00100.54           C  
ANISOU  626  CB  ILE A  85    14078  12820  11304   2484    867  -1049       C  
ATOM    627  CG1 ILE A  85      48.450  -7.553  20.837  1.00 95.34           C  
ANISOU  627  CG1 ILE A  85    13602  12138  10484   2470    985  -1014       C  
ATOM    628  CG2 ILE A  85      47.727  -9.448  22.310  1.00101.56           C  
ANISOU  628  CG2 ILE A  85    14102  12937  11548   2468    946  -1109       C  
ATOM    629  CD1 ILE A  85      49.909  -7.618  21.207  1.00 98.71           C  
ANISOU  629  CD1 ILE A  85    13959  12565  10980   2437   1188   -956       C  
ATOM    630  N   PHE A  86      44.201  -9.011  22.473  1.00113.30           N  
ANISOU  630  N   PHE A  86    15539  14498  13012   2513    473  -1263       N  
ATOM    631  CA  PHE A  86      43.269  -9.469  23.497  1.00108.56           C  
ANISOU  631  CA  PHE A  86    14760  13939  12548   2488    387  -1319       C  
ATOM    632  C   PHE A  86      43.776 -10.771  24.103  1.00112.45           C  
ANISOU  632  C   PHE A  86    15159  14408  13157   2433    508  -1331       C  
ATOM    633  O   PHE A  86      43.651 -11.832  23.491  1.00121.89           O  
ANISOU  633  O   PHE A  86    16413  15575  14327   2418    526  -1406       O  
ATOM    634  CB  PHE A  86      41.881  -9.690  22.892  1.00109.33           C  
ANISOU  634  CB  PHE A  86    14886  14068  12586   2506    212  -1438       C  
ATOM    635  CG  PHE A  86      41.210  -8.429  22.422  1.00110.06           C  
ANISOU  635  CG  PHE A  86    15052  14181  12587   2573     54  -1435       C  
ATOM    636  CD1 PHE A  86      41.692  -7.730  21.327  1.00108.18           C  
ANISOU  636  CD1 PHE A  86    15019  13900  12186   2614     55  -1382       C  
ATOM    637  CD2 PHE A  86      40.081  -7.955  23.065  1.00110.85           C  
ANISOU  637  CD2 PHE A  86    15019  14339  12760   2595    -98  -1490       C  
ATOM    638  CE1 PHE A  86      41.073  -6.575  20.896  1.00109.77           C  
ANISOU  638  CE1 PHE A  86    15306  14101  12300   2681   -108  -1371       C  
ATOM    639  CE2 PHE A  86      39.454  -6.803  22.637  1.00113.90           C  
ANISOU  639  CE2 PHE A  86    15471  14731  13074   2675   -259  -1494       C  
ATOM    640  CZ  PHE A  86      39.951  -6.112  21.551  1.00114.90           C  
ANISOU  640  CZ  PHE A  86    15818  14800  13039   2721   -271  -1428       C  
ATOM    641  N   LEU A  87      44.346 -10.688  25.302  1.00108.15           N  
ANISOU  641  N   LEU A  87    14481  13871  12741   2403    581  -1257       N  
ATOM    642  CA  LEU A  87      44.964 -11.847  25.943  1.00104.78           C  
ANISOU  642  CA  LEU A  87    13977  13408  12429   2359    689  -1247       C  
ATOM    643  C   LEU A  87      43.992 -13.004  26.145  1.00106.37           C  
ANISOU  643  C   LEU A  87    14129  13606  12680   2309    621  -1346       C  
ATOM    644  O   LEU A  87      42.808 -12.799  26.410  1.00111.11           O  
ANISOU  644  O   LEU A  87    14668  14263  13286   2286    495  -1409       O  
ATOM    645  CB  LEU A  87      45.599 -11.453  27.280  1.00104.54           C  
ANISOU  645  CB  LEU A  87    13808  13393  12519   2332    746  -1148       C  
ATOM    646  CG  LEU A  87      46.884 -10.623  27.233  1.00102.54           C  
ANISOU  646  CG  LEU A  87    13582  13131  12248   2361    857  -1045       C  
ATOM    647  CD1 LEU A  87      47.246 -10.125  28.620  1.00100.92           C  
ANISOU  647  CD1 LEU A  87    13233  12957  12156   2326    875   -960       C  
ATOM    648  CD2 LEU A  87      48.015 -11.449  26.655  1.00 99.04           C  
ANISOU  648  CD2 LEU A  87    13197  12630  11805   2377    998  -1040       C  
ATOM    649  N   ASP A  88      44.511 -14.219  26.013  1.00110.96           N  
ANISOU  649  N   ASP A  88    14737  14120  13302   2290    707  -1367       N  
ATOM    650  CA  ASP A  88      43.717 -15.429  26.176  1.00123.30           C  
ANISOU  650  CA  ASP A  88    16276  15660  14913   2229    660  -1457       C  
ATOM    651  C   ASP A  88      43.649 -15.830  27.644  1.00115.95           C  
ANISOU  651  C   ASP A  88    15202  14732  14123   2155    665  -1412       C  
ATOM    652  O   ASP A  88      44.680 -15.938  28.302  1.00109.51           O  
ANISOU  652  O   ASP A  88    14345  13878  13386   2160    758  -1320       O  
ATOM    653  CB  ASP A  88      44.317 -16.567  25.346  1.00137.23           C  
ANISOU  653  CB  ASP A  88    18151  17333  16656   2246    747  -1504       C  
ATOM    654  CG  ASP A  88      43.505 -17.846  25.429  1.00150.15           C  
ANISOU  654  CG  ASP A  88    19786  18929  18334   2176    697  -1601       C  
ATOM    655  OD1 ASP A  88      42.267 -17.764  25.552  1.00159.42           O  
ANISOU  655  OD1 ASP A  88    20918  20165  19491   2124    577  -1671       O  
ATOM    656  OD2 ASP A  88      44.108 -18.938  25.366  1.00149.20           O1-
ANISOU  656  OD2 ASP A  88    19708  18714  18267   2172    778  -1614       O1-
ATOM    657  N   PRO A  89      42.425 -16.027  28.161  1.00112.32           N  
ANISOU  657  N   PRO A  89    14663  14324  13689   2080    564  -1481       N  
ATOM    658  CA  PRO A  89      42.120 -16.483  29.521  1.00114.82           C  
ANISOU  658  CA  PRO A  89    14858  14653  14117   1979    559  -1458       C  
ATOM    659  C   PRO A  89      43.074 -17.549  30.059  1.00120.20           C  
ANISOU  659  C   PRO A  89    15554  15230  14887   1951    654  -1392       C  
ATOM    660  O   PRO A  89      43.580 -17.406  31.172  1.00128.07           O  
ANISOU  660  O   PRO A  89    16470  16229  15963   1919    689  -1298       O  
ATOM    661  CB  PRO A  89      40.719 -17.080  29.366  1.00118.74           C  
ANISOU  661  CB  PRO A  89    15333  15186  14595   1899    460  -1591       C  
ATOM    662  CG  PRO A  89      40.120 -16.382  28.157  1.00119.47           C  
ANISOU  662  CG  PRO A  89    15490  15330  14573   1976    374  -1670       C  
ATOM    663  CD  PRO A  89      41.203 -15.582  27.475  1.00113.16           C  
ANISOU  663  CD  PRO A  89    14786  14501  13710   2088    437  -1585       C  
ATOM    664  N   ALA A  90      43.314 -18.596  29.277  1.00119.66           N  
ANISOU  664  N   ALA A  90    15592  15068  14804   1968    689  -1443       N  
ATOM    665  CA  ALA A  90      44.150 -19.711  29.715  1.00120.51           C  
ANISOU  665  CA  ALA A  90    15724  15058  15005   1955    762  -1396       C  
ATOM    666  C   ALA A  90      45.605 -19.302  29.925  1.00117.66           C  
ANISOU  666  C   ALA A  90    15347  14667  14691   2041    860  -1284       C  
ATOM    667  O   ALA A  90      46.348 -19.966  30.647  1.00108.95           O  
ANISOU  667  O   ALA A  90    14222  13487  13688   2035    902  -1217       O  
ATOM    668  CB  ALA A  90      44.061 -20.857  28.725  1.00124.28           C  
ANISOU  668  CB  ALA A  90    16327  15440  15456   1966    776  -1494       C  
ATOM    669  N   PHE A  91      46.009 -18.211  29.283  1.00118.93           N  
ANISOU  669  N   PHE A  91    15522  14887  14778   2119    889  -1265       N  
ATOM    670  CA  PHE A  91      47.353 -17.678  29.458  1.00113.70           C  
ANISOU  670  CA  PHE A  91    14831  14217  14152   2188    985  -1167       C  
ATOM    671  C   PHE A  91      47.464 -16.957  30.799  1.00111.22           C  
ANISOU  671  C   PHE A  91    14391  13964  13905   2143    963  -1065       C  
ATOM    672  O   PHE A  91      48.444 -17.124  31.526  1.00110.60           O  
ANISOU  672  O   PHE A  91    14257  13851  13917   2155   1017   -979       O  
ATOM    673  CB  PHE A  91      47.701 -16.735  28.305  1.00105.55           C  
ANISOU  673  CB  PHE A  91    13875  13228  13003   2263   1027  -1182       C  
ATOM    674  CG  PHE A  91      48.983 -15.983  28.498  1.00102.37           C  
ANISOU  674  CG  PHE A  91    13430  12840  12625   2313   1125  -1086       C  
ATOM    675  CD1 PHE A  91      50.194 -16.552  28.146  1.00102.69           C  
ANISOU  675  CD1 PHE A  91    13490  12818  12711   2371   1242  -1079       C  
ATOM    676  CD2 PHE A  91      48.977 -14.699  29.019  1.00107.70           C  
ANISOU  676  CD2 PHE A  91    14043  13596  13283   2301   1102  -1014       C  
ATOM    677  CE1 PHE A  91      51.374 -15.860  28.317  1.00105.98           C  
ANISOU  677  CE1 PHE A  91    13853  13260  13153   2408   1335  -1002       C  
ATOM    678  CE2 PHE A  91      50.154 -14.003  29.194  1.00104.18           C  
ANISOU  678  CE2 PHE A  91    13559  13166  12858   2333   1193   -930       C  
ATOM    679  CZ  PHE A  91      51.354 -14.584  28.842  1.00105.60           C  
ANISOU  679  CZ  PHE A  91    13748  13293  13081   2383   1311   -925       C  
ATOM    680  N   LEU A  92      46.450 -16.158  31.118  1.00106.34           N  
ANISOU  680  N   LEU A  92    13724  13436  13244   2095    879  -1084       N  
ATOM    681  CA  LEU A  92      46.404 -15.432  32.382  1.00103.43           C  
ANISOU  681  CA  LEU A  92    13238  13134  12927   2042    855  -1007       C  
ATOM    682  C   LEU A  92      46.248 -16.386  33.558  1.00112.58           C  
ANISOU  682  C   LEU A  92    14339  14256  14179   1946    838   -979       C  
ATOM    683  O   LEU A  92      46.921 -16.247  34.579  1.00118.39           O  
ANISOU  683  O   LEU A  92    15006  14992  14983   1922    863   -881       O  
ATOM    684  CB  LEU A  92      45.247 -14.433  32.379  1.00 94.04           C  
ANISOU  684  CB  LEU A  92    12010  12046  11675   2019    765  -1062       C  
ATOM    685  CG  LEU A  92      45.281 -13.351  31.302  1.00 92.82           C  
ANISOU  685  CG  LEU A  92    11927  11924  11418   2108    755  -1079       C  
ATOM    686  CD1 LEU A  92      44.012 -12.521  31.350  1.00 90.21           C  
ANISOU  686  CD1 LEU A  92    11553  11679  11043   2094    640  -1147       C  
ATOM    687  CD2 LEU A  92      46.504 -12.468  31.472  1.00 94.93           C  
ANISOU  687  CD2 LEU A  92    12185  12193  11693   2155    837   -972       C  
ATOM    688  N   ALA A  93      45.362 -17.365  33.403  1.00113.65           N  
ANISOU  688  N   ALA A  93    14513  14358  14311   1882    791  -1062       N  
ATOM    689  CA  ALA A  93      45.078 -18.322  34.466  1.00112.60           C  
ANISOU  689  CA  ALA A  93    14351  14182  14249   1768    768  -1040       C  
ATOM    690  C   ALA A  93      46.182 -19.363  34.605  1.00115.66           C  
ANISOU  690  C   ALA A  93    14795  14436  14716   1803    822   -974       C  
ATOM    691  O   ALA A  93      45.953 -20.459  35.114  1.00133.91           O  
ANISOU  691  O   ALA A  93    17140  16666  17075   1723    798   -972       O  
ATOM    692  CB  ALA A  93      43.746 -19.002  34.216  1.00118.13           C  
ANISOU  692  CB  ALA A  93    15077  14892  14915   1675    704  -1159       C  
ATOM    693  N   GLU A  94      47.377 -19.016  34.141  1.00105.81           N  
ANISOU  693  N   GLU A  94    13558  13162  13484   1921    892   -923       N  
ATOM    694  CA  GLU A  94      48.525 -19.900  34.232  1.00104.11           C  
ANISOU  694  CA  GLU A  94    13373  12826  13358   1981    942   -870       C  
ATOM    695  C   GLU A  94      49.664 -19.163  34.920  1.00109.72           C  
ANISOU  695  C   GLU A  94    13995  13572  14123   2027    983   -755       C  
ATOM    696  O   GLU A  94      50.491 -19.768  35.600  1.00124.00           O  
ANISOU  696  O   GLU A  94    15783  15305  16027   2042    988   -680       O  
ATOM    697  CB  GLU A  94      48.960 -20.345  32.839  1.00104.52           C  
ANISOU  697  CB  GLU A  94    13520  12812  13382   2087   1004   -950       C  
ATOM    698  CG  GLU A  94      50.022 -21.426  32.839  1.00116.64           C  
ANISOU  698  CG  GLU A  94    15089  14209  15021   2158   1050   -928       C  
ATOM    699  CD  GLU A  94      50.644 -21.618  31.474  1.00129.78           C  
ANISOU  699  CD  GLU A  94    16823  15833  16654   2272   1138  -1010       C  
ATOM    700  OE1 GLU A  94      50.286 -22.598  30.788  1.00136.33           O  
ANISOU  700  OE1 GLU A  94    17752  16573  17473   2277   1135  -1104       O  
ATOM    701  OE2 GLU A  94      51.489 -20.784  31.087  1.00128.04           O1-
ANISOU  701  OE2 GLU A  94    16563  15673  16415   2347   1215   -986       O1-
ATOM    702  N   HIS A  95      49.694 -17.848  34.736  1.00105.10           N  
ANISOU  702  N   HIS A  95    13360  13096  13477   2049   1003   -743       N  
ATOM    703  CA  HIS A  95      50.691 -17.003  35.380  1.00114.23           C  
ANISOU  703  CA  HIS A  95    14428  14301  14674   2076   1040   -641       C  
ATOM    704  C   HIS A  95      50.135 -16.422  36.674  1.00113.93           C  
ANISOU  704  C   HIS A  95    14307  14341  14641   1969    978   -584       C  
ATOM    705  O   HIS A  95      50.888 -16.044  37.572  1.00115.01           O  
ANISOU  705  O   HIS A  95    14369  14500  14831   1958    987   -489       O  
ATOM    706  CB  HIS A  95      51.145 -15.888  34.440  1.00117.21           C  
ANISOU  706  CB  HIS A  95    14813  14740  14979   2153   1107   -656       C  
ATOM    707  CG  HIS A  95      51.825 -16.386  33.204  1.00115.63           C  
ANISOU  707  CG  HIS A  95    14691  14477  14767   2249   1188   -713       C  
ATOM    708  CD2 HIS A  95      53.129 -16.375  32.839  1.00121.14           C  
ANISOU  708  CD2 HIS A  95    15369  15153  15507   2330   1286   -689       C  
ATOM    709  ND1 HIS A  95      51.143 -16.993  32.172  1.00123.97           N  
ANISOU  709  ND1 HIS A  95    15853  15492  15758   2263   1179   -817       N  
ATOM    710  CE1 HIS A  95      51.997 -17.331  31.222  1.00130.35           C  
ANISOU  710  CE1 HIS A  95    16712  16252  16563   2348   1272   -856       C  
ATOM    711  NE2 HIS A  95      53.208 -16.966  31.602  1.00131.21           N  
ANISOU  711  NE2 HIS A  95    16741  16374  16739   2391   1341   -783       N  
ATOM    712  N   VAL A  96      48.810 -16.345  36.756  1.00105.46           N  
ANISOU  712  N   VAL A  96    13242  13317  13512   1886    916   -652       N  
ATOM    713  CA  VAL A  96      48.136 -16.012  38.003  1.00 96.82           C  
ANISOU  713  CA  VAL A  96    12072  12294  12423   1766    862   -623       C  
ATOM    714  C   VAL A  96      48.463 -17.106  39.008  1.00103.47           C  
ANISOU  714  C   VAL A  96    12920  13056  13339   1694    842   -552       C  
ATOM    715  O   VAL A  96      48.624 -16.855  40.204  1.00111.75           O  
ANISOU  715  O   VAL A  96    13906  14142  14412   1617    822   -474       O  
ATOM    716  CB  VAL A  96      46.604 -15.897  37.799  1.00 87.38           C  
ANISOU  716  CB  VAL A  96    10875  11163  11161   1693    804   -737       C  
ATOM    717  CG1 VAL A  96      45.835 -16.616  38.901  1.00 84.84           C  
ANISOU  717  CG1 VAL A  96    10526  10846  10862   1540    759   -740       C  
ATOM    718  CG2 VAL A  96      46.191 -14.440  37.720  1.00 88.55           C  
ANISOU  718  CG2 VAL A  96    10963  11426  11256   1715    789   -763       C  
ATOM    719  N   GLN A  97      48.586 -18.322  38.493  1.00 93.29           N  
ANISOU  719  N   GLN A  97    11716  11648  12080   1721    843   -579       N  
ATOM    720  CA  GLN A  97      48.894 -19.487  39.302  1.00 97.70           C  
ANISOU  720  CA  GLN A  97    12313  12099  12710   1665    812   -514       C  
ATOM    721  C   GLN A  97      50.377 -19.523  39.656  1.00104.26           C  
ANISOU  721  C   GLN A  97    13113  12875  13626   1758    836   -406       C  
ATOM    722  O   GLN A  97      50.749 -19.893  40.770  1.00119.12           O  
ANISOU  722  O   GLN A  97    14981  14721  15559   1700    793   -310       O  
ATOM    723  CB  GLN A  97      48.507 -20.754  38.539  1.00106.12           C  
ANISOU  723  CB  GLN A  97    13493  13045  13784   1672    802   -592       C  
ATOM    724  CG  GLN A  97      48.659 -22.031  39.332  1.00125.44           C  
ANISOU  724  CG  GLN A  97    16008  15358  16297   1602    755   -531       C  
ATOM    725  CD  GLN A  97      47.365 -22.478  39.976  1.00140.61           C  
ANISOU  725  CD  GLN A  97    17959  17298  18170   1416    702   -565       C  
ATOM    726  NE2 GLN A  97      46.264 -22.359  39.242  1.00138.08           N  
ANISOU  726  NE2 GLN A  97    17646  17038  17781   1376    704   -691       N  
ATOM    727  OE1 GLN A  97      47.356 -22.937  41.117  1.00151.98           O  
ANISOU  727  OE1 GLN A  97    19416  18699  19631   1303    659   -482       O  
ATOM    728  N   GLN A  98      51.218 -19.134  38.703  1.00105.22           N  
ANISOU  728  N   GLN A  98    13223  12995  13759   1896    905   -426       N  
ATOM    729  CA  GLN A  98      52.664 -19.157  38.896  1.00108.54           C  
ANISOU  729  CA  GLN A  98    13595  13375  14269   1995    938   -347       C  
ATOM    730  C   GLN A  98      53.087 -18.142  39.954  1.00104.39           C  
ANISOU  730  C   GLN A  98    12964  12951  13750   1950    925   -250       C  
ATOM    731  O   GLN A  98      54.051 -18.359  40.688  1.00102.65           O  
ANISOU  731  O   GLN A  98    12696  12697  13611   1974    906   -159       O  
ATOM    732  CB  GLN A  98      53.388 -18.874  37.578  1.00111.81           C  
ANISOU  732  CB  GLN A  98    14015  13789  14677   2132   1032   -409       C  
ATOM    733  CG  GLN A  98      54.774 -19.496  37.485  1.00112.67           C  
ANISOU  733  CG  GLN A  98    14098  13811  14901   2250   1070   -378       C  
ATOM    734  CD  GLN A  98      55.542 -19.031  36.262  1.00115.62           C  
ANISOU  734  CD  GLN A  98    14458  14215  15258   2364   1185   -442       C  
ATOM    735  NE2 GLN A  98      55.993 -19.979  35.449  1.00117.07           N  
ANISOU  735  NE2 GLN A  98    14695  14296  15491   2460   1229   -514       N  
ATOM    736  OE1 GLN A  98      55.727 -17.833  36.051  1.00119.94           O  
ANISOU  736  OE1 GLN A  98    14955  14873  15745   2360   1236   -432       O  
ATOM    737  N   ALA A  99      52.355 -17.036  40.027  1.00103.94           N  
ANISOU  737  N   ALA A  99    12870  13015  13608   1887    929   -274       N  
ATOM    738  CA  ALA A  99      52.627 -15.996  41.012  1.00 97.11           C  
ANISOU  738  CA  ALA A  99    11911  12249  12738   1833    919   -198       C  
ATOM    739  C   ALA A  99      52.372 -16.508  42.424  1.00 98.96           C  
ANISOU  739  C   ALA A  99    12135  12469  12994   1709    843   -123       C  
ATOM    740  O   ALA A  99      53.121 -16.202  43.350  1.00113.22           O  
ANISOU  740  O   ALA A  99    13879  14300  14839   1690    824    -28       O  
ATOM    741  CB  ALA A  99      51.776 -14.768  40.732  1.00 85.25           C  
ANISOU  741  CB  ALA A  99    10386  10862  11143   1799    931   -257       C  
ATOM    742  N   LEU A 100      51.311 -17.293  42.578  1.00 90.36           N  
ANISOU  742  N   LEU A 100    11114  11344  11876   1616    798   -167       N  
ATOM    743  CA  LEU A 100      50.938 -17.840  43.877  1.00 95.39           C  
ANISOU  743  CA  LEU A 100    11765  11964  12513   1472    731   -103       C  
ATOM    744  C   LEU A 100      52.005 -18.775  44.439  1.00 99.49           C  
ANISOU  744  C   LEU A 100    12318  12362  13121   1508    687      6       C  
ATOM    745  O   LEU A 100      52.239 -18.809  45.648  1.00110.32           O  
ANISOU  745  O   LEU A 100    13674  13743  14498   1419    632    103       O  
ATOM    746  CB  LEU A 100      49.604 -18.581  43.775  1.00 91.89           C  
ANISOU  746  CB  LEU A 100    11396  11498  12020   1360    705   -186       C  
ATOM    747  CG  LEU A 100      48.370 -17.726  43.491  1.00 98.00           C  
ANISOU  747  CG  LEU A 100    12123  12402  12711   1298    722   -297       C  
ATOM    748  CD1 LEU A 100      47.165 -18.608  43.221  1.00103.01           C  
ANISOU  748  CD1 LEU A 100    12825  13005  13311   1202    699   -392       C  
ATOM    749  CD2 LEU A 100      48.097 -16.801  44.661  1.00101.00           C  
ANISOU  749  CD2 LEU A 100    12415  12905  13053   1187    713   -263       C  
ATOM    750  N   ALA A 101      52.654 -19.527  43.557  1.00 78.81           N  
ANISOU  750  N   ALA A 101     9746   9629  10571   1641    705    -14       N  
ATOM    751  CA  ALA A 101      53.639 -20.517  43.977  1.00 83.46           C  
ANISOU  751  CA  ALA A 101    10368  10082  11259   1701    651     73       C  
ATOM    752  C   ALA A 101      54.977 -19.883  44.335  1.00 84.85           C  
ANISOU  752  C   ALA A 101    10435  10300  11503   1793    658    153       C  
ATOM    753  O   ALA A 101      55.910 -20.575  44.741  1.00 84.63           O  
ANISOU  753  O   ALA A 101    10411  10175  11571   1860    602    228       O  
ATOM    754  CB  ALA A 101      53.826 -21.564  42.896  1.00 96.89           C  
ANISOU  754  CB  ALA A 101    12152  11643  13017   1816    671      2       C  
ATOM    755  N   SER A 102      55.068 -18.567  44.180  1.00 89.01           N  
ANISOU  755  N   SER A 102    10867  10969  11984   1798    720    135       N  
ATOM    756  CA  SER A 102      56.293 -17.844  44.496  1.00104.07           C  
ANISOU  756  CA  SER A 102    12662  12934  13947   1866    736    201       C  
ATOM    757  C   SER A 102      56.076 -16.837  45.618  1.00113.17           C  
ANISOU  757  C   SER A 102    13750  14210  15039   1740    709    264       C  
ATOM    758  O   SER A 102      54.990 -16.276  45.763  1.00107.37           O  
ANISOU  758  O   SER A 102    13030  13554  14211   1634    720    219       O  
ATOM    759  CB  SER A 102      56.832 -17.129  43.257  1.00113.26           C  
ANISOU  759  CB  SER A 102    13773  14148  15114   1988    848    126       C  
ATOM    760  OG  SER A 102      55.869 -16.233  42.730  1.00120.57           O  
ANISOU  760  OG  SER A 102    14714  15164  15931   1936    898     53       O  
ATOM    761  N   ASP A 103      57.120 -16.606  46.406  1.00124.78           N  
ANISOU  761  N   ASP A 103    15143  15700  16566   1756    671    358       N  
ATOM    762  CA  ASP A 103      57.047 -15.658  47.508  1.00121.65           C  
ANISOU  762  CA  ASP A 103    14686  15419  16115   1638    644    418       C  
ATOM    763  C   ASP A 103      57.254 -14.237  47.003  1.00112.07           C  
ANISOU  763  C   ASP A 103    13386  14327  14868   1666    736    372       C  
ATOM    764  O   ASP A 103      57.061 -13.270  47.739  1.00116.08           O  
ANISOU  764  O   ASP A 103    13846  14938  15321   1572    732    394       O  
ATOM    765  CB  ASP A 103      58.087 -15.997  48.576  1.00129.46           C  
ANISOU  765  CB  ASP A 103    15634  16381  17175   1638    552    539       C  
ATOM    766  CG  ASP A 103      57.971 -17.428  49.065  1.00134.99           C  
ANISOU  766  CG  ASP A 103    16441  16937  17911   1618    447    599       C  
ATOM    767  OD1 ASP A 103      57.230 -17.667  50.043  1.00131.17           O  
ANISOU  767  OD1 ASP A 103    16028  16456  17353   1462    381    647       O  
ATOM    768  OD2 ASP A 103      58.619 -18.313  48.468  1.00136.26           O1-
ANISOU  768  OD2 ASP A 103    16621  16979  18173   1755    433    593       O1-
ATOM    769  N   ARG A 104      57.651 -14.120  45.741  1.00104.90           N  
ANISOU  769  N   ARG A 104    12468  13401  13988   1791    819    305       N  
ATOM    770  CA  ARG A 104      57.836 -12.820  45.114  1.00 94.70           C  
ANISOU  770  CA  ARG A 104    11123  12205  12654   1817    909    260       C  
ATOM    771  C   ARG A 104      56.738 -12.564  44.091  1.00 95.60           C  
ANISOU  771  C   ARG A 104    11313  12325  12684   1821    959    157       C  
ATOM    772  O   ARG A 104      56.825 -11.634  43.291  1.00 91.52           O  
ANISOU  772  O   ARG A 104    10789  11859  12126   1861   1032    111       O  
ATOM    773  CB  ARG A 104      59.212 -12.735  44.455  1.00 98.17           C  
ANISOU  773  CB  ARG A 104    11489  12635  13174   1940    975    263       C  
ATOM    774  CG  ARG A 104      60.369 -12.805  45.435  1.00102.73           C  
ANISOU  774  CG  ARG A 104    11965  13227  13840   1944    921    357       C  
ATOM    775  CD  ARG A 104      61.698 -12.809  44.706  1.00111.11           C  
ANISOU  775  CD  ARG A 104    12938  14286  14993   2071    995    337       C  
ATOM    776  NE  ARG A 104      61.848 -11.636  43.852  1.00114.18           N  
ANISOU  776  NE  ARG A 104    13304  14758  15322   2074   1115    281       N  
ATOM    777  CZ  ARG A 104      62.479 -10.525  44.215  1.00120.80           C  
ANISOU  777  CZ  ARG A 104    14053  15693  16152   2029   1148    313       C  
ATOM    778  NH1 ARG A 104      63.028 -10.436  45.418  1.00132.42           N1+
ANISOU  778  NH1 ARG A 104    15440  17201  17672   1979   1067    396       N1+
ATOM    779  NH2 ARG A 104      62.564  -9.504  43.373  1.00115.16           N  
ANISOU  779  NH2 ARG A 104    13345  15035  15375   2025   1256    264       N  
ATOM    780  N   LEU A 105      55.706 -13.402  44.131  1.00 98.66           N  
ANISOU  780  N   LEU A 105    11781  12659  13045   1774    911    122       N  
ATOM    781  CA  LEU A 105      54.550 -13.283  43.247  1.00 91.88           C  
ANISOU  781  CA  LEU A 105    10992  11809  12110   1770    935     19       C  
ATOM    782  C   LEU A 105      54.916 -13.285  41.765  1.00 91.45           C  
ANISOU  782  C   LEU A 105    10975  11718  12052   1895   1013    -48       C  
ATOM    783  O   LEU A 105      54.264 -12.630  40.955  1.00 81.89           O  
ANISOU  783  O   LEU A 105     9803  10548  10766   1907   1044   -121       O  
ATOM    784  CB  LEU A 105      53.720 -12.044  43.594  1.00 84.84           C  
ANISOU  784  CB  LEU A 105    10071  11028  11137   1689    933    -11       C  
ATOM    785  CG  LEU A 105      53.136 -11.980  45.005  1.00 85.03           C  
ANISOU  785  CG  LEU A 105    10064  11104  11141   1546    870     26       C  
ATOM    786  CD1 LEU A 105      52.067 -10.910  45.080  1.00 86.36           C  
ANISOU  786  CD1 LEU A 105    10211  11369  11232   1485    873    -48       C  
ATOM    787  CD2 LEU A 105      52.576 -13.331  45.422  1.00 88.96           C  
ANISOU  787  CD2 LEU A 105    10624  11527  11651   1478    813     32       C  
ATOM    788  N   GLY A 106      55.967 -14.019  41.418  1.00 93.20           N  
ANISOU  788  N   GLY A 106    11188  11866  12356   1989   1041    -28       N  
ATOM    789  CA  GLY A 106      56.355 -14.178  40.029  1.00 96.15           C  
ANISOU  789  CA  GLY A 106    11602  12203  12726   2100   1125   -101       C  
ATOM    790  C   GLY A 106      57.266 -13.084  39.508  1.00 96.13           C  
ANISOU  790  C   GLY A 106    11542  12272  12710   2147   1217    -97       C  
ATOM    791  O   GLY A 106      57.790 -13.184  38.400  1.00109.44           O  
ANISOU  791  O   GLY A 106    13253  13936  14393   2232   1303   -152       O  
ATOM    792  N   VAL A 107      57.454 -12.038  40.305  1.00 85.50           N  
ANISOU  792  N   VAL A 107    10125  11011  11350   2083   1206    -36       N  
ATOM    793  CA  VAL A 107      58.325 -10.932  39.923  1.00 85.14           C  
ANISOU  793  CA  VAL A 107    10028  11034  11289   2105   1291    -25       C  
ATOM    794  C   VAL A 107      59.772 -11.396  39.801  1.00 95.05           C  
ANISOU  794  C   VAL A 107    11198  12267  12648   2184   1348     -5       C  
ATOM    795  O   VAL A 107      60.325 -11.981  40.730  1.00103.10           O  
ANISOU  795  O   VAL A 107    12144  13265  13764   2186   1288     56       O  
ATOM    796  CB  VAL A 107      58.236  -9.776  40.935  1.00 79.50           C  
ANISOU  796  CB  VAL A 107     9254  10406  10547   2011   1258     35       C  
ATOM    797  CG1 VAL A 107      59.182  -8.655  40.545  1.00 74.86           C  
ANISOU  797  CG1 VAL A 107     8621   9879   9945   2021   1349     48       C  
ATOM    798  CG2 VAL A 107      56.812  -9.265  41.022  1.00 74.51           C  
ANISOU  798  CG2 VAL A 107     8689   9800   9821   1945   1207     -5       C  
ATOM    799  N   ALA A 108      60.377 -11.136  38.647  1.00102.63           N  
ANISOU  799  N   ALA A 108    12172  13237  13588   2247   1461    -61       N  
ATOM    800  CA  ALA A 108      61.730 -11.604  38.366  1.00106.25           C  
ANISOU  800  CA  ALA A 108    12539  13683  14149   2331   1533    -72       C  
ATOM    801  C   ALA A 108      62.796 -10.682  38.943  1.00 98.26           C  
ANISOU  801  C   ALA A 108    11396  12760  13177   2296   1569    -14       C  
ATOM    802  O   ALA A 108      62.556  -9.495  39.158  1.00 92.46           O  
ANISOU  802  O   ALA A 108    10670  12095  12364   2214   1579     16       O  
ATOM    803  CB  ALA A 108      61.931 -11.773  36.866  1.00103.52           C  
ANISOU  803  CB  ALA A 108    12261  13316  13756   2400   1654   -170       C  
ATOM    804  N   THR A 109      63.976 -11.241  39.187  1.00 98.46           N  
ANISOU  804  N   THR A 109    11298  12780  13331   2364   1584     -6       N  
ATOM    805  CA  THR A 109      65.094 -10.485  39.737  1.00104.90           C  
ANISOU  805  CA  THR A 109    11969  13685  14203   2335   1615     38       C  
ATOM    806  C   THR A 109      66.013  -9.982  38.631  1.00105.21           C  
ANISOU  806  C   THR A 109    11966  13780  14230   2363   1781    -34       C  
ATOM    807  O   THR A 109      66.620 -10.778  37.914  1.00111.31           O  
ANISOU  807  O   THR A 109    12705  14518  15070   2461   1849   -108       O  
ATOM    808  CB  THR A 109      65.912 -11.346  40.710  1.00113.45           C  
ANISOU  808  CB  THR A 109    12922  14741  15442   2392   1522     88       C  
ATOM    809  CG2 THR A 109      67.004 -10.518  41.374  1.00114.90           C  
ANISOU  809  CG2 THR A 109    12948  15030  15680   2350   1536    135       C  
ATOM    810  OG1 THR A 109      65.044 -11.886  41.713  1.00114.49           O  
ANISOU  810  OG1 THR A 109    13116  14815  15570   2351   1373    157       O  
ATOM    811  N   PRO A 110      66.115  -8.653  38.489  1.00 94.32           N  
ANISOU  811  N   PRO A 110    10594  12483  12759   2270   1849    -18       N  
ATOM    812  CA  PRO A 110      66.930  -8.004  37.456  1.00 94.13           C  
ANISOU  812  CA  PRO A 110    10552  12519  12694   2259   2015    -78       C  
ATOM    813  C   PRO A 110      68.419  -8.222  37.677  1.00105.90           C  
ANISOU  813  C   PRO A 110    11844  14069  14325   2300   2075    -98       C  
ATOM    814  O   PRO A 110      68.810  -8.914  38.616  1.00110.16           O  
ANISOU  814  O   PRO A 110    12265  14592  14997   2351   1972    -60       O  
ATOM    815  CB  PRO A 110      66.604  -6.517  37.637  1.00 92.58           C  
ANISOU  815  CB  PRO A 110    10414  12382  12380   2133   2028    -28       C  
ATOM    816  CG  PRO A 110      65.315  -6.487  38.372  1.00 97.47           C  
ANISOU  816  CG  PRO A 110    11123  12959  12953   2101   1885     25       C  
ATOM    817  CD  PRO A 110      65.352  -7.672  39.276  1.00 91.34           C  
ANISOU  817  CD  PRO A 110    10265  12139  12301   2161   1772     54       C  
ATOM    818  N   GLU A 111      69.237  -7.631  36.813  1.00116.93           N  
ANISOU  818  N   GLU A 111    13204  15534  15689   2272   2239   -158       N  
ATOM    819  CA  GLU A 111      70.680  -7.674  36.988  1.00125.01           C  
ANISOU  819  CA  GLU A 111    14018  16638  16842   2294   2311   -191       C  
ATOM    820  C   GLU A 111      71.036  -6.930  38.263  1.00121.92           C  
ANISOU  820  C   GLU A 111    13514  16315  16496   2210   2222    -97       C  
ATOM    821  O   GLU A 111      70.804  -5.726  38.371  1.00128.89           O  
ANISOU  821  O   GLU A 111    14457  17243  17270   2086   2248    -53       O  
