CNRS Nantes University UFIP UFIP
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***  PARP1  ***

elNémo ID: 21050818192752090

Job options:

ID        	=	 21050818192752090
JOBID     	=	 PARP1
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 PARP1

ATOM      1  N   LEU C 665      66.949  38.459 139.012  1.00 81.71      A    N  
ANISOU    1  N   LEU C 665     7681   9865  13501  -1500   1266   3144  A    N  
ATOM      2  CA  LEU C 665      65.509  38.383 139.199  1.00 75.46      A    C  
ANISOU    2  CA  LEU C 665     7198   8926  12549  -1396   1159   2901  A    C  
ATOM      3  C   LEU C 665      65.008  39.669 139.850  1.00 71.67      A    C  
ANISOU    3  C   LEU C 665     6822   8184  12224  -1585    906   2828  A    C  
ATOM      4  O   LEU C 665      65.702  40.257 140.678  1.00 66.81      A    O  
ANISOU    4  O   LEU C 665     6060   7504  11821  -1773    746   2849  A    O  
ATOM      5  CB  LEU C 665      65.122  37.154 140.037  1.00 76.00      A    C  
ANISOU    5  CB  LEU C 665     7315   9073  12487  -1222   1118   2660  A    C  
ATOM      6  CG  LEU C 665      64.840  35.898 139.200  1.00 78.43      A    C  
ANISOU    6  CG  LEU C 665     7718   9541  12539   -978   1349   2640  A    C  
ATOM      7  CD1 LEU C 665      66.122  35.179 138.817  1.00 83.85      A    C  
ANISOU    7  CD1 LEU C 665     8164  10450  13247   -908   1564   2817  A    C  
ATOM      8  CD2 LEU C 665      63.935  34.959 139.925  1.00 80.88      A    C  
ANISOU    8  CD2 LEU C 665     8191   9840  12700   -832   1261   2374  A    C  
ATOM      9  N   PRO C 666      63.801  40.114 139.461  1.00 73.48      A    N  
ANISOU    9  N   PRO C 666     7312   8261  12345  -1531    866   2745  A    N  
ATOM     10  CA  PRO C 666      63.144  41.289 140.048  1.00 74.10      A    C  
ANISOU   10  CA  PRO C 666     7539   8071  12543  -1657    642   2652  A    C  
ATOM     11  C   PRO C 666      63.073  41.214 141.574  1.00 71.28      A    C  
ANISOU   11  C   PRO C 666     7178   7640  12266  -1697    419   2421  A    C  
ATOM     12  O   PRO C 666      62.789  40.145 142.121  1.00 67.73      A    O  
ANISOU   12  O   PRO C 666     6737   7309  11687  -1547    425   2252  A    O  
ATOM     13  CB  PRO C 666      61.740  41.245 139.436  1.00 72.82      A    C  
ANISOU   13  CB  PRO C 666     7641   7842  12183  -1496    673   2563  A    C  
ATOM     14  CG  PRO C 666      61.928  40.537 138.137  1.00 73.48      A    C  
ANISOU   14  CG  PRO C 666     7704   8121  12093  -1379    925   2720  A    C  
ATOM     15  CD  PRO C 666      62.982  39.498 138.400  1.00 72.74      A    C  
ANISOU   15  CD  PRO C 666     7394   8245  12000  -1337   1036   2741  A    C  
ATOM     16  N   LYS C 667      63.329  42.338 142.236  1.00 70.30      A    N  
ANISOU   16  N   LYS C 667     7055   7312  12343  -1901    225   2418  A    N  
ATOM     17  CA  LYS C 667      63.327  42.426 143.697  1.00 70.03      A    C  
ANISOU   17  CA  LYS C 667     7036   7187  12385  -1965     -3   2205  A    C  
ATOM     18  C   LYS C 667      62.147  41.729 144.399  1.00 65.71      A    C  
ANISOU   18  C   LYS C 667     6674   6640  11654  -1759    -58   1927  A    C  
ATOM     19  O   LYS C 667      62.371  41.008 145.369  1.00 68.54      A    O  
ANISOU   19  O   LYS C 667     6963   7094  11985  -1724   -131   1788  A    O  
ATOM     20  CB  LYS C 667      63.379  43.899 144.120  1.00 76.08      A    C  
ANISOU   20  CB  LYS C 667     7895   7664  13348  -2185   -204   2212  A    C  
ATOM     21  CG  LYS C 667      63.318  44.146 145.615  1.00 79.31      A    C  
ANISOU   21  CG  LYS C 667     8372   7945  13819  -2260   -454   1981  A    C  
ATOM     22  CD  LYS C 667      64.618  43.773 146.298  1.00 84.79      A    C  
ANISOU   22  CD  LYS C 667     8800   8784  14630  -2412   -531   2034  A    C  
ATOM     23  CE  LYS C 667      64.851  44.647 147.530  1.00 89.52      A    C  
ANISOU   23  CE  LYS C 667     9473   9169  15370  -2618   -819   1897  A    C  
ATOM     24  NZ  LYS C 667      63.609  44.792 148.357  1.00 89.12      A    N1+
ANISOU   24  NZ  LYS C 667     9720   8948  15195  -2478   -938   1603  A    N1+
ATOM     25  N   PRO C 668      60.894  41.934 143.929  1.00 59.91      A    N  
ANISOU   25  N   PRO C 668     6162   5805  10794  -1626    -27   1859  A    N  
ATOM     26  CA  PRO C 668      59.793  41.232 144.618  1.00 55.47      A    C  
ANISOU   26  CA  PRO C 668     5745   5267  10066  -1441    -74   1614  A    C  
ATOM     27  C   PRO C 668      59.913  39.711 144.557  1.00 54.94      A    C  
ANISOU   27  C   PRO C 668     5583   5455   9836  -1290     56   1576  A    C  
ATOM     28  O   PRO C 668      59.560  39.022 145.506  1.00 54.84      A    O  
ANISOU   28  O   PRO C 668     5598   5492   9746  -1205    -15   1390  A    O  
ATOM     29  CB  PRO C 668      58.544  41.699 143.863  1.00 53.43      A    C  
ANISOU   29  CB  PRO C 668     5693   4896   9712  -1332    -35   1616  A    C  
ATOM     30  CG  PRO C 668      58.943  43.033 143.267  1.00 57.52      A    C  
ANISOU   30  CG  PRO C 668     6226   5228  10400  -1498    -60   1800  A    C  
ATOM     31  CD  PRO C 668      60.390  42.876 142.908  1.00 59.21      A    C  
ANISOU   31  CD  PRO C 668     6202   5569  10724  -1647     22   1996  A    C  
ATOM     32  N   VAL C 669      60.408  39.193 143.443  1.00 58.25      A    N  
ANISOU   32  N   VAL C 669     5906   6027  10198  -1252    252   1754  A    N  
ATOM     33  CA  VAL C 669      60.574  37.758 143.324  1.00 58.35      A    C  
ANISOU   33  CA  VAL C 669     5853   6259  10058  -1102    387   1723  A    C  
ATOM     34  C   VAL C 669      61.660  37.301 144.299  1.00 56.45      A    C  
ANISOU   34  C   VAL C 669     5408   6116   9924  -1163    326   1703  A    C  
ATOM     35  O   VAL C 669      61.483  36.312 145.007  1.00 51.15      A    O  
ANISOU   35  O   VAL C 669     4739   5539   9157  -1053    305   1559  A    O  
ATOM     36  CB  VAL C 669      60.926  37.339 141.891  1.00 59.36      A    C  
ANISOU   36  CB  VAL C 669     5941   6522  10090  -1038    622   1918  A    C  
ATOM     37  CG1 VAL C 669      61.116  35.835 141.832  1.00 63.55      A    C  
ANISOU   37  CG1 VAL C 669     6431   7252  10462   -872    758   1867  A    C  
ATOM     38  CG2 VAL C 669      59.828  37.768 140.937  1.00 56.22      A    C  
ANISOU   38  CG2 VAL C 669     5750   6040   9572   -981    663   1942  A    C  
ATOM     39  N   GLN C 670      62.761  38.050 144.361  1.00 56.31      A    N  
ANISOU   39  N   GLN C 670     5213   6074  10107  -1350    282   1856  A    N  
ATOM     40  CA  GLN C 670      63.850  37.724 145.276  1.00 57.53      A    C  
ANISOU   40  CA  GLN C 670     5149   6328  10381  -1432    200   1864  A    C  
ATOM     41  C   GLN C 670      63.342  37.674 146.707  1.00 56.70      A    C  
ANISOU   41  C   GLN C 670     5142   6140  10263  -1433    -18   1619  A    C  
ATOM     42  O   GLN C 670      63.636  36.732 147.444  1.00 56.14      A    O  
ANISOU   42  O   GLN C 670     4985   6202  10143  -1358    -40   1538  A    O  
ATOM     43  CB  GLN C 670      64.991  38.737 145.157  1.00 60.81      A    C  
ANISOU   43  CB  GLN C 670     5372   6700  11034  -1675    146   2070  A    C  
ATOM     44  CG  GLN C 670      65.755  38.642 143.851  1.00 63.03      A    C  
ANISOU   44  CG  GLN C 670     5491   7120  11336  -1673    383   2344  A    C  
ATOM     45  CD  GLN C 670      67.021  39.475 143.852  1.00 66.82      A    C  
ANISOU   45  CD  GLN C 670     5722   7603  12064  -1922    331   2569  A    C  
ATOM     46  NE2 GLN C 670      67.597  39.681 145.032  1.00 68.95      A    N  
ANISOU   46  NE2 GLN C 670     5873   7850  12477  -2072    114   2506  A    N  
ATOM     47  OE1 GLN C 670      67.484  39.913 142.801  0.99 65.65      A    O  
ANISOU   47  OE1 GLN C 670     5487   7486  11972  -1987    481   2805  A    O  
ATOM     48  N   ASP C 671      62.553  38.676 147.086  1.00 56.63      A    N  
ANISOU   48  N   ASP C 671     5323   5909  10285  -1502   -169   1503  A    N  
ATOM     49  CA  ASP C 671      61.960  38.717 148.418  1.00 56.37      A    C  
ANISOU   49  CA  ASP C 671     5417   5785  10215  -1486   -363   1261  A    C  
ATOM     50  C   ASP C 671      61.016  37.547 148.641  1.00 53.15      A    C  
ANISOU   50  C   ASP C 671     5116   5485   9593  -1259   -292   1104  A    C  
ATOM     51  O   ASP C 671      60.956  37.008 149.745  1.00 53.86      A    O  
ANISOU   51  O   ASP C 671     5209   5623   9633  -1220   -395    953  A    O  
ATOM     52  CB  ASP C 671      61.197  40.019 148.647  1.00 58.20      A    C  
ANISOU   52  CB  ASP C 671     5861   5749  10505  -1563   -502   1171  A    C  
ATOM     53  CG  ASP C 671      62.119  41.205 148.845  1.00 67.91      A    C  
ANISOU   53  CG  ASP C 671     7019   6827  11956  -1821   -644   1272  A    C  
ATOM     54  OD1 ASP C 671      63.316  41.000 149.142  1.00 67.89      A    O  
ANISOU   54  OD1 ASP C 671     6793   6939  12065  -1954   -687   1371  A    O  
ATOM     55  OD2 ASP C 671      61.636  42.349 148.721  1.00 75.77      A    O1-
ANISOU   55  OD2 ASP C 671     8184   7585  13021  -1893   -721   1256  A    O1-
ATOM     56  N   LEU C 672      60.266  37.179 147.606  1.00 48.61      A    N  
ANISOU   56  N   LEU C 672     4636   4945   8887  -1123   -129   1143  A    N  
ATOM     57  CA  LEU C 672      59.362  36.018 147.696  1.00 47.11      A    C  
ANISOU   57  CA  LEU C 672     4546   4860   8494   -927    -59   1015  A    C  
ATOM     58  C   LEU C 672      60.154  34.759 148.032  1.00 43.55      A    C  
ANISOU   58  C   LEU C 672     3941   4604   8001   -863      4   1026  A    C  
ATOM     59  O   LEU C 672      59.821  34.042 148.972  1.00 50.65      A    O  
ANISOU   59  O   LEU C 672     4876   5552   8818   -786    -63    878  A    O  
ATOM     60  CB  LEU C 672      58.594  35.804 146.387  1.00 43.83      A    C  
ANISOU   60  CB  LEU C 672     4241   4466   7948   -820    102   1087  A    C  
ATOM     61  CG  LEU C 672      57.692  34.558 146.321  1.00 47.11      A    C  
ANISOU   61  CG  LEU C 672     4758   4991   8152   -642    177    979  A    C  
ATOM     62  CD1 LEU C 672      56.540  34.646 147.323  1.00 44.71      A    C  
ANISOU   62  CD1 LEU C 672     4592   4609   7787   -589     39    780  A    C  
ATOM     63  CD2 LEU C 672      57.170  34.315 144.906  1.00 45.73      A    C  
ANISOU   63  CD2 LEU C 672     4674   4854   7846   -566    332   1079  A    C  
ATOM     64  N   ILE C 673      61.196  34.494 147.250  1.00 47.71      A    N  
ANISOU   64  N   ILE C 673     4299   5244   8584   -885    143   1215  A    N  
ATOM     65  CA  ILE C 673      62.062  33.331 147.466  1.00 49.28      A    C  
ANISOU   65  CA  ILE C 673     4334   5629   8761   -806    226   1258  A    C  
ATOM     66  C   ILE C 673      62.631  33.291 148.889  1.00 52.66      A    C  
ANISOU   66  C   ILE C 673     4651   6076   9281   -881     39   1175  A    C  
ATOM     67  O   ILE C 673      62.590  32.251 149.556  1.00 50.08      A    O  
ANISOU   67  O   ILE C 673     4316   5847   8864   -768     31   1085  A    O  
ATOM     68  CB  ILE C 673      63.231  33.306 146.458  1.00 52.90      A    C  
ANISOU   68  CB  ILE C 673     4596   6200   9303   -833    400   1500  A    C  
ATOM     69  CG1 ILE C 673      62.706  33.260 145.027  1.00 52.82      A    C  
ANISOU   69  CG1 ILE C 673     4712   6188   9169   -748    593   1583  A    C  
ATOM     70  CG2 ILE C 673      64.149  32.116 146.712  1.00 54.00      A    C  
ANISOU   70  CG2 ILE C 673     4557   6530   9429   -726    492   1553  A    C  
ATOM     71  CD1 ILE C 673      61.778  32.106 144.777  1.00 52.68      A    C  
ANISOU   71  CD1 ILE C 673     4875   6218   8922   -554    685   1457  A    C  
ATOM     72  N   LYS C 674      63.159  34.425 149.348  1.00 54.33      A    N  
ANISOU   72  N   LYS C 674     4789   6188   9668  -1078   -120   1210  A    N  
ATOM     73  CA  LYS C 674      63.735  34.509 150.687  1.00 54.56      A    C  
ANISOU   73  CA  LYS C 674     4722   6228   9780  -1179   -325   1135  A    C  
ATOM     74  C   LYS C 674      62.712  34.141 151.757  1.00 51.53      A    C  
ANISOU   74  C   LYS C 674     4531   5796   9253  -1085   -443    892  A    C  
ATOM     75  O   LYS C 674      63.001  33.367 152.662  1.00 50.22      A    O  
ANISOU   75  O   LYS C 674     4302   5736   9044  -1036   -509    827  A    O  
ATOM     76  CB  LYS C 674      64.271  35.912 150.961  1.00 57.98      A    C  
ANISOU   76  CB  LYS C 674     5108   6515  10407  -1426   -499   1186  A    C  
ATOM     77  CG  LYS C 674      65.625  36.209 150.346  0.78 62.16      A    C  
ANISOU   77  CG  LYS C 674     5364   7134  11118  -1569   -442   1443  A    C  
ATOM     78  CD  LYS C 674      66.046  37.646 150.634  0.79 67.48      A    C  
ANISOU   78  CD  LYS C 674     6025   7631  11985  -1840   -637   1485  A    C  
ATOM     79  CE  LYS C 674      67.196  38.082 149.742  1.00 73.51      A    C  
ANISOU   79  CE  LYS C 674     6537   8465  12928  -1990   -543   1774  A    C  
ATOM     80  NZ  LYS C 674      67.267  39.570 149.588  0.76 78.47      A    N1+
ANISOU   80  NZ  LYS C 674     7231   8864  13718  -2235   -675   1831  A    N1+
ATOM     81  N   MET C 675      61.510  34.688 151.660  1.00 49.57      A    N  
ANISOU   81  N   MET C 675     4509   5397   8929  -1051   -465    769  A    N  
ATOM     82  CA  MET C 675      60.555  34.468 152.738  1.00 52.53      A    C  
ANISOU   82  CA  MET C 675     5052   5728   9179   -972   -577    550  A    C  
ATOM     83  C   MET C 675      60.015  33.023 152.762  1.00 51.38      A    C  
ANISOU   83  C   MET C 675     4940   5729   8855   -776   -459    495  A    C  
ATOM     84  O   MET C 675      59.755  32.499 153.841  1.00 53.46      A    O  
ANISOU   84  O   MET C 675     5244   6033   9035   -724   -549    364  A    O  
ATOM     85  CB  MET C 675      59.404  35.476 152.663  1.00 51.73      A    C  
ANISOU   85  CB  MET C 675     5170   5430   9054   -973   -626    445  A    C  
ATOM     86  CG  MET C 675      58.143  34.975 152.010  1.00 52.41      A    C  
ANISOU   86  CG  MET C 675     5398   5532   8984   -802   -490    404  A    C  
ATOM     87  SD  MET C 675      56.842  36.236 152.046  1.00 67.22      A    S  
ANISOU   87  SD  MET C 675     7503   7185  10853   -789   -562    296  A    S  
ATOM     88  CE  MET C 675      57.433  37.351 150.789  1.00 62.96      A    C  
ANISOU   88  CE  MET C 675     6918   6526  10479   -926   -513    497  A    C  
ATOM     89  N   ILE C 676      59.875  32.360 151.611  1.00 46.05      A    N  
ANISOU   89  N   ILE C 676     4257   5128   8111   -673   -264    595  A    N  
ATOM     90  CA  ILE C 676      59.314  31.003 151.638  1.00 45.64      A    C  
ANISOU   90  CA  ILE C 676     4269   5185   7888   -503   -167    533  A    C  
ATOM     91  C   ILE C 676      60.363  29.957 152.002  1.00 45.12      A    C  
ANISOU   91  C   ILE C 676     4036   5273   7834   -455   -132    597  A    C  
ATOM     92  O   ILE C 676      60.029  28.888 152.523  1.00 42.50      A    O  
ANISOU   92  O   ILE C 676     3753   5012   7383   -340   -119    519  A    O  
ATOM     93  CB  ILE C 676      58.663  30.588 150.301  1.00 45.36      A    C  
ANISOU   93  CB  ILE C 676     4330   5161   7742   -405     15    592  A    C  
ATOM     94  CG1 ILE C 676      59.705  30.394 149.200  1.00 47.45      A    C  
ANISOU   94  CG1 ILE C 676     4458   5505   8064   -407    176    783  A    C  
ATOM     95  CG2 ILE C 676      57.573  31.575 149.892  1.00 44.83      A    C  
ANISOU   95  CG2 ILE C 676     4418   4956   7659   -434    -19    548  A    C  
ATOM     96  CD1 ILE C 676      59.081  30.132 147.844  1.00 50.02      A    C  
ANISOU   96  CD1 ILE C 676     4907   5830   8267   -326    342    838  A    C  
ATOM     97  N   PHE C 677      61.629  30.257 151.744  1.00 48.34      A    N  
ANISOU   97  N   PHE C 677     4241   5734   8392   -542   -116    752  A    N  
ATOM     98  CA  PHE C 677      62.690  29.324 152.106  1.00 53.01      A    C  
ANISOU   98  CA  PHE C 677     4646   6481   9014   -486    -85    834  A    C  
ATOM     99  C   PHE C 677      63.328  29.691 153.447  1.00 56.54      A    C  
ANISOU   99  C   PHE C 677     4978   6944   9559   -605   -308    794  A    C  
ATOM    100  O   PHE C 677      64.393  29.183 153.795  1.00 58.06      A    O  
ANISOU  100  O   PHE C 677     4968   7269   9824   -600   -320    896  A    O  
ATOM    101  CB  PHE C 677      63.754  29.272 151.009  1.00 54.04      A    C  
ANISOU  101  CB  PHE C 677     4590   6701   9240   -483     87   1053  A    C  
ATOM    102  CG  PHE C 677      63.402  28.358 149.863  1.00 54.46      A    C  
ANISOU  102  CG  PHE C 677     4739   6800   9152   -308    326   1094  A    C  
ATOM    103  CD1 PHE C 677      63.340  26.980 150.050  1.00 52.66      A    C  
ANISOU  103  CD1 PHE C 677     4552   6656   8801   -131    411   1052  A    C  
ATOM    104  CD2 PHE C 677      63.138  28.872 148.599  1.00 50.30      A    C  
ANISOU  104  CD2 PHE C 677     4280   6224   8608   -322    459   1174  A    C  
ATOM    105  CE1 PHE C 677      63.026  26.133 148.997  1.00 51.67      A    C  
ANISOU  105  CE1 PHE C 677     4546   6553   8535     23    620   1077  A    C  
ATOM    106  CE2 PHE C 677      62.820  28.033 147.540  1.00 45.33      A    C  
ANISOU  106  CE2 PHE C 677     3763   5634   7827   -168    667   1202  A    C  
ATOM    107  CZ  PHE C 677      62.762  26.663 147.739  1.00 49.08      A    C  
ANISOU  107  CZ  PHE C 677     4291   6180   8176      2    745   1146  A    C  
ATOM    108  N   ASP C 678      62.669  30.564 154.203  1.00 56.99      A    N  
ANISOU  108  N   ASP C 678     5172   6870   9612   -705   -485    646  A    N  
ATOM    109  CA  ASP C 678      63.210  31.006 155.490  1.00 59.62      A    C  
ANISOU  109  CA  ASP C 678     5438   7199  10016   -834   -716    587  A    C  
ATOM    110  C   ASP C 678      63.187  29.865 156.519  1.00 54.79      A    C  
ANISOU  110  C   ASP C 678     4824   6707   9286   -717   -765    509  A    C  
ATOM    111  O   ASP C 678      62.123  29.443 156.978  1.00 52.60      A    O  
ANISOU  111  O   ASP C 678     4736   6399   8852   -614   -767    357  A    O  
ATOM    112  CB  ASP C 678      62.432  32.213 156.027  1.00 60.06      A    C  
ANISOU  112  CB  ASP C 678     5686   7064  10070   -944   -877    429  A    C  
ATOM    113  CG  ASP C 678      63.196  32.964 157.105  1.00 66.69      A    C  
ANISOU  113  CG  ASP C 678     6458   7867  11012  -1131  -1123    395  A    C  
ATOM    114  OD1 ASP C 678      63.654  32.335 158.078  1.00 64.38      A    O  
ANISOU  114  OD1 ASP C 678     6090   7691  10681  -1118  -1229    366  A    O  
ATOM    115  OD2 ASP C 678      63.357  34.194 156.973  1.00 74.00      A    O1-
ANISOU  115  OD2 ASP C 678     7415   8643  12058  -1301  -1222    403  A    O1-
ATOM    116  N   VAL C 679      64.374  29.393 156.880  1.00 55.89      A    N  
ANISOU  116  N   VAL C 679     4738   6988   9508   -736   -807    629  A    N  
ATOM    117  CA  VAL C 679      64.536  28.283 157.810  1.00 57.84      A    C  
ANISOU  117  CA  VAL C 679     4954   7361   9662   -624   -852    595  A    C  
ATOM    118  C   VAL C 679      64.075  28.654 159.219  1.00 56.38      A    C  
ANISOU  118  C   VAL C 679     4902   7124   9397   -694  -1083    414  A    C  
ATOM    119  O   VAL C 679      63.470  27.838 159.917  1.00 55.72      A    O  
ANISOU  119  O   VAL C 679     4931   7080   9159   -573  -1091    313  A    O  
ATOM    120  CB  VAL C 679      66.008  27.808 157.839  1.00 66.14      A    C  
ANISOU  120  CB  VAL C 679     5702   8582  10844   -631   -853    794  A    C  
ATOM    121  CG1 VAL C 679      66.268  26.882 159.014  1.00 69.69      A    C  
ANISOU  121  CG1 VAL C 679     6112   9151  11217   -550   -963    763  A    C  
ATOM    122  CG2 VAL C 679      66.360  27.121 156.532  1.00 66.01      A    C  
ANISOU  122  CG2 VAL C 679     5588   8638  10853   -488   -582    956  A    C  
ATOM    123  N   GLU C 680      64.338  29.887 159.637  1.00 54.92      A    N  
ANISOU  123  N   GLU C 680     4720   6842   9306   -891  -1269    373  A    N  
ATOM    124  CA  GLU C 680      63.897  30.318 160.957  1.00 57.65      A    C  
ANISOU  124  CA  GLU C 680     5223   7124   9556   -955  -1485    186  A    C  
ATOM    125  C   GLU C 680      62.375  30.353 161.013  1.00 52.51      A    C  
ANISOU  125  C   GLU C 680     4850   6361   8739   -839  -1413      6  A    C  
ATOM    126  O   GLU C 680      61.780  30.073 162.051  1.00 50.97      A    O  
ANISOU  126  O   GLU C 680     4793   6178   8394   -781  -1497   -138  A    O  
ATOM    127  CB  GLU C 680      64.487  31.685 161.322  1.00 63.67      A    C  
ANISOU  127  CB  GLU C 680     5964   7774  10453  -1200  -1702    170  A    C  
ATOM    128  CG  GLU C 680      65.967  31.641 161.704  0.64 70.69      A    C  
ANISOU  128  CG  GLU C 680     6576   8799  11485  -1343  -1851    326  A    C  
ATOM    129  CD  GLU C 680      66.331  30.430 162.552  0.71 73.53      A    C  
ANISOU  129  CD  GLU C 680     6839   9352  11746  -1224  -1893    348  A    C  
ATOM    130  OE1 GLU C 680      65.687  30.214 163.603  0.99 75.92      A    O  
ANISOU  130  OE1 GLU C 680     7325   9643  11878  -1172  -1998    177  A    O  
ATOM    131  OE2 GLU C 680      67.270  29.696 162.171  1.00 73.48      A    O1-
ANISOU  131  OE2 GLU C 680     6573   9512  11833  -1174  -1814    545  A    O1-
ATOM    132  N   SER C 681      61.745  30.678 159.886  1.00 53.09      A    N  
ANISOU  132  N   SER C 681     4996   6341   8836   -802  -1252     28  A    N  
ATOM    133  CA  SER C 681      60.290  30.654 159.786  1.00 52.22      A    C  
ANISOU  133  CA  SER C 681     5112   6147   8581   -683  -1166   -109  A    C  
ATOM    134  C   SER C 681      59.724  29.246 159.980  1.00 48.99      A    C  
ANISOU  134  C   SER C 681     4740   5862   8013   -502  -1055   -128  A    C  
ATOM    135  O   SER C 681      58.706  29.058 160.657  1.00 46.59      A    O  
ANISOU  135  O   SER C 681     4599   5542   7562   -424  -1074   -266  A    O  
ATOM    136  CB  SER C 681      59.838  31.202 158.431  1.00 56.96      A    C  
ANISOU  136  CB  SER C 681     5752   6645   9244   -681  -1019    -45  A    C  
ATOM    137  OG  SER C 681      60.057  32.599 158.351  1.00 62.67      A    O  
ANISOU  137  OG  SER C 681     6506   7212  10094   -839  -1128    -56  A    O  
ATOM    138  N   MET C 682      60.377  28.265 159.366  1.00 46.28      A    N  
ANISOU  138  N   MET C 682     4250   5636   7700   -434   -932     16  A    N  
ATOM    139  CA  MET C 682      59.942  26.879 159.476  1.00 44.54      A    C  
ANISOU  139  CA  MET C 682     4071   5512   7342   -271   -826     13  A    C  
ATOM    140  C   MET C 682      60.020  26.425 160.942  1.00 46.07      A    C  
ANISOU  140  C   MET C 682     4283   5781   7442   -254   -975    -67  A    C  
ATOM    141  O   MET C 682      59.107  25.767 161.459  1.00 45.63      A    O  
ANISOU  141  O   MET C 682     4361   5744   7232   -156   -951   -154  A    O  
ATOM    142  CB  MET C 682      60.803  25.980 158.580  1.00 45.10      A    C  
ANISOU  142  CB  MET C 682     3986   5678   7474   -195   -672    184  A    C  
ATOM    143  CG  MET C 682      60.881  26.407 157.110  1.00 41.10      A    C  
ANISOU  143  CG  MET C 682     3451   5116   7048   -212   -518    282  A    C  
ATOM    144  SD  MET C 682      62.066  25.389 156.181  1.00 52.11      A    S  
ANISOU  144  SD  MET C 682     4654   6636   8508   -106   -331    486  A    S  
ATOM    145  CE  MET C 682      62.159  26.255 154.610  1.00 45.97      A    C  
ANISOU  145  CE  MET C 682     3856   5790   7821   -167   -186    590  A    C  
ATOM    146  N   LYS C 683      61.113  26.786 161.608  1.00 47.51      A    N  
ANISOU  146  N   LYS C 683     4325   6012   7716   -360  -1135    -25  A    N  
ATOM    147  CA  LYS C 683      61.291  26.444 163.013  1.00 48.77      A    C  
ANISOU  147  CA  LYS C 683     4498   6250   7781   -360  -1300    -91  A    C  
ATOM    148  C   LYS C 683      60.189  27.038 163.877  1.00 50.26      A    C  
ANISOU  148  C   LYS C 683     4915   6353   7830   -372  -1392   -289  A    C  
ATOM    149  O   LYS C 683      59.605  26.345 164.708  1.00 48.39      A    O  
ANISOU  149  O   LYS C 683     4777   6176   7432   -279  -1403   -360  A    O  
ATOM    150  CB  LYS C 683      62.650  26.925 163.514  1.00 48.75      A    C  
ANISOU  150  CB  LYS C 683     4304   6307   7911   -506  -1485    -10  A    C  
ATOM    151  CG  LYS C 683      63.821  26.222 162.876  1.00 49.95      A    C  
ANISOU  151  CG  LYS C 683     4199   6585   8194   -468  -1398    202  A    C  
ATOM    152  CD  LYS C 683      65.112  26.836 163.351  1.00 53.68      A    C  
ANISOU  152  CD  LYS C 683     4462   7122   8813   -638  -1597    294  A    C  
ATOM    153  CE  LYS C 683      66.301  26.183 162.692  0.97 57.96      A    C  
ANISOU  153  CE  LYS C 683     4717   7806   9498   -587  -1496    527  A    C  
ATOM    154  NZ  LYS C 683      67.535  26.964 162.991  0.88 62.47      A    N1+
ANISOU  154  NZ  LYS C 683     5056   8437  10243   -789  -1690    639  A    N1+
ATOM    155  N   LYS C 684      59.891  28.318 163.673  1.00 51.04      A    N  
ANISOU  155  N   LYS C 684     5099   6308   7986   -476  -1446   -370  A    N  
ATOM    156  CA  LYS C 684      58.875  28.976 164.485  1.00 54.13      A    C  
ANISOU  156  CA  LYS C 684     5712   6607   8248   -468  -1522   -559  A    C  
ATOM    157  C   LYS C 684      57.501  28.353 164.250  1.00 53.38      A    C  
ANISOU  157  C   LYS C 684     5751   6519   8011   -307  -1354   -612  A    C  
ATOM    158  O   LYS C 684      56.732  28.181 165.194  1.00 55.24      A    O  
ANISOU  158  O   LYS C 684     6123   6779   8086   -238  -1386   -728  A    O  
ATOM    159  CB  LYS C 684      58.869  30.492 164.211  1.00 56.91      A    C  
ANISOU  159  CB  LYS C 684     6137   6778   8707   -602  -1603   -624  A    C  
ATOM    160  CG  LYS C 684      60.228  31.103 164.514  0.66 62.94      A    C  
ANISOU  160  CG  LYS C 684     6766   7536   9612   -793  -1794   -566  A    C  
ATOM    161  CD  LYS C 684      60.336  32.615 164.345  0.87 67.13      A    C  
ANISOU  161  CD  LYS C 684     7382   7867  10258   -955  -1904   -626  A    C  
ATOM    162  CE  LYS C 684      61.780  33.033 164.654  1.00 71.46      A    C  
ANISOU  162  CE  LYS C 684     7758   8441  10952  -1166  -2105   -537  A    C  
ATOM    163  NZ  LYS C 684      62.040  34.501 164.636  0.83 77.00      A    N1+
ANISOU  163  NZ  LYS C 684     8546   8936  11772  -1365  -2257   -592  A    N1+
ATOM    164  N   ALA C 685      57.195  28.004 163.001  1.00 52.76      A    N  
ANISOU  164  N   ALA C 685     5633   6428   7986   -252  -1178   -519  A    N  
ATOM    165  CA  ALA C 685      55.955  27.288 162.707  1.00 50.84      A    C  
ANISOU  165  CA  ALA C 685     5493   6207   7617   -120  -1030   -544  A    C  
ATOM    166  C   ALA C 685      55.875  25.993 163.525  1.00 49.94      A    C  
ANISOU  166  C   ALA C 685     5380   6226   7367    -30  -1025   -537  A    C  
ATOM    167  O   ALA C 685      54.851  25.700 164.149  1.00 50.55      A    O  
ANISOU  167  O   ALA C 685     5580   6329   7298     44  -1006   -619  A    O  
ATOM    168  CB  ALA C 685      55.842  26.987 161.215  1.00 48.41      A    C  
ANISOU  168  CB  ALA C 685     5136   5878   7380    -91   -862   -431  A    C  
ATOM    169  N   MET C 686      56.968  25.236 163.543  1.00 44.98      A    N  
ANISOU  169  N   MET C 686     4610   5687   6792    -32  -1040   -426  A    N  
ATOM    170  CA  MET C 686      56.992  23.975 164.269  1.00 47.78      A    C  
ANISOU  170  CA  MET C 686     4964   6157   7033     58  -1036   -396  A    C  
ATOM    171  C   MET C 686      56.781  24.223 165.756  1.00 47.59      A    C  
ANISOU  171  C   MET C 686     5026   6173   6882     43  -1190   -510  A    C  
ATOM    172  O   MET C 686      56.052  23.494 166.416  1.00 45.84      A    O  
ANISOU  172  O   MET C 686     4898   6012   6508    125  -1162   -544  A    O  
ATOM    173  CB  MET C 686      58.315  23.236 164.027  1.00 53.70      A    C  
ANISOU  173  CB  MET C 686     5532   6989   7881     70  -1031   -245  A    C  
ATOM    174  CG  MET C 686      58.473  22.711 162.593  1.00 53.14      A    C  
ANISOU  174  CG  MET C 686     5405   6895   7891    127   -844   -131  A    C  
ATOM    175  SD  MET C 686      60.090  21.968 162.272  1.00 59.67      A    S  
ANISOU  175  SD  MET C 686     6003   7820   8846    168   -816     56  A    S  
ATOM    176  CE  MET C 686      60.021  20.482 163.268  1.00 58.44      A    C  
ANISOU  176  CE  MET C 686     5892   7761   8554    300   -829     79  A    C  
ATOM    177  N   VAL C 687      57.411  25.269 166.274  1.00 49.02      A    N  
ANISOU  177  N   VAL C 687     5187   6318   7119    -70  -1354   -568  A    N  
ATOM    178  CA  VAL C 687      57.306  25.583 167.691  1.00 53.96      A    C  
ANISOU  178  CA  VAL C 687     5916   6976   7610    -92  -1516   -687  A    C  
ATOM    179  C   VAL C 687      55.861  25.962 168.015  1.00 54.94      A    C  
ANISOU  179  C   VAL C 687     6242   7044   7590    -22  -1453   -830  A    C  
ATOM    180  O   VAL C 687      55.297  25.504 169.011  1.00 52.18      A    O  
ANISOU  180  O   VAL C 687     5991   6771   7064     50  -1469   -890  A    O  
ATOM    181  CB  VAL C 687      58.287  26.708 168.082  1.00 55.18      A    C  
ANISOU  181  CB  VAL C 687     6027   7078   7861   -251  -1720   -726  A    C  
ATOM    182  CG1 VAL C 687      57.912  27.315 169.418  1.00 59.02      A    C  
ANISOU  182  CG1 VAL C 687     6694   7548   8185   -275  -1876   -898  A    C  
ATOM    183  CG2 VAL C 687      59.707  26.164 168.121  1.00 53.80      A    C  
ANISOU  183  CG2 VAL C 687     5632   7015   7794   -307  -1808   -573  A    C  
ATOM    184  N   GLU C 688      55.255  26.755 167.135  1.00 54.45      A    N  
ANISOU  184  N   GLU C 688     6226   6858   7603    -31  -1368   -865  A    N  
ATOM    185  CA  GLU C 688      53.841  27.110 167.229  1.00 56.01      A    C  
ANISOU  185  CA  GLU C 688     6582   7009   7692     55  -1280   -969  A    C  
ATOM    186  C   GLU C 688      52.920  25.881 167.307  1.00 53.81      A    C  
ANISOU  186  C   GLU C 688     6323   6841   7281    175  -1144   -923  A    C  
ATOM    187  O   GLU C 688      51.824  25.945 167.861  1.00 54.31      A    O  
ANISOU  187  O   GLU C 688     6502   6927   7208    254  -1097  -1002  A    O  
ATOM    188  CB  GLU C 688      53.454  27.971 166.026  1.00 60.50      A    C  
ANISOU  188  CB  GLU C 688     7156   7440   8390     33  -1197   -961  A    C  
ATOM    189  CG  GLU C 688      52.118  28.669 166.126  0.89 64.26      A    C  
ANISOU  189  CG  GLU C 688     7783   7846   8788    115  -1134  -1070  A    C  
ATOM    190  CD  GLU C 688      52.033  29.857 165.187  0.51 68.95      A    C  
ANISOU  190  CD  GLU C 688     8398   8274   9525     67  -1120  -1077  A    C  
ATOM    191  OE1 GLU C 688      51.122  29.878 164.335  0.73 70.91      A    O  
ANISOU  191  OE1 GLU C 688     8655   8498   9787    133   -990  -1038  A    O  
ATOM    192  OE2 GLU C 688      52.884  30.766 165.298  0.75 71.48      A    O1-
ANISOU  192  OE2 GLU C 688     8724   8489   9945    -46  -1247  -1112  A    O1-
ATOM    193  N   TYR C 689      53.356  24.764 166.740  1.00 51.65      A    N  
ANISOU  193  N   TYR C 689     5940   6633   7051    190  -1074   -789  A    N  
ATOM    194  CA  TYR C 689      52.593  23.523 166.841  1.00 53.28      A    C  
ANISOU  194  CA  TYR C 689     6175   6930   7141    279   -966   -735  A    C  
ATOM    195  C   TYR C 689      52.965  22.688 168.062  1.00 55.43      A    C  
ANISOU  195  C   TYR C 689     6453   7320   7289    310  -1043   -720  A    C  
ATOM    196  O   TYR C 689      52.603  21.514 168.142  1.00 57.11      A    O  
ANISOU  196  O   TYR C 689     6672   7601   7426    371   -966   -645  A    O  
ATOM    197  CB  TYR C 689      52.794  22.671 165.595  1.00 54.90      A    C  
ANISOU  197  CB  TYR C 689     6299   7124   7436    291   -845   -606  A    C  
ATOM    198  CG  TYR C 689      51.979  23.094 164.410  1.00 56.42      A    C  
ANISOU  198  CG  TYR C 689     6519   7235   7682    289   -734   -604  A    C  
ATOM    199  CD1 TYR C 689      50.586  23.015 164.435  1.00 55.39      A    C  
ANISOU  199  CD1 TYR C 689     6476   7119   7452    338   -660   -639  A    C  
ATOM    200  CD2 TYR C 689      52.599  23.535 163.247  1.00 58.70      A    C  
ANISOU  200  CD2 TYR C 689     6737   7449   8119    240   -701   -548  A    C  
ATOM    201  CE1 TYR C 689      49.832  23.393 163.335  1.00 56.31      A    C  
ANISOU  201  CE1 TYR C 689     6606   7173   7616    335   -573   -622  A    C  
ATOM    202  CE2 TYR C 689      51.858  23.918 162.154  1.00 60.66      A    C  
ANISOU  202  CE2 TYR C 689     7017   7629   8403    239   -608   -536  A    C  
ATOM    203  CZ  TYR C 689      50.478  23.842 162.201  1.00 60.59      A    C  
ANISOU  203  CZ  TYR C 689     7093   7634   8294    286   -553   -574  A    C  
ATOM    204  OH  TYR C 689      49.751  24.220 161.099  1.00 66.52      A    O  
ANISOU  204  OH  TYR C 689     7865   8329   9081    282   -476   -549  A    O  
ATOM    205  N   GLU C 690      53.701  23.289 168.989  1.00 53.84      A    N  
ANISOU  205  N   GLU C 690     6255   7133   7066    260  -1204   -785  A    N  
ATOM    206  CA  GLU C 690      54.162  22.615 170.201  1.00 57.23      A    C  
ANISOU  206  CA  GLU C 690     6692   7681   7373    281  -1306   -768  A    C  
ATOM    207  C   GLU C 690      55.090  21.434 169.931  1.00 55.23      A    C  
ANISOU  207  C   GLU C 690     6304   7494   7186    300  -1296   -608  A    C  
ATOM    208  O   GLU C 690      55.186  20.528 170.751  1.00 55.64      A    O  
ANISOU  208  O   GLU C 690     6370   7646   7126    353  -1326   -557  A    O  
ATOM    209  CB  GLU C 690      52.982  22.130 171.041  1.00 59.65      A    C  
ANISOU  209  CB  GLU C 690     7128   8062   7472    369  -1242   -812  A    C  
ATOM    210  CG  GLU C 690      52.049  23.211 171.509  1.00 62.08      A    C  
ANISOU  210  CG  GLU C 690     7575   8327   7683    389  -1241   -967  A    C  
ATOM    211  CD  GLU C 690      51.219  22.743 172.677  0.23 62.58      A    C  
ANISOU  211  CD  GLU C 690     7751   8506   7520    473  -1214  -1001  A    C  
ATOM    212  OE1 GLU C 690      50.120  22.209 172.430  0.94 64.96      A    O  
ANISOU  212  OE1 GLU C 690     8071   8843   7767    540  -1064   -958  A    O  
ATOM    213  OE2 GLU C 690      51.674  22.899 173.833  1.00 60.58      A    O1-
ANISOU  213  OE2 GLU C 690     7564   8314   7140    466  -1347  -1062  A    O1-
ATOM    214  N   ILE C 691      55.780  21.453 168.798  1.00 49.38      A    N  
ANISOU  214  N   ILE C 691     5438   6698   6624    270  -1248   -523  A    N  
ATOM    215  CA  ILE C 691      56.766  20.430 168.501  1.00 47.67      A    C  
ANISOU  215  CA  ILE C 691     5089   6537   6485    308  -1229   -371  A    C  
ATOM    216  C   ILE C 691      58.045  20.716 169.277  1.00 50.28      A    C  
ANISOU  216  C   ILE C 691     5304   6942   6859    247  -1419   -339  A    C  
ATOM    217  O   ILE C 691      58.461  21.873 169.401  1.00 49.52      A    O  
ANISOU  217  O   ILE C 691     5181   6807   6827    136  -1543   -408  A    O  
ATOM    218  CB  ILE C 691      57.059  20.357 166.994  1.00 47.56      A    C  
ANISOU  218  CB  ILE C 691     4987   6449   6633    311  -1092   -288  A    C  
ATOM    219  CG1 ILE C 691      55.859  19.761 166.274  1.00 50.41      A    C  
ANISOU  219  CG1 ILE C 691     5463   6759   6932    374   -920   -293  A    C  
ATOM    220  CG2 ILE C 691      58.278  19.486 166.712  1.00 47.58      A    C  
ANISOU  220  CG2 ILE C 691     4835   6510   6733    363  -1077   -131  A    C  
ATOM    221  CD1 ILE C 691      55.831  20.100 164.834  1.00 55.19      A    C  
ANISOU  221  CD1 ILE C 691     6038   7276   7657    355   -804   -265  A    C  
ATOM    222  N   ASP C 692      58.651  19.660 169.817  1.00 50.85      A    N  
ANISOU  222  N   ASP C 692     5310   7116   6894    314  -1454   -227  A    N  
ATOM    223  CA  ASP C 692      59.904  19.800 170.548  1.00 52.85      A    C  
ANISOU  223  CA  ASP C 692     5428   7465   7189    262  -1645   -167  A    C  
ATOM    224  C   ASP C 692      61.048  19.892 169.563  1.00 53.63      A    C  
ANISOU  224  C   ASP C 692     5310   7558   7508    237  -1619    -37  A    C  
ATOM    225  O   ASP C 692      61.551  18.868 169.087  1.00 54.69      A    O  
ANISOU  225  O   ASP C 692     5344   7731   7706    344  -1516    109  A    O  
ATOM    226  CB  ASP C 692      60.122  18.622 171.498  1.00 55.77      A    C  
ANISOU  226  CB  ASP C 692     5801   7953   7437    359  -1692    -76  A    C  
ATOM    227  CG  ASP C 692      61.260  18.866 172.497  1.00 57.44      A    C  
ANISOU  227  CG  ASP C 692     5896   8282   7647    293  -1931    -32  A    C  
ATOM    228  OD1 ASP C 692      62.213  19.619 172.174  1.00 58.62      A    O  
ANISOU  228  OD1 ASP C 692     5887   8434   7954    188  -2033     -1  A    O  
ATOM    229  OD2 ASP C 692      61.191  18.282 173.599  1.00 55.47      A    O1-
ANISOU  229  OD2 ASP C 692     5712   8129   7236    340  -2020    -15  A    O1-
ATOM    230  N   LEU C 693      61.460  21.118 169.263  1.00 53.42      A    N  
ANISOU  230  N   LEU C 693     5221   7480   7597     99  -1706    -86  A    N  