ATOM    822  CB  GLU A 111      71.389  -7.037  35.795  1.00132.44           C  
ANISOU  822  CB  GLU A 111    14960  17652  17711   2243   2520   -277       C  
ATOM    823  CG  GLU A 111      72.905  -7.124  35.857  1.00139.73           C  
ANISOU  823  CG  GLU A 111    15646  18671  18773   2265   2616   -339       C  
ATOM    824  CD  GLU A 111      73.573  -6.368  34.726  1.00147.29           C  
ANISOU  824  CD  GLU A 111    16612  19713  19637   2177   2837   -422       C  
ATOM    825  OE1 GLU A 111      72.903  -5.519  34.102  1.00150.44           O  
ANISOU  825  OE1 GLU A 111    17207  20100  19854   2075   2893   -398       O  
ATOM    826  OE2 GLU A 111      74.766  -6.624  34.458  1.00145.55           O1-
ANISOU  826  OE2 GLU A 111    16206  19572  19525   2209   2953   -513       O1-
ATOM    827  N   LYS A 112      71.590  -7.657  39.226  1.00111.99           N  
ANISOU  827  N   LYS A 112    12102  15055  15395   2280   2110    -67       N  
ATOM    828  CA  LYS A 112      71.898  -7.096  40.535  1.00113.42           C  
ANISOU  828  CA  LYS A 112    12178  15296  15620   2205   2002     25       C  
ATOM    829  C   LYS A 112      72.836  -5.899  40.439  1.00110.05           C  
ANISOU  829  C   LYS A 112    11646  14994  15175   2095   2120     10       C  
ATOM    830  O   LYS A 112      74.052  -6.053  40.339  1.00112.94           O  
ANISOU  830  O   LYS A 112    11823  15433  15655   2129   2187    -46       O  
ATOM    831  CB  LYS A 112      72.497  -8.167  41.446  1.00125.12           C  
ANISOU  831  CB  LYS A 112    13510  16754  17278   2313   1863     51       C  
ATOM    832  CG  LYS A 112      72.664  -7.721  42.886  1.00128.47           C  
ANISOU  832  CG  LYS A 112    13853  17227  17734   2236   1721    156       C  
ATOM    833  CD  LYS A 112      73.097  -8.874  43.775  1.00139.47           C  
ANISOU  833  CD  LYS A 112    15139  18570  19282   2347   1556    195       C  
ATOM    834  CE  LYS A 112      73.155  -8.446  45.232  1.00139.79           C  
ANISOU  834  CE  LYS A 112    15129  18658  19328   2257   1402    307       C  
ATOM    835  NZ  LYS A 112      73.479  -9.580  46.141  1.00143.81           N1+
ANISOU  835  NZ  LYS A 112    15569  19103  19968   2358   1218    362       N1+
ATOM    836  N   GLN A 113      72.252  -4.706  40.465  1.00111.48           N  
ANISOU  836  N   GLN A 113    11947  15195  15214   1962   2144     55       N  
ATOM    837  CA  GLN A 113      73.019  -3.471  40.399  1.00118.25           C  
ANISOU  837  CA  GLN A 113    12740  16155  16033   1833   2252     50       C  
ATOM    838  C   GLN A 113      73.485  -3.053  41.788  1.00117.52           C  
ANISOU  838  C   GLN A 113    12510  16129  16014   1767   2137    124       C  
ATOM    839  O   GLN A 113      73.431  -3.833  42.738  1.00119.01           O  
ANISOU  839  O   GLN A 113    12627  16293  16298   1835   1983    171       O  
ATOM    840  CB  GLN A 113      72.168  -2.351  39.798  1.00125.42           C  
ANISOU  840  CB  GLN A 113    13861  17038  16756   1723   2317     66       C  
ATOM    841  CG  GLN A 113      71.696  -2.599  38.376  1.00135.96           C  
ANISOU  841  CG  GLN A 113    15353  18314  17990   1766   2430     -2       C  
ATOM    842  CD  GLN A 113      72.606  -1.968  37.341  1.00145.05           C  
ANISOU  842  CD  GLN A 113    16487  19535  19089   1692   2632    -71       C  
ATOM    843  NE2 GLN A 113      72.013  -1.440  36.278  1.00152.53           N  
ANISOU  843  NE2 GLN A 113    17641  20440  19873   1644   2720    -89       N  
ATOM    844  OE1 GLN A 113      73.826  -1.947  37.499  1.00143.01           O  
ANISOU  844  OE1 GLN A 113    16033  19370  18933   1671   2707   -109       O  
ATOM    845  N   THR A 114      73.946  -1.813  41.891  1.00110.62           N  
ANISOU  845  N   THR A 114    11611  15335  15086   1626   2209    135       N  
ATOM    846  CA  THR A 114      74.274  -1.212  43.176  1.00100.34           C  
ANISOU  846  CA  THR A 114    10208  14096  13820   1535   2106    203       C  
ATOM    847  C   THR A 114      73.898   0.261  43.134  1.00104.34           C  
ANISOU  847  C   THR A 114    10843  14616  14185   1374   2163    231       C  
ATOM    848  O   THR A 114      74.618   1.082  42.567  1.00100.18           O  
ANISOU  848  O   THR A 114    10288  14150  13624   1278   2305    192       O  
ATOM    849  CB  THR A 114      75.766  -1.356  43.521  1.00 97.45           C  
ANISOU  849  CB  THR A 114     9581  13844  13604   1539   2129    167       C  
ATOM    850  CG2 THR A 114      76.085  -0.626  44.817  1.00 77.84           C  
ANISOU  850  CG2 THR A 114     7007  11430  11138   1427   2023    237       C  
ATOM    851  OG1 THR A 114      76.090  -2.743  43.673  1.00110.25           O  
ANISOU  851  OG1 THR A 114    11084  15437  15370   1705   2046    146       O  
ATOM    852  N   ILE A 115      72.758   0.591  43.730  1.00107.41           N  
ANISOU  852  N   ILE A 115    11378  14943  14491   1342   2054    293       N  
ATOM    853  CA  ILE A 115      72.215   1.939  43.639  1.00 99.67           C  
ANISOU  853  CA  ILE A 115    10548  13947  13376   1213   2092    313       C  
ATOM    854  C   ILE A 115      72.352   2.709  44.949  1.00 95.46           C  
ANISOU  854  C   ILE A 115     9954  13465  12852   1101   1999    368       C  
ATOM    855  O   ILE A 115      72.286   2.130  46.030  1.00 96.99           O  
ANISOU  855  O   ILE A 115    10062  13675  13115   1131   1861    410       O  
ATOM    856  CB  ILE A 115      70.728   1.912  43.224  1.00 97.23           C  
ANISOU  856  CB  ILE A 115    10460  13528  12954   1257   2050    321       C  
ATOM    857  CG1 ILE A 115      70.492   0.849  42.146  1.00 90.43           C  
ANISOU  857  CG1 ILE A 115     9648  12613  12099   1386   2100    270       C  
ATOM    858  CG2 ILE A 115      70.280   3.281  42.743  1.00 95.58           C  
ANISOU  858  CG2 ILE A 115    10421  13288  12608   1151   2115    323       C  
ATOM    859  CD1 ILE A 115      69.102   0.884  41.548  1.00 85.17           C  
ANISOU  859  CD1 ILE A 115     9195  11849  11315   1423   2072    264       C  
ATOM    860  N   VAL A 116      72.548   4.018  44.839  1.00 86.18           N  
ANISOU  860  N   VAL A 116     8836  12311  11599    965   2074    368       N  
ATOM    861  CA  VAL A 116      72.609   4.893  46.001  1.00 82.70           C  
ANISOU  861  CA  VAL A 116     8365  11910  11149    844   1998    410       C  
ATOM    862  C   VAL A 116      71.463   5.897  45.974  1.00 95.35           C  
ANISOU  862  C   VAL A 116    10181  13429  12620    784   1981    424       C  
ATOM    863  O   VAL A 116      71.304   6.641  45.010  1.00 93.38           O  
ANISOU  863  O   VAL A 116    10072  13129  12279    744   2085    402       O  
ATOM    864  CB  VAL A 116      73.939   5.660  46.053  1.00 83.40           C  
ANISOU  864  CB  VAL A 116     8317  12098  11274    718   2093    391       C  
ATOM    865  CG1 VAL A 116      73.878   6.763  47.095  1.00 90.90           C  
ANISOU  865  CG1 VAL A 116     9282  13071  12184    575   2031    426       C  
ATOM    866  CG2 VAL A 116      75.084   4.709  46.339  1.00 86.99           C  
ANISOU  866  CG2 VAL A 116     8524  12649  11880    782   2076    372       C  
ATOM    867  N   VAL A 117      70.666   5.915  47.035  1.00 95.48           N  
ANISOU  867  N   VAL A 117    10225  13429  12626    777   1848    456       N  
ATOM    868  CA  VAL A 117      69.533   6.828  47.109  1.00 81.74           C  
ANISOU  868  CA  VAL A 117     8667  11613  10779    735   1819    454       C  
ATOM    869  C   VAL A 117      69.771   7.955  48.110  1.00 78.28           C  
ANISOU  869  C   VAL A 117     8209  11212  10321    592   1788    468       C  
ATOM    870  O   VAL A 117      70.053   7.710  49.281  1.00 94.93           O  
ANISOU  870  O   VAL A 117    10195  13389  12484    554   1698    493       O  
ATOM    871  CB  VAL A 117      68.245   6.086  47.478  1.00 73.92           C  
ANISOU  871  CB  VAL A 117     7743  10570   9774    827   1706    457       C  
ATOM    872  CG1 VAL A 117      67.055   7.021  47.375  1.00 82.32           C  
ANISOU  872  CG1 VAL A 117     8986  11556  10736    804   1685    434       C  
ATOM    873  CG2 VAL A 117      68.061   4.886  46.571  1.00 62.79           C  
ANISOU  873  CG2 VAL A 117     6342   9124   8390    963   1728    441       C  
ATOM    874  N   ASP A 118      69.648   9.191  47.638  1.00 79.11           N  
ANISOU  874  N   ASP A 118     8449  11265  10344    509   1857    452       N  
ATOM    875  CA  ASP A 118      69.865  10.360  48.477  1.00 78.98           C  
ANISOU  875  CA  ASP A 118     8437  11267  10303    367   1839    456       C  
ATOM    876  C   ASP A 118      68.533  10.970  48.876  1.00 95.44           C  
ANISOU  876  C   ASP A 118    10676  13268  12317    374   1761    438       C  
ATOM    877  O   ASP A 118      67.874  11.614  48.067  1.00 95.27           O  
ANISOU  877  O   ASP A 118    10832  13147  12221    396   1795    419       O  
ATOM    878  CB  ASP A 118      70.706  11.397  47.730  1.00 81.84           C  
ANISOU  878  CB  ASP A 118     8849  11620  10625    253   1971    447       C  
ATOM    879  CG  ASP A 118      71.215  12.510  48.635  1.00 98.55           C  
ANISOU  879  CG  ASP A 118    10936  13773  12737     90   1962    448       C  
ATOM    880  OD1 ASP A 118      70.415  13.091  49.399  1.00111.80           O  
ANISOU  880  OD1 ASP A 118    12695  15407  14377     63   1878    441       O  
ATOM    881  OD2 ASP A 118      72.428  12.802  48.583  1.00106.78           O1-
ANISOU  881  OD2 ASP A 118    11867  14892  13814    -15   2041    447       O1-
ATOM    882  N   TYR A 119      68.143  10.782  50.131  1.00101.71           N  
ANISOU  882  N   TYR A 119    11405  14107  13134    355   1654    441       N  
ATOM    883  CA  TYR A 119      66.873  11.318  50.607  1.00 90.72           C  
ANISOU  883  CA  TYR A 119    10134  12652  11684    360   1584    406       C  
ATOM    884  C   TYR A 119      66.932  11.931  52.001  1.00 86.39           C  
ANISOU  884  C   TYR A 119     9532  12158  11134    241   1520    397       C  
ATOM    885  O   TYR A 119      67.991  11.993  52.622  1.00 90.19           O  
ANISOU  885  O   TYR A 119     9886  12726  11655    146   1522    424       O  
ATOM    886  CB  TYR A 119      65.737  10.284  50.505  1.00 82.80           C  
ANISOU  886  CB  TYR A 119     9158  11622  10681    491   1517    392       C  
ATOM    887  CG  TYR A 119      65.920   8.974  51.259  1.00 80.57           C  
ANISOU  887  CG  TYR A 119     8732  11420  10461    523   1446    426       C  
ATOM    888  CD1 TYR A 119      67.091   8.229  51.156  1.00 75.84           C  
ANISOU  888  CD1 TYR A 119     7997  10884   9935    533   1470    471       C  
ATOM    889  CD2 TYR A 119      64.897   8.470  52.053  1.00 85.56           C  
ANISOU  889  CD2 TYR A 119     9370  12058  11079    544   1355    410       C  
ATOM    890  CE1 TYR A 119      67.240   7.036  51.834  1.00 86.28           C  
ANISOU  890  CE1 TYR A 119     9206  12260  11316    572   1388    507       C  
ATOM    891  CE2 TYR A 119      65.038   7.280  52.732  1.00 79.90           C  
ANISOU  891  CE2 TYR A 119     8550  11399  10408    563   1285    450       C  
ATOM    892  CZ  TYR A 119      66.209   6.567  52.619  1.00 87.81           C  
ANISOU  892  CZ  TYR A 119     9432  12448  11482    583   1294    503       C  
ATOM    893  OH  TYR A 119      66.348   5.379  53.297  1.00 96.47           O  
ANISOU  893  OH  TYR A 119    10442  13584  12627    611   1208    548       O  
ATOM    894  N   SER A 120      65.775  12.397  52.464  1.00 95.18           N  
ANISOU  894  N   SER A 120    10740  13222  12201    248   1464    348       N  
ATOM    895  CA  SER A 120      65.631  13.052  53.762  1.00 99.32           C  
ANISOU  895  CA  SER A 120    11240  13788  12708    136   1409    319       C  
ATOM    896  C   SER A 120      66.486  14.313  53.875  1.00 92.40           C  
ANISOU  896  C   SER A 120    10385  12903  11818      2   1463    316       C  
ATOM    897  O   SER A 120      66.009  15.418  53.621  1.00 96.40           O  
ANISOU  897  O   SER A 120    11033  13316  12280    -21   1484    270       O  
ATOM    898  CB  SER A 120      65.943  12.081  54.902  1.00 97.76           C  
ANISOU  898  CB  SER A 120    10891  13708  12547    103   1333    356       C  
ATOM    899  OG  SER A 120      65.230  12.427  56.075  1.00 99.15           O  
ANISOU  899  OG  SER A 120    11079  13911  12682     34   1267    310       O  
ATOM    900  N   ALA A 121      67.744  14.132  54.265  1.00 85.71           N  
ANISOU  900  N   ALA A 121     9399  12154  11014    -86   1478    360       N  
ATOM    901  CA  ALA A 121      68.702  15.233  54.402  1.00 96.40           C  
ANISOU  901  CA  ALA A 121    10748  13520  12362   -234   1533    357       C  
ATOM    902  C   ALA A 121      68.242  16.357  55.332  1.00104.72           C  
ANISOU  902  C   ALA A 121    11876  14545  13367   -340   1496    302       C  
ATOM    903  O   ALA A 121      67.918  17.452  54.872  1.00108.65           O  
ANISOU  903  O   ALA A 121    12527  14931  13822   -366   1538    264       O  
ATOM    904  CB  ALA A 121      69.065  15.795  53.033  1.00101.55           C  
ANISOU  904  CB  ALA A 121    11506  14085  12994   -227   1645    363       C  
ATOM    905  N   PRO A 122      68.210  16.089  56.646  1.00102.38           N  
ANISOU  905  N   PRO A 122    11483  14343  13074   -402   1413    295       N  
ATOM    906  CA  PRO A 122      67.839  17.118  57.620  1.00 94.51           C  
ANISOU  906  CA  PRO A 122    10544  13334  12031   -513   1382    231       C  
ATOM    907  C   PRO A 122      69.042  17.954  58.036  1.00 91.60           C  
ANISOU  907  C   PRO A 122    10121  13014  11667   -684   1412    237       C  
ATOM    908  O   PRO A 122      70.154  17.709  57.571  1.00104.19           O  
ANISOU  908  O   PRO A 122    11620  14661  13306   -714   1458    289       O  
ATOM    909  CB  PRO A 122      67.351  16.294  58.806  1.00104.42           C  
ANISOU  909  CB  PRO A 122    11713  14686  13277   -514   1285    227       C  
ATOM    910  CG  PRO A 122      68.182  15.062  58.746  1.00 99.53           C  
ANISOU  910  CG  PRO A 122    10943  14161  12714   -476   1257    313       C  
ATOM    911  CD  PRO A 122      68.405  14.776  57.286  1.00 99.47           C  
ANISOU  911  CD  PRO A 122    10965  14086  12744   -364   1337    343       C  
ATOM    912  N   ASN A 123      68.815  18.928  58.909  1.00 94.58           N  
ANISOU  912  N   ASN A 123    10553  13380  12004   -798   1389    175       N  
ATOM    913  CA  ASN A 123      69.888  19.788  59.389  1.00108.10           C  
ANISOU  913  CA  ASN A 123    12223  15136  13715   -976   1412    170       C  
ATOM    914  C   ASN A 123      70.283  19.493  60.830  1.00112.26           C  
ANISOU  914  C   ASN A 123    12614  15807  14233  -1086   1323    171       C  
ATOM    915  O   ASN A 123      69.581  18.779  61.542  1.00118.48           O  
ANISOU  915  O   ASN A 123    13373  16643  14999  -1037   1247    166       O  
ATOM    916  CB  ASN A 123      69.504  21.258  59.232  1.00118.55           C  
ANISOU  916  CB  ASN A 123    13727  16322  14994  -1045   1458     98       C  
ATOM    917  CG  ASN A 123      69.720  21.763  57.825  1.00125.70           C  
ANISOU  917  CG  ASN A 123    14756  17103  15902  -1011   1553    122       C  
ATOM    918  ND2 ASN A 123      69.452  23.043  57.609  1.00129.58           N  
ANISOU  918  ND2 ASN A 123    15424  17456  16356  -1070   1586     70       N  
ATOM    919  OD1 ASN A 123      70.123  21.010  56.940  1.00130.48           O  
ANISOU  919  OD1 ASN A 123    15307  17731  16538   -936   1595    183       O  
ATOM    920  N   VAL A 124      71.412  20.050  61.252  1.00107.55           N  
ANISOU  920  N   VAL A 124    11939  15280  13647  -1244   1332    177       N  
ATOM    921  CA  VAL A 124      71.953  19.788  62.579  1.00115.54           C  
ANISOU  921  CA  VAL A 124    12817  16437  14648  -1360   1238    185       C  
ATOM    922  C   VAL A 124      71.626  20.918  63.553  1.00121.79           C  
ANISOU  922  C   VAL A 124    13697  17209  15370  -1505   1222     98       C  
ATOM    923  O   VAL A 124      71.646  22.088  63.176  1.00123.49           O  
ANISOU  923  O   VAL A 124    14030  17319  15570  -1573   1294     45       O  
ATOM    924  CB  VAL A 124      73.479  19.540  62.505  1.00117.27           C  
ANISOU  924  CB  VAL A 124    12855  16771  14931  -1439   1240    242       C  
ATOM    925  CG1 VAL A 124      74.164  19.849  63.829  1.00121.06           C  
ANISOU  925  CG1 VAL A 124    13235  17375  15387  -1613   1155    227       C  
ATOM    926  CG2 VAL A 124      73.752  18.112  62.075  1.00115.96           C  
ANISOU  926  CG2 VAL A 124    12557  16668  14833  -1293   1205    320       C  
ATOM    927  N   ALA A 125      71.306  20.547  64.793  1.00122.95           N  
ANISOU  927  N   ALA A 125    13798  17448  15468  -1554   1127     82       N  
ATOM    928  CA  ALA A 125      70.966  21.487  65.862  1.00122.06           C  
ANISOU  928  CA  ALA A 125    13757  17338  15281  -1695   1105    -10       C  
ATOM    929  C   ALA A 125      69.673  22.230  65.570  1.00118.28           C  
ANISOU  929  C   ALA A 125    13460  16710  14770  -1628   1159   -110       C  
ATOM    930  O   ALA A 125      69.466  23.353  66.026  1.00122.34           O  
ANISOU  930  O   ALA A 125    14071  17169  15246  -1730   1180   -204       O  
ATOM    931  CB  ALA A 125      72.107  22.463  66.129  1.00126.12           C  
ANISOU  931  CB  ALA A 125    14237  17883  15799  -1880   1125    -28       C  
ATOM    932  N   LYS A 126      68.805  21.584  64.804  1.00113.11           N  
ANISOU  932  N   LYS A 126    12849  15989  14137  -1450   1175    -94       N  
ATOM    933  CA  LYS A 126      67.495  22.135  64.514  1.00108.57           C  
ANISOU  933  CA  LYS A 126    12426  15283  13542  -1358   1207   -191       C  
ATOM    934  C   LYS A 126      66.460  21.022  64.450  1.00 99.52           C  
ANISOU  934  C   LYS A 126    11260  14160  12393  -1211   1174   -184       C  
ATOM    935  O   LYS A 126      66.699  19.975  63.850  1.00 96.09           O  
ANISOU  935  O   LYS A 126    10755  13758  11997  -1114   1163    -90       O  
ATOM    936  CB  LYS A 126      67.523  22.905  63.198  1.00107.53           C  
ANISOU  936  CB  LYS A 126    12420  14988  13448  -1291   1286   -192       C  
ATOM    937  CG  LYS A 126      66.601  24.103  63.184  1.00118.45           C  
ANISOU  937  CG  LYS A 126    13975  16221  14808  -1278   1309   -313       C  
ATOM    938  CD  LYS A 126      66.611  24.793  61.835  1.00134.91           C  
ANISOU  938  CD  LYS A 126    16206  18132  16921  -1205   1370   -296       C  
ATOM    939  CE  LYS A 126      66.016  23.896  60.765  1.00145.55           C  
ANISOU  939  CE  LYS A 126    17564  19441  18296  -1011   1374   -243       C  
ATOM    940  NZ  LYS A 126      65.174  24.650  59.793  1.00147.00           N1+
ANISOU  940  NZ  LYS A 126    17939  19432  18484   -892   1393   -291       N1+
ATOM    941  N   GLU A 127      65.315  21.254  65.083  1.00101.88           N  
ANISOU  941  N   GLU A 127    11619  14445  12646  -1201   1160   -292       N  
ATOM    942  CA  GLU A 127      64.223  20.292  65.073  1.00108.64           C  
ANISOU  942  CA  GLU A 127    12461  15323  13493  -1080   1137   -307       C  
ATOM    943  C   GLU A 127      63.755  20.101  63.636  1.00106.75           C  
ANISOU  943  C   GLU A 127    12286  14962  13311   -897   1174   -284       C  
ATOM    944  O   GLU A 127      63.530  21.077  62.921  1.00109.57           O  
ANISOU  944  O   GLU A 127    12759  15183  13689   -851   1216   -334       O  
ATOM    945  CB  GLU A 127      63.072  20.794  65.946  1.00117.94           C  
ANISOU  945  CB  GLU A 127    13693  16502  14616  -1113   1136   -457       C  
ATOM    946  CG  GLU A 127      62.131  19.705  66.432  1.00130.11           C  
ANISOU  946  CG  GLU A 127    15184  18130  16121  -1070   1105   -475       C  
ATOM    947  CD  GLU A 127      62.690  18.946  67.618  1.00135.14           C  
ANISOU  947  CD  GLU A 127    15728  18928  16690  -1215   1045   -411       C  
ATOM    948  OE1 GLU A 127      63.684  19.418  68.209  1.00126.43           O  
ANISOU  948  OE1 GLU A 127    14598  17876  15565  -1354   1024   -382       O  
ATOM    949  OE2 GLU A 127      62.136  17.880  67.962  1.00143.64           O1-
ANISOU  949  OE2 GLU A 127    16766  20078  17733  -1195   1013   -387       O1-
ATOM    950  N   MET A 128      63.623  18.846  63.214  1.00100.88           N  
ANISOU  950  N   MET A 128    11480  14261  12590   -795   1153   -205       N  
ATOM    951  CA  MET A 128      63.312  18.540  61.819  1.00 95.46           C  
ANISOU  951  CA  MET A 128    10845  13474  11953   -629   1185   -170       C  
ATOM    952  C   MET A 128      62.001  19.163  61.363  1.00 91.08           C  
ANISOU  952  C   MET A 128    10410  12800  11397   -520   1200   -286       C  
ATOM    953  O   MET A 128      60.941  18.912  61.934  1.00 76.08           O  
ANISOU  953  O   MET A 128     8500  10933   9474   -495   1176   -372       O  
ATOM    954  CB  MET A 128      63.299  17.030  61.561  1.00 98.54           C  
ANISOU  954  CB  MET A 128    11148  13931  12363   -544   1153    -82       C  
ATOM    955  CG  MET A 128      63.073  16.675  60.094  1.00 91.74           C  
ANISOU  955  CG  MET A 128    10338  12972  11546   -381   1189    -45       C  
ATOM    956  SD  MET A 128      62.892  14.910  59.781  1.00118.15           S  
ANISOU  956  SD  MET A 128    13598  16378  14916   -273   1153     37       S  
ATOM    957  CE  MET A 128      64.560  14.338  60.053  1.00 61.51           C  
ANISOU  957  CE  MET A 128     6290   9303   7779   -355   1136    162       C  
ATOM    958  N   HIS A 129      62.092  19.979  60.322  1.00117.48           N  
ANISOU  958  N   HIS A 129    13867  16005  14765   -459   1238   -288       N  
ATOM    959  CA  HIS A 129      60.946  20.712  59.813  1.00126.38           C  
ANISOU  959  CA  HIS A 129    15122  16999  15900   -346   1236   -394       C  
ATOM    960  C   HIS A 129      60.161  19.894  58.789  1.00110.92           C  
ANISOU  960  C   HIS A 129    13181  15000  13965   -169   1222   -376       C  
ATOM    961  O   HIS A 129      60.662  18.910  58.245  1.00 95.75           O  
ANISOU  961  O   HIS A 129    11202  13124  12056   -133   1231   -271       O  
ATOM    962  CB  HIS A 129      61.389  22.065  59.243  1.00147.08           C  
ANISOU  962  CB  HIS A 129    17885  19474  18525   -376   1268   -405       C  
ATOM    963  CG  HIS A 129      62.716  22.033  58.555  1.00151.58           C  
ANISOU  963  CG  HIS A 129    18452  20039  19101   -438   1316   -279       C  
ATOM    964  CD2 HIS A 129      63.056  22.249  57.260  1.00152.62           C  
ANISOU  964  CD2 HIS A 129    18685  20062  19240   -379   1355   -214       C  
ATOM    965  ND1 HIS A 129      63.901  21.771  59.216  1.00140.33           N  
ANISOU  965  ND1 HIS A 129    16907  18739  17673   -587   1330   -213       N  
ATOM    966  CE1 HIS A 129      64.902  21.811  58.358  1.00138.31           C  
ANISOU  966  CE1 HIS A 129    16661  18458  17431   -612   1382   -122       C  
ATOM    967  NE2 HIS A 129      64.417  22.104  57.166  1.00150.55           N  
ANISOU  967  NE2 HIS A 129    18351  19868  18982   -495   1405   -120       N  
ATOM    968  N   VAL A 130      58.925  20.307  58.537  1.00106.12           N  
ANISOU  968  N   VAL A 130    12649  14307  13366    -56   1197   -487       N  
ATOM    969  CA  VAL A 130      58.013  19.535  57.704  1.00102.61           C  
ANISOU  969  CA  VAL A 130    12211  13837  12940    107   1172   -494       C  
ATOM    970  C   VAL A 130      58.400  19.593  56.227  1.00 97.07           C  
ANISOU  970  C   VAL A 130    11614  13019  12248    202   1189   -405       C  
ATOM    971  O   VAL A 130      57.895  18.825  55.408  1.00 94.44           O  
ANISOU  971  O   VAL A 130    11285  12673  11924    326   1173   -383       O  
ATOM    972  CB  VAL A 130      56.565  20.032  57.884  1.00108.05           C  
ANISOU  972  CB  VAL A 130    12937  14474  13643    202   1133   -656       C  
ATOM    973  CG1 VAL A 130      56.319  21.258  57.023  1.00110.65           C  
ANISOU  973  CG1 VAL A 130    13434  14617  13992    293   1116   -698       C  
ATOM    974  CG2 VAL A 130      55.574  18.930  57.552  1.00114.44           C  
ANISOU  974  CG2 VAL A 130    13683  15333  14465    320   1105   -683       C  
ATOM    975  N   GLY A 131      59.311  20.499  55.892  1.00 87.37           N  
ANISOU  975  N   GLY A 131    10476  11711  11010    131   1225   -356       N  
ATOM    976  CA  GLY A 131      59.734  20.671  54.516  1.00 78.88           C  
ANISOU  976  CA  GLY A 131     9520  10526   9927    193   1252   -274       C  
ATOM    977  C   GLY A 131      60.663  19.576  54.027  1.00 89.90           C  
ANISOU  977  C   GLY A 131    10825  12009  11325    177   1299   -152       C  
ATOM    978  O   GLY A 131      61.123  19.611  52.886  1.00116.12           O  
ANISOU  978  O   GLY A 131    14230  15259  14630    211   1339    -82       O  
ATOM    979  N   HIS A 132      60.945  18.605  54.891  1.00 75.76           N  
ANISOU  979  N   HIS A 132     8867  10369   9549    123   1293   -128       N  
ATOM    980  CA  HIS A 132      61.825  17.494  54.550  1.00 86.83           C  
ANISOU  980  CA  HIS A 132    10166  11857  10968    118   1325    -23       C  
ATOM    981  C   HIS A 132      61.055  16.178  54.561  1.00 75.89           C  
ANISOU  981  C   HIS A 132     8704  10534   9597    222   1283    -26       C  
ATOM    982  O   HIS A 132      61.618  15.111  54.309  1.00 69.51           O  
ANISOU  982  O   HIS A 132     7809   9789   8810    241   1296     50       O  
ATOM    983  CB  HIS A 132      63.002  17.413  55.528  1.00100.45           C  
ANISOU  983  CB  HIS A 132    11762  13701  12704    -38   1340     25       C  
ATOM    984  CG  HIS A 132      63.989  18.531  55.388  1.00118.09           C  
ANISOU  984  CG  HIS A 132    14050  15889  14928   -156   1394     45       C  
ATOM    985  CD2 HIS A 132      63.890  19.741  54.789  1.00135.45           C  
ANISOU  985  CD2 HIS A 132    16413  17951  17102   -167   1424     15       C  
ATOM    986  ND1 HIS A 132      65.263  18.466  55.911  1.00114.78           N  
ANISOU  986  ND1 HIS A 132    13515  15570  14525   -290   1420    100       N  
ATOM    987  CE1 HIS A 132      65.907  19.587  55.639  1.00127.07           C  
ANISOU  987  CE1 HIS A 132    15154  17061  16067   -389   1473     99       C  
ATOM    988  NE2 HIS A 132      65.096  20.377  54.956  1.00137.83           N  
ANISOU  988  NE2 HIS A 132    16697  18272  17401   -319   1478     53       N  
ATOM    989  N   LEU A 133      59.765  16.263  54.861  1.00 73.64           N  
ANISOU  989  N   LEU A 133     8448  10227   9304    286   1234   -124       N  
ATOM    990  CA  LEU A 133      58.919  15.082  54.945  1.00 84.86           C  
ANISOU  990  CA  LEU A 133     9801  11706  10734    366   1196   -143       C  
ATOM    991  C   LEU A 133      58.796  14.404  53.585  1.00 92.15           C  
ANISOU  991  C   LEU A 133    10774  12573  11667    498   1206    -95       C  
ATOM    992  O   LEU A 133      58.840  13.178  53.482  1.00 96.31           O  
ANISOU  992  O   LEU A 133    11225  13159  12208    533   1200    -49       O  
ATOM    993  CB  LEU A 133      57.536  15.470  55.469  1.00 75.91           C  
ANISOU  993  CB  LEU A 133     8687  10562   9593    403   1151   -279       C  
ATOM    994  CG  LEU A 133      56.537  14.332  55.650  1.00 67.00           C  
ANISOU  994  CG  LEU A 133     7488   9500   8468    462   1117   -320       C  
ATOM    995  CD1 LEU A 133      57.132  13.290  56.564  1.00 58.65           C  
ANISOU  995  CD1 LEU A 133     6312   8571   7402    358   1116   -247       C  
ATOM    996  CD2 LEU A 133      55.230  14.856  56.214  1.00 62.02           C  
ANISOU  996  CD2 LEU A 133     6859   8870   7834    483   1086   -474       C  
ATOM    997  N   ARG A 134      58.654  15.217  52.543  1.00102.44           N  
ANISOU  997  N   ARG A 134    12216  13752  12955    567   1219   -106       N  
ATOM    998  CA  ARG A 134      58.471  14.715  51.187  1.00 91.70           C  
ANISOU  998  CA  ARG A 134    10929  12327  11586    688   1227    -70       C  
ATOM    999  C   ARG A 134      59.669  13.896  50.726  1.00 85.00           C  
ANISOU  999  C   ARG A 134    10020  11529  10749    660   1290     38       C  
ATOM   1000  O   ARG A 134      59.514  12.779  50.235  1.00 89.57           O  
ANISOU 1000  O   ARG A 134    10561  12134  11339    736   1288     63       O  
ATOM   1001  CB  ARG A 134      58.228  15.872  50.219  1.00 84.30           C  
ANISOU 1001  CB  ARG A 134    10174  11240  10616    743   1224    -90       C  
ATOM   1002  CG  ARG A 134      56.972  15.725  49.382  1.00 87.04           C  
ANISOU 1002  CG  ARG A 134    10608  11512  10953    900   1159   -151       C  
ATOM   1003  CD  ARG A 134      57.302  15.468  47.928  1.00 88.21           C  
ANISOU 1003  CD  ARG A 134    10866  11588  11061    969   1189    -80       C  
ATOM   1004  NE  ARG A 134      56.305  16.059  47.041  1.00 83.86           N  
ANISOU 1004  NE  ARG A 134    10473  10910  10479   1093   1118   -132       N  
ATOM   1005  CZ  ARG A 134      55.351  15.374  46.421  1.00100.69           C  
ANISOU 1005  CZ  ARG A 134    12615  13034  12608   1221   1059   -171       C  
ATOM   1006  NH1 ARG A 134      55.264  14.062  46.576  1.00 87.08           N1+
ANISOU 1006  NH1 ARG A 134    10761  11416  10909   1234   1073   -163       N1+
ATOM   1007  NH2 ARG A 134      54.487  16.003  45.637  1.00124.85           N  
ANISOU 1007  NH2 ARG A 134    15821  15976  15642   1334    979   -219       N  
ATOM   1008  N   SER A 135      60.861  14.457  50.890  1.00 79.72           N  
ANISOU 1008  N   SER A 135     9337  10873  10080    549   1347     92       N  
ATOM   1009  CA  SER A 135      62.089  13.790  50.475  1.00 74.52           C  
ANISOU 1009  CA  SER A 135     8603  10270   9442    517   1413    179       C  
ATOM   1010  C   SER A 135      62.281  12.452  51.179  1.00 83.17           C  
ANISOU 1010  C   SER A 135     9535  11482  10586    521   1383    209       C  
ATOM   1011  O   SER A 135      62.710  11.474  50.570  1.00 91.23           O  
ANISOU 1011  O   SER A 135    10507  12524  11631    579   1410    256       O  
ATOM   1012  CB  SER A 135      63.296  14.687  50.746  1.00 78.76           C  
ANISOU 1012  CB  SER A 135     9126  10820   9978    377   1473    214       C  
ATOM   1013  OG  SER A 135      64.507  13.973  50.575  1.00 87.75           O  
ANISOU 1013  OG  SER A 135    10144  12042  11154    340   1530    281       O  
ATOM   1014  N   THR A 136      61.957  12.421  52.467  1.00 90.08           N  
ANISOU 1014  N   THR A 136    10335  12424  11468    457   1326    180       N  
ATOM   1015  CA  THR A 136      62.172  11.239  53.291  1.00 86.43           C  
ANISOU 1015  CA  THR A 136     9736  12066  11039    437   1283    217       C  
ATOM   1016  C   THR A 136      61.271  10.086  52.869  1.00 83.91           C  
ANISOU 1016  C   THR A 136     9422  11734  10725    554   1250    206       C  
ATOM   1017  O   THR A 136      61.728   8.952  52.717  1.00 88.41           O  
ANISOU 1017  O   THR A 136     9920  12339  11331    590   1246    263       O  