ATOM    231  CA  LEU C 693      62.524  21.353 168.306  1.00 54.73      A    C  
ANISOU  231  CA  LEU C 693     5171   7647   7977     55  -1675     45  A    C  
ATOM    232  C   LEU C 693      63.838  20.740 168.746  1.00 58.37      A    C  
ANISOU  232  C   LEU C 693     5414   8255   8511     79  -1780    213  A    C  
ATOM    233  O   LEU C 693      64.621  20.290 167.916  1.00 61.34      A    O  
ANISOU  233  O   LEU C 693     5606   8666   9032    141  -1672    371  A    O  
ATOM    234  CB  LEU C 693      62.705  22.849 168.080  1.00 58.20      A    C  
ANISOU  234  CB  LEU C 693     5595   7999   8518   -124  -1781    -36  A    C  
ATOM    235  CG  LEU C 693      62.989  23.214 166.628  1.00 61.84      A    C  
ANISOU  235  CG  LEU C 693     5946   8389   9162   -147  -1629     47  A    C  
ATOM    236  CD1 LEU C 693      61.935  22.614 165.714  1.00 58.87      A    C  
ANISOU  236  CD1 LEU C 693     5702   7938   8726    -15  -1389     25  A    C  
ATOM    237  CD2 LEU C 693      63.029  24.723 166.481  1.00 66.15      A    C  
ANISOU  237  CD2 LEU C 693     6514   8824   9795   -329  -1739    -40  A    C  
ATOM    238  N   GLN C 694      64.089  20.724 170.051  1.00 58.92      A    N  
ANISOU  238  N   GLN C 694     5500   8416   8471     40  -1987    186  A    N  
ATOM    239  CA  GLN C 694      65.340  20.164 170.549  1.00 58.44      A    C  
ANISOU  239  CA  GLN C 694     5220   8511   8475     61  -2114    358  A    C  
ATOM    240  C   GLN C 694      65.349  18.652 170.390  1.00 57.75      A    C  
ANISOU  240  C   GLN C 694     5112   8477   8355    276  -1953    492  A    C  
ATOM    241  O   GLN C 694      66.369  18.062 170.066  1.00 60.92      A    O  
ANISOU  241  O   GLN C 694     5296   8965   8885    356  -1924    678  A    O  
ATOM    242  CB  GLN C 694      65.572  20.548 172.011  1.00 62.12      A    C  
ANISOU  242  CB  GLN C 694     5730   9063   8809    -45  -2396    291  A    C  
ATOM    243  CG  GLN C 694      66.983  21.079 172.297  1.00 68.58      A    C  
ANISOU  243  CG  GLN C 694     6291   9992   9773   -190  -2625    408  A    C  
ATOM    244  N   LYS C 695      64.201  18.026 170.611  1.00 55.55      A    N  
ANISOU  244  N   LYS C 695     5060   8140   7905    372  -1846    405  A    N  
ATOM    245  CA  LYS C 695      64.106  16.581 170.498  1.00 55.24      A    C  
ANISOU  245  CA  LYS C 695     5045   8119   7823    563  -1701    520  A    C  
ATOM    246  C   LYS C 695      63.919  16.150 169.029  1.00 59.25      A    C  
ANISOU  246  C   LYS C 695     5551   8521   8439    659  -1442    567  A    C  
ATOM    247  O   LYS C 695      64.349  15.069 168.630  1.00 62.61      A    O  
ANISOU  247  O   LYS C 695     5920   8958   8909    817  -1319    706  A    O  
ATOM    248  CB  LYS C 695      62.963  16.084 171.372  1.00 53.65      A    C  
ANISOU  248  CB  LYS C 695     5085   7905   7396    604  -1703    422  A    C  
ATOM    249  CG  LYS C 695      63.080  14.669 171.844  1.00 54.55      A    C  
ANISOU  249  CG  LYS C 695     5220   8073   7435    764  -1664    555  A    C  
ATOM    250  CD  LYS C 695      62.196  14.457 173.051  1.00 55.65      A    C  
ANISOU  250  CD  LYS C 695     5555   8248   7343    755  -1745    471  A    C  
ATOM    251  CE  LYS C 695      61.742  13.024 173.139  1.00 57.69      A    C  
ANISOU  251  CE  LYS C 695     5920   8481   7516    906  -1615    569  A    C  
ATOM    252  NZ  LYS C 695      62.893  12.105 173.193  1.00 64.53      A    N1+
ANISOU  252  NZ  LYS C 695     6629   9415   8475   1035  -1636    770  A    N1+
ATOM    253  N   MET C 696      63.274  16.999 168.226  1.00 55.93      A    N  
ANISOU  253  N   MET C 696     5207   7992   8051    571  -1360    451  A    N  
ATOM    254  CA  MET C 696      63.222  16.780 166.780  1.00 54.46      A    C  
ANISOU  254  CA  MET C 696     5007   7718   7969    637  -1139    497  A    C  
ATOM    255  C   MET C 696      63.470  18.075 166.012  1.00 50.83      A    C  
ANISOU  255  C   MET C 696     4456   7213   7643    498  -1146    460  A    C  
ATOM    256  O   MET C 696      62.530  18.816 165.700  1.00 49.80      A    O  
ANISOU  256  O   MET C 696     4468   6983   7470    416  -1119    323  A    O  
ATOM    257  CB  MET C 696      61.882  16.170 166.359  0.87 56.65      A    C  
ANISOU  257  CB  MET C 696     5525   7882   8119    702   -977    410  A    C  
ATOM    258  CG  MET C 696      61.711  16.073 164.843  1.00 56.44      A    C  
ANISOU  258  CG  MET C 696     5520   7755   8171    746   -767    430  A    C  
ATOM    259  SD  MET C 696      60.669  14.700 164.399  0.83 92.70      A    S  
ANISOU  259  SD  MET C 696    10344  12247  12633    875   -588    420  A    S  
ATOM    260  CE  MET C 696      61.560  13.404 165.288  0.92 66.41      A    C  
ANISOU  260  CE  MET C 696     6944   9002   9288   1029   -631    569  A    C  
ATOM    261  N   PRO C 697      64.746  18.355 165.717  1.00 53.11      A    N  
ANISOU  261  N   PRO C 697     4498   7580   8101    471  -1183    597  A    N  
ATOM    262  CA  PRO C 697      65.155  19.496 164.894  1.00 52.64      A    C  
ANISOU  262  CA  PRO C 697     4322   7486   8195    340  -1175    607  A    C  
ATOM    263  C   PRO C 697      64.500  19.464 163.510  1.00 52.55      A    C  
ANISOU  263  C   PRO C 697     4417   7356   8195    394   -938    582  A    C  
ATOM    264  O   PRO C 697      64.071  18.408 163.052  1.00 51.62      A    O  
ANISOU  264  O   PRO C 697     4406   7203   8003    548   -770    601  A    O  
ATOM    265  CB  PRO C 697      66.671  19.319 164.775  1.00 51.51      A    C  
ANISOU  265  CB  PRO C 697     3872   7478   8221    363  -1204    814  A    C  
ATOM    266  CG  PRO C 697      67.055  18.465 165.915  1.00 55.29      A    C  
ANISOU  266  CG  PRO C 697     4309   8072   8627    448  -1328    875  A    C  
ATOM    267  CD  PRO C 697      65.898  17.553 166.159  1.00 53.54      A    C  
ANISOU  267  CD  PRO C 697     4353   7772   8216    573  -1232    773  A    C  
ATOM    268  N   LEU C 698      64.440  20.618 162.861  1.00 53.99      A    N  
ANISOU  268  N   LEU C 698     4577   7470   8465    259   -938    544  A    N  
ATOM    269  CA  LEU C 698      63.958  20.731 161.492  1.00 54.75      A    C  
ANISOU  269  CA  LEU C 698     4749   7470   8584    292   -732    542  A    C  
ATOM    270  C   LEU C 698      64.643  19.708 160.581  1.00 55.58      A    C  
ANISOU  270  C   LEU C 698     4754   7622   8740    462   -526    700  A    C  
ATOM    271  O   LEU C 698      63.991  19.040 159.773  1.00 54.39      A    O  
ANISOU  271  O   LEU C 698     4759   7399   8509    574   -344    676  A    O  
ATOM    272  CB  LEU C 698      64.194  22.158 160.989  1.00 55.25      A    C  
ANISOU  272  CB  LEU C 698     4736   7480   8775    116   -784    536  A    C  
ATOM    273  CG  LEU C 698      63.909  22.523 159.538  1.00 54.93      A    C  
ANISOU  273  CG  LEU C 698     4733   7356   8783    119   -595    564  A    C  
ATOM    274  CD1 LEU C 698      62.480  22.191 159.175  1.00 50.16      A    C  
ANISOU  274  CD1 LEU C 698     4391   6647   8021    186   -492    433  A    C  
ATOM    275  CD2 LEU C 698      64.192  24.003 159.325  1.00 56.36      A    C  
ANISOU  275  CD2 LEU C 698     4839   7481   9094    -77   -695    563  A    C  
ATOM    276  N   GLY C 699      65.954  19.558 160.751  1.00 57.97      A    N  
ANISOU  276  N   GLY C 699     4802   8052   9173    487   -560    863  A    N  
ATOM    277  CA  GLY C 699      66.752  18.666 159.923  1.00 59.98      A    C  
ANISOU  277  CA  GLY C 699     4933   8365   9491    669   -357   1029  A    C  
ATOM    278  C   GLY C 699      66.496  17.169 160.036  1.00 62.58      A    C  
ANISOU  278  C   GLY C 699     5393   8681   9703    889   -241   1041  A    C  
ATOM    279  O   GLY C 699      66.969  16.397 159.203  1.00 64.75      A    O  
ANISOU  279  O   GLY C 699     5634   8963  10004   1063    -38   1149  A    O  
ATOM    280  N   LYS C 700      65.759  16.734 161.051  1.00 60.83      A    N  
ANISOU  280  N   LYS C 700     5332   8432   9348    889   -359    934  A    N  
ATOM    281  CA  LYS C 700      65.514  15.302 161.189  1.00 63.38      A    C  
ANISOU  281  CA  LYS C 700     5790   8726   9566   1084   -258    956  A    C  
ATOM    282  C   LYS C 700      64.058  14.938 160.869  1.00 59.14      A    C  
ANISOU  282  C   LYS C 700     5564   8041   8866   1084   -177    803  A    C  
ATOM    283  O   LYS C 700      63.689  13.759 160.886  1.00 58.79      A    O  
ANISOU  283  O   LYS C 700     5675   7939   8725   1220    -89    806  A    O  
ATOM    284  CB  LYS C 700      65.910  14.824 162.589  1.00 67.60      A    C  
ANISOU  284  CB  LYS C 700     6252   9361  10073   1112   -437   1003  A    C  
ATOM    285  CG  LYS C 700      66.907  13.657 162.575  0.73 73.62      A    C  
ANISOU  285  CG  LYS C 700     6887  10193  10890   1334   -344   1185  A    C  
ATOM    286  CD  LYS C 700      68.116  13.931 163.465  0.75 79.39      A    C  
ANISOU  286  CD  LYS C 700     7321  11105  11737   1306   -530   1327  A    C  
ATOM    287  CE  LYS C 700      69.285  12.975 163.183  1.00 84.21      A    C  
ANISOU  287  CE  LYS C 700     7739  11806  12453   1539   -405   1544  A    C  
ATOM    288  NZ  LYS C 700      69.861  13.102 161.813  1.00 86.52      A    N1+
ANISOU  288  NZ  LYS C 700     7915  12094  12865   1623   -176   1637  A    N1+
ATOM    289  N   LEU C 701      63.246  15.948 160.559  1.00 55.87      A    N  
ANISOU  289  N   LEU C 701     5236   7564   8429    930   -209    680  A    N  
ATOM    290  CA  LEU C 701      61.907  15.737 159.990  1.00 52.73      A    C  
ANISOU  290  CA  LEU C 701     5094   7039   7902    920   -116    558  A    C  
ATOM    291  C   LEU C 701      62.000  14.819 158.776  1.00 49.79      A    C  
ANISOU  291  C   LEU C 701     4811   6596   7510   1068    107    617  A    C  
ATOM    292  O   LEU C 701      62.786  15.083 157.868  1.00 52.87      A    O  
ANISOU  292  O   LEU C 701     5082   7009   7998   1107    221    704  A    O  
ATOM    293  CB  LEU C 701      61.288  17.068 159.564  1.00 54.16      A    C  
ANISOU  293  CB  LEU C 701     5301   7173   8104    757   -155    461  A    C  
ATOM    294  CG  LEU C 701      60.090  17.703 160.257  1.00 54.56      A    C  
ANISOU  294  CG  LEU C 701     5487   7185   8060    639   -280    311  A    C  
ATOM    295  CD1 LEU C 701      59.586  18.849 159.377  1.00 52.13      A    C  
ANISOU  295  CD1 LEU C 701     5210   6805   7792    532   -248    253  A    C  
ATOM    296  CD2 LEU C 701      58.995  16.680 160.527  1.00 51.81      A    C  
ANISOU  296  CD2 LEU C 701     5345   6789   7552    701   -239    251  A    C  
ATOM    297  N   SER C 702      61.214  13.752 158.738  1.00 47.60      A    N  
ANISOU  297  N   SER C 702     4753   6231   7102   1146    173    572  A    N  
ATOM    298  CA  SER C 702      61.260  12.875 157.570  1.00 50.50      A    C  
ANISOU  298  CA  SER C 702     5249   6507   7430   1281    378    607  A    C  
ATOM    299  C   SER C 702      59.875  12.475 157.071  1.00 51.11      A    C  
ANISOU  299  C   SER C 702     5605   6455   7360   1233    422    492  A    C  
ATOM    300  O   SER C 702      58.907  12.415 157.848  1.00 50.62      A    O  
ANISOU  300  O   SER C 702     5642   6378   7214   1146    310    413  A    O  
ATOM    301  CB  SER C 702      62.082  11.619 157.872  1.00 50.64      A    C  
ANISOU  301  CB  SER C 702     5250   6534   7458   1480    446    717  A    C  
ATOM    302  OG  SER C 702      61.303  10.627 158.508  1.00 52.31      A    O  
ANISOU  302  OG  SER C 702     5661   6666   7547   1508    407    670  A    O  
ATOM    303  N   LYS C 703      59.792  12.209 155.769  1.00 48.05      A    N  
ANISOU  303  N   LYS C 703     5337   5984   6934   1287    586    491  A    N  
ATOM    304  CA  LYS C 703      58.547  11.788 155.134  1.00 49.77      A    C  
ANISOU  304  CA  LYS C 703     5819   6080   7011   1234    626    396  A    C  
ATOM    305  C   LYS C 703      58.008  10.504 155.745  1.00 46.96      A    C  
ANISOU  305  C   LYS C 703     5646   5643   6553   1284    603    378  A    C  
ATOM    306  O   LYS C 703      56.807  10.363 155.965  1.00 45.95      A    O  
ANISOU  306  O   LYS C 703     5666   5466   6329   1173    533    300  A    O  
ATOM    307  CB  LYS C 703      58.751  11.601 153.627  1.00 51.34      A    C  
ANISOU  307  CB  LYS C 703     6127   6206   7173   1307    809    410  A    C  
ATOM    308  CG  LYS C 703      58.742  12.880 152.819  0.77 54.83      A    C  
ANISOU  308  CG  LYS C 703     6475   6693   7665   1207    827    404  A    C  
ATOM    309  CD  LYS C 703      58.502  12.586 151.335  0.66 58.25      A    C  
ANISOU  309  CD  LYS C 703     7100   7038   7996   1250    988    389  A    C  
ATOM    310  CE  LYS C 703      57.216  11.781 151.089  0.34 57.48      A    C  
ANISOU  310  CE  LYS C 703     7296   6815   7731   1197    963    289  A    C  
ATOM    311  NZ  LYS C 703      55.963  12.402 151.631  0.81 55.96      A    N1+
ANISOU  311  NZ  LYS C 703     7115   6637   7512   1012    796    211  A    N1+
ATOM    312  N   ARG C 704      58.917   9.576 156.021  1.00 49.28      A    N  
ANISOU  312  N   ARG C 704     5920   5928   6876   1454    666    464  A    N  
ATOM    313  CA  ARG C 704      58.584   8.289 156.629  1.00 49.91      A    C  
ANISOU  313  CA  ARG C 704     6172   5918   6875   1522    652    473  A    C  
ATOM    314  C   ARG C 704      57.863   8.448 157.982  1.00 44.86      A    C  
ANISOU  314  C   ARG C 704     5501   5340   6204   1399    472    442  A    C  
ATOM    315  O   ARG C 704      56.839   7.811 158.250  1.00 44.56      A    O  
ANISOU  315  O   ARG C 704     5649   5221   6059   1333    435    398  A    O  
ATOM    316  CB  ARG C 704      59.866   7.471 156.816  1.00 51.56      A    C  
ANISOU  316  CB  ARG C 704     6305   6133   7152   1745    738    595  A    C  
ATOM    317  CG  ARG C 704      59.676   6.000 157.153  0.87 57.50      A    C  
ANISOU  317  CG  ARG C 704     7276   6748   7824   1859    770    619  A    C  
ATOM    318  N   GLN C 705      58.421   9.294 158.831  1.00 42.44      A    N  
ANISOU  318  N   GLN C 705     4961   5180   5985   1366    360    471  A    N  
ATOM    319  CA  GLN C 705      57.857   9.560 160.147  1.00 47.72      A    C  
ANISOU  319  CA  GLN C 705     5594   5926   6614   1264    195    440  A    C  
ATOM    320  C   GLN C 705      56.475  10.232 160.079  1.00 44.58      A    C  
ANISOU  320  C   GLN C 705     5286   5514   6137   1091    140    325  A    C  
ATOM    321  O   GLN C 705      55.584   9.937 160.884  1.00 43.88      A    O  
ANISOU  321  O   GLN C 705     5283   5432   5958   1026     64    296  A    O  
ATOM    322  CB  GLN C 705      58.833  10.434 160.933  1.00 55.62      A    C  
ANISOU  322  CB  GLN C 705     6335   7078   7720   1257     83    485  A    C  
ATOM    323  CG  GLN C 705      58.176  11.532 161.721  1.00 62.76      A    C  
ANISOU  323  CG  GLN C 705     7186   8061   8598   1097    -68    394  A    C  
ATOM    324  N   ILE C 706      56.301  11.141 159.123  1.00 39.81      A    N  
ANISOU  324  N   ILE C 706     4656   4902   5570   1023    182    274  A    N  
ATOM    325  CA  ILE C 706      55.028  11.854 158.995  1.00 39.55      A    C  
ANISOU  325  CA  ILE C 706     4688   4864   5477    876    133    180  A    C  
ATOM    326  C   ILE C 706      53.951  10.905 158.478  1.00 38.59      A    C  
ANISOU  326  C   ILE C 706     4792   4633   5238    846    187    157  A    C  
ATOM    327  O   ILE C 706      52.818  10.905 158.965  1.00 38.83      A    O  
ANISOU  327  O   ILE C 706     4886   4676   5191    748    121    116  A    O  
ATOM    328  CB  ILE C 706      55.174  13.080 158.082  1.00 39.24      A    C  
ANISOU  328  CB  ILE C 706     4561   4837   5513    819    160    149  A    C  
ATOM    329  CG1 ILE C 706      56.071  14.116 158.778  1.00 40.04      A    C  
ANISOU  329  CG1 ILE C 706     4444   5041   5727    801     67    164  A    C  
ATOM    330  CG2 ILE C 706      53.805  13.690 157.775  1.00 38.09      A    C  
ANISOU  330  CG2 ILE C 706     4500   4671   5301    693    128     67  A    C  
ATOM    331  CD1 ILE C 706      56.592  15.228 157.866  1.00 42.88      A    C  
ANISOU  331  CD1 ILE C 706     4693   5406   6194    761    106    174  A    C  
ATOM    332  N   GLN C 707      54.332  10.078 157.514  1.00 39.06      A    N  
ANISOU  332  N   GLN C 707     4973   4587   5283    932    307    188  A    N  
ATOM    333  CA  GLN C 707      53.479   9.012 157.009  1.00 43.31      A    C  
ANISOU  333  CA  GLN C 707     5753   4995   5707    905    349    171  A    C  
ATOM    334  C   GLN C 707      53.020   8.061 158.119  1.00 42.00      A    C  
ANISOU  334  C   GLN C 707     5666   4813   5481    895    282    201  A    C  
ATOM    335  O   GLN C 707      51.852   7.683 158.175  1.00 40.37      A    O  
ANISOU  335  O   GLN C 707     5589   4565   5186    780    243    177  A    O  
ATOM    336  CB  GLN C 707      54.215   8.211 155.923  1.00 44.07      A    C  
ANISOU  336  CB  GLN C 707     5982   4969   5794   1037    496    198  A    C  
ATOM    337  CG  GLN C 707      53.365   7.115 155.282  0.67 46.36      A    C  
ANISOU  337  CG  GLN C 707     6561   5096   5957    996    532    166  A    C  
ATOM    338  CD  GLN C 707      54.156   6.226 154.330  0.24 49.66      A    C  
ANISOU  338  CD  GLN C 707     7145   5375   6348   1156    684    183  A    C  
ATOM    339  NE2 GLN C 707      55.061   5.418 154.872  0.69 49.06      A    N  
ANISOU  339  NE2 GLN C 707     7064   5265   6313   1325    732    254  A    N  
ATOM    340  OE1 GLN C 707      53.950   6.271 153.121  0.56 51.60      A    O  
ANISOU  340  OE1 GLN C 707     7527   5547   6529   1139    759    137  A    O  
ATOM    341  N   ALA C 708      53.946   7.651 158.978  1.00 41.22      A    N  
ANISOU  341  N   ALA C 708     5484   4750   5427   1013    269    270  A    N  
ATOM    342  CA  ALA C 708      53.593   6.760 160.080  1.00 42.18      A    C  
ANISOU  342  CA  ALA C 708     5676   4862   5489   1013    206    317  A    C  
ATOM    343  C   ALA C 708      52.730   7.492 161.113  1.00 39.04      A    C  
ANISOU  343  C   ALA C 708     5185   4596   5053    884     85    284  A    C  
ATOM    344  O   ALA C 708      51.885   6.879 161.769  1.00 40.43      A    O  
ANISOU  344  O   ALA C 708     5455   4762   5145    818     42    306  A    O  
ATOM    345  CB  ALA C 708      54.849   6.188 160.743  1.00 42.12      A    C  
ANISOU  345  CB  ALA C 708     5590   4873   5539   1184    214    414  A    C  
ATOM    346  N   ALA C 709      52.939   8.799 161.259  1.00 37.11      A    N  
ANISOU  346  N   ALA C 709     4764   4470   4867    849     35    236  A    N  
ATOM    347  CA  ALA C 709      52.130   9.559 162.204  1.00 36.46      A    C  
ANISOU  347  CA  ALA C 709     4612   4503   4739    749    -64    190  A    C  
ATOM    348  C   ALA C 709      50.703   9.667 161.698  1.00 36.68      A    C  
ANISOU  348  C   ALA C 709     4739   4502   4698    622    -52    143  A    C  
ATOM    349  O   ALA C 709      49.761   9.543 162.495  1.00 36.84      A    O  
ANISOU  349  O   ALA C 709     4781   4579   4639    554    -99    147  A    O  
ATOM    350  CB  ALA C 709      52.712  10.947 162.462  1.00 35.05      A    C  
ANISOU  350  CB  ALA C 709     4248   4429   4639    742   -126    141  A    C  
ATOM    351  N   TYR C 710      50.543   9.909 160.390  1.00 33.32      A    N  
ANISOU  351  N   TYR C 710     4362   4000   4298    592     12    109  A    N  
ATOM    352  CA  TYR C 710      49.219   9.921 159.779  1.00 35.05      A    C  
ANISOU  352  CA  TYR C 710     4675   4190   4452    469     15     81  A    C  
ATOM    353  C   TYR C 710      48.497   8.591 160.087  1.00 34.38      A    C  
ANISOU  353  C   TYR C 710     4749   4037   4275    419     10    136  A    C  
ATOM    354  O   TYR C 710      47.317   8.577 160.476  1.00 33.45      A    O  
ANISOU  354  O   TYR C 710     4641   3973   4096    309    -33    145  A    O  
ATOM    355  CB  TYR C 710      49.313  10.108 158.267  1.00 33.99      A    C  
ANISOU  355  CB  TYR C 710     4609   3968   4340    458     84     53  A    C  
ATOM    356  CG  TYR C 710      49.321  11.526 157.728  1.00 30.92      A    C  
ANISOU  356  CG  TYR C 710     4096   3638   4014    431     79      4  A    C  
ATOM    357  CD1 TYR C 710      48.351  12.456 158.098  1.00 30.36      A    C  
ANISOU  357  CD1 TYR C 710     3946   3656   3935    348     15    -32  A    C  
ATOM    358  CD2 TYR C 710      50.288  11.918 156.800  1.00 33.44      A    C  
ANISOU  358  CD2 TYR C 710     4386   3919   4402    496    149      3  A    C  
ATOM    359  CE1 TYR C 710      48.339  13.766 157.544  1.00 29.86      A    C  
ANISOU  359  CE1 TYR C 710     3789   3622   3934    330     11    -72  A    C  
ATOM    360  CE2 TYR C 710      50.293  13.217 156.246  1.00 34.34      A    C  
ANISOU  360  CE2 TYR C 710     4398   4073   4577    462    144    -29  A    C  
ATOM    361  CZ  TYR C 710      49.324  14.133 156.626  1.00 33.25      A    C  
ANISOU  361  CZ  TYR C 710     4196   4003   4434    378     71    -68  A    C  
ATOM    362  OH  TYR C 710      49.345  15.406 156.069  1.00 32.18      A    O  
ANISOU  362  OH  TYR C 710     3977   3885   4365    353     67    -92  A    O  
ATOM    363  N   SER C 711      49.217   7.483 159.917  1.00 32.57      A    N  
ANISOU  363  N   SER C 711     4641   3691   4044    503     59    181  A    N  
ATOM    364  CA  SER C 711      48.639   6.149 160.118  1.00 34.71      A    C  
ANISOU  364  CA  SER C 711     5094   3858   4238    455     56    238  A    C  
ATOM    365  C   SER C 711      48.175   5.950 161.552  1.00 37.40      A    C  
ANISOU  365  C   SER C 711     5375   4300   4533    422    -12    295  A    C  
ATOM    366  O   SER C 711      47.142   5.339 161.786  1.00 42.70      A    O  
ANISOU  366  O   SER C 711     6136   4953   5135    304    -39    338  A    O  
ATOM    367  CB  SER C 711      49.642   5.052 159.755  1.00 41.61      A    C  
ANISOU  367  CB  SER C 711     6112   4574   5125    589    128    277  A    C  
ATOM    368  OG  SER C 711      49.819   4.962 158.352  1.00 51.79      A    O  
ANISOU  368  OG  SER C 711     7525   5743   6412    604    205    228  A    O  
ATOM    369  N   ILE C 712      48.942   6.451 162.516  1.00 39.30      A    N  
ANISOU  369  N   ILE C 712     5468   4656   4809    518    -43    304  A    N  
ATOM    370  CA  ILE C 712      48.507   6.388 163.916  1.00 37.40      A    C  
ANISOU  370  CA  ILE C 712     5172   4534   4503    493   -107    351  A    C  
ATOM    371  C   ILE C 712      47.201   7.143 164.103  1.00 36.49      A    C  
ANISOU  371  C   ILE C 712     4995   4532   4339    365   -134    315  A    C  
ATOM    372  O   ILE C 712      46.310   6.665 164.813  1.00 36.66      A    O  
ANISOU  372  O   ILE C 712     5047   4601   4279    290   -152    376  A    O  
ATOM    373  CB  ILE C 712      49.576   6.945 164.877  1.00 36.02      A    C  
ANISOU  373  CB  ILE C 712     4850   4474   4362    609   -155    352  A    C  
ATOM    374  CG1 ILE C 712      50.747   5.963 164.961  1.00 42.20      A    C  
ANISOU  374  CG1 ILE C 712     5685   5168   5183    745   -134    432  A    C  
ATOM    375  CG2 ILE C 712      48.993   7.180 166.273  1.00 34.04      A    C  
ANISOU  375  CG2 ILE C 712     4542   4373   4018    573   -222    372  A    C  
ATOM    376  CD1 ILE C 712      52.006   6.576 165.498  1.00 48.18      A    C  
ANISOU  376  CD1 ILE C 712     6276   6024   6006    857   -182    435  A    C  
ATOM    377  N   LEU C 713      47.085   8.319 163.466  1.00 34.55      A    N  
ANISOU  377  N   LEU C 713     4655   4330   4142    346   -131    228  A    N  
ATOM    378  CA  LEU C 713      45.860   9.116 163.554  1.00 34.80      A    C  
ANISOU  378  CA  LEU C 713     4618   4466   4138    251   -148    197  A    C  
ATOM    379  C   LEU C 713      44.685   8.340 162.965  1.00 34.51      A    C  
ANISOU  379  C   LEU C 713     4686   4372   4052    117   -135    252  A    C  
ATOM    380  O   LEU C 713      43.558   8.449 163.442  1.00 34.29      A    O  
ANISOU  380  O   LEU C 713     4613   4446   3970     34   -149    288  A    O  
ATOM    381  CB  LEU C 713      46.017  10.453 162.833  1.00 33.86      A    C  
ANISOU  381  CB  LEU C 713     4401   4370   4092    264   -145    105  A    C  
ATOM    382  CG  LEU C 713      46.968  11.479 163.450  1.00 37.41      A    C  
ANISOU  382  CG  LEU C 713     4730   4890   4594    355   -180     44  A    C  
ATOM    383  CD1 LEU C 713      46.817  12.807 162.703  1.00 38.61      A    C  
ANISOU  383  CD1 LEU C 713     4806   5051   4814    337   -178    -34  A    C  
ATOM    384  CD2 LEU C 713      46.707  11.651 164.982  1.00 33.89      A    C  
ANISOU  384  CD2 LEU C 713     4234   4576   4066    378   -229     47  A    C  
ATOM    385  N   SER C 714      44.954   7.556 161.926  1.00 33.74      A    N  
ANISOU  385  N   SER C 714     4732   4115   3972     95   -108    261  A    N  
ATOM    386  CA  SER C 714      43.913   6.730 161.337  1.00 35.90      A    C  
ANISOU  386  CA  SER C 714     5134   4312   4194    -53   -118    311  A    C  
ATOM    387  C   SER C 714      43.534   5.592 162.311  1.00 38.58      A    C  
ANISOU  387  C   SER C 714     5549   4640   4470   -102   -136    417  A    C  
ATOM    388  O   SER C 714      42.382   5.161 162.360  1.00 39.55      A    O  
ANISOU  388  O   SER C 714     5699   4785   4545   -252   -164    485  A    O  
ATOM    389  CB  SER C 714      44.361   6.184 159.974  1.00 40.11      A    C  
ANISOU  389  CB  SER C 714     5838   4661   4742    -56    -87    278  A    C  
ATOM    390  OG  SER C 714      44.323   7.208 158.974  1.00 37.73      A    O  
ANISOU  390  OG  SER C 714     5475   4385   4477    -61    -77    205  A    O  
ATOM    391  N   GLU C 715      44.495   5.128 163.104  1.00 36.73      A    N  
ANISOU  391  N   GLU C 715     5335   4383   4239     20   -126    446  A    N  
ATOM    392  CA  GLU C 715      44.174   4.189 164.176  1.00 39.69      A    C  
ANISOU  392  CA  GLU C 715     5762   4770   4550    -12   -143    557  A    C  
ATOM    393  C   GLU C 715      43.352   4.852 165.291  1.00 38.00      A    C  
ANISOU  393  C   GLU C 715     5387   4772   4278    -50   -162    588  A    C  
ATOM    394  O   GLU C 715      42.451   4.239 165.849  1.00 40.55      A    O  
ANISOU  394  O   GLU C 715     5734   5137   4538   -156   -169    691  A    O  
ATOM    395  CB  GLU C 715      45.449   3.585 164.760  1.00 41.52      A    C  
ANISOU  395  CB  GLU C 715     6044   4934   4796    145   -133    591  A    C  
ATOM    396  CG  GLU C 715      46.140   2.594 163.838  1.00 42.72      A    C  
ANISOU  396  CG  GLU C 715     6392   4855   4984    196    -95    595  A    C  
ATOM    397  CD  GLU C 715      47.303   1.899 164.537  1.00 49.96      A    C  
ANISOU  397  CD  GLU C 715     7348   5718   5917    363    -84    660  A    C  
ATOM    398  OE1 GLU C 715      47.053   1.034 165.404  1.00 56.25      A    O  
ANISOU  398  OE1 GLU C 715     8217   6495   6661    340   -107    769  A    O  
ATOM    399  OE2 GLU C 715      48.467   2.240 164.251  1.00 48.68      A    O1-
ANISOU  399  OE2 GLU C 715     7128   5546   5824    517    -54    618  A    O1-
ATOM    400  N   VAL C 716      43.654   6.105 165.618  1.00 38.78      A    N  
ANISOU  400  N   VAL C 716     5331   5007   4396     38   -164    503  A    N  
ATOM    401  CA  VAL C 716      42.851   6.813 166.614  1.00 36.54      A    C  
ANISOU  401  CA  VAL C 716     4917   4922   4046     24   -167    514  A    C  
ATOM    402  C   VAL C 716      41.428   6.989 166.073  1.00 37.84      A    C  
ANISOU  402  C   VAL C 716     5040   5138   4199   -120   -154    545  A    C  
ATOM    403  O   VAL C 716      40.438   6.791 166.787  1.00 36.23      A    O  
ANISOU  403  O   VAL C 716     4785   5055   3924   -189   -141    634  A    O  
ATOM    404  CB  VAL C 716      43.463   8.185 166.976  1.00 35.28      A    C  
ANISOU  404  CB  VAL C 716     4630   4866   3910    142   -180    398  A    C  
ATOM    405  CG1 VAL C 716      42.521   8.966 167.859  1.00 37.13      A    C  
ANISOU  405  CG1 VAL C 716     4757   5287   4065    138   -167    392  A    C  
ATOM    406  CG2 VAL C 716      44.834   8.012 167.668  1.00 33.16      A    C  
ANISOU  406  CG2 VAL C 716     4373   4580   3645    268   -214    390  A    C  
ATOM    407  N   GLN C 717      41.338   7.351 164.798  1.00 35.92      A    N  
ANISOU  407  N   GLN C 717     4810   4814   4024   -163   -158    483  A    N  
ATOM    408  CA  GLN C 717      40.051   7.481 164.124  1.00 35.88      A    C  
ANISOU  408  CA  GLN C 717     4765   4850   4017   -306   -166    521  A    C  
ATOM    409  C   GLN C 717      39.192   6.234 164.290  1.00 39.08      A    C  
ANISOU  409  C   GLN C 717     5252   5227   4371   -465   -183    660  A    C  
ATOM    410  O   GLN C 717      38.010   6.320 164.614  1.00 43.20      A    O  
ANISOU  410  O   GLN C 717     5671   5886   4859   -564   -180    745  A    O  
ATOM    411  CB  GLN C 717      40.259   7.762 162.646  1.00 34.43      A    C  
ANISOU  411  CB  GLN C 717     4638   4547   3898   -336   -180    448  A    C  
ATOM    412  CG  GLN C 717      39.025   7.604 161.779  1.00 39.01      A    C  
ANISOU  412  CG  GLN C 717     5219   5134   4470   -508   -214    503  A    C  
ATOM    413  CD  GLN C 717      39.319   8.008 160.343  1.00 39.09      A    C  
ANISOU  413  CD  GLN C 717     5289   5039   4524   -518   -229    423  A    C  
ATOM    414  NE2 GLN C 717      39.656   7.030 159.507  1.00 38.84      A    N  
ANISOU  414  NE2 GLN C 717     5457   4824   4478   -582   -246    421  A    N  
ATOM    415  OE1 GLN C 717      39.281   9.192 160.001  1.00 39.64      A    O  
ANISOU  415  OE1 GLN C 717     5244   5183   4636   -458   -220    362  A    O  
ATOM    416  N   GLN C 718      39.789   5.076 164.076  1.00 39.51      A    N  
ANISOU  416  N   GLN C 718     5489   5100   4423   -488   -197    690  A    N  
ATOM    417  CA AGLN C 718      39.016   3.849 164.153  0.45 42.30      A    C  
ANISOU  417  CA AGLN C 718     5950   5387   4736   -659   -225    822  A    C  
ATOM    418  CA BGLN C 718      39.081   3.801 164.163  0.55 42.23      A    C  
ANISOU  418  CA BGLN C 718     5950   5368   4726   -654   -224    821  A    C  
ATOM    419  C   GLN C 718      38.736   3.470 165.607  1.00 46.25      A    C  
ANISOU  419  C   GLN C 718     6391   6012   5169   -650   -202    939  A    C  
ATOM    420  O   GLN C 718      37.654   2.976 165.909  1.00 49.51      A    O  
ANISOU  420  O   GLN C 718     6775   6492   5545   -806   -212   1068  A    O  
ATOM    421  CB AGLN C 718      39.725   2.714 163.414  0.45 43.64      A    C  
ANISOU  421  CB AGLN C 718     6368   5292   4919   -679   -244    812  A    C  
ATOM    422  CB BGLN C 718      39.922   2.673 163.554  0.55 42.46      A    C  
ANISOU  422  CB BGLN C 718     6226   5137   4770   -649   -237    810  A    C  
ATOM    423  CG AGLN C 718      39.069   2.344 162.073  0.45 48.25      A    C  
ANISOU  423  CG AGLN C 718     7074   5748   5509   -855   -296    801  A    C  
ATOM    424  CG BGLN C 718      39.299   1.281 163.681  0.55 46.91      A    C  
ANISOU  424  CG BGLN C 718     6951   5577   5294   -822   -274    943  A    C  
ATOM    425  CD AGLN C 718      38.902   3.534 161.128  0.45 47.50      A    C  
ANISOU  425  CD AGLN C 718     6868   5729   5449   -839   -300    698  A    C  
ATOM    426  CD BGLN C 718      40.050   0.225 162.886  0.55 54.28      A    C  
ANISOU  426  CD BGLN C 718     8163   6222   6240   -812   -284    910  A    C  
ATOM    427  NE2AGLN C 718      37.656   3.951 160.909  0.45 44.85      A    N  
ANISOU  427  NE2AGLN C 718     6406   5530   5108   -986   -342    752  A    N  
ATOM    428  NE2BGLN C 718      39.309  -0.706 162.288  0.55 57.89      A    N  
ANISOU  428  NE2BGLN C 718     8792   6529   6675  -1018   -343    969  A    N  
ATOM    429  OE1AGLN C 718      39.883   4.060 160.592  0.45 47.21      A    O  
ANISOU  429  OE1AGLN C 718     6854   5634   5449   -695   -264    586  A    O  
ATOM    430  OE1BGLN C 718      41.279   0.252 162.800  0.55 56.11      A    O  
ANISOU  430  OE1BGLN C 718     8454   6365   6499   -621   -239    836  A    O  
ATOM    431  N   ALA C 719      39.684   3.727 166.503  1.00 49.01      A    N  
ANISOU  431  N   ALA C 719     6716   6406   5499   -475   -176    903  A    N  
ATOM    432  CA  ALA C 719      39.462   3.453 167.919  1.00 53.44      A    C  
ANISOU  432  CA  ALA C 719     7227   7103   5974   -451   -153   1009  A    C  
ATOM    433  C   ALA C 719      38.305   4.301 168.423  1.00 55.88      A    C  
ANISOU  433  C   ALA C 719     7345   7652   6236   -488   -117   1040  A    C  
ATOM    434  O   ALA C 719      37.413   3.809 169.100  1.00 55.43      A    O  
ANISOU  434  O   ALA C 719     7248   7699   6115   -586    -94   1182  A    O  
ATOM    435  CB  ALA C 719      40.729   3.722 168.740  1.00 53.90      A    C  
ANISOU  435  CB  ALA C 719     7285   7182   6012   -254   -151    951  A    C  
ATOM    436  N   VAL C 720      38.306   5.578 168.066  1.00 54.53      A    N  
ANISOU  436  N   VAL C 720     7053   7567   6100   -408   -105    915  A    N  
ATOM    437  CA  VAL C 720      37.247   6.469 168.516  1.00 53.47      A    C  
ANISOU  437  CA  VAL C 720     6739   7652   5925   -405    -57    934  A    C  
ATOM    438  C   VAL C 720      35.853   6.002 168.069  1.00 56.11      A    C  
ANISOU  438  C   VAL C 720     7012   8039   6267   -601    -57   1073  A    C  
ATOM    439  O   VAL C 720      34.913   6.006 168.867  1.00 57.54      A    O  
ANISOU  439  O   VAL C 720     7076   8405   6383   -634     -4   1190  A    O  
ATOM    440  CB  VAL C 720      37.500   7.897 168.025  1.00 51.98      A    C  
ANISOU  440  CB  VAL C 720     6459   7500   5791   -290    -52    776  A    C  
ATOM    441  CG1 VAL C 720      36.206   8.708 168.028  1.00 56.21      A    C  
ANISOU  441  CG1 VAL C 720     6823   8218   6316   -313     -5    810  A    C  
ATOM    442  CG2 VAL C 720      38.585   8.558 168.880  1.00 48.29      A    C  
ANISOU  442  CG2 VAL C 720     5998   7063   5287   -109    -49    664  A    C  
ATOM    443  N   SER C 721      35.719   5.565 166.820  1.00 53.97      A    N  
ANISOU  443  N   SER C 721     6822   7614   6069   -735   -118   1070  A    N  
ATOM    444  CA  SER C 721      34.405   5.167 166.314  1.00 57.95      A    C  
ANISOU  444  CA  SER C 721     7262   8170   6587   -944   -147   1202  A    C  
ATOM    445  C   SER C 721      33.890   3.860 166.942  1.00 62.40      A    C  
ANISOU  445  C   SER C 721     7887   8721   7101  -1104   -155   1387  A    C  
ATOM    446  O   SER C 721      32.688   3.613 166.972  1.00 65.03      A    O  
ANISOU  446  O   SER C 721     8106   9173   7429  -1269   -160   1536  A    O  
ATOM    447  CB  SER C 721      34.436   5.055 164.783  1.00 60.31      A    C  
ANISOU  447  CB  SER C 721     7658   8299   6957  -1054   -227   1139  A    C  
ATOM    448  OG  SER C 721      35.243   3.975 164.360  1.00 64.37      A    O  
ANISOU  448  OG  SER C 721     8414   8567   7477  -1100   -272   1119  A    O  
ATOM    449  N   GLN C 722      34.786   3.038 167.473  1.00 66.16      A    N  
ANISOU  449  N   GLN C 722     8531   9061   7545  -1056   -156   1394  A    N  
ATOM    450  CA  GLN C 722      34.356   1.853 168.218  1.00 68.89      A    C  
ANISOU  450  CA  GLN C 722     8939   9396   7838  -1188   -155   1580  A    C  
ATOM    451  C   GLN C 722      34.096   2.145 169.706  1.00 68.55      A    C  
ANISOU  451  C   GLN C 722     8759   9590   7697  -1086    -64   1668  A    C  
ATOM    452  O   GLN C 722      35.000   2.099 170.545  1.00 67.78      A    O  
ANISOU  452  O   GLN C 722     8727   9484   7541   -929    -38   1632  A    O  
ATOM    453  CB  GLN C 722      35.387   0.736 168.070  0.76 66.84      A    C  
ANISOU  453  CB  GLN C 722     8943   8865   7590  -1182   -199   1568  A    C  
ATOM    454  CG  GLN C 722      35.539   0.248 166.638  1.00 64.71      A    C  
ANISOU  454  CG  GLN C 722     8849   8348   7392  -1298   -278   1499  A    C  
ATOM    455  CD  GLN C 722      36.803  -0.562 166.430  0.40 63.03      A    C  
ANISOU  455  CD  GLN C 722     8888   7869   7193  -1200   -293   1437  A    C  
ATOM    456  NE2 GLN C 722      37.050  -0.962 165.191  0.58 61.55      A    N  
ANISOU  456  NE2 GLN C 722     8881   7457   7049  -1265   -344   1358  A    N  
ATOM    457  OE1 GLN C 722      37.545  -0.831 167.372  0.43 63.31      A    O  
ANISOU  457  OE1 GLN C 722     8957   7904   7194  -1060   -256   1466  A    O  
ATOM    458  N   SER C 724      36.010   2.599 172.498  1.00 67.57      A    N  
ANISOU  458  N   SER C 724     8680   9638   7354   -638     36   1599  A    N  
ATOM    459  CA  SER C 724      37.401   2.283 172.757  1.00 71.68      A    C  
ANISOU  459  CA  SER C 724     9347  10017   7870   -505     -8   1529  A    C  
ATOM    460  C   SER C 724      37.969   2.789 174.090  1.00 73.95      A    C  
ANISOU  460  C   SER C 724     9600  10468   8032   -324     20   1502  A    C  
ATOM    461  O   SER C 724      37.686   3.915 174.509  1.00 75.94      A    O  
ANISOU  461  O   SER C 724     9724  10905   8224   -229     65   1416  A    O  
ATOM    462  CB  SER C 724      38.255   2.835 171.647  1.00 72.35      A    C  
ANISOU  462  CB  SER C 724     9470   9951   8068   -432    -57   1344  A    C  