ATOM   1018  CB  THR A 136      61.912  11.549  54.776  1.00 74.17           C  
ANISOU 1018  CB  THR A 136     8129  10583   9468    326   1229    182       C  
ATOM   1019  CG2 THR A 136      62.319  10.376  55.643  1.00 66.18           C  
ANISOU 1019  CG2 THR A 136     6993   9674   8480    288   1178    242       C  
ATOM   1020  OG1 THR A 136      62.662  12.707  55.162  1.00 76.54           O  
ANISOU 1020  OG1 THR A 136     8437  10887   9759    214   1258    180       O  
ATOM   1021  N   ILE A 137      59.989  10.384  52.683  1.00 79.26           N  
ANISOU 1021  N   ILE A 137     8916  11093  10106    612   1222    125       N  
ATOM   1022  CA  ILE A 137      59.002   9.363  52.346  1.00 77.14           C  
ANISOU 1022  CA  ILE A 137     8652  10818   9839    708   1187     96       C  
ATOM   1023  C   ILE A 137      59.258   8.728  50.985  1.00 89.68           C  
ANISOU 1023  C   ILE A 137    10284  12352  11440    817   1223    137       C  
ATOM   1024  O   ILE A 137      59.407   7.512  50.878  1.00 92.17           O  
ANISOU 1024  O   ILE A 137    10542  12694  11783    854   1214    176       O  
ATOM   1025  CB  ILE A 137      57.575   9.935  52.347  1.00 75.59           C  
ANISOU 1025  CB  ILE A 137     8524  10580   9615    754   1150    -16       C  
ATOM   1026  CG1 ILE A 137      57.216  10.469  53.733  1.00 85.47           C  
ANISOU 1026  CG1 ILE A 137     9727  11896  10853    646   1123    -77       C  
ATOM   1027  CG2 ILE A 137      56.581   8.869  51.917  1.00 70.57           C  
ANISOU 1027  CG2 ILE A 137     7887   9944   8983    846   1116    -50       C  
ATOM   1028  CD1 ILE A 137      55.940  11.271  53.756  1.00 84.62           C  
ANISOU 1028  CD1 ILE A 137     9676  11747  10730    691   1095   -206       C  
ATOM   1029  N   ILE A 138      59.300   9.559  49.948  1.00 89.34           N  
ANISOU 1029  N   ILE A 138    10353  12223  11370    863   1261    125       N  
ATOM   1030  CA  ILE A 138      59.456   9.079  48.577  1.00 88.57           C  
ANISOU 1030  CA  ILE A 138    10320  12069  11262    959   1301    152       C  
ATOM   1031  C   ILE A 138      60.769   8.335  48.390  1.00 85.28           C  
ANISOU 1031  C   ILE A 138     9816  11700  10886    938   1361    231       C  
ATOM   1032  O   ILE A 138      60.829   7.317  47.700  1.00 74.63           O  
ANISOU 1032  O   ILE A 138     8456  10345   9554   1016   1376    247       O  
ATOM   1033  CB  ILE A 138      59.385  10.235  47.560  1.00 86.96           C  
ANISOU 1033  CB  ILE A 138    10272  11763  11005    987   1332    137       C  
ATOM   1034  CG1 ILE A 138      58.084  11.019  47.730  1.00 79.04           C  
ANISOU 1034  CG1 ILE A 138     9353  10704   9976   1029   1258     49       C  
ATOM   1035  CG2 ILE A 138      59.485   9.706  46.135  1.00 75.42           C  
ANISOU 1035  CG2 ILE A 138     8891  10249   9516   1078   1373    159       C  
ATOM   1036  CD1 ILE A 138      57.918  12.119  46.709  1.00 80.76           C  
ANISOU 1036  CD1 ILE A 138     9746  10800  10139   1071   1263     39       C  
ATOM   1037  N   GLY A 139      61.820   8.855  49.012  1.00 70.30           N  
ANISOU 1037  N   GLY A 139     7850   9852   9010    834   1392    270       N  
ATOM   1038  CA  GLY A 139      63.125   8.229  48.959  1.00 64.31           C  
ANISOU 1038  CA  GLY A 139     6980   9152   8305    810   1442    333       C  
ATOM   1039  C   GLY A 139      63.098   6.834  49.549  1.00 78.20           C  
ANISOU 1039  C   GLY A 139     8627  10966  10119    847   1383    359       C  
ATOM   1040  O   GLY A 139      63.689   5.905  49.002  1.00 71.03           O  
ANISOU 1040  O   GLY A 139     7666  10066   9256    908   1412    388       O  
ATOM   1041  N   ASP A 140      62.395   6.688  50.667  1.00 83.55           N  
ANISOU 1041  N   ASP A 140     9276  11679  10790    806   1302    343       N  
ATOM   1042  CA  ASP A 140      62.317   5.407  51.354  1.00 85.02           C  
ANISOU 1042  CA  ASP A 140     9379  11910  11016    818   1236    375       C  
ATOM   1043  C   ASP A 140      61.495   4.423  50.535  1.00 76.51           C  
ANISOU 1043  C   ASP A 140     8357  10777   9936    933   1228    351       C  
ATOM   1044  O   ASP A 140      61.757   3.220  50.545  1.00 74.33           O  
ANISOU 1044  O   ASP A 140     8028  10507   9706    978   1203    388       O  
ATOM   1045  CB  ASP A 140      61.721   5.583  52.754  1.00 92.94           C  
ANISOU 1045  CB  ASP A 140    10357  12967  11990    722   1162    358       C  
ATOM   1046  CG  ASP A 140      62.138   4.483  53.704  1.00 87.05           C  
ANISOU 1046  CG  ASP A 140     9517  12280  11279    686   1092    423       C  
ATOM   1047  OD1 ASP A 140      63.337   4.425  54.053  1.00 83.46           O  
ANISOU 1047  OD1 ASP A 140     8971  11871  10869    649   1085    483       O  
ATOM   1048  OD2 ASP A 140      61.267   3.684  54.102  1.00 68.52           O1-
ANISOU 1048  OD2 ASP A 140     7188   9932   8913    692   1038    411       O1-
ATOM   1049  N   ALA A 141      60.503   4.948  49.822  1.00 71.25           N  
ANISOU 1049  N   ALA A 141     7801  10051   9218    982   1241    286       N  
ATOM   1050  CA  ALA A 141      59.676   4.140  48.937  1.00 71.73           C  
ANISOU 1050  CA  ALA A 141     7925  10061   9270   1087   1233    252       C  
ATOM   1051  C   ALA A 141      60.509   3.600  47.785  1.00 75.78           C  
ANISOU 1051  C   ALA A 141     8444  10539   9808   1164   1300    285       C  
ATOM   1052  O   ALA A 141      60.351   2.450  47.370  1.00 73.82           O  
ANISOU 1052  O   ALA A 141     8191  10272   9586   1235   1289    287       O  
ATOM   1053  CB  ALA A 141      58.516   4.963  48.404  1.00 67.04           C  
ANISOU 1053  CB  ALA A 141     7441   9413   8616   1125   1222    173       C  
ATOM   1054  N   ALA A 142      61.398   4.444  47.273  1.00 72.84           N  
ANISOU 1054  N   ALA A 142     8088  10161   9428   1140   1374    304       N  
ATOM   1055  CA  ALA A 142      62.303   4.050  46.205  1.00 78.00           C  
ANISOU 1055  CA  ALA A 142     8738  10799  10101   1193   1459    324       C  
ATOM   1056  C   ALA A 142      63.240   2.953  46.689  1.00 84.44           C  
ANISOU 1056  C   ALA A 142     9410  11666  11007   1202   1450    370       C  
ATOM   1057  O   ALA A 142      63.429   1.943  46.016  1.00 89.80           O  
ANISOU 1057  O   ALA A 142    10077  12321  11720   1287   1473    366       O  
ATOM   1058  CB  ALA A 142      63.100   5.247  45.724  1.00 66.53           C  
ANISOU 1058  CB  ALA A 142     7324   9341   8614   1132   1545    334       C  
ATOM   1059  N   VAL A 143      63.815   3.165  47.869  1.00 72.99           N  
ANISOU 1059  N   VAL A 143     7855  10281   9595   1117   1410    409       N  
ATOM   1060  CA  VAL A 143      64.733   2.210  48.476  1.00 75.68           C  
ANISOU 1060  CA  VAL A 143     8056  10671  10026   1124   1376    458       C  
ATOM   1061  C   VAL A 143      64.071   0.852  48.683  1.00 76.18           C  
ANISOU 1061  C   VAL A 143     8125  10702  10117   1195   1297    465       C  
ATOM   1062  O   VAL A 143      64.634  -0.181  48.319  1.00 71.31           O  
ANISOU 1062  O   VAL A 143     7455  10070   9569   1275   1302    480       O  
ATOM   1063  CB  VAL A 143      65.267   2.732  49.825  1.00 68.16           C  
ANISOU 1063  CB  VAL A 143     7010   9795   9092   1009   1319    498       C  
ATOM   1064  CG1 VAL A 143      66.064   1.653  50.535  1.00 57.48           C  
ANISOU 1064  CG1 VAL A 143     5527   8485   7829   1028   1248    555       C  
ATOM   1065  CG2 VAL A 143      66.117   3.969  49.615  1.00 60.29           C  
ANISOU 1065  CG2 VAL A 143     5993   8832   8083    931   1401    493       C  
ATOM   1066  N   ARG A 144      62.875   0.864  49.263  1.00 79.01           N  
ANISOU 1066  N   ARG A 144     8549  11050  10423   1162   1230    446       N  
ATOM   1067  CA  ARG A 144      62.112  -0.364  49.470  1.00 83.42           C  
ANISOU 1067  CA  ARG A 144     9130  11574  10991   1205   1161    447       C  
ATOM   1068  C   ARG A 144      61.848  -1.086  48.152  1.00 80.55           C  
ANISOU 1068  C   ARG A 144     8830  11139  10635   1323   1208    410       C  
ATOM   1069  O   ARG A 144      62.014  -2.302  48.056  1.00 70.58           O  
ANISOU 1069  O   ARG A 144     7546   9843   9427   1385   1178    429       O  
ATOM   1070  CB  ARG A 144      60.779  -0.071  50.159  1.00 81.30           C  
ANISOU 1070  CB  ARG A 144     8923  11315  10653   1139   1106    409       C  
ATOM   1071  CG  ARG A 144      60.874   0.348  51.616  1.00 78.06           C  
ANISOU 1071  CG  ARG A 144     8457  10975  10226   1014   1046    440       C  
ATOM   1072  CD  ARG A 144      59.484   0.385  52.227  1.00 91.85           C  
ANISOU 1072  CD  ARG A 144    10257  12732  11908    955   1003    385       C  
ATOM   1073  NE  ARG A 144      59.438   1.090  53.503  1.00 96.15           N  
ANISOU 1073  NE  ARG A 144    10768  13349  12414    826    969    388       N  
ATOM   1074  CZ  ARG A 144      59.591   0.504  54.684  1.00101.27           C  
ANISOU 1074  CZ  ARG A 144    11379  14044  13057    737    899    442       C  
ATOM   1075  NH1 ARG A 144      59.808  -0.801  54.753  1.00101.05           N1+
ANISOU 1075  NH1 ARG A 144    11343  13985  13065    770    848    503       N1+
ATOM   1076  NH2 ARG A 144      59.533   1.225  55.796  1.00110.16           N  
ANISOU 1076  NH2 ARG A 144    12483  15239  14135    613    876    434       N  
ATOM   1077  N   THR A 145      61.435  -0.330  47.140  1.00 75.77           N  
ANISOU 1077  N   THR A 145     8314  10505   9971   1353   1274    356       N  
ATOM   1078  CA  THR A 145      61.122  -0.900  45.834  1.00 70.99           C  
ANISOU 1078  CA  THR A 145     7786   9836   9352   1454   1319    314       C  
ATOM   1079  C   THR A 145      62.353  -1.529  45.200  1.00 78.99           C  
ANISOU 1079  C   THR A 145     8735  10843  10434   1518   1386    333       C  
ATOM   1080  O   THR A 145      62.297  -2.644  44.680  1.00 83.84           O  
ANISOU 1080  O   THR A 145     9360  11411  11083   1601   1385    317       O  
ATOM   1081  CB  THR A 145      60.567   0.163  44.870  1.00 82.13           C  
ANISOU 1081  CB  THR A 145     9315  11217  10676   1467   1370    263       C  
ATOM   1082  CG2 THR A 145      60.216  -0.466  43.530  1.00 88.25           C  
ANISOU 1082  CG2 THR A 145    10178  11929  11422   1565   1408    218       C  
ATOM   1083  OG1 THR A 145      59.394   0.759  45.436  1.00 78.63           O  
ANISOU 1083  OG1 THR A 145     8917  10777  10181   1424   1304    228       O  
ATOM   1084  N   LEU A 146      63.466  -0.805  45.246  1.00 73.77           N  
ANISOU 1084  N   LEU A 146     8003  10230   9796   1477   1448    358       N  
ATOM   1085  CA  LEU A 146      64.714  -1.299  44.681  1.00 75.44           C  
ANISOU 1085  CA  LEU A 146     8128  10455  10081   1530   1523    360       C  
ATOM   1086  C   LEU A 146      65.211  -2.524  45.438  1.00 87.99           C  
ANISOU 1086  C   LEU A 146     9604  12049  11781   1573   1445    399       C  
ATOM   1087  O   LEU A 146      65.678  -3.489  44.832  1.00100.49           O  
ANISOU 1087  O   LEU A 146    11153  13599  13428   1669   1474    378       O  
ATOM   1088  CB  LEU A 146      65.784  -0.204  44.692  1.00 71.40           C  
ANISOU 1088  CB  LEU A 146     7550  10008   9572   1453   1604    373       C  
ATOM   1089  CG  LEU A 146      65.540   1.033  43.823  1.00 76.18           C  
ANISOU 1089  CG  LEU A 146     8279  10595  10070   1407   1692    344       C  
ATOM   1090  CD1 LEU A 146      66.611   2.079  44.075  1.00 74.75           C  
ANISOU 1090  CD1 LEU A 146     8025  10478   9897   1305   1759    364       C  
ATOM   1091  CD2 LEU A 146      65.492   0.656  42.355  1.00 74.06           C  
ANISOU 1091  CD2 LEU A 146     8101  10278   9762   1486   1785    295       C  
ATOM   1092  N   GLU A 147      65.105  -2.481  46.764  1.00 88.91           N  
ANISOU 1092  N   GLU A 147     9669  12200  11913   1503   1342    452       N  
ATOM   1093  CA  GLU A 147      65.570  -3.577  47.608  1.00 83.92           C  
ANISOU 1093  CA  GLU A 147     8946  11566  11374   1532   1244    504       C  
ATOM   1094  C   GLU A 147      64.826  -4.879  47.335  1.00 78.96           C  
ANISOU 1094  C   GLU A 147     8392  10850  10761   1614   1194    492       C  
ATOM   1095  O   GLU A 147      65.431  -5.950  47.293  1.00 81.05           O  
ANISOU 1095  O   GLU A 147     8601  11076  11120   1699   1162    507       O  
ATOM   1096  CB  GLU A 147      65.463  -3.210  49.090  1.00 89.03           C  
ANISOU 1096  CB  GLU A 147     9556  12267  12005   1420   1141    565       C  
ATOM   1097  CG  GLU A 147      66.647  -2.421  49.624  1.00 98.98           C  
ANISOU 1097  CG  GLU A 147    10690  13615  13305   1356   1153    596       C  
ATOM   1098  CD  GLU A 147      66.666  -2.359  51.138  1.00104.27           C  
ANISOU 1098  CD  GLU A 147    11315  14333  13968   1257   1031    662       C  
ATOM   1099  OE1 GLU A 147      65.671  -2.787  51.758  1.00111.25           O  
ANISOU 1099  OE1 GLU A 147    12281  15188  14801   1222    952    679       O  
ATOM   1100  OE2 GLU A 147      67.674  -1.889  51.707  1.00102.41           O1-
ANISOU 1100  OE2 GLU A 147    10965  14171  13774   1206   1014    692       O1-
ATOM   1101  N   PHE A 148      63.514  -4.780  47.151  1.00 77.67           N  
ANISOU 1101  N   PHE A 148     8352  10652  10509   1590   1183    459       N  
ATOM   1102  CA  PHE A 148      62.697  -5.949  46.853  1.00 84.73           C  
ANISOU 1102  CA  PHE A 148     9325  11464  11404   1649   1141    438       C  
ATOM   1103  C   PHE A 148      63.119  -6.590  45.541  1.00 99.44           C  
ANISOU 1103  C   PHE A 148    11203  13270  13309   1771   1221    387       C  
ATOM   1104  O   PHE A 148      63.091  -7.812  45.396  1.00107.89           O  
ANISOU 1104  O   PHE A 148    12288  14269  14436   1844   1183    384       O  
ATOM   1105  CB  PHE A 148      61.220  -5.571  46.773  1.00 82.94           C  
ANISOU 1105  CB  PHE A 148     9211  11229  11074   1597   1128    392       C  
ATOM   1106  CG  PHE A 148      60.352  -6.659  46.214  1.00 88.26           C  
ANISOU 1106  CG  PHE A 148     9971  11823  11739   1654   1106    351       C  
ATOM   1107  CD1 PHE A 148      60.020  -7.758  46.986  1.00 84.72           C  
ANISOU 1107  CD1 PHE A 148     9535  11334  11323   1631   1014    388       C  
ATOM   1108  CD2 PHE A 148      59.868  -6.585  44.917  1.00 98.71           C  
ANISOU 1108  CD2 PHE A 148    11376  13110  13018   1720   1173    276       C  
ATOM   1109  CE1 PHE A 148      59.225  -8.763  46.478  1.00 92.44           C  
ANISOU 1109  CE1 PHE A 148    10596  12235  12293   1670    995    347       C  
ATOM   1110  CE2 PHE A 148      59.071  -7.589  44.405  1.00100.22           C  
ANISOU 1110  CE2 PHE A 148    11646  13231  13200   1764   1150    232       C  
ATOM   1111  CZ  PHE A 148      58.750  -8.678  45.187  1.00 98.02           C  
ANISOU 1111  CZ  PHE A 148    11371  12912  12959   1737   1064    265       C  
ATOM   1112  N   LEU A 149      63.501  -5.753  44.585  1.00 99.66           N  
ANISOU 1112  N   LEU A 149    11238  13327  13303   1786   1334    343       N  
ATOM   1113  CA  LEU A 149      63.917  -6.230  43.275  1.00 96.88           C  
ANISOU 1113  CA  LEU A 149    10906  12934  12969   1887   1431    282       C  
ATOM   1114  C   LEU A 149      65.237  -6.982  43.362  1.00109.25           C  
ANISOU 1114  C   LEU A 149    12338  14503  14668   1960   1443    294       C  
ATOM   1115  O   LEU A 149      65.543  -7.810  42.508  1.00125.33           O  
ANISOU 1115  O   LEU A 149    14379  16489  16751   2061   1494    241       O  
ATOM   1116  CB  LEU A 149      64.020  -5.066  42.289  1.00 85.24           C  
ANISOU 1116  CB  LEU A 149     9486  11493  11408   1862   1549    240       C  
ATOM   1117  CG  LEU A 149      62.684  -4.430  41.907  1.00 72.74           C  
ANISOU 1117  CG  LEU A 149     8050   9886   9701   1827   1534    211       C  
ATOM   1118  CD1 LEU A 149      62.894  -3.285  40.935  1.00 68.12           C  
ANISOU 1118  CD1 LEU A 149     7535   9319   9028   1804   1639    182       C  
ATOM   1119  CD2 LEU A 149      61.763  -5.483  41.316  1.00 53.35           C  
ANISOU 1119  CD2 LEU A 149     5687   7356   7228   1898   1501    162       C  
ATOM   1120  N   GLY A 150      66.019  -6.686  44.395  1.00103.63           N  
ANISOU 1120  N   GLY A 150    11503  13853  14018   1913   1392    355       N  
ATOM   1121  CA  GLY A 150      67.222  -7.450  44.666  1.00104.25           C  
ANISOU 1121  CA  GLY A 150    11439  13935  14236   1990   1368    370       C  
ATOM   1122  C   GLY A 150      68.527  -6.697  44.515  1.00108.60           C  
ANISOU 1122  C   GLY A 150    11844  14580  14837   1974   1458    355       C  
ATOM   1123  O   GLY A 150      69.601  -7.280  44.653  1.00117.50           O  
ANISOU 1123  O   GLY A 150    12829  15723  16092   2048   1445    349       O  
ATOM   1124  N   HIS A 151      68.447  -5.402  44.233  1.00104.11           N  
ANISOU 1124  N   HIS A 151    11309  14074  14174   1877   1545    344       N  
ATOM   1125  CA  HIS A 151      69.649  -4.595  44.077  1.00106.43           C  
ANISOU 1125  CA  HIS A 151    11476  14462  14502   1833   1642    326       C  
ATOM   1126  C   HIS A 151      70.293  -4.350  45.435  1.00106.45           C  
ANISOU 1126  C   HIS A 151    11340  14532  14572   1772   1537    396       C  
ATOM   1127  O   HIS A 151      69.713  -4.670  46.471  1.00113.80           O  
ANISOU 1127  O   HIS A 151    12301  15438  15498   1748   1397    461       O  
ATOM   1128  CB  HIS A 151      69.320  -3.255  43.418  1.00107.27           C  
ANISOU 1128  CB  HIS A 151    11685  14596  14475   1734   1754    304       C  
ATOM   1129  CG  HIS A 151      68.630  -3.379  42.095  1.00115.97           C  
ANISOU 1129  CG  HIS A 151    12942  15633  15488   1782   1844    242       C  
ATOM   1130  CD2 HIS A 151      68.334  -4.462  41.338  1.00118.64           C  
ANISOU 1130  CD2 HIS A 151    13330  15903  15846   1893   1858    193       C  
ATOM   1131  ND1 HIS A 151      68.156  -2.287  41.402  1.00121.60           N  
ANISOU 1131  ND1 HIS A 151    13790  16344  16068   1709   1923    226       N  
ATOM   1132  CE1 HIS A 151      67.597  -2.691  40.275  1.00123.80           C  
ANISOU 1132  CE1 HIS A 151    14193  16561  16284   1773   1978    173       C  
ATOM   1133  NE2 HIS A 151      67.691  -4.007  40.212  1.00121.18           N  
ANISOU 1133  NE2 HIS A 151    13810  16192  16042   1882   1945    148       N  
ATOM   1134  N   LYS A 152      71.496  -3.789  45.428  1.00104.37           N  
ANISOU 1134  N   LYS A 152    10928  14362  14367   1737   1605    379       N  
ATOM   1135  CA  LYS A 152      72.143  -3.383  46.668  1.00104.20           C  
ANISOU 1135  CA  LYS A 152    10776  14419  14397   1661   1511    439       C  
ATOM   1136  C   LYS A 152      71.996  -1.881  46.847  1.00101.18           C  
ANISOU 1136  C   LYS A 152    10442  14097  13906   1504   1569    450       C  
ATOM   1137  O   LYS A 152      72.674  -1.097  46.186  1.00103.04           O  
ANISOU 1137  O   LYS A 152    10635  14389  14128   1451   1704    404       O  
ATOM   1138  CB  LYS A 152      73.619  -3.780  46.680  1.00109.66           C  
ANISOU 1138  CB  LYS A 152    11245  15182  15240   1723   1527    407       C  
ATOM   1139  CG  LYS A 152      74.360  -3.327  47.929  1.00118.13           C  
ANISOU 1139  CG  LYS A 152    12172  16346  16365   1641   1423    464       C  
ATOM   1140  CD  LYS A 152      75.757  -3.918  47.994  1.00131.31           C  
ANISOU 1140  CD  LYS A 152    13606  18079  18205   1731   1406    428       C  
ATOM   1141  CE  LYS A 152      76.507  -3.425  49.219  1.00134.48           C  
ANISOU 1141  CE  LYS A 152    13861  18582  18655   1644   1294    482       C  
ATOM   1142  NZ  LYS A 152      76.753  -1.957  49.158  1.00132.25           N1+
ANISOU 1142  NZ  LYS A 152    13569  18392  18286   1473   1408    464       N1+
ATOM   1143  N   VAL A 153      71.098  -1.488  47.742  1.00 94.88           N  
ANISOU 1143  N   VAL A 153     9738  13282  13030   1426   1470    506       N  
ATOM   1144  CA  VAL A 153      70.784  -0.081  47.935  1.00 94.39           C  
ANISOU 1144  CA  VAL A 153     9746  13254  12863   1287   1512    511       C  
ATOM   1145  C   VAL A 153      71.560   0.527  49.094  1.00 95.90           C  
ANISOU 1145  C   VAL A 153     9810  13539  13090   1180   1449    552       C  
ATOM   1146  O   VAL A 153      71.495   0.042  50.221  1.00100.56           O  
ANISOU 1146  O   VAL A 153    10354  14143  13713   1173   1307    608       O  
ATOM   1147  CB  VAL A 153      69.284   0.122  48.187  1.00 91.48           C  
ANISOU 1147  CB  VAL A 153     9554  12818  12384   1260   1455    525       C  
ATOM   1148  CG1 VAL A 153      68.962   1.602  48.272  1.00 88.80           C  
ANISOU 1148  CG1 VAL A 153     9296  12500  11946   1135   1503    516       C  
ATOM   1149  CG2 VAL A 153      68.474  -0.543  47.091  1.00 83.42           C  
ANISOU 1149  CG2 VAL A 153     8657  11710  11330   1364   1499    483       C  
ATOM   1150  N   ILE A 154      72.299   1.592  48.806  1.00 90.78           N  
ANISOU 1150  N   ILE A 154     9112  12955  12426   1087   1553    525       N  
ATOM   1151  CA  ILE A 154      73.002   2.329  49.845  1.00 97.25           C  
ANISOU 1151  CA  ILE A 154     9821  13866  13265    965   1503    554       C  
ATOM   1152  C   ILE A 154      72.246   3.603  50.183  1.00103.11           C  
ANISOU 1152  C   ILE A 154    10702  14593  13883    833   1515    561       C  
ATOM   1153  O   ILE A 154      72.277   4.575  49.430  1.00103.35           O  
ANISOU 1153  O   ILE A 154    10808  14610  13849    770   1637    525       O  
ATOM   1154  CB  ILE A 154      74.437   2.690  49.423  1.00 98.25           C  
ANISOU 1154  CB  ILE A 154     9776  14085  13468    929   1607    513       C  
ATOM   1155  CG1 ILE A 154      75.251   1.422  49.171  1.00100.19           C  
ANISOU 1155  CG1 ILE A 154     9858  14352  13857   1072   1586    492       C  
ATOM   1156  CG2 ILE A 154      75.110   3.539  50.493  1.00103.63           C  
ANISOU 1156  CG2 ILE A 154    10352  14863  14160    787   1554    538       C  
ATOM   1157  CD1 ILE A 154      76.703   1.689  48.859  1.00102.18           C  
ANISOU 1157  CD1 ILE A 154     9904  14715  14205   1041   1680    436       C  
ATOM   1158  N   ARG A 155      71.549   3.581  51.312  1.00 99.60           N  
ANISOU 1158  N   ARG A 155    10299  14143  13402    792   1387    603       N  
ATOM   1159  CA  ARG A 155      70.830   4.751  51.788  1.00 87.65           C  
ANISOU 1159  CA  ARG A 155     8902  12619  11784    673   1385    598       C  
ATOM   1160  C   ARG A 155      71.808   5.872  52.099  1.00 85.32           C  
ANISOU 1160  C   ARG A 155     8525  12400  11492    537   1433    590       C  
ATOM   1161  O   ARG A 155      72.766   5.678  52.843  1.00 94.82           O  
ANISOU 1161  O   ARG A 155     9568  13693  12768    498   1373    615       O  
ATOM   1162  CB  ARG A 155      70.027   4.400  53.036  1.00 95.38           C  
ANISOU 1162  CB  ARG A 155     9912  13599  12730    645   1243    635       C  
ATOM   1163  CG  ARG A 155      68.944   3.374  52.800  1.00 93.00           C  
ANISOU 1163  CG  ARG A 155     9704  13221  12413    752   1198    638       C  
ATOM   1164  CD  ARG A 155      68.448   2.808  54.113  1.00 88.20           C  
ANISOU 1164  CD  ARG A 155     9093  12632  11787    712   1056    685       C  
ATOM   1165  NE  ARG A 155      67.306   1.921  53.925  1.00 86.44           N  
ANISOU 1165  NE  ARG A 155     8972  12336  11535    787   1021    680       N  
ATOM   1166  CZ  ARG A 155      67.406   0.630  53.627  1.00 89.58           C  
ANISOU 1166  CZ  ARG A 155     9348  12692  11997    897    981    707       C  
ATOM   1167  NH1 ARG A 155      68.600   0.074  53.476  1.00 97.40           N1+
ANISOU 1167  NH1 ARG A 155    10211  13706  13091    959    969    735       N1+
ATOM   1168  NH2 ARG A 155      66.312  -0.103  53.477  1.00 86.00           N  
ANISOU 1168  NH2 ARG A 155     8996  12172  11509    944    952    697       N  
ATOM   1169  N   ALA A 156      71.567   7.044  51.525  1.00 72.64           N  
ANISOU 1169  N   ALA A 156     7035  10757   9808    462   1533    555       N  
ATOM   1170  CA  ALA A 156      72.474   8.167  51.707  1.00 79.79           C  
ANISOU 1170  CA  ALA A 156     7885  11722  10709    319   1594    542       C  
ATOM   1171  C   ALA A 156      71.776   9.365  52.328  1.00 90.77           C  
ANISOU 1171  C   ALA A 156     9403  13078  12006    203   1571    532       C  
ATOM   1172  O   ALA A 156      70.935  10.001  51.698  1.00 96.06           O  
ANISOU 1172  O   ALA A 156    10248  13654  12598    211   1622    506       O  
ATOM   1173  CB  ALA A 156      73.103   8.552  50.383  1.00 90.22           C  
ANISOU 1173  CB  ALA A 156     9222  13030  12028    313   1755    507       C  
ATOM   1174  N   ASN A 157      72.140   9.673  53.567  1.00 96.97           N  
ANISOU 1174  N   ASN A 157    10103  13938  12802     99   1488    549       N  
ATOM   1175  CA  ASN A 157      71.557  10.801  54.278  1.00 94.44           C  
ANISOU 1175  CA  ASN A 157     9888  13594  12401    -18   1463    528       C  
ATOM   1176  C   ASN A 157      72.507  11.993  54.296  1.00101.76           C  
ANISOU 1176  C   ASN A 157    10784  14557  13321   -172   1538    508       C  
ATOM   1177  O   ASN A 157      73.392  12.086  55.145  1.00101.83           O  
ANISOU 1177  O   ASN A 157    10650  14669  13372   -267   1490    520       O  
ATOM   1178  CB  ASN A 157      71.178  10.389  55.700  1.00 89.53           C  
ANISOU 1178  CB  ASN A 157     9219  13026  11771    -48   1321    551       C  
ATOM   1179  CG  ASN A 157      70.137  11.300  56.312  1.00 94.69           C  
ANISOU 1179  CG  ASN A 157    10014  13633  12333   -122   1297    510       C  
ATOM   1180  ND2 ASN A 157      69.245  10.727  57.112  1.00105.10           N  
ANISOU 1180  ND2 ASN A 157    11357  14956  13620    -97   1203    514       N  
ATOM   1181  OD1 ASN A 157      70.129  12.504  56.066  1.00 84.53           O  
ANISOU 1181  OD1 ASN A 157     8813  12300  11003   -202   1365    471       O  
ATOM   1182  N   HIS A 158      72.313  12.900  53.346  1.00102.48           N  
ANISOU 1182  N   HIS A 158    11019  14562  13357   -201   1648    478       N  
ATOM   1183  CA  HIS A 158      73.176  14.064  53.189  1.00107.44           C  
ANISOU 1183  CA  HIS A 158    11650  15204  13970   -357   1737    459       C  
ATOM   1184  C   HIS A 158      72.835  15.143  54.211  1.00103.21           C  
ANISOU 1184  C   HIS A 158    11185  14651  13378   -487   1683    436       C  
ATOM   1185  O   HIS A 158      72.186  16.137  53.888  1.00105.80           O  
ANISOU 1185  O   HIS A 158    11697  14867  13633   -521   1721    407       O  
ATOM   1186  CB  HIS A 158      73.042  14.615  51.770  1.00110.63           C  
ANISOU 1186  CB  HIS A 158    12213  15503  14319   -344   1870    444       C  
ATOM   1187  CG  HIS A 158      74.211  15.434  51.327  1.00101.55           C  
ANISOU 1187  CG  HIS A 158    11028  14388  13170   -496   1991    431       C  
ATOM   1188  CD2 HIS A 158      75.444  15.069  50.906  1.00 96.07           C  
ANISOU 1188  CD2 HIS A 158    10164  13796  12541   -532   2076    427       C  
ATOM   1189  ND1 HIS A 158      74.181  16.811  51.283  1.00103.97           N  
ANISOU 1189  ND1 HIS A 158    11482  14619  13402   -638   2041    414       N  
ATOM   1190  CE1 HIS A 158      75.348  17.259  50.853  1.00108.12           C  
ANISOU 1190  CE1 HIS A 158    11940  15201  13942   -770   2155    404       C  
ATOM   1191  NE2 HIS A 158      76.131  16.222  50.617  1.00106.68           N  
ANISOU 1191  NE2 HIS A 158    11554  15134  13845   -709   2182    407       N  
ATOM   1192  N   VAL A 159      73.281  14.939  55.444  1.00101.71           N  
ANISOU 1192  N   VAL A 159    10853  14570  13222   -556   1589    447       N  
ATOM   1193  CA  VAL A 159      72.950  15.830  56.548  1.00111.24           C  
ANISOU 1193  CA  VAL A 159    12114  15777  14376   -679   1528    418       C  
ATOM   1194  C   VAL A 159      73.780  17.108  56.509  1.00111.42           C  
ANISOU 1194  C   VAL A 159    12153  15801  14381   -856   1606    390       C  
ATOM   1195  O   VAL A 159      74.983  17.066  56.272  1.00116.97           O  
ANISOU 1195  O   VAL A 159    12716  16589  15138   -925   1658    400       O  
ATOM   1196  CB  VAL A 159      73.173  15.129  57.902  1.00117.16           C  
ANISOU 1196  CB  VAL A 159    12714  16648  15152   -704   1392    444       C  
ATOM   1197  CG1 VAL A 159      72.612  15.967  59.035  1.00123.72           C  
ANISOU 1197  CG1 VAL A 159    13624  17473  15910   -819   1332    403       C  
ATOM   1198  CG2 VAL A 159      72.533  13.756  57.894  1.00113.41           C  
ANISOU 1198  CG2 VAL A 159    12214  16174  14701   -541   1320    482       C  
ATOM   1199  N   GLY A 160      73.133  18.245  56.740  1.00110.49           N  
ANISOU 1199  N   GLY A 160    12204  15587  14192   -932   1614    346       N  
ATOM   1200  CA  GLY A 160      73.833  19.515  56.795  1.00119.47           C  
ANISOU 1200  CA  GLY A 160    13381  16707  15304  -1113   1680    316       C  
ATOM   1201  C   GLY A 160      74.554  19.700  58.117  1.00113.24           C  
ANISOU 1201  C   GLY A 160    12446  16048  14533  -1259   1604    304       C  
ATOM   1202  O   GLY A 160      74.183  20.554  58.921  1.00111.32           O  
ANISOU 1202  O   GLY A 160    12287  15773  14237  -1359   1567    259       O  
ATOM   1203  N   ASP A 161      75.592  18.900  58.340  1.00112.67           N  
ANISOU 1203  N   ASP A 161    12153  16122  14535  -1268   1577    340       N  
ATOM   1204  CA  ASP A 161      76.313  18.918  59.608  1.00118.06           C  
ANISOU 1204  CA  ASP A 161    12679  16943  15237  -1393   1480    337       C  
ATOM   1205  C   ASP A 161      77.538  19.826  59.599  1.00132.37           C  
ANISOU 1205  C   ASP A 161    14412  18814  17067  -1586   1549    308       C  
ATOM   1206  O   ASP A 161      78.439  19.670  60.421  1.00136.95           O  
ANISOU 1206  O   ASP A 161    14810  19537  17689  -1680   1477    310       O  
ATOM   1207  CB  ASP A 161      76.713  17.499  60.030  1.00113.99           C  
ANISOU 1207  CB  ASP A 161    11963  16554  14795  -1287   1374    391       C  
ATOM   1208  CG  ASP A 161      77.450  16.743  58.939  1.00109.01           C  
ANISOU 1208  CG  ASP A 161    11209  15955  14253  -1188   1449    416       C  
ATOM   1209  OD1 ASP A 161      78.045  17.384  58.049  1.00103.10           O  
ANISOU 1209  OD1 ASP A 161    10473  15185  13515  -1258   1583    390       O  
ATOM   1210  OD2 ASP A 161      77.439  15.495  58.979  1.00109.92           O1-
ANISOU 1210  OD2 ASP A 161    11220  16116  14427  -1045   1375    459       O1-
ATOM   1211  N   TRP A 162      77.569  20.776  58.672  1.00140.55           N  
ANISOU 1211  N   TRP A 162    15591  19741  18069  -1653   1683    282       N  
ATOM   1212  CA  TRP A 162      78.690  21.699  58.593  1.00144.40           C  
ANISOU 1212  CA  TRP A 162    16026  20274  18566  -1858   1765    251       C  
ATOM   1213  C   TRP A 162      78.261  23.045  58.032  1.00136.70           C  
ANISOU 1213  C   TRP A 162    15304  19126  17509  -1958   1866    217       C  