ATOM    463  OG  SER C 724      39.632   2.686 171.991  1.00 71.67      A    O  
ANISOU  463  OG  SER C 724     9479   9772   7980   -279    -92   1282  A    O  
ATOM    464  N   SER C 725      38.818   1.966 174.709  1.00 70.03      A    N  
ANISOU  464  N   SER C 725     9232   9885   7491   -269    -15   1569  A    N  
ATOM    465  CA  SER C 725      39.240   2.163 176.095  1.00 69.26      A    C  
ANISOU  465  CA  SER C 725     9126   9948   7244   -134     -3   1595  A    C  
ATOM    466  C   SER C 725      40.293   3.250 176.314  1.00 68.17      A    C  
ANISOU  466  C   SER C 725     8954   9856   7093     50    -48   1403  A    C  
ATOM    467  O   SER C 725      41.013   3.659 175.399  1.00 65.45      A    O  
ANISOU  467  O   SER C 725     8615   9380   6873     91    -97   1265  A    O  
ATOM    468  CB  SER C 725      39.782   0.853 176.671  1.00 68.59      A    C  
ANISOU  468  CB  SER C 725     9190   9752   7119   -143    -38   1755  A    C  
ATOM    469  OG  SER C 725      41.030   0.518 176.089  1.00 69.32      A    O  
ANISOU  469  OG  SER C 725     9390   9634   7316    -61   -114   1682  A    O  
ATOM    470  N   ASP C 726      40.383   3.678 177.567  1.00 69.19      A    N  
ANISOU  470  N   ASP C 726     9057  10173   7058    153    -34   1406  A    N  
ATOM    471  CA  ASP C 726      41.318   4.706 178.001  1.00 70.89      A    C  
ANISOU  471  CA  ASP C 726     9252  10453   7229    309    -93   1237  A    C  
ATOM    472  C   ASP C 726      42.774   4.297 177.765  1.00 68.89      A    C  
ANISOU  472  C   ASP C 726     9076  10039   7061    379   -202   1208  A    C  
ATOM    473  O   ASP C 726      43.623   5.144 177.468  1.00 64.37      A    O  
ANISOU  473  O   ASP C 726     8465   9441   6550    462   -266   1051  A    O  
ATOM    474  CB  ASP C 726      41.089   5.026 179.488  1.00 74.99      A    C  
ANISOU  474  CB  ASP C 726     9770  11200   7523    392    -64   1271  A    C  
ATOM    475  CG  ASP C 726      40.128   6.189 179.697  1.00 79.93      A    C  
ANISOU  475  CG  ASP C 726    10297  12003   8071    426     29   1174  A    C  
ATOM    476  OD1 ASP C 726      39.255   6.411 178.831  1.00 79.75      A    O  
ANISOU  476  OD1 ASP C 726    10189  11960   8153    346     94   1169  A    O  
ATOM    477  OD2 ASP C 726      40.230   6.874 180.736  1.00 84.67      A    O1-
ANISOU  477  OD2 ASP C 726    10911  12763   8498    538     35   1106  A    O1-
ATOM    478  N   SER C 727      43.066   3.003 177.885  1.00 69.02      A    N  
ANISOU  478  N   SER C 727     9195   9944   7087    349   -221   1369  A    N  
ATOM    479  CA  SER C 727      44.454   2.552 177.818  1.00 67.51      A    C  
ANISOU  479  CA  SER C 727     9065   9623   6961    446   -314   1371  A    C  
ATOM    480  C   SER C 727      44.940   2.336 176.379  1.00 61.68      A    C  
ANISOU  480  C   SER C 727     8352   8658   6425    428   -322   1306  A    C  
ATOM    481  O   SER C 727      46.124   2.489 176.087  1.00 60.38      A    O  
ANISOU  481  O   SER C 727     8179   8420   6344    532   -384   1241  A    O  
ATOM    482  CB  SER C 727      44.642   1.273 178.648  1.00 74.00      A    C  
ANISOU  482  CB  SER C 727    10000  10419   7699    455   -330   1578  A    C  
ATOM    483  OG  SER C 727      44.124   0.136 177.982  1.00 78.31      A    O  
ANISOU  483  OG  SER C 727    10645  10781   8330    338   -284   1705  A    O  
ATOM    484  N   GLN C 728      44.048   1.979 175.468  1.00 61.80      A    N  
ANISOU  484  N   GLN C 728     8396   8570   6514    296   -260   1329  A    N  
ATOM    485  CA  GLN C 728      44.488   1.929 174.083  1.00 61.29      A    C  
ANISOU  485  CA  GLN C 728     8365   8309   6615    287   -264   1242  A    C  
ATOM    486  C   GLN C 728      44.540   3.339 173.502  1.00 52.25      A    C  
ANISOU  486  C   GLN C 728     7092   7235   5527    314   -265   1056  A    C  
ATOM    487  O   GLN C 728      45.327   3.605 172.606  1.00 53.89      A    O  
ANISOU  487  O   GLN C 728     7295   7329   5853    365   -284    962  A    O  
ATOM    488  CB  GLN C 728      43.613   1.007 173.236  1.00 67.70      A    C  
ANISOU  488  CB  GLN C 728     9281   8959   7481    127   -221   1325  A    C  
ATOM    489  CG  GLN C 728      42.159   1.338 173.153  0.38 70.59      A    C  
ANISOU  489  CG  GLN C 728     9573   9441   7807    -28   -173   1347  A    C  
ATOM    490  NE2 GLN C 728      40.458  -0.367 172.849  1.00 75.80      A    N  
ANISOU  490  NE2 GLN C 728    10370   9973   8458   -342   -140   1603  A    N  
ATOM    491  OE1 GLN C 728      41.716   0.237 171.079  0.78 69.99      A    O  
ANISOU  491  OE1 GLN C 728     9686   9010   7897   -227   -177   1353  A    O  
ATOM    492  N   ILE C 729      43.730   4.248 174.036  1.00 48.88      A    N  
ANISOU  492  N   ILE C 729     6564   6996   5012    292   -238   1008  A    N  
ATOM    493  CA  ILE C 729      43.856   5.668 173.687  1.00 49.46      A    C  
ANISOU  493  CA  ILE C 729     6528   7138   5126    340   -247    833  A    C  
ATOM    494  C   ILE C 729      45.202   6.201 174.178  1.00 47.29      A    C  
ANISOU  494  C   ILE C 729     6229   6889   4852    473   -332    751  A    C  
ATOM    495  O   ILE C 729      45.914   6.897 173.455  1.00 43.70      A    O  
ANISOU  495  O   ILE C 729     5724   6370   4508    512   -364    635  A    O  
ATOM    496  CB  ILE C 729      42.722   6.519 174.285  1.00 52.97      A    C  
ANISOU  496  CB  ILE C 729     6887   7778   5463    319   -192    804  A    C  
ATOM    497  CG1 ILE C 729      41.396   6.216 173.580  1.00 54.24      A    C  
ANISOU  497  CG1 ILE C 729     7022   7927   5659    179   -120    875  A    C  
ATOM    498  CG2 ILE C 729      43.048   8.005 174.177  1.00 51.53      A    C  
ANISOU  498  CG2 ILE C 729     6621   7654   5304    400   -217    620  A    C  
ATOM    499  CD1 ILE C 729      41.369   6.652 172.117  1.00 52.66      A    C  
ANISOU  499  CD1 ILE C 729     6798   7600   5610    131   -124    778  A    C  
ATOM    500  N   LEU C 730      45.545   5.856 175.416  1.00 48.16      A    N  
ANISOU  500  N   LEU C 730     6368   7098   4834    533   -373    826  A    N  
ATOM    501  CA  LEU C 730      46.821   6.244 176.010  1.00 49.32      A    C  
ANISOU  501  CA  LEU C 730     6488   7286   4965    644   -478    776  A    C  
ATOM    502  C   LEU C 730      48.008   5.755 175.183  1.00 50.81      A    C  
ANISOU  502  C   LEU C 730     6682   7309   5314    694   -519    791  A    C  
ATOM    503  O   LEU C 730      48.937   6.512 174.913  1.00 51.76      A    O  
ANISOU  503  O   LEU C 730     6724   7426   5515    750   -582    693  A    O  
ATOM    504  CB  LEU C 730      46.917   5.704 177.441  1.00 50.37      A    C  
ANISOU  504  CB  LEU C 730     6673   7546   4919    689   -519    891  A    C  
ATOM    505  CG  LEU C 730      48.193   5.920 178.253  1.00 51.65      A    C  
ANISOU  505  CG  LEU C 730     6817   7775   5033    793   -651    878  A    C  
ATOM    506  CD1 LEU C 730      48.503   7.403 178.458  1.00 51.76      A    C  
ANISOU  506  CD1 LEU C 730     6757   7886   5024    817   -720    690  A    C  
ATOM    507  CD2 LEU C 730      48.089   5.183 179.599  1.00 48.67      A    C  
ANISOU  507  CD2 LEU C 730     6514   7516   4461    823   -677   1026  A    C  
ATOM    508  N   ASP C 731      47.976   4.491 174.776  1.00 51.02      A    N  
ANISOU  508  N   ASP C 731     6804   7194   5387    677   -477    920  A    N  
ATOM    509  CA  ASP C 731      49.076   3.947 173.994  1.00 53.40      A    C  
ANISOU  509  CA  ASP C 731     7126   7333   5830    753   -491    942  A    C  
ATOM    510  C   ASP C 731      49.193   4.565 172.595  1.00 50.77      A    C  
ANISOU  510  C   ASP C 731     6750   6897   5645    730   -449    818  A    C  
ATOM    511  O   ASP C 731      50.304   4.837 172.138  1.00 50.94      A    O  
ANISOU  511  O   ASP C 731     6708   6876   5772    816   -478    779  A    O  
ATOM    512  CB  ASP C 731      48.954   2.435 173.857  1.00 56.09      A    C  
ANISOU  512  CB  ASP C 731     7616   7517   6179    747   -448   1100  A    C  
ATOM    513  CG  ASP C 731      50.170   1.820 173.175  1.00 63.10      A    C  
ANISOU  513  CG  ASP C 731     8536   8240   7197    868   -451   1133  A    C  
ATOM    514  OD1 ASP C 731      51.318   2.138 173.569  1.00 68.72      A    O  
ANISOU  514  OD1 ASP C 731     9150   9022   7939    990   -522   1133  A    O  
ATOM    515  OD2 ASP C 731      49.985   1.024 172.234  1.00 65.18      A    O1-
ANISOU  515  OD2 ASP C 731     8924   8307   7533    844   -381   1160  A    O1-
ATOM    516  N   LEU C 732      48.067   4.763 171.910  1.00 44.05      A    N  
ANISOU  516  N   LEU C 732     5923   6015   4799    614   -381    772  A    N  
ATOM    517  CA  LEU C 732      48.113   5.411 170.600  1.00 42.85      A    C  
ANISOU  517  CA  LEU C 732     5734   5779   4768    588   -346    659  A    C  
ATOM    518  C   LEU C 732      48.689   6.811 170.759  1.00 40.63      A    C  
ANISOU  518  C   LEU C 732     5313   5609   4518    636   -399    533  A    C  
ATOM    519  O   LEU C 732      49.480   7.272 169.935  1.00 40.42      A    O  
ANISOU  519  O   LEU C 732     5232   5519   4608    677   -401    470  A    O  
ATOM    520  CB  LEU C 732      46.725   5.479 169.949  1.00 41.45      A    C  
ANISOU  520  CB  LEU C 732     5591   5582   4577    448   -285    641  A    C  
ATOM    521  CG  LEU C 732      46.208   4.166 169.365  1.00 45.90      A    C  
ANISOU  521  CG  LEU C 732     6309   5983   5147    365   -242    742  A    C  
ATOM    522  CD1 LEU C 732      44.743   4.268 168.990  1.00 45.25      A    C  
ANISOU  522  CD1 LEU C 732     6228   5932   5033    205   -210    749  A    C  
ATOM    523  CD2 LEU C 732      47.048   3.763 168.173  1.00 46.30      A    C  
ANISOU  523  CD2 LEU C 732     6441   5842   5309    420   -217    710  A    C  
ATOM    524  N   SER C 733      48.284   7.480 171.830  1.00 39.73      A    N  
ANISOU  524  N   SER C 733     5148   5656   4290    630   -441    501  A    N  
ATOM    525  CA  SER C 733      48.737   8.834 172.070  1.00 42.45      A    C  
ANISOU  525  CA  SER C 733     5390   6091   4648    660   -504    372  A    C  
ATOM    526  C   SER C 733      50.241   8.826 172.299  1.00 43.06      A    C  
ANISOU  526  C   SER C 733     5411   6164   4788    748   -594    386  A    C  
ATOM    527  O   SER C 733      50.964   9.657 171.767  1.00 44.01      A    O  
ANISOU  527  O   SER C 733     5443   6263   5015    761   -629    305  A    O  
ATOM    528  CB  SER C 733      48.001   9.444 173.264  1.00 43.85      A    C  
ANISOU  528  CB  SER C 733     5563   6434   4664    652   -525    334  A    C  
ATOM    529  OG  SER C 733      46.629   9.608 172.950  1.00 43.75      A    O  
ANISOU  529  OG  SER C 733     5562   6442   4617    580   -433    323  A    O  
ATOM    530  N   ASN C 734      50.705   7.859 173.080  1.00 42.29      A    N  
ANISOU  530  N   ASN C 734     5354   6086   4628    806   -632    508  A    N  
ATOM    531  CA  ASN C 734      52.120   7.750 173.378  1.00 44.09      A    C  
ANISOU  531  CA  ASN C 734     5511   6330   4912    898   -725    552  A    C  
ATOM    532  C   ASN C 734      52.903   7.367 172.119  1.00 43.63      A    C  
ANISOU  532  C   ASN C 734     5424   6124   5031    949   -668    580  A    C  
ATOM    533  O   ASN C 734      54.009   7.859 171.885  1.00 44.20      A    O  
ANISOU  533  O   ASN C 734     5376   6212   5207    999   -723    563  A    O  
ATOM    534  CB  ASN C 734      52.350   6.736 174.507  1.00 47.21      A    C  
ANISOU  534  CB  ASN C 734     5965   6782   5192    958   -776    696  A    C  
ATOM    535  CG  ASN C 734      53.824   6.596 174.869  1.00 54.06      A    C  
ANISOU  535  CG  ASN C 734     6738   7685   6118   1062   -886    765  A    C  
ATOM    536  ND2 ASN C 734      54.383   5.417 174.633  1.00 57.05      A    N  
ANISOU  536  ND2 ASN C 734     7153   7964   6557   1154   -853    907  A    N  
ATOM    537  OD1 ASN C 734      54.446   7.536 175.360  1.00 53.79      A    O  
ANISOU  537  OD1 ASN C 734     6602   7764   6074   1058  -1005    695  A    O  
ATOM    538  N   ARG C 735      52.317   6.501 171.299  1.00 41.67      A    N  
ANISOU  538  N   ARG C 735     5288   5735   4811    930   -557    624  A    N  
ATOM    539  CA  ARG C 735      52.926   6.151 170.017  1.00 42.84      A    C  
ANISOU  539  CA  ARG C 735     5443   5733   5100    982   -480    633  A    C  
ATOM    540  C   ARG C 735      53.063   7.387 169.124  1.00 39.81      A    C  
ANISOU  540  C   ARG C 735     4956   5356   4813    939   -466    506  A    C  
ATOM    541  O   ARG C 735      54.112   7.617 168.509  1.00 40.63      A    O  
ANISOU  541  O   ARG C 735     4969   5431   5038   1008   -458    508  A    O  
ATOM    542  CB  ARG C 735      52.106   5.065 169.316  1.00 45.10      A    C  
ANISOU  542  CB  ARG C 735     5907   5857   5372    942   -377    680  A    C  
ATOM    543  CG  ARG C 735      52.369   3.658 169.878  1.00 52.79      A    C  
ANISOU  543  CG  ARG C 735     6997   6756   6304   1020   -374    830  A    C  
ATOM    544  CD  ARG C 735      51.441   2.627 169.263  1.00 55.70      A    C  
ANISOU  544  CD  ARG C 735     7565   6952   6646    945   -291    870  A    C  
ATOM    545  NE  ARG C 735      51.643   2.490 167.820  1.00 55.68      A    N  
ANISOU  545  NE  ARG C 735     7631   6786   6740    961   -205    814  A    N  
ATOM    546  CZ  ARG C 735      50.720   2.041 166.972  1.00 58.30      A    C  
ANISOU  546  CZ  ARG C 735     8116   6981   7054    851   -147    789  A    C  
ATOM    547  NH1 ARG C 735      49.519   1.694 167.409  1.00 61.08      A    N1+
ANISOU  547  NH1 ARG C 735     8545   7347   7316    707   -165    827  A    N1+
ATOM    548  NH2 ARG C 735      50.992   1.946 165.679  1.00 58.57      A    N  
ANISOU  548  NH2 ARG C 735     8225   6874   7156    878    -73    731  A    N  
ATOM    549  N   PHE C 736      52.009   8.193 169.066  1.00 38.22      A    N  
ANISOU  549  N   PHE C 736     4761   5199   4563    831   -460    408  A    N  
ATOM    550  CA  PHE C 736      52.056   9.400 168.246  1.00 39.18      A    C  
ANISOU  550  CA  PHE C 736     4797   5317   4771    787   -450    295  A    C  
ATOM    551  C   PHE C 736      53.164  10.334 168.736  1.00 39.70      A    C  
ANISOU  551  C   PHE C 736     4715   5476   4894    823   -554    259  A    C  
ATOM    552  O   PHE C 736      54.010  10.747 167.952  1.00 38.22      A    O  
ANISOU  552  O   PHE C 736     4438   5249   4834    847   -541    250  A    O  
ATOM    553  CB  PHE C 736      50.699  10.118 168.233  1.00 37.45      A    C  
ANISOU  553  CB  PHE C 736     4607   5140   4485    684   -431    209  A    C  
ATOM    554  CG  PHE C 736      50.648  11.297 167.283  1.00 38.65      A    C  
ANISOU  554  CG  PHE C 736     4692   5264   4728    643   -412    106  A    C  
ATOM    555  CD1 PHE C 736      50.312  11.110 165.948  1.00 35.66      A    C  
ANISOU  555  CD1 PHE C 736     4362   4774   4411    609   -324    103  A    C  
ATOM    556  CD2 PHE C 736      50.942  12.580 167.726  1.00 36.99      A    C  
ANISOU  556  CD2 PHE C 736     4388   5131   4536    633   -489     16  A    C  
ATOM    557  CE1 PHE C 736      50.268  12.179 165.067  1.00 36.39      A    C  
ANISOU  557  CE1 PHE C 736     4398   4844   4583    574   -307     26  A    C  
ATOM    558  CE2 PHE C 736      50.902  13.670 166.841  1.00 36.98      A    C  
ANISOU  558  CE2 PHE C 736     4335   5089   4627    593   -472    -66  A    C  
ATOM    559  CZ  PHE C 736      50.563  13.464 165.510  1.00 36.28      A    C  
ANISOU  559  CZ  PHE C 736     4283   4901   4601    567   -378    -54  A    C  
ATOM    560  N   TYR C 737      53.178  10.630 170.036  1.00 41.64      A    N  
ANISOU  560  N   TYR C 737     4939   5845   5039    820   -660    249  A    N  
ATOM    561  CA  TYR C 737      54.106  11.626 170.587  1.00 42.14      A    C  
ANISOU  561  CA  TYR C 737     4878   5998   5136    819   -789    198  A    C  
ATOM    562  C   TYR C 737      55.551  11.130 170.556  1.00 46.15      A    C  
ANISOU  562  C   TYR C 737     5278   6512   5745    904   -837    307  A    C  
ATOM    563  O   TYR C 737      56.494  11.926 170.559  1.00 47.19      A    O  
ANISOU  563  O   TYR C 737     5274   6691   5967    890   -927    286  A    O  
ATOM    564  CB  TYR C 737      53.726  11.995 172.031  1.00 44.24      A    C  
ANISOU  564  CB  TYR C 737     5180   6394   5235    797   -896    155  A    C  
ATOM    565  CG  TYR C 737      52.457  12.805 172.161  1.00 45.75      A    C  
ANISOU  565  CG  TYR C 737     5441   6606   5337    732   -857     35  A    C  
ATOM    566  CD1 TYR C 737      52.113  13.755 171.209  1.00 42.57      A    C  
ANISOU  566  CD1 TYR C 737     5011   6135   5029    682   -809    -64  A    C  
ATOM    567  CD2 TYR C 737      51.596  12.622 173.244  1.00 50.86      A    C  
ANISOU  567  CD2 TYR C 737     6176   7349   5800    734   -862     32  A    C  
ATOM    568  CE1 TYR C 737      50.932  14.499 171.318  1.00 42.63      A    C  
ANISOU  568  CE1 TYR C 737     5074   6163   4961    645   -767   -161  A    C  
ATOM    569  CE2 TYR C 737      50.409  13.368 173.365  1.00 47.91      A    C  
ANISOU  569  CE2 TYR C 737     5851   7006   5345    699   -808    -67  A    C  
ATOM    570  CZ  TYR C 737      50.090  14.306 172.400  1.00 46.70      A    C  
ANISOU  570  CZ  TYR C 737     5666   6779   5300    660   -763   -163  A    C  
ATOM    571  OH  TYR C 737      48.934  15.059 172.514  1.00 48.11      A    O  
ANISOU  571  OH  TYR C 737     5883   6989   5406    646   -707   -251  A    O  
ATOM    572  N   THR C 738      55.728   9.812 170.545  1.00 44.17      A    N  
ANISOU  572  N   THR C 738     5085   6214   5483    992   -781    433  A    N  
ATOM    573  CA  THR C 738      57.071   9.242 170.435  1.00 51.76      A    C  
ANISOU  573  CA  THR C 738     5941   7176   6550   1106   -801    555  A    C  
ATOM    574  C   THR C 738      57.638   9.537 169.044  1.00 51.41      A    C  
ANISOU  574  C   THR C 738     5816   7046   6672   1128   -702    545  A    C  
ATOM    575  O   THR C 738      58.789   9.931 168.882  1.00 47.70      A    O  
ANISOU  575  O   THR C 738     5176   6628   6321   1166   -748    590  A    O  
ATOM    576  CB  THR C 738      57.046   7.726 170.697  1.00 54.81      A    C  
ANISOU  576  CB  THR C 738     6439   7502   6886   1212   -747    693  A    C  
ATOM    577  CG2 THR C 738      58.396   7.095 170.364  1.00 56.64      A    C  
ANISOU  577  CG2 THR C 738     6565   7712   7244   1362   -730    825  A    C  
ATOM    578  OG1 THR C 738      56.747   7.499 172.083  1.00 58.03      A    O  
ANISOU  578  OG1 THR C 738     6891   8017   7140   1199   -854    729  A    O  
ATOM    579  N   LEU C 739      56.780   9.380 168.045  1.00 51.10      A    N  
ANISOU  579  N   LEU C 739     5896   6885   6633   1095   -569    491  A    N  
ATOM    580  CA  LEU C 739      57.134   9.605 166.656  1.00 48.75      A    C  
ANISOU  580  CA  LEU C 739     5564   6499   6459   1114   -456    477  A    C  
ATOM    581  C   LEU C 739      57.323  11.090 166.369  1.00 44.68      A    C  
ANISOU  581  C   LEU C 739     4917   6040   6020   1016   -510    384  A    C  
ATOM    582  O   LEU C 739      58.283  11.487 165.701  1.00 41.90      A    O  
ANISOU  582  O   LEU C 739     4429   5692   5798   1047   -484    419  A    O  
ATOM    583  CB  LEU C 739      56.043   9.021 165.764  1.00 47.67      A    C  
ANISOU  583  CB  LEU C 739     5618   6223   6271   1084   -326    440  A    C  
ATOM    584  CG  LEU C 739      56.362   8.706 164.320  1.00 50.27      A    C  
ANISOU  584  CG  LEU C 739     5990   6429   6682   1142   -182    452  A    C  
ATOM    585  CD1 LEU C 739      57.517   7.707 164.228  1.00 49.96      A    C  
ANISOU  585  CD1 LEU C 739     5927   6352   6704   1319   -124    578  A    C  
ATOM    586  CD2 LEU C 739      55.101   8.139 163.719  1.00 51.51      A    C  
ANISOU  586  CD2 LEU C 739     6357   6465   6750   1074   -105    407  A    C  
ATOM    587  N   ILE C 740      56.393  11.900 166.872  1.00 42.16      A    N  
ANISOU  587  N   ILE C 740     4642   5759   5617    904   -576    274  A    N  
ATOM    588  CA  ILE C 740      56.462  13.350 166.748  1.00 41.98      A    C  
ANISOU  588  CA  ILE C 740     4528   5770   5653    808   -642    176  A    C  
ATOM    589  C   ILE C 740      56.510  13.985 168.124  1.00 42.63      A    C  
ANISOU  589  C   ILE C 740     4579   5964   5655    759   -808    123  A    C  
ATOM    590  O   ILE C 740      55.478  14.348 168.670  1.00 43.04      A    O  
ANISOU  590  O   ILE C 740     4730   6034   5589    708   -829     34  A    O  
ATOM    591  CB  ILE C 740      55.251  13.958 166.010  1.00 45.03      A    C  
ANISOU  591  CB  ILE C 740     5009   6086   6013    728   -567     72  A    C  
ATOM    592  CG1 ILE C 740      54.841  13.122 164.798  1.00 45.12      A    C  
ANISOU  592  CG1 ILE C 740     5120   5986   6039    762   -413    112  A    C  
ATOM    593  CG2 ILE C 740      55.560  15.409 165.625  1.00 46.01      A    C  
ANISOU  593  CG2 ILE C 740     5036   6211   6237    650   -615     -4  A    C  
ATOM    594  CD1 ILE C 740      55.744  13.306 163.615  1.00 48.78      A    C  
ANISOU  594  CD1 ILE C 740     5501   6397   6636    798   -334    151  A    C  
ATOM    595  N   PRO C 741      57.712  14.133 168.686  1.00 43.19      A    N  
ANISOU  595  N   PRO C 741     4512   6117   5783    776   -928    182  A    N  
ATOM    596  CA  PRO C 741      57.846  14.686 170.035  1.00 45.53      A    C  
ANISOU  596  CA  PRO C 741     4795   6520   5983    725  -1107    132  A    C  
ATOM    597  C   PRO C 741      57.268  16.096 170.154  1.00 43.35      A    C  
ANISOU  597  C   PRO C 741     4560   6228   5683    611  -1168    -29  A    C  
ATOM    598  O   PRO C 741      57.597  16.979 169.361  1.00 45.48      A    O  
ANISOU  598  O   PRO C 741     4754   6442   6084    549  -1161    -66  A    O  
ATOM    599  CB  PRO C 741      59.363  14.698 170.255  1.00 49.34      A    C  
ANISOU  599  CB  PRO C 741     5088   7082   6579    745  -1223    238  A    C  
ATOM    600  CG  PRO C 741      59.895  13.688 169.279  1.00 48.20      A    C  
ANISOU  600  CG  PRO C 741     4884   6883   6546    863  -1074    374  A    C  
ATOM    601  CD  PRO C 741      59.016  13.823 168.086  1.00 44.39      A    C  
ANISOU  601  CD  PRO C 741     4504   6274   6088    843   -905    304  A    C  
ATOM    602  N   HIS C 742      56.410  16.294 171.141  1.00 41.72      A    N  
ANISOU  602  N   HIS C 742     4478   6067   5306    594  -1217   -117  A    N  
ATOM    603  CA  HIS C 742      55.890  17.613 171.448  1.00 44.19      A    C  
ANISOU  603  CA  HIS C 742     4851   6364   5574    512  -1282   -274  A    C  
ATOM    604  C   HIS C 742      56.491  18.164 172.738  1.00 50.51      A    C  
ANISOU  604  C   HIS C 742     5652   7256   6283    468  -1486   -328  A    C  
ATOM    605  O   HIS C 742      56.973  17.411 173.575  1.00 50.57      A    O  
ANISOU  605  O   HIS C 742     5643   7363   6209    511  -1566   -245  A    O  
ATOM    606  CB  HIS C 742      54.373  17.577 171.588  1.00 44.99      A    C  
ANISOU  606  CB  HIS C 742     5104   6452   5538    535  -1173   -349  A    C  
ATOM    607  CG  HIS C 742      53.646  17.322 170.306  1.00 45.67      A    C  
ANISOU  607  CG  HIS C 742     5204   6444   5705    544  -1003   -326  A    C  
ATOM    608  CD2 HIS C 742      52.527  17.889 169.795  1.00 46.46      A    C  
ANISOU  608  CD2 HIS C 742     5369   6491   5792    525   -913   -403  A    C  
ATOM    609  ND1 HIS C 742      54.063  16.389 169.380  1.00 45.61      A    N  
ANISOU  609  ND1 HIS C 742     5144   6387   5797    580   -912   -209  A    N  
ATOM    610  CE1 HIS C 742      53.223  16.380 168.360  1.00 48.76      A    C  
ANISOU  610  CE1 HIS C 742     5590   6707   6230    569   -784   -223  A    C  
ATOM    611  NE2 HIS C 742      52.282  17.281 168.586  1.00 48.45      A    N  
ANISOU  611  NE2 HIS C 742     5609   6671   6130    533   -786   -332  A    N  
ATOM    612  N   ASP C 743      56.441  19.477 172.908  1.00 55.31      A    N  
ANISOU  612  N   ASP C 743     6296   7824   6895    383  -1577   -467  A    N  
ATOM    613  CA  ASP C 743      56.795  20.056 174.190  1.00 55.41      A    C  
ANISOU  613  CA  ASP C 743     6367   7908   6778    333  -1773   -551  A    C  
ATOM    614  C   ASP C 743      55.566  20.667 174.841  1.00 50.94      A    C  
ANISOU  614  C   ASP C 743     5999   7329   6026    354  -1741   -711  A    C  
ATOM    615  O   ASP C 743      55.074  21.704 174.397  1.00 50.00      A    O  
ANISOU  615  O   ASP C 743     5939   7105   5954    318  -1707   -831  A    O  
ATOM    616  CB  ASP C 743      57.888  21.104 174.037  1.00 62.87      A    C  
ANISOU  616  CB  ASP C 743     7209   8813   7865    206  -1942   -585  A    C  
ATOM    617  CG  ASP C 743      58.263  21.734 175.362  1.00 67.78      A    C  
ANISOU  617  CG  ASP C 743     7915   9497   8341    134  -2170   -685  A    C  
ATOM    618  OD1 ASP C 743      58.318  20.997 176.371  1.00 69.68      A    O  
ANISOU  618  OD1 ASP C 743     8197   9862   8415    189  -2236   -643  A    O  
ATOM    619  OD2 ASP C 743      58.487  22.962 175.394  1.00 69.03      A    O1-
ANISOU  619  OD2 ASP C 743     8115   9572   8543     21  -2288   -807  A    O1-
ATOM    620  N   PHE C 744      55.072  20.029 175.899  1.00 47.46      A    N  
ANISOU  620  N   PHE C 744     5661   6997   5375    423  -1743   -705  A    N  
ATOM    621  CA  PHE C 744      53.868  20.512 176.560  1.00 50.57      A    C  
ANISOU  621  CA  PHE C 744     6236   7403   5576    469  -1683   -839  A    C  
ATOM    622  C   PHE C 744      54.173  21.264 177.844  1.00 54.50      A    C  
ANISOU  622  C   PHE C 744     6859   7952   5895    436  -1869   -969  A    C  
ATOM    623  O   PHE C 744      53.271  21.552 178.631  1.00 56.05      A    O  
ANISOU  623  O   PHE C 744     7222   8189   5887    498  -1826  -1074  A    O  
ATOM    624  CB  PHE C 744      52.916  19.342 176.825  1.00 53.87      A    C  
ANISOU  624  CB  PHE C 744     6699   7907   5863    567  -1529   -742  A    C  
ATOM    625  CG  PHE C 744      52.325  18.768 175.564  1.00 50.70      A    C  
ANISOU  625  CG  PHE C 744     6226   7433   5604    589  -1343   -654  A    C  
ATOM    626  CD1 PHE C 744      51.537  19.555 174.738  1.00 48.83      A    C  
ANISOU  626  CD1 PHE C 744     6008   7100   5445    580  -1238   -738  A    C  
ATOM    627  CD2 PHE C 744      52.588  17.460 175.186  1.00 52.90      A    C  
ANISOU  627  CD2 PHE C 744     6431   7729   5938    617  -1283   -488  A    C  
ATOM    628  CE1 PHE C 744      51.006  19.043 173.558  1.00 50.70      A    C  
ANISOU  628  CE1 PHE C 744     6187   7274   5801    587  -1087   -658  A    C  
ATOM    629  CE2 PHE C 744      52.057  16.939 174.009  1.00 52.05      A    C  
ANISOU  629  CE2 PHE C 744     6287   7542   5948    625  -1126   -420  A    C  
ATOM    630  CZ  PHE C 744      51.268  17.732 173.194  1.00 49.98      A    C  
ANISOU  630  CZ  PHE C 744     6039   7199   5752    603  -1034   -505  A    C  
ATOM    631  N   GLY C 745      55.446  21.597 178.045  1.00 51.38      A    N  
ANISOU  631  N   GLY C 745     6386   7561   5575    337  -2075   -961  A    N  
ATOM    632  CA  GLY C 745      55.833  22.362 179.210  1.00 52.88      A    C  
ANISOU  632  CA  GLY C 745     6705   7786   5599    278  -2285  -1093  A    C  
ATOM    633  C   GLY C 745      55.459  21.611 180.468  1.00 54.67      A    C  
ANISOU  633  C   GLY C 745     7050   8171   5551    364  -2299  -1069  A    C  
ATOM    634  O   GLY C 745      55.768  20.435 180.615  1.00 57.70      A    O  
ANISOU  634  O   GLY C 745     7339   8661   5925    410  -2286   -898  A    O  
ATOM    635  N   MET C 746      54.756  22.275 181.369  1.00 55.08      A    N  
ANISOU  635  N   MET C 746     7320   8235   5372    400  -2312  -1236  A    N  
ATOM    636  CA  MET C 746      54.399  21.635 182.620  1.00 56.08      A    C  
ANISOU  636  CA  MET C 746     7573   8522   5211    481  -2324  -1216  A    C  
ATOM    637  C   MET C 746      53.016  20.964 182.580  1.00 57.29      A    C  
ANISOU  637  C   MET C 746     7779   8729   5261    620  -2058  -1165  A    C  
ATOM    638  O   MET C 746      52.483  20.579 183.621  1.00 58.37      A    O  
ANISOU  638  O   MET C 746     8045   8995   5138    699  -2026  -1163  A    O  
ATOM    639  CB  MET C 746      54.471  22.660 183.742  1.00 57.65      A    C  
ANISOU  639  CB  MET C 746     7999   8728   5179    449  -2493  -1419  A    C  
ATOM    640  CG  MET C 746      55.876  23.177 183.973  1.00 58.60      A    C  
ANISOU  640  CG  MET C 746     8069   8828   5370    288  -2795  -1445  A    C  
ATOM    641  SD  MET C 746      56.973  21.904 184.636  1.00 61.90      A    S  
ANISOU  641  SD  MET C 746     8335   9446   5738    268  -2968  -1219  A    S  
ATOM    642  CE  MET C 746      56.246  21.612 186.243  1.00 64.14      A    C  
ANISOU  642  CE  MET C 746     8887   9893   5589    375  -2975  -1285  A    C  
ATOM    643  N   LYS C 747      52.448  20.802 181.386  1.00 55.82      A    N  
ANISOU  643  N   LYS C 747     7486   8451   5272    641  -1872  -1111  A    N  
ATOM    644  CA  LYS C 747      51.152  20.129 181.264  1.00 60.87      A    C  
ANISOU  644  CA  LYS C 747     8145   9143   5838    745  -1634  -1041  A    C  
ATOM    645  C   LYS C 747      51.329  18.637 181.011  1.00 61.05      A    C  
ANISOU  645  C   LYS C 747     8043   9232   5920    758  -1576   -817  A    C  
ATOM    646  O   LYS C 747      52.303  18.216 180.387  1.00 57.99      A    O  
ANISOU  646  O   LYS C 747     7516   8798   5718    704  -1651   -719  A    O  
ATOM    647  CB  LYS C 747      50.307  20.730 180.133  1.00 62.65      A    C  
ANISOU  647  CB  LYS C 747     8339   9243   6224    760  -1468  -1098  A    C  
ATOM    648  CG  LYS C 747      50.344  22.244 180.032  1.00 68.05      A    C  
ANISOU  648  CG  LYS C 747     9118   9801   6939    734  -1535  -1301  A    C  
ATOM    649  CD  LYS C 747      49.937  22.909 181.341  1.00 73.99      A    C  
ANISOU  649  CD  LYS C 747    10091  10614   7409    803  -1577  -1461  A    C  
ATOM    650  CE  LYS C 747      49.731  24.408 181.152  1.00 75.54      A    C  
ANISOU  650  CE  LYS C 747    10413  10651   7636    802  -1601  -1668  A    C  
ATOM    651  NZ  LYS C 747      48.619  24.709 180.204  1.00 71.28      A    N1+
ANISOU  651  NZ  LYS C 747     9830  10038   7216    880  -1385  -1666  A    N1+
ATOM    652  N   LYS C 748      50.386  17.838 181.495  1.00 63.81      A    N  
ANISOU  652  N   LYS C 748     8447   9686   6112    835  -1435   -730  A    N  
ATOM    653  CA  LYS C 748      50.300  16.442 181.077  1.00 64.38      A    C  
ANISOU  653  CA  LYS C 748     8423   9778   6259    844  -1342   -523  A    C  
ATOM    654  C   LYS C 748      50.037  16.407 179.567  1.00 56.01      A    C  
ANISOU  654  C   LYS C 748     7249   8577   5454    811  -1222   -495  A    C  
ATOM    655  O   LYS C 748      49.249  17.201 179.059  1.00 54.58      A    O  
ANISOU  655  O   LYS C 748     7086   8339   5312    816  -1126   -599  A    O  
ATOM    656  CB  LYS C 748      49.194  15.714 181.849  1.00 69.56      A    C  
ANISOU  656  CB  LYS C 748     9164  10563   6701    913  -1203   -437  A    C  
ATOM    657  CG  LYS C 748      49.072  14.230 181.549  1.00 71.92      A    C  
ANISOU  657  CG  LYS C 748     9398  10870   7057    911  -1120   -218  A    C  
ATOM    658  CD  LYS C 748      47.950  13.590 182.357  1.00 73.82      A    C  
ANISOU  658  CD  LYS C 748     9719  11244   7085    960   -985   -124  A    C  
ATOM    659  CE  LYS C 748      46.579  14.097 181.919  1.00 76.97      A    C  
ANISOU  659  CE  LYS C 748    10117  11643   7486    975   -800   -183  A    C  
ATOM    660  NZ  LYS C 748      46.229  13.703 180.513  1.00 79.50      A    N1+
ANISOU  660  NZ  LYS C 748    10327  11833   8046    916   -703   -116  A    N1+
ATOM    661  N   PRO C 749      50.732  15.521 178.836  1.00 53.80      A    N  
ANISOU  661  N   PRO C 749     6860   8239   5342    785  -1231   -358  A    N  
ATOM    662  CA  PRO C 749      50.494  15.400 177.389  1.00 53.35      A    C  
ANISOU  662  CA  PRO C 749     6716   8051   5502    756  -1116   -328  A    C  
ATOM    663  C   PRO C 749      49.040  14.996 177.091  1.00 53.62      A    C  
ANISOU  663  C   PRO C 749     6790   8095   5490    772   -930   -287  A    C  
ATOM    664  O   PRO C 749      48.572  13.980 177.607  1.00 52.94      A    O  
ANISOU  664  O   PRO C 749     6741   8082   5292    794   -872   -165  A    O  
ATOM    665  CB  PRO C 749      51.477  14.304 176.951  1.00 54.36      A    C  
ANISOU  665  CB  PRO C 749     6759   8141   5757    758  -1150   -172  A    C  
ATOM    666  CG  PRO C 749      52.541  14.281 178.022  1.00 58.18      A    C  
ANISOU  666  CG  PRO C 749     7237   8719   6149    771  -1333   -152  A    C  
ATOM    667  CD  PRO C 749      51.863  14.696 179.301  1.00 57.49      A    C  
ANISOU  667  CD  PRO C 749     7281   8754   5807    792  -1360   -233  A    C  
ATOM    668  N   PRO C 750      48.330  15.797 176.281  1.00 53.46      A    N  
ANISOU  668  N   PRO C 750     6752   8006   5554    756   -845   -377  A    N  
ATOM    669  CA  PRO C 750      46.902  15.564 176.017  1.00 51.41      A    C  
ANISOU  669  CA  PRO C 750     6506   7776   5251    765   -683   -338  A    C  
ATOM    670  C   PRO C 750      46.667  14.267 175.256  1.00 49.60      A    C  
ANISOU  670  C   PRO C 750     6239   7497   5109    722   -603   -176  A    C  
ATOM    671  O   PRO C 750      47.355  14.018 174.274  1.00 47.69      A    O  
ANISOU  671  O   PRO C 750     5948   7139   5033    688   -624   -150  A    O  
ATOM    672  CB  PRO C 750      46.497  16.774 175.159  1.00 52.09      A    C  
ANISOU  672  CB  PRO C 750     6564   7777   5451    757   -644   -463  A    C  
ATOM    673  CG  PRO C 750      47.588  17.784 175.366  1.00 54.35      A    C  
ANISOU  673  CG  PRO C 750     6863   8010   5778    749   -790   -593  A    C  
ATOM    674  CD  PRO C 750      48.833  16.985 175.573  1.00 50.16      A    C  
ANISOU  674  CD  PRO C 750     6295   7484   5281    723   -903   -505  A    C  
ATOM    675  N   LEU C 751      45.708  13.458 175.694  1.00 48.45      A    N  
ANISOU  675  N   LEU C 751     6125   7434   4849    720   -511    -68  A    N  
ATOM    676  CA  LEU C 751      45.384  12.224 174.982  1.00 46.75      A    C  
ANISOU  676  CA  LEU C 751     5901   7153   4709    660   -444     81  A    C  
ATOM    677  C   LEU C 751      44.706  12.551 173.655  1.00 42.53      A    C  
ANISOU  677  C   LEU C 751     5316   6529   4315    604   -368     55  A    C  
ATOM    678  O   LEU C 751      44.038  13.564 173.532  1.00 45.45      A    O  
ANISOU  678  O   LEU C 751     5655   6935   4680    620   -328    -37  A    O  
ATOM    679  CB  LEU C 751      44.493  11.320 175.842  1.00 50.29      A    C  
ANISOU  679  CB  LEU C 751     6392   7715   4999    652   -372    217  A    C  
ATOM    680  CG  LEU C 751      45.121  10.865 177.167  1.00 51.88      A    C  
ANISOU  680  CG  LEU C 751     6657   8014   5043    707   -446    270  A    C  
ATOM    681  CD1 LEU C 751      44.077  10.321 178.140  1.00 54.05      A    C  
ANISOU  681  CD1 LEU C 751     6971   8437   5129    708   -357    384  A    C  
ATOM    682  CD2 LEU C 751      46.178   9.827 176.899  1.00 52.77      A    C  
ANISOU  682  CD2 LEU C 751     6785   8019   5244    701   -516    373  A    C  
ATOM    683  N   LEU C 752      44.895  11.698 172.660  1.00 41.73      A    N  
ANISOU  683  N   LEU C 752     5218   6306   4332    545   -350    135  A    N  
ATOM    684  CA  LEU C 752      44.220  11.858 171.376  1.00 41.65      A    C  
ANISOU  684  CA  LEU C 752     5177   6214   4434    478   -288    126  A    C  
ATOM    685  C   LEU C 752      42.899  11.096 171.475  1.00 45.75      A    C  
ANISOU  685  C   LEU C 752     5707   6795   4882    406   -207    246  A    C  
ATOM    686  O   LEU C 752      42.822   9.915 171.139  1.00 47.48      A    O  
ANISOU  686  O   LEU C 752     5981   6939   5120    337   -195    361  A    O  
ATOM    687  CB  LEU C 752      45.104  11.342 170.228  1.00 37.41      A    C  
ANISOU  687  CB  LEU C 752     4660   5512   4041    454   -308    143  A    C  
ATOM    688  CG  LEU C 752      46.509  11.968 170.183  1.00 38.52      A    C  
ANISOU  688  CG  LEU C 752     4765   5610   4261    520   -387     61  A    C  
ATOM    689  CD1 LEU C 752      47.313  11.453 168.986  1.00 37.23      A    C  
ANISOU  689  CD1 LEU C 752     4612   5299   4236    513   -375     90  A    C  
ATOM    690  CD2 LEU C 752      46.422  13.499 170.144  1.00 36.32      A    C  
ANISOU  690  CD2 LEU C 752     4427   5366   4009    536   -410    -78  A    C  
ATOM    691  N   ASN C 753      41.863  11.774 171.959  1.00 43.57      A    N  
ANISOU  691  N   ASN C 753     5378   6653   4525    423   -151    226  A    N  
ATOM    692  CA  ASN C 753      40.707  11.064 172.485  1.00 46.77      A    C  
ANISOU  692  CA  ASN C 753     5772   7172   4829    370    -77    363  A    C  
ATOM    693  C   ASN C 753      39.437  11.185 171.640  1.00 45.58      A    C  
ANISOU  693  C   ASN C 753     5541   7043   4734    284    -10    413  A    C  
ATOM    694  O   ASN C 753      38.492  10.424 171.835  1.00 46.62      A    O  