ATOM   1214  O   TRP A 162      77.280  23.144  57.297  1.00127.64           O  
ANISOU 1214  O   TRP A 162    14355  17828  16316  -1842   1900    225       O  
ATOM   1215  CB  TRP A 162      79.811  21.111  57.738  1.00147.57           C  
ANISOU 1215  CB  TRP A 162    16243  20777  19051  -1848   1854    266       C  
ATOM   1216  CG  TRP A 162      81.174  21.603  58.110  1.00155.15           C  
ANISOU 1216  CG  TRP A 162    17021  21872  20056  -2049   1882    231       C  
ATOM   1217  CD1 TRP A 162      81.743  22.790  57.754  1.00159.17           C  
ANISOU 1217  CD1 TRP A 162    17603  22346  20529  -2253   2002    191       C  
ATOM   1218  CD2 TRP A 162      82.144  20.917  58.909  1.00155.91           C  
ANISOU 1218  CD2 TRP A 162    16832  22163  20243  -2069   1783    232       C  
ATOM   1219  CE2 TRP A 162      83.277  21.749  58.997  1.00156.91           C  
ANISOU 1219  CE2 TRP A 162    16855  22375  20389  -2289   1851    182       C  
ATOM   1220  CE3 TRP A 162      82.165  19.679  59.559  1.00148.72           C  
ANISOU 1220  CE3 TRP A 162    15751  21356  19400  -1923   1634    270       C  
ATOM   1221  NE1 TRP A 162      83.006  22.888  58.284  1.00161.97           N  
ANISOU 1221  NE1 TRP A 162    17722  22870  20947  -2406   1991    159       N  
ATOM   1222  CZ2 TRP A 162      84.418  21.386  59.708  1.00148.83           C  
ANISOU 1222  CZ2 TRP A 162    15546  21547  19455  -2360   1770    163       C  
ATOM   1223  CZ3 TRP A 162      83.299  19.319  60.264  1.00143.73           C  
ANISOU 1223  CZ3 TRP A 162    14852  20904  18853  -1986   1547    260       C  
ATOM   1224  CH2 TRP A 162      84.409  20.169  60.333  1.00141.52           C  
ANISOU 1224  CH2 TRP A 162    14457  20717  18597  -2198   1612    204       C  
ATOM   1225  N   GLY A 163      79.012  24.080  58.388  1.00138.30           N  
ANISOU 1225  N   GLY A 163    15503  19348  17695  -2174   1905    177       N  
ATOM   1226  CA  GLY A 163      78.722  25.428  57.944  1.00143.56           C  
ANISOU 1226  CA  GLY A 163    16417  19844  18286  -2293   1991    146       C  
ATOM   1227  C   GLY A 163      79.287  26.433  58.924  1.00153.43           C  
ANISOU 1227  C   GLY A 163    17650  21130  19516  -2520   1967     92       C  
ATOM   1228  O   GLY A 163      80.006  26.069  59.855  1.00152.12           O  
ANISOU 1228  O   GLY A 163    17266  21137  19395  -2592   1890     82       O  
ATOM   1229  N   THR A 164      78.959  27.703  58.718  1.00159.20           N  
ANISOU 1229  N   THR A 164    18619  21691  20178  -2632   2023     57       N  
ATOM   1230  CA  THR A 164      79.454  28.767  59.577  1.00153.29           C  
ANISOU 1230  CA  THR A 164    17889  20950  19404  -2859   2010     -3       C  
ATOM   1231  C   THR A 164      78.773  28.715  60.935  1.00147.56           C  
ANISOU 1231  C   THR A 164    17151  20256  18659  -2828   1868    -45       C  
ATOM   1232  O   THR A 164      79.403  28.942  61.967  1.00145.14           O  
ANISOU 1232  O   THR A 164    16718  20070  18357  -2980   1809    -82       O  
ATOM   1233  CB  THR A 164      79.167  30.148  58.972  1.00149.52           C  
ANISOU 1233  CB  THR A 164    17706  20250  18856  -2972   2101    -30       C  
ATOM   1234  CG2 THR A 164      78.951  30.041  57.471  1.00142.82           C  
ANISOU 1234  CG2 THR A 164    16999  19278  17987  -2878   2210     25       C  
ATOM   1235  OG1 THR A 164      77.996  30.701  59.585  1.00151.44           O  
ANISOU 1235  OG1 THR A 164    18140  20348  19052  -2907   2018    -77       O  
ATOM   1236  N   GLN A 165      77.481  28.403  60.917  1.00147.77           N  
ANISOU 1236  N   GLN A 165    17307  20179  18660  -2635   1814    -43       N  
ATOM   1237  CA  GLN A 165      76.621  28.494  62.096  1.00152.87           C  
ANISOU 1237  CA  GLN A 165    17992  20821  19270  -2606   1703    -99       C  
ATOM   1238  C   GLN A 165      77.103  27.720  63.322  1.00157.05           C  
ANISOU 1238  C   GLN A 165    18286  21568  19820  -2647   1590    -95       C  
ATOM   1239  O   GLN A 165      76.613  27.942  64.427  1.00160.56           O  
ANISOU 1239  O   GLN A 165    18756  22031  20219  -2686   1507   -150       O  
ATOM   1240  CB  GLN A 165      75.200  28.045  61.746  1.00150.79           C  
ANISOU 1240  CB  GLN A 165    17860  20444  18991  -2374   1672    -96       C  
ATOM   1241  CG  GLN A 165      75.058  26.551  61.496  1.00150.86           C  
ANISOU 1241  CG  GLN A 165    17712  20565  19044  -2192   1632    -24       C  
ATOM   1242  CD  GLN A 165      75.586  26.123  60.139  1.00150.82           C  
ANISOU 1242  CD  GLN A 165    17681  20546  19079  -2129   1728     44       C  
ATOM   1243  NE2 GLN A 165      75.378  24.857  59.800  1.00142.87           N  
ANISOU 1243  NE2 GLN A 165    16564  19607  18111  -1956   1701     99       N  
ATOM   1244  OE1 GLN A 165      76.168  26.920  59.404  1.00158.19           O  
ANISOU 1244  OE1 GLN A 165    18699  21405  20002  -2242   1831     45       O  
ATOM   1245  N   PHE A 166      78.055  26.815  63.134  1.00155.47           N  
ANISOU 1245  N   PHE A 166    17860  21528  19684  -2636   1583    -33       N  
ATOM   1246  CA  PHE A 166      78.544  26.004  64.243  1.00153.79           C  
ANISOU 1246  CA  PHE A 166    17427  21513  19493  -2658   1457    -16       C  
ATOM   1247  C   PHE A 166      79.327  26.811  65.271  1.00156.10           C  
ANISOU 1247  C   PHE A 166    17658  21894  19760  -2896   1415    -73       C  
ATOM   1248  O   PHE A 166      79.415  26.424  66.434  1.00162.41           O  
ANISOU 1248  O   PHE A 166    18351  22821  20539  -2933   1290    -78       O  
ATOM   1249  CB  PHE A 166      79.358  24.819  63.731  1.00152.28           C  
ANISOU 1249  CB  PHE A 166    17010  21458  19392  -2564   1450     58       C  
ATOM   1250  CG  PHE A 166      78.512  23.679  63.261  1.00151.40           C  
ANISOU 1250  CG  PHE A 166    16912  21313  19298  -2322   1424    115       C  
ATOM   1251  CD1 PHE A 166      77.756  23.794  62.108  1.00152.99           C  
ANISOU 1251  CD1 PHE A 166    17287  21355  19489  -2200   1523    123       C  
ATOM   1252  CD2 PHE A 166      78.456  22.499  63.980  1.00148.29           C  
ANISOU 1252  CD2 PHE A 166    16373  21041  18928  -2224   1293    160       C  
ATOM   1253  CE1 PHE A 166      76.968  22.750  61.676  1.00152.31           C  
ANISOU 1253  CE1 PHE A 166    17213  21240  19418  -1986   1497    168       C  
ATOM   1254  CE2 PHE A 166      77.670  21.452  63.553  1.00148.34           C  
ANISOU 1254  CE2 PHE A 166    16403  21010  18951  -2014   1270    209       C  
ATOM   1255  CZ  PHE A 166      76.925  21.577  62.399  1.00151.35           C  
ANISOU 1255  CZ  PHE A 166    16942  21240  19324  -1896   1375    209       C  
ATOM   1256  N   GLY A 167      79.893  27.933  64.841  1.00150.61           N  
ANISOU 1256  N   GLY A 167    17041  21127  19058  -3065   1518   -115       N  
ATOM   1257  CA  GLY A 167      80.532  28.847  65.767  1.00144.83           C  
ANISOU 1257  CA  GLY A 167    16286  20450  18292  -3304   1489   -182       C  
ATOM   1258  C   GLY A 167      79.476  29.428  66.684  1.00139.53           C  
ANISOU 1258  C   GLY A 167    15794  19686  17536  -3315   1429   -253       C  
ATOM   1259  O   GLY A 167      79.662  29.522  67.895  1.00144.06           O  
ANISOU 1259  O   GLY A 167    16298  20367  18069  -3428   1331   -294       O  
ATOM   1260  N   MET A 168      78.352  29.807  66.087  1.00129.18           N  
ANISOU 1260  N   MET A 168    14711  18176  16196  -3194   1486   -272       N  
ATOM   1261  CA  MET A 168      77.209  30.323  66.824  1.00128.75           C  
ANISOU 1261  CA  MET A 168    14827  18019  16073  -3170   1442   -354       C  
ATOM   1262  C   MET A 168      76.570  29.205  67.637  1.00139.27           C  
ANISOU 1262  C   MET A 168    16059  19473  17386  -3039   1328   -334       C  
ATOM   1263  O   MET A 168      75.967  29.444  68.684  1.00146.28           O  
ANISOU 1263  O   MET A 168    16998  20373  18208  -3080   1265   -408       O  
ATOM   1264  CB  MET A 168      76.195  30.908  65.841  1.00125.52           C  
ANISOU 1264  CB  MET A 168    14667  17369  15655  -3044   1523   -375       C  
ATOM   1265  CG  MET A 168      74.937  31.458  66.477  1.00127.64           C  
ANISOU 1265  CG  MET A 168    15109  17518  15870  -2991   1486   -476       C  
ATOM   1266  SD  MET A 168      73.922  32.321  65.269  1.00181.97           S  
ANISOU 1266  SD  MET A 168    22283  24102  22755  -2858   1567   -505       S  
ATOM   1267  CE  MET A 168      73.716  31.043  64.033  1.00104.18           C  
ANISOU 1267  CE  MET A 168    12359  14275  12952  -2629   1591   -382       C  
ATOM   1268  N   LEU A 169      76.717  27.979  67.146  1.00142.97           N  
ANISOU 1268  N   LEU A 169    16387  20027  17906  -2890   1306   -238       N  
ATOM   1269  CA  LEU A 169      76.132  26.810  67.791  1.00138.55           C  
ANISOU 1269  CA  LEU A 169    15742  19571  17331  -2761   1201   -203       C  
ATOM   1270  C   LEU A 169      76.963  26.326  68.972  1.00141.14           C  
ANISOU 1270  C   LEU A 169    15879  20105  17642  -2883   1079   -182       C  
ATOM   1271  O   LEU A 169      76.490  26.314  70.109  1.00147.11           O  
ANISOU 1271  O   LEU A 169    16659  20914  18320  -2936    995   -226       O  
ATOM   1272  CB  LEU A 169      75.974  25.677  66.777  1.00129.67           C  
ANISOU 1272  CB  LEU A 169    14554  18444  16272  -2552   1221   -109       C  
ATOM   1273  CG  LEU A 169      74.600  25.470  66.140  1.00120.45           C  
ANISOU 1273  CG  LEU A 169    13546  17129  15091  -2357   1257   -119       C  
ATOM   1274  CD1 LEU A 169      73.917  26.798  65.872  1.00113.62           C  
ANISOU 1274  CD1 LEU A 169    12907  16075  14188  -2394   1331   -212       C  
ATOM   1275  CD2 LEU A 169      74.750  24.677  64.853  1.00122.61           C  
ANISOU 1275  CD2 LEU A 169    13775  17377  15435  -2197   1312    -35       C  
ATOM   1276  N   ILE A 170      78.199  25.924  68.689  1.00142.22           N  
ANISOU 1276  N   ILE A 170    15827  20360  17851  -2927   1067   -120       N  
ATOM   1277  CA  ILE A 170      79.095  25.371  69.701  1.00144.22           C  
ANISOU 1277  CA  ILE A 170    15877  20814  18105  -3022    932    -89       C  
ATOM   1278  C   ILE A 170      79.290  26.314  70.886  1.00150.89           C  
ANISOU 1278  C   ILE A 170    16763  21704  18866  -3244    881   -174       C  
ATOM   1279  O   ILE A 170      79.284  25.881  72.041  1.00148.13           O  
ANISOU 1279  O   ILE A 170    16353  21477  18455  -3294    748   -169       O  
ATOM   1280  CB  ILE A 170      80.466  25.001  69.093  1.00140.60           C  
ANISOU 1280  CB  ILE A 170    15201  20465  17755  -3044    946    -35       C  
ATOM   1281  CG1 ILE A 170      80.328  23.780  68.183  1.00132.12           C  
ANISOU 1281  CG1 ILE A 170    14049  19387  16761  -2815    957     53       C  
ATOM   1282  CG2 ILE A 170      81.487  24.723  70.181  1.00145.02           C  
ANISOU 1282  CG2 ILE A 170    15558  21225  18318  -3175    800    -24       C  
ATOM   1283  CD1 ILE A 170      81.636  23.313  67.585  1.00126.85           C  
ANISOU 1283  CD1 ILE A 170    13151  18837  16210  -2816    973     92       C  
ATOM   1284  N   ALA A 171      79.449  27.602  70.595  1.00159.61           N  
ANISOU 1284  N   ALA A 171    17984  22702  19959  -3383    985   -253       N  
ATOM   1285  CA  ALA A 171      79.606  28.609  71.638  1.00163.96           C  
ANISOU 1285  CA  ALA A 171    18595  23272  20429  -3601    953   -349       C  
ATOM   1286  C   ALA A 171      78.405  28.606  72.572  1.00160.27           C  
ANISOU 1286  C   ALA A 171    18265  22773  19858  -3568    897   -408       C  
ATOM   1287  O   ALA A 171      78.553  28.712  73.789  1.00158.31           O  
ANISOU 1287  O   ALA A 171    17987  22635  19531  -3705    800   -450       O  
ATOM   1288  CB  ALA A 171      79.792  29.984  71.024  1.00167.67           C  
ANISOU 1288  CB  ALA A 171    19212  23589  20907  -3730   1086   -424       C  
ATOM   1289  N   TRP A 172      77.216  28.480  71.992  1.00162.16           N  
ANISOU 1289  N   TRP A 172    18651  22867  20096  -3391    961   -416       N  
ATOM   1290  CA  TRP A 172      75.994  28.415  72.778  1.00164.02           C  
ANISOU 1290  CA  TRP A 172    19004  23075  20242  -3344    926   -483       C  
ATOM   1291  C   TRP A 172      75.979  27.137  73.607  1.00160.65           C  
ANISOU 1291  C   TRP A 172    18443  22822  19773  -3302    792   -409       C  
ATOM   1292  O   TRP A 172      75.628  27.162  74.784  1.00164.44           O  
ANISOU 1292  O   TRP A 172    18951  23378  20150  -3396    720   -463       O  
ATOM   1293  CB  TRP A 172      74.761  28.492  71.874  1.00165.02           C  
ANISOU 1293  CB  TRP A 172    19292  23016  20392  -3149   1017   -508       C  
ATOM   1294  CG  TRP A 172      73.473  28.722  72.615  1.00169.84           C  
ANISOU 1294  CG  TRP A 172    20034  23577  20920  -3121   1010   -617       C  
ATOM   1295  CD1 TRP A 172      72.364  27.930  72.590  1.00168.68           C  
ANISOU 1295  CD1 TRP A 172    19914  23421  20757  -2952    998   -611       C  
ATOM   1296  CD2 TRP A 172      73.172  29.813  73.489  1.00179.87           C  
ANISOU 1296  CD2 TRP A 172    21420  24807  22116  -3271   1021   -759       C  
ATOM   1297  CE2 TRP A 172      71.853  29.620  73.960  1.00180.22           C  
ANISOU 1297  CE2 TRP A 172    21549  24825  22103  -3179   1020   -842       C  
ATOM   1298  CE3 TRP A 172      73.876  30.939  73.927  1.00186.29           C  
ANISOU 1298  CE3 TRP A 172    22274  25604  22905  -3480   1035   -835       C  
ATOM   1299  NE1 TRP A 172      71.384  28.462  73.392  1.00173.99           N  
ANISOU 1299  NE1 TRP A 172    20700  24057  21350  -2989   1006   -747       N  
ATOM   1300  CZ2 TRP A 172      71.234  30.504  74.837  1.00182.77           C  
ANISOU 1300  CZ2 TRP A 172    21987  25109  22350  -3280   1037  -1002       C  
ATOM   1301  CZ3 TRP A 172      73.261  31.816  74.799  1.00187.54           C  
ANISOU 1301  CZ3 TRP A 172    22560  25713  22985  -3580   1045   -987       C  
ATOM   1302  CH2 TRP A 172      71.953  31.594  75.245  1.00185.46           C  
ANISOU 1302  CH2 TRP A 172    22371  25426  22669  -3475   1048  -1073       C  
ATOM   1303  N   LEU A 173      76.378  26.030  72.987  1.00151.89           N  
ANISOU 1303  N   LEU A 173    17198  21774  18742  -3165    759   -287       N  
ATOM   1304  CA  LEU A 173      76.483  24.750  73.679  1.00144.19           C  
ANISOU 1304  CA  LEU A 173    16097  20950  17740  -3117    620   -198       C  
ATOM   1305  C   LEU A 173      77.447  24.847  74.853  1.00152.96           C  
ANISOU 1305  C   LEU A 173    17094  22228  18794  -3315    493   -198       C  
ATOM   1306  O   LEU A 173      77.133  24.418  75.963  1.00163.07           O  
ANISOU 1306  O   LEU A 173    18384  23603  19972  -3369    383   -196       O  
ATOM   1307  CB  LEU A 173      76.951  23.657  72.716  1.00131.45           C  
ANISOU 1307  CB  LEU A 173    14346  19359  16240  -2944    610    -76       C  
ATOM   1308  CG  LEU A 173      77.252  22.295  73.346  1.00125.48           C  
ANISOU 1308  CG  LEU A 173    13450  18749  15477  -2888    451     30       C  
ATOM   1309  CD1 LEU A 173      76.000  21.709  73.977  1.00122.31           C  
ANISOU 1309  CD1 LEU A 173    13166  18332  14975  -2824    409     27       C  
ATOM   1310  CD2 LEU A 173      77.835  21.338  72.319  1.00124.88           C  
ANISOU 1310  CD2 LEU A 173    13233  18684  15533  -2720    453    131       C  
ATOM   1311  N   GLU A 174      78.618  25.422  74.597  1.00147.70           N  
ANISOU 1311  N   GLU A 174    16324  21602  18192  -3432    508   -204       N  
ATOM   1312  CA  GLU A 174      79.633  25.614  75.624  1.00143.05           C  
ANISOU 1312  CA  GLU A 174    15615  21175  17563  -3629    387   -213       C  
ATOM   1313  C   GLU A 174      79.069  26.438  76.775  1.00151.14           C  
ANISOU 1313  C   GLU A 174    16785  22196  18443  -3798    368   -325       C  
ATOM   1314  O   GLU A 174      79.394  26.207  77.940  1.00154.01           O  
ANISOU 1314  O   GLU A 174    17096  22704  18718  -3921    230   -320       O  
ATOM   1315  CB  GLU A 174      80.850  26.319  75.029  1.00131.92           C  
ANISOU 1315  CB  GLU A 174    14093  19783  16246  -3742    446   -231       C  
ATOM   1316  CG  GLU A 174      82.182  25.824  75.558  1.00129.19           C  
ANISOU 1316  CG  GLU A 174    13506  19639  15942  -3830    300   -177       C  
ATOM   1317  CD  GLU A 174      83.351  26.589  74.974  1.00133.82           C  
ANISOU 1317  CD  GLU A 174    13976  20250  16620  -3963    376   -215       C  
ATOM   1318  OE1 GLU A 174      83.159  27.759  74.586  1.00135.67           O  
ANISOU 1318  OE1 GLU A 174    14355  20356  16837  -4068    517   -302       O  
ATOM   1319  OE2 GLU A 174      84.459  26.020  74.898  1.00133.98           O1-
ANISOU 1319  OE2 GLU A 174    13762  20416  16730  -3963    295   -163       O1-
ATOM   1320  N   LYS A 175      78.212  27.395  76.437  1.00152.29           N  
ANISOU 1320  N   LYS A 175    17122  22176  18567  -3800    505   -429       N  
ATOM   1321  CA  LYS A 175      77.581  28.248  77.433  1.00147.95           C  
ANISOU 1321  CA  LYS A 175    16722  21602  17891  -3944    512   -560       C  
ATOM   1322  C   LYS A 175      76.355  27.583  78.049  1.00151.87           C  
ANISOU 1322  C   LYS A 175    17307  22108  18290  -3853    478   -572       C  
ATOM   1323  O   LYS A 175      76.138  27.665  79.259  1.00164.41           O  
ANISOU 1323  O   LYS A 175    18932  23786  19748  -3988    406   -629       O  
ATOM   1324  CB  LYS A 175      77.195  29.591  76.815  1.00142.79           C  
ANISOU 1324  CB  LYS A 175    16237  20753  17264  -3978    665   -677       C  
ATOM   1325  CG  LYS A 175      76.408  30.492  77.747  1.00142.89           C  
ANISOU 1325  CG  LYS A 175    16417  20712  17161  -4096    688   -832       C  
ATOM   1326  CD  LYS A 175      76.360  31.910  77.218  1.00143.93           C  
ANISOU 1326  CD  LYS A 175    16699  20658  17330  -4167    812   -944       C  
ATOM   1327  CE  LYS A 175      77.751  32.515  77.182  1.00145.49           C  
ANISOU 1327  CE  LYS A 175    16807  20911  17563  -4364    800   -932       C  
ATOM   1328  NZ  LYS A 175      78.393  32.474  78.526  1.00148.54           N1+
ANISOU 1328  NZ  LYS A 175    17099  21488  17851  -4568    675   -960       N1+
ATOM   1329  N   GLN A 176      75.559  26.918  77.215  1.00151.94           N  
ANISOU 1329  N   GLN A 176    17347  22028  18355  -3637    534   -522       N  
ATOM   1330  CA  GLN A 176      74.346  26.249  77.681  1.00158.91           C  
ANISOU 1330  CA  GLN A 176    18308  22916  19155  -3546    518   -536       C  
ATOM   1331  C   GLN A 176      74.683  25.065  78.583  1.00164.13           C  
ANISOU 1331  C   GLN A 176    18863  23756  19743  -3579    357   -430       C  
ATOM   1332  O   GLN A 176      73.826  24.561  79.308  1.00165.62           O  
ANISOU 1332  O   GLN A 176    19117  23986  19822  -3578    324   -448       O  
ATOM   1333  CB  GLN A 176      73.488  25.787  76.497  1.00161.36           C  
ANISOU 1333  CB  GLN A 176    18664  23092  19552  -3308    609   -503       C  
ATOM   1334  CG  GLN A 176      72.073  25.355  76.861  1.00164.45           C  
ANISOU 1334  CG  GLN A 176    19156  23459  19867  -3222    629   -558       C  
ATOM   1335  CD  GLN A 176      71.160  26.525  77.183  1.00167.86           C  
ANISOU 1335  CD  GLN A 176    19746  23789  20246  -3280    725   -741       C  
ATOM   1336  NE2 GLN A 176      69.915  26.222  77.533  1.00159.96           N  
ANISOU 1336  NE2 GLN A 176    18818  22778  19181  -3217    753   -814       N  
ATOM   1337  OE1 GLN A 176      71.565  27.685  77.113  1.00174.67           O  
ANISOU 1337  OE1 GLN A 176    20661  24578  21126  -3381    774   -823       O  
ATOM   1338  N   GLN A 177      75.934  24.622  78.536  1.00165.78           N  
ANISOU 1338  N   GLN A 177    18907  24070  20010  -3610    255   -322       N  
ATOM   1339  CA  GLN A 177      76.388  23.556  79.419  1.00170.14           C  
ANISOU 1339  CA  GLN A 177    19362  24788  20498  -3645     76   -216       C  
ATOM   1340  C   GLN A 177      76.676  24.077  80.823  1.00182.81           C  
ANISOU 1340  C   GLN A 177    20995  26511  21952  -3885    -18   -283       C  
ATOM   1341  O   GLN A 177      76.808  23.300  81.766  1.00187.65           O  
ANISOU 1341  O   GLN A 177    21581  27252  22464  -3942   -170   -213       O  
ATOM   1342  CB  GLN A 177      77.626  22.863  78.849  1.00160.14           C  
ANISOU 1342  CB  GLN A 177    17894  23591  19362  -3572    -12    -86       C  
ATOM   1343  CG  GLN A 177      77.313  21.825  77.792  1.00151.52           C  
ANISOU 1343  CG  GLN A 177    16760  22430  18379  -3329     19     15       C  
ATOM   1344  CD  GLN A 177      78.241  20.633  77.867  1.00149.76           C  
ANISOU 1344  CD  GLN A 177    16359  22324  18221  -3257   -146    157       C  
ATOM   1345  NE2 GLN A 177      77.875  19.553  77.188  1.00144.56           N  
ANISOU 1345  NE2 GLN A 177    15680  21616  17631  -3053   -148    248       N  
ATOM   1346  OE1 GLN A 177      79.272  20.678  78.537  1.00155.81           O  
ANISOU 1346  OE1 GLN A 177    17005  23219  18976  -3381   -277    180       O  
ATOM   1347  N   GLN A 178      76.768  25.396  80.956  1.00183.99           N  
ANISOU 1347  N   GLN A 178    21215  26612  22083  -4030     69   -417       N  
ATOM   1348  CA  GLN A 178      77.037  26.011  82.250  1.00178.60           C  
ANISOU 1348  CA  GLN A 178    20570  26034  21256  -4269     -5   -501       C  
ATOM   1349  C   GLN A 178      75.746  26.400  82.964  1.00174.97           C  
ANISOU 1349  C   GLN A 178    20297  25532  20652  -4324     68   -633       C  
ATOM   1350  O   GLN A 178      75.669  27.445  83.610  1.00172.66           O  
ANISOU 1350  O   GLN A 178    20093  25234  20277  -4497    108   -774       O  
ATOM   1351  CB  GLN A 178      77.950  27.225  82.084  1.00176.65           C  
ANISOU 1351  CB  GLN A 178    20289  25768  21063  -4420     40   -581       C  
ATOM   1352  CG  GLN A 178      79.332  26.875  81.558  1.00176.65           C  
ANISOU 1352  CG  GLN A 178    20079  25848  21190  -4408    -40   -471       C  
ATOM   1353  CD  GLN A 178      80.165  28.100  81.254  1.00177.77           C  
ANISOU 1353  CD  GLN A 178    20195  25957  21394  -4560     33   -557       C  
ATOM   1354  NE2 GLN A 178      81.384  27.883  80.774  1.00178.49           N  
ANISOU 1354  NE2 GLN A 178    20091  26126  21601  -4567    -17   -483       N  
ATOM   1355  OE1 GLN A 178      79.718  29.231  81.446  1.00177.09           O  
ANISOU 1355  OE1 GLN A 178    20261  25773  21254  -4674    135   -695       O  
ATOM   1356  N   GLU A 179      74.733  25.549  82.840  1.00177.39           N  
ANISOU 1356  N   GLU A 179    20657  25810  20933  -4179     89   -596       N  
ATOM   1357  CA  GLU A 179      73.455  25.762  83.509  1.00181.88           C  
ANISOU 1357  CA  GLU A 179    21380  26358  21368  -4221    162   -724       C  
ATOM   1358  C   GLU A 179      72.882  24.442  84.002  1.00182.56           C  
ANISOU 1358  C   GLU A 179    21473  26532  21359  -4170     78   -626       C  
ATOM   1359  O   GLU A 179      72.200  24.391  85.026  1.00185.86           O  
ANISOU 1359  O   GLU A 179    21987  27020  21610  -4290     71   -700       O  
ATOM   1360  CB  GLU A 179      72.456  26.437  82.567  1.00181.54           C  
ANISOU 1360  CB  GLU A 179    21434  26126  21416  -4078    345   -839       C  
ATOM   1361  CG  GLU A 179      72.776  27.884  82.241  1.00182.86           C  
ANISOU 1361  CG  GLU A 179    21654  26180  21644  -4154    440   -965       C  
ATOM   1362  CD  GLU A 179      71.765  28.506  81.302  1.00180.96           C  
ANISOU 1362  CD  GLU A 179    21522  25740  21493  -3996    598  -1069       C  
ATOM   1363  OE1 GLU A 179      70.716  27.874  81.051  1.00176.76           O  
ANISOU 1363  OE1 GLU A 179    21024  25176  20961  -3846    639  -1070       O  
ATOM   1364  OE2 GLU A 179      72.018  29.627  80.812  1.00182.97           O1-
ANISOU 1364  OE2 GLU A 179    21833  25869  21818  -4025    675  -1149       O1-
ATOM   1365  N   ASN A 180      73.162  23.374  83.263  1.00176.19           N  
ANISOU 1365  N   ASN A 180    20569  25718  20655  -3997     20   -464       N  
ATOM   1366  CA  ASN A 180      72.624  22.060  83.584  1.00168.86           C  
ANISOU 1366  CA  ASN A 180    19657  24848  19655  -3931    -58   -358       C  
ATOM   1367  C   ASN A 180      73.700  21.112  84.101  1.00155.22           C  
ANISOU 1367  C   ASN A 180    17823  23253  17901  -3974   -270   -186       C  
ATOM   1368  O   ASN A 180      74.747  21.549  84.576  1.00151.02           O  
ANISOU 1368  O   ASN A 180    17220  22806  17355  -4109   -368   -179       O  
ATOM   1369  CB  ASN A 180      71.936  21.459  82.357  1.00177.95           C  
ANISOU 1369  CB  ASN A 180    20800  25873  20938  -3685     35   -312       C  
ATOM   1370  CG  ASN A 180      70.994  22.437  81.683  1.00182.52           C  
ANISOU 1370  CG  ASN A 180    21468  26307  21574  -3614    227   -473       C  
ATOM   1371  ND2 ASN A 180      70.708  22.200  80.407  1.00177.12           N  
ANISOU 1371  ND2 ASN A 180    20760  25501  21036  -3405    305   -436       N  
ATOM   1372  OD1 ASN A 180      70.528  23.395  82.300  1.00186.64           O  
ANISOU 1372  OD1 ASN A 180    22082  26823  22009  -3744    297   -633       O  
ATOM   1373  N   ASP A 188      65.713  18.372  74.321  1.00101.30           N  
ANISOU 1373  N   ASP A 188    11239  15329  11923  -2170    687   -291       N  
ATOM   1374  CA  ASP A 188      66.727  19.298  74.814  1.00125.87           C  
ANISOU 1374  CA  ASP A 188    14331  18477  15018  -2315    662   -308       C  
ATOM   1375  C   ASP A 188      66.934  20.430  73.814  1.00133.67           C  
ANISOU 1375  C   ASP A 188    15347  19330  16110  -2248    755   -370       C  
ATOM   1376  O   ASP A 188      67.056  21.594  74.196  1.00121.99           O  
ANISOU 1376  O   ASP A 188    13917  17828  14604  -2359    793   -477       O  
ATOM   1377  CB  ASP A 188      68.048  18.565  75.067  1.00138.30           C  
ANISOU 1377  CB  ASP A 188    15795  20147  16605  -2362    535   -146       C  
ATOM   1378  CG  ASP A 188      68.901  19.238  76.128  1.00144.57           C  
ANISOU 1378  CG  ASP A 188    16569  21040  17321  -2570    470   -169       C  
ATOM   1379  OD1 ASP A 188      68.691  20.437  76.403  1.00144.95           O  
ANISOU 1379  OD1 ASP A 188    16683  21055  17336  -2665    542   -305       O  
ATOM   1380  OD2 ASP A 188      69.787  18.560  76.690  1.00142.29           O1-
ANISOU 1380  OD2 ASP A 188    16201  20859  17005  -2636    339    -53       O1-
ATOM   1381  N   LEU A 189      66.978  20.080  72.531  1.00147.33           N  
ANISOU 1381  N   LEU A 189    17057  20967  17953  -2072    790   -303       N  
ATOM   1382  CA  LEU A 189      67.088  21.079  71.478  1.00145.43           C  
ANISOU 1382  CA  LEU A 189    16868  20586  17801  -2001    879   -350       C  
ATOM   1383  C   LEU A 189      65.694  21.486  71.014  1.00152.11           C  
ANISOU 1383  C   LEU A 189    17824  21315  18657  -1883    961   -473       C  
ATOM   1384  O   LEU A 189      64.925  20.669  70.507  1.00158.71           O  
ANISOU 1384  O   LEU A 189    18658  22128  19515  -1743    968   -451       O  
ATOM   1385  CB  LEU A 189      67.962  20.576  70.317  1.00127.47           C  
ANISOU 1385  CB  LEU A 189    14520  18277  15635  -1889    880   -219       C  
ATOM   1386  CG  LEU A 189      67.495  19.472  69.363  1.00115.99           C  
ANISOU 1386  CG  LEU A 189    13047  16783  14242  -1695    886   -141       C  
ATOM   1387  CD1 LEU A 189      66.934  20.080  68.088  1.00120.77           C  
ANISOU 1387  CD1 LEU A 189    13746  17227  14913  -1557    984   -192       C  
ATOM   1388  CD2 LEU A 189      68.629  18.519  69.038  1.00108.27           C  
ANISOU 1388  CD2 LEU A 189    11938  15874  13325  -1662    825      6       C  
ATOM   1389  N   GLU A 190      65.361  22.752  71.225  1.00151.68           N  
ANISOU 1389  N   GLU A 190    17860  21185  18586  -1942   1015   -612       N  
ATOM   1390  CA  GLU A 190      64.046  23.258  70.867  1.00155.44           C  
ANISOU 1390  CA  GLU A 190    18434  21548  19079  -1830   1080   -750       C  
ATOM   1391  C   GLU A 190      64.141  24.725  70.480  1.00165.92           C  
ANISOU 1391  C   GLU A 190    19868  22726  20446  -1843   1135   -846       C  
ATOM   1392  O   GLU A 190      63.581  25.146  69.469  1.00170.80           O  
ANISOU 1392  O   GLU A 190    20570  23194  21134  -1696   1177   -881       O  
ATOM   1393  CB  GLU A 190      63.072  23.072  72.028  1.00150.94           C  
ANISOU 1393  CB  GLU A 190    17866  21071  18412  -1902   1077   -869       C  
ATOM   1394  CG  GLU A 190      61.646  23.463  71.703  1.00150.16           C  
ANISOU 1394  CG  GLU A 190    17836  20877  18339  -1774   1139  -1026       C  
ATOM   1395  CD  GLU A 190      60.637  22.604  72.433  1.00159.33           C  
ANISOU 1395  CD  GLU A 190    18957  22154  19426  -1788   1138  -1085       C  
ATOM   1396  OE1 GLU A 190      59.819  23.162  73.193  1.00167.99           O  
ANISOU 1396  OE1 GLU A 190    20085  23274  20471  -1848   1180  -1260       O  
ATOM   1397  OE2 GLU A 190      60.662  21.369  72.245  1.00155.49           O1-
ANISOU 1397  OE2 GLU A 190    18410  21735  18935  -1743   1100   -963       O1-
ATOM   1398  N   GLY A 191      64.859  25.496  71.287  1.00167.45           N  
ANISOU 1398  N   GLY A 191    20070  22959  20593  -2025   1126   -885       N  
ATOM   1399  CA  GLY A 191      65.109  26.892  70.984  1.00164.81           C  
ANISOU 1399  CA  GLY A 191    19846  22481  20292  -2067   1172   -965       C  
ATOM   1400  C   GLY A 191      66.589  27.140  70.772  1.00163.22           C  
ANISOU 1400  C   GLY A 191    19603  22301  20112  -2186   1159   -854       C  
ATOM   1401  O   GLY A 191      67.102  28.203  71.106  1.00171.32           O  
ANISOU 1401  O   GLY A 191    20687  23284  21124  -2324   1176   -916       O  
ATOM   1402  N   PHE A 192      67.275  26.150  70.210  1.00154.78           N  
ANISOU 1402  N   PHE A 192    18427  21300  19081  -2134   1131   -697       N  
ATOM   1403  CA  PHE A 192      68.723  26.216  70.038  1.00150.17           C  
ANISOU 1403  CA  PHE A 192    17763  20769  18524  -2245   1116   -594       C  
ATOM   1404  C   PHE A 192      69.131  27.213  68.960  1.00154.18           C  
ANISOU 1404  C   PHE A 192    18372  21113  19096  -2235   1192   -596       C  
ATOM   1405  O   PHE A 192      69.565  28.326  69.262  1.00158.22           O  
ANISOU 1405  O   PHE A 192    18952  21572  19591  -2379   1216   -663       O  
ATOM   1406  CB  PHE A 192      69.287  24.831  69.706  1.00143.59           C  
ANISOU 1406  CB  PHE A 192    16782  20050  17726  -2171   1066   -440       C  
ATOM   1407  CG  PHE A 192      70.479  24.451  70.535  1.00135.64           C  
ANISOU 1407  CG  PHE A 192    15632  19212  16694  -2325    985   -369       C  
ATOM   1408  CD1 PHE A 192      70.352  23.563  71.590  1.00130.62           C  
ANISOU 1408  CD1 PHE A 192    14920  18723  15988  -2367    891   -341       C  
ATOM   1409  CD2 PHE A 192      71.723  24.995  70.269  1.00133.87           C  
ANISOU 1409  CD2 PHE A 192    15353  19000  16511  -2435   1000   -333       C  
ATOM   1410  CE1 PHE A 192      71.446  23.217  72.359  1.00131.16           C  
ANISOU 1410  CE1 PHE A 192    14862  18942  16032  -2501    795   -272       C  
ATOM   1411  CE2 PHE A 192      72.821  24.655  71.034  1.00133.93           C  
ANISOU 1411  CE2 PHE A 192    15214  19170  16503  -2571    913   -276       C  
ATOM   1412  CZ  PHE A 192      72.683  23.765  72.080  1.00134.67           C  
ANISOU 1412  CZ  PHE A 192    15235  19403  16529  -2597    803   -243       C  
ATOM   1413  N   TYR A 193      68.982  26.799  67.705  1.00155.60           N  
ANISOU 1413  N   TYR A 193    18572  21209  19341  -2072   1230   -521       N  
ATOM   1414  CA  TYR A 193      69.358  27.608  66.550  1.00159.14           C  
ANISOU 1414  CA  TYR A 193    19129  21500  19839  -2056   1303   -502       C  
ATOM   1415  C   TYR A 193      68.656  28.961  66.568  1.00168.37           C  
ANISOU 1415  C   TYR A 193    20492  22488  20992  -2072   1338   -634       C  
ATOM   1416  O   TYR A 193      69.173  29.948  66.045  1.00173.22           O  
ANISOU 1416  O   TYR A 193    21215  22980  21622  -2148   1387   -639       O  
ATOM   1417  CB  TYR A 193      69.008  26.862  65.260  1.00152.67           C  
ANISOU 1417  CB  TYR A 193    18319  20616  19070  -1857   1331   -419       C  
ATOM   1418  CG  TYR A 193      69.826  27.264  64.052  1.00152.35           C  
ANISOU 1418  CG  TYR A 193    18329  20485  19072  -1870   1403   -346       C  
ATOM   1419  CD1 TYR A 193      70.969  26.558  63.702  1.00152.38           C  
ANISOU 1419  CD1 TYR A 193    18180  20606  19110  -1909   1416   -238       C  
ATOM   1420  CD2 TYR A 193      69.451  28.339  63.255  1.00153.86           C  
ANISOU 1420  CD2 TYR A 193    18723  20472  19266  -1843   1457   -389       C  
ATOM   1421  CE1 TYR A 193      71.719  26.912  62.599  1.00152.22           C  
ANISOU 1421  CE1 TYR A 193    18200  20516  19120  -1936   1498   -182       C  
ATOM   1422  CE2 TYR A 193      70.198  28.701  62.146  1.00151.45           C  
ANISOU 1422  CE2 TYR A 193    18480  20084  18980  -1875   1530   -319       C  
ATOM   1423  CZ  TYR A 193      71.332  27.983  61.824  1.00147.33           C  
ANISOU 1423  CZ  TYR A 193    17796  19696  18487  -1928   1558   -220       C  
ATOM   1424  OH  TYR A 193      72.084  28.330  60.725  1.00137.69           O  
ANISOU 1424  OH  TYR A 193    16631  18407  17280  -1975   1646   -161       O  
ATOM   1425  N   ARG A 194      67.477  28.996  67.180  1.00168.59           N  
ANISOU 1425  N   ARG A 194    20565  22500  20991  -2002   1312   -745       N  
ATOM   1426  CA  ARG A 194      66.689  30.219  67.273  1.00164.68           C  
ANISOU 1426  CA  ARG A 194    20243  21835  20493  -1991   1334   -891       C  
ATOM   1427  C   ARG A 194      67.287  31.225  68.256  1.00160.89           C  
ANISOU 1427  C   ARG A 194    19794  21367  19969  -2209   1337   -976       C  
ATOM   1428  O   ARG A 194      67.437  32.401  67.928  1.00159.03           O  
ANISOU 1428  O   ARG A 194    19709  20965  19749  -2261   1371  -1029       O  
ATOM   1429  CB  ARG A 194      65.247  29.891  67.665  1.00166.33           C  
ANISOU 1429  CB  ARG A 194    20461  22046  20692  -1851   1312  -1003       C  
ATOM   1430  CG  ARG A 194      64.468  29.130  66.603  1.00168.94           C  
ANISOU 1430  CG  ARG A 194    20798  22322  21071  -1626   1310   -950       C  
ATOM   1431  CD  ARG A 194      63.768  27.922  67.201  1.00167.71           C  
ANISOU 1431  CD  ARG A 194    20511  22325  20887  -1564   1277   -957       C  
ATOM   1432  NE  ARG A 194      62.527  27.598  66.504  1.00160.50           N  
ANISOU 1432  NE  ARG A 194    19639  21329  20013  -1353   1275  -1003       N  
ATOM   1433  CZ  ARG A 194      61.742  26.573  66.818  1.00148.11           C  
ANISOU 1433  CZ  ARG A 194    17977  19870  18427  -1279   1255  -1018       C  
ATOM   1434  NH1 ARG A 194      62.075  25.766  67.815  1.00137.08           N1+
ANISOU 1434  NH1 ARG A 194    16455  18659  16969  -1397   1231   -982       N1+
ATOM   1435  NH2 ARG A 194      60.628  26.351  66.135  1.00145.65           N  
ANISOU 1435  NH2 ARG A 194    17702  19482  18158  -1092   1252  -1069       N  
ATOM   1436  N   ASP A 195      67.623  30.766  69.458  1.00162.49           N  
ANISOU 1436  N   ASP A 195    19866  21761  20112  -2341   1295   -988       N  
ATOM   1437  CA  ASP A 195      68.172  31.655  70.481  1.00161.71           C  
ANISOU 1437  CA  ASP A 195    19788  21694  19959  -2558   1289  -1076       C  
ATOM   1438  C   ASP A 195      69.571  32.145  70.134  1.00165.29           C  
ANISOU 1438  C   ASP A 195    20228  22141  20432  -2715   1309   -993       C  
ATOM   1439  O   ASP A 195      69.863  33.335  70.243  1.00170.62           O  
ANISOU 1439  O   ASP A 195    21023  22704  21103  -2839   1340  -1071       O  
ATOM   1440  CB  ASP A 195      68.194  30.980  71.853  1.00153.75           C  
ANISOU 1440  CB  ASP A 195    18650  20902  18867  -2667   1229  -1100       C  
ATOM   1441  CG  ASP A 195      66.814  30.857  72.466  1.00150.76           C  
ANISOU 1441  CG  ASP A 195    18308  20526  18447  -2581   1230  -1236       C  
ATOM   1442  OD1 ASP A 195      65.929  31.663  72.110  1.00149.32           O  
ANISOU 1442  OD1 ASP A 195    18262  20173  18301  -2483   1273  -1358       O  
ATOM   1443  OD2 ASP A 195      66.616  29.955  73.307  1.00150.26           O1-
ANISOU 1443  OD2 ASP A 195    18140  20637  18316  -2616   1186  -1223       O1-
ATOM   1444  N   ALA A 196      70.436  31.221  69.725  1.00157.91           N  
ANISOU 1444  N   ALA A 196    19144  21329  19523  -2713   1292   -845       N  
ATOM   1445  CA  ALA A 196      71.817  31.550  69.387  1.00149.36           C  
ANISOU 1445  CA  ALA A 196    18009  20274  18466  -2865   1316   -769       C  
ATOM   1446  C   ALA A 196      71.881  32.567  68.255  1.00156.99           C  
ANISOU 1446  C   ALA A 196    19154  21019  19474  -2852   1400   -775       C  
ATOM   1447  O   ALA A 196      72.839  33.332  68.145  1.00159.98           O  
ANISOU 1447  O   ALA A 196    19558  21369  19856  -3026   1437   -771       O  
ATOM   1448  CB  ALA A 196      72.583  30.294  69.019  1.00138.89           C  
ANISOU 1448  CB  ALA A 196    16487  19107  17177  -2818   1287   -622       C  
ATOM   1449  N   LYS A 197      70.852  32.565  67.415  1.00165.11           N  
ANISOU 1449  N   LYS A 197    20312  21891  20532  -2652   1425   -785       N  
ATOM   1450  CA  LYS A 197      70.736  33.536  66.338  1.00172.90           C  
ANISOU 1450  CA  LYS A 197    21505  22643  21547  -2620   1488   -791       C  
ATOM   1451  C   LYS A 197      70.503  34.937  66.895  1.00184.17           C  
ANISOU 1451  C   LYS A 197    23107  23922  22949  -2737   1496   -929       C  
ATOM   1452  O   LYS A 197      71.011  35.917  66.355  1.00192.13           O  
ANISOU 1452  O   LYS A 197    24260  24778  23963  -2839   1545   -926       O  
ATOM   1453  CB  LYS A 197      69.598  33.148  65.393  1.00164.92           C  
ANISOU 1453  CB  LYS A 197    20586  21509  20568  -2365   1489   -775       C  
ATOM   1454  CG  LYS A 197      69.366  34.129  64.259  1.00157.68           C  
ANISOU 1454  CG  LYS A 197    19907  20334  19670  -2314   1535   -775       C  
ATOM   1455  CD  LYS A 197      70.606  34.288  63.396  1.00152.41           C  
ANISOU 1455  CD  LYS A 197    19246  19657  19008  -2440   1605   -659       C  
ATOM   1456  CE  LYS A 197      70.356  35.269  62.263  1.00149.97           C  
ANISOU 1456  CE  LYS A 197    19202  19080  18699  -2402   1646   -650       C  
ATOM   1457  NZ  LYS A 197      71.553  35.447  61.396  1.00148.40           N1+
ANISOU 1457  NZ  LYS A 197    19020  18874  18492  -2546   1731   -542       N1+
ATOM   1458  N   LYS A 198      69.740  35.022  67.983  1.00180.84           N  
ANISOU 1458  N   LYS A 198    22675  23541  22494  -2729   1451  -1055       N  
ATOM   1459  CA  LYS A 198      69.423  36.304  68.607  1.00177.29           C  
ANISOU 1459  CA  LYS A 198    22384  22954  22023  -2826   1456  -1210       C  
ATOM   1460  C   LYS A 198      70.683  36.989  69.133  1.00179.63           C  
ANISOU 1460  C   LYS A 198    22664  23300  22288  -3100   1474  -1212       C  
ATOM   1461  O   LYS A 198      70.730  38.212  69.264  1.00186.28           O  
ANISOU 1461  O   LYS A 198    23675  23978  23124  -3206   1497  -1307       O  
ATOM   1462  CB  LYS A 198      68.403  36.115  69.734  1.00173.02           C  
ANISOU 1462  CB  LYS A 198    21804  22490  21447  -2774   1415  -1352       C  
ATOM   1463  CG  LYS A 198      67.907  37.409  70.361  1.00175.36           C  
ANISOU 1463  CG  LYS A 198    22265  22634  21730  -2839   1424  -1537       C  
ATOM   1464  CD  LYS A 198      67.229  38.297  69.330  1.00176.91           C  
ANISOU 1464  CD  LYS A 198    22689  22538  21990  -2689   1443  -1578       C  
ATOM   1465  CE  LYS A 198      66.737  39.594  69.954  1.00177.99           C  
ANISOU 1465  CE  LYS A 198    22995  22508  22127  -2740   1445  -1772       C  
ATOM   1466  NZ  LYS A 198      65.742  39.354  71.035  1.00176.32           N1+
ANISOU 1466  NZ  LYS A 198    22706  22399  21888  -2684   1425  -1937       N1+
ATOM   1467  N   HIS A 199      71.703  36.193  69.431  1.00173.33           N  
ANISOU 1467  N   HIS A 199    21660  22724  21475  -3212   1456  -1111       N  
ATOM   1468  CA  HIS A 199      72.995  36.734  69.830  1.00169.05           C  
ANISOU 1468  CA  HIS A 199    21068  22252  20911  -3472   1468  -1102       C  
ATOM   1469  C   HIS A 199      73.730  37.325  68.631  1.00161.61           C  
ANISOU 1469  C   HIS A 199    20228  21168  20010  -3531   1546  -1024       C  
ATOM   1470  O   HIS A 199      73.883  38.540  68.523  1.00154.58           O  
ANISOU 1470  O   HIS A 199    19520  20102  19112  -3654   1586  -1091       O  
ATOM   1471  CB  HIS A 199      73.850  35.653  70.493  1.00170.97           C  
ANISOU 1471  CB  HIS A 199    21047  22780  21135  -3555   1410  -1020       C  
ATOM   1472  CG  HIS A 199      73.502  35.402  71.927  1.00176.22           C  
ANISOU 1472  CG  HIS A 199    21636  23593  21727  -3616   1334  -1108       C  
ATOM   1473  CD2 HIS A 199      74.284  35.278  73.025  1.00177.75           C  
ANISOU 1473  CD2 HIS A 199    21694  23978  21864  -3809   1271  -1122       C  
ATOM   1474  ND1 HIS A 199      72.203  35.249  72.363  1.00179.97           N  
ANISOU 1474  ND1 HIS A 199    22177  24030  22172  -3477   1316  -1201       N  
ATOM   1475  CE1 HIS A 199      72.201  35.042  73.667  1.00180.53           C  
ANISOU 1475  CE1 HIS A 199    22167  24263  22163  -3591   1255  -1266       C  
ATOM   1476  NE2 HIS A 199      73.451  35.055  74.094  1.00179.20           N  
ANISOU 1476  NE2 HIS A 199    21882  24232  21974  -3791   1220  -1216       N  
ATOM   1477  N   TYR A 200      74.163  36.457  67.723  1.00168.03           N  
ANISOU 1477  N   TYR A 200    20931  22052  20862  -3448   1570   -886       N  
ATOM   1478  CA  TYR A 200      74.955  36.862  66.563  1.00185.65           C  
ANISOU 1478  CA  TYR A 200    23232  24186  23121  -3519   1656   -803       C  
ATOM   1479  C   TYR A 200      74.182  37.778  65.605  1.00200.45           C  
ANISOU 1479  C   TYR A 200    25400  25760  25000  -3423   1702   -827       C  
ATOM   1480  O   TYR A 200      74.003  37.445  64.434  1.00202.35           O  
ANISOU 1480  O   TYR A 200    25700  25920  25264  -3289   1742   -737       O  
ATOM   1481  CB  TYR A 200      75.462  35.615  65.826  1.00187.90           C  
ANISOU 1481  CB  TYR A 200    23325  24623  23446  -3423   1672   -666       C  
ATOM   1482  CG  TYR A 200      76.554  35.848  64.795  1.00194.86           C  
ANISOU 1482  CG  TYR A 200    24202  25484  24350  -3543   1769   -583       C  
ATOM   1483  CD1 TYR A 200      77.090  34.782  64.084  1.00195.01           C  
ANISOU 1483  CD1 TYR A 200    24045  25638  24410  -3466   1798   -474       C  
ATOM   1484  CD2 TYR A 200      77.052  37.120  64.536  1.00200.42           C  
ANISOU 1484  CD2 TYR A 200    25081  26037  25032  -3741   1838   -620       C  
ATOM   1485  CE1 TYR A 200      78.082  34.975  63.142  1.00197.96           C  
ANISOU 1485  CE1 TYR A 200    24406  26009  24801  -3583   1901   -412       C  
ATOM   1486  CE2 TYR A 200      78.042  37.323  63.594  1.00203.36           C  
ANISOU 1486  CE2 TYR A 200    25452  26401  25416  -3870   1940   -549       C  
ATOM   1487  CZ  TYR A 200      78.554  36.247  62.901  1.00203.76           C  
ANISOU 1487  CZ  TYR A 200    25314  26601  25505  -3791   1975   -449       C  
ATOM   1488  OH  TYR A 200      79.542  36.443  61.965  1.00208.35           O  
ANISOU 1488  OH  TYR A 200    25884  27185  26093  -3928   2091   -393       O  
ATOM   1489  N   ASP A 201      73.733  38.922  66.121  1.00207.19           N  
ANISOU 1489  N   ASP A 201    26443  26448  25832  -3491   1690   -950       N  
ATOM   1490  CA  ASP A 201      73.171  40.012  65.318  1.00208.96           C  
ANISOU 1490  CA  ASP A 201    26970  26363  26061  -3442   1721   -982       C  
ATOM   1491  C   ASP A 201      72.821  41.214  66.194  1.00210.44           C  
ANISOU 1491  C   ASP A 201    27319  26409  26229  -3544   1696  -1140       C  
ATOM   1492  O   ASP A 201      73.485  42.248  66.139  1.00211.01           O  
ANISOU 1492  O   ASP A 201    27530  26360  26284  -3748   1738  -1163       O  
ATOM   1493  CB  ASP A 201      71.948  39.570  64.499  1.00206.02           C  
ANISOU 1493  CB  ASP A 201    26693  25869  25717  -3144   1694   -957       C  
ATOM   1494  CG  ASP A 201      70.986  38.712  65.293  1.00202.70           C  
ANISOU 1494  CG  ASP A 201    26126  25585  25306  -2970   1623  -1022       C  
ATOM   1495  OD1 ASP A 201      71.038  38.754  66.539  1.00210.07           O  
ANISOU 1495  OD1 ASP A 201    26958  26646  26215  -3073   1590  -1116       O  
ATOM   1496  OD2 ASP A 201      70.172  37.999  64.668  1.00191.74           O1-
ANISOU 1496  OD2 ASP A 201    24730  24179  23943  -2741   1602   -980       O1-
ATOM   1497  N   GLU A 202      71.779  41.061  67.005  1.00211.66           N  
ANISOU 1497  N   GLU A 202    27454  26582  26385  -3410   1633  -1256       N  
ATOM   1498  CA  GLU A 202      71.289  42.134  67.864  1.00214.39           C  
ANISOU 1498  CA  GLU A 202    27946  26795  26717  -3473   1610  -1430       C  
ATOM   1499  C   GLU A 202      70.619  41.565  69.111  1.00212.07           C  
ANISOU 1499  C   GLU A 202    27495  26681  26401  -3416   1556  -1543       C  
ATOM   1500  O   GLU A 202      69.533  40.992  69.027  1.00208.44           O  
ANISOU 1500  O   GLU A 202    27010  26223  25964  -3188   1525  -1572       O  
ATOM   1501  CB  GLU A 202      70.293  43.011  67.101  1.00214.57           C  
ANISOU 1501  CB  GLU A 202    28256  26493  26780  -3303   1600  -1487       C  
ATOM   1502  CG  GLU A 202      70.926  44.134  66.297  1.00214.42           C  
ANISOU 1502  CG  GLU A 202    28483  26231  26758  -3444   1646  -1442       C  
ATOM   1503  CD  GLU A 202      71.430  45.262  67.175  1.00213.93           C  
ANISOU 1503  CD  GLU A 202    28517  26099  26669  -3688   1658  -1564       C  
ATOM   1504  OE1 GLU A 202      70.669  45.714  68.055  1.00213.16           O  
ANISOU 1504  OE1 GLU A 202    28467  25947  26578  -3640   1616  -1732       O  
ATOM   1505  OE2 GLU A 202      72.588  45.691  66.989  1.00212.98           O1-
ANISOU 1505  OE2 GLU A 202    28420  25982  26520  -3934   1713  -1501       O1-
ATOM   1506  N   ASP A 203      71.260  41.719  70.267  1.00211.71           N  
ANISOU 1506  N   ASP A 203    27345  26791  26304  -3633   1546  -1609       N  
ATOM   1507  CA  ASP A 203      72.563  42.364  70.367  1.00210.98           C  
ANISOU 1507  CA  ASP A 203    27263  26712  26188  -3911   1580  -1579       C  
ATOM   1508  C   ASP A 203      73.511  41.440  71.119  1.00204.39           C  
ANISOU 1508  C   ASP A 203    26147  26199  25313  -4056   1551  -1514       C  
ATOM   1509  O   ASP A 203      73.069  40.596  71.898  1.00200.83           O  
ANISOU 1509  O   ASP A 203    25544  25930  24834  -3982   1498  -1538       O  
ATOM   1510  CB  ASP A 203      72.448  43.699  71.105  1.00216.41           C  
ANISOU 1510  CB  ASP A 203    28133  27242  26852  -4060   1583  -1752       C  
ATOM   1511  CG  ASP A 203      71.022  44.216  71.163  1.00218.39           C  
ANISOU 1511  CG  ASP A 203    28562  27284  27132  -3852   1562  -1897       C  
ATOM   1512  OD1 ASP A 203      70.105  43.412  71.433  1.00218.70           O  
ANISOU 1512  OD1 ASP A 203    28496  27425  27177  -3659   1529  -1928       O  
ATOM   1513  OD2 ASP A 203      70.819  45.428  70.941  1.00218.56           O1-
ANISOU 1513  OD2 ASP A 203    28829  27038  27175  -3882   1576  -1985       O1-
ATOM   1514  N   GLU A 204      74.812  41.603  70.892  1.00205.99           N  
ANISOU 1514  N   GLU A 204    26282  26470  25514  -4265   1583  -1434       N  
ATOM   1515  CA  GLU A 204      75.804  40.745  71.530  1.00209.47           C  
ANISOU 1515  CA  GLU A 204    26448  27211  25931  -4397   1543  -1368       C  
ATOM   1516  C   GLU A 204      77.213  41.317  71.389  1.00209.82           C  
ANISOU 1516  C   GLU A 204    26455  27292  25977  -4669   1585  -1335       C  
ATOM   1517  O   GLU A 204      77.503  42.053  70.446  1.00211.18           O  
ANISOU 1517  O   GLU A 204    26786  27277  26175  -4724   1663  -1305       O  
ATOM   1518  CB  GLU A 204      75.739  39.336  70.936  1.00213.99           C  
ANISOU 1518  CB  GLU A 204    26838  27928  26539  -4203   1525  -1225       C  
ATOM   1519  CG  GLU A 204      76.196  38.234  71.873  1.00218.75           C  
ANISOU 1519  CG  GLU A 204    27171  28831  27112  -4241   1441  -1185       C  
ATOM   1520  CD  GLU A 204      77.691  38.027  71.832  1.00223.83           C  
ANISOU 1520  CD  GLU A 204    27627  29645  27773  -4432   1440  -1103       C  
ATOM   1521  OE1 GLU A 204      78.320  38.490  70.859  1.00226.72           O  
ANISOU 1521  OE1 GLU A 204    28047  29913  28182  -4499   1523  -1053       O  
ATOM   1522  OE2 GLU A 204      78.237  37.413  72.772  1.00224.42           O1-
ANISOU 1522  OE2 GLU A 204    27501  29951  27815  -4521   1353  -1093       O1-
ATOM   1523  N   GLU A 205      78.085  40.972  72.332  1.00206.08           N  
ANISOU 1523  N   GLU A 205    25771  27061  25468  -4846   1529  -1340       N  
ATOM   1524  CA  GLU A 205      79.462  41.457  72.321  1.00200.15           C  
ANISOU 1524  CA  GLU A 205    24944  26383  24721  -5119   1559  -1324       C  
ATOM   1525  C   GLU A 205      80.470  40.391  71.886  1.00193.63           C  
ANISOU 1525  C   GLU A 205    23842  25786  23942  -5121   1551  -1185       C  
ATOM   1526  O   GLU A 205      81.238  40.603  70.949  1.00190.24           O  
ANISOU 1526  O   GLU A 205    23405  25321  23557  -5204   1636  -1119       O  
ATOM   1527  CB  GLU A 205      79.843  42.027  73.691  1.00199.10           C  
ANISOU 1527  CB  GLU A 205    24780  26348  24519  -5351   1497  -1449       C  
ATOM   1528  CG  GLU A 205      79.438  41.155  74.870  1.00194.88           C  
ANISOU 1528  CG  GLU A 205    24091  26027  23928  -5285   1384  -1477       C  
ATOM   1529  CD  GLU A 205      80.043  41.627  76.175  1.00191.49           C  
ANISOU 1529  CD  GLU A 205    23603  25732  23421  -5544   1317  -1583       C  
ATOM   1530  OE1 GLU A 205      80.751  42.655  76.165  1.00188.09           O  
ANISOU 1530  OE1 GLU A 205    23253  25225  22989  -5772   1361  -1643       O  
ATOM   1531  OE2 GLU A 205      79.813  40.967  77.211  1.00192.83           O1-
ANISOU 1531  OE2 GLU A 205    23656  26086  23525  -5528   1219  -1605       O1-
ATOM   1532  N   PHE A 206      80.462  39.246  72.565  1.00193.92           N  
ANISOU 1532  N   PHE A 206    23657  26054  23969  -5033   1451  -1144       N  
ATOM   1533  CA  PHE A 206      81.429  38.187  72.290  1.00197.93           C  
ANISOU 1533  CA  PHE A 206    23886  26789  24530  -5025   1422  -1026       C  
ATOM   1534  C   PHE A 206      80.973  37.227  71.194  1.00194.24           C  
ANISOU 1534  C   PHE A 206    23387  26291  24123  -4761   1459   -908       C  
ATOM   1535  O   PHE A 206      80.878  36.019  71.415  1.00186.72           O  
ANISOU 1535  O   PHE A 206    22256  25502  23187  -4615   1381   -838       O  
ATOM   1536  CB  PHE A 206      81.757  37.406  73.564  1.00205.65           C  
ANISOU 1536  CB  PHE A 206    24642  28028  25466  -5069   1277  -1029       C  
ATOM   1537  CG  PHE A 206      82.503  38.206  74.592  1.00213.39           C  
ANISOU 1537  CG  PHE A 206    25595  29092  26390  -5355   1231  -1129       C  
ATOM   1538  CD1 PHE A 206      83.837  38.529  74.404  1.00215.91           C  
ANISOU 1538  CD1 PHE A 206    25777  29509  26750  -5570   1254  -1118       C  
ATOM   1539  CD2 PHE A 206      81.873  38.627  75.752  1.00212.01           C  
ANISOU 1539  CD2 PHE A 206    25528  28907  26121  -5416   1168  -1242       C  
ATOM   1540  CE1 PHE A 206      84.527  39.263  75.350  1.00216.11           C  
ANISOU 1540  CE1 PHE A 206    25773  29615  26723  -5840   1206  -1214       C  
ATOM   1541  CE2 PHE A 206      82.558  39.360  76.702  1.00211.30           C  
ANISOU 1541  CE2 PHE A 206    25418  28894  25972  -5685   1122  -1339       C  
ATOM   1542  CZ  PHE A 206      83.886  39.679  76.501  1.00213.28           C  
ANISOU 1542  CZ  PHE A 206    25534  29239  26265  -5897   1137  -1323       C  
ATOM   1543  N   ALA A 207      80.684  37.771  70.017  1.00196.04           N  
ANISOU 1543  N   ALA A 207    23803  26303  24380  -4705   1573   -887       N  
ATOM   1544  CA  ALA A 207      80.387  36.953  68.849  1.00189.88           C  
ANISOU 1544  CA  ALA A 207    23003  25489  23654  -4484   1622   -777       C  
ATOM   1545  C   ALA A 207      81.691  36.689  68.116  1.00188.95           C  
ANISOU 1545  C   ALA A 207    22709  25490  23594  -4595   1689   -701       C  
ATOM   1546  O   ALA A 207      81.776  35.808  67.259  1.00183.00           O  
ANISOU 1546  O   ALA A 207    21856  24783  22891  -4443   1722   -607       O  
ATOM   1547  CB  ALA A 207      79.400  37.655  67.942  1.00187.06           C  
ANISOU 1547  CB  ALA A 207    22944  24841  23289  -4365   1700   -791       C  
ATOM   1548  N   GLU A 208      82.707  37.471  68.466  1.00192.06           N  
ANISOU 1548  N   GLU A 208    23062  25934  23979  -4869   1714   -753       N  
ATOM   1549  CA  GLU A 208      84.055  37.264  67.963  1.00191.00           C  
ANISOU 1549  CA  GLU A 208    22720  25951  23901  -5014   1774   -708       C  
ATOM   1550  C   GLU A 208      84.602  35.991  68.594  1.00188.25           C  
ANISOU 1550  C   GLU A 208    22039  25890  23599  -4944   1656   -664       C  
ATOM   1551  O   GLU A 208      85.533  35.375  68.078  1.00186.67           O  
ANISOU 1551  O   GLU A 208    21616  25840  23470  -4956   1686   -610       O  
ATOM   1552  CB  GLU A 208      84.936  38.464  68.310  1.00193.02           C  
ANISOU 1552  CB  GLU A 208    23016  26191  24131  -5339   1819   -792       C  
ATOM   1553  CG  GLU A 208      86.185  38.597  67.457  1.00196.09           C  
ANISOU 1553  CG  GLU A 208    23279  26656  24571  -5512   1938   -762       C  
ATOM   1554  CD  GLU A 208      86.750  40.003  67.481  1.00198.98           C  
ANISOU 1554  CD  GLU A 208    23801  26905  24896  -5823   2022   -841       C  
ATOM   1555  OE1 GLU A 208      87.861  40.212  66.951  1.00197.85           O  
ANISOU 1555  OE1 GLU A 208    23542  26846  24787  -6019   2120   -838       O  
ATOM   1556  OE2 GLU A 208      86.077  40.903  68.028  1.00201.17           O1-
ANISOU 1556  OE2 GLU A 208    24320  27005  25111  -5874   1994   -915       O1-
ATOM   1557  N   ARG A 209      84.011  35.611  69.722  1.00185.75           N  
ANISOU 1557  N   ARG A 209    21696  25642  23238  -4873   1519   -691       N  
ATOM   1558  CA  ARG A 209      84.273  34.324  70.344  1.00181.88           C  
ANISOU 1558  CA  ARG A 209    20943  25387  22777  -4764   1385   -634       C  
ATOM   1559  C   ARG A 209      83.747  33.222  69.433  1.00176.77           C  
ANISOU 1559  C   ARG A 209    20261  24719  22184  -4486   1408   -533       C  
ATOM   1560  O   ARG A 209      84.383  32.183  69.262  1.00172.31           O  
ANISOU 1560  O   ARG A 209    19455  24324  21689  -4406   1364   -464       O  
ATOM   1561  CB  ARG A 209      83.576  34.252  71.703  1.00178.40           C  
ANISOU 1561  CB  ARG A 209    20546  24989  22251  -4757   1249   -687       C  
ATOM   1562  CG  ARG A 209      83.687  32.910  72.404  1.00175.34           C  
ANISOU 1562  CG  ARG A 209    19934  24816  21872  -4637   1095   -619       C  
ATOM   1563  CD  ARG A 209      84.504  33.023  73.681  1.00181.10           C  
ANISOU 1563  CD  ARG A 209    20511  25741  22559  -4842    961   -665       C  
ATOM   1564  NE  ARG A 209      84.006  34.080  74.558  1.00187.07           N  
ANISOU 1564  NE  ARG A 209    21460  26408  23208  -4999    955   -781       N  
ATOM   1565  CZ  ARG A 209      84.486  34.335  75.771  1.00189.94           C  
ANISOU 1565  CZ  ARG A 209    21753  26911  23503  -5188    841   -842       C  
ATOM   1566  NH1 ARG A 209      85.477  33.605  76.263  1.00189.51           N1+
ANISOU 1566  NH1 ARG A 209    21435  27090  23478  -5239    711   -790       N1+
ATOM   1567  NH2 ARG A 209      83.971  35.319  76.496  1.00190.98           N  
ANISOU 1567  NH2 ARG A 209    22079  26947  23539  -5322    852   -958       N  
ATOM   1568  N   ALA A 210      82.581  33.467  68.845  1.00174.50           N  
ANISOU 1568  N   ALA A 210    20218  24217  21867  -4336   1473   -532       N  
ATOM   1569  CA  ALA A 210      81.947  32.505  67.952  1.00173.15           C  
ANISOU 1569  CA  ALA A 210    20050  24003  21738  -4073   1498   -446       C  
ATOM   1570  C   ALA A 210      82.611  32.487  66.580  1.00179.77           C  
ANISOU 1570  C   ALA A 210    20857  24807  22639  -4074   1633   -392       C  
ATOM   1571  O   ALA A 210      82.882  31.421  66.027  1.00180.49           O  
ANISOU 1571  O   ALA A 210    20782  25000  22795  -3933   1633   -317       O  
ATOM   1572  CB  ALA A 210      80.466  32.813  67.815  1.00169.31           C  
ANISOU 1572  CB  ALA A 210    19826  23306  21198  -3918   1512   -475       C  
ATOM   1573  N   ARG A 211      82.871  33.671  66.035  1.00182.94           N  
ANISOU 1573  N   ARG A 211    21429  25063  23019  -4242   1750   -433       N  
ATOM   1574  CA  ARG A 211      83.477  33.788  64.712  1.00181.54           C  
ANISOU 1574  CA  ARG A 211    21259  24840  22879  -4277   1896   -388       C  
ATOM   1575  C   ARG A 211      84.902  33.242  64.702  1.00180.24           C  
ANISOU 1575  C   ARG A 211    20774  24919  22790  -4392   1906   -374       C  
ATOM   1576  O   ARG A 211      85.461  32.960  63.642  1.00174.67           O  
ANISOU 1576  O   ARG A 211    19998  24238  22132  -4384   2019   -334       O  
ATOM   1577  CB  ARG A 211      83.454  35.242  64.234  1.00183.64           C  
ANISOU 1577  CB  ARG A 211    21799  24886  23089  -4460   2009   -436       C  
ATOM   1578  CG  ARG A 211      82.805  35.432  62.872  1.00187.14           C  
ANISOU 1578  CG  ARG A 211    22480  25111  23513  -4336   2120   -382       C  
ATOM   1579  CD  ARG A 211      82.783  36.896  62.467  1.00193.35           C  
ANISOU 1579  CD  ARG A 211    23561  25663  24239  -4523   2213   -423       C  
ATOM   1580  NE  ARG A 211      82.249  37.080  61.121  1.00198.94           N  
ANISOU 1580  NE  ARG A 211    24504  26165  24919  -4417   2310   -362       N  
ATOM   1581  CZ  ARG A 211      82.987  37.058  60.016  1.00204.36           C  
ANISOU 1581  CZ  ARG A 211    25179  26860  25608  -4504   2444   -309       C  
ATOM   1582  NH1 ARG A 211      84.296  36.860  60.094  1.00203.99           N1+
ANISOU 1582  NH1 ARG A 211    24879  27025  25603  -4694   2504   -320       N1+
ATOM   1583  NH2 ARG A 211      82.417  37.233  58.832  1.00207.73           N  
ANISOU 1583  NH2 ARG A 211    25845  27090  25992  -4404   2518   -251       N  
ATOM   1584  N   ASN A 212      85.484  33.099  65.888  1.00185.95           N  
ANISOU 1584  N   ASN A 212    21303  25827  23525  -4501   1786   -413       N  
ATOM   1585  CA  ASN A 212      86.793  32.475  66.030  1.00193.08           C  
ANISOU 1585  CA  ASN A 212    21869  26980  24512  -4581   1758   -406       C  
ATOM   1586  C   ASN A 212      86.655  30.984  66.300  1.00189.51           C  
ANISOU 1586  C   ASN A 212    21206  26679  24119  -4340   1631   -339       C  
ATOM   1587  O   ASN A 212      87.507  30.190  65.906  1.00189.12           O  
ANISOU 1587  O   ASN A 212    20904  26789  24164  -4297   1638   -310       O  
ATOM   1588  CB  ASN A 212      87.585  33.132  67.160  1.00200.14           C  
ANISOU 1588  CB  ASN A 212    22657  27999  25387  -4838   1681   -485       C  
ATOM   1589  CG  ASN A 212      88.953  32.507  67.353  1.00205.97           C  
ANISOU 1589  CG  ASN A 212    23029  29006  26222  -4918   1633   -489       C  
ATOM   1590  ND2 ASN A 212      89.435  32.509  68.590  1.00205.60           N  
ANISOU 1590  ND2 ASN A 212    22832  29121  26167  -5034   1482   -531       N  
ATOM   1591  OD1 ASN A 212      89.567  32.023  66.402  1.00210.56           O  
ANISOU 1591  OD1 ASN A 212    23463  29654  26886  -4874   1729   -461       O  
ATOM   1592  N   TYR A 213      85.569  30.611  66.970  1.00186.69           N  
ANISOU 1592  N   TYR A 213    20958  26267  23707  -4187   1519   -320       N  
ATOM   1593  CA  TYR A 213      85.325  29.221  67.345  1.00184.64           C  
ANISOU 1593  CA  TYR A 213    20538  26131  23488  -3970   1385   -252       C  
ATOM   1594  C   TYR A 213      85.202  28.288  66.145  1.00182.32           C  
ANISOU 1594  C   TYR A 213    20194  25813  23267  -3754   1460   -179       C  
ATOM   1595  O   TYR A 213      85.413  27.082  66.266  1.00184.35           O  
ANISOU 1595  O   TYR A 213    20255  26200  23589  -3600   1367   -125       O  
ATOM   1596  CB  TYR A 213      84.065  29.115  68.202  1.00182.46           C  
ANISOU 1596  CB  TYR A 213    20430  25776  23122  -3869   1281   -255       C  
ATOM   1597  CG  TYR A 213      84.313  29.210  69.689  1.00183.13           C  
ANISOU 1597  CG  TYR A 213    20434  25995  23153  -4002   1125   -295       C  
ATOM   1598  CD1 TYR A 213      85.603  29.197  70.203  1.00185.02           C  
ANISOU 1598  CD1 TYR A 213    20434  26428  23436  -4165   1056   -311       C  
ATOM   1599  CD2 TYR A 213      83.254  29.304  70.579  1.00181.61           C  
ANISOU 1599  CD2 TYR A 213    20399  25743  22862  -3967   1046   -322       C  
ATOM   1600  CE1 TYR A 213      85.829  29.277  71.564  1.00182.83           C  
ANISOU 1600  CE1 TYR A 213    20092  26276  23098  -4291    901   -345       C  
ATOM   1601  CE2 TYR A 213      83.469  29.386  71.938  1.00179.22           C  
ANISOU 1601  CE2 TYR A 213    20037  25567  22493  -4099    907   -360       C  
ATOM   1602  CZ  TYR A 213      84.757  29.373  72.426  1.00176.02           C  
ANISOU 1602  CZ  TYR A 213    19407  25348  22124  -4260    830   -367       C  
ATOM   1603  OH  TYR A 213      84.974  29.454  73.782  1.00170.68           O  
ANISOU 1603  OH  TYR A 213    18680  24799  21372  -4396    680   -402       O  
ATOM   1604  N   VAL A 214      84.853  28.846  64.992  1.00176.92           N  
ANISOU 1604  N   VAL A 214    19699  24956  22567  -3742   1622   -179       N  
ATOM   1605  CA  VAL A 214      84.683  28.048  63.783  1.00166.99           C  