ANISOU  694  O   ASN C 753     5649   7248   4817    200     41    555  A    O  
ATOM    695  CB  ASN C 753      40.424  11.548 173.909  1.00 46.10      A    C  
ANISOU  695  CB  ASN C 753     5682   7264   4570    467    -45    343  A    C  
ATOM    696  CG  ASN C 753      39.945  12.992 173.943  1.00 52.35      A    C  
ANISOU  696  CG  ASN C 753     6416   8126   5350    554     -6    208  A    C  
ATOM    697  ND2 ASN C 753      38.859  13.245 174.670  1.00 56.92      A    N  
ANISOU  697  ND2 ASN C 753     6950   8872   5804    600     94    250  A    N  
ATOM    698  OD1 ASN C 753      40.538  13.869 173.312  1.00 51.25      A    O  
ANISOU  698  OD1 ASN C 753     6273   7887   5314    583    -58     77  A    O  
ATOM    699  N   ASN C 754      39.406  12.129 170.706  1.00 41.73      A    N  
ANISOU  699  N   ASN C 754     5005   6499   4352    298    -17    311  A    N  
ATOM    700  CA  ASN C 754      38.195  12.330 169.923  1.00 41.86      A    C  
ANISOU  700  CA  ASN C 754     4931   6555   4418    226     33    365  A    C  
ATOM    701  C   ASN C 754      38.494  12.904 168.536  1.00 39.93      A    C  
ANISOU  701  C   ASN C 754     4680   6176   4317    201     -7    284  A    C  
ATOM    702  O   ASN C 754      39.655  13.152 168.193  1.00 36.05      A    O  
ANISOU  702  O   ASN C 754     4246   5562   3887    240    -60    189  A    O  
ATOM    703  CB  ASN C 754      37.227  13.239 170.690  1.00 41.90      A    C  
ANISOU  703  CB  ASN C 754     4839   6744   4337    321    115    353  A    C  
ATOM    704  CG  ASN C 754      37.835  14.606 171.005  1.00 45.02      A    C  
ANISOU  704  CG  ASN C 754     5252   7127   4729    470    100    173  A    C  
ATOM    705  ND2 ASN C 754      37.186  15.356 171.908  1.00 45.21      A    N  
ANISOU  705  ND2 ASN C 754     5238   7295   4643    588    176    141  A    N  
ATOM    706  OD1 ASN C 754      38.863  14.988 170.433  1.00 40.22      A    O  
ANISOU  706  OD1 ASN C 754     4693   6376   4212    478     25     69  A    O  
ATOM    707  N   ALA C 755      37.449  13.131 167.750  1.00 41.18      A    N  
ANISOU  707  N   ALA C 755     4756   6369   4522    136     20    334  A    N  
ATOM    708  CA  ALA C 755      37.613  13.625 166.385  1.00 42.80      A    C  
ANISOU  708  CA  ALA C 755     4958   6457   4845    102    -17    278  A    C  
ATOM    709  C   ALA C 755      38.333  14.963 166.375  1.00 41.80      A    C  
ANISOU  709  C   ALA C 755     4825   6291   4767    231    -28    126  A    C  
ATOM    710  O   ALA C 755      39.070  15.270 165.444  1.00 43.43      A    O  
ANISOU  710  O   ALA C 755     5068   6367   5065    221    -68     62  A    O  
ATOM    711  CB  ALA C 755      36.235  13.750 165.674  1.00 35.03      A    C  
ANISOU  711  CB  ALA C 755     3865   5554   3889     18      5    372  A    C  
ATOM    712  N   ASP C 756      38.106  15.771 167.404  1.00 40.72      A    N  
ANISOU  712  N   ASP C 756     4648   6262   4560    350     11     70  A    N  
ATOM    713  CA  ASP C 756      38.756  17.079 167.478  1.00 39.18      A    C  
ANISOU  713  CA  ASP C 756     4469   6013   4405    462    -11    -79  A    C  
ATOM    714  C   ASP C 756      40.268  16.941 167.493  1.00 36.19      A    C  
ANISOU  714  C   ASP C 756     4174   5512   4065    461    -88   -155  A    C  
ATOM    715  O   ASP C 756      40.976  17.732 166.862  1.00 33.56      A    O  
ANISOU  715  O   ASP C 756     3850   5073   3830    479   -128   -242  A    O  
ATOM    716  CB  ASP C 756      38.288  17.848 168.716  1.00 41.54      A    C  
ANISOU  716  CB  ASP C 756     4752   6439   4593    594     43   -136  A    C  
ATOM    717  CG  ASP C 756      37.014  18.630 168.455  1.00 45.97      A    C  
ANISOU  717  CG  ASP C 756     5212   7087   5166    654    121   -110  A    C  
ATOM    718  OD1 ASP C 756      36.457  18.497 167.343  1.00 41.32      A    O  
ANISOU  718  OD1 ASP C 756     4555   6476   4670    574    119    -32  A    O  
ATOM    719  OD2 ASP C 756      36.566  19.357 169.362  1.00 45.46      A    O1-
ANISOU  719  OD2 ASP C 756     5142   7117   5014    787    185   -163  A    O1-
ATOM    720  N   SER C 757      40.774  15.934 168.197  1.00 35.52      A    N  
ANISOU  720  N   SER C 757     4142   5445   3909    441   -108   -107  A    N  
ATOM    721  CA  SER C 757      42.231  15.835 168.305  1.00 41.61      A    C  
ANISOU  721  CA  SER C 757     4968   6122   4719    458   -183   -164  A    C  
ATOM    722  C   SER C 757      42.772  15.265 167.006  1.00 39.97      A    C  
ANISOU  722  C   SER C 757     4780   5779   4629    385   -197   -126  A    C  
ATOM    723  O   SER C 757      43.867  15.625 166.575  1.00 39.87      A    O  
ANISOU  723  O   SER C 757     4773   5674   4702    403   -241   -183  A    O  
ATOM    724  CB  SER C 757      42.682  14.985 169.513  1.00 47.52      A    C  
ANISOU  724  CB  SER C 757     5767   6936   5353    481   -208   -118  A    C  
ATOM    725  OG  SER C 757      42.077  13.708 169.545  1.00 50.07      A    O  
ANISOU  725  OG  SER C 757     6111   7287   5628    411   -168     21  A    O  
ATOM    726  N   VAL C 758      41.996  14.395 166.367  1.00 34.67      A    N  
ANISOU  726  N   VAL C 758     4121   5096   3956    298   -160    -26  A    N  
ATOM    727  CA  VAL C 758      42.392  13.840 165.072  1.00 35.87      A    C  
ANISOU  727  CA  VAL C 758     4322   5113   4195    231   -165      1  A    C  
ATOM    728  C   VAL C 758      42.537  14.930 164.014  1.00 36.70      A    C  
ANISOU  728  C   VAL C 758     4388   5156   4399    239   -168    -72  A    C  
ATOM    729  O   VAL C 758      43.517  14.942 163.249  1.00 37.45      A    O  
ANISOU  729  O   VAL C 758     4514   5144   4573    245   -180    -99  A    O  
ATOM    730  CB  VAL C 758      41.386  12.785 164.579  1.00 34.68      A    C  
ANISOU  730  CB  VAL C 758     4210   4957   4011    114   -142    113  A    C  
ATOM    731  CG1 VAL C 758      41.636  12.431 163.107  1.00 35.58      A    C  
ANISOU  731  CG1 VAL C 758     4394   4929   4196     46   -148    117  A    C  
ATOM    732  CG2 VAL C 758      41.480  11.534 165.431  1.00 36.01      A    C  
ANISOU  732  CG2 VAL C 758     4446   5137   4101     92   -143    201  A    C  
ATOM    733  N   GLN C 759      41.570  15.841 163.969  1.00 31.52      A    N  
ANISOU  733  N   GLN C 759     3663   4573   3742    250   -149    -91  A    N  
ATOM    734  CA  GLN C 759      41.615  16.956 163.021  1.00 34.69      A    C  
ANISOU  734  CA  GLN C 759     4029   4916   4236    265   -153   -149  A    C  
ATOM    735  C   GLN C 759      42.803  17.880 163.298  1.00 33.64      A    C  
ANISOU  735  C   GLN C 759     3894   4726   4163    338   -189   -252  A    C  
ATOM    736  O   GLN C 759      43.530  18.279 162.385  1.00 30.84      A    O  
ANISOU  736  O   GLN C 759     3544   4273   3902    326   -201   -276  A    O  
ATOM    737  CB  GLN C 759      40.324  17.771 163.083  1.00 38.05      A    C  
ANISOU  737  CB  GLN C 759     4376   5437   4646    289   -124   -140  A    C  
ATOM    738  CG  GLN C 759      40.337  19.027 162.215  1.00 46.03      A    C  
ANISOU  738  CG  GLN C 759     5354   6384   5750    322   -130   -193  A    C  
ATOM    739  CD  GLN C 759      38.946  19.423 161.758  1.00 55.60      A    C  
ANISOU  739  CD  GLN C 759     6489   7675   6962    315   -102   -129  A    C  
ATOM    740  NE2 GLN C 759      38.866  20.398 160.850  1.00 58.11      A    N  
ANISOU  740  NE2 GLN C 759     6784   7933   7362    335   -110   -148  A    N  
ATOM    741  OE1 GLN C 759      37.950  18.872 162.235  1.00 58.58      A    O  
ANISOU  741  OE1 GLN C 759     6815   8174   7269    293    -74    -50  A    O  
ATOM    742  N   ALA C 760      42.990  18.222 164.566  1.00 32.18      A    N  
ANISOU  742  N   ALA C 760     3704   4605   3917    405   -210   -307  A    N  
ATOM    743  CA  ALA C 760      44.091  19.105 164.959  1.00 33.30      A    C  
ANISOU  743  CA  ALA C 760     3847   4697   4107    453   -269   -406  A    C  
ATOM    744  C   ALA C 760      45.456  18.482 164.597  1.00 34.57      A    C  
ANISOU  744  C   ALA C 760     4019   4782   4333    425   -305   -381  A    C  
ATOM    745  O   ALA C 760      46.335  19.153 164.062  1.00 32.45      A    O  
ANISOU  745  O   ALA C 760     3726   4436   4169    420   -335   -419  A    O  
ATOM    746  CB  ALA C 760      44.012  19.420 166.456  1.00 36.25      A    C  
ANISOU  746  CB  ALA C 760     4241   5161   4370    521   -296   -468  A    C  
ATOM    747  N   LYS C 761      45.634  17.191 164.841  1.00 31.13      A    N  
ANISOU  747  N   LYS C 761     3617   4366   3846    411   -294   -305  A    N  
ATOM    748  CA  LYS C 761      46.916  16.589 164.506  1.00 31.59      A    C  
ANISOU  748  CA  LYS C 761     3680   4356   3968    414   -313   -272  A    C  
ATOM    749  C   LYS C 761      47.097  16.426 162.970  1.00 30.92      A    C  
ANISOU  749  C   LYS C 761     3608   4168   3973    377   -261   -238  A    C  
ATOM    750  O   LYS C 761      48.207  16.550 162.465  1.00 32.29      A    O  
ANISOU  750  O   LYS C 761     3753   4283   4235    395   -264   -236  A    O  
ATOM    751  CB  LYS C 761      47.070  15.226 165.206  1.00 33.75      A    C  
ANISOU  751  CB  LYS C 761     4002   4662   4160    427   -313   -193  A    C  
ATOM    752  CG  LYS C 761      47.193  15.317 166.728  1.00 39.13      A    C  
ANISOU  752  CG  LYS C 761     4677   5448   4743    471   -373   -215  A    C  
ATOM    753  CD  LYS C 761      48.184  16.404 167.108  1.00 43.98      A    C  
ANISOU  753  CD  LYS C 761     5236   6064   5411    500   -458   -303  A    C  
ATOM    754  CE  LYS C 761      48.278  16.575 168.597  1.00 53.11      A    C  
ANISOU  754  CE  LYS C 761     6409   7322   6447    537   -531   -340  A    C  
ATOM    755  NZ  LYS C 761      48.939  17.864 168.960  1.00 56.10      A    N1+
ANISOU  755  NZ  LYS C 761     6758   7693   6863    540   -626   -452  A    N1+
ATOM    756  N   VAL C 762      46.016  16.110 162.255  1.00 31.41      A    N  
ANISOU  756  N   VAL C 762     3711   4220   4004    325   -213   -203  A    N  
ATOM    757  CA  VAL C 762      46.079  15.930 160.807  1.00 31.64      A    C  
ANISOU  757  CA  VAL C 762     3779   4157   4086    286   -169   -176  A    C  
ATOM    758  C   VAL C 762      46.466  17.248 160.130  1.00 33.09      A    C  
ANISOU  758  C   VAL C 762     3901   4304   4367    295   -174   -226  A    C  
ATOM    759  O   VAL C 762      47.267  17.273 159.206  1.00 35.59      A    O  
ANISOU  759  O   VAL C 762     4224   4548   4750    298   -144   -212  A    O  
ATOM    760  CB  VAL C 762      44.737  15.412 160.246  1.00 29.25      A    C  
ANISOU  760  CB  VAL C 762     3530   3864   3719    207   -146   -127  A    C  
ATOM    761  N   GLU C 763      45.885  18.337 160.592  1.00 30.10      A    N  
ANISOU  761  N   GLU C 763     3471   3972   3994    306   -203   -280  A    N  
ATOM    762  CA  GLU C 763      46.250  19.649 160.073  1.00 30.75      A    C  
ANISOU  762  CA  GLU C 763     3508   4003   4174    312   -217   -326  A    C  
ATOM    763  C   GLU C 763      47.729  19.975 160.338  1.00 32.49      A    C  
ANISOU  763  C   GLU C 763     3684   4186   4476    332   -255   -350  A    C  
ATOM    764  O   GLU C 763      48.456  20.424 159.443  1.00 32.93      A    O  
ANISOU  764  O   GLU C 763     3711   4175   4625    316   -238   -333  A    O  
ATOM    765  CB  GLU C 763      45.347  20.718 160.686  1.00 35.25      A    C  
ANISOU  765  CB  GLU C 763     4051   4615   4725    342   -241   -385  A    C  
ATOM    766  CG  GLU C 763      44.130  21.022 159.839  0.56 41.92      A    C  
ANISOU  766  CG  GLU C 763     4893   5468   5565    322   -206   -347  A    C  
ATOM    767  CD  GLU C 763      43.067  21.791 160.592  0.33 48.83      A    C  
ANISOU  767  CD  GLU C 763     5740   6413   6401    380   -206   -385  A    C  
ATOM    768  OE1 GLU C 763      41.874  21.430 160.475  0.82 53.03      A    O  
ANISOU  768  OE1 GLU C 763     6250   7022   6875    369   -176   -325  A    O  
ATOM    769  OE2 GLU C 763      43.427  22.755 161.300  0.36 51.21      A    O1-
ANISOU  769  OE2 GLU C 763     6040   6689   6726    436   -238   -470  A    O1-
ATOM    770  N   MET C 764      48.191  19.722 161.559  1.00 30.88      A    N  
ANISOU  770  N   MET C 764     3466   4035   4233    362   -309   -376  A    N  
ATOM    771  CA  MET C 764      49.607  19.928 161.832  1.00 31.51      A    C  
ANISOU  771  CA  MET C 764     3484   4097   4390    368   -361   -379  A    C  
ATOM    772  C   MET C 764      50.530  19.063 160.969  1.00 34.45      A    C  
ANISOU  772  C   MET C 764     3840   4432   4818    379   -302   -293  A    C  
ATOM    773  O   MET C 764      51.545  19.555 160.455  1.00 33.76      A    O  
ANISOU  773  O   MET C 764     3678   4308   4839    370   -304   -272  A    O  
ATOM    774  CB  MET C 764      49.937  19.676 163.290  1.00 35.35      A    C  
ANISOU  774  CB  MET C 764     3966   4660   4807    397   -441   -408  A    C  
ATOM    775  CG  MET C 764      51.436  19.786 163.475  1.00 40.13      A    C  
ANISOU  775  CG  MET C 764     4487   5260   5502    393   -507   -387  A    C  
ATOM    776  SD  MET C 764      52.066  18.259 164.108  1.00 62.94      A    S  
ANISOU  776  SD  MET C 764     7372   8211   8330    451   -509   -298  A    S  
ATOM    777  CE  MET C 764      51.655  18.642 165.812  1.00 38.18      A    C  
ANISOU  777  CE  MET C 764     4273   5168   5064    456   -623   -382  A    C  
ATOM    778  N   LEU C 765      50.200  17.777 160.816  1.00 32.00      A    N  
ANISOU  778  N   LEU C 765     3600   4125   4433    400   -246   -239  A    N  
ATOM    779  CA  LEU C 765      50.965  16.929 159.911  1.00 32.41      A    C  
ANISOU  779  CA  LEU C 765     3670   4121   4521    431   -170   -167  A    C  
ATOM    780  C   LEU C 765      50.967  17.477 158.466  1.00 35.19      A    C  
ANISOU  780  C   LEU C 765     4029   4407   4934    403   -100   -156  A    C  
ATOM    781  O   LEU C 765      51.994  17.396 157.795  1.00 35.14      A    O  
ANISOU  781  O   LEU C 765     3981   4370   4999    437    -47   -108  A    O  
ATOM    782  CB  LEU C 765      50.426  15.483 159.913  1.00 31.97      A    C  
ANISOU  782  CB  LEU C 765     3734   4049   4366    448   -123   -122  A    C  
ATOM    783  CG  LEU C 765      50.675  14.717 161.212  1.00 32.08      A    C  
ANISOU  783  CG  LEU C 765     3748   4117   4323    491   -173    -97  A    C  
ATOM    784  CD1 LEU C 765      50.183  13.295 161.098  1.00 32.02      A    C  
ANISOU  784  CD1 LEU C 765     3872   4062   4231    497   -124    -41  A    C  
ATOM    785  CD2 LEU C 765      52.175  14.776 161.639  1.00 31.38      A    C  
ANISOU  785  CD2 LEU C 765     3551   4055   4318    559   -208    -64  A    C  
ATOM    786  N   ASP C 766      49.832  18.007 157.988  1.00 33.69      A    N  
ANISOU  786  N   ASP C 766     3884   4205   4711    350    -97   -187  A    N  
ATOM    787  CA  ASP C 766      49.778  18.587 156.636  1.00 38.56      A    C  
ANISOU  787  CA  ASP C 766     4513   4766   5373    321    -42   -169  A    C  
ATOM    788  C   ASP C 766      50.857  19.660 156.510  1.00 36.64      A    C  
ANISOU  788  C   ASP C 766     4156   4507   5256    322    -57   -166  A    C  
ATOM    789  O   ASP C 766      51.569  19.744 155.517  1.00 38.58      A    O  
ANISOU  789  O   ASP C 766     4384   4716   5557    330     12   -113  A    O  
ATOM    790  CB  ASP C 766      48.422  19.242 156.320  1.00 33.92      A    C  
ANISOU  790  CB  ASP C 766     3956   4184   4747    270    -63   -195  A    C  
ATOM    791  CG  ASP C 766      47.286  18.245 156.140  1.00 39.59      A    C  
ANISOU  791  CG  ASP C 766     4775   4918   5351    237    -50   -173  A    C  
ATOM    792  OD1 ASP C 766      47.487  17.007 156.168  1.00 39.77      A    O  
ANISOU  792  OD1 ASP C 766     4873   4922   5315    246    -21   -145  A    O  
ATOM    793  OD2 ASP C 766      46.149  18.735 155.974  1.00 44.89      A    O1-
ANISOU  793  OD2 ASP C 766     5444   5618   5995    198    -73   -178  A    O1-
ATOM    794  N   ASN C 767      50.971  20.482 157.542  1.00 34.87      A    N  
ANISOU  794  N   ASN C 767     3863   4312   5073    310   -149   -220  A    N  
ATOM    795  CA  ASN C 767      51.951  21.551 157.519  1.00 36.16      A    C  
ANISOU  795  CA  ASN C 767     3924   4452   5364    282   -190   -218  A    C  
ATOM    796  C   ASN C 767      53.380  21.017 157.680  1.00 39.07      A    C  
ANISOU  796  C   ASN C 767     4197   4850   5796    312   -182   -153  A    C  
ATOM    797  O   ASN C 767      54.292  21.474 156.991  1.00 40.29      A    O  
ANISOU  797  O   ASN C 767     4266   4984   6057    294   -148    -93  A    O  
ATOM    798  CB  ASN C 767      51.602  22.584 158.577  1.00 37.25      A    C  
ANISOU  798  CB  ASN C 767     4048   4593   5511    254   -301   -308  A    C  
ATOM    799  CG  ASN C 767      50.330  23.347 158.215  1.00 48.01      A    C  
ANISOU  799  CG  ASN C 767     5478   5919   6846    243   -291   -351  A    C  
ATOM    800  ND2 ASN C 767      49.186  22.863 158.681  1.00 49.81      A    N  
ANISOU  800  ND2 ASN C 767     5768   6197   6961    274   -284   -381  A    N  
ATOM    801  OD1 ASN C 767      50.378  24.338 157.500  1.00 55.44      A    O  
ANISOU  801  OD1 ASN C 767     6405   6791   7869    210   -286   -341  A    O  
ATOM    802  N   LEU C 768      53.570  20.019 158.537  1.00 38.13      A    N  
ANISOU  802  N   LEU C 768     4087   4786   5616    363   -204   -148  A    N  
ATOM    803  CA  LEU C 768      54.900  19.433 158.692  1.00 41.28      A    C  
ANISOU  803  CA  LEU C 768     4386   5223   6077    413   -193    -69  A    C  
ATOM    804  C   LEU C 768      55.377  18.847 157.365  1.00 40.98      A    C  
ANISOU  804  C   LEU C 768     4358   5148   6065    467    -46     17  A    C  
ATOM    805  O   LEU C 768      56.539  18.983 156.997  1.00 41.10      A    O  
ANISOU  805  O   LEU C 768     4250   5183   6183    491     -8     96  A    O  
ATOM    806  CB  LEU C 768      54.898  18.349 159.769  1.00 45.51      A    C  
ANISOU  806  CB  LEU C 768     4952   5813   6527    474   -234    -65  A    C  
ATOM    807  CG  LEU C 768      54.939  18.799 161.231  1.00 46.63      A    C  
ANISOU  807  CG  LEU C 768     5053   6020   6643    443   -383   -124  A    C  
ATOM    808  CD1 LEU C 768      55.159  17.587 162.146  1.00 45.99      A    C  
ANISOU  808  CD1 LEU C 768     4992   5999   6483    517   -406    -81  A    C  
ATOM    809  CD2 LEU C 768      56.054  19.806 161.404  1.00 48.02      A    C  
ANISOU  809  CD2 LEU C 768     5081   6215   6950    387   -473   -111  A    C  
ATOM    810  N   LEU C 769      54.464  18.199 156.654  1.00 38.07      A    N  
ANISOU  810  N   LEU C 769     4139   4730   5597    484     37      3  A    N  
ATOM    811  CA  LEU C 769      54.793  17.576 155.384  1.00 38.99      A    C  
ANISOU  811  CA  LEU C 769     4316   4799   5699    542    179     65  A    C  
ATOM    812  C   LEU C 769      55.325  18.625 154.412  1.00 39.12      A    C  
ANISOU  812  C   LEU C 769     4246   4804   5813    505    228    107  A    C  
ATOM    813  O   LEU C 769      56.333  18.405 153.750  1.00 40.25      A    O  
ANISOU  813  O   LEU C 769     4327   4956   6010    568    331    190  A    O  
ATOM    814  CB  LEU C 769      53.571  16.874 154.791  1.00 40.68      A    C  
ANISOU  814  CB  LEU C 769     4723   4954   5778    527    224     29  A    C  
ATOM    815  CG  LEU C 769      53.862  15.843 153.692  1.00 44.95      A    C  
ANISOU  815  CG  LEU C 769     5390   5432   6257    604    362     73  A    C  
ATOM    816  CD1 LEU C 769      54.696  14.732 154.254  1.00 46.37      A    C  
ANISOU  816  CD1 LEU C 769     5566   5614   6440    718    398    117  A    C  
ATOM    817  CD2 LEU C 769      52.576  15.279 153.094  1.00 46.55      A    C  
ANISOU  817  CD2 LEU C 769     5792   5572   6323    549    371     31  A    C  
ATOM    818  N   ASP C 770      54.647  19.767 154.339  1.00 36.93      A    N  
ANISOU  818  N   ASP C 770     3965   4508   5559    412    163     59  A    N  
ATOM    819  CA  ASP C 770      55.088  20.843 153.450  1.00 43.32      A    C  
ANISOU  819  CA  ASP C 770     4702   5295   6464    363    200    108  A    C  
ATOM    820  C   ASP C 770      56.415  21.445 153.909  1.00 41.11      A    C  
ANISOU  820  C   ASP C 770     4230   5058   6334    342    157    167  A    C  
ATOM    821  O   ASP C 770      57.203  21.908 153.094  1.00 38.67      A    O  
ANISOU  821  O   ASP C 770     3831   4750   6113    330    230    256  A    O  
ATOM    822  CB  ASP C 770      54.049  21.962 153.366  1.00 46.65      A    C  
ANISOU  822  CB  ASP C 770     5169   5673   6885    277    128     48  A    C  
ATOM    823  CG  ASP C 770      52.833  21.582 152.523  1.00 57.16      A    C  
ANISOU  823  CG  ASP C 770     6655   6971   8090    279    179     29  A    C  
ATOM    824  OD1 ASP C 770      52.921  20.644 151.706  1.00 56.78      A    O  
ANISOU  824  OD1 ASP C 770     6694   6914   7964    326    282     67  A    O  
ATOM    825  OD2 ASP C 770      51.782  22.239 152.683  1.00 62.25      A    O1-
ANISOU  825  OD2 ASP C 770     7338   7599   8713    233    112    -21  A    O1-
ATOM    826  N   ILE C 771      56.628  21.491 155.219  1.00 39.39      A    N  
ANISOU  826  N   ILE C 771     3946   4880   6141    326     29    123  A    N  
ATOM    827  CA  ILE C 771      57.868  22.038 155.739  1.00 40.36      A    C  
ANISOU  827  CA  ILE C 771     3883   5052   6402    285    -44    181  A    C  
ATOM    828  C   ILE C 771      59.008  21.088 155.409  1.00 42.42      A    C  
ANISOU  828  C   ILE C 771     4039   5379   6700    387     63    301  A    C  
ATOM    829  O   ILE C 771      60.104  21.534 155.062  1.00 43.41      A    O  
ANISOU  829  O   ILE C 771     3994   5545   6955    365     89    407  A    O  
ATOM    830  CB  ILE C 771      57.781  22.294 157.245  1.00 38.06      A    C  
ANISOU  830  CB  ILE C 771     3569   4790   6101    241   -221     97  A    C  
ATOM    831  CG1 ILE C 771      56.917  23.546 157.491  1.00 40.58      A    C  
ANISOU  831  CG1 ILE C 771     3962   5034   6421    143   -317     -9  A    C  
ATOM    832  CG2 ILE C 771      59.177  22.477 157.838  1.00 36.36      A    C  
ANISOU  832  CG2 ILE C 771     3156   4649   6009    209   -306    175  A    C  
ATOM    833  CD1 ILE C 771      56.568  23.797 158.951  1.00 41.94      A    C  
ANISOU  833  CD1 ILE C 771     4172   5225   6538    117   -473   -120  A    C  
ATOM    834  N   GLU C 772      58.740  19.780 155.483  1.00 38.23      A    N  
ANISOU  834  N   GLU C 772     3612   4855   6060    503    133    295  A    N  
ATOM    835  CA  GLU C 772      59.768  18.798 155.161  1.00 38.43      A    C  
ANISOU  835  CA  GLU C 772     3563   4928   6110    635    251    407  A    C  
ATOM    836  C   GLU C 772      60.127  18.925 153.681  1.00 38.29      A    C  
ANISOU  836  C   GLU C 772     3545   4888   6116    672    429    486  A    C  
ATOM    837  O   GLU C 772      61.296  18.851 153.312  1.00 43.33      A    O  
ANISOU  837  O   GLU C 772     4024   5590   6851    736    517    611  A    O  
ATOM    838  CB  GLU C 772      59.306  17.366 155.503  1.00 41.32      A    C  
ANISOU  838  CB  GLU C 772     4082   5270   6345    751    291    376  A    C  
ATOM    839  CG  GLU C 772      60.404  16.285 155.383  1.00 45.80      A    C  
ANISOU  839  CG  GLU C 772     4581   5878   6942    917    402    491  A    C  
ATOM    840  CD  GLU C 772      60.760  15.947 153.933  1.00 52.71      A    C  
ANISOU  840  CD  GLU C 772     5508   6714   7803   1016    613    556  A    C  
ATOM    841  OE1 GLU C 772      59.859  15.999 153.057  1.00 51.14      A    O  
ANISOU  841  OE1 GLU C 772     5492   6432   7505    979    677    490  A    O  
ATOM    842  OE2 GLU C 772      61.942  15.645 153.665  1.00 55.12      A    O1-
ANISOU  842  OE2 GLU C 772     5667   7082   8192   1133    716    679  A    O1-
ATOM    843  N   VAL C 773      59.129  19.118 152.827  1.00 39.49      A    N  
ANISOU  843  N   VAL C 773     3868   4961   6176    636    483    426  A    N  
ATOM    844  CA  VAL C 773      59.418  19.282 151.406  1.00 44.91      A    C  
ANISOU  844  CA  VAL C 773     4574   5629   6859    667    648    500  A    C  
ATOM    845  C   VAL C 773      60.306  20.514 151.179  1.00 42.71      A    C  
ANISOU  845  C   VAL C 773     4084   5399   6746    579    634    597  A    C  
ATOM    846  O   VAL C 773      61.315  20.429 150.485  1.00 42.63      A    O  
ANISOU  846  O   VAL C 773     3957   5442   6798    645    772    724  A    O  
ATOM    847  CB  VAL C 773      58.129  19.398 150.566  1.00 49.71      A    C  
ANISOU  847  CB  VAL C 773     5400   6153   7336    620    674    422  A    C  
ATOM    848  CG1 VAL C 773      58.470  19.769 149.113  1.00 47.19      A    C  
ANISOU  848  CG1 VAL C 773     5096   5826   7010    636    829    506  A    C  
ATOM    849  CG2 VAL C 773      57.353  18.088 150.624  1.00 48.47      A    C  
ANISOU  849  CG2 VAL C 773     5452   5945   7019    694    701    350  A    C  
ATOM    850  N   ALA C 774      59.954  21.648 151.787  1.00 40.92      A    N  
ANISOU  850  N   ALA C 774     3807   5150   6592    433    473    544  A    N  
ATOM    851  CA  ALA C 774      60.786  22.853 151.672  1.00 42.36      A    C  
ANISOU  851  CA  ALA C 774     3799   5355   6941    321    432    634  A    C  
ATOM    852  C   ALA C 774      62.230  22.629 152.123  1.00 43.29      A    C  
ANISOU  852  C   ALA C 774     3673   5584   7191    352    432    759  A    C  
ATOM    853  O   ALA C 774      63.187  22.987 151.417  1.00 45.29      A    O  
ANISOU  853  O   ALA C 774     3764   5891   7551    344    531    906  A    O  
ATOM    854  CB  ALA C 774      60.162  24.002 152.471  1.00 40.69      A    C  
ANISOU  854  CB  ALA C 774     3605   5080   6776    171    236    533  A    C  
ATOM    855  N   TYR C 775      62.401  22.028 153.296  1.00 45.06      A    N  
ANISOU  855  N   TYR C 775     3859   5855   7406    389    322    718  A    N  
ATOM    856  CA  TYR C 775      63.747  21.865 153.830  1.00 46.83      A    C  
ANISOU  856  CA  TYR C 775     3833   6198   7761    409    289    845  A    C  
ATOM    857  C   TYR C 775      64.544  20.875 152.999  1.00 49.36      A    C  
ANISOU  857  C   TYR C 775     4087   6589   8079    593    510    982  A    C  
ATOM    858  O   TYR C 775      65.745  21.045 152.831  1.00 48.25      A    O  
ANISOU  858  O   TYR C 775     3702   6553   8077    604    557   1143  A    O  
ATOM    859  CB  TYR C 775      63.719  21.420 155.294  1.00 47.68      A    C  
ANISOU  859  CB  TYR C 775     3929   6346   7843    414    112    775  A    C  
ATOM    860  CG  TYR C 775      65.065  21.571 155.986  1.00 50.75      A    C  
ANISOU  860  CG  TYR C 775     4039   6861   8383    379     10    904  A    C  
ATOM    861  CD1 TYR C 775      65.567  22.829 156.298  1.00 54.31      A    C  
ANISOU  861  CD1 TYR C 775     4337   7324   8974    185   -146    934  A    C  
ATOM    862  CD2 TYR C 775      65.825  20.461 156.327  1.00 52.41      A    C  
ANISOU  862  CD2 TYR C 775     4141   7175   8599    537     59   1002  A    C  
ATOM    863  CE1 TYR C 775      66.796  22.984 156.928  1.00 57.55      A    C  
ANISOU  863  CE1 TYR C 775     4481   7860   9527    128   -263   1061  A    C  
ATOM    864  CE2 TYR C 775      67.058  20.602 156.959  1.00 57.47      A    C  
ANISOU  864  CE2 TYR C 775     4502   7951   9383    504    -48   1138  A    C  
ATOM    865  CZ  TYR C 775      67.537  21.867 157.257  1.00 59.95      A    C  
ANISOU  865  CZ  TYR C 775     4656   8289   9835    290   -215   1168  A    C  
ATOM    866  OH  TYR C 775      68.759  22.008 157.879  1.00 65.05      A    O  
ANISOU  866  OH  TYR C 775     5015   9078  10626    235   -341   1313  A    O  
ATOM    867  N   SER C 776      63.874  19.860 152.459  1.00 48.59      A    N  
ANISOU  867  N   SER C 776     4207   6432   7824    735    649    922  A    N  
ATOM    868  CA  SER C 776      64.542  18.901 151.586  1.00 52.23      A    C  
ANISOU  868  CA  SER C 776     4659   6931   8255    931    880   1031  A    C  
ATOM    869  C   SER C 776      65.013  19.580 150.310  1.00 51.67      A    C  
ANISOU  869  C   SER C 776     4512   6883   8238    911   1039   1143  A    C  
ATOM    870  O   SER C 776      66.024  19.197 149.742  1.00 48.70      A    O  
ANISOU  870  O   SER C 776     3997   6593   7912   1043   1213   1291  A    O  
ATOM    871  CB  SER C 776      63.621  17.738 151.229  1.00 56.01      A    C  
ANISOU  871  CB  SER C 776     5436   7308   8538   1060    977    923  A    C  
ATOM    872  OG  SER C 776      63.548  16.808 152.290  1.00 62.04      A    O  
ANISOU  872  OG  SER C 776     6235   8073   9265   1137    892    882  A    O  
ATOM    873  N   LEU C 777      64.271  20.582 149.849  1.00 50.93      A    N  
ANISOU  873  N   LEU C 777     4509   6716   8128    759    991   1083  A    N  
ATOM    874  CA  LEU C 777      64.707  21.306 148.657  1.00 56.21      A    C  
ANISOU  874  CA  LEU C 777     5105   7406   8846    725   1133   1204  A    C  
ATOM    875  C   LEU C 777      66.017  22.055 148.921  1.00 58.24      A    C  
ANISOU  875  C   LEU C 777     5025   7782   9321    643   1100   1378  A    C  
ATOM    876  O   LEU C 777      66.948  22.011 148.112  1.00 59.97      A    O  
ANISOU  876  O   LEU C 777     5093   8093   9598    719   1285   1548  A    O  
ATOM    877  CB  LEU C 777      63.622  22.273 148.186  1.00 56.59      A    C  
ANISOU  877  CB  LEU C 777     5315   7345   8842    575   1067   1115  A    C  
ATOM    878  CG  LEU C 777      62.523  21.635 147.341  1.00 52.28      A    C  
ANISOU  878  CG  LEU C 777     5070   6712   8084    656   1169   1014  A    C  
ATOM    879  CD1 LEU C 777      61.515  22.698 146.918  1.00 50.68      A    C  
ANISOU  879  CD1 LEU C 777     4983   6420   7852    507   1087    954  A    C  
ATOM    880  CD2 LEU C 777      63.119  20.932 146.133  1.00 54.19      A    C  
ANISOU  880  CD2 LEU C 777     5350   6995   8242    821   1428   1116  A    C  
ATOM    881  N   LEU C 778      66.093  22.722 150.069  1.00 59.81      A    N  
ANISOU  881  N   LEU C 778     5106   7984   9634    485    862   1340  A    N  
ATOM    882  CA  LEU C 778      67.322  23.378 150.512  1.00 64.84      A    C  
ANISOU  882  CA  LEU C 778     5421   8734  10481    378    778   1497  A    C  
ATOM    883  C   LEU C 778      68.473  22.387 150.737  1.00 69.14      A    C  
ANISOU  883  C   LEU C 778     5754   9434  11084    551    875   1642  A    C  
ATOM    884  O   LEU C 778      69.625  22.784 150.944  1.00 72.39      A    O  
ANISOU  884  O   LEU C 778     5859   9974  11674    489    841   1816  A    O  
ATOM    885  CB  LEU C 778      67.046  24.162 151.793  1.00 62.65      A    C  
ANISOU  885  CB  LEU C 778     5123   8409  10273    183    482   1389  A    C  
ATOM    886  CG  LEU C 778      66.233  25.449 151.666  1.00 57.00      A    C  
ANISOU  886  CG  LEU C 778     4535   7552   9569    -12    366   1293  A    C  
ATOM    887  CD1 LEU C 778      65.957  25.991 153.045  1.00 56.90      A    C  
ANISOU  887  CD1 LEU C 778     4539   7491   9589   -154     89   1163  A    C  
ATOM    888  CD2 LEU C 778      66.993  26.489 150.842  1.00 56.73      A    C  
ANISOU  888  CD2 LEU C 778     4324   7536   9694   -146    422   1467  A    C  
ATOM    889  N   ARG C 779      68.131  21.100 150.691  1.00 70.99      A    N  
ANISOU  889  N   ARG C 779     6154   9651  11169    767    991   1577  A    N  
ATOM    890  CA  ARG C 779      69.050  19.979 150.874  1.00 75.12      A    C  
ANISOU  890  CA  ARG C 779     6538  10289  11714    984   1105   1694  A    C  
ATOM    891  C   ARG C 779      69.594  19.952 152.292  1.00 80.75      A    C  
ANISOU  891  C   ARG C 779     7054  11090  12538    924    875   1719  A    C  
ATOM    892  O   ARG C 779      68.918  19.458 153.200  1.00 81.49      A    O  
ANISOU  892  O   ARG C 779     7305  11121  12535    936    737   1576  A    O  
ATOM    893  CB  ARG C 779      70.183  20.026 149.848  1.00 73.19      A    C  
ANISOU  893  CB  ARG C 779     6071  10172  11567   1084   1342   1918  A    C  
ATOM    894  CG  ARG C 779      69.677  19.895 148.414  0.76 71.62      A    C  
ANISOU  894  CG  ARG C 779     6096   9895  11221   1177   1589   1894  A    C  
ATOM    895  CD  ARG C 779      69.488  18.439 148.013  0.65 69.22      A    C  
ANISOU  895  CD  ARG C 779     6009   9548  10743   1459   1789   1842  A    C  
ATOM    896  NE  ARG C 779      68.108  18.082 147.680  0.44 64.82      A    N  
ANISOU  896  NE  ARG C 779     5841   8815   9973   1456   1782   1632  A    N  
ATOM    897  CZ  ARG C 779      67.460  18.462 146.580  0.24 62.07      A    C  
ANISOU  897  CZ  ARG C 779     5686   8390   9508   1414   1886   1585  A    C  
ATOM    898  NH1 ARG C 779      68.045  19.244 145.683  0.35 64.75      A    N1+
ANISOU  898  NH1 ARG C 779     5882   8804   9915   1372   2015   1730  A    N1+
ATOM    899  NH2 ARG C 779      66.214  18.062 146.377  1.00 57.16      A    N  
ANISOU  899  NH2 ARG C 779     5396   7623   8700   1406   1853   1403  A    N  
ATOM    900  N   SER C 785      79.979  28.333 144.930  1.00111.24      A    N  
ANISOU  900  N   SER C 785     8662  15936  17669   -175   1640   3909  A    N  
ATOM    901  CA  SER C 785      79.246  29.555 144.616  1.00109.06      A    C  
ANISOU  901  CA  SER C 785     8507  15500  17432   -423   1545   3861  A    C  
ATOM    902  C   SER C 785      78.964  29.674 143.119  1.00109.56      A    C  
ANISOU  902  C   SER C 785     8694  15550  17384   -318   1835   3937  A    C  
ATOM    903  O   SER C 785      79.378  30.639 142.473  1.00109.20      A    O  
ANISOU  903  O   SER C 785     8567  15509  17415   -477   1858   4089  A    O  
ATOM    904  CB  SER C 785      80.018  30.780 145.103  1.00110.08      A    C  
ANISOU  904  CB  SER C 785     8433  15634  17759   -746   1304   3980  A    C  
ATOM    905  OG  SER C 785      79.353  31.975 144.736  1.00108.23      A    O  
ANISOU  905  OG  SER C 785     8332  15228  17563   -976   1224   3944  A    O  
ATOM    906  N   SER C 786      78.260  28.682 142.581  1.00110.18      A    N  
ANISOU  906  N   SER C 786     8983  15608  17272    -51   2050   3830  A    N  
ATOM    907  CA  SER C 786      77.856  28.669 141.177  1.00109.94      A    C  
ANISOU  907  CA  SER C 786     9124  15558  17092     71   2324   3869  A    C  
ATOM    908  C   SER C 786      77.062  29.931 140.809  1.00107.55      A    C  
ANISOU  908  C   SER C 786     8942  15098  16824   -178   2231   3844  A    C  
ATOM    909  O   SER C 786      77.347  30.589 139.804  1.00109.25      A    O  
ANISOU  909  O   SER C 786     9141  15334  17035   -233   2358   3994  A    O  
ATOM    910  CB  SER C 786      77.028  27.411 140.882  1.00106.54      A    C  
ANISOU  910  CB  SER C 786     8951  15090  16441    365   2508   3704  A    C  
ATOM    911  OG  SER C 786      77.503  26.304 141.629  1.00105.46      A    O  
ANISOU  911  OG  SER C 786     8739  15036  16295    550   2498   3668  A    O  
ATOM    912  N   LYS C 787      76.072  30.261 141.635  1.00101.89      A    N  
ANISOU  912  N   LYS C 787     8351  14221  16142   -323   2008   3659  A    N  
ATOM    913  CA  LYS C 787      75.242  31.442 141.424  1.00 94.45      A    C  
ANISOU  913  CA  LYS C 787     7544  13101  15243   -556   1893   3618  A    C  
ATOM    914  C   LYS C 787      74.769  32.007 142.762  1.00 88.06      A    C  
ANISOU  914  C   LYS C 787     6740  12151  14567   -780   1554   3465  A    C  
ATOM    915  O   LYS C 787      75.045  31.429 143.817  1.00 86.70      A    O  
ANISOU  915  O   LYS C 787     6475  12033  14435   -746   1418   3389  A    O  
ATOM    916  CB  LYS C 787      74.043  31.108 140.532  1.00 90.60      A    C  
ANISOU  916  CB  LYS C 787     7344  12523  14556   -415   2080   3519  A    C  
ATOM    917  N   ASP C 788      74.072  33.142 142.712  1.00 84.97      A    N  
ANISOU  917  N   ASP C 788     6473  11575  14235  -1003   1416   3422  A    N  
ATOM    918  CA  ASP C 788      73.377  33.691 143.879  1.00 82.39      A    C  
ANISOU  918  CA  ASP C 788     6230  11074  14000  -1193   1110   3241  A    C  
ATOM    919  C   ASP C 788      72.500  32.595 144.488  1.00 79.15      A    C  
ANISOU  919  C   ASP C 788     5940  10653  13480  -1012   1112   3040  A    C  
ATOM    920  O   ASP C 788      71.819  31.875 143.755  1.00 77.79      A    O  
ANISOU  920  O   ASP C 788     5915  10492  13152   -812   1332   3003  A    O  
ATOM    921  CB  ASP C 788      72.525  34.907 143.470  1.00 82.76      A    C  
ANISOU  921  CB  ASP C 788     6466  10900  14080  -1384   1032   3212  A    C  
ATOM    922  CG  ASP C 788      72.054  35.758 144.661  1.00 82.88      A    C  
ANISOU  922  CG  ASP C 788     6560  10714  14216  -1619    692   3049  A    C  
ATOM    923  OD1 ASP C 788      71.687  35.216 145.722  1.00 78.47      A    O  
ANISOU  923  OD1 ASP C 788     6025  10141  13648  -1584    547   2877  A    O  
ATOM    924  OD2 ASP C 788      72.010  36.997 144.517  1.00 87.80      A    O1-
ANISOU  924  OD2 ASP C 788     7248  11180  14932  -1833    572   3086  A    O1-
ATOM    925  N   PRO C 789      72.540  32.444 145.823  1.00 77.17      A    N  
ANISOU  925  N   PRO C 789     5635  10386  13298  -1080    867   2913  A    N  
ATOM    926  CA  PRO C 789      71.611  31.554 146.528  1.00 74.96      A    C  
ANISOU  926  CA  PRO C 789     5501  10067  12914   -939    819   2700  A    C  
ATOM    927  C   PRO C 789      70.148  31.779 146.140  1.00 71.24      A    C  
ANISOU  927  C   PRO C 789     5416   9394  12260   -899    820   2491  A    C  
ATOM    928  O   PRO C 789      69.374  30.823 146.120  1.00 68.03      A    O  
ANISOU  928  O   PRO C 789     5216   8977  11654   -691    896   2330  A    O  
ATOM    929  CB  PRO C 789      71.843  31.909 147.996  1.00 75.67      A    C  
ANISOU  929  CB  PRO C 789     5501  10121  13130  -1117    492   2606  A    C  
ATOM    930  CG  PRO C 789      73.281  32.290 148.045  1.00 79.58      A    C  
ANISOU  930  CG  PRO C 789     5762  10744  13731  -1219    448   2790  A    C  
ATOM    931  CD  PRO C 789      73.576  32.979 146.726  1.00 81.33      A    C  
ANISOU  931  CD  PRO C 789     5970  10959  13973  -1266    633   2969  A    C  
ATOM    932  N   ILE C 790      69.781  33.020 145.833  1.00 73.32      A    N  
ANISOU  932  N   ILE C 790     5767   9497  12594  -1097    731   2506  A    N  
ATOM    933  CA  ILE C 790      68.408  33.337 145.434  1.00 71.40      A    C  
ANISOU  933  CA  ILE C 790     5864   9069  12195  -1062    725   2336  A    C  
ATOM    934  C   ILE C 790      68.002  32.613 144.155  1.00 67.38      A    C  
ANISOU  934  C   ILE C 790     5489   8623  11489   -847   1010   2376  A    C  
ATOM    935  O   ILE C 790      66.925  32.021 144.085  1.00 65.41      A    O  
ANISOU  935  O   ILE C 790     5496   8312  11043   -702   1030   2193  A    O  
ATOM    936  CB  ILE C 790      68.213  34.848 145.219  1.00 71.58      A    C  
ANISOU  936  CB  ILE C 790     5939   8908  12348  -1303    601   2387  A    C  
ATOM    937  CG1 ILE C 790      68.507  35.593 146.511  1.00 72.33      A    C  
ANISOU  937  CG1 ILE C 790     5964   8906  12614  -1523    298   2312  A    C  
ATOM    938  CG2 ILE C 790      66.781  35.135 144.806  1.00 69.54      A    C  
ANISOU  938  CG2 ILE C 790     6017   8475  11931  -1240    599   2227  A    C  
ATOM    939  CD1 ILE C 790      67.638  35.124 147.642  1.00 71.12      A    C  
ANISOU  939  CD1 ILE C 790     6001   8682  12340  -1438    131   2031  A    C  
ATOM    940  N   ASP C 791      68.875  32.672 143.154  1.00 64.82      A    N  
ANISOU  940  N   ASP C 791     4989   8424  11213   -834   1225   2620  A    N  
ATOM    941  CA  ASP C 791      68.636  32.042 141.861  1.00 66.73      A    C  
ANISOU  941  CA  ASP C 791     5357   8738  11261   -636   1511   2680  A    C  
ATOM    942  C   ASP C 791      68.579  30.518 141.981  1.00 64.56      A    C  
ANISOU  942  C   ASP C 791     5143   8573  10815   -369   1638   2575  A    C  
ATOM    943  O   ASP C 791      67.741  29.872 141.353  1.00 63.04      A    O  
ANISOU  943  O   ASP C 791     5210   8346  10397   -209   1754   2464  A    O  
ATOM    944  CB  ASP C 791      69.727  32.458 140.856  1.00 74.40      A    C  
ANISOU  944  CB  ASP C 791     6095   9841  12332   -680   1723   2986  A    C  
ATOM    945  CG  ASP C 791      69.473  33.829 140.241  1.00 80.64      A    C  
ANISOU  945  CG  ASP C 791     6939  10497  13201   -889   1677   3095  A    C  
ATOM    946  OD1 ASP C 791      68.559  34.540 140.708  1.00 78.19      A    O  
ANISOU  946  OD1 ASP C 791     6819   9987  12905  -1011   1459   2937  A    O  
ATOM    947  OD2 ASP C 791      70.204  34.210 139.299  1.00 85.85      A    O1-
ANISOU  947  OD2 ASP C 791     7469  11251  13901   -920   1853   3333  A    O1-
ATOM    948  N   VAL C 792      69.477  29.947 142.781  1.00 64.80      A    N  
ANISOU  948  N   VAL C 792     4939   8730  10954   -328   1609   2617  A    N  
ATOM    949  CA  VAL C 792      69.493  28.503 142.994  1.00 64.69      A    C  
ANISOU  949  CA  VAL C 792     4977   8804  10799    -74   1718   2527  A    C  
ATOM    950  C   VAL C 792      68.170  28.022 143.586  1.00 61.70      A    C  
ANISOU  950  C   VAL C 792     4908   8281  10255    -21   1572   2243  A    C  
ATOM    951  O   VAL C 792      67.560  27.084 143.081  1.00 61.52      A    O  
ANISOU  951  O   VAL C 792     5108   8246  10022    167   1707   2144  A    O  
ATOM    952  CB  VAL C 792      70.645  28.082 143.914  1.00 64.01      A    C  
ANISOU  952  CB  VAL C 792     4573   8869  10880    -58   1663   2625  A    C  
ATOM    953  CG1 VAL C 792      70.623  26.579 144.138  1.00 62.59      A    C  
ANISOU  953  CG1 VAL C 792     4470   8757  10554    219   1776   2534  A    C  
ATOM    954  CG2 VAL C 792      71.967  28.514 143.314  1.00 66.55      A    C  
ANISOU  954  CG2 VAL C 792     4563   9355  11367   -107   1813   2925  A    C  
ATOM    955  N   ASN C 793      67.728  28.685 144.649  1.00 60.13      A    N  
ANISOU  955  N   ASN C 793     4727   7973  10148   -194   1296   2118  A    N  
ATOM    956  CA  ASN C 793      66.477  28.337 145.289  1.00 57.22      A    C  
ANISOU  956  CA  ASN C 793     4622   7481   9640   -158   1153   1867  A    C  
ATOM    957  C   ASN C 793      65.284  28.566 144.378  1.00 56.03      A    C  
ANISOU  957  C   ASN C 793     4756   7212   9322   -137   1214   1784  A    C  
ATOM    958  O   ASN C 793      64.376  27.744 144.348  1.00 53.96      A    O  
ANISOU  958  O   ASN C 793     4715   6913   8875    -11   1235   1632  A    O  
ATOM    959  CB  ASN C 793      66.302  29.113 146.594  1.00 59.87      A    C  
ANISOU  959  CB  ASN C 793     4916   7726  10105   -344    859   1760  A    C  
ATOM    960  CG  ASN C 793      67.279  28.664 147.661  1.00 65.93      A    C  
ANISOU  960  CG  ASN C 793     5448   8613  10989   -345    761   1799  A    C  
ATOM    961  ND2 ASN C 793      67.333  29.390 148.773  1.00 69.36      A    N  
ANISOU  961  ND2 ASN C 793     5826   8987  11542   -524    503   1730  A    N  
ATOM    962  OD1 ASN C 793      67.970  27.663 147.489  1.00 66.76      A    O  
ANISOU  962  OD1 ASN C 793     5434   8860  11070   -179    914   1889  A    O  
ATOM    963  N   TYR C 794      65.280  29.668 143.635  1.00 57.04      A    N  
ANISOU  963  N   TYR C 794     4875   7284   9514   -268   1234   1895  A    N  
ATOM    964  CA  TYR C 794      64.211  29.902 142.657  1.00 56.87      A    C  
ANISOU  964  CA  TYR C 794     5107   7169   9331   -242   1299   1850  A    C  
ATOM    965  C   TYR C 794      64.113  28.719 141.694  1.00 54.38      A    C  
ANISOU  965  C   TYR C 794     4922   6940   8799    -29   1536   1858  A    C  
ATOM    966  O   TYR C 794      63.033  28.194 141.445  1.00 50.99      A    O  
ANISOU  966  O   TYR C 794     4744   6451   8179     52   1532   1714  A    O  
ATOM    967  CB  TYR C 794      64.454  31.203 141.891  1.00 56.58      A    C  
ANISOU  967  CB  TYR C 794     5013   7081   9404   -399   1320   2019  A    C  
ATOM    968  CG  TYR C 794      63.531  31.443 140.707  1.00 56.52      A    C  
ANISOU  968  CG  TYR C 794     5238   7009   9228   -361   1415   2026  A    C  
ATOM    969  CD1 TYR C 794      62.262  31.966 140.891  1.00 55.61      A    C  
ANISOU  969  CD1 TYR C 794     5329   6743   9058   -411   1258   1884  A    C  
ATOM    970  CD2 TYR C 794      63.947  31.180 139.406  1.00 56.55      A    C  
ANISOU  970  CD2 TYR C 794     5251   7111   9125   -273   1662   2186  A    C  
ATOM    971  CE1 TYR C 794      61.421  32.207 139.819  1.00 54.27      A    C  
ANISOU  971  CE1 TYR C 794     5356   6526   8738   -381   1326   1907  A    C  
ATOM    972  CE2 TYR C 794      63.109  31.416 138.324  1.00 57.34      A    C  
ANISOU  972  CE2 TYR C 794     5571   7160   9057   -247   1732   2198  A    C  
ATOM    973  CZ  TYR C 794      61.842  31.933 138.541  1.00 54.92      A    C  
ANISOU  973  CZ  TYR C 794     5455   6705   8707   -307   1553   2061  A    C  
ATOM    974  OH  TYR C 794      60.985  32.186 137.485  1.00 51.60      A    O  
ANISOU  974  OH  TYR C 794     5240   6242   8122   -285   1601   2085  A    O  
ATOM    975  N   GLU C 795      65.263  28.293 141.183  1.00 56.34      A    N  
ANISOU  975  N   GLU C 795     4998   7331   9077     61   1738   2027  A    N  
ATOM    976  CA  GLU C 795      65.321  27.200 140.223  1.00 55.67      A    C  
ANISOU  976  CA  GLU C 795     5043   7324   8785    277   1987   2045  A    C  
ATOM    977  C   GLU C 795      64.791  25.901 140.828  1.00 56.29      A    C  
ANISOU  977  C   GLU C 795     5281   7382   8725    430   1954   1851  A    C  
ATOM    978  O   GLU C 795      64.164  25.099 140.143  1.00 54.70      A    O  
ANISOU  978  O   GLU C 795     5329   7155   8301    562   2064   1767  A    O  
ATOM    979  CB  GLU C 795      66.753  27.013 139.719  1.00 57.07      A    C  
ANISOU  979  CB  GLU C 795     4968   7669   9046    361   2215   2273  A    C  
ATOM    980  N   LYS C 796      65.010  25.709 142.122  1.00 57.87      A    N  
ANISOU  980  N   LYS C 796     5353   7587   9050    399   1790   1781  A    N  
ATOM    981  CA  LYS C 796      64.512  24.510 142.791  1.00 56.62      A    C  
ANISOU  981  CA  LYS C 796     5337   7403   8774    530   1745   1611  A    C  
ATOM    982  C   LYS C 796      62.986  24.434 142.784  1.00 52.91      A    C  
ANISOU  982  C   LYS C 796     5163   6800   8139    495   1627   1419  A    C  
ATOM    983  O   LYS C 796      62.418  23.361 142.933  1.00 56.02      A    O  
ANISOU  983  O   LYS C 796     5738   7163   8383    609   1638   1292  A    O  
ATOM    984  CB  LYS C 796      65.034  24.447 144.229  1.00 56.35      A    C  
ANISOU  984  CB  LYS C 796     5100   7405   8907    484   1572   1587  A    C  
ATOM    985  CG  LYS C 796      66.536  24.198 144.314  1.00 57.59      A    C  
ANISOU  985  CG  LYS C 796     4956   7718   9208    558   1689   1776  A    C  
ATOM    986  CD  LYS C 796      67.013  24.264 145.751  1.00 59.98      A    C  
ANISOU  986  CD  LYS C 796     5057   8060   9675    480   1479   1759  A    C  
ATOM    987  CE  LYS C 796      68.475  23.858 145.892  1.00 62.03      A    C  
ANISOU  987  CE  LYS C 796     5004   8492  10072    575   1585   1954  A    C  
ATOM    988  NZ  LYS C 796      68.938  24.120 147.277  1.00 63.61      A    N1+
ANISOU  988  NZ  LYS C 796     4998   8735  10438    456   1342   1950  A    N1+
ATOM    989  N   LEU C 797      62.322  25.568 142.603  1.00 48.60      A    N  
ANISOU  989  N   LEU C 797     4663   6175   7629    337   1514   1409  A    N  
ATOM    990  CA  LEU C 797      60.868  25.600 142.637  1.00 49.20      A    C  
ANISOU  990  CA  LEU C 797     4980   6142   7573    301   1392   1249  A    C  
ATOM    991  C   LEU C 797      60.232  25.097 141.341  1.00 51.01      A    C  
ANISOU  991  C   LEU C 797     5450   6358   7574    386   1536   1242  A    C  
ATOM    992  O   LEU C 797      59.043  24.788 141.321  1.00 53.41      A    O  
ANISOU  992  O   LEU C 797     5960   6595   7738    382   1451   1112  A    O  
ATOM    993  CB  LEU C 797      60.371  27.017 142.932  1.00 50.36      A    C  
ANISOU  993  CB  LEU C 797     5091   6200   7842    122   1220   1246  A    C  
ATOM    994  CG  LEU C 797      60.678  27.565 144.327  1.00 50.28      A    C  
ANISOU  994  CG  LEU C 797     4919   6167   8019     17   1026   1198  A    C  
ATOM    995  CD1 LEU C 797      60.173  28.988 144.421  1.00 49.64      A    C  
ANISOU  995  CD1 LEU C 797     4850   5972   8040   -142    884   1196  A    C  
ATOM    996  CD2 LEU C 797      60.056  26.684 145.415  1.00 44.70      A    C  
ANISOU  996  CD2 LEU C 797     4295   5451   7238     79    914   1023  A    C  
ATOM    997  N   LYS C 798      61.024  25.023 140.272  1.00 52.55      A    N  
ANISOU  997  N   LYS C 798     5616   6625   7727    459   1749   1387  A    N  
ATOM    998  CA  LYS C 798      60.538  24.636 138.940  1.00 52.78      A    C  
ANISOU  998  CA  LYS C 798     5882   6648   7523    536   1894   1394  A    C  
ATOM    999  C   LYS C 798      59.221  25.327 138.616  1.00 51.02      A    C  
ANISOU  999  C   LYS C 798     5827   6335   7222    419   1750   1330  A    C  
ATOM   1000  O   LYS C 798      58.248  24.699 138.189  1.00 51.95      A    O  
ANISOU 1000  O   LYS C 798     6186   6413   7138    456   1731   1226  A    O  
ATOM   1001  CB  LYS C 798      60.391  23.114 138.831  0.83 54.94      A    C  
ANISOU 1001  CB  LYS C 798     6346   6922   7605    706   1990   1284  A    C  
ATOM   1002  CG  LYS C 798      61.664  22.361 139.205  1.00 58.12      A    C  
ANISOU 1002  CG  LYS C 798     6584   7410   8088    853   2134   1349  A    C  
ATOM   1003  CD  LYS C 798      61.869  21.147 138.322  0.68 63.72      A    C  
ANISOU 1003  CD  LYS C 798     7502   8131   8578   1056   2356   1331  A    C  
ATOM   1004  CE  LYS C 798      62.570  21.515 137.014  0.54 67.55      A    C  
ANISOU 1004  CE  LYS C 798     7972   8698   8995   1120   2595   1498  A    C  
ATOM   1005  NZ  LYS C 798      64.067  21.444 137.092  0.93 70.97      A    N1+
ANISOU 1005  NZ  LYS C 798     8127   9264   9577   1237   2782   1670  A    N1+
ATOM   1006  N   THR C 799      59.205  26.632 138.853  1.00 49.37      A    N  
ANISOU 1006  N   THR C 799     5485   6090   7183    275   1640   1400  A    N  
ATOM   1007  CA  THR C 799      58.031  27.448 138.622  1.00 49.43      A    C  
ANISOU 1007  CA  THR C 799     5616   6011   7155    174   1500   1364  A    C  
ATOM   1008  C   THR C 799      58.453  28.770 137.995  1.00 51.70      A    C  
ANISOU 1008  C   THR C 799     5802   6283   7559     71   1532   1540  A    C  
ATOM   1009  O   THR C 799      59.379  29.434 138.468  1.00 55.22      A    O  
ANISOU 1009  O   THR C 799     6030   6736   8214     -3   1523   1635  A    O  
ATOM   1010  CB  THR C 799      57.264  27.707 139.933  1.00 47.89      A    C  
ANISOU 1010  CB  THR C 799     5395   5738   7062    103   1272   1219  A    C  
ATOM   1011  CG2 THR C 799      55.991  28.473 139.662  1.00 44.36      A    C  
ANISOU 1011  CG2 THR C 799     5074   5210   6569     31   1144   1188  A    C  
ATOM   1012  OG1 THR C 799      56.950  26.451 140.551  1.00 52.95      A    O  
ANISOU 1012  OG1 THR C 799     6115   6398   7604    191   1250   1076  A    O  
ATOM   1013  N   ASP C 800      57.791  29.147 136.917  1.00 52.21      A    N  
ANISOU 1013  N   ASP C 800     6024   6328   7487     58   1563   1596  A    N  
ATOM   1014  CA  ASP C 800      58.024  30.468 136.376  1.00 56.60      A    C  
ANISOU 1014  CA  ASP C 800     6506   6846   8155    -50   1567   1763  A    C  
ATOM   1015  C   ASP C 800      57.230  31.490 137.187  1.00 54.14      A    C  
ANISOU 1015  C   ASP C 800     6176   6403   7992   -164   1339   1698  A    C  
ATOM   1016  O   ASP C 800      56.014  31.404 137.294  1.00 53.97      A    O  
ANISOU 1016  O   ASP C 800     6302   6331   7873   -150   1220   1585  A    O  
ATOM   1017  CB  ASP C 800      57.647  30.537 134.907  1.00 62.64      A    C  
ANISOU 1017  CB  ASP C 800     7447   7641   8711    -17   1685   1865  A    C  
ATOM   1018  CG  ASP C 800      57.916  31.901 134.319  1.00 68.09      A    C  
ANISOU 1018  CG  ASP C 800     8065   8290   9518   -128   1698   2060  A    C  
ATOM   1019  OD1 ASP C 800      59.098  32.220 134.114  1.00 70.80      A    O  
ANISOU 1019  OD1 ASP C 800     8236   8688   9976   -155   1832   2220  A    O  
ATOM   1020  OD2 ASP C 800      56.957  32.661 134.083  1.00 72.32      A    O1-
ANISOU 1020  OD2 ASP C 800     8703   8737  10038   -188   1572   2067  A    O1-
ATOM   1021  N   ILE C 801      57.935  32.434 137.791  1.00 51.26      A    N  
ANISOU 1021  N   ILE C 801     5629   5983   7864   -274   1279   1770  A    N  
ATOM   1022  CA  ILE C 801      57.299  33.464 138.592  1.00 46.64      A    C  
ANISOU 1022  CA  ILE C 801     5040   5253   7427   -373   1074   1705  A    C  
ATOM   1023  C   ILE C 801      57.564  34.811 137.966  1.00 53.86      A    C  
ANISOU 1023  C   ILE C 801     5920   6081   8464   -488   1078   1886  A    C  
ATOM   1024  O   ILE C 801      58.722  35.218 137.871  1.00 54.37      A    O  
ANISOU 1024  O   ILE C 801     5818   6169   8671   -569   1151   2031  A    O  
ATOM   1025  CB  ILE C 801      57.835  33.470 140.036  1.00 46.66      A    C  
ANISOU 1025  CB  ILE C 801     4891   5230   7608   -424    955   1604  A    C  
ATOM   1026  CG1 ILE C 801      57.767  32.065 140.649  1.00 47.00      A    C  
ANISOU 1026  CG1 ILE C 801     4950   5370   7538   -307    972   1455  A    C  
ATOM   1027  CG2 ILE C 801      57.093  34.493 140.880  1.00 43.68      A    C  
ANISOU 1027  CG2 ILE C 801     4554   4692   7352   -504    749   1511  A    C  
ATOM   1028  CD1 ILE C 801      58.226  32.002 142.082  1.00 44.97      A    C  
ANISOU 1028  CD1 ILE C 801     4559   5100   7427   -347    845   1355  A    C  
ATOM   1029  N   LYS C 802      56.513  35.506 137.534  1.00 53.72      A    N  
ANISOU 1029  N   LYS C 802     6046   5965   8398   -498   1000   1894  A    N  
ATOM   1030  CA  LYS C 802      56.696  36.839 136.957  1.00 56.37      A    C  
ANISOU 1030  CA  LYS C 802     6369   6192   8856   -606    993   2073  A    C  
ATOM   1031  C   LYS C 802      55.928  37.850 137.784  1.00 57.30      A    C  
ANISOU 1031  C   LYS C 802     6535   6122   9115   -661    789   1984  A    C  
ATOM   1032  O   LYS C 802      54.904  37.520 138.380  1.00 56.90      A    O  
ANISOU 1032  O   LYS C 802     6575   6050   8994   -584    682   1813  A    O  
ATOM   1033  CB  LYS C 802      56.241  36.891 135.496  1.00 52.99      A    C  
ANISOU 1033  CB  LYS C 802     6080   5812   8242   -559   1105   2213  A    C  
ATOM   1034  N   VAL C 803      56.434  39.075 137.843  1.00 54.55      A    N  
ANISOU 1034  N   VAL C 803     6127   5633   8967   -793    740   2103  A    N  
ATOM   1035  CA  VAL C 803      55.732  40.136 138.544  1.00 54.33      A    C  
ANISOU 1035  CA  VAL C 803     6176   5397   9071   -835    559   2027  A    C  
ATOM   1036  C   VAL C 803      54.600  40.635 137.644  1.00 54.76      A    C  
ANISOU 1036  C   VAL C 803     6395   5391   9020   -766    552   2099  A    C  
ATOM   1037  O   VAL C 803      54.828  40.917 136.470  1.00 54.78      A    O  
ANISOU 1037  O   VAL C 803     6419   5424   8971   -790    660   2296  A    O  
ATOM   1038  CB  VAL C 803      56.687  41.297 138.915  1.00 60.55      A    C  
ANISOU 1038  CB  VAL C 803     6866   6026  10114  -1016    495   2129  A    C  
ATOM   1039  CG1 VAL C 803      55.917  42.468 139.502  1.00 60.91      A    C  
ANISOU 1039  CG1 VAL C 803     7038   5823  10281  -1043    321   2056  A    C  
ATOM   1040  CG2 VAL C 803      57.756  40.821 139.880  1.00 60.45      A    C  
ANISOU 1040  CG2 VAL C 803     6678   6082  10208  -1091    471   2058  A    C  
ATOM   1041  N   VAL C 804      53.378  40.712 138.168  1.00 54.01      A    N  
ANISOU 1041  N   VAL C 804     6409   5229   8883   -672    430   1953  A    N  
ATOM   1042  CA  VAL C 804      52.281  41.316 137.404  1.00 51.85      A    C  
ANISOU 1042  CA  VAL C 804     6272   4890   8539   -606    399   2036  A    C  
ATOM   1043  C   VAL C 804      52.330  42.829 137.573  1.00 53.99      A    C  
ANISOU 1043  C   VAL C 804     6581   4914   9020   -684    309   2120  A    C  
ATOM   1044  O   VAL C 804      52.406  43.319 138.696  1.00 57.90      A    O  
ANISOU 1044  O   VAL C 804     7068   5264   9668   -718    196   1992  A    O  
ATOM   1045  CB  VAL C 804      50.897  40.786 137.841  1.00 49.03      A    C  
ANISOU 1045  CB  VAL C 804     5997   4578   8054   -464    312   1872  A    C  
ATOM   1046  CG1 VAL C 804      49.771  41.647 137.243  1.00 47.97      A    C  
ANISOU 1046  CG1 VAL C 804     5978   4348   7902   -396    248   1967  A    C  
ATOM   1047  CG2 VAL C 804      50.727  39.324 137.440  1.00 44.44      A    C  
ANISOU 1047  CG2 VAL C 804     5417   4221   7246   -398    395   1817  A    C  
ATOM   1048  N   ASP C 805      52.307  43.567 136.465  1.00 54.71      A    N  
ANISOU 1048  N   ASP C 805     6728   4948   9110   -715    358   2335  A    N  
ATOM   1049  CA  ASP C 805      52.358  45.033 136.522  1.00 58.78      A    C  
ANISOU 1049  CA  ASP C 805     7301   5205   9827   -793    277   2439  A    C  
ATOM   1050  C   ASP C 805      51.124  45.569 137.243  1.00 59.62      A    C  
ANISOU 1050  C   ASP C 805     7525   5158   9972   -671    134   2299  A    C  
ATOM   1051  O   ASP C 805      49.985  45.223 136.892  1.00 57.81      A    O  
ANISOU 1051  O   ASP C 805     7360   5014   9589   -525    122   2280  A    O  
ATOM   1052  CB  ASP C 805      52.471  45.628 135.105  1.00 60.90      A    C  
ANISOU 1052  CB  ASP C 805     7618   5462  10059   -832    366   2715  A    C  
ATOM   1053  CG  ASP C 805      52.884  47.095 135.102  0.73 66.41      A    C  
ANISOU 1053  CG  ASP C 805     8355   5890  10989   -959    307   2860  A    C  
ATOM   1054  OD1 ASP C 805      52.173  47.936 135.696  0.75 68.29      A    O  
ANISOU 1054  OD1 ASP C 805     8701   5907  11339   -911    174   2785  A    O  
ATOM   1055  OD2 ASP C 805      53.927  47.411 134.491  0.35 68.91      A    O1-
ANISOU 1055  OD2 ASP C 805     8597   6209  11376  -1106    399   3057  A    O1-
ATOM   1056  N   ARG C 806      51.355  46.398 138.260  1.00 59.81      A    N  
ANISOU 1056  N   ARG C 806     7574   4959  10193   -730     24   2204  A    N  
ATOM   1057  CA  ARG C 806      50.273  46.933 139.085  1.00 64.02      A    C  
ANISOU 1057  CA  ARG C 806     8223   5334  10770   -598    -97   2053  A    C  
ATOM   1058  C   ARG C 806      49.235  47.715 138.272  1.00 67.40      A    C  
ANISOU 1058  C   ARG C 806     8773   5660  11175   -482   -113   2197  A    C  
ATOM   1059  O   ARG C 806      48.102  47.892 138.718  1.00 67.65      A    O  
ANISOU 1059  O   ARG C 806     8879   5642  11183   -316   -180   2097  A    O  
ATOM   1060  CB  ARG C 806      50.841  47.826 140.191  1.00 66.22      A    C  
ANISOU 1060  CB  ARG C 806     8543   5356  11261   -702   -208   1945  A    C  
ATOM   1061  N   ASP C 807      49.611  48.157 137.076  1.00 71.00      A    N  
ANISOU 1061  N   ASP C 807     9241   6102  11635   -558    -45   2443  A    N  
ATOM   1062  CA  ASP C 807      48.714  48.954 136.235  1.00 76.51      A    C  
ANISOU 1062  CA  ASP C 807    10054   6701  12317   -457    -64   2613  A    C  
ATOM   1063  C   ASP C 807      47.951  48.155 135.180  1.00 73.97      A    C  
ANISOU 1063  C   ASP C 807     9720   6633  11753   -350     -3   2710  A    C  
ATOM   1064  O   ASP C 807      47.186  48.727 134.404  1.00 77.30      A    O  
ANISOU 1064  O   ASP C 807    10223   7009  12137   -263    -25   2868  A    O  
ATOM   1065  CB  ASP C 807      49.498  50.057 135.533  1.00 83.08      A    C  
ANISOU 1065  CB  ASP C 807    10931   7338  13297   -607    -41   2850  A    C  
ATOM   1066  CG  ASP C 807      50.221  50.958 136.502  1.00 90.06      A    C  
ANISOU 1066  CG  ASP C 807    11851   7940  14429   -739   -126   2772  A    C  
ATOM   1067  OD1 ASP C 807      49.607  51.348 137.520  1.00 92.61      A    O  
ANISOU 1067  OD1 ASP C 807    12264   8097  14828   -639   -232   2585  A    O  
ATOM   1068  OD2 ASP C 807      51.401  51.279 136.245  1.00 93.03      A    O1-
ANISOU 1068  OD2 ASP C 807    12168   8261  14917   -945    -88   2901  A    O1-
ATOM   1069  N   SER C 808      48.159  46.845 135.152  1.00 67.18      A    N  
ANISOU 1069  N   SER C 808     8768   6030  10725   -357     63   2617  A    N  
ATOM   1070  CA  SER C 808      47.533  45.987 134.153  1.00 63.64      A    C  
ANISOU 1070  CA  SER C 808     8328   5823  10030   -283    113   2691  A    C  
ATOM   1071  C   SER C 808      46.058  45.763 134.457  1.00 61.79      A    C  
ANISOU 1071  C   SER C 808     8125   5643   9710   -109     15   2595  A    C  
ATOM   1072  O   SER C 808      45.603  46.033 135.563  1.00 61.18      A    O  
ANISOU 1072  O   SER C 808     8045   5456   9745    -34    -64   2436  A    O  
ATOM   1073  CB  SER C 808      48.245  44.641 134.101  1.00 61.56      A    C  
ANISOU 1073  CB  SER C 808     7979   5789   9622   -341    214   2605  A    C  
ATOM   1074  OG  SER C 808      48.202  44.024 135.380  1.00 58.05      A    O  
ANISOU 1074  OG  SER C 808     7472   5367   9217   -313    166   2361  A    O  
ATOM   1075  N   GLU C 809      45.318  45.248 133.483  1.00 61.61      A    N  
ANISOU 1075  N   GLU C 809     8129   5800   9481    -48     19   2695  A    N  
ATOM   1076  CA  GLU C 809      43.929  44.879 133.711  1.00 62.49      A    C  
ANISOU 1076  CA  GLU C 809     8236   6010   9497     98    -75   2623  A    C  
ATOM   1077  C   GLU C 809      43.895  43.751 134.734  1.00 58.27      A    C  
ANISOU 1077  C   GLU C 809     7626   5601   8915    107    -78   2378  A    C  
ATOM   1078  O   GLU C 809      43.058  43.743 135.638  1.00 56.08      A    O  
ANISOU 1078  O   GLU C 809     7317   5308   8683    214   -153   2248  A    O  
ATOM   1079  CB  GLU C 809      43.250  44.451 132.409  1.00 67.52      A    C  
ANISOU 1079  CB  GLU C 809     8916   6835   9905    125    -84   2784  A    C  
ATOM   1080  CG  GLU C 809      42.156  45.402 131.927  1.00 76.32      A    C  
ANISOU 1080  CG  GLU C 809    10075   7876  11046    245   -180   2952  A    C  
ATOM   1081  CD  GLU C 809      40.857  45.259 132.706  1.00 79.49      A    C  
ANISOU 1081  CD  GLU C 809    10417   8322  11464    398   -287   2841  A    C  
ATOM   1082  OE1 GLU C 809      40.249  44.166 132.670  1.00 75.97      A    O  
ANISOU 1082  OE1 GLU C 809     9923   8098  10846    408   -321   2765  A    O  
ATOM   1083  OE2 GLU C 809      40.443  46.248 133.350  1.00 82.99      A    O1-
ANISOU 1083  OE2 GLU C 809    10866   8573  12091    509   -334   2836  A    O1-
ATOM   1084  N   GLU C 810      44.816  42.804 134.553  1.00 57.54      A    N  
ANISOU 1084  N   GLU C 810     7503   5634   8725      2     15   2329  A    N  
ATOM   1085  CA  GLU C 810      45.086  41.703 135.486  1.00 56.03      A    C  
ANISOU 1085  CA  GLU C 810     7244   5546   8499    -12     32   2114  A    C  
ATOM   1086  C   GLU C 810      45.108  42.135 136.946  1.00 49.99      A    C  
ANISOU 1086  C   GLU C 810     6436   4636   7922     21    -27   1944  A    C  
ATOM   1087  O   GLU C 810      44.359  41.623 137.777  1.00 49.77      A    O  
ANISOU 1087  O   GLU C 810     6376   4672   7863    102    -82   1793  A    O  
ATOM   1088  CB  GLU C 810      46.435  41.061 135.147  1.00 62.69      A    C  
ANISOU 1088  CB  GLU C 810     8060   6461   9296   -130    159   2124  A    C  
ATOM   1089  CG  GLU C 810      46.378  39.706 134.465  1.00 68.37      A    C  
ANISOU 1089  CG  GLU C 810     8807   7402   9768   -133    222   2104  A    C  
ATOM   1090  CD  GLU C 810      47.761  39.234 134.010  1.00 73.75      A    C  
ANISOU 1090  CD  GLU C 810     9468   8141  10414   -220    374   2149  A    C  
ATOM   1091  OE1 GLU C 810      48.011  38.004 134.008  1.00 72.43      A    O  
ANISOU 1091  OE1 GLU C 810     9303   8116  10103   -216    437   2051  A    O  
ATOM   1092  OE2 GLU C 810      48.595  40.101 133.648  1.00 77.20      A    O1-
ANISOU 1092  OE2 GLU C 810     9884   8477  10970   -289    436   2292  A    O1-
ATOM   1093  N   ALA C 811      45.997  43.067 137.258  1.00 50.29      A    N  
ANISOU 1093  N   ALA C 811     6479   4480   8148    -54    -16   1971  A    N  
ATOM   1094  CA  ALA C 811      46.156  43.531 138.631  1.00 53.22      A    C  
ANISOU 1094  CA  ALA C 811     6838   4694   8689    -42    -78   1803  A    C  
ATOM   1095  C   ALA C 811      44.860  44.185 139.133  1.00 53.72      A    C  
ANISOU 1095  C   ALA C 811     6954   4661   8796    121   -169   1758  A    C  
ATOM   1096  O   ALA C 811      44.449  43.971 140.273  1.00 50.62      A    O  
ANISOU 1096  O   ALA C 811     6544   4264   8424    196   -212   1576  A    O  
ATOM   1097  CB  ALA C 811      47.340  44.502 138.732  1.00 48.60      A    C  
ANISOU 1097  CB  ALA C 811     6265   3904   8298   -178    -68   1867  A    C  
ATOM   1098  N   GLU C 812      44.210  44.951 138.259  1.00 55.26      A    N  
ANISOU 1098  N   GLU C 812     7210   4792   8993    186   -188   1935  A    N  
ATOM   1099  CA  GLU C 812      42.926  45.592 138.564  1.00 57.84      A    C  
ANISOU 1099  CA  GLU C 812     7576   5044   9358    367   -261   1933  A    C  
ATOM   1100  C   GLU C 812      41.843  44.605 138.966  1.00 51.65      A    C  
ANISOU 1100  C   GLU C 812     6715   4478   8431    482   -287   1827  A    C  
ATOM   1101  O   GLU C 812      41.173  44.790 139.984  1.00 51.63      A    O  
ANISOU 1101  O   GLU C 812     6703   4429   8483    610   -324   1698  A    O  
ATOM   1102  CB  GLU C 812      42.429  46.396 137.356  1.00 63.05      A    C  
ANISOU 1102  CB  GLU C 812     8296   5648  10013    415   -275   2178  A    C  
ATOM   1103  CG  GLU C 812      42.372  47.898 137.555  1.00 72.36      A    C  
ANISOU 1103  CG  GLU C 812     9581   6520  11394    477   -315   2245  A    C  
ATOM   1104  CD  GLU C 812      41.823  48.616 136.327  1.00 79.59      A    C  
ANISOU 1104  CD  GLU C 812    10552   7398  12292    536   -331   2507  A    C  
ATOM   1105  OE1 GLU C 812      40.692  48.299 135.895  1.00 81.36      A    O  
ANISOU 1105  OE1 GLU C 812    10734   7786  12394    667   -367   2577  A    O  
ATOM   1106  OE2 GLU C 812      42.535  49.483 135.781  1.00 85.21      A    O1-
ANISOU 1106  OE2 GLU C 812    11343   7925  13109    442   -312   2655  A    O1-
ATOM   1107  N   ILE C 813      41.645  43.586 138.136  1.00 48.49      A    N  
ANISOU 1107  N   ILE C 813     6270   4310   7844    437   -266   1892  A    N  
ATOM   1108  CA  ILE C 813      40.673  42.528 138.424  1.00 48.12      A    C  
ANISOU 1108  CA  ILE C 813     6148   4483   7653    505   -299   1808  A    C  
ATOM   1109  C   ILE C 813      40.980  41.854 139.759  1.00 47.90      A    C  
ANISOU 1109  C   ILE C 813     6071   4481   7649    496   -284   1578  A    C  
ATOM   1110  O   ILE C 813      40.094  41.654 140.597  1.00 47.75      A    O  
ANISOU 1110  O   ILE C 813     6001   4517   7624    609   -319   1479  A    O  
ATOM   1111  CB  ILE C 813      40.657  41.454 137.308  1.00 50.64      A    C  
ANISOU 1111  CB  ILE C 813     6461   5022   7757    415   -281   1894  A    C  
ATOM   1112  CG1 ILE C 813      40.126  42.052 135.996  1.00 56.53      A    C  
ANISOU 1112  CG1 ILE C 813     7256   5779   8443    441   -316   2128  A    C  
ATOM   1113  CG2 ILE C 813      39.845  40.228 137.743  1.00 47.28      A    C  
ANISOU 1113  CG2 ILE C 813     5964   4807   7194    440   -318   1782  A    C  
ATOM   1114  CD1 ILE C 813      40.053  41.070 134.849  1.00 57.19      A    C  
ANISOU 1114  CD1 ILE C 813     7368   6070   8292    356   -312   2211  A    C  
ATOM   1115  N   ILE C 814      42.247  41.516 139.956  1.00 48.20      A    N  
ANISOU 1115  N   ILE C 814     6115   4489   7711    364   -228   1508  A    N  
ATOM   1116  CA  ILE C 814      42.648  40.792 141.150  1.00 46.20      A    C  
ANISOU 1116  CA  ILE C 814     5815   4276   7464    341   -218   1306  A    C  
ATOM   1117  C   ILE C 814      42.484  41.661 142.400  1.00 48.14      A    C  
ANISOU 1117  C   ILE C 814     6086   4345   7862    429   -261   1180  A    C  
ATOM   1118  O   ILE C 814      42.017  41.184 143.430  1.00 47.40      A    O  
ANISOU 1118  O   ILE C 814     5955   4316   7737    500   -278   1030  A    O  
ATOM   1119  CB  ILE C 814      44.079  40.274 140.995  1.00 48.10      A    C  
ANISOU 1119  CB  ILE C 814     6042   4531   7703    189   -150   1288  A    C  
ATOM   1120  CG1 ILE C 814      44.069  39.133 139.975  1.00 47.85      A    C  
ANISOU 1120  CG1 ILE C 814     6002   4700   7476    140    -98   1359  A    C  
ATOM   1121  CG2 ILE C 814      44.611  39.749 142.310  1.00 49.13      A    C  
ANISOU 1121  CG2 ILE C 814     6128   4667   7873    167   -155   1093  A    C  
ATOM   1122  CD1 ILE C 814      45.430  38.602 139.592  1.00 50.00      A    C  
ANISOU 1122  CD1 ILE C 814     6263   5008   7729     20     -4   1377  A    C  
ATOM   1123  N   ARG C 815      42.822  42.944 142.307  1.00 50.15      A    N  
ANISOU 1123  N   ARG C 815     6416   4369   8268    428   -279   1242  A    N  
ATOM   1124  CA  ARG C 815      42.590  43.847 143.429  1.00 52.47      A    C  
ANISOU 1124  CA  ARG C 815     6776   4468   8693    525   -323   1118  A    C  
ATOM   1125  C   ARG C 815      41.099  44.003 143.722  1.00 54.85      A    C  
ANISOU 1125  C   ARG C 815     7067   4819   8956    737   -345   1109  A    C  
ATOM   1126  O   ARG C 815      40.709  44.137 144.876  1.00 55.92      A    O  
ANISOU 1126  O   ARG C 815     7220   4911   9117    845   -358    954  A    O  
ATOM   1127  CB  ARG C 815      43.209  45.223 143.170  1.00 56.29      A    C  
ANISOU 1127  CB  ARG C 815     7368   4669   9350    474   -346   1201  A    C  
ATOM   1128  CG  ARG C 815      44.731  45.254 143.283  1.00 57.72      A    C  
ANISOU 1128  CG  ARG C 815     7548   4768   9616    266   -338   1179  A    C  
ATOM   1129  CD  ARG C 815      45.223  46.687 143.408  1.00 62.07      A    C  
ANISOU 1129  CD  ARG C 815     8222   5003  10360    218   -387   1216  A    C  
ATOM   1130  NE  ARG C 815      44.810  47.507 142.273  1.00 65.90      A    N  
ANISOU 1130  NE  ARG C 815     8766   5390  10883    258   -377   1432  A    N  
ATOM   1131  CZ  ARG C 815      45.533  47.670 141.168  1.00 67.06      A    C  
ANISOU 1131  CZ  ARG C 815     8895   5535  11049    118   -336   1628  A    C  
ATOM   1132  NH1 ARG C 815      46.712  47.070 141.043  1.00 64.96      A    N1+
ANISOU 1132  NH1 ARG C 815     8543   5364  10773    -63   -292   1634  A    N1+
ATOM   1133  NH2 ARG C 815      45.077  48.436 140.190  1.00 68.37      A    N  
ANISOU 1133  NH2 ARG C 815     9125   5611  11240    169   -333   1828  A    N  
ATOM   1134  N   LYS C 816      40.271  43.991 142.681  1.00 52.48      A    N  
ANISOU 1134  N   LYS C 816     6733   4620   8588    798   -349   1284  A    N  
ATOM   1135  CA  LYS C 816      38.823  44.074 142.873  1.00 53.55      A    C  
ANISOU 1135  CA  LYS C 816     6819   4840   8686    997   -370   1309  A    C  
ATOM   1136  C   LYS C 816      38.306  42.820 143.572  1.00 49.95      A    C  
ANISOU 1136  C   LYS C 816     6252   4624   8101   1015   -362   1186  A    C  
ATOM   1137  O   LYS C 816      37.508  42.897 144.512  1.00 49.33      A    O  
ANISOU 1137  O   LYS C 816     6141   4567   8033   1169   -359   1094  A    O  
ATOM   1138  CB  LYS C 816      38.098  44.260 141.540  1.00 57.27      A    C  
ANISOU 1138  CB  LYS C 816     7264   5394   9103   1035   -396   1542  A    C  
ATOM   1139  CG  LYS C 816      36.590  44.526 141.678  1.00 62.21      A    C  
ANISOU 1139  CG  LYS C 816     7818   6098   9720   1254   -426   1608  A    C  
ATOM   1140  CD  LYS C 816      35.962  44.951 140.344  1.00 64.95      A    C  
ANISOU 1140  CD  LYS C 816     8152   6487  10037   1293   -471   1860  A    C  
ATOM   1141  CE  LYS C 816      34.487  45.312 140.501  1.00 67.38      A    C  
ANISOU 1141  CE  LYS C 816     8368   6871  10361   1526   -504   1947  A    C  
ATOM   1142  NZ  LYS C 816      33.842  45.646 139.196  1.00 66.98      A    N1+
ANISOU 1142  NZ  LYS C 816     8289   6890  10268   1560   -566   2206  A    N1+
ATOM   1143  N   TYR C 817      38.760  41.666 143.102  1.00 47.48      A    N  
ANISOU 1143  N   TYR C 817     5889   4485   7665    864   -350   1190  A    N  
ATOM   1144  CA  TYR C 817      38.399  40.397 143.717  1.00 44.32      A    C  
ANISOU 1144  CA  TYR C 817     5401   4295   7144    850   -344   1081  A    C  
ATOM   1145  C   TYR C 817      38.774  40.446 145.209  1.00 46.84      A    C  
ANISOU 1145  C   TYR C 817     5739   4533   7526    888   -324    874  A    C  
ATOM   1146  O   TYR C 817      37.967  40.120 146.069  1.00 45.85      A    O  
ANISOU 1146  O   TYR C 817     5556   4505   7362    997   -321    794  A    O  
ATOM   1147  CB  TYR C 817      39.086  39.249 142.951  1.00 41.98      A    C  
ANISOU 1147  CB  TYR C 817     5094   4136   6719    674   -326   1107  A    C  
ATOM   1148  CG  TYR C 817      38.556  37.829 143.177  1.00 40.89      A    C  
ANISOU 1148  CG  TYR C 817     4880   4228   6430    640   -334   1051  A    C  
ATOM   1149  CD1 TYR C 817      37.461  37.570 143.996  1.00 41.13      A    C  
ANISOU 1149  CD1 TYR C 817     4825   4363   6438    750   -357   1001  A    C  
ATOM   1150  CD2 TYR C 817      39.121  36.758 142.491  1.00 40.98      A    C  
ANISOU 1150  CD2 TYR C 817     4911   4345   6314    499   -315   1064  A    C  
ATOM   1151  CE1 TYR C 817      36.977  36.271 144.153  1.00 39.63      A    C  
ANISOU 1151  CE1 TYR C 817     4568   4374   6116    695   -371    970  A    C  
ATOM   1152  CE2 TYR C 817      38.662  35.459 142.658  1.00 40.97      A    C  
ANISOU 1152  CE2 TYR C 817     4866   4523   6176    455   -330   1015  A    C  
ATOM   1153  CZ  TYR C 817      37.592  35.217 143.482  1.00 41.49      A    C  
ANISOU 1153  CZ  TYR C 817     4843   4687   6233    541   -364    973  A    C  
ATOM   1154  OH  TYR C 817      37.141  33.918 143.623  1.00 39.05      A    O  
ANISOU 1154  OH  TYR C 817     4494   4548   5795    475   -385    940  A    O  
ATOM   1155  N   VAL C 818      39.978  40.906 145.519  1.00 50.25      A    N  
ANISOU 1155  N   VAL C 818     6250   4790   8052    798   -316    800  A    N  
ATOM   1156  CA  VAL C 818      40.386  41.037 146.918  1.00 53.34      A    C  
ANISOU 1156  CA  VAL C 818     6679   5093   8495    822   -318    605  A    C  
ATOM   1157  C   VAL C 818      39.516  42.030 147.699  1.00 56.75      A    C  
ANISOU 1157  C   VAL C 818     7168   5398   8995   1022   -326    547  A    C  