ANISOU 1605  CA  VAL A 214    18425  23662  21362  -3549   1707   -118       C  
ATOM   1606  C   VAL A 214      86.018  27.733  63.106  1.00162.44           C  
ANISOU 1606  C   VAL A 214    17602  23236  20882  -3621   1792   -121       C  
ATOM   1607  O   VAL A 214      86.233  26.617  62.631  1.00154.83           O  
ANISOU 1607  O   VAL A 214    16473  22359  19998  -3450   1784    -77       O  
ATOM   1608  CB  VAL A 214      83.718  28.729  62.782  1.00160.53           C  
ANISOU 1608  CB  VAL A 214    17923  22595  20477  -3497   1836   -112       C  
ATOM   1609  CG1 VAL A 214      84.074  30.196  62.605  1.00161.83           C  
ANISOU 1609  CG1 VAL A 214    18250  22649  20588  -3747   1943   -171       C  
ATOM   1610  CG2 VAL A 214      83.721  28.002  61.445  1.00154.76           C  
ANISOU 1610  CG2 VAL A 214    17170  21838  19792  -3339   1940    -56       C  
ATOM   1611  N   VAL A 215      86.924  28.706  63.089  1.00167.44           N  
ANISOU 1611  N   VAL A 215    18204  23904  21512  -3878   1875   -182       N  
ATOM   1612  CA  VAL A 215      88.197  28.549  62.390  1.00173.21           C  
ANISOU 1612  CA  VAL A 215    18705  24777  22331  -3977   1984   -205       C  
ATOM   1613  C   VAL A 215      89.084  27.482  63.038  1.00182.39           C  
ANISOU 1613  C   VAL A 215    19500  26192  23607  -3915   1848   -206       C  
ATOM   1614  O   VAL A 215      90.087  27.062  62.463  1.00186.14           O  
ANISOU 1614  O   VAL A 215    19737  26808  24181  -3933   1918   -228       O  
ATOM   1615  CB  VAL A 215      88.964  29.888  62.287  1.00169.57           C  
ANISOU 1615  CB  VAL A 215    18299  24297  21834  -4294   2105   -277       C  
ATOM   1616  CG1 VAL A 215      89.713  30.175  63.574  1.00167.78           C  
ANISOU 1616  CG1 VAL A 215    17886  24237  21626  -4473   1975   -336       C  
ATOM   1617  CG2 VAL A 215      89.922  29.868  61.103  1.00168.22           C  
ANISOU 1617  CG2 VAL A 215    18004  24193  21720  -4383   2291   -297       C  
ATOM   1618  N   LYS A 216      88.707  27.040  64.233  1.00184.08           N  
ANISOU 1618  N   LYS A 216    19673  26463  23807  -3840   1649   -184       N  
ATOM   1619  CA  LYS A 216      89.436  25.971  64.903  1.00183.48           C  
ANISOU 1619  CA  LYS A 216    19279  26605  23831  -3755   1487   -170       C  
ATOM   1620  C   LYS A 216      88.835  24.610  64.574  1.00179.50           C  
ANISOU 1620  C   LYS A 216    18742  26086  23375  -3452   1423    -91       C  
ATOM   1621  O   LYS A 216      89.478  23.578  64.764  1.00179.03           O  
ANISOU 1621  O   LYS A 216    18418  26183  23422  -3339   1318    -72       O  
ATOM   1622  CB  LYS A 216      89.456  26.187  66.418  1.00180.67           C  
ANISOU 1622  CB  LYS A 216    18891  26331  23424  -3858   1293   -185       C  
ATOM   1623  CG  LYS A 216      88.653  27.385  66.886  1.00176.53           C  
ANISOU 1623  CG  LYS A 216    18666  25647  22763  -4004   1321   -220       C  
ATOM   1624  CD  LYS A 216      89.532  28.385  67.624  1.00178.53           C  
ANISOU 1624  CD  LYS A 216    18845  25995  22995  -4297   1300   -303       C  
ATOM   1625  CE  LYS A 216      90.688  28.856  66.754  1.00179.32           C  
ANISOU 1625  CE  LYS A 216    18800  26163  23172  -4464   1460   -357       C  
ATOM   1626  NZ  LYS A 216      91.440  29.982  67.374  1.00181.03           N1+
ANISOU 1626  NZ  LYS A 216    18988  26439  23354  -4774   1466   -446       N1+
ATOM   1627  N   LEU A 217      87.602  24.611  64.079  1.00176.47           N  
ANISOU 1627  N   LEU A 217    18626  25508  22916  -3319   1481    -48       N  
ATOM   1628  CA  LEU A 217      86.931  23.369  63.716  1.00177.08           C  
ANISOU 1628  CA  LEU A 217    18702  25552  23029  -3042   1432     24       C  
ATOM   1629  C   LEU A 217      87.521  22.788  62.436  1.00185.44           C  
ANISOU 1629  C   LEU A 217    19626  26645  24187  -2947   1567     24       C  
ATOM   1630  O   LEU A 217      87.705  21.576  62.321  1.00188.61           O  
ANISOU 1630  O   LEU A 217    19856  27127  24681  -2757   1494     60       O  
ATOM   1631  CB  LEU A 217      85.426  23.588  63.557  1.00170.63           C  
ANISOU 1631  CB  LEU A 217    18203  24526  22103  -2938   1455     57       C  
ATOM   1632  CG  LEU A 217      84.589  22.334  63.291  1.00162.58           C  
ANISOU 1632  CG  LEU A 217    17207  23463  21105  -2665   1394    128       C  
ATOM   1633  CD1 LEU A 217      84.769  21.327  64.414  1.00163.57           C  
ANISOU 1633  CD1 LEU A 217    17155  23728  21266  -2584   1184    169       C  
ATOM   1634  CD2 LEU A 217      83.122  22.693  63.124  1.00152.95           C  
ANISOU 1634  CD2 LEU A 217    16291  22044  19779  -2587   1426    141       C  
ATOM   1635  N   GLN A 218      87.815  23.661  61.475  1.00185.60           N  
ANISOU 1635  N   GLN A 218    19735  26599  24184  -3086   1765    -19       N  
ATOM   1636  CA  GLN A 218      88.446  23.244  60.228  1.00181.26           C  
ANISOU 1636  CA  GLN A 218    19066  26091  23715  -3037   1921    -36       C  
ATOM   1637  C   GLN A 218      89.835  22.674  60.492  1.00187.97           C  
ANISOU 1637  C   GLN A 218    19535  27180  24706  -3072   1873    -84       C  
ATOM   1638  O   GLN A 218      90.257  21.719  59.839  1.00192.20           O  
ANISOU 1638  O   GLN A 218    19890  27793  25346  -2921   1907    -87       O  
ATOM   1639  CB  GLN A 218      88.528  24.412  59.242  1.00171.88           C  
ANISOU 1639  CB  GLN A 218    18068  24786  22451  -3223   2140    -73       C  
ATOM   1640  CG  GLN A 218      87.204  24.773  58.585  1.00160.11           C  
ANISOU 1640  CG  GLN A 218    16936  23051  20846  -3133   2207    -24       C  
ATOM   1641  CD  GLN A 218      86.782  23.770  57.527  1.00154.42           C  
ANISOU 1641  CD  GLN A 218    16230  22287  20156  -2900   2268     18       C  
ATOM   1642  NE2 GLN A 218      85.577  23.942  56.996  1.00149.42           N  
ANISOU 1642  NE2 GLN A 218    15888  21453  19430  -2792   2298     62       N  
ATOM   1643  OE1 GLN A 218      87.531  22.855  57.187  1.00156.29           O  
ANISOU 1643  OE1 GLN A 218    16214  22668  20500  -2815   2285      4       O  
ATOM   1644  N   SER A 219      90.541  23.266  61.450  1.00187.01           N  
ANISOU 1644  N   SER A 219    19289  27175  24590  -3267   1791   -130       N  
ATOM   1645  CA  SER A 219      91.827  22.736  61.885  1.00187.55           C  
ANISOU 1645  CA  SER A 219    18982  27480  24796  -3295   1703   -179       C  
ATOM   1646  C   SER A 219      91.600  21.394  62.567  1.00188.93           C  
ANISOU 1646  C   SER A 219    19024  27720  25043  -3044   1481   -115       C  
ATOM   1647  O   SER A 219      92.085  20.360  62.107  1.00188.77           O  
ANISOU 1647  O   SER A 219    18788  27787  25149  -2873   1469   -118       O  
ATOM   1648  CB  SER A 219      92.515  23.705  62.844  1.00187.65           C  
ANISOU 1648  CB  SER A 219    18920  27594  24784  -3565   1643   -239       C  
ATOM   1649  OG  SER A 219      91.787  23.826  64.053  1.00186.60           O  
ANISOU 1649  OG  SER A 219    18925  27412  24563  -3558   1457   -193       O  
ATOM   1650  N   GLY A 220      90.859  21.418  63.670  1.00190.10           N  
ANISOU 1650  N   GLY A 220    19308  27818  25105  -3026   1306    -60       N  
ATOM   1651  CA  GLY A 220      90.414  20.195  64.307  1.00189.97           C  
ANISOU 1651  CA  GLY A 220    19243  27820  25119  -2797   1101     18       C  
ATOM   1652  C   GLY A 220      91.222  19.753  65.509  1.00194.80           C  
ANISOU 1652  C   GLY A 220    19605  28616  25795  -2821    868     19       C  
ATOM   1653  O   GLY A 220      92.382  19.362  65.388  1.00201.89           O  
ANISOU 1653  O   GLY A 220    20198  29679  26832  -2816    841    -29       O  
ATOM   1654  N   ASP A 221      90.596  19.822  66.678  1.00193.89           N  
ANISOU 1654  N   ASP A 221    19619  28474  25574  -2847    698     68       N  
ATOM   1655  CA  ASP A 221      91.142  19.233  67.892  1.00200.26           C  
ANISOU 1655  CA  ASP A 221    20240  29432  26416  -2835    440     95       C  
ATOM   1656  C   ASP A 221      89.974  18.752  68.744  1.00197.72           C  
ANISOU 1656  C   ASP A 221    20135  29015  25975  -2735    287    188       C  
ATOM   1657  O   ASP A 221      89.031  19.508  68.980  1.00195.77           O  
ANISOU 1657  O   ASP A 221    20152  28645  25585  -2827    349    186       O  
ATOM   1658  CB  ASP A 221      92.012  20.235  68.654  1.00207.97           C  
ANISOU 1658  CB  ASP A 221    21105  30541  27372  -3106    398     20       C  
ATOM   1659  CG  ASP A 221      91.323  21.567  68.861  1.00211.25           C  
ANISOU 1659  CG  ASP A 221    21802  30835  27629  -3315    510    -15       C  
ATOM   1660  OD1 ASP A 221      90.473  21.934  68.023  1.00209.28           O  
ANISOU 1660  OD1 ASP A 221    21784  30410  27322  -3279    689    -10       O  
ATOM   1661  OD2 ASP A 221      91.634  22.249  69.861  1.00213.18           O1-
ANISOU 1661  OD2 ASP A 221    22036  31155  27808  -3512    413    -52       O1-
ATOM   1662  N   GLU A 222      90.056  17.500  69.197  1.00185.00           N  
ANISOU 1662  N   GLU A 222    19489  27473  23329    116    594   -269       N  
ATOM   1663  CA  GLU A 222      88.940  16.769  69.818  1.00189.02           C  
ANISOU 1663  CA  GLU A 222    20148  27947  23723    226    569   -144       C  
ATOM   1664  C   GLU A 222      87.926  17.599  70.611  1.00191.80           C  
ANISOU 1664  C   GLU A 222    20637  28272  23965    234    541    -75       C  
ATOM   1665  O   GLU A 222      86.729  17.307  70.590  1.00194.05           O  
ANISOU 1665  O   GLU A 222    21049  28516  24165    251    591     43       O  
ATOM   1666  CB  GLU A 222      89.461  15.630  70.699  1.00191.97           C  
ANISOU 1666  CB  GLU A 222    20499  28347  24094    389    450   -162       C  
ATOM   1667  CG  GLU A 222      88.358  14.708  71.197  1.00191.01           C  
ANISOU 1667  CG  GLU A 222    20524  28187  23865    492    441    -22       C  
ATOM   1668  CD  GLU A 222      88.774  13.877  72.390  1.00188.61           C  
ANISOU 1668  CD  GLU A 222    20233  27903  23527    655    298    -27       C  
ATOM   1669  OE1 GLU A 222      89.888  13.314  72.368  1.00189.72           O  
ANISOU 1669  OE1 GLU A 222    20255  28072  23757    705    229   -124       O  
ATOM   1670  OE2 GLU A 222      87.983  13.791  73.353  1.00183.48           O1-
ANISOU 1670  OE2 GLU A 222    19713  27241  22759    733    253     65       O1-
ATOM   1671  N   TYR A 223      88.411  18.625  71.303  1.00190.51           N  
ANISOU 1671  N   TYR A 223    20441  28133  23810    222    461   -157       N  
ATOM   1672  CA  TYR A 223      87.546  19.505  72.082  1.00190.67           C  
ANISOU 1672  CA  TYR A 223    20577  28136  23732    233    425   -115       C  
ATOM   1673  C   TYR A 223      86.441  20.115  71.225  1.00187.98           C  
ANISOU 1673  C   TYR A 223    20324  27738  23362    115    544    -35       C  
ATOM   1674  O   TYR A 223      85.260  19.976  71.534  1.00193.50           O  
ANISOU 1674  O   TYR A 223    21151  28408  23961    156    566     65       O  
ATOM   1675  CB  TYR A 223      88.363  20.606  72.758  1.00194.73           C  
ANISOU 1675  CB  TYR A 223    21021  28679  24288    220    320   -237       C  
ATOM   1676  CG  TYR A 223      87.523  21.562  73.571  1.00197.64           C  
ANISOU 1676  CG  TYR A 223    21502  29034  24559    237    273   -212       C  
ATOM   1677  CD1 TYR A 223      86.725  21.102  74.611  1.00196.20           C  
ANISOU 1677  CD1 TYR A 223    21442  28863  24242    369    223   -138       C  
ATOM   1678  CD2 TYR A 223      87.529  22.925  73.303  1.00199.24           C  
ANISOU 1678  CD2 TYR A 223    21688  29210  24804    120    278   -264       C  
ATOM   1679  CE1 TYR A 223      85.954  21.971  75.358  1.00195.31           C  
ANISOU 1679  CE1 TYR A 223    21425  28747  24036    390    184   -125       C  
ATOM   1680  CE2 TYR A 223      86.764  23.801  74.045  1.00198.48           C  
ANISOU 1680  CE2 TYR A 223    21690  29100  24624    143    227   -254       C  
ATOM   1681  CZ  TYR A 223      85.979  23.320  75.071  1.00196.25           C  
ANISOU 1681  CZ  TYR A 223    21522  28840  24204    281    182   -189       C  
ATOM   1682  OH  TYR A 223      85.215  24.192  75.811  1.00195.83           O  
ANISOU 1682  OH  TYR A 223    21560  28782  24063    309    135   -189       O  
ATOM   1683  N   PHE A 224      86.827  20.780  70.142  1.00178.64           N  
ANISOU 1683  N   PHE A 224    19072  26538  22266    -31    620    -78       N  
ATOM   1684  CA  PHE A 224      85.855  21.350  69.216  1.00168.89           C  
ANISOU 1684  CA  PHE A 224    17921  25243  21009   -146    728     -6       C  
ATOM   1685  C   PHE A 224      85.249  20.280  68.317  1.00155.37           C  
ANISOU 1685  C   PHE A 224    16249  23502  19282   -144    831     84       C  
ATOM   1686  O   PHE A 224      84.207  20.493  67.696  1.00143.63           O  
ANISOU 1686  O   PHE A 224    14859  21958  17756   -202    908    162       O  
ATOM   1687  CB  PHE A 224      86.498  22.449  68.373  1.00169.77           C  
ANISOU 1687  CB  PHE A 224    17954  25341  21211   -307    771    -76       C  
ATOM   1688  CG  PHE A 224      86.746  23.718  69.128  1.00173.07           C  
ANISOU 1688  CG  PHE A 224    18361  25756  21640   -332    678   -146       C  
ATOM   1689  CD1 PHE A 224      85.794  24.721  69.147  1.00168.93           C  
ANISOU 1689  CD1 PHE A 224    17944  25175  21066   -388    681   -106       C  
ATOM   1690  CD2 PHE A 224      87.927  23.907  69.827  1.00179.37           C  
ANISOU 1690  CD2 PHE A 224    19041  26605  22505   -295    577   -260       C  
ATOM   1691  CE1 PHE A 224      86.014  25.889  69.842  1.00168.68           C  
ANISOU 1691  CE1 PHE A 224    17904  25137  21051   -406    584   -177       C  
ATOM   1692  CE2 PHE A 224      88.153  25.076  70.525  1.00180.15           C  
ANISOU 1692  CE2 PHE A 224    19130  26696  22622   -313    480   -330       C  
ATOM   1693  CZ  PHE A 224      87.195  26.069  70.533  1.00175.01           C  
ANISOU 1693  CZ  PHE A 224    18588  25989  21920   -369    484   -288       C  
ATOM   1694  N   ARG A 225      85.909  19.130  68.248  1.00154.54           N  
ANISOU 1694  N   ARG A 225    16069  23432  19215    -73    822     65       N  
ATOM   1695  CA  ARG A 225      85.404  18.009  67.468  1.00150.37           C  
ANISOU 1695  CA  ARG A 225    15574  22878  18683    -53    902    140       C  
ATOM   1696  C   ARG A 225      84.299  17.291  68.232  1.00145.89           C  
ANISOU 1696  C   ARG A 225    15129  22281  18020     62    873    250       C  
ATOM   1697  O   ARG A 225      83.332  16.812  67.639  1.00140.17           O  
ANISOU 1697  O   ARG A 225    14483  21506  17270     52    947    340       O  
ATOM   1698  CB  ARG A 225      86.536  17.042  67.122  1.00157.59           C  
ANISOU 1698  CB  ARG A 225    16357  23838  19681    -14    894     70       C  
ATOM   1699  CG  ARG A 225      86.089  15.766  66.432  1.00164.08           C  
ANISOU 1699  CG  ARG A 225    17205  24633  20505     30    953    136       C  
ATOM   1700  CD  ARG A 225      87.286  14.952  65.976  1.00171.28           C  
ANISOU 1700  CD  ARG A 225    17974  25595  21512     57    947     44       C  
ATOM   1701  NE  ARG A 225      86.930  13.573  65.657  1.00176.05           N  
ANISOU 1701  NE  ARG A 225    18601  26173  22118    141    958    100       N  
ATOM   1702  CZ  ARG A 225      86.498  13.166  64.468  1.00174.98           C  
ANISOU 1702  CZ  ARG A 225    18481  26005  21997     90   1060    134       C  
ATOM   1703  NH1 ARG A 225      86.361  14.035  63.475  1.00173.50           N1+
ANISOU 1703  NH1 ARG A 225    18298  25812  21813    -47   1163    123       N1+
ATOM   1704  NH2 ARG A 225      86.200  11.889  64.273  1.00173.20           N  
ANISOU 1704  NH2 ARG A 225    18274  25751  21782    178   1051    178       N  
ATOM   1705  N   GLU A 226      84.441  17.221  69.552  1.00149.18           N  
ANISOU 1705  N   GLU A 226    15564  22730  18386    171    766    241       N  
ATOM   1706  CA  GLU A 226      83.404  16.623  70.380  1.00150.76           C  
ANISOU 1706  CA  GLU A 226    15885  22911  18486    275    743    349       C  
ATOM   1707  C   GLU A 226      82.176  17.517  70.367  1.00143.87           C  
ANISOU 1707  C   GLU A 226    15121  21997  17546    217    793    409       C  
ATOM   1708  O   GLU A 226      81.069  17.053  70.110  1.00140.70           O  
ANISOU 1708  O   GLU A 226    14806  21547  17105    224    856    510       O  
ATOM   1709  CB  GLU A 226      83.886  16.406  71.814  1.00166.32           C  
ANISOU 1709  CB  GLU A 226    17857  24933  20403    404    615    324       C  
ATOM   1710  CG  GLU A 226      82.904  15.619  72.667  1.00182.05           C  
ANISOU 1710  CG  GLU A 226    19971  26912  22289    514    599    445       C  
ATOM   1711  CD  GLU A 226      82.410  16.400  73.867  1.00188.82           C  
ANISOU 1711  CD  GLU A 226    20911  27799  23035    563    542    454       C  
ATOM   1712  OE1 GLU A 226      83.243  17.031  74.552  1.00195.39           O  
ANISOU 1712  OE1 GLU A 226    21695  28680  23866    592    445    356       O  
ATOM   1713  OE2 GLU A 226      81.188  16.387  74.123  1.00182.51           O1-
ANISOU 1713  OE2 GLU A 226    20219  26974  22151    575    593    552       O1-
ATOM   1714  N   MET A 227      82.387  18.807  70.620  1.00144.85           N  
ANISOU 1714  N   MET A 227    15234  22135  17668    158    760    340       N  
ATOM   1715  CA  MET A 227      81.315  19.800  70.594  1.00145.45           C  
ANISOU 1715  CA  MET A 227    15403  22169  17691    100    793    374       C  
ATOM   1716  C   MET A 227      80.577  19.807  69.256  1.00148.64           C  
ANISOU 1716  C   MET A 227    15844  22504  18128     -4    908    429       C  
ATOM   1717  O   MET A 227      79.450  20.292  69.160  1.00151.20           O  
ANISOU 1717  O   MET A 227    16261  22781  18408    -33    943    482       O  
ATOM   1718  CB  MET A 227      81.874  21.194  70.885  1.00141.31           C  
ANISOU 1718  CB  MET A 227    14840  21662  17190     39    732    273       C  
ATOM   1719  CG  MET A 227      82.496  21.362  72.267  1.00139.89           C  
ANISOU 1719  CG  MET A 227    14636  21546  16970    146    605    208       C  
ATOM   1720  SD  MET A 227      81.293  21.430  73.607  1.00215.47           S  
ANISOU 1720  SD  MET A 227    24345  31135  26390    265    561    275       S  
ATOM   1721  CE  MET A 227      81.357  19.750  74.220  1.00112.74           C  
ANISOU 1721  CE  MET A 227    11354  18159  13325    408    546    356       C  
ATOM   1722  N   TRP A 228      81.225  19.276  68.224  1.00142.61           N  
ANISOU 1722  N   TRP A 228    15006  21736  17442    -56    962    410       N  
ATOM   1723  CA  TRP A 228      80.591  19.099  66.926  1.00129.06           C  
ANISOU 1723  CA  TRP A 228    13327  19959  15752   -138   1066    462       C  
ATOM   1724  C   TRP A 228      79.748  17.829  66.912  1.00120.29           C  
ANISOU 1724  C   TRP A 228    12276  18818  14613    -53   1097    561       C  
ATOM   1725  O   TRP A 228      78.534  17.883  66.719  1.00120.08           O  
ANISOU 1725  O   TRP A 228    12344  18733  14549    -63   1140    635       O  
ATOM   1726  CB  TRP A 228      81.644  19.044  65.817  1.00131.06           C  
ANISOU 1726  CB  TRP A 228    13476  20230  16092   -225   1116    397       C  
ATOM   1727  CG  TRP A 228      81.074  18.724  64.471  1.00125.12           C  
ANISOU 1727  CG  TRP A 228    12762  19421  15355   -294   1219    446       C  
ATOM   1728  CD1 TRP A 228      80.337  19.552  63.677  1.00116.20           C  
ANISOU 1728  CD1 TRP A 228    11709  18230  14213   -398   1276    474       C  
ATOM   1729  CD2 TRP A 228      81.197  17.489  63.758  1.00124.98           C  
ANISOU 1729  CD2 TRP A 228    12713  19402  15370   -258   1266    467       C  
ATOM   1730  CE2 TRP A 228      80.507  17.640  62.540  1.00122.81           C  
ANISOU 1730  CE2 TRP A 228    12500  19067  15096   -342   1354    506       C  
ATOM   1731  CE3 TRP A 228      81.823  16.269  64.032  1.00130.00           C  
ANISOU 1731  CE3 TRP A 228    13278  20078  16038   -158   1234    452       C  
ATOM   1732  NE1 TRP A 228      79.990  18.909  62.516  1.00115.88           N  
ANISOU 1732  NE1 TRP A 228    11689  18151  14187   -427   1357    512       N  
ATOM   1733  CZ2 TRP A 228      80.425  16.620  61.597  1.00133.88           C  
ANISOU 1733  CZ2 TRP A 228    13891  20451  16525   -327   1412    527       C  
ATOM   1734  CZ3 TRP A 228      81.741  15.257  63.095  1.00133.62           C  
ANISOU 1734  CZ3 TRP A 228    13723  20516  16531   -146   1290    472       C  
ATOM   1735  CH2 TRP A 228      81.047  15.438  61.891  1.00137.54           C  
ANISOU 1735  CH2 TRP A 228    14278  20956  17024   -228   1379    508       C  
ATOM   1736  N   ARG A 229      80.399  16.690  67.128  1.00117.12           N  
ANISOU 1736  N   ARG A 229    11813  18449  14236     30   1069    557       N  
ATOM   1737  CA  ARG A 229      79.724  15.394  67.110  1.00120.40           C  
ANISOU 1737  CA  ARG A 229    12275  18831  14642    111   1088    649       C  
ATOM   1738  C   ARG A 229      78.628  15.285  68.171  1.00129.06           C  
ANISOU 1738  C   ARG A 229    13476  19911  15651    187   1064    740       C  
ATOM   1739  O   ARG A 229      77.568  14.711  67.919  1.00134.32           O  
ANISOU 1739  O   ARG A 229    14210  20520  16305    202   1114    831       O  
ATOM   1740  CB  ARG A 229      80.740  14.262  67.280  1.00124.42           C  
ANISOU 1740  CB  ARG A 229    12697  19379  15198    194   1039    618       C  
ATOM   1741  CG  ARG A 229      80.120  12.891  67.492  1.00136.63           C  
ANISOU 1741  CG  ARG A 229    14291  20886  16735    292   1033    716       C  
ATOM   1742  CD  ARG A 229      80.389  11.956  66.322  1.00152.93           C  
ANISOU 1742  CD  ARG A 229    16302  22922  18883    280   1079    705       C  
ATOM   1743  NE  ARG A 229      79.674  12.345  65.109  1.00163.56           N  
ANISOU 1743  NE  ARG A 229    17686  24215  20246    181   1176    723       N  
ATOM   1744  CZ  ARG A 229      79.693  11.645  63.979  1.00163.38           C  
ANISOU 1744  CZ  ARG A 229    17635  24160  20282    163   1227    718       C  
ATOM   1745  NH1 ARG A 229      80.392  10.521  63.910  1.00165.97           N1+
ANISOU 1745  NH1 ARG A 229    17892  24504  20665    238   1189    692       N1+
ATOM   1746  NH2 ARG A 229      79.016  12.066  62.921  1.00156.40           N  
ANISOU 1746  NH2 ARG A 229    16798  23226  19401     77   1307    734       N  
ATOM   1747  N   LYS A 230      78.893  15.833  69.353  1.00129.22           N  
ANISOU 1747  N   LYS A 230    13503  19984  15612    237    989    711       N  
ATOM   1748  CA  LYS A 230      77.905  15.868  70.426  1.00128.14           C  
ANISOU 1748  CA  LYS A 230    13462  19849  15377    306    972    785       C  
ATOM   1749  C   LYS A 230      76.652  16.593  69.960  1.00126.38           C  
ANISOU 1749  C   LYS A 230    13316  19569  15134    234   1043    824       C  
ATOM   1750  O   LYS A 230      75.533  16.147  70.203  1.00133.34           O  
ANISOU 1750  O   LYS A 230    14272  20417  15975    270   1080    916       O  
ATOM   1751  CB  LYS A 230      78.479  16.577  71.653  1.00136.15           C  
ANISOU 1751  CB  LYS A 230    14468  20934  16328    359    877    722       C  
ATOM   1752  CG  LYS A 230      77.439  17.070  72.642  1.00143.28           C  
ANISOU 1752  CG  LYS A 230    15469  21848  17121    403    871    770       C  
ATOM   1753  CD  LYS A 230      76.753  15.913  73.342  1.00151.63           C  
ANISOU 1753  CD  LYS A 230    16594  22906  18113    504    881    888       C  
ATOM   1754  CE  LYS A 230      77.765  15.030  74.053  1.00163.30           C  
ANISOU 1754  CE  LYS A 230    18036  24430  19580    605    795    881       C  
ATOM   1755  NZ  LYS A 230      78.603  15.809  75.007  1.00169.90           N1+
ANISOU 1755  NZ  LYS A 230    18848  25340  20367    650    692    785       N1+
ATOM   1756  N   LEU A 231      76.856  17.714  69.281  1.00116.13           N  
ANISOU 1756  N   LEU A 231    11998  18257  13871    129   1058    753       N  
ATOM   1757  CA  LEU A 231      75.754  18.514  68.778  1.00115.68           C  
ANISOU 1757  CA  LEU A 231    12012  18139  13804     56   1109    775       C  
ATOM   1758  C   LEU A 231      75.059  17.801  67.623  1.00114.51           C  
ANISOU 1758  C   LEU A 231    11890  17914  13704     19   1191    840       C  
ATOM   1759  O   LEU A 231      73.850  17.940  67.432  1.00109.31           O  
ANISOU 1759  O   LEU A 231    11305  17199  13029      5   1232    893       O  
ATOM   1760  CB  LEU A 231      76.269  19.878  68.326  1.00119.74           C  
ANISOU 1760  CB  LEU A 231    12498  18649  14349    -50   1092    684       C  
ATOM   1761  CG  LEU A 231      75.253  21.016  68.281  1.00125.14           C  
ANISOU 1761  CG  LEU A 231    13260  19283  15003   -103   1098    682       C  
ATOM   1762  CD1 LEU A 231      74.511  21.105  69.601  1.00124.49           C  
ANISOU 1762  CD1 LEU A 231    13233  19235  14832     -6   1059    708       C  
ATOM   1763  CD2 LEU A 231      75.962  22.319  67.981  1.00126.25           C  
ANISOU 1763  CD2 LEU A 231    13366  19423  15180   -201   1061    591       C  
ATOM   1764  N   VAL A 232      75.830  17.035  66.858  1.00117.68           N  
ANISOU 1764  N   VAL A 232    12227  18317  14169      8   1211    827       N  
ATOM   1765  CA  VAL A 232      75.294  16.310  65.712  1.00107.83           C  
ANISOU 1765  CA  VAL A 232    10998  17002  12972    -20   1280    875       C  
ATOM   1766  C   VAL A 232      74.515  15.074  66.145  1.00106.51           C  
ANISOU 1766  C   VAL A 232    10869  16806  12794     74   1287    972       C  
ATOM   1767  O   VAL A 232      73.377  14.869  65.722  1.00 99.44           O  
ANISOU 1767  O   VAL A 232    10035  15841  11908     63   1334   1034       O  
ATOM   1768  CB  VAL A 232      76.409  15.890  64.730  1.00100.66           C  
ANISOU 1768  CB  VAL A 232    10003  16112  12133    -59   1300    818       C  
ATOM   1769  CG1 VAL A 232      75.902  14.837  63.756  1.00 88.80           C  
ANISOU 1769  CG1 VAL A 232     8516  14548  10675    -49   1353    869       C  
ATOM   1770  CG2 VAL A 232      76.936  17.102  63.979  1.00104.09           C  
ANISOU 1770  CG2 VAL A 232    10413  16550  12585   -181   1322    742       C  
ATOM   1771  N   ASP A 233      75.130  14.262  66.999  1.00113.50           N  
ANISOU 1771  N   ASP A 233    11717  17742  13665    166   1236    986       N  
ATOM   1772  CA  ASP A 233      74.540  12.993  67.414  1.00111.64           C  
ANISOU 1772  CA  ASP A 233    11514  17477  13428    254   1237   1085       C  
ATOM   1773  C   ASP A 233      73.215  13.161  68.154  1.00103.78           C  
ANISOU 1773  C   ASP A 233    10606  16457  12368    280   1260   1168       C  
ATOM   1774  O   ASP A 233      72.372  12.268  68.130  1.00 97.46           O  
ANISOU 1774  O   ASP A 233     9842  15602  11585    315   1292   1259       O  
ATOM   1775  CB  ASP A 233      75.523  12.193  68.271  1.00116.06           C  
ANISOU 1775  CB  ASP A 233    12026  18095  13977    349   1162   1080       C  
ATOM   1776  CG  ASP A 233      76.730  11.723  67.484  1.00135.46           C  
ANISOU 1776  CG  ASP A 233    14385  20568  16515    339   1145   1003       C  
ATOM   1777  OD1 ASP A 233      77.027  12.324  66.430  1.00147.03           O  
ANISOU 1777  OD1 ASP A 233    15813  22026  18024    248   1188    936       O  
ATOM   1778  OD2 ASP A 233      77.385  10.753  67.920  1.00138.96           O1-
ANISOU 1778  OD2 ASP A 233    14790  21032  16977    423   1086   1009       O1-
ATOM   1779  N   ILE A 234      73.037  14.300  68.812  1.00 93.49           N  
ANISOU 1779  N   ILE A 234     9331  15193  10997    262   1244   1132       N  
ATOM   1780  CA  ILE A 234      71.786  14.580  69.506  1.00101.76           C  
ANISOU 1780  CA  ILE A 234    10453  16229  11981    284   1271   1194       C  
ATOM   1781  C   ILE A 234      70.676  14.860  68.501  1.00102.07           C  
ANISOU 1781  C   ILE A 234    10531  16180  12070    212   1339   1213       C  
ATOM   1782  O   ILE A 234      69.547  14.392  68.658  1.00109.47           O  
ANISOU 1782  O   ILE A 234    11513  17074  13007    236   1382   1292       O  
ATOM   1783  CB  ILE A 234      71.932  15.766  70.478  1.00 95.80           C  
ANISOU 1783  CB  ILE A 234     9715  15544  11140    293   1226   1134       C  
ATOM   1784  CG1 ILE A 234      72.854  15.383  71.635  1.00 98.30           C  
ANISOU 1784  CG1 ILE A 234    10010  15946  11395    384   1152   1127       C  
ATOM   1785  CG2 ILE A 234      70.578  16.180  71.031  1.00 69.47           C  
ANISOU 1785  CG2 ILE A 234     6452  12199   7747    305   1265   1180       C  
ATOM   1786  CD1 ILE A 234      72.373  14.185  72.419  1.00 91.65           C  
ANISOU 1786  CD1 ILE A 234     9208  15107  10506    477   1162   1242       C  
ATOM   1787  N   THR A 235      71.011  15.615  67.461  1.00100.36           N  
ANISOU 1787  N   THR A 235    10296  15935  11900    124   1346   1139       N  
ATOM   1788  CA  THR A 235      70.051  15.952  66.421  1.00102.63           C  
ANISOU 1788  CA  THR A 235    10626  16134  12234     54   1395   1146       C  
ATOM   1789  C   THR A 235      69.608  14.695  65.682  1.00103.63           C  
ANISOU 1789  C   THR A 235    10753  16192  12430     74   1436   1214       C  
ATOM   1790  O   THR A 235      68.423  14.509  65.402  1.00110.99           O  
ANISOU 1790  O   THR A 235    11731  17054  13389     70   1473   1263       O  
ATOM   1791  CB  THR A 235      70.648  16.940  65.408  1.00 98.10           C  
ANISOU 1791  CB  THR A 235    10038  15545  11689    -47   1392   1061       C  
ATOM   1792  CG2 THR A 235      69.549  17.557  64.560  1.00 94.01           C  
ANISOU 1792  CG2 THR A 235     9586  14937  11196   -113   1424   1063       C  
ATOM   1793  OG1 THR A 235      71.350  17.978  66.104  1.00111.63           O  
ANISOU 1793  OG1 THR A 235    11732  17326  13356    -62   1341    992       O  
ATOM   1794  N   MET A 236      70.569  13.828  65.379  1.00 91.50           N  
ANISOU 1794  N   MET A 236     9159  14675  10930     99   1421   1208       N  
ATOM   1795  CA  MET A 236      70.293  12.602  64.641  1.00 95.04           C  
ANISOU 1795  CA  MET A 236     9600  15059  11453    123   1446   1259       C  
ATOM   1796  C   MET A 236      69.632  11.534  65.504  1.00101.71           C  
ANISOU 1796  C   MET A 236    10464  15887  12295    208   1446   1362       C  
ATOM   1797  O   MET A 236      69.145  10.527  64.992  1.00106.25           O  
ANISOU 1797  O   MET A 236    11041  16391  12939    230   1464   1417       O  
ATOM   1798  CB  MET A 236      71.575  12.058  64.005  1.00 96.94           C  
ANISOU 1798  CB  MET A 236     9767  15329  11737    124   1427   1205       C  
ATOM   1799  CG  MET A 236      72.190  12.990  62.971  1.00109.57           C  
ANISOU 1799  CG  MET A 236    11346  16939  13347     28   1446   1113       C  
ATOM   1800  SD  MET A 236      70.984  13.577  61.766  1.00102.20           S  
ANISOU 1800  SD  MET A 236    10491  15902  12437    -52   1499   1121       S  