ATOM   1158  O   VAL C 818      38.942  41.686 148.730  1.00 55.98      A    O  
ANISOU 1158  O   VAL C 818     7043   5381   8844   1128   -310    426  A    O  
ATOM   1159  CB  VAL C 818      41.863  41.478 147.046  1.00 52.42      A    C  
ANISOU 1159  CB  VAL C 818     6634   4800   8483    671   -331    557  A    C  
ATOM   1160  CG1 VAL C 818      42.183  41.863 148.476  1.00 52.27      A    C  
ANISOU 1160  CG1 VAL C 818     6683   4656   8521    704   -361    362  A    C  
ATOM   1161  CG2 VAL C 818      42.770  40.371 146.593  1.00 46.81      A    C  
ANISOU 1161  CG2 VAL C 818     5856   4233   7698    507   -302    578  A    C  
ATOM   1162  N   LYS C 819      39.419  43.258 147.205  1.00 57.61      A    N  
ANISOU 1162  N   LYS C 819     7365   5305   9219   1084   -342    639  A    N  
ATOM   1163  CA  LYS C 819      38.662  44.300 147.897  1.00 58.70      A    C  
ANISOU 1163  CA  LYS C 819     7587   5284   9432   1294   -339    584  A    C  
ATOM   1164  C   LYS C 819      37.215  43.896 148.175  1.00 59.90      A    C  
ANISOU 1164  C   LYS C 819     7627   5635   9496   1493   -304    608  A    C  
ATOM   1165  O   LYS C 819      36.731  44.018 149.302  1.00 62.56      A    O  
ANISOU 1165  O   LYS C 819     7986   5965   9819   1642   -273    473  A    O  
ATOM   1166  CB  LYS C 819      38.677  45.595 147.083  1.00 60.83      A    C  
ANISOU 1166  CB  LYS C 819     7961   5319   9834   1333   -360    726  A    C  
ATOM   1167  N   ASN C 820      36.536  43.408 147.142  1.00 58.92      A    N  
ANISOU 1167  N   ASN C 820     7382   5698   9307   1488   -311    787  A    N  
ATOM   1168  CA  ASN C 820      35.108  43.093 147.211  1.00 58.03      A    C  
ANISOU 1168  CA  ASN C 820     7133   5787   9129   1660   -294    862  A    C  
ATOM   1169  C   ASN C 820      34.761  41.902 148.103  1.00 60.38      A    C  
ANISOU 1169  C   ASN C 820     7321   6315   9307   1650   -265    749  A    C  
ATOM   1170  O   ASN C 820      33.718  41.891 148.757  1.00 62.60      A    O  
ANISOU 1170  O   ASN C 820     7521   6701   9564   1829   -226    739  A    O  
ATOM   1171  CB  ASN C 820      34.575  42.826 145.807  1.00 57.18      A    C  
ANISOU 1171  CB  ASN C 820     6930   5825   8972   1612   -337   1089  A    C  
ATOM   1172  CG  ASN C 820      34.167  44.089 145.087  1.00 61.91      A    C  
ANISOU 1172  CG  ASN C 820     7585   6260   9678   1745   -355   1249  A    C  
ATOM   1173  ND2 ASN C 820      33.468  43.932 143.968  1.00 62.51      A    N  
ANISOU 1173  ND2 ASN C 820     7566   6482   9702   1747   -401   1458  A    N  
ATOM   1174  OD1 ASN C 820      34.480  45.191 145.523  1.00 65.90      A    O  
ANISOU 1174  OD1 ASN C 820     8228   6504  10308   1841   -336   1189  A    O  
ATOM   1175  N   THR C 821      35.616  40.884 148.110  1.00 58.69      A    N  
ANISOU 1175  N   THR C 821     7182   6393   8725   1564    324    313  A    N  
ATOM   1176  CA  THR C 821      35.314  39.694 148.894  1.00 59.69      A    C  
ANISOU 1176  CA  THR C 821     7283   6751   8645   1508    329    188  A    C  
ATOM   1177  C   THR C 821      36.070  39.719 150.218  1.00 66.54      A    C  
ANISOU 1177  C   THR C 821     8338   7514   9430   1431    372    -98  A    C  
ATOM   1178  O   THR C 821      36.248  38.688 150.872  1.00 64.90      A    O  
ANISOU 1178  O   THR C 821     8152   7478   9029   1330    342   -207  A    O  
ATOM   1179  CB  THR C 821      35.641  38.389 148.130  1.00 49.82      A    C  
ANISOU 1179  CB  THR C 821     5965   5755   7208   1339    192    291  A    C  
ATOM   1180  CG2 THR C 821      34.977  38.368 146.755  1.00 46.34      A    C  
ANISOU 1180  CG2 THR C 821     5377   5426   6804   1372    118    569  A    C  
ATOM   1181  OG1 THR C 821      37.061  38.243 147.990  1.00 51.10      A    O  
ANISOU 1181  OG1 THR C 821     6248   5845   7322   1173    118    224  A    O  
ATOM   1182  N   HIS C 822      36.510  40.906 150.613  1.00 73.11      A    N  
ANISOU 1182  N   HIS C 822     9315   8057  10407   1468    432   -212  A    N  
ATOM   1183  CA  HIS C 822      37.107  41.079 151.928  1.00 78.66      A    C  
ANISOU 1183  CA  HIS C 822    10220   8646  11023   1392    466   -493  A    C  
ATOM   1184  C   HIS C 822      36.020  41.250 152.989  1.00 81.19      A    C  
ANISOU 1184  C   HIS C 822    10580   8958  11310   1556    654   -635  A    C  
ATOM   1185  O   HIS C 822      35.437  42.326 153.129  1.00 84.87      A    O  
ANISOU 1185  O   HIS C 822    11088   9202  11955   1729    808   -660  A    O  
ATOM   1186  CB  HIS C 822      38.051  42.278 151.942  1.00 83.89      A    C  
ANISOU 1186  CB  HIS C 822    11045   8985  11843   1330    447   -577  A    C  
ATOM   1187  CG  HIS C 822      38.591  42.593 153.300  1.00 89.59      A    C  
ANISOU 1187  CG  HIS C 822    11999   9571  12471   1237    467   -874  A    C  
ATOM   1188  CD2 HIS C 822      38.756  43.773 153.944  1.00 94.02      A    C  
ANISOU 1188  CD2 HIS C 822    12767   9821  13137   1257    553  -1060  A    C  
ATOM   1189  ND1 HIS C 822      39.006  41.613 154.177  1.00 89.58      A    N  
ANISOU 1189  ND1 HIS C 822    12053   9760  12223   1097    389  -1012  A    N  
ATOM   1190  CE1 HIS C 822      39.418  42.178 155.298  1.00 93.03      A    C  
ANISOU 1190  CE1 HIS C 822    12722  10030  12596   1022    407  -1265  A    C  
ATOM   1191  NE2 HIS C 822      39.275  43.487 155.183  1.00 96.00      A    N  
ANISOU 1191  NE2 HIS C 822    13205  10094  13178   1110    510  -1314  A    N  
ATOM   1192  N   ALA C 828      38.283  42.037 161.030  1.00103.25      A    N  
ANISOU 1192  N   ALA C 828    14945  11355  12931    959    806  -2308  A    N  
ATOM   1193  CA  ALA C 828      39.208  42.519 162.050  1.00105.44      A    C  
ANISOU 1193  CA  ALA C 828    15547  11489  13027    735    690  -2573  A    C  
ATOM   1194  C   ALA C 828      40.436  43.159 161.399  1.00105.70      A    C  
ANISOU 1194  C   ALA C 828    15576  11327  13258    552    458  -2534  A    C  
ATOM   1195  O   ALA C 828      40.780  44.306 161.690  1.00108.32      A    O  
ANISOU 1195  O   ALA C 828    16143  11345  13668    487    480  -2722  A    O  
ATOM   1196  CB  ALA C 828      39.613  41.380 162.974  1.00103.99      A    C  
ANISOU 1196  CB  ALA C 828    15424  11596  12492    559    539  -2618  A    C  
ATOM   1197  N   TYR C 829      41.094  42.406 160.521  1.00102.60      A    N  
ANISOU 1197  N   TYR C 829    14920  11112  12951    465    252  -2290  A    N  
ATOM   1198  CA  TYR C 829      42.148  42.947 159.668  1.00 99.64      A    C  
ANISOU 1198  CA  TYR C 829    14468  10575  12814    330     75  -2185  A    C  
ATOM   1199  C   TYR C 829      41.521  43.599 158.446  1.00 96.52      A    C  
ANISOU 1199  C   TYR C 829    13919  10027  12729    541    228  -2011  A    C  
ATOM   1200  O   TYR C 829      40.394  43.274 158.075  1.00 96.44      A    O  
ANISOU 1200  O   TYR C 829    13768  10129  12745    767    401  -1897  A    O  
ATOM   1201  CB  TYR C 829      43.114  41.844 159.224  1.00 96.76      A    C  
ANISOU 1201  CB  TYR C 829    13887  10462  12416    167   -171  -1988  A    C  
ATOM   1202  CG  TYR C 829      42.430  40.728 158.461  1.00 93.85      A    C  
ANISOU 1202  CG  TYR C 829    13253  10362  12043    322   -103  -1757  A    C  
ATOM   1203  CD1 TYR C 829      42.185  40.832 157.093  1.00 93.18      A    C  
ANISOU 1203  CD1 TYR C 829    12960  10254  12190    441    -52  -1533  A    C  
ATOM   1204  CD2 TYR C 829      42.010  39.579 159.113  1.00 93.07      A    C  
ANISOU 1204  CD2 TYR C 829    13132  10535  11695    335    -94  -1762  A    C  
ATOM   1205  CE1 TYR C 829      41.545  39.816 156.399  1.00 90.27      A    C  
ANISOU 1205  CE1 TYR C 829    12378  10126  11795    552     -6  -1339  A    C  
ATOM   1206  CE2 TYR C 829      41.374  38.560 158.432  1.00 91.20      A    C  
ANISOU 1206  CE2 TYR C 829    12671  10524  11458    451    -38  -1564  A    C  
ATOM   1207  CZ  TYR C 829      41.142  38.682 157.078  1.00 90.67      A    C  
ANISOU 1207  CZ  TYR C 829    12410  10428  11612    553      0  -1363  A    C  
ATOM   1208  OH  TYR C 829      40.504  37.660 156.410  1.00 89.97      A    O  
ANISOU 1208  OH  TYR C 829    12125  10562  11499    638     39  -1182  A    O  
ATOM   1209  N   ASP C 830      42.249  44.508 157.813  1.00 93.80      A    N  
ANISOU 1209  N   ASP C 830    13587   9431  12622    457    154  -1968  A    N  
ATOM   1210  CA  ASP C 830      41.884  44.943 156.473  1.00 89.98      A    C  
ANISOU 1210  CA  ASP C 830    12915   8852  12421    618    236  -1727  A    C  
ATOM   1211  C   ASP C 830      43.055  44.706 155.523  1.00 84.06      A    C  
ANISOU 1211  C   ASP C 830    11997   8146  11794    443     33  -1525  A    C  
ATOM   1212  O   ASP C 830      44.220  44.830 155.906  1.00 83.00      A    O  
ANISOU 1212  O   ASP C 830    11940   7950  11646    201   -145  -1608  A    O  
ATOM   1213  CB  ASP C 830      41.424  46.399 156.472  1.00 93.49      A    C  
ANISOU 1213  CB  ASP C 830    13528   8909  13084    746    417  -1826  A    C  
ATOM   1214  CG  ASP C 830      40.052  46.570 157.112  1.00 95.54      A    C  
ANISOU 1214  CG  ASP C 830    13876   9143  13283   1000    687  -1948  A    C  
ATOM   1215  OD1 ASP C 830      39.238  45.623 157.022  1.00 95.55      A    O  
ANISOU 1215  OD1 ASP C 830    13698   9437  13171   1134    749  -1834  A    O  
ATOM   1216  OD2 ASP C 830      39.782  47.640 157.695  1.00 96.40      A    O1-
ANISOU 1216  OD2 ASP C 830    14228   8931  13468   1064    851  -2154  A    O1-
ATOM   1217  N   LEU C 831      42.722  44.349 154.285  1.00 77.19      A    N  
ANISOU 1217  N   LEU C 831    10896   7393  11039    563     64  -1254  A    N  
ATOM   1218  CA  LEU C 831      43.661  43.708 153.372  1.00 70.11      A    C  
ANISOU 1218  CA  LEU C 831     9815   6640  10185    430    -85  -1045  A    C  
ATOM   1219  C   LEU C 831      44.238  44.630 152.297  1.00 65.21      A    C  
ANISOU 1219  C   LEU C 831     9147   5793   9836    395    -94   -880  A    C  
ATOM   1220  O   LEU C 831      43.502  45.324 151.608  1.00 63.51      A    O  
ANISOU 1220  O   LEU C 831     8913   5442   9775    567     32   -766  A    O  
ATOM   1221  CB  LEU C 831      42.968  42.527 152.702  1.00 68.31      A    C  
ANISOU 1221  CB  LEU C 831     9386   6722   9847    550    -51   -860  A    C  
ATOM   1222  CG  LEU C 831      43.727  41.216 152.568  1.00 70.38      A    C  
ANISOU 1222  CG  LEU C 831     9522   7248   9972    413   -183   -777  A    C  
ATOM   1223  CD1 LEU C 831      44.236  40.751 153.920  1.00 71.59      A    C  
ANISOU 1223  CD1 LEU C 831     9786   7475   9940    272   -288   -978  A    C  
ATOM   1224  CD2 LEU C 831      42.818  40.166 151.953  1.00 70.46      A    C  
ANISOU 1224  CD2 LEU C 831     9382   7517   9872    541   -120   -630  A    C  
ATOM   1225  N   GLU C 832      45.559  44.595 152.143  1.00 61.28      A    N  
ANISOU 1225  N   GLU C 832     8613   5269   9402    174   -244   -841  A    N  
ATOM   1226  CA  GLU C 832      46.259  45.341 151.103  1.00 60.24      A    C  
ANISOU 1226  CA  GLU C 832     8418   4951   9520    108   -254   -659  A    C  
ATOM   1227  C   GLU C 832      47.146  44.435 150.239  1.00 57.73      A    C  
ANISOU 1227  C   GLU C 832     7892   4842   9200      4   -333   -443  A    C  
ATOM   1228  O   GLU C 832      47.936  43.643 150.754  1.00 57.04      A    O  
ANISOU 1228  O   GLU C 832     7749   4910   9013   -144   -456   -490  A    O  
ATOM   1229  CB  GLU C 832      47.104  46.446 151.733  1.00 67.35      A    C  
ANISOU 1229  CB  GLU C 832     9484   5539  10568    -83   -331   -820  A    C  
ATOM   1230  CG  GLU C 832      48.038  47.143 150.764  1.00 75.80      A    C  
ANISOU 1230  CG  GLU C 832    10474   6424  11903   -204   -360   -628  A    C  
ATOM   1231  CD  GLU C 832      49.082  47.998 151.468  1.00 84.15      A    C  
ANISOU 1231  CD  GLU C 832    11663   7221  13090   -465   -490   -785  A    C  
ATOM   1232  OE1 GLU C 832      48.932  48.243 152.687  1.00 83.90      A    O  
ANISOU 1232  OE1 GLU C 832    11836   7104  12938   -530   -539  -1065  A    O  
ATOM   1233  OE2 GLU C 832      50.048  48.432 150.799  1.00 89.30      A    O1-
ANISOU 1233  OE2 GLU C 832    12221   7753  13958   -617   -541   -628  A    O1-
ATOM   1234  N   VAL C 833      47.016  44.553 148.922  1.00 53.91      A    N  
ANISOU 1234  N   VAL C 833     7300   4359   8824     86   -252   -199  A    N  
ATOM   1235  CA  VAL C 833      47.817  43.747 148.015  1.00 52.69      A    C  
ANISOU 1235  CA  VAL C 833     6976   4379   8664      3   -277      2  A    C  
ATOM   1236  C   VAL C 833      49.190  44.361 147.768  1.00 55.58      A    C  
ANISOU 1236  C   VAL C 833     7302   4570   9247   -199   -337     75  A    C  
ATOM   1237  O   VAL C 833      49.300  45.446 147.209  1.00 60.49      A    O  
ANISOU 1237  O   VAL C 833     7965   4951  10068   -205   -286    166  A    O  
ATOM   1238  CB  VAL C 833      47.112  43.552 146.670  1.00 50.14      A    C  
ANISOU 1238  CB  VAL C 833     6576   4154   8319    155   -165    237  A    C  
ATOM   1239  CG1 VAL C 833      47.962  42.694 145.769  1.00 44.61      A    C  
ANISOU 1239  CG1 VAL C 833     5741   3621   7586     66   -158    414  A    C  
ATOM   1240  CG2 VAL C 833      45.752  42.908 146.878  1.00 48.87      A    C  
ANISOU 1240  CG2 VAL C 833     6420   4183   7965    333   -122    189  A    C  
ATOM   1241  N   ILE C 834      50.244  43.667 148.183  1.00 53.69      A    N  
ANISOU 1241  N   ILE C 834     6966   4448   8988   -364   -447     55  A    N  
ATOM   1242  CA  ILE C 834      51.592  44.200 148.018  1.00 55.78      A    C  
ANISOU 1242  CA  ILE C 834     7150   4564   9479   -574   -516    136  A    C  
ATOM   1243  C   ILE C 834      52.172  43.839 146.651  1.00 51.96      A    C  
ANISOU 1243  C   ILE C 834     6497   4159   9085   -571   -405    416  A    C  
ATOM   1244  O   ILE C 834      52.585  44.707 145.880  1.00 53.97      A    O  
ANISOU 1244  O   ILE C 834     6737   4228   9542   -621   -341    564  A    O  
ATOM   1245  CB  ILE C 834      52.553  43.682 149.110  1.00 58.42      A    C  
ANISOU 1245  CB  ILE C 834     7426   4985   9785   -768   -704     19  A    C  
ATOM   1246  CG1 ILE C 834      51.992  43.960 150.508  1.00 60.18      A    C  
ANISOU 1246  CG1 ILE C 834     7852   5154   9860   -787   -810   -270  A    C  
ATOM   1247  CG2 ILE C 834      53.936  44.289 148.914  1.00 61.39      A    C  
ANISOU 1247  CG2 ILE C 834     7685   5207  10432   -998   -786    128  A    C  
ATOM   1248  CD1 ILE C 834      51.546  45.393 150.706  1.00 67.62      A    C  
ANISOU 1248  CD1 ILE C 834     9002   5769  10921   -786   -771   -399  A    C  
ATOM   1249  N   ASP C 835      52.225  42.546 146.367  1.00 46.51      A    N  
ANISOU 1249  N   ASP C 835     5695   3735   8242   -517   -368    485  A    N  
ATOM   1250  CA  ASP C 835      52.736  42.067 145.087  1.00 51.61      A    C  
ANISOU 1250  CA  ASP C 835     6211   4470   8928   -504   -230    725  A    C  
ATOM   1251  C   ASP C 835      51.785  41.030 144.503  1.00 49.95      A    C  
ANISOU 1251  C   ASP C 835     6025   4487   8466   -334   -128    761  A    C  
ATOM   1252  O   ASP C 835      51.202  40.226 145.242  1.00 47.98      A    O  
ANISOU 1252  O   ASP C 835     5804   4391   8035   -274   -186    620  A    O  
ATOM   1253  CB  ASP C 835      54.128  41.449 145.245  1.00 55.85      A    C  
ANISOU 1253  CB  ASP C 835     6557   5079   9584   -654   -270    799  A    C  
ATOM   1254  CG  ASP C 835      55.216  42.490 145.443  1.00 64.16      A    C  
ANISOU 1254  CG  ASP C 835     7540   5912  10927   -854   -351    844  A    C  
ATOM   1255  OD1 ASP C 835      55.136  43.581 144.830  1.00 68.34      A    O  
ANISOU 1255  OD1 ASP C 835     8135   6235  11597   -869   -283    925  A    O  
ATOM   1256  OD2 ASP C 835      56.158  42.211 146.218  1.00 66.87      A    O1-
ANISOU 1256  OD2 ASP C 835     7755   6287  11364  -1007   -493    811  A    O1-
ATOM   1257  N   ILE C 836      51.636  41.055 143.184  1.00 46.91      A    N  
ANISOU 1257  N   ILE C 836     5638   4122   8062   -274     19    954  A    N  
ATOM   1258  CA  ILE C 836      50.946  39.996 142.467  1.00 46.94      A    C  
ANISOU 1258  CA  ILE C 836     5663   4345   7827   -163    112   1010  A    C  
ATOM   1259  C   ILE C 836      51.965  39.302 141.572  1.00 49.01      A    C  
ANISOU 1259  C   ILE C 836     5828   4683   8111   -223    252   1170  A    C  
ATOM   1260  O   ILE C 836      52.708  39.963 140.833  1.00 46.80      A    O  
ANISOU 1260  O   ILE C 836     5508   4281   7992   -289    342   1332  A    O  
ATOM   1261  CB  ILE C 836      49.776  40.537 141.630  1.00 45.54      A    C  
ANISOU 1261  CB  ILE C 836     5594   4154   7556    -41    161   1104  A    C  
ATOM   1262  CG1 ILE C 836      48.861  41.371 142.512  1.00 42.92      A    C  
ANISOU 1262  CG1 ILE C 836     5339   3701   7267     35     62    963  A    C  
ATOM   1263  CG2 ILE C 836      48.992  39.382 141.030  1.00 42.43      A    C  
ANISOU 1263  CG2 ILE C 836     5230   4002   6891     40    212   1132  A    C  
ATOM   1264  CD1 ILE C 836      47.755  42.078 141.768  1.00 43.78      A    C  
ANISOU 1264  CD1 ILE C 836     5519   3761   7354    167     98   1086  A    C  
ATOM   1265  N   PHE C 837      52.039  37.974 141.674  1.00 46.50      A    N  
ANISOU 1265  N   PHE C 837     5471   4550   7646   -199    288   1127  A    N  
ATOM   1266  CA  PHE C 837      52.941  37.198 140.823  1.00 43.41      A    C  
ANISOU 1266  CA  PHE C 837     5005   4225   7265   -228    463   1264  A    C  
ATOM   1267  C   PHE C 837      52.122  36.314 139.906  1.00 46.43      A    C  
ANISOU 1267  C   PHE C 837     5509   4765   7367   -143    581   1291  A    C  
ATOM   1268  O   PHE C 837      51.125  35.718 140.328  1.00 42.86      A    O  
ANISOU 1268  O   PHE C 837     5128   4431   6727    -79    500   1168  A    O  
ATOM   1269  CB  PHE C 837      53.909  36.335 141.648  1.00 40.68      A    C  
ANISOU 1269  CB  PHE C 837     4503   3932   7022   -279    432   1215  A    C  
ATOM   1270  CG  PHE C 837      54.729  37.114 142.645  1.00 46.19      A    C  
ANISOU 1270  CG  PHE C 837     5077   4500   7972   -398    269   1181  A    C  
ATOM   1271  CD1 PHE C 837      55.895  37.765 142.249  1.00 47.16      A    C  
ANISOU 1271  CD1 PHE C 837     5064   4496   8360   -507    329   1336  A    C  
ATOM   1272  CD2 PHE C 837      54.349  37.179 143.980  1.00 44.44      A    C  
ANISOU 1272  CD2 PHE C 837     4883   4289   7713   -418     57    998  A    C  
ATOM   1273  CE1 PHE C 837      56.660  38.481 143.167  1.00 47.61      A    C  
ANISOU 1273  CE1 PHE C 837     5007   4434   8649   -651    152   1305  A    C  
ATOM   1274  CE2 PHE C 837      55.112  37.890 144.901  1.00 44.71      A    C  
ANISOU 1274  CE2 PHE C 837     4834   4206   7948   -558   -112    954  A    C  
ATOM   1275  CZ  PHE C 837      56.266  38.547 144.490  1.00 44.91      A    C  
ANISOU 1275  CZ  PHE C 837     4717   4101   8244   -683    -79   1106  A    C  
ATOM   1276  N   LYS C 838      52.520  36.246 138.642  1.00 47.95      A    N  
ANISOU 1276  N   LYS C 838     5738   4959   7521   -155    773   1452  A    N  
ATOM   1277  CA  LYS C 838      51.917  35.290 137.741  1.00 49.52      A    C  
ANISOU 1277  CA  LYS C 838     6074   5308   7436   -110    892   1467  A    C  
ATOM   1278  C   LYS C 838      52.793  34.049 137.854  1.00 48.84      A    C  
ANISOU 1278  C   LYS C 838     5913   5276   7368   -117   1032   1437  A    C  
ATOM   1279  O   LYS C 838      54.011  34.153 137.794  1.00 49.36      A    O  
ANISOU 1279  O   LYS C 838     5842   5260   7654   -158   1147   1530  A    O  
ATOM   1280  CB  LYS C 838      51.839  35.841 136.313  1.00 56.95      A    C  
ANISOU 1280  CB  LYS C 838     7133   6227   8278   -126   1032   1651  A    C  
ATOM   1281  CG  LYS C 838      51.303  34.858 135.289  1.00 62.61      A    C  
ANISOU 1281  CG  LYS C 838     8024   7096   8667   -115   1156   1665  A    C  
ATOM   1282  CD  LYS C 838      49.847  34.508 135.558  1.00 65.18      A    C  
ANISOU 1282  CD  LYS C 838     8444   7554   8769    -72    975   1557  A    C  
ATOM   1283  N   ILE C 839      52.188  32.891 138.097  1.00 47.03      A    N  
ANISOU 1283  N   ILE C 839     5752   5172   6943    -76   1019   1316  A    N  
ATOM   1284  CA  ILE C 839      52.975  31.680 138.283  1.00 50.16      A    C  
ANISOU 1284  CA  ILE C 839     6081   5597   7380    -64   1154   1290  A    C  
ATOM   1285  C   ILE C 839      52.550  30.573 137.334  1.00 50.38      A    C  
ANISOU 1285  C   ILE C 839     6295   5713   7134    -45   1332   1267  A    C  
ATOM   1286  O   ILE C 839      51.362  30.392 137.048  1.00 51.94      A    O  
ANISOU 1286  O   ILE C 839     6652   6005   7076    -46   1249   1203  A    O  
ATOM   1287  CB  ILE C 839      52.896  31.160 139.732  1.00 49.02      A    C  
ANISOU 1287  CB  ILE C 839     5828   5489   7308    -45    974   1157  A    C  
ATOM   1288  CG1 ILE C 839      51.448  30.882 140.139  1.00 45.57      A    C  
ANISOU 1288  CG1 ILE C 839     5519   5160   6634    -14    819   1019  A    C  
ATOM   1289  CG2 ILE C 839      53.547  32.151 140.699  1.00 47.90      A    C  
ANISOU 1289  CG2 ILE C 839     5514   5251   7435    -94    808   1169  A    C  
ATOM   1290  CD1 ILE C 839      51.347  30.101 141.439  1.00 48.06      A    C  
ANISOU 1290  CD1 ILE C 839     5764   5533   6965      5    694    899  A    C  
ATOM   1291  N   GLU C 840      53.548  29.852 136.839  1.00 48.87      A    N  
ANISOU 1291  N   GLU C 840     6078   5482   7009    -33   1584   1325  A    N  
ATOM   1292  CA  GLU C 840      53.340  28.718 135.957  1.00 49.10      A    C  
ANISOU 1292  CA  GLU C 840     6304   5557   6793    -22   1798   1284  A    C  
ATOM   1293  C   GLU C 840      54.268  27.605 136.386  1.00 49.65      A    C  
ANISOU 1293  C   GLU C 840     6262   5577   7025     36   1963   1265  A    C  
ATOM   1294  O   GLU C 840      55.481  27.665 136.158  1.00 51.72      A    O  
ANISOU 1294  O   GLU C 840     6381   5751   7517     61   2164   1386  A    O  
ATOM   1295  CB  GLU C 840      53.598  29.071 134.490  1.00 51.92      A    C  
ANISOU 1295  CB  GLU C 840     6819   5892   7017    -58   2033   1403  A    C  
ATOM   1296  CG  GLU C 840      52.399  29.685 133.745  1.00 58.62      A    C  
ANISOU 1296  CG  GLU C 840     7874   6827   7573   -115   1903   1417  A    C  
ATOM   1297  CD  GLU C 840      52.486  31.202 133.608  1.00 59.39      A    C  
ANISOU 1297  CD  GLU C 840     7888   6869   7811   -135   1803   1565  A    C  
ATOM   1298  N   ARG C 841      53.700  26.602 137.038  1.00 46.49      A    N  
ANISOU 1298  N   ARG C 841     5906   5229   6529     61   1878   1134  A    N  
ATOM   1299  CA  ARG C 841      54.478  25.451 137.446  1.00 46.21      A    C  
ANISOU 1299  CA  ARG C 841     5780   5137   6641    130   2033   1127  A    C  
ATOM   1300  C   ARG C 841      54.805  24.575 136.230  1.00 49.24      A    C  
ANISOU 1300  C   ARG C 841     6361   5461   6889    152   2396   1127  A    C  
ATOM   1301  O   ARG C 841      53.944  24.345 135.384  1.00 47.56      A    O  
ANISOU 1301  O   ARG C 841     6423   5297   6351     93   2440   1045  A    O  
ATOM   1302  CB  ARG C 841      53.726  24.658 138.493  1.00 41.11      A    C  
ANISOU 1302  CB  ARG C 841     5142   4554   5923    144   1840    999  A    C  
ATOM   1303  CG  ARG C 841      53.452  25.416 139.798  1.00 45.28      A    C  
ANISOU 1303  CG  ARG C 841     5499   5137   6569    127   1511    981  A    C  
ATOM   1304  CD  ARG C 841      53.246  24.414 140.928  1.00 47.63      A    C  
ANISOU 1304  CD  ARG C 841     5744   5469   6883    163   1403    909  A    C  
ATOM   1305  NE  ARG C 841      52.435  23.328 140.436  1.00 49.84      A    N  
ANISOU 1305  NE  ARG C 841     6246   5775   6917    159   1508    808  A    N  
ATOM   1306  CZ  ARG C 841      52.845  22.083 140.225  1.00 49.17      A    C  
ANISOU 1306  CZ  ARG C 841     6215   5617   6850    208   1720    802  A    C  
ATOM   1307  NH1 ARG C 841      54.076  21.677 140.521  1.00 54.58      A    N1+
ANISOU 1307  NH1 ARG C 841     6719   6209   7811    290   1856    912  A    N1+
ATOM   1308  NH2 ARG C 841      51.977  21.231 139.735  1.00 46.01      A    N  
ANISOU 1308  NH2 ARG C 841     6050   5234   6200    169   1788    690  A    N  
ATOM   1309  N   GLU C 842      56.048  24.106 136.142  1.00 50.34      A    N  
ANISOU 1309  N   GLU C 842     6358   5493   7275    232   2659   1224  A    N  
ATOM   1310  CA  GLU C 842      56.444  23.235 135.039  1.00 54.12      A    C  
ANISOU 1310  CA  GLU C 842     7032   5886   7645    272   3056   1212  A    C  
ATOM   1311  C   GLU C 842      55.526  22.023 134.974  1.00 50.05      A    C  
ANISOU 1311  C   GLU C 842     6784   5380   6851    257   3070   1029  A    C  
ATOM   1312  O   GLU C 842      55.262  21.382 135.987  1.00 45.18      A    O  
ANISOU 1312  O   GLU C 842     6081   4772   6312    290   2911    970  A    O  
ATOM   1313  CB  GLU C 842      57.897  22.780 135.184  1.00 61.56      A    C  
ANISOU 1313  CB  GLU C 842     7732   6703   8957    394   3333   1350  A    C  
ATOM   1314  CG  GLU C 842      58.927  23.879 134.955  0.44 66.30      A    C  
ANISOU 1314  CG  GLU C 842     8088   7275   9830    390   3406   1549  A    C  
ATOM   1315  CD  GLU C 842      60.349  23.349 134.959  0.55 72.06      A    C  
ANISOU 1315  CD  GLU C 842     8577   7886  10917    519   3675   1686  A    C  
ATOM   1316  OE1 GLU C 842      61.279  24.129 135.260  1.00 75.93      A    O  
ANISOU 1316  OE1 GLU C 842     8761   8363  11727    519   3612   1855  A    O  
ATOM   1317  OE2 GLU C 842      60.537  22.151 134.658  0.72 73.00      A    O1-
ANISOU 1317  OE2 GLU C 842     8830   7914  10991    622   3881   1604  A    O1-
ATOM   1318  N   GLY C 843      55.023  21.736 133.781  1.00 48.86      A    N  
ANISOU 1318  N   GLY C 843     6969   5232   6365    188   3247    945  A    N  
ATOM   1319  CA  GLY C 843      54.229  20.547 133.568  1.00 52.95      A    C  
ANISOU 1319  CA  GLY C 843     7770   5736   6613    144   3294    767  A    C  
ATOM   1320  C   GLY C 843      52.759  20.715 133.882  1.00 51.35      A    C  
ANISOU 1320  C   GLY C 843     7676   5684   6148     23   2929    660  A    C  
ATOM   1321  O   GLY C 843      51.952  19.918 133.430  1.00 49.74      A    O  
ANISOU 1321  O   GLY C 843     7749   5494   5655    -67   2946    520  A    O  
ATOM   1322  N   GLU C 844      52.390  21.758 134.619  1.00 53.00      A    N  
ANISOU 1322  N   GLU C 844     7677   6002   6458     12   2608    724  A    N  
ATOM   1323  CA  GLU C 844      51.029  21.805 135.153  1.00 51.87      A    C  
ANISOU 1323  CA  GLU C 844     7578   5993   6138    -67   2278    632  A    C  
ATOM   1324  C   GLU C 844      49.988  22.242 134.112  1.00 46.17      A    C  
ANISOU 1324  C   GLU C 844     7097   5384   5060   -199   2187    609  A    C  
ATOM   1325  O   GLU C 844      48.838  21.831 134.180  1.00 45.91      A    O  
ANISOU 1325  O   GLU C 844     7185   5447   4813   -289   2010    514  A    O  
ATOM   1326  CB  GLU C 844      50.954  22.718 136.385  1.00 47.26      A    C  
ANISOU 1326  CB  GLU C 844     6704   5470   5782    -22   1986    692  A    C  
ATOM   1327  CG  GLU C 844      49.678  22.514 137.206  1.00 44.71      A    C  
ANISOU 1327  CG  GLU C 844     6386   5263   5339    -66   1701    593  A    C  
ATOM   1328  CD  GLU C 844      49.564  23.475 138.374  1.00 45.45      A    C  
ANISOU 1328  CD  GLU C 844     6241   5408   5619    -24   1443    632  A    C  
ATOM   1329  OE1 GLU C 844      49.210  24.648 138.138  1.00 43.53      A    O  
ANISOU 1329  OE1 GLU C 844     5973   5212   5356    -45   1319    685  A    O  
ATOM   1330  OE2 GLU C 844      49.831  23.054 139.528  1.00 46.71      A    O1-
ANISOU 1330  OE2 GLU C 844     6255   5553   5939     28   1369    610  A    O1-
ATOM   1331  N   CYS C 845      50.385  23.065 133.156  1.00 45.49      A    N  
ANISOU 1331  N   CYS C 845     7071   5295   4917   -218   2300    714  A    N  
ATOM   1332  CA  CYS C 845      49.466  23.472 132.084  1.00 51.55      A    C  
ANISOU 1332  CA  CYS C 845     8077   6176   5332   -348   2214    725  A    C  
ATOM   1333  C   CYS C 845      48.994  22.255 131.262  1.00 54.67      A    C  
ANISOU 1333  C   CYS C 845     8817   6572   5384   -464   2350    580  A    C  
ATOM   1334  O   CYS C 845      47.815  22.119 130.923  1.00 50.75      A    O  
ANISOU 1334  O   CYS C 845     8481   6202   4601   -599   2145    527  A    O  
ATOM   1335  CB  CYS C 845      50.139  24.501 131.171  1.00 52.53      A    C  
ANISOU 1335  CB  CYS C 845     8221   6278   5462   -343   2357    886  A    C  
ATOM   1336  SG  CYS C 845      49.177  24.957 129.692  1.00 63.08      A    S  
ANISOU 1336  SG  CYS C 845     9881   7754   6334   -507   2284    942  A    S  
ATOM   1337  N   GLN C 846      49.937  21.383 130.938  1.00 52.46      A    N  
ANISOU 1337  N   GLN C 846     8646   6139   5147   -416   2701    522  A    N  
ATOM   1338  CA  GLN C 846      49.632  20.164 130.211  1.00 53.77      A    C  
ANISOU 1338  CA  GLN C 846     9158   6254   5018   -520   2870    357  A    C  
ATOM   1339  C   GLN C 846      48.769  19.225 131.050  1.00 53.06      A    C  
ANISOU 1339  C   GLN C 846     9071   6182   4909   -568   2684    219  A    C  
ATOM   1340  O   GLN C 846      47.843  18.604 130.529  1.00 50.22      A    O  
ANISOU 1340  O   GLN C 846     8969   5875   4236   -733   2593     98  A    O  
ATOM   1341  CB  GLN C 846      50.929  19.480 129.780  1.00 52.08      A    C  
ANISOU 1341  CB  GLN C 846     8963   5841   4985   -402   3224    318  A    C  
ATOM   1342  CG  GLN C 846      51.729  20.292 128.777  1.00 57.21      A    C  
ANISOU 1342  CG  GLN C 846     9620   6480   5638   -372   3383    433  A    C  
ATOM   1343  CD  GLN C 846      51.140  20.212 127.377  1.00 67.21      A    C  
ANISOU 1343  CD  GLN C 846    11221   7816   6499   -531   3353    357  A    C  
ATOM   1344  NE2 GLN C 846      51.792  20.861 126.416  1.00 69.35      A    N  
ANISOU 1344  NE2 GLN C 846    11534   8085   6731   -517   3503    453  A    N  
ATOM   1345  OE1 GLN C 846      50.127  19.544 127.159  1.00 70.79      A    O  
ANISOU 1345  OE1 GLN C 846    11887   8325   6685   -673   3194    218  A    O  
ATOM   1346  N   ARG C 847      49.051  19.139 132.350  1.00 48.76      A    N  
ANISOU 1346  N   ARG C 847     8223   5599   4702   -438   2592    245  A    N  
ATOM   1347  CA  ARG C 847      48.263  18.272 133.228  1.00 47.65      A    C  
ANISOU 1347  CA  ARG C 847     8062   5476   4566   -476   2418    137  A    C  
ATOM   1348  C   ARG C 847      46.825  18.765 133.330  1.00 47.23      A    C  
ANISOU 1348  C   ARG C 847     8006   5627   4312   -610   2047    132  A    C  
ATOM   1349  O   ARG C 847      45.882  17.962 133.380  1.00 43.54      A    O  
ANISOU 1349  O   ARG C 847     7675   5201   3667   -738   1934     22  A    O  
ATOM   1350  CB  ARG C 847      48.877  18.197 134.635  1.00 45.28      A    C  
ANISOU 1350  CB  ARG C 847     7434   5117   4653   -311   2374    194  A    C  
ATOM   1351  CG  ARG C 847      48.116  17.315 135.602  1.00 42.47      A    C  
ANISOU 1351  CG  ARG C 847     7050   4778   4310   -342   2212    106  A    C  
ATOM   1352  CD  ARG C 847      48.702  17.362 137.010  1.00 43.53      A    C  
ANISOU 1352  CD  ARG C 847     6867   4883   4790   -191   2134    186  A    C  
ATOM   1353  NE  ARG C 847      48.338  18.582 137.723  1.00 41.37      A    N  
ANISOU 1353  NE  ARG C 847     6362   4761   4598   -171   1845    265  A    N  
ATOM   1354  CZ  ARG C 847      48.741  18.876 138.958  1.00 42.27      A    C  
ANISOU 1354  CZ  ARG C 847     6213   4884   4963    -72   1720    331  A    C  
ATOM   1355  NH1 ARG C 847      49.524  18.036 139.624  1.00 39.93      A    N1+
ANISOU 1355  NH1 ARG C 847     5826   4475   4871     21   1836    357  A    N1+
ATOM   1356  NH2 ARG C 847      48.342  20.006 139.536  1.00 39.80      A    N  
ANISOU 1356  NH2 ARG C 847     5741   4689   4691    -68   1476    374  A    N  
ATOM   1357  N   TYR C 848      46.651  20.084 133.374  1.00 42.52      A    N  
ANISOU 1357  N   TYR C 848     7240   5149   3768   -580   1862    262  A    N  
ATOM   1358  CA  TYR C 848      45.317  20.654 133.581  1.00 41.76      A    C  
ANISOU 1358  CA  TYR C 848     7079   5239   3549   -666   1518    291  A    C  
ATOM   1359  C   TYR C 848      44.494  20.667 132.298  1.00 45.77      A    C  
ANISOU 1359  C   TYR C 848     7858   5857   3675   -852   1450    287  A    C  
ATOM   1360  O   TYR C 848      43.263  20.614 132.341  1.00 45.67      A    O  
ANISOU 1360  O   TYR C 848     7852   5991   3510   -969   1191    278  A    O  
ATOM   1361  CB  TYR C 848      45.418  22.078 134.129  1.00 43.75      A    C  
ANISOU 1361  CB  TYR C 848     7059   5548   4017   -553   1357    433  A    C  
ATOM   1362  CG  TYR C 848      44.076  22.777 134.328  1.00 44.38      A    C  
ANISOU 1362  CG  TYR C 848     7048   5801   4012   -604   1036    486  A    C  
ATOM   1363  CD1 TYR C 848      43.260  22.456 135.403  1.00 41.15      A    C  
ANISOU 1363  CD1 TYR C 848     6497   5460   3678   -594    855    430  A    C  
ATOM   1364  CD2 TYR C 848      43.632  23.760 133.433  1.00 45.46      A    C  
ANISOU 1364  CD2 TYR C 848     7236   6032   4006   -653    931    612  A    C  
ATOM   1365  CE1 TYR C 848      42.030  23.087 135.598  1.00 40.75      A    C  
ANISOU 1365  CE1 TYR C 848     6339   5564   3581   -622    593    491  A    C  
ATOM   1366  CE2 TYR C 848      42.399  24.399 133.614  1.00 46.00      A    C  
ANISOU 1366  CE2 TYR C 848     7193   6251   4034   -678    648    687  A    C  
ATOM   1367  CZ  TYR C 848      41.599  24.057 134.704  1.00 45.41      A    C  
ANISOU 1367  CZ  TYR C 848     6960   6239   4054   -657    489    623  A    C  
ATOM   1368  OH  TYR C 848      40.368  24.675 134.911  1.00 43.36      A    O  
ANISOU 1368  OH  TYR C 848     6564   6125   3785   -662    239    708  A    O  
ATOM   1369  N   LYS C 849      45.191  20.735 131.166  1.00 45.96      A    N  
ANISOU 1369  N   LYS C 849     8100   5817   3546   -884   1684    306  A    N  
ATOM   1370  CA  LYS C 849      44.574  20.983 129.868  1.00 53.50      A    C  
ANISOU 1370  CA  LYS C 849     9319   6888   4121  -1059   1617    341  A    C  
ATOM   1371  C   LYS C 849      43.314  20.147 129.562  1.00 55.79      A    C  
ANISOU 1371  C   LYS C 849     9807   7289   4100  -1279   1418    231  A    C  
ATOM   1372  O   LYS C 849      42.303  20.723 129.172  1.00 55.10      A    O  
ANISOU 1372  O   LYS C 849     9712   7387   3836  -1392   1135    329  A    O  
ATOM   1373  CB  LYS C 849      45.623  20.802 128.758  0.98 55.14      A    C  
ANISOU 1373  CB  LYS C 849     9762   6973   4215  -1056   1960    322  A    C  
ATOM   1374  CG  LYS C 849      45.087  20.964 127.344  1.00 58.42      A    C  
ANISOU 1374  CG  LYS C 849    10397   7496   4303  -1210   1852    336  A    C  
ATOM   1375  CD  LYS C 849      46.200  20.912 126.314  1.00 60.76      A    C  
ANISOU 1375  CD  LYS C 849    10841   7670   4576  -1163   2165    323  A    C  
ATOM   1376  CE  LYS C 849      45.642  20.909 124.904  1.00 65.76      A    C  
ANISOU 1376  CE  LYS C 849    11730   8406   4849  -1333   2067    313  A    C  
ATOM   1377  NZ  LYS C 849      46.724  20.929 123.856  1.00 71.47      A    N1+
ANISOU 1377  NZ  LYS C 849    12609   9021   5523  -1290   2384    311  A    N1+
ATOM   1378  N   PRO C 850      43.345  18.808 129.768  1.00 55.57      A    N  
ANISOU 1378  N   PRO C 850     9905   7143   4065  -1329   1534     44  A    N  
ATOM   1379  CA  PRO C 850      42.113  18.058 129.478  1.00 54.01      A    C  
ANISOU 1379  CA  PRO C 850     9824   7039   3657  -1540   1294    -53  A    C  
ATOM   1380  C   PRO C 850      40.895  18.532 130.272  1.00 55.11      A    C  
ANISOU 1380  C   PRO C 850     9750   7386   3803  -1596    945     44  A    C  
ATOM   1381  O   PRO C 850      39.775  18.394 129.791  1.00 57.26      A    O  
ANISOU 1381  O   PRO C 850    10058   7800   3899  -1772    684     52  A    O  
ATOM   1382  CB  PRO C 850      42.471  16.624 129.875  1.00 53.03      A    C  
ANISOU 1382  CB  PRO C 850     9819   6712   3618  -1546   1499   -245  A    C  
ATOM   1383  CG  PRO C 850      43.941  16.560 129.760  1.00 56.36      A    C  
ANISOU 1383  CG  PRO C 850    10268   6931   4214  -1363   1869   -258  A    C  
ATOM   1384  CD  PRO C 850      44.440  17.912 130.176  1.00 53.70      A    C  
ANISOU 1384  CD  PRO C 850     9697   6675   4033  -1205   1866    -70  A    C  
ATOM   1385  N   PHE C 851      41.107  19.082 131.465  1.00 52.70      A    N  
ANISOU 1385  N   PHE C 851     9111   7072   3841  -1394    902    117  A    N  
ATOM   1386  CA  PHE C 851      39.987  19.533 132.282  1.00 51.79      A    C  
ANISOU 1386  CA  PHE C 851     8718   7121   3837  -1386    587    200  A    C  
ATOM   1387  C   PHE C 851      39.433  20.867 131.782  1.00 56.57      A    C  
ANISOU 1387  C   PHE C 851     9211   7894   4389  -1377    371    394  A    C  
ATOM   1388  O   PHE C 851      38.369  21.286 132.215  1.00 60.48      A    O  
ANISOU 1388  O   PHE C 851     9500   8541   4938  -1387    109    484  A    O  
ATOM   1389  CB  PHE C 851      40.398  19.599 133.771  1.00 48.35      A    C  
ANISOU 1389  CB  PHE C 851     7993   6607   3770  -1178    625    189  A    C  
ATOM   1390  CG  PHE C 851      40.671  18.250 134.353  1.00 46.67      A    C  
ANISOU 1390  CG  PHE C 851     7860   6259   3614  -1199    773     37  A    C  
ATOM   1391  CD1 PHE C 851      39.635  17.469 134.830  1.00 47.33      A    C  
ANISOU 1391  CD1 PHE C 851     7925   6412   3647  -1325    620    -23  A    C  
ATOM   1392  CD2 PHE C 851      41.947  17.718 134.331  1.00 48.31      A    C  
ANISOU 1392  CD2 PHE C 851     8170   6263   3924  -1102   1078    -32  A    C  
ATOM   1393  CE1 PHE C 851      39.874  16.194 135.325  1.00 47.38      A    C  
ANISOU 1393  CE1 PHE C 851     8024   6274   3705  -1352    764   -151  A    C  
ATOM   1394  CE2 PHE C 851      42.193  16.441 134.808  1.00 47.79      A    C  
ANISOU 1394  CE2 PHE C 851     8189   6051   3919  -1113   1225   -154  A    C  
ATOM   1395  CZ  PHE C 851      41.156  15.680 135.311  1.00 46.39      A    C  
ANISOU 1395  CZ  PHE C 851     8007   5932   3686  -1240   1066   -215  A    C  
ATOM   1396  N   LYS C 852      40.126  21.519 130.850  1.00 59.31      A    N  
ANISOU 1396  N   LYS C 852     9690   8209   4635  -1357    492    474  A    N  
ATOM   1397  CA  LYS C 852      39.560  22.713 130.221  1.00 64.27      A    C  
ANISOU 1397  CA  LYS C 852    10254   8989   5177  -1371    285    679  A    C  
ATOM   1398  C   LYS C 852      38.356  22.303 129.377  1.00 68.76      A    C  
ANISOU 1398  C   LYS C 852    10986   9744   5397  -1626     41    705  A    C  
ATOM   1399  O   LYS C 852      37.523  23.137 129.034  1.00 68.26      A    O  
ANISOU 1399  O   LYS C 852    10809   9848   5279  -1656   -216    895  A    O  
ATOM   1400  CB  LYS C 852      40.592  23.460 129.366  1.00 65.29      A    C  
ANISOU 1400  CB  LYS C 852    10509   9039   5260  -1310    483    774  A    C  
ATOM   1401  CG  LYS C 852      41.447  24.435 130.165  1.00 62.97      A    C  
ANISOU 1401  CG  LYS C 852     9951   8628   5345  -1070    581    853  A    C  
ATOM   1402  CD  LYS C 852      42.240  25.393 129.294  1.00 63.46      A    C  
ANISOU 1402  CD  LYS C 852    10090   8642   5378  -1027    717   1004  A    C  
ATOM   1403  CE  LYS C 852      42.846  26.494 130.167  0.97 66.22      A    C  
ANISOU 1403  CE  LYS C 852    10146   8891   6123   -819    734   1098  A    C  
ATOM   1404  NZ  LYS C 852      43.906  27.295 129.482  1.00 70.29      A    N1+
ANISOU 1404  NZ  LYS C 852    10714   9307   6684   -768    935   1226  A    N1+
ATOM   1405  N   GLN C 853      38.261  21.011 129.062  1.00 71.98      A    N  
ANISOU 1405  N   GLN C 853    11612  10097   5641  -1786    112    511  A    N  
ATOM   1406  CA  GLN C 853      37.077  20.464 128.401  1.00 72.83      A    C  
ANISOU 1406  CA  GLN C 853    11776  10329   5567  -2002   -138    490  A    C  
ATOM   1407  C   GLN C 853      35.902  20.393 129.389  1.00 67.54      A    C  
ANISOU 1407  C   GLN C 853    10837   9805   5019  -2036   -405    545  A    C  
ATOM   1408  O   GLN C 853      34.749  20.275 128.993  1.00 72.71      A    O  
ANISOU 1408  O   GLN C 853    11428  10608   5589  -2192   -671    608  A    O  
ATOM   1409  CB  GLN C 853      37.358  19.068 127.825  1.00 75.07      A    C  
ANISOU 1409  CB  GLN C 853    12356  10460   5706  -2154     33    253  A    C  
ATOM   1410  CG  GLN C 853      38.503  18.997 126.814  1.00 78.89      A    C  
ANISOU 1410  CG  GLN C 853    13110  10793   6073  -2122    326    183  A    C  
ATOM   1411  CD  GLN C 853      38.668  20.262 125.990  1.00 85.30      A    C  
ANISOU 1411  CD  GLN C 853    13906  11710   6794  -2065    271    381  A    C  
ATOM   1412  NE2 GLN C 853      39.810  20.928 126.158  1.00 85.43      A    N  
ANISOU 1412  NE2 GLN C 853    13890  11628   6942  -1873    516    441  A    N  
ATOM   1413  OE1 GLN C 853      37.775  20.652 125.229  1.00 88.63      A    O  
ANISOU 1413  OE1 GLN C 853    14331  12297   7046  -2193     11    497  A    O  
ATOM   1414  N   LEU C 854      36.198  20.484 130.674  1.00 59.28      A    N  
ANISOU 1414  N   LEU C 854     9606   8713   4205  -1880   -328    530  A    N  
ATOM   1415  CA  LEU C 854      35.191  20.249 131.700  1.00 56.60      A    C  
ANISOU 1415  CA  LEU C 854     8991   8469   4044  -1876   -515    544  A    C  
ATOM   1416  C   LEU C 854      34.490  21.582 131.972  1.00 59.46      A    C  
ANISOU 1416  C   LEU C 854     9028   8984   4579  -1736   -732    776  A    C  
ATOM   1417  O   LEU C 854      35.122  22.629 131.946  1.00 60.23      A    O  
ANISOU 1417  O   LEU C 854     9054   9025   4805  -1550   -655    872  A    O  
ATOM   1418  CB  LEU C 854      35.873  19.668 132.952  1.00 52.45      A    C  
ANISOU 1418  CB  LEU C 854     8372   7767   3788  -1716   -300    397  A    C  
ATOM   1419  CG  LEU C 854      35.196  18.882 134.083  1.00 48.99      A    C  
ANISOU 1419  CG  LEU C 854     7769   7347   3498  -1736   -362    327  A    C  
ATOM   1420  CD1 LEU C 854      34.589  17.576 133.575  1.00 55.41      A    C  
ANISOU 1420  CD1 LEU C 854     8811   8174   4068  -2030   -418    209  A    C  
ATOM   1421  CD2 LEU C 854      36.078  18.660 135.262  1.00 46.83      A    C  
ANISOU 1421  CD2 LEU C 854     7394   6906   3491  -1530   -152    239  A    C  
ATOM   1422  N  AHIS C 855      33.191  21.574 132.222  0.51 61.46      A    N  
ANISOU 1422  N  AHIS C 855     9076   9419   4856  -1820   -993    876  A    N  
ATOM   1423  N  BHIS C 855      33.188  21.529 132.235  0.49 61.42      A    N  
ANISOU 1423  N  BHIS C 855     9075   9413   4850  -1825   -991    870  A    N  
ATOM   1424  CA AHIS C 855      32.529  22.856 132.400  0.51 60.42      A    C  
ANISOU 1424  CA AHIS C 855     8642   9413   4901  -1668  -1172   1110  A    C  
ATOM   1425  CA BHIS C 855      32.415  22.744 132.465  0.49 60.47      A    C  
ANISOU 1425  CA BHIS C 855     8637   9431   4909  -1684  -1186   1103  A    C  
ATOM   1426  C  AHIS C 855      32.668  23.333 133.840  0.51 56.02      A    C  
ANISOU 1426  C  AHIS C 855     7800   8771   4713  -1399  -1067   1088  A    C  
ATOM   1427  C  BHIS C 855      32.670  23.322 133.853  0.49 56.02      A    C  
ANISOU 1427  C  BHIS C 855     7800   8770   4715  -1399  -1066   1085  A    C  
ATOM   1428  O  AHIS C 855      33.225  22.634 134.693  0.51 55.28      A    O  
ANISOU 1428  O  AHIS C 855     7735   8550   4720  -1349   -890    909  A    O  
ATOM   1429  O  BHIS C 855      33.296  22.670 134.696  0.49 55.07      A    O  
ANISOU 1429  O  BHIS C 855     7713   8513   4699  -1339   -879    907  A    O  
ATOM   1430  CB AHIS C 855      31.057  22.773 132.002  0.51 63.55      A    C  
ANISOU 1430  CB AHIS C 855     8899  10053   5193  -1853  -1499   1273  A    C  
ATOM   1431  CB BHIS C 855      30.914  22.479 132.289  0.49 62.41      A    C  
ANISOU 1431  CB BHIS C 855     8722   9909   5080  -1870  -1494   1232  A    C  
ATOM   1432  CG AHIS C 855      30.809  22.932 130.532  0.51 68.37      A    C  
ANISOU 1432  CG AHIS C 855     9680  10726   5574  -2013  -1626   1360  A    C  
ATOM   1433  CG BHIS C 855      30.372  21.365 133.138  0.49 57.81      A    C  
ANISOU 1433  CG BHIS C 855     8063   9337   4567  -1971  -1495   1097  A    C  
ATOM   1434  CD2AHIS C 855      29.906  22.334 129.719  0.51 72.14      A    C  
ANISOU 1434  CD2AHIS C 855    10203  11294   5912  -2246  -1804   1366  A    C  
ATOM   1435  CD2BHIS C 855      29.751  21.386 134.342  0.49 52.99      A    C  
ANISOU 1435  CD2BHIS C 855     7143   8763   4229  -1847  -1506   1119  A    C  
ATOM   1436  ND1AHIS C 855      31.531  23.793 129.734  0.51 69.59      A    N  
ANISOU 1436  ND1AHIS C 855     9969  10827   5646  -1928  -1558   1450  A    N  
ATOM   1437  ND1BHIS C 855      30.440  20.037 132.770  0.49 58.02      A    N  
ANISOU 1437  ND1BHIS C 855     8359   9314   4372  -2226  -1459    915  A    N  
ATOM   1438  CE1AHIS C 855      31.080  23.723 128.493  0.51 72.70      A    C  
ANISOU 1438  CE1AHIS C 855    10488  11288   5845  -2095  -1690   1505  A    C  
ATOM   1439  CE1BHIS C 855      29.866  19.292 133.698  0.49 53.70      A    C  
ANISOU 1439  CE1BHIS C 855     7665   8786   3953  -2271  -1473    852  A    C  
ATOM   1440  NE2AHIS C 855      30.095  22.843 128.458  0.51 75.04      A    N  
ANISOU 1440  NE2AHIS C 855    10737  11674   6102  -2294  -1847   1454  A    N  
ATOM   1441  NE2BHIS C 855      29.450  20.085 134.670  0.49 50.32      A    N  
ANISOU 1441  NE2BHIS C 855     6882   8415   3823  -2039  -1492    973  A    N  
ATOM   1442  N   ASN C 856      32.172  24.537 134.090  1.00 51.68      A    N  
ANISOU 1442  N   ASN C 856     6994   8286   4358  -1227  -1174   1275  A    N  
ATOM   1443  CA  ASN C 856      32.182  25.137 135.417  1.00 46.25      A    C  
ANISOU 1443  CA  ASN C 856     6051   7524   3998   -977  -1087   1260  A    C  
ATOM   1444  C   ASN C 856      33.595  25.287 135.995  1.00 44.41      A    C  
ANISOU 1444  C   ASN C 856     5917   7069   3886   -824   -834   1107  A    C  
ATOM   1445  O   ASN C 856      33.945  24.696 137.018  1.00 49.88      A    O  
ANISOU 1445  O   ASN C 856     6585   7681   4685   -773   -710    952  A    O  
ATOM   1446  CB  ASN C 856      31.281  24.324 136.358  1.00 45.49      A    C  
ANISOU 1446  CB  ASN C 856     5787   7516   3980  -1026  -1136   1197  A    C  
ATOM   1447  CG  ASN C 856      31.097  24.991 137.690  1.00 47.69      A    C  
ANISOU 1447  CG  ASN C 856     5810   7751   4560   -780  -1058   1198  A    C  
ATOM   1448  ND2 ASN C 856      30.731  24.208 138.711  1.00 42.73      A    N  
ANISOU 1448  ND2 ASN C 856     5092   7142   4001   -794  -1006   1092  A    N  
ATOM   1449  OD1 ASN C 856      31.296  26.201 137.811  1.00 50.97      A    O  
ANISOU 1449  OD1 ASN C 856     6128   8102   5137   -585  -1032   1288  A    O  
ATOM   1450  N   ARG C 857      34.400  26.090 135.314  1.00 41.97      A    N  
ANISOU 1450  N   ARG C 857     5713   6671   3563   -762   -769   1174  A    N  
ATOM   1451  CA  ARG C 857      35.744  26.403 135.747  1.00 43.89      A    C  
ANISOU 1451  CA  ARG C 857     6016   6715   3945   -627   -554   1074  A    C  
ATOM   1452  C   ARG C 857      35.696  27.775 136.427  1.00 45.01      A    C  
ANISOU 1452  C   ARG C 857     5947   6792   4364   -407   -570   1168  A    C  
ATOM   1453  O   ARG C 857      35.058  28.714 135.929  1.00 41.02      A    O  
ANISOU 1453  O   ARG C 857     5349   6349   3889   -360   -697   1357  A    O  
ATOM   1454  CB  ARG C 857      36.712  26.383 134.559  1.00 42.80      A    C  
ANISOU 1454  CB  ARG C 857     6132   6506   3626   -711   -442   1088  A    C  
ATOM   1455  CG  ARG C 857      36.721  25.056 133.810  1.00 48.74      A    C  
ANISOU 1455  CG  ARG C 857     7137   7300   4081   -934   -406    980  A    C  
ATOM   1456  CD  ARG C 857      36.898  25.283 132.311  1.00 56.05      A    C  
ANISOU 1456  CD  ARG C 857     8295   8269   4732  -1064   -418   1083  A    C  
ATOM   1457  NE  ARG C 857      38.087  26.086 132.059  1.00 57.79      A    N  
ANISOU 1457  NE  ARG C 857     8562   8342   5053   -937   -232   1129  A    N  
ATOM   1458  CZ  ARG C 857      38.329  26.766 130.945  1.00 55.06      A    C  
ANISOU 1458  CZ  ARG C 857     8347   8015   4558   -974   -229   1278  A    C  
ATOM   1459  NH1 ARG C 857      37.465  26.745 129.940  1.00 55.66      A    N1+
ANISOU 1459  NH1 ARG C 857     8537   8262   4350  -1140   -421   1400  A    N1+
ATOM   1460  NH2 ARG C 857      39.454  27.460 130.843  1.00 53.31      A    N  
ANISOU 1460  NH2 ARG C 857     8141   7645   4471   -858    -38   1318  A    N  
ATOM   1461  N   ARG C 858      36.340  27.865 137.585  1.00 41.06      A    N  
ANISOU 1461  N   ARG C 858     5377   6162   4061   -279   -445   1039  A    N  
ATOM   1462  CA  ARG C 858      36.290  29.062 138.418  1.00 42.44      A    C  
ANISOU 1462  CA  ARG C 858     5382   6252   4492    -85   -443   1075  A    C  
ATOM   1463  C   ARG C 858      37.676  29.439 138.936  1.00 40.47      A    C  
ANISOU 1463  C   ARG C 858     5183   5808   4387     -5   -290    975  A    C  
ATOM   1464  O   ARG C 858      38.510  28.568 139.241  1.00 38.06      A    O  
ANISOU 1464  O   ARG C 858     4964   5451   4046    -58   -184    843  A    O  
ATOM   1465  CB  ARG C 858      35.334  28.863 139.606  1.00 38.42      A    C  
ANISOU 1465  CB  ARG C 858     4695   5817   4088    -14   -486   1017  A    C  
ATOM   1466  CG  ARG C 858      33.922  28.505 139.181  1.00 47.03      A    C  
ANISOU 1466  CG  ARG C 858     5681   7108   5080    -97   -645   1136  A    C  
ATOM   1467  CD  ARG C 858      32.867  28.714 140.263  1.00 52.46      A    C  
ANISOU 1467  CD  ARG C 858     6140   7863   5929     21   -670   1143  A    C  
ATOM   1468  NE  ARG C 858      31.577  28.222 139.777  1.00 56.25      A    N  
ANISOU 1468  NE  ARG C 858     6503   8551   6318    -93   -830   1273  A    N  
ATOM   1469  CZ  ARG C 858      30.443  28.210 140.471  1.00 54.85      A    C  
ANISOU 1469  CZ  ARG C 858     6101   8484   6257    -32   -867   1325  A    C  
ATOM   1470  NH1 ARG C 858      30.404  28.675 141.712  1.00 54.27      A    N1+
ANISOU 1470  NH1 ARG C 858     5921   8327   6372    152   -737   1241  A    N1+
ATOM   1471  NH2 ARG C 858      29.339  27.738 139.909  1.00 55.99      A    N  
ANISOU 1471  NH2 ARG C 858     6128   8825   6322   -167  -1034   1465  A    N  
ATOM   1472  N   LEU C 859      37.899  30.744 139.033  1.00 39.17      A    N  
ANISOU 1472  N   LEU C 859     4954   5529   4402    120   -287   1053  A    N  
ATOM   1473  CA  LEU C 859      39.118  31.297 139.594  1.00 38.38      A    C  
ANISOU 1473  CA  LEU C 859     4869   5240   4472    185   -177    976  A    C  
ATOM   1474  C   LEU C 859      38.890  31.451 141.088  1.00 37.24      A    C  
ANISOU 1474  C   LEU C 859     4617   5057   4476    286   -179    842  A    C  
ATOM   1475  O   LEU C 859      38.058  32.265 141.502  1.00 36.77      A    O  
ANISOU 1475  O   LEU C 859     4455   4990   4527    397   -228    881  A    O  
ATOM   1476  CB  LEU C 859      39.453  32.644 138.945  1.00 40.85      A    C  
ANISOU 1476  CB  LEU C 859     5187   5430   4904    247   -173   1125  A    C  
ATOM   1477  CG  LEU C 859      40.874  33.153 139.157  1.00 41.46      A    C  
ANISOU 1477  CG  LEU C 859     5301   5316   5135    257    -61   1081  A    C  
ATOM   1478  CD1 LEU C 859      41.865  32.203 138.465  1.00 39.96      A    C  
ANISOU 1478  CD1 LEU C 859     5231   5141   4810    138     53   1060  A    C  
ATOM   1479  CD2 LEU C 859      40.990  34.599 138.666  1.00 36.90      A    C  
ANISOU 1479  CD2 LEU C 859     4710   4599   4710    326    -69   1236  A    C  
ATOM   1480  N   LEU C 860      39.601  30.662 141.892  1.00 32.53      A    N  
ANISOU 1480  N   LEU C 860     4047   4435   3876    251   -117    693  A    N  
ATOM   1481  CA  LEU C 860      39.329  30.627 143.330  1.00 34.87      A    C  
ANISOU 1481  CA  LEU C 860     4272   4728   4251    320   -124    563  A    C  
ATOM   1482  C   LEU C 860      40.571  30.786 144.225  1.00 33.99      A    C  
ANISOU 1482  C   LEU C 860     4182   4480   4253    326    -78    450  A    C  
ATOM   1483  O   LEU C 860      41.699  30.583 143.801  1.00 32.76      A    O  
ANISOU 1483  O   LEU C 860     4074   4254   4120    267    -27    465  A    O  
ATOM   1484  CB  LEU C 860      38.612  29.322 143.699  1.00 34.15      A    C  
ANISOU 1484  CB  LEU C 860     4167   4795   4014    258   -139    505  A    C  
ATOM   1485  CG  LEU C 860      37.278  29.041 142.998  1.00 35.06      A    C  
ANISOU 1485  CG  LEU C 860     4232   5070   4018    221   -217    610  A    C  
ATOM   1486  CD1 LEU C 860      36.816  27.593 143.226  1.00 34.27      A    C  
ANISOU 1486  CD1 LEU C 860     4149   5100   3773    111   -222    549  A    C  
ATOM   1487  CD2 LEU C 860      36.218  30.023 143.466  1.00 33.11      A    C  
ANISOU 1487  CD2 LEU C 860     3844   4844   3894    356   -259    664  A    C  
ATOM   1488  N   TRP C 861      40.318  31.144 145.481  1.00 34.59      A    N  
ANISOU 1488  N   TRP C 861     4219   4528   4396    395    -95    342  A    N  
ATOM   1489  CA  TRP C 861      41.354  31.430 146.456  1.00 35.30      A    C  
ANISOU 1489  CA  TRP C 861     4330   4501   4580    387    -93    235  A    C  
ATOM   1490  C   TRP C 861      41.783  30.169 147.195  1.00 36.26      A    C  
ANISOU 1490  C   TRP C 861     4462   4703   4612    323    -91    158  A    C  
ATOM   1491  O   TRP C 861      40.939  29.343 147.553  1.00 31.55      A    O  
ANISOU 1491  O   TRP C 861     3854   4236   3897    323    -89    130  A    O  
ATOM   1492  CB  TRP C 861      40.860  32.454 147.484  1.00 32.22      A    C  
ANISOU 1492  CB  TRP C 861     3937   4033   4273    480   -108    140  A    C  
ATOM   1493  CG  TRP C 861      40.500  33.791 146.918  1.00 36.51      A    C  
ANISOU 1493  CG  TRP C 861     4472   4451   4950    564    -98    216  A    C  
ATOM   1494  CD1 TRP C 861      39.240  34.310 146.763  1.00 39.91      A    C  
ANISOU 1494  CD1 TRP C 861     4848   4910   5405    679    -82    273  A    C  
ATOM   1495  CD2 TRP C 861      41.413  34.804 146.472  1.00 38.56      A    C  
ANISOU 1495  CD2 TRP C 861     4765   4525   5363    546    -99    260  A    C  
ATOM   1496  CE2 TRP C 861      40.636  35.902 146.036  1.00 42.72      A    C  
ANISOU 1496  CE2 TRP C 861     5275   4963   5994    656    -82    345  A    C  
ATOM   1497  CE3 TRP C 861      42.810  34.879 146.381  1.00 38.46      A    C  
ANISOU 1497  CE3 TRP C 861     4777   4409   5428    446   -109    257  A    C  
ATOM   1498  NE1 TRP C 861      39.319  35.585 146.236  1.00 44.21      A    N  
ANISOU 1498  NE1 TRP C 861     5401   5287   6109    744    -73    355  A    N  
ATOM   1499  CZ2 TRP C 861      41.218  37.068 145.527  1.00 43.30      A    C  
ANISOU 1499  CZ2 TRP C 861     5380   4835   6237    663    -72    419  A    C  
ATOM   1500  CZ3 TRP C 861      43.382  36.037 145.873  1.00 42.32      A    C  
ANISOU 1500  CZ3 TRP C 861     5282   4711   6085    441   -100    328  A    C  
ATOM   1501  CH2 TRP C 861      42.584  37.119 145.459  1.00 41.90      A    C  
ANISOU 1501  CH2 TRP C 861     5238   4561   6124    546    -81    403  A    C  
ATOM   1502  N   HIS C 862      43.091  30.029 147.399  1.00 35.60      A    N  
ANISOU 1502  N   HIS C 862     4385   4538   4602    268    -93    146  A    N  
ATOM   1503  CA  HIS C 862      43.632  29.038 148.324  1.00 34.21      A    C  
ANISOU 1503  CA  HIS C 862     4204   4410   4383    224   -111     88  A    C  
ATOM   1504  C   HIS C 862      44.704  29.680 149.195  1.00 34.84      A    C  
ANISOU 1504  C   HIS C 862     4270   4385   4583    195   -183     37  A    C  
ATOM   1505  O   HIS C 862      45.789  30.038 148.715  1.00 34.24      A    O  
ANISOU 1505  O   HIS C 862     4158   4208   4643    153   -179    101  A    O  
ATOM   1506  CB  HIS C 862      44.228  27.827 147.599  1.00 32.43      A    C  
ANISOU 1506  CB  HIS C 862     3981   4214   4126    171    -39    161  A    C  
ATOM   1507  CG  HIS C 862      44.794  26.805 148.537  1.00 33.15      A    C  
ANISOU 1507  CG  HIS C 862     4054   4339   4203    143    -57    134  A    C  
ATOM   1508  CD2 HIS C 862      45.993  26.736 149.166  1.00 33.22      A    C  
ANISOU 1508  CD2 HIS C 862     4010   4291   4323    117   -100    150  A    C  
ATOM   1509  ND1 HIS C 862      44.077  25.709 148.964  1.00 38.08      A    N  
ANISOU 1509  ND1 HIS C 862     4703   5069   4694    136    -43    108  A    N  
ATOM   1510  CE1 HIS C 862      44.817  24.994 149.798  1.00 38.03      A    C  
ANISOU 1510  CE1 HIS C 862     4674   5063   4713    118    -68    114  A    C  
ATOM   1511  NE2 HIS C 862      45.982  25.599 149.938  1.00 36.39      A    N  
ANISOU 1511  NE2 HIS C 862     4410   4765   4651    107   -113    144  A    N  
ATOM   1512  N   GLY C 863      44.404  29.815 150.479  1.00 32.51      A    N  
ANISOU 1512  N   GLY C 863     4006   4117   4228    203   -249    -74  A    N  
ATOM   1513  CA  GLY C 863      45.362  30.374 151.415  1.00 36.42      A    C  
ANISOU 1513  CA  GLY C 863     4511   4530   4797    143   -351   -137  A    C  
ATOM   1514  C   GLY C 863      46.157  29.281 152.107  1.00 36.99      A    C  
ANISOU 1514  C   GLY C 863     4545   4677   4834     80   -412   -108  A    C  
ATOM   1515  O   GLY C 863      45.700  28.138 152.201  1.00 35.89      A    O  
ANISOU 1515  O   GLY C 863     4404   4651   4582    100   -368    -82  A    O  
ATOM   1516  N   SER C 864      47.348  29.624 152.588  1.00 34.16      A    N  
ANISOU 1516  N   SER C 864     4146   4250   4585     -2   -522    -96  A    N  
ATOM   1517  CA  SER C 864      48.162  28.668 153.325  1.00 36.22      A    C  
ANISOU 1517  CA  SER C 864     4346   4581   4834    -59   -609    -38  A    C  
ATOM   1518  C   SER C 864      49.224  29.414 154.104  1.00 38.59      A    C  
ANISOU 1518  C   SER C 864     4620   4814   5229   -170   -784    -57  A    C  
ATOM   1519  O   SER C 864      49.468  30.599 153.853  1.00 40.52      A    O  
ANISOU 1519  O   SER C 864     4882   4932   5583   -210   -812   -102  A    O  
ATOM   1520  CB  SER C 864      48.807  27.643 152.375  1.00 35.94      A    C  
ANISOU 1520  CB  SER C 864     4199   4550   4905    -38   -507    120  A    C  
ATOM   1521  OG  SER C 864      49.350  26.550 153.100  1.00 38.24      A    O  
ANISOU 1521  OG  SER C 864     4433   4915   5181    -57   -564    193  A    O  
ATOM   1522  N   ARG C 865      49.852  28.739 155.056  1.00 39.18      A    N  
ANISOU 1522  N   ARG C 865     4655   4969   5263   -234   -916    -13  A    N  
ATOM   1523  CA  ARG C 865      50.984  29.344 155.765  1.00 45.23      A    C  
ANISOU 1523  CA  ARG C 865     5370   5690   6126   -373  -1122     -1  A    C  
ATOM   1524  C   ARG C 865      52.136  29.586 154.801  1.00 43.48      A    C  
ANISOU 1524  C   ARG C 865     4963   5367   6190   -406  -1101    151  A    C  
ATOM   1525  O   ARG C 865      52.333  28.831 153.844  1.00 39.95      A    O  
ANISOU 1525  O   ARG C 865     4410   4923   5846   -323   -944    283  A    O  
ATOM   1526  CB  ARG C 865      51.461  28.454 156.912  1.00 50.62      A    C  
ANISOU 1526  CB  ARG C 865     6022   6502   6710   -434  -1285     64  A    C  
ATOM   1527  CG  ARG C 865      50.497  28.326 158.064  1.00 52.62      A    C  
ANISOU 1527  CG  ARG C 865     6470   6860   6665   -435  -1329    -81  A    C  
ATOM   1528  CD  ARG C 865      51.076  27.379 159.102  1.00 60.05      A    C  
ANISOU 1528  CD  ARG C 865     7369   7933   7515   -500  -1497     32  A    C  
ATOM   1529  NE  ARG C 865      50.180  27.211 160.238  1.00 64.21      A    N  
ANISOU 1529  NE  ARG C 865     8096   8571   7732   -509  -1525    -94  A    N  
ATOM   1530  CZ  ARG C 865      50.311  27.867 161.382  1.00 70.81      A    C  
ANISOU 1530  CZ  ARG C 865     9082   9434   8389   -639  -1705   -216  A    C  
ATOM   1531  NH1 ARG C 865      51.300  28.745 161.541  1.00 74.21      A    N1+
ANISOU 1531  NH1 ARG C 865     9479   9783   8933   -786  -1899   -231  A    N1+
ATOM   1532  NH2 ARG C 865      49.448  27.650 162.364  1.00 73.17      A    N  
ANISOU 1532  NH2 ARG C 865     9574   9837   8389   -633  -1684   -325  A    N  
ATOM   1533  N   THR C 866      52.892  30.646 155.048  1.00 44.22      A    N  
ANISOU 1533  N   THR C 866     5028   5361   6411   -535  -1245    128  A    N  
ATOM   1534  CA  THR C 866      54.012  30.994 154.189  1.00 45.21      A    C  
ANISOU 1534  CA  THR C 866     4965   5387   6827   -585  -1223    281  A    C  
ATOM   1535  C   THR C 866      55.031  29.857 154.115  1.00 45.69      A    C  
ANISOU 1535  C   THR C 866     4798   5524   7037   -574  -1231    500  A    C  
ATOM   1536  O   THR C 866      55.646  29.639 153.068  1.00 45.32      A    O  
ANISOU 1536  O   THR C 866     4597   5422   7200   -524  -1075    651  A    O  
ATOM   1537  CB  THR C 866      54.690  32.296 154.684  1.00 46.24      A    C  
ANISOU 1537  CB  THR C 866     5102   5399   7068   -766  -1419    219  A    C  
ATOM   1538  CG2 THR C 866      55.977  32.584 153.920  1.00 46.80      A    C  
ANISOU 1538  CG2 THR C 866     4934   5382   7466   -841  -1413    411  A    C  
ATOM   1539  OG1 THR C 866      53.779  33.384 154.490  1.00 48.00      A    O  
ANISOU 1539  OG1 THR C 866     5524   5500   7213   -741  -1346     39  A    O  
ATOM   1540  N   THR C 867      55.186  29.122 155.217  1.00 44.73      A    N  
ANISOU 1540  N   THR C 867     4664   5526   6805   -609  -1395    526  A    N  
ATOM   1541  CA  THR C 867      56.147  28.012 155.282  1.00 45.94      A    C  
ANISOU 1541  CA  THR C 867     4592   5748   7117   -584  -1418    756  A    C  
ATOM   1542  C   THR C 867      55.750  26.823 154.399  1.00 45.43      A    C  
ANISOU 1542  C   THR C 867     4511   5694   7057   -402  -1141    836  A    C  
ATOM   1543  O   THR C 867      56.496  25.845 154.287  1.00 49.41      A    O  
ANISOU 1543  O   THR C 867     4838   6218   7719   -345  -1094   1028  A    O  
ATOM   1544  CB  THR C 867      56.308  27.509 156.724  1.00 47.10      A    C  
ANISOU 1544  CB  THR C 867     4752   6030   7113   -665  -1675    779  A    C  
ATOM   1545  CG2 THR C 867      57.093  28.506 157.547  1.00 43.47      A    C  
ANISOU 1545  CG2 THR C 867     4256   5561   6700   -880  -1979    758  A    C  
ATOM   1546  OG1 THR C 867      55.000  27.342 157.297  1.00 48.53      A    O  
ANISOU 1546  OG1 THR C 867     5193   6281   6965   -618  -1645    590  A    O  
ATOM   1547  N   ASN C 868      54.572  26.894 153.785  1.00 42.04      A    N  
ANISOU 1547  N   ASN C 868     4268   5246   6460   -316   -963    692  A    N  
ATOM   1548  CA  ASN C 868      54.115  25.812 152.924  1.00 42.34      A    C  
ANISOU 1548  CA  ASN C 868     4330   5288   6470   -178   -716    738  A    C  
ATOM   1549  C   ASN C 868      54.330  26.063 151.444  1.00 43.90      A    C  
ANISOU 1549  C   ASN C 868     4492   5379   6810   -126   -486    786  A    C  
ATOM   1550  O   ASN C 868      54.094  25.173 150.621  1.00 40.08      A    O  
ANISOU 1550  O   ASN C 868     4039   4880   6309    -30   -270    824  A    O  
ATOM   1551  CB  ASN C 868      52.631  25.544 153.162  1.00 38.65      A    C  
ANISOU 1551  CB  ASN C 868     4079   4892   5714   -130   -671    576  A    C  
ATOM   1552  CG  ASN C 868      52.362  25.000 154.544  1.00 41.14      A    C  
ANISOU 1552  CG  ASN C 868     4445   5324   5861   -160   -836    553  A    C  
ATOM   1553  ND2 ASN C 868      51.120  25.108 154.997  1.00 42.38      A    N  
ANISOU 1553  ND2 ASN C 868     4781   5547   5775   -147   -832    398  A    N  
ATOM   1554  OD1 ASN C 868      53.269  24.503 155.205  1.00 43.32      A    O  
ANISOU 1554  OD1 ASN C 868     4594   5636   6230   -196   -964    690  A    O  
ATOM   1555  N   PHE C 869      54.731  27.279 151.085  1.00 40.46      A    N  
ANISOU 1555  N   PHE C 869     4017   4860   6495   -198   -523    776  A    N  
ATOM   1556  CA  PHE C 869      54.641  27.640 149.674  1.00 42.16      A    C  
ANISOU 1556  CA  PHE C 869     4261   4988   6772   -151   -300    798  A    C  
ATOM   1557  C   PHE C 869      55.793  27.118 148.814  1.00 44.67      A    C  
ANISOU 1557  C   PHE C 869     4397   5244   7333   -111   -114    990  A    C  
ATOM   1558  O   PHE C 869      55.628  26.970 147.603  1.00 43.47      A    O  
ANISOU 1558  O   PHE C 869     4307   5042   7167    -48    124   1011  A    O  
ATOM   1559  CB  PHE C 869      54.491  29.158 149.519  1.00 42.84      A    C  
ANISOU 1559  CB  PHE C 869     4401   4989   6887   -230   -377    721  A    C  
ATOM   1560  CG  PHE C 869      53.057  29.605 149.535  1.00 41.77      A    C  
ANISOU 1560  CG  PHE C 869     4480   4874   6515   -191   -378    549  A    C  
ATOM   1561  CD1 PHE C 869      52.396  29.837 150.735  1.00 43.25      A    C  
ANISOU 1561  CD1 PHE C 869     4770   5117   6546   -221   -549    404  A    C  
ATOM   1562  CD2 PHE C 869      52.351  29.734 148.354  1.00 43.93      A    C  
ANISOU 1562  CD2 PHE C 869     4850   5123   6716   -122   -201    547  A    C  
ATOM   1563  CE1 PHE C 869      51.061  30.221 150.751  1.00 44.65      A    C  
ANISOU 1563  CE1 PHE C 869     5116   5314   6536   -165   -521    264  A    C  
ATOM   1564  CE2 PHE C 869      51.016  30.122 148.358  1.00 46.69      A    C  
ANISOU 1564  CE2 PHE C 869     5359   5503   6878    -78   -210    422  A    C  
ATOM   1565  CZ  PHE C 869      50.370  30.368 149.554  1.00 45.64      A    C  
ANISOU 1565  CZ  PHE C 869     5300   5415   6628    -90   -358    284  A    C  
ATOM   1566  N   ALA C 870      56.945  26.824 149.415  1.00 43.50      A    N  
ANISOU 1566  N   ALA C 870     4026   5101   7401   -145   -213   1137  A    N  
ATOM   1567  CA  ALA C 870      57.997  26.186 148.652  1.00 47.61      A    C  
ANISOU 1567  CA  ALA C 870     4356   5563   8171    -75      1   1333  A    C  
ATOM   1568  C   ALA C 870      57.494  24.825 148.178  1.00 48.47      A    C  
ANISOU 1568  C   ALA C 870     4578   5681   8158     65    231   1322  A    C  
ATOM   1569  O   ALA C 870      57.672  24.452 147.013  1.00 48.08      A    O  
ANISOU 1569  O   ALA C 870     4556   5556   8156    143    522   1369  A    O  
ATOM   1570  CB  ALA C 870      59.260  26.039 149.483  1.00 52.74      A    C  
ANISOU 1570  CB  ALA C 870     4716   6234   9090   -129   -171   1519  A    C  
ATOM   1571  N   GLY C 871      56.855  24.098 149.093  1.00 46.12      A    N  
ANISOU 1571  N   GLY C 871     4365   5466   7690     83    104   1255  A    N  
ATOM   1572  CA  GLY C 871      56.263  22.802 148.795  1.00 42.58      A    C  
ANISOU 1572  CA  GLY C 871     4047   5017   7112    189    288   1227  A    C  
ATOM   1573  C   GLY C 871      55.150  22.892 147.774  1.00 43.39      A    C  
ANISOU 1573  C   GLY C 871     4398   5105   6983    204    456   1073  A    C  
ATOM   1574  O   GLY C 871      55.052  22.056 146.867  1.00 47.86      A    O  
ANISOU 1574  O   GLY C 871     5055   5610   7519    275    710   1079  A    O  
ATOM   1575  N   ILE C 872      54.310  23.912 147.913  1.00 40.21      A    N  
ANISOU 1575  N   ILE C 872     4108   4752   6417    133    314    939  A    N  
ATOM   1576  CA  ILE C 872      53.200  24.122 146.992  1.00 37.85      A    C  
ANISOU 1576  CA  ILE C 872     4018   4460   5904    137    424    819  A    C  
ATOM   1577  C   ILE C 872      53.659  24.494 145.587  1.00 38.54      A    C  
ANISOU 1577  C   ILE C 872     4118   4459   6068    149    644    881  A    C  
ATOM   1578  O   ILE C 872      53.106  24.008 144.615  1.00 37.29      A    O  
ANISOU 1578  O   ILE C 872     4121   4290   5758    173    823    840  A    O  
ATOM   1579  CB  ILE C 872      52.251  25.203 147.524  1.00 36.99      A    C  
ANISOU 1579  CB  ILE C 872     3994   4412   5649     80    227    689  A    C  
ATOM   1580  CG1 ILE C 872      51.482  24.648 148.728  1.00 40.05      A    C  
ANISOU 1580  CG1 ILE C 872     4438   4903   5878     79     79    604  A    C  
ATOM   1581  CG2 ILE C 872      51.278  25.667 146.440  1.00 39.51      A    C  
ANISOU 1581  CG2 ILE C 872     4472   4730   5809     85    325    621  A    C  
ATOM   1582  CD1 ILE C 872      50.714  25.707 149.502  1.00 39.12      A    C  
ANISOU 1582  CD1 ILE C 872     4384   4832   5648     36   -104    479  A    C  
ATOM   1583  N   LEU C 873      54.661  25.358 145.461  1.00 40.02      A    N  
ANISOU 1583  N   LEU C 873     4146   4583   6476    116    631    984  A    N  
ATOM   1584  CA  LEU C 873      55.149  25.683 144.126  1.00 42.10      A    C  
ANISOU 1584  CA  LEU C 873     4420   4764   6811    127    868   1064  A    C  
ATOM   1585  C   LEU C 873      55.935  24.507 143.497  1.00 44.00      A    C  
ANISOU 1585  C   LEU C 873     4618   4940   7162    214   1154   1165  A    C  
ATOM   1586  O   LEU C 873      55.807  24.253 142.299  1.00 45.15      A    O  
ANISOU 1586  O   LEU C 873     4908   5040   7205    241   1405   1159  A    O  
ATOM   1587  CB  LEU C 873      55.998  26.960 144.169  1.00 45.80      A    C  
ANISOU 1587  CB  LEU C 873     4722   5173   7506     56    784   1158  A    C  
ATOM   1588  CG  LEU C 873      55.180  28.221 144.507  1.00 45.56      A    C  
ANISOU 1588  CG  LEU C 873     4787   5156   7368    -18    572   1049  A    C  
ATOM   1589  CD1 LEU C 873      56.069  29.457 144.523  1.00 45.32      A    C  
ANISOU 1589  CD1 LEU C 873     4607   5035   7579   -107    500   1140  A    C  
ATOM   1590  CD2 LEU C 873      54.007  28.415 143.547  1.00 43.13      A    C  
ANISOU 1590  CD2 LEU C 873     4708   4869   6808      7    666    970  A    C  
ATOM   1591  N   SER C 874      56.735  23.766 144.268  1.00 40.31      A    N  
ANISOU 1591  N   SER C 874     3964   4460   6893    262   1131   1262  A    N  
ATOM   1592  CA  SER C 874      57.496  22.697 143.624  1.00 45.30      A    C  
ANISOU 1592  CA  SER C 874     4551   5000   7662    369   1443   1367  A    C  
ATOM   1593  C   SER C 874      56.620  21.493 143.254  1.00 44.89      A    C  
ANISOU 1593  C   SER C 874     4753   4935   7369    422   1596   1243  A    C  
ATOM   1594  O   SER C 874      56.847  20.869 142.227  1.00 46.35      A    O  
ANISOU 1594  O   SER C 874     5048   5025   7536    481   1912   1250  A    O  
ATOM   1595  CB  SER C 874      58.676  22.225 144.492  1.00 51.57      A    C  
ANISOU 1595  CB  SER C 874     5038   5772   8783    423   1389   1550  A    C  
ATOM   1596  OG  SER C 874      58.273  21.780 145.762  1.00 51.79      A    O  
ANISOU 1596  OG  SER C 874     5048   5883   8748    410   1127   1517  A    O  
ATOM   1597  N   GLN C 875      55.617  21.180 144.071  1.00 42.62      A    N  
ANISOU 1597  N   GLN C 875     4570   4735   6890    389   1385   1127  A    N  
ATOM   1598  CA  GLN C 875      54.831  19.963 143.865  1.00 44.71      A    C  
ANISOU 1598  CA  GLN C 875     5048   4980   6960    419   1506   1025  A    C  
ATOM   1599  C   GLN C 875      53.378  20.221 143.475  1.00 43.65      A    C  
ANISOU 1599  C   GLN C 875     5165   4931   6490    331   1424    851  A    C  
ATOM   1600  O   GLN C 875      52.657  19.292 143.101  1.00 43.56      A    O  
ANISOU 1600  O   GLN C 875     5353   4903   6296    320   1528    758  A    O  
ATOM   1601  CB  GLN C 875      54.876  19.095 145.126  1.00 41.10      A    C  
ANISOU 1601  CB  GLN C 875     4494   4545   6577    459   1367   1069  A    C  
ATOM   1602  CG  GLN C 875      56.283  18.616 145.443  1.00 47.30      A    C  
ANISOU 1602  CG  GLN C 875     5023   5241   7707    562   1463   1273  A    C  
ATOM   1603  CD  GLN C 875      56.294  17.480 146.437  1.00 57.75      A    C  
ANISOU 1603  CD  GLN C 875     6298   6556   9087    623   1396   1338  A    C  
ATOM   1604  NE2 GLN C 875      57.491  17.052 146.831  1.00 59.70      A    N  
ANISOU 1604  NE2 GLN C 875     6291   6739   9654    720   1441   1549  A    N  
ATOM   1605  OE1 GLN C 875      55.239  16.983 146.846  1.00 58.92      A    O  
ANISOU 1605  OE1 GLN C 875     6623   6756   9008    583   1306   1220  A    O  
ATOM   1606  N   GLY C 876      52.952  21.480 143.562  1.00 40.61      A    N  
ANISOU 1606  N   GLY C 876     4761   4628   6039    264   1237    818  A    N  
ATOM   1607  CA  GLY C 876      51.556  21.829 143.350  1.00 36.34      A    C  
ANISOU 1607  CA  GLY C 876     4402   4184   5223    195   1122    687  A    C  
ATOM   1608  C   GLY C 876      50.728  21.536 144.593  1.00 37.46      A    C  
ANISOU 1608  C   GLY C 876     4533   4423   5276    180    904    615  A    C  
ATOM   1609  O   GLY C 876      51.228  20.970 145.569  1.00 39.72      A    O  
ANISOU 1609  O   GLY C 876     4705   4702   5684    216    847    665  A    O  
ATOM   1610  N   LEU C 877      49.460  21.919 144.558  1.00 32.89      A    N  
ANISOU 1610  N   LEU C 877     4068   3941   4490    128    788    516  A    N  
ATOM   1611  CA  LEU C 877      48.534  21.557 145.614  1.00 35.51      A    C  
ANISOU 1611  CA  LEU C 877     4411   4369   4710    113    631    446  A    C  
ATOM   1612  C   LEU C 877      48.311  20.045 145.590  1.00 37.44      A    C  
ANISOU 1612  C   LEU C 877     4751   4587   4887    111    747    429  A    C  
ATOM   1613  O   LEU C 877      48.107  19.453 144.527  1.00 34.21      A    O  
ANISOU 1613  O   LEU C 877     4489   4127   4381     81    911    400  A    O  
ATOM   1614  CB  LEU C 877      47.211  22.313 145.452  1.00 36.88      A    C  
ANISOU 1614  CB  LEU C 877     4661   4646   4707     70    516    366  A    C  
ATOM   1615  CG  LEU C 877      47.297  23.802 145.811  1.00 38.09      A    C  
ANISOU 1615  CG  LEU C 877     4725   4807   4940     83    380    369  A    C  
ATOM   1616  CD1 LEU C 877      45.972  24.504 145.564  1.00 34.01      A    C  
ANISOU 1616  CD1 LEU C 877     4270   4373   4279     70    299    315  A    C  
ATOM   1617  CD2 LEU C 877      47.731  23.979 147.271  1.00 35.17      A    C  
ANISOU 1617  CD2 LEU C 877     4244   4451   4667     99    237    359  A    C  
ATOM   1618  N   ARG C 878      48.360  19.428 146.764  1.00 33.16      A    N  
ANISOU 1618  N   ARG C 878     4142   4069   4386    133    662    449  A    N  
ATOM   1619  CA  ARG C 878      48.274  17.987 146.858  1.00 34.13      A    C  
ANISOU 1619  CA  ARG C 878     4342   4136   4489    139    775    457  A    C  
ATOM   1620  C   ARG C 878      47.225  17.610 147.876  1.00 35.88      A    C  
ANISOU 1620  C   ARG C 878     4589   4469   4576     98    633    410  A    C  