ATOM   1801  CE  MET A 236      70.439  12.035  61.047  1.00 95.81           C  
ANISOU 1801  CE  MET A 236     9681  15014  11709      5   1517   1179       C  
ATOM   1802  N   THR A 237      69.628  11.749  66.815  1.00109.11           N  
ANISOU 1802  N   THR A 237    11417  16888  13152    256   1423   1389       N  
ATOM   1803  CA  THR A 237      68.937  10.845  67.723  1.00100.31           C  
ANISOU 1803  CA  THR A 237    10332  15763  12018    328   1432   1498       C  
ATOM   1804  C   THR A 237      67.475  11.262  67.819  1.00 91.22           C  
ANISOU 1804  C   THR A 237     9235  14565  10859    303   1489   1542       C  
ATOM   1805  O   THR A 237      66.577  10.422  67.871  1.00 98.00           O  
ANISOU 1805  O   THR A 237    10112  15363  11759    327   1525   1631       O  
ATOM   1806  CB  THR A 237      69.574  10.840  69.124  1.00 96.28           C  
ANISOU 1806  CB  THR A 237     9824  15349  11411    398   1383   1512       C  
ATOM   1807  CG2 THR A 237      68.798   9.930  70.064  1.00 84.72           C  
ANISOU 1807  CG2 THR A 237     8402  13872   9914    465   1403   1638       C  
ATOM   1808  OG1 THR A 237      70.926  10.375  69.033  1.00102.15           O  
ANISOU 1808  OG1 THR A 237    10509  16129  12175    428   1322   1466       O  
ATOM   1809  N   GLN A 238      67.247  12.571  67.834  1.00 76.76           N  
ANISOU 1809  N   GLN A 238     7424  12757   8984    254   1494   1474       N  
ATOM   1810  CA  GLN A 238      65.897  13.114  67.798  1.00 88.23           C  
ANISOU 1810  CA  GLN A 238     8921  14163  10440    226   1540   1489       C  
ATOM   1811  C   GLN A 238      65.214  12.738  66.490  1.00100.35           C  
ANISOU 1811  C   GLN A 238    10460  15584  12083    181   1572   1497       C  
ATOM   1812  O   GLN A 238      64.008  12.499  66.452  1.00101.02           O  
ANISOU 1812  O   GLN A 238    10568  15607  12207    183   1613   1547       O  
ATOM   1813  CB  GLN A 238      65.938  14.636  67.937  1.00 87.45           C  
ANISOU 1813  CB  GLN A 238     8839  14103  10285    181   1520   1396       C  
ATOM   1814  CG  GLN A 238      64.590  15.313  67.768  1.00 94.16           C  
ANISOU 1814  CG  GLN A 238     9730  14898  11150    149   1555   1389       C  
ATOM   1815  CD  GLN A 238      63.682  15.104  68.960  1.00102.33           C  
ANISOU 1815  CD  GLN A 238    10783  15971  12127    207   1592   1452       C  
ATOM   1816  NE2 GLN A 238      62.482  14.596  68.710  1.00102.79           N  
ANISOU 1816  NE2 GLN A 238    10852  15957  12246    206   1647   1510       N  
ATOM   1817  OE1 GLN A 238      64.056  15.395  70.096  1.00106.86           O  
ANISOU 1817  OE1 GLN A 238    11361  16640  12601    254   1573   1447       O  
ATOM   1818  N   ASN A 239      65.999  12.688  65.418  1.00102.94           N  
ANISOU 1818  N   ASN A 239    10764  15888  12460    143   1552   1444       N  
ATOM   1819  CA  ASN A 239      65.471  12.404  64.088  1.00 92.02           C  
ANISOU 1819  CA  ASN A 239     9391  14402  11169    103   1572   1437       C  
ATOM   1820  C   ASN A 239      65.267  10.918  63.826  1.00 84.46           C  
ANISOU 1820  C   ASN A 239     8413  13387  10291    153   1581   1511       C  
ATOM   1821  O   ASN A 239      64.399  10.534  63.041  1.00 82.12           O  
ANISOU 1821  O   ASN A 239     8133  12994  10075    141   1600   1530       O  
ATOM   1822  CB  ASN A 239      66.375  12.999  63.010  1.00 90.29           C  
ANISOU 1822  CB  ASN A 239     9161  14187  10958     39   1555   1349       C  
ATOM   1823  CG  ASN A 239      66.339  14.514  62.991  1.00 93.38           C  
ANISOU 1823  CG  ASN A 239     9585  14597  11297    -27   1544   1279       C  
ATOM   1824  ND2 ASN A 239      67.347  15.123  62.379  1.00 78.16           N  
ANISOU 1824  ND2 ASN A 239     7641  12700   9358    -84   1529   1209       N  
ATOM   1825  OD1 ASN A 239      65.411  15.131  63.513  1.00100.65           O  
ANISOU 1825  OD1 ASN A 239    10544  15505  12194    -27   1550   1286       O  
ATOM   1826  N   GLN A 240      66.068  10.083  64.477  1.00 82.10           N  
ANISOU 1826  N   GLN A 240     8079  13140   9976    211   1556   1549       N  
ATOM   1827  CA  GLN A 240      65.903   8.644  64.338  1.00 85.85           C  
ANISOU 1827  CA  GLN A 240     8534  13555  10529    263   1552   1623       C  
ATOM   1828  C   GLN A 240      64.585   8.233  64.972  1.00 92.32           C  
ANISOU 1828  C   GLN A 240     9384  14324  11369    285   1591   1722       C  
ATOM   1829  O   GLN A 240      63.949   7.271  64.544  1.00 95.74           O  
ANISOU 1829  O   GLN A 240     9812  14666  11898    301   1601   1779       O  
ATOM   1830  CB  GLN A 240      67.057   7.890  64.991  1.00 75.18           C  
ANISOU 1830  CB  GLN A 240     7144  12269   9153    325   1505   1641       C  
ATOM   1831  CG  GLN A 240      67.027   6.396  64.718  1.00 80.06           C  
ANISOU 1831  CG  GLN A 240     7739  12816   9864    378   1484   1706       C  
ATOM   1832  CD  GLN A 240      67.158   6.072  63.242  1.00 92.21           C  
ANISOU 1832  CD  GLN A 240     9253  14286  11497    354   1479   1646       C  
ATOM   1833  NE2 GLN A 240      66.431   5.058  62.793  1.00 96.72           N  
ANISOU 1833  NE2 GLN A 240     9827  14755  12169    378   1480   1703       N  
ATOM   1834  OE1 GLN A 240      67.897   6.734  62.512  1.00 88.45           O  
ANISOU 1834  OE1 GLN A 240     8756  13848  11002    312   1476   1548       O  
ATOM   1835  N   ILE A 241      64.188   8.972  66.002  1.00 81.31           N  
ANISOU 1835  N   ILE A 241     8017  12992   9887    286   1614   1737       N  
ATOM   1836  CA  ILE A 241      62.892   8.784  66.632  1.00 87.15           C  
ANISOU 1836  CA  ILE A 241     8781  13700  10635    296   1666   1819       C  
ATOM   1837  C   ILE A 241      61.792   9.114  65.638  1.00 78.84           C  
ANISOU 1837  C   ILE A 241     7739  12547   9670    247   1695   1788       C  
ATOM   1838  O   ILE A 241      60.830   8.363  65.484  1.00 82.03           O  
ANISOU 1838  O   ILE A 241     8139  12866  10162    254   1725   1854       O  
ATOM   1839  CB  ILE A 241      62.726   9.708  67.845  1.00 96.09           C  
ANISOU 1839  CB  ILE A 241     9938  14931  11642    306   1685   1814       C  
ATOM   1840  CG1 ILE A 241      63.732   9.350  68.938  1.00 91.32           C  
ANISOU 1840  CG1 ILE A 241     9331  14423  10942    366   1649   1849       C  
ATOM   1841  CG2 ILE A 241      61.308   9.627  68.384  1.00 84.57           C  
ANISOU 1841  CG2 ILE A 241     8496  13442  10194    308   1752   1882       C  
ATOM   1842  CD1 ILE A 241      63.681  10.283  70.126  1.00 76.22           C  
ANISOU 1842  CD1 ILE A 241     7447  12617   8898    384   1657   1831       C  
ATOM   1843  N   THR A 242      61.945  10.249  64.965  1.00 79.92           N  
ANISOU 1843  N   THR A 242     7891  12687   9788    195   1680   1687       N  
ATOM   1844  CA  THR A 242      60.971  10.692  63.979  1.00 89.18           C  
ANISOU 1844  CA  THR A 242     9086  13764  11035    149   1691   1645       C  
ATOM   1845  C   THR A 242      60.877   9.693  62.835  1.00 86.49           C  
ANISOU 1845  C   THR A 242     8731  13320  10811    152   1678   1658       C  
ATOM   1846  O   THR A 242      59.795   9.441  62.309  1.00 85.42           O  
ANISOU 1846  O   THR A 242     8603  13084  10766    145   1692   1672       O  
ATOM   1847  CB  THR A 242      61.338  12.069  63.405  1.00 89.22           C  
ANISOU 1847  CB  THR A 242     9118  13788  10992     90   1664   1537       C  
ATOM   1848  CG2 THR A 242      60.199  12.605  62.553  1.00 81.85           C  
ANISOU 1848  CG2 THR A 242     8221  12754  10126     50   1668   1498       C  
ATOM   1849  OG1 THR A 242      61.599  12.983  64.476  1.00 91.45           O  
ANISOU 1849  OG1 THR A 242     9409  14170  11168     93   1662   1514       O  
ATOM   1850  N   TYR A 243      62.018   9.126  62.457  1.00 64.78           N  
ANISOU 1850  N   TYR A 243     5956  10594   8061    169   1646   1646       N  
ATOM   1851  CA  TYR A 243      62.058   8.114  61.408  1.00 64.51           C  
ANISOU 1851  CA  TYR A 243     5905  10473   8132    184   1626   1650       C  
ATOM   1852  C   TYR A 243      61.310   6.860  61.842  1.00 76.89           C  
ANISOU 1852  C   TYR A 243     7454  11974   9787    232   1638   1754       C  
ATOM   1853  O   TYR A 243      60.474   6.334  61.105  1.00 81.44           O  
ANISOU 1853  O   TYR A 243     8031  12441  10473    232   1637   1765       O  
ATOM   1854  CB  TYR A 243      63.505   7.754  61.068  1.00 69.89           C  
ANISOU 1854  CB  TYR A 243     6553  11212   8790    199   1591   1610       C  
ATOM   1855  CG  TYR A 243      64.266   8.834  60.335  1.00 76.50           C  
ANISOU 1855  CG  TYR A 243     7402  12095   9568    141   1584   1507       C  
ATOM   1856  CD1 TYR A 243      63.604   9.762  59.543  1.00 69.52           C  
ANISOU 1856  CD1 TYR A 243     6567  11159   8688     82   1594   1456       C  
ATOM   1857  CD2 TYR A 243      65.648   8.924  60.433  1.00 76.05           C  
ANISOU 1857  CD2 TYR A 243     7307  12130   9458    143   1564   1461       C  
ATOM   1858  CE1 TYR A 243      64.299  10.752  58.870  1.00 57.70           C  
ANISOU 1858  CE1 TYR A 243     5088   9698   7136     21   1590   1373       C  
ATOM   1859  CE2 TYR A 243      66.350   9.908  59.765  1.00 71.95           C  
ANISOU 1859  CE2 TYR A 243     6794  11652   8892     79   1566   1374       C  
ATOM   1860  CZ  TYR A 243      65.670  10.820  58.985  1.00 66.22           C  
ANISOU 1860  CZ  TYR A 243     6124  10871   8164     16   1581   1335       C  
ATOM   1861  OH  TYR A 243      66.366  11.803  58.318  1.00 84.86           O  
ANISOU 1861  OH  TYR A 243     8499  13268  10477    -55   1584   1259       O  
ATOM   1862  N   ASP A 244      61.624   6.396  63.048  1.00 82.78           N  
ANISOU 1862  N   ASP A 244     8185  12784  10482    273   1645   1831       N  
ATOM   1863  CA  ASP A 244      61.014   5.201  63.619  1.00 77.50           C  
ANISOU 1863  CA  ASP A 244     7503  12061   9884    314   1658   1947       C  
ATOM   1864  C   ASP A 244      59.505   5.355  63.721  1.00 78.77           C  
ANISOU 1864  C   ASP A 244     7674  12151  10103    289   1712   1986       C  
ATOM   1865  O   ASP A 244      58.754   4.393  63.545  1.00 71.77           O  
ANISOU 1865  O   ASP A 244     6770  11166   9334    303   1719   2054       O  
ATOM   1866  CB  ASP A 244      61.605   4.921  65.001  1.00 77.77           C  
ANISOU 1866  CB  ASP A 244     7538  12190   9822    356   1659   2021       C  
ATOM   1867  CG  ASP A 244      63.039   4.438  64.931  1.00100.82           C  
ANISOU 1867  CG  ASP A 244    10434  15158  12717    394   1595   1994       C  
ATOM   1868  OD1 ASP A 244      63.657   4.567  63.853  1.00114.84           O  
ANISOU 1868  OD1 ASP A 244    12189  16918  14527    379   1563   1903       O  
ATOM   1869  OD2 ASP A 244      63.549   3.934  65.953  1.00108.26           O1-
ANISOU 1869  OD2 ASP A 244    11377  16154  13603    442   1576   2061       O1-
ATOM   1870  N   ARG A 245      59.070   6.576  64.009  1.00 79.92           N  
ANISOU 1870  N   ARG A 245     7844  12345  10177    254   1744   1937       N  
ATOM   1871  CA  ARG A 245      57.652   6.889  64.059  1.00 85.37           C  
ANISOU 1871  CA  ARG A 245     8537  12976  10922    230   1792   1949       C  
ATOM   1872  C   ARG A 245      57.073   6.868  62.656  1.00 92.56           C  
ANISOU 1872  C   ARG A 245     9450  13763  11955    205   1764   1886       C  
ATOM   1873  O   ARG A 245      55.936   6.452  62.440  1.00 81.69           O  
ANISOU 1873  O   ARG A 245     8057  12289  10691    202   1784   1916       O  
ATOM   1874  CB  ARG A 245      57.437   8.268  64.678  1.00 82.55           C  
ANISOU 1874  CB  ARG A 245     8205  12706  10454    205   1819   1893       C  
ATOM   1875  CG  ARG A 245      57.442   8.271  66.187  1.00 81.78           C  
ANISOU 1875  CG  ARG A 245     8108  12713  10251    233   1865   1966       C  
ATOM   1876  CD  ARG A 245      56.141   8.856  66.715  1.00 76.16           C  
ANISOU 1876  CD  ARG A 245     7394  12002   9541    218   1929   1967       C  
ATOM   1877  NE  ARG A 245      56.098  10.306  66.570  1.00 63.41           N  
ANISOU 1877  NE  ARG A 245     5802  10428   7861    189   1910   1851       N  
ATOM   1878  CZ  ARG A 245      54.999  11.035  66.722  1.00 78.59           C  
ANISOU 1878  CZ  ARG A 245     7723  12338   9800    172   1945   1810       C  
ATOM   1879  NH1 ARG A 245      53.847  10.447  67.007  1.00 55.90           N1+
ANISOU 1879  NH1 ARG A 245     4817   9416   7007    177   2008   1873       N1+
ATOM   1880  NH2 ARG A 245      55.052  12.351  66.581  1.00 68.40           N  
ANISOU 1880  NH2 ARG A 245     6457  11078   8452    150   1912   1702       N  
ATOM   1881  N   LEU A 246      57.881   7.314  61.703  1.00 95.58           N  
ANISOU 1881  N   LEU A 246     9852  14150  12314    188   1716   1797       N  
ATOM   1882  CA  LEU A 246      57.439   7.498  60.331  1.00 84.41           C  
ANISOU 1882  CA  LEU A 246     8457  12632  10983    165   1683   1724       C  
ATOM   1883  C   LEU A 246      57.553   6.196  59.551  1.00 85.38           C  
ANISOU 1883  C   LEU A 246     8555  12665  11221    199   1648   1749       C  
ATOM   1884  O   LEU A 246      57.120   6.112  58.403  1.00 95.73           O  
ANISOU 1884  O   LEU A 246     9880  13878  12614    193   1616   1696       O  
ATOM   1885  CB  LEU A 246      58.292   8.578  59.669  1.00 70.53           C  
ANISOU 1885  CB  LEU A 246     6738  10926   9136    126   1654   1623       C  
ATOM   1886  CG  LEU A 246      57.654   9.552  58.685  1.00 73.05           C  
ANISOU 1886  CG  LEU A 246     7107  11175   9472     81   1632   1538       C  
ATOM   1887  CD1 LEU A 246      56.182   9.715  58.976  1.00 69.18           C  
ANISOU 1887  CD1 LEU A 246     6616  10614   9055     81   1653   1553       C  
ATOM   1888  CD2 LEU A 246      58.362  10.879  58.821  1.00 69.40           C  
ANISOU 1888  CD2 LEU A 246     6680  10802   8887     35   1626   1473       C  
ATOM   1889  N   ASN A 247      58.136   5.188  60.194  1.00 80.57           N  
ANISOU 1889  N   ASN A 247     7910  12086  10615    241   1647   1827       N  
ATOM   1890  CA  ASN A 247      58.407   3.892  59.575  1.00 76.75           C  
ANISOU 1890  CA  ASN A 247     7398  11526  10237    283   1603   1851       C  
ATOM   1891  C   ASN A 247      59.360   3.998  58.383  1.00 87.43           C  
ANISOU 1891  C   ASN A 247     8760  12886  11574    284   1555   1751       C  
ATOM   1892  O   ASN A 247      59.250   3.254  57.408  1.00 96.86           O  
ANISOU 1892  O   ASN A 247     9944  13989  12867    310   1514   1726       O  
ATOM   1893  CB  ASN A 247      57.106   3.179  59.190  1.00 70.79           C  
ANISOU 1893  CB  ASN A 247     6627  10629   9640    291   1601   1889       C  
ATOM   1894  CG  ASN A 247      57.287   1.681  59.024  1.00 89.01           C  
ANISOU 1894  CG  ASN A 247     8897  12861  12064    342   1559   1950       C  
ATOM   1895  ND2 ASN A 247      56.355   1.046  58.325  1.00 98.34           N  
ANISOU 1895  ND2 ASN A 247    10062  13905  13398    352   1534   1953       N  
ATOM   1896  OD1 ASN A 247      58.253   1.103  59.518  1.00 82.56           O  
ANISOU 1896  OD1 ASN A 247     8063  12101  11204    375   1540   1990       O  
ATOM   1897  N   VAL A 248      60.298   4.935  58.477  1.00 75.64           N  
ANISOU 1897  N   VAL A 248     7284  11503   9955    256   1562   1693       N  
ATOM   1898  CA  VAL A 248      61.329   5.106  57.466  1.00 64.91           C  
ANISOU 1898  CA  VAL A 248     5927  10174   8562    249   1533   1602       C  
ATOM   1899  C   VAL A 248      62.524   4.216  57.795  1.00 72.65           C  
ANISOU 1899  C   VAL A 248     6856  11214   9532    298   1506   1619       C  
ATOM   1900  O   VAL A 248      62.926   4.115  58.949  1.00 99.55           O  
ANISOU 1900  O   VAL A 248    10244  14693  12887    317   1514   1675       O  
ATOM   1901  CB  VAL A 248      61.775   6.573  57.393  1.00 72.38           C  
ANISOU 1901  CB  VAL A 248     6909  11204   9388    186   1554   1531       C  
ATOM   1902  CG1 VAL A 248      62.865   6.755  56.355  1.00 80.68           C  
ANISOU 1902  CG1 VAL A 248     7960  12294  10401    168   1537   1444       C  
ATOM   1903  CG2 VAL A 248      60.590   7.455  57.072  1.00 71.39           C  
ANISOU 1903  CG2 VAL A 248     6837  11011   9276    143   1566   1510       C  
ATOM   1904  N   THR A 249      63.089   3.575  56.776  1.00 73.24           N  
ANISOU 1904  N   THR A 249     6910  11261   9657    325   1469   1563       N  
ATOM   1905  CA  THR A 249      64.142   2.583  56.975  1.00 76.48           C  
ANISOU 1905  CA  THR A 249     7265  11710  10086    384   1430   1569       C  
ATOM   1906  C   THR A 249      65.530   3.183  57.201  1.00 88.98           C  
ANISOU 1906  C   THR A 249     8822  13428  11559    368   1436   1507       C  
ATOM   1907  O   THR A 249      66.524   2.460  57.243  1.00100.23           O  
ANISOU 1907  O   THR A 249    10195  14893  12996    416   1399   1486       O  
ATOM   1908  CB  THR A 249      64.210   1.610  55.785  1.00 67.07           C  
ANISOU 1908  CB  THR A 249     6051  10436   8996    428   1383   1521       C  
ATOM   1909  CG2 THR A 249      62.845   1.008  55.515  1.00 61.84           C  
ANISOU 1909  CG2 THR A 249     5407   9631   8458    444   1368   1573       C  
ATOM   1910  OG1 THR A 249      64.654   2.314  54.619  1.00 75.80           O  
ANISOU 1910  OG1 THR A 249     7177  11574  10050    391   1396   1412       O  
ATOM   1911  N   LEU A 250      65.597   4.502  57.344  1.00 81.61           N  
ANISOU 1911  N   LEU A 250     7922  12561  10527    302   1476   1472       N  
ATOM   1912  CA  LEU A 250      66.873   5.174  57.558  1.00 83.85           C  
ANISOU 1912  CA  LEU A 250     8177  12966  10715    277   1483   1411       C  
ATOM   1913  C   LEU A 250      67.497   4.798  58.892  1.00 96.40           C  
ANISOU 1913  C   LEU A 250     9729  14627  12272    324   1460   1462       C  
ATOM   1914  O   LEU A 250      66.804   4.386  59.819  1.00105.42           O  
ANISOU 1914  O   LEU A 250    10888  15738  13430    355   1457   1557       O  
ATOM   1915  CB  LEU A 250      66.710   6.691  57.460  1.00 82.26           C  
ANISOU 1915  CB  LEU A 250     8024  12804  10428    194   1522   1369       C  
ATOM   1916  CG  LEU A 250      66.768   7.265  56.046  1.00 83.59           C  
ANISOU 1916  CG  LEU A 250     8224  12948  10588    138   1539   1287       C  
ATOM   1917  CD1 LEU A 250      66.422   8.732  56.074  1.00 84.12           C  
ANISOU 1917  CD1 LEU A 250     8350  13031  10581     57   1565   1265       C  
ATOM   1918  CD2 LEU A 250      68.149   7.056  55.456  1.00 87.14           C  
ANISOU 1918  CD2 LEU A 250     8617  13476  11017    139   1538   1210       C  
ATOM   1919  N   THR A 251      68.813   4.951  58.979  1.00 98.67           N  
ANISOU 1919  N   THR A 251     9967  15012  12513    328   1443   1399       N  
ATOM   1920  CA  THR A 251      69.544   4.596  60.183  1.00104.41           C  
ANISOU 1920  CA  THR A 251    10658  15808  13206    380   1406   1432       C  
ATOM   1921  C   THR A 251      70.656   5.612  60.428  1.00121.60           C  
ANISOU 1921  C   THR A 251    12805  18102  15296    340   1411   1352       C  
ATOM   1922  O   THR A 251      70.892   6.489  59.600  1.00126.22           O  
ANISOU 1922  O   THR A 251    13393  18711  15855    270   1447   1275       O  
ATOM   1923  CB  THR A 251      70.148   3.189  60.055  1.00102.39           C  
ANISOU 1923  CB  THR A 251    10346  15527  13030    461   1347   1436       C  
ATOM   1924  CG2 THR A 251      70.207   2.508  61.412  1.00115.22           C  
ANISOU 1924  CG2 THR A 251    11972  17160  14646    528   1301   1530       C  
ATOM   1925  OG1 THR A 251      69.342   2.402  59.169  1.00107.67           O  
ANISOU 1925  OG1 THR A 251    11029  16082  13799    478   1343   1456       O  
ATOM   1926  N   ARG A 252      71.326   5.503  61.571  1.00123.79           N  
ANISOU 1926  N   ARG A 252    13056  18449  15529    384   1372   1370       N  
ATOM   1927  CA  ARG A 252      72.450   6.378  61.879  1.00118.27           C  
ANISOU 1927  CA  ARG A 252    12316  17859  14763    356   1364   1289       C  
ATOM   1928  C   ARG A 252      73.619   6.101  60.947  1.00119.83           C  
ANISOU 1928  C   ARG A 252    12433  18095  15003    353   1354   1184       C  
ATOM   1929  O   ARG A 252      74.213   7.026  60.395  1.00123.51           O  
ANISOU 1929  O   ARG A 252    12875  18616  15439    282   1387   1100       O  
ATOM   1930  CB  ARG A 252      72.891   6.222  63.334  1.00119.21           C  
ANISOU 1930  CB  ARG A 252    12428  18037  14828    418   1311   1330       C  
ATOM   1931  CG  ARG A 252      71.997   6.926  64.331  1.00124.55           C  
ANISOU 1931  CG  ARG A 252    13176  18720  15427    405   1333   1400       C  
ATOM   1932  CD  ARG A 252      71.166   5.935  65.120  1.00135.56           C  
ANISOU 1932  CD  ARG A 252    14613  20059  16834    471   1320   1526       C  
ATOM   1933  NE  ARG A 252      70.452   6.579  66.217  1.00141.04           N  
ANISOU 1933  NE  ARG A 252    15366  20783  17439    469   1343   1587       N  
ATOM   1934  CZ  ARG A 252      71.002   6.879  67.390  1.00154.08           C  
ANISOU 1934  CZ  ARG A 252    17024  22519  19001    508   1305   1591       C  
ATOM   1935  NH1 ARG A 252      72.278   6.597  67.618  1.00156.24           N1+
ANISOU 1935  NH1 ARG A 252    17245  22849  19271    552   1237   1536       N1+
ATOM   1936  NH2 ARG A 252      70.277   7.465  68.333  1.00160.91           N  
ANISOU 1936  NH2 ARG A 252    17945  23413  19780    508   1332   1641       N  
ATOM   1937  N   ASP A 253      73.947   4.826  60.765  1.00122.26           N  
ANISOU 1937  N   ASP A 253    12698  18373  15384    429   1308   1189       N  
ATOM   1938  CA  ASP A 253      75.004   4.452  59.828  1.00123.66           C  
ANISOU 1938  CA  ASP A 253    12790  18586  15608    436   1301   1082       C  
ATOM   1939  C   ASP A 253      74.518   4.485  58.381  1.00117.00           C  
ANISOU 1939  C   ASP A 253    11967  17690  14799    388   1356   1046       C  
ATOM   1940  O   ASP A 253      74.807   3.590  57.589  1.00123.91           O  
ANISOU 1940  O   ASP A 253    12799  18540  15741    432   1339   1002       O  
ATOM   1941  CB  ASP A 253      75.613   3.092  60.178  1.00129.60           C  
ANISOU 1941  CB  ASP A 253    13485  19329  16429    542   1218   1084       C  
ATOM   1942  CG  ASP A 253      74.574   2.070  60.585  1.00140.71           C  
ANISOU 1942  CG  ASP A 253    14949  20628  17887    604   1183   1206       C  
ATOM   1943  OD1 ASP A 253      73.380   2.272  60.280  1.00149.88           O  
ANISOU 1943  OD1 ASP A 253    16180  21716  19052    566   1230   1269       O  
ATOM   1944  OD2 ASP A 253      74.957   1.060  61.211  1.00141.20           O1-
ANISOU 1944  OD2 ASP A 253    14985  20674  17989    691   1104   1238       O1-
ATOM   1945  N   ASP A 254      73.762   5.530  58.063  1.00102.81           N  
ANISOU 1945  N   ASP A 254    10239  15872  12952    305   1415   1062       N  
ATOM   1946  CA  ASP A 254      73.353   5.834  56.703  1.00 90.42           C  
ANISOU 1946  CA  ASP A 254     8703  14262  11391    248   1467   1021       C  
ATOM   1947  C   ASP A 254      73.626   7.312  56.472  1.00 94.68           C  
ANISOU 1947  C   ASP A 254     9264  14859  11850    141   1521    975       C  
ATOM   1948  O   ASP A 254      73.280   7.872  55.433  1.00104.54           O  
ANISOU 1948  O   ASP A 254    10559  16080  13081     75   1568    947       O  
ATOM   1949  CB  ASP A 254      71.869   5.533  56.502  1.00 68.73           C  
ANISOU 1949  CB  ASP A 254     6039  11394   8681    258   1469   1103       C  
ATOM   1950  CG  ASP A 254      71.597   4.059  56.277  1.00 86.23           C  
ANISOU 1950  CG  ASP A 254     8232  13534  10996    349   1421   1132       C  
ATOM   1951  OD1 ASP A 254      72.486   3.367  55.737  1.00105.73           O  
ANISOU 1951  OD1 ASP A 254    10634  16035  13504    390   1399   1062       O  
ATOM   1952  OD2 ASP A 254      70.494   3.592  56.634  1.00 90.96           O1-
ANISOU 1952  OD2 ASP A 254     8879  14040  11641    378   1405   1222       O1-
ATOM   1953  N   VAL A 255      74.256   7.936  57.462  1.00 94.91           N  
ANISOU 1953  N   VAL A 255     9263  14965  11832    128   1507    966       N  
ATOM   1954  CA  VAL A 255      74.551   9.361  57.417  1.00 97.75           C  
ANISOU 1954  CA  VAL A 255     9638  15376  12125     28   1545    926       C  
ATOM   1955  C   VAL A 255      75.875   9.644  56.716  1.00107.46           C  
ANISOU 1955  C   VAL A 255    10784  16692  13352    -21   1576    822       C  
ATOM   1956  O   VAL A 255      76.930   9.174  57.140  1.00107.31           O  
ANISOU 1956  O   VAL A 255    10671  16745  13358     25   1544    773       O  
ATOM   1957  CB  VAL A 255      74.592   9.967  58.830  1.00 95.96           C  
ANISOU 1957  CB  VAL A 255     9417  15191  11852     37   1509    958       C  
ATOM   1958  CG1 VAL A 255      75.202  11.356  58.793  1.00 90.11           C  
ANISOU 1958  CG1 VAL A 255     8666  14512  11059    -59   1533    896       C  
ATOM   1959  CG2 VAL A 255      73.196  10.005  59.428  1.00 91.86           C  
ANISOU 1959  CG2 VAL A 255     8987  14596  11318     59   1502   1054       C  
ATOM   1960  N   MET A 256      75.803  10.415  55.637  1.00110.17           N  
ANISOU 1960  N   MET A 256    11164  17028  13667   -115   1637    788       N  
ATOM   1961  CA  MET A 256      76.982  10.818  54.885  1.00101.27           C  
ANISOU 1961  CA  MET A 256     9965  15984  12529   -182   1687    695       C  
ATOM   1962  C   MET A 256      76.830  12.274  54.478  1.00104.06           C  
ANISOU 1962  C   MET A 256    10381  16334  12821   -309   1736    691       C  
ATOM   1963  O   MET A 256      76.661  12.584  53.302  1.00116.41           O  
ANISOU 1963  O   MET A 256    11994  17876  14362   -375   1792    676       O  
ATOM   1964  CB  MET A 256      77.142   9.940  53.646  1.00 94.94           C  
ANISOU 1964  CB  MET A 256     9141  15174  11757   -157   1721    652       C  
ATOM   1965  CG  MET A 256      77.525   8.505  53.953  1.00100.39           C  
ANISOU 1965  CG  MET A 256     9751  15874  12519    -34   1666    636       C  
ATOM   1966  SD  MET A 256      76.925   7.358  52.705  1.00102.00           S  
ANISOU 1966  SD  MET A 256     9985  16004  12767     26   1673    628       S  
ATOM   1967  CE  MET A 256      77.515   8.161  51.225  1.00198.62           C  
ANISOU 1967  CE  MET A 256    22221  28302  24942    -85   1777    544       C  
ATOM   1968  N   GLY A 257      76.886  13.163  55.462  1.00 93.13           N  
ANISOU 1968  N   GLY A 257     9003  14970  11411   -340   1707    705       N  
ATOM   1969  CA  GLY A 257      76.595  14.565  55.237  1.00105.36           C  
ANISOU 1969  CA  GLY A 257    10623  16498  12911   -453   1732    711       C  
ATOM   1970  C   GLY A 257      77.774  15.407  54.798  1.00117.84           C  
ANISOU 1970  C   GLY A 257    12140  18155  14479   -558   1779    639       C  
ATOM   1971  O   GLY A 257      78.839  14.887  54.468  1.00127.56           O  
ANISOU 1971  O   GLY A 257    13266  19462  15739   -550   1807    575       O  
ATOM   1972  N   GLU A 258      77.578  16.722  54.805  1.00117.90           N  
ANISOU 1972  N   GLU A 258    12206  18139  14450   -658   1784    648       N  
ATOM   1973  CA  GLU A 258      78.602  17.675  54.383  1.00121.56           C  
ANISOU 1973  CA  GLU A 258    12621  18661  14906   -778   1830    592       C  
ATOM   1974  C   GLU A 258      79.830  17.655  55.288  1.00133.78           C  
ANISOU 1974  C   GLU A 258    14030  20305  16493   -758   1800    528       C  
ATOM   1975  O   GLU A 258      80.208  18.675  55.858  1.00142.94           O  
ANISOU 1975  O   GLU A 258    15173  21484  17654   -820   1774    508       O  
ATOM   1976  CB  GLU A 258      78.021  19.090  54.344  1.00116.70           C  
ANISOU 1976  CB  GLU A 258    12107  17982  14251   -881   1820    623       C  
ATOM   1977  CG  GLU A 258      76.748  19.224  53.528  1.00122.75           C  
ANISOU 1977  CG  GLU A 258    13017  18641  14981   -899   1831    683       C  
ATOM   1978  CD  GLU A 258      76.145  20.611  53.625  1.00138.96           C  
ANISOU 1978  CD  GLU A 258    15170  20624  17004   -986   1800    708       C  
ATOM   1979  OE1 GLU A 258      76.848  21.531  54.090  1.00140.86           O  
ANISOU 1979  OE1 GLU A 258    15367  20902  17250  -1056   1785    677       O  
ATOM   1980  OE2 GLU A 258      74.968  20.780  53.241  1.00148.43           O1-
ANISOU 1980  OE2 GLU A 258    16489  21727  18181   -983   1783    754       O1-
ATOM   1981  N   SER A 259      80.452  16.490  55.414  1.00128.36           N  
ANISOU 1981  N   SER A 259    13246  19677  15848   -667   1795    490       N  
ATOM   1982  CA  SER A 259      81.650  16.343  56.226  1.00122.86           C  
ANISOU 1982  CA  SER A 259    12413  19070  15198   -634   1757    419       C  
ATOM   1983  C   SER A 259      82.604  15.413  55.496  1.00122.21           C  
ANISOU 1983  C   SER A 259    12218  19059  15159   -610   1806    347       C  
ATOM   1984  O   SER A 259      83.794  15.695  55.360  1.00132.57           O  
ANISOU 1984  O   SER A 259    13412  20453  16506   -663   1836    264       O  
ATOM   1985  CB  SER A 259      81.299  15.771  57.599  1.00118.16           C  
ANISOU 1985  CB  SER A 259    11821  18465  14610   -505   1657    452       C  
ATOM   1986  OG  SER A 259      80.360  16.595  58.268  1.00106.49           O  
ANISOU 1986  OG  SER A 259    10447  16929  13087   -520   1618    512       O  
ATOM   1987  N   LEU A 260      82.056  14.301  55.018  1.00114.77           N  
ANISOU 1987  N   LEU A 260    11307  18081  14219   -528   1811    374       N  
ATOM   1988  CA  LEU A 260      82.801  13.354  54.207  1.00119.81           C  
ANISOU 1988  CA  LEU A 260    11851  18777  14895   -495   1856    304       C  
ATOM   1989  C   LEU A 260      83.177  14.021  52.891  1.00134.36           C  
ANISOU 1989  C   LEU A 260    13694  20652  16704   -625   1970    268       C  
ATOM   1990  O   LEU A 260      84.214  13.721  52.302  1.00127.76           O  
ANISOU 1990  O   LEU A 260    12744  19903  15897   -644   2028    181       O  
ATOM   1991  CB  LEU A 260      81.943  12.118  53.944  1.00105.31           C  
ANISOU 1991  CB  LEU A 260    10071  16875  13068   -384   1829    350       C  
ATOM   1992  CG  LEU A 260      82.659  10.813  53.606  1.00115.53           C  
ANISOU 1992  CG  LEU A 260    11256  18218  14421   -289   1821    277       C  
ATOM   1993  CD1 LEU A 260      83.759  10.536  54.617  1.00125.36           C  
ANISOU 1993  CD1 LEU A 260    12368  19539  15724   -231   1755    210       C  
ATOM   1994  CD2 LEU A 260      81.656   9.672  53.581  1.00 99.58           C  
ANISOU 1994  CD2 LEU A 260     9306  16110  12420   -177   1770    341       C  
ATOM   1995  N   TYR A 261      82.322  14.934  52.441  1.00150.33           N  
ANISOU 1995  N   TYR A 261    15849  22605  18666   -715   2002    335       N  
ATOM   1996  CA  TYR A 261      82.553  15.667  51.204  1.00153.25           C  
ANISOU 1996  CA  TYR A 261    16250  22990  18988   -848   2107    322       C  
ATOM   1997  C   TYR A 261      83.080  17.061  51.517  1.00154.83           C  
ANISOU 1997  C   TYR A 261    16433  23211  19182   -979   2123    315       C  
ATOM   1998  O   TYR A 261      82.509  18.060  51.080  1.00158.81           O  
ANISOU 1998  O   TYR A 261    17052  23655  19634  -1081   2148    368       O  
ATOM   1999  CB  TYR A 261      81.259  15.795  50.398  1.00143.58           C  
ANISOU 1999  CB  TYR A 261    15194  21662  17700   -865   2123    400       C  
ATOM   2000  CG  TYR A 261      80.453  14.522  50.275  1.00131.65           C  
ANISOU 2000  CG  TYR A 261    13720  20096  16204   -732   2081    425       C  
ATOM   2001  CD1 TYR A 261      81.073  13.292  50.096  1.00131.45           C  
ANISOU 2001  CD1 TYR A 261    13588  20130  16225   -637   2084    361       C  
ATOM   2002  CD2 TYR A 261      79.066  14.553  50.337  1.00128.21           C  
ANISOU 2002  CD2 TYR A 261    13422  19545  15746   -700   2035    507       C  
ATOM   2003  CE1 TYR A 261      80.332  12.130  49.984  1.00133.87           C  
ANISOU 2003  CE1 TYR A 261    13931  20377  16558   -518   2038    385       C  
ATOM   2004  CE2 TYR A 261      78.319  13.399  50.225  1.00130.50           C  
ANISOU 2004  CE2 TYR A 261    13742  19778  16065   -585   1996    531       C  
ATOM   2005  CZ  TYR A 261      78.955  12.191  50.049  1.00131.34           C  
ANISOU 2005  CZ  TYR A 261    13745  19939  16218   -495   1996    473       C  
ATOM   2006  OH  TYR A 261      78.208  11.043  49.938  1.00124.15           O  
ANISOU 2006  OH  TYR A 261    12863  18961  15346   -383   1949    498       O  
ATOM   2007  N   ASN A 262      84.162  17.128  52.283  1.00150.28           N  
ANISOU 2007  N   ASN A 262    15717  22716  18667   -973   2098    245       N  
ATOM   2008  CA  ASN A 262      84.753  18.416  52.639  1.00150.02           C  
ANISOU 2008  CA  ASN A 262    15650  22703  18647  -1093   2103    227       C  
ATOM   2009  C   ASN A 262      86.282  18.488  52.540  1.00148.92           C  
ANISOU 2009  C   ASN A 262    15331  22679  18572  -1148   2155    122       C  
ATOM   2010  O   ASN A 262      86.814  19.469  52.022  1.00140.75           O  
ANISOU 2010  O   ASN A 262    14276  21667  17534  -1294   2228    109       O  
ATOM   2011  CB  ASN A 262      84.276  18.887  54.015  1.00149.39           C  
ANISOU 2011  CB  ASN A 262    15607  22573  18579  -1045   1986    262       C  
ATOM   2012  CG  ASN A 262      84.710  20.303  54.322  1.00145.73           C  
ANISOU 2012  CG  ASN A 262    15132  22109  18128  -1171   1979    249       C  
ATOM   2013  ND2 ASN A 262      83.915  21.273  53.884  1.00137.51           N  
ANISOU 2013  ND2 ASN A 262    14226  20986  17035  -1265   1994    316       N  
ATOM   2014  OD1 ASN A 262      85.753  20.527  54.934  1.00144.54           O  
ANISOU 2014  OD1 ASN A 262    14850  22026  18041  -1182   1953    176       O  
ATOM   2015  N   PRO A 263      87.000  17.460  53.035  1.00151.78           N  
ANISOU 2015  N   PRO A 263    15559  23112  18998  -1034   2116     46       N  
ATOM   2016  CA  PRO A 263      88.448  17.485  52.800  1.00154.12           C  
ANISOU 2016  CA  PRO A 263    15676  23521  19363  -1087   2175    -67       C  
ATOM   2017  C   PRO A 263      88.785  17.191  51.339  1.00159.73           C  
ANISOU 2017  C   PRO A 263    16362  24287  20042  -1152   2316    -98       C  
ATOM   2018  O   PRO A 263      89.952  17.230  50.953  1.00162.47           O  
ANISOU 2018  O   PRO A 263    16559  24734  20437  -1211   2391   -192       O  
ATOM   2019  CB  PRO A 263      88.963  16.355  53.695  1.00146.26           C  
ANISOU 2019  CB  PRO A 263    14563  22570  18439   -927   2080   -136       C  
ATOM   2020  CG  PRO A 263      87.805  15.433  53.835  1.00141.79           C  
ANISOU 2020  CG  PRO A 263    14118  21926  17829   -800   2022    -58       C  
ATOM   2021  CD  PRO A 263      86.614  16.333  53.904  1.00145.52           C  
ANISOU 2021  CD  PRO A 263    14764  22299  18228   -862   2012     54       C  
ATOM   2022  N   MET A 264      87.765  16.898  50.540  1.00156.24           N  
ANISOU 2022  N   MET A 264    16064  23782  19519  -1140   2349    -24       N  
ATOM   2023  CA  MET A 264      87.949  16.632  49.121  1.00150.63           C  
ANISOU 2023  CA  MET A 264    15358  23118  18758  -1194   2478    -47       C  
ATOM   2024  C   MET A 264      88.085  17.931  48.342  1.00152.88           C  
ANISOU 2024  C   MET A 264    15700  23402  18987  -1383   2584     -9       C  
ATOM   2025  O   MET A 264      88.750  17.977  47.311  1.00151.69           O  
ANISOU 2025  O   MET A 264    15495  23330  18809  -1467   2711    -53       O  
ATOM   2026  CB  MET A 264      86.770  15.827  48.579  1.00135.94           C  
ANISOU 2026  CB  MET A 264    13636  21180  16835  -1101   2459     15       C  
ATOM   2027  CG  MET A 264      86.537  14.523  49.309  1.00122.51           C  
ANISOU 2027  CG  MET A 264    11894  19464  15190   -919   2353     -5       C  
ATOM   2028  SD  MET A 264      85.084  13.641  48.722  1.00134.91           S  
ANISOU 2028  SD  MET A 264    13626  20926  16706   -818   2322     73       S  
ATOM   2029  CE  MET A 264      85.193  12.151  49.704  1.00139.07           C  
ANISOU 2029  CE  MET A 264    14060  21455  17326   -624   2201     34       C  
ATOM   2030  N   LEU A 265      87.460  18.985  48.857  1.00152.36           N  
ANISOU 2030  N   LEU A 265    15742  23245  18901  -1450   2528     72       N  
ATOM   2031  CA  LEU A 265      87.401  20.282  48.176  1.00152.80           C  
ANISOU 2031  CA  LEU A 265    15886  23269  18903  -1629   2605    128       C  
ATOM   2032  C   LEU A 265      88.714  20.855  47.611  1.00157.03           C  
ANISOU 2032  C   LEU A 265    16288  23909  19466  -1776   2729     64       C  
ATOM   2033  O   LEU A 265      88.693  21.489  46.556  1.00159.10           O  
ANISOU 2033  O   LEU A 265    16627  24168  19656  -1911   2836    107       O  
ATOM   2034  CB  LEU A 265      86.696  21.329  49.049  1.00153.03           C  
ANISOU 2034  CB  LEU A 265    16017  23191  18936  -1664   2502    200       C  
ATOM   2035  CG  LEU A 265      85.215  21.100  49.367  1.00145.03           C  
ANISOU 2035  CG  LEU A 265    15171  22059  17874  -1566   2407    284       C  
ATOM   2036  CD1 LEU A 265      84.500  22.434  49.517  1.00136.52           C  
ANISOU 2036  CD1 LEU A 265    14232  20876  16764  -1667   2364    362       C  
ATOM   2037  CD2 LEU A 265      84.538  20.241  48.309  1.00141.05           C  
ANISOU 2037  CD2 LEU A 265    14758  21535  17299  -1510   2457    311       C  
ATOM   2038  N   PRO A 266      89.852  20.662  48.308  1.00156.88           N  
ANISOU 2038  N   PRO A 266    16073  23981  19554  -1755   2714    -37       N  
ATOM   2039  CA  PRO A 266      91.104  21.102  47.677  1.00154.62           C  
ANISOU 2039  CA  PRO A 266    15646  23802  19302  -1895   2846   -105       C  
ATOM   2040  C   PRO A 266      91.421  20.352  46.385  1.00147.33           C  
ANISOU 2040  C   PRO A 266    14712  22943  18322  -1888   2975   -143       C  
ATOM   2041  O   PRO A 266      91.284  20.917  45.301  1.00134.35           O  
ANISOU 2041  O   PRO A 266    13186  21265  16597  -2000   3074    -84       O  
ATOM   2042  CB  PRO A 266      92.167  20.795  48.743  1.00151.79           C  
ANISOU 2042  CB  PRO A 266    15077  23517  19078  -1830   2779   -221       C  
ATOM   2043  CG  PRO A 266      91.500  19.874  49.720  1.00147.87           C  
ANISOU 2043  CG  PRO A 266    14614  22971  18597  -1634   2629   -217       C  
ATOM   2044  CD  PRO A 266      90.068  20.284  49.714  1.00152.68           C  
ANISOU 2044  CD  PRO A 266    15448  23450  19115  -1631   2576    -87       C  
ATOM   2045  N   GLY A 267      91.825  19.090  46.501  1.00154.02           N  
ANISOU 2045  N   GLY A 267    15448  23855  19216  -1740   2953   -237       N  
ATOM   2046  CA  GLY A 267      92.208  18.295  45.348  1.00153.59           C  
ANISOU 2046  CA  GLY A 267    15388  23845  19126  -1703   3048   -291       C  
ATOM   2047  C   GLY A 267      91.060  17.903  44.435  1.00145.87           C  
ANISOU 2047  C   GLY A 267    14583  22823  18016  -1671   3080   -215       C  
ATOM   2048  O   GLY A 267      91.065  16.823  43.847  1.00139.19           O  
ANISOU 2048  O   GLY A 267    13718  22018  17149  -1565   3104   -270       O  
ATOM   2049  N   ILE A 268      90.072  18.784  44.319  1.00143.11           N  
ANISOU 2049  N   ILE A 268    14399  22391  17583  -1760   3075    -94       N  
ATOM   2050  CA  ILE A 268      88.953  18.583  43.409  1.00141.05           C  
ANISOU 2050  CA  ILE A 268    14315  22082  17194  -1748   3104    -17       C  
ATOM   2051  C   ILE A 268      88.885  19.758  42.438  1.00141.49           C  
ANISOU 2051  C   ILE A 268    14511  22090  17157  -1923   3201     63       C  
ATOM   2052  O   ILE A 268      88.579  19.585  41.259  1.00133.10           O  
ANISOU 2052  O   ILE A 268    13559  21025  15989  -1939   3281     87       O  
ATOM   2053  CB  ILE A 268      87.619  18.411  44.171  1.00126.15           C  
ANISOU 2053  CB  ILE A 268    12568  20055  15307  -1638   2950     65       C  
ATOM   2054  CG1 ILE A 268      87.483  16.973  44.668  1.00123.67           C  
ANISOU 2054  CG1 ILE A 268    12182  19755  15054  -1441   2864      4       C  
ATOM   2055  CG2 ILE A 268      86.433  18.721  43.277  1.00113.74           C  
ANISOU 2055  CG2 ILE A 268    11219  18381  13616  -1669   2962    165       C  
ATOM   2056  CD1 ILE A 268      87.337  15.962  43.556  1.00125.00           C  
ANISOU 2056  CD1 ILE A 268    12369  19961  15162  -1368   2926    -36       C  
ATOM   2057  N   VAL A 269      89.191  20.950  42.938  1.00138.96           N  
ANISOU 2057  N   VAL A 269    14184  21735  16878  -2054   3192    102       N  
ATOM   2058  CA  VAL A 269      89.308  22.125  42.085  1.00130.80           C  
ANISOU 2058  CA  VAL A 269    13265  20657  15776  -2232   3282    176       C  
ATOM   2059  C   VAL A 269      90.736  22.252  41.565  1.00135.19           C  
ANISOU 2059  C   VAL A 269    13699  21284  16383  -2302   3393    104       C  
ATOM   2060  O   VAL A 269      90.972  22.809  40.494  1.00143.22           O  
ANISOU 2060  O   VAL A 269    14802  22293  17323  -2417   3503    148       O  
ATOM   2061  CB  VAL A 269      88.902  23.413  42.823  1.00119.32           C  
ANISOU 2061  CB  VAL A 269    11869  19125  14344  -2351   3215    259       C  
ATOM   2062  CG1 VAL A 269      87.393  23.465  43.004  1.00113.42           C  
ANISOU 2062  CG1 VAL A 269    11313  18253  13530  -2286   3106    350       C  
ATOM   2063  CG2 VAL A 269      89.610  23.508  44.162  1.00120.80           C  
ANISOU 2063  CG2 VAL A 269    11872  19351  14674  -2325   3137    188       C  
ATOM   2064  N   ALA A 270      91.686  21.725  42.331  1.00132.98           N  
ANISOU 2064  N   ALA A 270    13219  21075  16231  -2230   3362     -7       N  
ATOM   2065  CA  ALA A 270      93.084  21.726  41.919  1.00135.39           C  
ANISOU 2065  CA  ALA A 270    13383  21457  16603  -2280   3460    -91       C  
ATOM   2066  C   ALA A 270      93.258  20.794  40.731  1.00143.98           C  
ANISOU 2066  C   ALA A 270    14488  22606  17611  -2213   3559   -138       C  
ATOM   2067  O   ALA A 270      93.892  21.144  39.736  1.00152.88           O  
ANISOU 2067  O   ALA A 270    15627  23765  18694  -2309   3687   -135       O  
ATOM   2068  CB  ALA A 270      93.976  21.293  43.069  1.00129.22           C  
ANISOU 2068  CB  ALA A 270    12384  20735  15979  -2201   3385   -207       C  
ATOM   2069  N   ASP A 271      92.679  19.604  40.845  1.00140.11           N  
ANISOU 2069  N   ASP A 271    13996  22136  17102  -2049   3497   -179       N  
ATOM   2070  CA  ASP A 271      92.688  18.639  39.758  1.00144.39           C  
ANISOU 2070  CA  ASP A 271    14561  22737  17565  -1969   3573   -229       C  
ATOM   2071  C   ASP A 271      91.820  19.149  38.618  1.00150.15           C  
ANISOU 2071  C   ASP A 271    15508  23413  18128  -2051   3645   -119       C  
ATOM   2072  O   ASP A 271      92.005  18.771  37.464  1.00156.90           O  
ANISOU 2072  O   ASP A 271    16404  24319  18893  -2046   3747   -143       O  
ATOM   2073  CB  ASP A 271      92.170  17.288  40.244  1.00146.56           C  
ANISOU 2073  CB  ASP A 271    14786  23032  17869  -1775   3472   -291       C  
ATOM   2074  CG  ASP A 271      92.306  16.206  39.197  1.00155.18           C  
ANISOU 2074  CG  ASP A 271    15867  24195  18900  -1681   3539   -368       C  
ATOM   2075  OD1 ASP A 271      91.322  15.947  38.474  1.00153.57           O  
ANISOU 2075  OD1 ASP A 271    15811  23963  18576  -1651   3552   -314       O  
ATOM   2076  OD2 ASP A 271      93.403  15.618  39.096  1.00160.85           O1-
ANISOU 2076  OD2 ASP A 271    16424  25000  19691  -1634   3577   -488       O1-
ATOM   2077  N   LEU A 272      90.867  20.010  38.956  1.00150.16           N  
ANISOU 2077  N   LEU A 272    15651  23315  18087  -2123   3587     -2       N  
ATOM   2078  CA  LEU A 272      89.997  20.619  37.962  1.00150.09           C  
ANISOU 2078  CA  LEU A 272    15861  23242  17924  -2210   3637    110       C  
ATOM   2079  C   LEU A 272      90.760  21.711  37.224  1.00145.92           C  
ANISOU 2079  C   LEU A 272    15368  22714  17361  -2388   3758    155       C  
ATOM   2080  O   LEU A 272      90.431  22.055  36.089  1.00140.77           O  
ANISOU 2080  O   LEU A 272    14872  22043  16570  -2458   3840    223       O  
ATOM   2081  CB  LEU A 272      88.756  21.204  38.631  1.00147.63           C  
ANISOU 2081  CB  LEU A 272    15679  22824  17591  -2230   3526    214       C  
ATOM   2082  CG  LEU A 272      87.437  21.161  37.861  1.00139.32           C  
ANISOU 2082  CG  LEU A 272    14838  21708  16390  -2219   3516    299       C  
ATOM   2083  CD1 LEU A 272      87.091  19.736  37.462  1.00128.49           C  
ANISOU 2083  CD1 LEU A 272    13441  20395  14984  -2050   3511    227       C  
ATOM   2084  CD2 LEU A 272      86.331  21.759  38.712  1.00136.96           C  
ANISOU 2084  CD2 LEU A 272    14630  21309  16098  -2237   3397    389       C  
ATOM   2085  N   LYS A 273      91.777  22.257  37.883  1.00149.29           N  
ANISOU 2085  N   LYS A 273    15648  23162  17913  -2460   3764    120       N  
ATOM   2086  CA  LYS A 273      92.663  23.226  37.251  1.00156.03           C  
ANISOU 2086  CA  LYS A 273    16498  24026  18760  -2627   3883    153       C  
ATOM   2087  C   LYS A 273      93.822  22.526  36.555  1.00152.08           C  
ANISOU 2087  C   LYS A 273    15862  23645  18276  -2591   4003     46       C  
ATOM   2088  O   LYS A 273      94.315  22.993  35.529  1.00141.75           O  
ANISOU 2088  O   LYS A 273    14601  22363  16894  -2697   4135     80       O  
ATOM   2089  CB  LYS A 273      93.194  24.232  38.272  1.00158.89           C  
ANISOU 2089  CB  LYS A 273    16765  24350  19256  -2734   3834    166       C  
ATOM   2090  CG  LYS A 273      92.246  25.378  38.550  1.00157.81           C  
ANISOU 2090  CG  LYS A 273    16792  24092  19075  -2845   3766    296       C  
ATOM   2091  CD  LYS A 273      92.983  26.574  39.119  1.00158.09           C  
ANISOU 2091  CD  LYS A 273    16749  24098  19221  -2999   3765    318       C  
ATOM   2092  CE  LYS A 273      92.083  27.795  39.171  1.00151.84           C  
ANISOU 2092  CE  LYS A 273    16137  23182  18372  -3130   3712    452       C  
ATOM   2093  NZ  LYS A 273      92.816  28.999  39.649  1.00149.77           N1+
ANISOU 2093  NZ  LYS A 273    15798  22887  18219  -3292   3713    474       N1+
ATOM   2094  N   ALA A 274      94.246  21.396  37.114  1.00154.25           N  
ANISOU 2094  N   ALA A 274    15970  23993  18645  -2440   3954    -81       N  
ATOM   2095  CA  ALA A 274      95.325  20.607  36.529  1.00153.91           C  
ANISOU 2095  CA  ALA A 274    15784  24069  18627  -2387   4050   -200       C  
ATOM   2096  C   ALA A 274      94.808  19.716  35.404  1.00161.98           C  
ANISOU 2096  C   ALA A 274    16906  25133  19505  -2296   4107   -217       C  
ATOM   2097  O   ALA A 274      95.381  18.666  35.115  1.00169.78           O  
ANISOU 2097  O   ALA A 274    17775  26217  20516  -2185   4139   -338       O  
ATOM   2098  CB  ALA A 274      96.019  19.775  37.597  1.00147.20           C  
ANISOU 2098  CB  ALA A 274    14713  23275  17941  -2263   3963   -336       C  
ATOM   2099  N   LYS A 275      93.714  20.141  34.782  1.00160.14           N  
ANISOU 2099  N   LYS A 275    16893  24828  19125  -2340   4114   -101       N  
ATOM   2100  CA  LYS A 275      93.156  19.458  33.623  1.00159.82           C  
ANISOU 2100  CA  LYS A 275    16973  24823  18930  -2272   4172   -105       C  
ATOM   2101  C   LYS A 275      92.664  20.490  32.617  1.00164.57           C  
ANISOU 2101  C   LYS A 275    17792  25367  19370  -2417   4255     31       C  
ATOM   2102  O   LYS A 275      92.129  20.144  31.563  1.00172.34           O  
ANISOU 2102  O   LYS A 275    18912  26369  20200  -2386   4308     49       O  
ATOM   2103  CB  LYS A 275      92.015  18.527  34.036  1.00154.33           C  
ANISOU 2103  CB  LYS A 275    16325  24093  18220  -2115   4046   -120       C  
ATOM   2104  CG  LYS A 275      92.472  17.263  34.747  1.00154.53           C  
ANISOU 2104  CG  LYS A 275    16151  24188  18374  -1948   3975   -263       C  
ATOM   2105  CD  LYS A 275      91.292  16.469  35.281  1.00152.57           C  
ANISOU 2105  CD  LYS A 275    15951  23894  18126  -1807   3843   -257       C  
ATOM   2106  CE  LYS A 275      90.528  15.782  34.163  1.00157.84           C  
ANISOU 2106  CE  LYS A 275    16743  24583  18645  -1732   3879   -261       C  
ATOM   2107  NZ  LYS A 275      91.334  14.704  33.526  1.00163.12           N1+
ANISOU 2107  NZ  LYS A 275    17286  25373  19320  -1629   3944   -404       N1+
ATOM   2108  N   GLY A 276      92.854  21.762  32.955  1.00157.56           N  
ANISOU 2108  N   GLY A 276    16937  24409  18520  -2576   4260    125       N  
ATOM   2109  CA  GLY A 276      92.460  22.859  32.092  1.00153.89           C  
ANISOU 2109  CA  GLY A 276    16676  23877  17918  -2729   4329    262       C  
ATOM   2110  C   GLY A 276      90.956  22.970  31.934  1.00148.96           C  
ANISOU 2110  C   GLY A 276    16273  23153  17174  -2705   4241    357       C  
ATOM   2111  O   GLY A 276      90.412  22.637  30.883  1.00154.10           O  
ANISOU 2111  O   GLY A 276    17068  23817  17665  -2673   4289    379       O  
ATOM   2112  N   LEU A 277      90.284  23.437  32.980  1.00146.36           N  
ANISOU 2112  N   LEU A 277    15967  22726  16918  -2718   4110    408       N  
ATOM   2113  CA  LEU A 277      88.833  23.594  32.952  1.00138.57           C  
ANISOU 2113  CA  LEU A 277    15179  21638  15834  -2699   4016    496       C  
ATOM   2114  C   LEU A 277      88.373  24.747  33.833  1.00127.84           C  
ANISOU 2114  C   LEU A 277    13876  20161  14536  -2808   3919    591       C  
ATOM   2115  O   LEU A 277      87.180  25.033  33.923  1.00101.43           O  
ANISOU 2115  O   LEU A 277    10691  16722  11126  -2810   3831    670       O  
ATOM   2116  CB  LEU A 277      88.147  22.300  33.394  1.00132.41           C  
ANISOU 2116  CB  LEU A 277    14348  20885  15076  -2507   3924    418       C  
ATOM   2117  CG  LEU A 277      87.815  21.295  32.291  1.00132.62           C  
ANISOU 2117  CG  LEU A 277    14442  20977  14971  -2401   3980    371       C  
ATOM   2118  CD1 LEU A 277      87.892  19.880  32.826  1.00131.40           C  
ANISOU 2118  CD1 LEU A 277    14122  20898  14906  -2214   3925    242       C  
ATOM   2119  CD2 LEU A 277      86.432  21.574  31.727  1.00133.28           C  
ANISOU 2119  CD2 LEU A 277    14766  20971  14902  -2415   3934    472       C  
ATOM   2120  N   ALA A 278      89.324  25.411  34.479  1.00140.89           N  
ANISOU 2120  N   ALA A 278    15393  21822  16318  -2900   3933    578       N  
ATOM   2121  CA  ALA A 278      88.989  26.469  35.423  1.00137.29           C  
ANISOU 2121  CA  ALA A 278    14961  21265  15937  -2997   3835    648       C  
ATOM   2122  C   ALA A 278      89.746  27.771  35.167  1.00146.68           C  
ANISOU 2122  C   ALA A 278    16163  22420  17149  -3194   3906    717       C  
ATOM   2123  O   ALA A 278      90.925  27.763  34.816  1.00150.33           O  
ANISOU 2123  O   ALA A 278    16503  22961  17655  -3239   4017    669       O  
ATOM   2124  CB  ALA A 278      89.205  25.993  36.848  1.00127.11           C  
ANISOU 2124  CB  ALA A 278    13480  20005  14810  -2898   3732    560       C  
ATOM   2125  N   VAL A 279      89.051  28.888  35.355  1.00147.98           N  
ANISOU 2125  N   VAL A 279    16473  22464  17288  -3313   3838    829       N  
ATOM   2126  CA  VAL A 279      89.619  30.213  35.144  1.00153.44           C  
ANISOU 2126  CA  VAL A 279    17199  23100  18002  -3511   3886    910       C  
ATOM   2127  C   VAL A 279      89.269  31.115  36.327  1.00152.16           C  
ANISOU 2127  C   VAL A 279    17020  22845  17947  -3582   3754    945       C  
ATOM   2128  O   VAL A 279      88.134  31.113  36.798  1.00148.84           O  
ANISOU 2128  O   VAL A 279    16701  22356  17497  -3533   3636    978       O  
ATOM   2129  CB  VAL A 279      89.113  30.824  33.814  1.00153.73           C  
ANISOU 2129  CB  VAL A 279    17483  23069  17859  -3615   3951   1035       C  
ATOM   2130  CG1 VAL A 279      87.798  30.182  33.396  1.00145.60           C  
ANISOU 2130  CG1 VAL A 279    16629  22004  16688  -3502   3889   1059       C  
ATOM   2131  CG2 VAL A 279      88.979  32.341  33.913  1.00156.14           C  
ANISOU 2131  CG2 VAL A 279    17901  23247  18178  -3810   3912   1156       C  
ATOM   2132  N   GLU A 280      90.244  31.877  36.817  1.00157.49           N  
ANISOU 2132  N   GLU A 280    17563  23524  18752  -3698   3774    933       N  
ATOM   2133  CA  GLU A 280      90.031  32.718  37.996  1.00165.34           C  
ANISOU 2133  CA  GLU A 280    18515  24444  19861  -3765   3648    949       C  
ATOM   2134  C   GLU A 280      89.213  33.983  37.706  1.00169.02           C  
ANISOU 2134  C   GLU A 280    19201  24763  20256  -3921   3592   1090       C  
ATOM   2135  O   GLU A 280      89.541  35.069  38.184  1.00166.53           O  
ANISOU 2135  O   GLU A 280    18857  24384  20034  -4065   3553   1127       O  
ATOM   2136  CB  GLU A 280      91.367  33.080  38.659  1.00175.01           C  
ANISOU 2136  CB  GLU A 280    19512  25723  21261  -3833   3678    877       C  
ATOM   2137  CG  GLU A 280      92.339  33.853  37.772  1.00189.54           C  
ANISOU 2137  CG  GLU A 280    21353  27560  23103  -4001   3813    929       C  
ATOM   2138  CD  GLU A 280      93.476  32.997  37.247  1.00198.07           C  
ANISOU 2138  CD  GLU A 280    22275  28775  24206  -3939   3953    836       C  
ATOM   2139  OE1 GLU A 280      93.280  31.776  37.075  1.00203.17           O  
ANISOU 2139  OE1 GLU A 280    22896  29501  24798  -3772   3966    763       O  
ATOM   2140  OE2 GLU A 280      94.572  33.550  37.012  1.00196.78           O1-
ANISOU 2140  OE2 GLU A 280    22009  28638  24121  -4059   4047    834       O1-
ATOM   2141  N   SER A 281      88.137  33.829  36.938  1.00173.79           N  
ANISOU 2141  N   SER A 281    20023  25309  20700  -3892   3578   1165       N  
ATOM   2142  CA  SER A 281      87.287  34.953  36.553  1.00178.20           C  
ANISOU 2142  CA  SER A 281    20814  25719  21174  -4030   3516   1301       C  
ATOM   2143  C   SER A 281      86.673  35.675  37.747  1.00177.34           C  
ANISOU 2143  C   SER A 281    20703  25516  21161  -4065   3352   1317       C  
ATOM   2144  O   SER A 281      86.366  35.058  38.768  1.00182.80           O  
ANISOU 2144  O   SER A 281    21296  26217  21941  -3893   3240   1229       O  
ATOM   2145  CB  SER A 281      86.173  34.484  35.615  1.00177.40           C  
ANISOU 2145  CB  SER A 281    20936  25579  20889  -3959   3511   1358       C  
ATOM   2146  OG  SER A 281      85.179  35.484  35.477  1.00176.76           O  
ANISOU 2146  OG  SER A 281    21078  25342  20742  -4064   3410   1477       O  
ATOM   2147  N   GLU A 282      86.519  36.991  37.612  1.00172.79           N  
ANISOU 2147  N   GLU A 282    20259  24801  20593  -4228   3298   1418       N  
ATOM   2148  CA  GLU A 282      85.852  37.833  38.609  1.00169.61           C  
ANISOU 2148  CA  GLU A 282    19912  24234  20297  -4206   3089   1429       C  
ATOM   2149  C   GLU A 282      86.551  37.871  39.973  1.00166.97           C  
ANISOU 2149  C   GLU A 282    19340  23951  20153  -4169   3026   1324       C  
ATOM   2150  O   GLU A 282      86.471  38.867  40.692  1.00162.29           O  
ANISOU 2150  O   GLU A 282    18754  23243  19664  -4229   2898   1338       O  
ATOM   2151  CB  GLU A 282      84.383  37.421  38.764  1.00171.80           C  
ANISOU 2151  CB  GLU A 282    20357  24405  20513  -4020   2934   1431       C  
ATOM   2152  CG  GLU A 282      83.544  38.373  39.598  1.00175.22           C  
ANISOU 2152  CG  GLU A 282    20889  24659  21029  -4004   2721   1452       C  
ATOM   2153  CD  GLU A 282      82.116  37.896  39.766  1.00173.40           C  
ANISOU 2153  CD  GLU A 282    20800  24336  20748  -3817   2581   1441       C  
ATOM   2154  OE1 GLU A 282      81.341  38.572  40.475  1.00170.48           O  
ANISOU 2154  OE1 GLU A 282    20506  23828  20442  -3780   2405   1444       O  
ATOM   2155  OE2 GLU A 282      81.767  36.844  39.190  1.00171.22           O1-
ANISOU 2155  OE2 GLU A 282    20555  24126  20373  -3706   2645   1425       O1-
ATOM   2156  N   GLY A 283      87.238  36.790  40.321  1.00164.88           N  
ANISOU 2156  N   GLY A 283    18864  23851  19930  -4066   3108   1216       N  
ATOM   2157  CA  GLY A 283      87.904  36.679  41.602  1.00156.43           C  
ANISOU 2157  CA  GLY A 283    17568  22839  19029  -4008   3045   1106       C  
ATOM   2158  C   GLY A 283      87.635  35.308  42.182  1.00150.58           C  
ANISOU 2158  C   GLY A 283    16731  22191  18292  -3776   3012   1005       C  
ATOM   2159  O   GLY A 283      87.998  35.014  43.320  1.00150.44           O  
ANISOU 2159  O   GLY A 283    16546  22219  18397  -3680   2937    910       O  
ATOM   2160  N   ALA A 284      86.994  34.464  41.380  1.00151.68           N  
ANISOU 2160  N   ALA A 284    16982  22353  18296  -3685   3064   1027       N  
ATOM   2161  CA  ALA A 284      86.611  33.129  41.815  1.00152.07           C  
ANISOU 2161  CA  ALA A 284    16967  22473  18341  -3466   3029    946       C  
ATOM   2162  C   ALA A 284      86.937  32.076  40.764  1.00153.48           C  
ANISOU 2162  C   ALA A 284    17121  22781  18415  -3433   3191    924       C  
ATOM   2163  O   ALA A 284      86.910  32.348  39.564  1.00159.61           O  
ANISOU 2163  O   ALA A 284    18022  23553  19069  -3544   3299    998       O  
ATOM   2164  CB  ALA A 284      85.134  33.093  42.146  1.00148.54           C  
ANISOU 2164  CB  ALA A 284    16699  21886  17854  -3334   2866    983       C  
ATOM   2165  N   THR A 285      87.239  30.870  41.229  1.00148.15           N  
ANISOU 2165  N   THR A 285    16287  22219  17783  -3277   3200    820       N  
ATOM   2166  CA  THR A 285      87.511  29.749  40.343  1.00146.98           C  
ANISOU 2166  CA  THR A 285    16101  22195  17549  -3213   3332    778       C  
ATOM   2167  C   THR A 285      86.217  29.288  39.685  1.00140.73           C  
ANISOU 2167  C   THR A 285    15523  21320  16628  -3111   3285    835       C  
ATOM   2168  O   THR A 285      85.265  28.920  40.370  1.00147.02           O  
ANISOU 2168  O   THR A 285    16374  22034  17452  -2963   3141    829       O  
ATOM   2169  CB  THR A 285      88.124  28.574  41.117  1.00152.60           C  
ANISOU 2169  CB  THR A 285    16598  23018  18364  -3048   3317    648       C  
ATOM   2170  CG2 THR A 285      88.536  27.467  40.164  1.00153.58           C  
ANISOU 2170  CG2 THR A 285    16699  23224  18431  -2952   3422    591       C  
ATOM   2171  OG1 THR A 285      89.269  29.029  41.848  1.00155.21           O  
ANISOU 2171  OG1 THR A 285    16744  23390  18838  -3111   3319    586       O  
ATOM   2172  N   VAL A 286      86.179  29.318  38.356  1.00136.45           N  
ANISOU 2172  N   VAL A 286    15103  20798  15945  -3190   3404    889       N  
ATOM   2173  CA  VAL A 286      84.958  28.992  37.623  1.00133.99           C  
ANISOU 2173  CA  VAL A 286    15009  20396  15506  -3105   3355    944       C  
ATOM   2174  C   VAL A 286      85.204  28.013  36.474  1.00130.98           C  
ANISOU 2174  C   VAL A 286    14630  20130  15005  -3058   3492    909       C  
ATOM   2175  O   VAL A 286      86.309  27.939  35.941  1.00134.97           O  
ANISOU 2175  O   VAL A 286    15051  20709  15524  -3095   3607    869       O  
ATOM   2176  CB  VAL A 286      84.283  30.262  37.066  1.00130.90           C  
ANISOU 2176  CB  VAL A 286    14852  19850  15033  -3244   3313   1072       C  
ATOM   2177  CG1 VAL A 286      84.015  31.268  38.175  1.00125.20           C  
ANISOU 2177  CG1 VAL A 286    14133  19007  14430  -3286   3167   1099       C  
ATOM   2178  CG2 VAL A 286      85.123  30.883  35.962  1.00130.00           C  
ANISOU 2178  CG2 VAL A 286    14772  19797  14824  -3441   3485   1129       C  
ATOM   2179  N   VAL A 287      84.165  27.271  36.094  1.00121.97           N  
ANISOU 2179  N   VAL A 287    13617  18935  13790  -2914   3427    911       N  
ATOM   2180  CA  VAL A 287      84.268  26.255  35.045  1.00120.07           C  
ANISOU 2180  CA  VAL A 287    13387  18796  13438  -2842   3533    867       C  
ATOM   2181  C   VAL A 287      83.173  26.408  33.991  1.00124.31           C  
ANISOU 2181  C   VAL A 287    14188  19222  13821  -2831   3500    947       C  
ATOM   2182  O   VAL A 287      81.989  26.264  34.290  1.00118.12           O  
ANISOU 2182  O   VAL A 287    13524  18305  13051  -2718   3348    969       O  
ATOM   2183  CB  VAL A 287      84.179  24.837  35.632  1.00108.02           C  
ANISOU 2183  CB  VAL A 287    11717  17330  11993  -2631   3478    756       C  
ATOM   2184  CG1 VAL A 287      84.154  23.803  34.516  1.00112.83           C  
ANISOU 2184  CG1 VAL A 287    12357  18024  12488  -2544   3564    707       C  
ATOM   2185  CG2 VAL A 287      85.331  24.583  36.585  1.00 97.67           C  
ANISOU 2185  CG2 VAL A 287    10147  16136  10828  -2628   3509    666       C  
ATOM   2186  N   PHE A 288      83.576  26.673  32.753  1.00130.25           N  
ANISOU 2186  N   PHE A 288    15029  20035  14424  -2944   3643    986       N  
ATOM   2187  CA  PHE A 288      82.634  27.033  31.694  1.00134.89           C  
ANISOU 2187  CA  PHE A 288    15887  20513  14851  -2963   3615   1075       C  
ATOM   2188  C   PHE A 288      81.940  25.871  30.983  1.00136.16           C  
ANISOU 2188  C   PHE A 288    16126  20685  14924  -2787   3592   1023       C  
ATOM   2189  O   PHE A 288      82.563  24.864  30.650  1.00142.08           O  
ANISOU 2189  O   PHE A 288    16744  21584  15656  -2712   3694    929       O  
ATOM   2190  CB  PHE A 288      83.309  27.954  30.675  1.00137.66           C  
ANISOU 2190  CB  PHE A 288    16334  20888  15081  -3156   3756   1156       C  
ATOM   2191  CG  PHE A 288      83.413  29.379  31.132  1.00136.15           C  
ANISOU 2191  CG  PHE A 288    16196  20587  14948  -3328   3712   1253       C  
ATOM   2192  CD1 PHE A 288      82.443  30.301  30.780  1.00131.23           C  
ANISOU 2192  CD1 PHE A 288    15820  19806  14234  -34