ATOM   1621  O   ARG C 878      46.798  18.436 148.664  1.00 32.64      A    O  
ANISOU 1621  O   ARG C 878     4114   4170   4118     89    460    383  A    O  
ATOM   1622  CB  ARG C 878      49.630  17.371 147.222  1.00 35.74      A    C  
ANISOU 1622  CB  ARG C 878     4420   4226   4932    227    863    588  A    C  
ATOM   1623  CG  ARG C 878      50.608  17.375 146.022  1.00 41.78      A    C  
ANISOU 1623  CG  ARG C 878     5188   4855   5833    275   1100    638  A    C  
ATOM   1624  CD  ARG C 878      51.946  16.767 146.361  1.00 46.78      A    C  
ANISOU 1624  CD  ARG C 878     5656   5373   6744    382   1205    795  A    C  
ATOM   1625  NE  ARG C 878      51.840  15.373 146.792  1.00 55.66      A    N  
ANISOU 1625  NE  ARG C 878     6837   6421   7888    423   1287    824  A    N  
ATOM   1626  CZ  ARG C 878      51.781  14.326 145.971  1.00 56.94      A    C  
ANISOU 1626  CZ  ARG C 878     7172   6435   8028    445   1549    782  A    C  
ATOM   1627  NH1 ARG C 878      51.806  14.501 144.654  1.00 58.74      A    N1+
ANISOU 1627  NH1 ARG C 878     7546   6592   8182    423   1755    702  A    N1+
ATOM   1628  NH2 ARG C 878      51.695  13.100 146.471  1.00 52.82      A    N  
ANISOU 1628  NH2 ARG C 878     6696   5825   7549    482   1609    820  A    N  
ATOM   1629  N   ILE C 879      46.806  16.355 147.825  1.00 34.14      A    N  
ANISOU 1629  N   ILE C 879     4475   4202   4293     71    728    397  A    N  
ATOM   1630  CA  ILE C 879      45.800  15.836 148.728  1.00 33.34      A    C  
ANISOU 1630  CA  ILE C 879     4402   4195   4071     22    629    370  A    C  
ATOM   1631  C   ILE C 879      46.486  15.096 149.860  1.00 33.72      A    C  
ANISOU 1631  C   ILE C 879     4367   4206   4238     83    603    482  A    C  
ATOM   1632  O   ILE C 879      47.550  14.519 149.658  1.00 35.02      A    O  
ANISOU 1632  O   ILE C 879     4495   4233   4576    153    722    574  A    O  
ATOM   1633  CB  ILE C 879      44.833  14.920 147.949  1.00 33.06      A    C  
ANISOU 1633  CB  ILE C 879     4542   4130   3891    -78    732    294  A    C  
ATOM   1634  CG1 ILE C 879      44.098  15.761 146.896  1.00 33.83      A    C  
ANISOU 1634  CG1 ILE C 879     4702   4302   3851   -149    704    211  A    C  
ATOM   1635  CG2 ILE C 879      43.836  14.211 148.865  1.00 32.89      A    C  
ANISOU 1635  CG2 ILE C 879     4538   4188   3772   -139    659    290  A    C  
ATOM   1636  CD1 ILE C 879      43.175  14.941 146.002  1.00 33.70      A    C  
ANISOU 1636  CD1 ILE C 879     4864   4268   3672   -283    774    136  A    C  
ATOM   1637  N   ALA C 880      45.889  15.126 151.052  1.00 33.79      A    N  
ANISOU 1637  N   ALA C 880     4343   4339   4159     62    457    490  A    N  
ATOM   1638  CA  ALA C 880      46.360  14.275 152.132  1.00 36.94      A    C  
ANISOU 1638  CA  ALA C 880     4693   4717   4625    100    423    613  A    C  
ATOM   1639  C   ALA C 880      46.401  12.803 151.682  1.00 38.16      A    C  
ANISOU 1639  C   ALA C 880     4948   4712   4839    101    608    658  A    C  
ATOM   1640  O   ALA C 880      45.516  12.349 150.959  1.00 35.60      A    O  
ANISOU 1640  O   ALA C 880     4763   4359   4404     19    703    561  A    O  
ATOM   1641  CB  ALA C 880      45.459  14.445 153.388  1.00 30.25      A    C  
ANISOU 1641  CB  ALA C 880     3847   4036   3610     55    272    596  A    C  
ATOM   1642  N   PRO C 881      47.430  12.057 152.122  1.00 38.42      A    N  
ANISOU 1642  N   PRO C 881     4910   4634   5055    189    653    813  A    N  
ATOM   1643  CA  PRO C 881      47.675  10.660 151.704  1.00 36.67      A    C  
ANISOU 1643  CA  PRO C 881     4780   4208   4943    221    861    872  A    C  
ATOM   1644  C   PRO C 881      46.632   9.645 152.177  1.00 42.11      A    C  
ANISOU 1644  C   PRO C 881     5597   4894   5508    137    875    862  A    C  
ATOM   1645  O   PRO C 881      45.809   9.943 153.063  1.00 40.54      A    O  
ANISOU 1645  O   PRO C 881     5382   4871   5151     72    717    850  A    O  
ATOM   1646  CB  PRO C 881      49.047  10.333 152.330  1.00 44.05      A    C  
ANISOU 1646  CB  PRO C 881     5545   5063   6130    357    852   1086  A    C  
ATOM   1647  CG  PRO C 881      49.222  11.349 153.458  1.00 46.56      A    C  
ANISOU 1647  CG  PRO C 881     5710   5588   6393    345    575   1141  A    C  
ATOM   1648  CD  PRO C 881      48.526  12.603 152.946  1.00 40.00      A    C  
ANISOU 1648  CD  PRO C 881     4924   4882   5394    265    508    950  A    C  
ATOM   1649  N   PRO C 882      46.672   8.430 151.593  1.00 39.62      A    N  
ANISOU 1649  N   PRO C 882     5418   4365   5271    136   1084    867  A    N  
ATOM   1650  CA  PRO C 882      45.761   7.363 151.984  1.00 45.02      A    C  
ANISOU 1650  CA  PRO C 882     6229   5005   5871     42   1117    871  A    C  
ATOM   1651  C   PRO C 882      45.751   7.117 153.476  1.00 41.07      A    C  
ANISOU 1651  C   PRO C 882     5625   4608   5371     73    967   1041  A    C  
ATOM   1652  O   PRO C 882      44.692   6.861 154.013  1.00 40.84      A    O  
ANISOU 1652  O   PRO C 882     5654   4678   5187    -35    906   1019  A    O  
ATOM   1653  CB  PRO C 882      46.320   6.148 151.250  1.00 49.20      A    C  
ANISOU 1653  CB  PRO C 882     6892   5232   6569     90   1379    893  A    C  
ATOM   1654  CG  PRO C 882      46.899   6.734 150.023  1.00 50.06      A    C  
ANISOU 1654  CG  PRO C 882     7029   5275   6716    128   1504    786  A    C  
ATOM   1655  CD  PRO C 882      47.500   8.037 150.439  1.00 43.68      A    C  
ANISOU 1655  CD  PRO C 882     6001   4655   5942    207   1326    845  A    C  
ATOM   1656  N   GLU C 883      46.904   7.212 154.130  1.00 41.38      A    N  
ANISOU 1656  N   GLU C 883     5509   4637   5577    208    903   1219  A    N  
ATOM   1657  CA  GLU C 883      46.965   6.878 155.549  1.00 46.51      A    C  
ANISOU 1657  CA  GLU C 883     6082   5380   6209    229    754   1406  A    C  
ATOM   1658  C   GLU C 883      46.499   8.036 156.441  1.00 43.00      A    C  
ANISOU 1658  C   GLU C 883     5567   5219   5551    170    513   1360  A    C  
ATOM   1659  O   GLU C 883      46.324   7.849 157.637  1.00 42.87      A    O  
ANISOU 1659  O   GLU C 883     5531   5318   5441    154    386   1480  A    O  
ATOM   1660  CB  GLU C 883      48.375   6.443 155.944  1.00 52.70      A    C  
ANISOU 1660  CB  GLU C 883     6719   6048   7258    386    755   1648  A    C  
ATOM   1661  CG  GLU C 883      49.454   7.269 155.329  1.00 59.99      A    C  
ANISOU 1661  CG  GLU C 883     7497   6954   8345    477    757   1644  A    C  
ATOM   1662  CD  GLU C 883      49.928   6.671 154.009  1.00 65.72      A    C  
ANISOU 1662  CD  GLU C 883     8292   7413   9265    552   1057   1596  A    C  
ATOM   1663  OE1 GLU C 883      50.616   5.619 154.034  1.00 70.53      A    O  
ANISOU 1663  OE1 GLU C 883     8879   7809  10109    670   1211   1765  A    O  
ATOM   1664  OE2 GLU C 883      49.583   7.236 152.954  1.00 57.80      A    O1-
ANISOU 1664  OE2 GLU C 883     7381   6407   8172    494   1147   1391  A    O1-
ATOM   1665  N   ALA C 884      46.297   9.217 155.864  1.00 36.97      A    N  
ANISOU 1665  N   ALA C 884     4783   4557   4707    140    466   1189  A    N  
ATOM   1666  CA  ALA C 884      45.729  10.313 156.643  1.00 35.91      A    C  
ANISOU 1666  CA  ALA C 884     4616   4657   4371     85    279   1115  A    C  
ATOM   1667  C   ALA C 884      44.264  10.012 156.935  1.00 37.69      A    C  
ANISOU 1667  C   ALA C 884     4950   4979   4393    -22    306   1035  A    C  
ATOM   1668  O   ALA C 884      43.570   9.388 156.127  1.00 35.67      A    O  
ANISOU 1668  O   ALA C 884     4788   4631   4134    -87    446    962  A    O  
ATOM   1669  CB  ALA C 884      45.898  11.656 155.921  1.00 32.77      A    C  
ANISOU 1669  CB  ALA C 884     4168   4311   3970     90    236    968  A    C  
ATOM   1670  N   PRO C 885      43.795  10.409 158.124  1.00 34.06      A    N  
ANISOU 1670  N   PRO C 885     4481   4703   3759    -52    178   1056  A    N  
ATOM   1671  CA  PRO C 885      42.438  10.028 158.515  1.00 32.27      A    C  
ANISOU 1671  CA  PRO C 885     4330   4569   3362   -146    228   1019  A    C  
ATOM   1672  C   PRO C 885      41.389  10.881 157.794  1.00 38.60      A    C  
ANISOU 1672  C   PRO C 885     5136   5460   4070   -203    257    826  A    C  
ATOM   1673  O   PRO C 885      41.478  12.105 157.810  1.00 37.64      A    O  
ANISOU 1673  O   PRO C 885     4966   5432   3902   -167    172    730  A    O  
ATOM   1674  CB  PRO C 885      42.433  10.272 160.037  1.00 33.33      A    C  
ANISOU 1674  CB  PRO C 885     4459   4873   3333   -143     97   1110  A    C  
ATOM   1675  CG  PRO C 885      43.455  11.389 160.225  1.00 36.62      A    C  
ANISOU 1675  CG  PRO C 885     4801   5337   3776    -79    -58   1084  A    C  
ATOM   1676  CD  PRO C 885      44.525  11.119 159.191  1.00 34.22      A    C  
ANISOU 1676  CD  PRO C 885     4430   4844   3729    -12     -9   1129  A    C  
ATOM   1677  N   VAL C 886      40.405  10.249 157.159  1.00 37.34      A    N  
ANISOU 1677  N   VAL C 886     5029   5263   3893   -297    365    780  A    N  
ATOM   1678  CA  VAL C 886      39.406  11.029 156.422  1.00 36.28      A    C  
ANISOU 1678  CA  VAL C 886     4874   5222   3689   -352    372    632  A    C  
ATOM   1679  C   VAL C 886      38.609  11.957 157.346  1.00 32.12      A    C  
ANISOU 1679  C   VAL C 886     4289   4904   3011   -340    311    591  A    C  
ATOM   1680  O   VAL C 886      38.190  13.041 156.934  1.00 36.68      A    O  
ANISOU 1680  O   VAL C 886     4815   5559   3561   -318    281    483  A    O  
ATOM   1681  CB  VAL C 886      38.415  10.117 155.646  1.00 46.30      A    C  
ANISOU 1681  CB  VAL C 886     6202   6434   4956   -491    469    606  A    C  
ATOM   1682  CG1 VAL C 886      37.441   9.420 156.605  1.00 43.84      A    C  
ANISOU 1682  CG1 VAL C 886     5888   6212   4556   -574    500    689  A    C  
ATOM   1683  CG2 VAL C 886      37.670  10.927 154.592  1.00 46.18      A    C  
ANISOU 1683  CG2 VAL C 886     6153   6489   4904   -542    448    478  A    C  
ATOM   1684  N   THR C 887      38.432  11.550 158.602  1.00 32.97      A    N  
ANISOU 1684  N   THR C 887     4414   5093   3021   -345    306    685  A    N  
ATOM   1685  CA  THR C 887      37.643  12.323 159.556  1.00 39.09      A    C  
ANISOU 1685  CA  THR C 887     5165   6056   3632   -332    293    643  A    C  
ATOM   1686  C   THR C 887      38.408  13.568 159.985  1.00 38.63      A    C  
ANISOU 1686  C   THR C 887     5102   6043   3532   -239    184    570  A    C  
ATOM   1687  O   THR C 887      37.866  14.418 160.661  1.00 37.79      A    O  
ANISOU 1687  O   THR C 887     4999   6063   3295   -213    184    496  A    O  
ATOM   1688  CB  THR C 887      37.271  11.508 160.826  1.00 41.93      A    C  
ANISOU 1688  CB  THR C 887     5572   6493   3865   -373    334    773  A    C  
ATOM   1689  CG2 THR C 887      36.300  10.377 160.497  1.00 43.22      A    C  
ANISOU 1689  CG2 THR C 887     5732   6625   4065   -489    451    839  A    C  
ATOM   1690  OG1 THR C 887      38.455  10.949 161.392  1.00 42.42      A    O  
ANISOU 1690  OG1 THR C 887     5686   6478   3952   -337    258    904  A    O  
ATOM   1691  N   GLY C 888      39.661  13.679 159.569  1.00 37.63      A    N  
ANISOU 1691  N   GLY C 888     4969   5800   3527   -194    103    589  A    N  
ATOM   1692  CA  GLY C 888      40.463  14.834 159.923  1.00 39.75      A    C  
ANISOU 1692  CA  GLY C 888     5229   6095   3780   -134    -19    527  A    C  
ATOM   1693  C   GLY C 888      40.202  16.043 159.048  1.00 39.25      A    C  
ANISOU 1693  C   GLY C 888     5124   6022   3768   -102    -14    378  A    C  
ATOM   1694  O   GLY C 888      40.788  17.093 159.275  1.00 36.39      A    O  
ANISOU 1694  O   GLY C 888     4760   5662   3403    -65   -107    310  A    O  
ATOM   1695  N   TYR C 889      39.329  15.891 158.048  1.00 34.19      A    N  
ANISOU 1695  N   TYR C 889     4452   5367   3173   -129     80    337  A    N  
ATOM   1696  CA  TYR C 889      39.135  16.922 157.031  1.00 34.74      A    C  
ANISOU 1696  CA  TYR C 889     4476   5413   3312    -99     78    234  A    C  
ATOM   1697  C   TYR C 889      37.628  17.152 156.847  1.00 36.55      A    C  
ANISOU 1697  C   TYR C 889     4660   5750   3479   -120    152    189  A    C  
ATOM   1698  O   TYR C 889      36.863  16.202 156.664  1.00 35.30      A    O  
ANISOU 1698  O   TYR C 889     4491   5619   3303   -198    217    243  A    O  
ATOM   1699  CB  TYR C 889      39.825  16.515 155.712  1.00 34.91      A    C  
ANISOU 1699  CB  TYR C 889     4495   5292   3476   -115     98    259  A    C  
ATOM   1700  CG  TYR C 889      41.292  16.174 155.929  1.00 36.02      A    C  
ANISOU 1700  CG  TYR C 889     4641   5327   3717    -81     52    338  A    C  
ATOM   1701  CD1 TYR C 889      41.673  14.908 156.361  1.00 35.73      A    C  
ANISOU 1701  CD1 TYR C 889     4633   5239   3705    -99     82    456  A    C  
ATOM   1702  CD2 TYR C 889      42.290  17.130 155.750  1.00 32.80      A    C  
ANISOU 1702  CD2 TYR C 889     4193   4871   3399    -30    -24    314  A    C  
ATOM   1703  CE1 TYR C 889      43.001  14.595 156.604  1.00 36.44      A    C  
ANISOU 1703  CE1 TYR C 889     4693   5238   3913    -52     35    562  A    C  
ATOM   1704  CE2 TYR C 889      43.631  16.824 156.015  1.00 34.48      A    C  
ANISOU 1704  CE2 TYR C 889     4369   5003   3727     -1    -79    414  A    C  
ATOM   1705  CZ  TYR C 889      43.973  15.547 156.425  1.00 33.43      A    C  
ANISOU 1705  CZ  TYR C 889     4248   4829   3627     -5    -48    544  A    C  
ATOM   1706  OH  TYR C 889      45.282  15.209 156.657  1.00 33.78      A    O  
ANISOU 1706  OH  TYR C 889     4225   4795   3817     38   -100    676  A    O  
ATOM   1707  N   MET C 890      37.221  18.414 156.935  1.00 34.99      A    N  
ANISOU 1707  N   MET C 890     4427   5601   3265    -52    143    101  A    N  
ATOM   1708  CA  MET C 890      35.813  18.802 156.947  1.00 36.79      A    C  
ANISOU 1708  CA  MET C 890     4580   5941   3459    -38    220     77  A    C  
ATOM   1709  C   MET C 890      35.013  18.205 155.776  1.00 35.91      A    C  
ANISOU 1709  C   MET C 890     4393   5842   3409   -121    242    130  A    C  
ATOM   1710  O   MET C 890      33.877  17.792 155.953  1.00 34.23      A    O  
ANISOU 1710  O   MET C 890     4107   5733   3166   -169    303    173  A    O  
ATOM   1711  CB  MET C 890      35.699  20.327 156.921  1.00 40.93      A    C  
ANISOU 1711  CB  MET C 890     5080   6458   4014     68    211    -20  A    C  
ATOM   1712  CG  MET C 890      34.262  20.852 156.901  1.00 44.54      A    C  
ANISOU 1712  CG  MET C 890     5427   7016   4479    118    305    -26  A    C  
ATOM   1713  SD  MET C 890      34.109  22.648 157.048  1.00 71.27      A    S  
ANISOU 1713  SD  MET C 890     8805  10356   7919    271    333   -137  A    S  
ATOM   1714  CE  MET C 890      34.831  22.947 158.668  1.00 81.41      A    C  
ANISOU 1714  CE  MET C 890    10263  11628   9042    297    345   -247  A    C  
ATOM   1715  N   PHE C 891      35.621  18.151 154.591  1.00 32.27      A    N  
ANISOU 1715  N   PHE C 891     3955   5280   3028   -152    192    130  A    N  
ATOM   1716  CA  PHE C 891      34.970  17.559 153.435  1.00 35.34      A    C  
ANISOU 1716  CA  PHE C 891     4317   5674   3438   -260    192    167  A    C  
ATOM   1717  C   PHE C 891      35.813  16.428 152.845  1.00 35.79      A    C  
ANISOU 1717  C   PHE C 891     4487   5598   3513   -346    204    188  A    C  
ATOM   1718  O   PHE C 891      35.835  16.196 151.624  1.00 34.00      A    O  
ANISOU 1718  O   PHE C 891     4303   5314   3302   -421    194    181  A    O  
ATOM   1719  CB  PHE C 891      34.678  18.647 152.382  1.00 34.16      A    C  
ANISOU 1719  CB  PHE C 891     4104   5534   3340   -222    141    147  A    C  
ATOM   1720  CG  PHE C 891      33.545  19.564 152.790  1.00 34.51      A    C  
ANISOU 1720  CG  PHE C 891     4013   5703   3398   -145    157    153  A    C  
ATOM   1721  CD1 PHE C 891      32.252  19.072 152.884  1.00 33.67      A    C  
ANISOU 1721  CD1 PHE C 891     3792   5725   3276   -215    186    219  A    C  
ATOM   1722  CD2 PHE C 891      33.777  20.881 153.128  1.00 34.98      A    C  
ANISOU 1722  CD2 PHE C 891     4054   5737   3502     -2    159     99  A    C  
ATOM   1723  CE1 PHE C 891      31.200  19.882 153.270  1.00 37.50      A    C  
ANISOU 1723  CE1 PHE C 891     4125   6320   3803   -124    230    244  A    C  
ATOM   1724  CE2 PHE C 891      32.714  21.704 153.518  1.00 37.52      A    C  
ANISOU 1724  CE2 PHE C 891     4253   6147   3855     91    210    106  A    C  
ATOM   1725  CZ  PHE C 891      31.431  21.202 153.576  1.00 37.06      A    C  
ANISOU 1725  CZ  PHE C 891     4061   6224   3795     41    253    185  A    C  
ATOM   1726  N   GLY C 892      36.511  15.731 153.728  1.00 36.12      A    N  
ANISOU 1726  N   GLY C 892     4588   5587   3548   -332    231    221  A    N  
ATOM   1727  CA  GLY C 892      37.368  14.643 153.306  1.00 34.69      A    C  
ANISOU 1727  CA  GLY C 892     4508   5256   3417   -380    271    255  A    C  
ATOM   1728  C   GLY C 892      38.627  15.162 152.644  1.00 35.09      A    C  
ANISOU 1728  C   GLY C 892     4589   5188   3557   -306    258    231  A    C  
ATOM   1729  O   GLY C 892      38.908  16.366 152.616  1.00 30.97      A    O  
ANISOU 1729  O   GLY C 892     4014   4695   3056   -227    201    191  A    O  
ATOM   1730  N   LYS C 893      39.376  14.234 152.075  1.00 31.03      A    N  
ANISOU 1730  N   LYS C 893     4160   4521   3107   -334    330    258  A    N  
ATOM   1731  CA  LYS C 893      40.702  14.528 151.605  1.00 29.85      A    C  
ANISOU 1731  CA  LYS C 893     4023   4248   3070   -255    352    266  A    C  
ATOM   1732  C   LYS C 893      40.700  15.001 150.153  1.00 32.74      A    C  
ANISOU 1732  C   LYS C 893     4436   4570   3434   -285    386    204  A    C  
ATOM   1733  O   LYS C 893      40.722  14.213 149.217  1.00 33.57      A    O  
ANISOU 1733  O   LYS C 893     4655   4573   3527   -359    483    184  A    O  
ATOM   1734  CB  LYS C 893      41.577  13.294 151.803  1.00 33.14      A    C  
ANISOU 1734  CB  LYS C 893     4497   4512   3584   -239    443    347  A    C  
ATOM   1735  CG  LYS C 893      41.698  12.930 153.309  1.00 32.25      A    C  
ANISOU 1735  CG  LYS C 893     4334   4457   3463   -201    382    442  A    C  
ATOM   1736  CD  LYS C 893      42.686  11.801 153.552  1.00 33.71      A    C  
ANISOU 1736  CD  LYS C 893     4546   4483   3780   -156    457    563  A    C  
ATOM   1737  CE  LYS C 893      42.000  10.467 153.302  1.00 34.25      A    C  
ANISOU 1737  CE  LYS C 893     4731   4458   3826   -253    574    574  A    C  
ATOM   1738  NZ  LYS C 893      42.947   9.350 153.415  1.00 37.31      A    N1+
ANISOU 1738  NZ  LYS C 893     5156   4649   4370   -193    679    694  A    N1+
ATOM   1739  N   GLY C 894      40.670  16.318 149.974  1.00 29.32      A    N  
ANISOU 1739  N   GLY C 894     3932   4208   3001   -233    311    173  A    N  
ATOM   1740  CA  GLY C 894      40.711  16.878 148.641  1.00 27.90      A    C  
ANISOU 1740  CA  GLY C 894     3794   3997   2810   -256    333    140  A    C  
ATOM   1741  C   GLY C 894      41.494  18.170 148.721  1.00 30.49      A    C  
ANISOU 1741  C   GLY C 894     4041   4313   3229   -154    283    146  A    C  
ATOM   1742  O   GLY C 894      42.221  18.384 149.691  1.00 30.80      A    O  
ANISOU 1742  O   GLY C 894     4016   4337   3350    -85    244    172  A    O  
ATOM   1743  N   ILE C 895      41.353  19.015 147.711  1.00 31.18      A    N  
ANISOU 1743  N   ILE C 895     4140   4406   3301   -160    274    133  A    N  
ATOM   1744  CA  ILE C 895      42.007  20.319 147.690  1.00 32.58      A    C  
ANISOU 1744  CA  ILE C 895     4249   4558   3574    -80    230    143  A    C  
ATOM   1745  C   ILE C 895      40.923  21.387 147.809  1.00 30.51      A    C  
ANISOU 1745  C   ILE C 895     3926   4404   3264    -60    133    122  A    C  
ATOM   1746  O   ILE C 895      39.940  21.371 147.063  1.00 27.00      A    O  
ANISOU 1746  O   ILE C 895     3500   4030   2728   -115    117    132  A    O  
ATOM   1747  CB  ILE C 895      42.826  20.529 146.403  1.00 32.10      A    C  
ANISOU 1747  CB  ILE C 895     4246   4393   3556    -86    321    171  A    C  
ATOM   1748  CG1 ILE C 895      43.786  19.365 146.192  1.00 34.14      A    C  
ANISOU 1748  CG1 ILE C 895     4569   4531   3873    -91    463    193  A    C  
ATOM   1749  CG2 ILE C 895      43.581  21.865 146.456  1.00 31.22      A    C  
ANISOU 1749  CG2 ILE C 895     4052   4238   3572    -14    278    197  A    C  
ATOM   1750  CD1 ILE C 895      44.447  19.357 144.802  1.00 34.25      A    C  
ANISOU 1750  CD1 ILE C 895     4678   4443   3891   -108    610    210  A    C  
ATOM   1751  N   TYR C 896      41.126  22.308 148.750  1.00 30.55      A    N  
ANISOU 1751  N   TYR C 896     3860   4413   3335     17     69     99  A    N  
ATOM   1752  CA  TYR C 896      40.091  23.232 149.232  1.00 30.84      A    C  
ANISOU 1752  CA  TYR C 896     3838   4533   3345     66     10     67  A    C  
ATOM   1753  C   TYR C 896      40.314  24.648 148.718  1.00 32.28      A    C  
ANISOU 1753  C   TYR C 896     3997   4650   3619    126    -19     75  A    C  
ATOM   1754  O   TYR C 896      41.454  25.142 148.706  1.00 31.16      A    O  
ANISOU 1754  O   TYR C 896     3861   4400   3577    142    -24     76  A    O  
ATOM   1755  CB  TYR C 896      40.068  23.269 150.777  1.00 30.09      A    C  
ANISOU 1755  CB  TYR C 896     3723   4475   3233    106    -20     12  A    C  
ATOM   1756  CG  TYR C 896      39.537  22.017 151.460  1.00 32.48      A    C  
ANISOU 1756  CG  TYR C 896     4039   4864   3438     57      8     21  A    C  
ATOM   1757  CD1 TYR C 896      40.158  20.777 151.283  1.00 32.66      A    C  
ANISOU 1757  CD1 TYR C 896     4109   4840   3460     -3     47     65  A    C  
ATOM   1758  CD2 TYR C 896      38.435  22.085 152.305  1.00 30.79      A    C  
ANISOU 1758  CD2 TYR C 896     3791   4762   3147     78     17     -6  A    C  
ATOM   1759  CE1 TYR C 896      39.664  19.629 151.906  1.00 32.38      A    C  
ANISOU 1759  CE1 TYR C 896     4093   4862   3347    -52     77     86  A    C  
ATOM   1760  CE2 TYR C 896      37.940  20.951 152.938  1.00 31.31      A    C  
ANISOU 1760  CE2 TYR C 896     3866   4904   3127     24     52     18  A    C  
ATOM   1761  CZ  TYR C 896      38.557  19.727 152.739  1.00 32.74      A    C  
ANISOU 1761  CZ  TYR C 896     4101   5030   3308    -47     73     67  A    C  
ATOM   1762  OH  TYR C 896      38.062  18.604 153.377  1.00 31.79      A    O  
ANISOU 1762  OH  TYR C 896     3996   4966   3115   -105    112    104  A    O  
ATOM   1763  N   PHE C 897      39.226  25.301 148.328  1.00 33.06      A    N  
ANISOU 1763  N   PHE C 897     4053   4810   3700    157    -41     97  A    N  
ATOM   1764  CA  PHE C 897      39.255  26.668 147.815  1.00 33.65      A    C  
ANISOU 1764  CA  PHE C 897     4103   4813   3868    225    -64    127  A    C  
ATOM   1765  C   PHE C 897      38.088  27.489 148.375  1.00 35.79      A    C  
ANISOU 1765  C   PHE C 897     4299   5134   4164    320    -76    112  A    C  
ATOM   1766  O   PHE C 897      37.096  26.933 148.845  1.00 31.93      A    O  
ANISOU 1766  O   PHE C 897     3760   4766   3607    318    -64    107  A    O  
ATOM   1767  CB  PHE C 897      39.178  26.689 146.281  1.00 29.00      A    C  
ANISOU 1767  CB  PHE C 897     3542   4226   3250    174    -64    227  A    C  
ATOM   1768  CG  PHE C 897      40.319  26.003 145.609  1.00 31.76      A    C  
ANISOU 1768  CG  PHE C 897     3979   4506   3584    100     -4    241  A    C  
ATOM   1769  CD1 PHE C 897      40.280  24.628 145.375  1.00 31.12      A    C  
ANISOU 1769  CD1 PHE C 897     3961   4470   3393     10     41    228  A    C  
ATOM   1770  CD2 PHE C 897      41.434  26.724 145.197  1.00 30.49      A    C  
ANISOU 1770  CD2 PHE C 897     3834   4219   3532    121     27    271  A    C  
ATOM   1771  CE1 PHE C 897      41.349  23.979 144.751  1.00 28.19      A    C  
ANISOU 1771  CE1 PHE C 897     3677   4011   3024    -36    136    237  A    C  
ATOM   1772  CE2 PHE C 897      42.505  26.090 144.560  1.00 31.01      A    C  
ANISOU 1772  CE2 PHE C 897     3961   4216   3604     68    118    296  A    C  
ATOM   1773  CZ  PHE C 897      42.461  24.718 144.337  1.00 33.23      A    C  
ANISOU 1773  CZ  PHE C 897     4313   4535   3777      0    183    276  A    C  
ATOM   1774  N   ALA C 898      38.213  28.812 148.291  1.00 33.82      A    N  
ANISOU 1774  N   ALA C 898     4040   4779   4031    405    -83    115  A    N  
ATOM   1775  CA  ALA C 898      37.146  29.732 148.678  1.00 36.04      A    C  
ANISOU 1775  CA  ALA C 898     4250   5067   4375    525    -64    115  A    C  
ATOM   1776  C   ALA C 898      36.906  30.742 147.554  1.00 37.06      A    C  
ANISOU 1776  C   ALA C 898     4341   5132   4606    579    -88    238  A    C  
ATOM   1777  O   ALA C 898      37.800  30.971 146.722  1.00 35.34      A    O  
ANISOU 1777  O   ALA C 898     4180   4828   4418    528   -111    289  A    O  
ATOM   1778  CB  ALA C 898      37.500  30.448 149.974  1.00 35.61      A    C  
ANISOU 1778  CB  ALA C 898     4252   4909   4371    593    -28    -27  A    C  
ATOM   1779  N   ASP C 899      35.710  31.338 147.511  1.00 38.82      A    N  
ANISOU 1779  N   ASP C 899     4459   5396   4893    686    -76    308  A    N  
ATOM   1780  CA  ASP C 899      35.473  32.402 146.532  1.00 40.32      A    C  
ANISOU 1780  CA  ASP C 899     4607   5511   5201    758   -106    451  A    C  
ATOM   1781  C   ASP C 899      35.545  33.773 147.186  1.00 44.29      A    C  
ANISOU 1781  C   ASP C 899     5129   5820   5879    905    -37    388  A    C  
ATOM   1782  O   ASP C 899      35.295  34.785 146.540  1.00 48.10      A    O  
ANISOU 1782  O   ASP C 899     5574   6205   6496    994    -43    509  A    O  
ATOM   1783  CB  ASP C 899      34.130  32.224 145.783  1.00 39.56      A    C  
ANISOU 1783  CB  ASP C 899     4363   5580   5089    776   -164    627  A    C  
ATOM   1784  CG  ASP C 899      32.922  32.084 146.691  1.00 43.34      A    C  
ANISOU 1784  CG  ASP C 899     4704   6162   5603    870   -105    607  A    C  
ATOM   1785  OD1 ASP C 899      32.921  32.556 147.855  1.00 43.88      A    O  
ANISOU 1785  OD1 ASP C 899     4794   6137   5740    979      7    472  A    O  
ATOM   1786  OD2 ASP C 899      31.923  31.509 146.194  1.00 47.32      A    O1-
ANISOU 1786  OD2 ASP C 899     5074   6845   6061    825   -171    738  A    O1-
ATOM   1787  N   MET C 900      35.905  33.799 148.466  1.00 41.82      A    N  
ANISOU 1787  N   MET C 900     4892   5443   5556    922     26    202  A    N  
ATOM   1788  CA  MET C 900      36.096  35.058 149.184  1.00 41.84      A    C  
ANISOU 1788  CA  MET C 900     4966   5234   5698   1030     97     95  A    C  
ATOM   1789  C   MET C 900      37.426  35.051 149.917  1.00 42.01      A    C  
ANISOU 1789  C   MET C 900     5136   5145   5681    925     71    -71  A    C  
ATOM   1790  O   MET C 900      37.754  34.106 150.651  1.00 36.08      A    O  
ANISOU 1790  O   MET C 900     4424   4499   4787    838     53   -167  A    O  
ATOM   1791  CB  MET C 900      34.939  35.318 150.151  1.00 44.87      A    C  
ANISOU 1791  CB  MET C 900     5300   5643   6107   1177    219     26  A    C  
ATOM   1792  CG  MET C 900      33.601  35.447 149.434  1.00 51.02      A    C  
ANISOU 1792  CG  MET C 900     5884   6525   6974   1294    236    225  A    C  
ATOM   1793  SD  MET C 900      32.244  36.096 150.432  1.00 59.61      A    S  
ANISOU 1793  SD  MET C 900     6879   7586   8184   1521    431    184  A    S  
ATOM   1794  CE  MET C 900      32.863  37.731 150.820  1.00 51.61      A    C  
ANISOU 1794  CE  MET C 900     6039   6218   7353   1641    528     56  A    C  
ATOM   1795  N   VAL C 901      38.189  36.117 149.700  1.00 43.06      A    N  
ANISOU 1795  N   VAL C 901     5342   5064   5954    925     59    -84  A    N  
ATOM   1796  CA  VAL C 901      39.577  36.167 150.120  1.00 44.14      A    C  
ANISOU 1796  CA  VAL C 901     5585   5097   6090    793     -3   -190  A    C  
ATOM   1797  C   VAL C 901      39.698  36.129 151.651  1.00 46.61      A    C  
ANISOU 1797  C   VAL C 901     6009   5392   6311    773     11   -406  A    C  
ATOM   1798  O   VAL C 901      40.671  35.599 152.184  1.00 46.15      A    O  
ANISOU 1798  O   VAL C 901     6002   5361   6174    641    -71   -477  A    O  
ATOM   1799  CB  VAL C 901      40.294  37.417 149.539  1.00 44.65      A    C  
ANISOU 1799  CB  VAL C 901     5696   4921   6349    786    -16   -144  A    C  
ATOM   1800  CG1 VAL C 901      39.797  38.708 150.196  1.00 49.53      A    C  
ANISOU 1800  CG1 VAL C 901     6398   5326   7094    905     65   -253  A    C  
ATOM   1801  CG2 VAL C 901      41.803  37.277 149.677  1.00 47.22      A    C  
ANISOU 1801  CG2 VAL C 901     6069   5181   6691    619   -102   -188  A    C  
ATOM   1802  N   SER C 902      38.691  36.639 152.349  1.00 49.74      A    N  
ANISOU 1802  N   SER C 902     6438   5754   6708    904    121   -495  A    N  
ATOM   1803  CA  SER C 902      38.717  36.658 153.809  1.00 56.48      A    C  
ANISOU 1803  CA  SER C 902     7433   6590   7436    887    159   -709  A    C  
ATOM   1804  C   SER C 902      38.572  35.254 154.406  1.00 54.80      A    C  
ANISOU 1804  C   SER C 902     7191   6621   7009    820    135   -723  A    C  
ATOM   1805  O   SER C 902      39.140  34.959 155.460  1.00 56.08      A    O  
ANISOU 1805  O   SER C 902     7473   6804   7030    725     87   -858  A    O  
ATOM   1806  CB  SER C 902      37.629  37.589 154.350  1.00 63.03      A    C  
ANISOU 1806  CB  SER C 902     8315   7303   8330   1066    333   -800  A    C  
ATOM   1807  OG  SER C 902      36.394  37.378 153.694  1.00 66.57      A    O  
ANISOU 1807  OG  SER C 902     8583   7869   8842   1214    421   -636  A    O  
ATOM   1808  N   LYS C 903      37.822  34.389 153.733  1.00 51.09      A    N  
ANISOU 1808  N   LYS C 903     6568   6332   6510    856    155   -574  A    N  
ATOM   1809  CA  LYS C 903      37.781  32.990 154.128  1.00 49.49      A    C  
ANISOU 1809  CA  LYS C 903     6335   6337   6131    774    125   -560  A    C  
ATOM   1810  C   LYS C 903      39.193  32.419 154.039  1.00 49.60      A    C  
ANISOU 1810  C   LYS C 903     6389   6345   6113    617    -13   -551  A    C  
ATOM   1811  O   LYS C 903      39.732  31.915 155.021  1.00 48.56      A    O  
ANISOU 1811  O   LYS C 903     6336   6259   5855    536    -63   -635  A    O  
ATOM   1812  CB  LYS C 903      36.812  32.182 153.251  1.00 50.50      A    C  
ANISOU 1812  CB  LYS C 903     6298   6635   6254    804    150   -395  A    C  
ATOM   1813  CG  LYS C 903      36.832  30.661 153.522  1.00 52.13      A    C  
ANISOU 1813  CG  LYS C 903     6481   7028   6299    700    119   -367  A    C  
ATOM   1814  CD  LYS C 903      36.578  30.340 154.999  1.00 55.38      A    C  
ANISOU 1814  CD  LYS C 903     6976   7504   6562    704    184   -494  A    C  
ATOM   1815  CE  LYS C 903      36.482  28.835 155.264  1.00 57.35      A    C  
ANISOU 1815  CE  LYS C 903     7195   7927   6669    609    165   -439  A    C  
ATOM   1816  N   SER C 904      39.799  32.542 152.863  1.00 50.73      A    N  
ANISOU 1816  N   SER C 904     6472   6429   6375    580    -68   -433  A    N  
ATOM   1817  CA  SER C 904      41.113  31.957 152.608  1.00 48.20      A    C  
ANISOU 1817  CA  SER C 904     6149   6103   6063    453   -165   -390  A    C  
ATOM   1818  C   SER C 904      42.239  32.626 153.381  1.00 48.40      A    C  
ANISOU 1818  C   SER C 904     6263   5993   6133    372   -253   -494  A    C  
ATOM   1819  O   SER C 904      43.275  32.014 153.612  1.00 48.29      A    O  
ANISOU 1819  O   SER C 904     6235   6008   6107    266   -343   -470  A    O  
ATOM   1820  CB  SER C 904      41.431  32.006 151.113  1.00 46.67      A    C  
ANISOU 1820  CB  SER C 904     5881   5872   5979    441   -164   -238  A    C  
ATOM   1821  OG  SER C 904      40.725  31.002 150.423  1.00 47.40      A    O  
ANISOU 1821  OG  SER C 904     5910   6115   5984    446   -128   -142  A    O  
ATOM   1822  N   ALA C 905      42.043  33.884 153.756  1.00 50.28      A    N  
ANISOU 1822  N   ALA C 905     6588   6076   6439    417   -229   -600  A    N  
ATOM   1823  CA  ALA C 905      43.038  34.623 154.533  1.00 53.91      A    C  
ANISOU 1823  CA  ALA C 905     7159   6392   6933    312   -328   -722  A    C  
ATOM   1824  C   ALA C 905      43.237  34.029 155.934  1.00 55.66      A    C  
ANISOU 1824  C   ALA C 905     7477   6718   6953    233   -398   -843  A    C  
ATOM   1825  O   ALA C 905      44.306  34.168 156.521  1.00 56.82      A    O  
ANISOU 1825  O   ALA C 905     7676   6819   7095     94   -541   -892  A    O  
ATOM   1826  CB  ALA C 905      42.643  36.094 154.641  1.00 57.99      A    C  
ANISOU 1826  CB  ALA C 905     7781   6693   7558    382   -260   -829  A    C  
ATOM   1827  N   ASN C 906      42.200  33.381 156.459  1.00 56.95      A    N  
ANISOU 1827  N   ASN C 906     7658   7029   6952    313   -304   -875  A    N  
ATOM   1828  CA  ASN C 906      42.269  32.711 157.754  1.00 62.54      A    C  
ANISOU 1828  CA  ASN C 906     8463   7861   7439    245   -352   -962  A    C  
ATOM   1829  C   ASN C 906      43.338  31.607 157.775  1.00 58.03      A    C  
ANISOU 1829  C   ASN C 906     7809   7398   6843    122   -502   -842  A    C  
ATOM   1830  O   ASN C 906      43.959  31.353 158.806  1.00 59.66      A    O  
ANISOU 1830  O   ASN C 906     8097   7651   6919     14   -626   -892  A    O  
ATOM   1831  CB  ASN C 906      40.892  32.131 158.116  1.00 72.11      A    C  
ANISOU 1831  CB  ASN C 906     9670   9219   8509    361   -192   -973  A    C  
ATOM   1832  CG  ASN C 906      40.913  31.318 159.406  1.00 82.86      A    C  
ANISOU 1832  CG  ASN C 906    11132  10727   9624    292   -225  -1030  A    C  
ATOM   1833  ND2 ASN C 906      40.892  32.006 160.551  1.00 85.85      A    N  
ANISOU 1833  ND2 ASN C 906    11712  11050   9856    264   -215  -1214  A    N  
ATOM   1834  OD1 ASN C 906      40.919  30.083 159.372  1.00 86.30      A    O  
ANISOU 1834  OD1 ASN C 906    11483  11318   9991    261   -249   -910  A    O  
ATOM   1835  N   TYR C 907      43.552  30.972 156.622  1.00 56.13      A    N  
ANISOU 1835  N   TYR C 907     7411   7188   6727    140   -486   -677  A    N  
ATOM   1836  CA  TYR C 907      44.487  29.849 156.489  1.00 54.08      A    C  
ANISOU 1836  CA  TYR C 907     7055   7010   6482     61   -575   -543  A    C  
ATOM   1837  C   TYR C 907      45.943  30.304 156.334  1.00 53.12      A    C  
ANISOU 1837  C   TYR C 907     6883   6779   6520    -48   -717   -497  A    C  
ATOM   1838  O   TYR C 907      46.850  29.475 156.329  1.00 51.50      A    O  
ANISOU 1838  O   TYR C 907     6581   6624   6361   -109   -795   -377  A    O  
ATOM   1839  CB  TYR C 907      44.069  28.943 155.304  1.00 52.79      A    C  
ANISOU 1839  CB  TYR C 907     6776   6910   6371    123   -467   -404  A    C  
ATOM   1840  CG  TYR C 907      42.684  28.359 155.507  1.00 58.48      A    C  
ANISOU 1840  CG  TYR C 907     7516   7756   6946    197   -355   -424  A    C  
ATOM   1841  CD1 TYR C 907      41.551  29.071 155.132  1.00 59.48      A    C  
ANISOU 1841  CD1 TYR C 907     7647   7865   7088    293   -252   -467  A    C  
ATOM   1842  CD2 TYR C 907      42.506  27.117 156.112  1.00 63.06      A    C  
ANISOU 1842  CD2 TYR C 907     8097   8470   7393    171   -353   -383  A    C  
ATOM   1843  CE1 TYR C 907      40.285  28.561 155.336  1.00 62.15      A    C  
ANISOU 1843  CE1 TYR C 907     7967   8327   7321    354   -152   -466  A    C  
ATOM   1844  CE2 TYR C 907      41.232  26.595 156.321  1.00 64.22      A    C  
ANISOU 1844  CE2 TYR C 907     8247   8731   7422    222   -247   -391  A    C  
ATOM   1845  CZ  TYR C 907      40.128  27.327 155.928  1.00 63.52      A    C  
ANISOU 1845  CZ  TYR C 907     8141   8634   7360    310   -148   -433  A    C  
ATOM   1846  OH  TYR C 907      38.858  26.835 156.122  1.00 65.50      A    O  
ANISOU 1846  OH  TYR C 907     8358   9005   7522    356    -43   -420  A    O  
ATOM   1847  N   CYS C 908      46.154  31.617 156.224  1.00 54.87      A    N  
ANISOU 1847  N   CYS C 908     7160   6841   6846    -72   -742   -582  A    N  
ATOM   1848  CA  CYS C 908      47.501  32.198 156.232  1.00 57.90      A    C  
ANISOU 1848  CA  CYS C 908     7500   7112   7386   -205   -891   -554  A    C  
ATOM   1849  C   CYS C 908      48.082  32.237 157.650  1.00 62.99      A    C  
ANISOU 1849  C   CYS C 908     8242   7796   7897   -344  -1081   -646  A    C  
ATOM   1850  O   CYS C 908      49.299  32.237 157.828  1.00 62.85      A    O  
ANISOU 1850  O   CYS C 908     8138   7760   7983   -478  -1251   -570  A    O  
ATOM   1851  CB  CYS C 908      47.491  33.616 155.637  1.00 60.17      A    C  
ANISOU 1851  CB  CYS C 908     7831   7196   7836   -199   -852   -611  A    C  
ATOM   1852  SG  CYS C 908      47.027  33.703 153.881  1.00 62.84      A    S  
ANISOU 1852  SG  CYS C 908     8057   7487   8335    -69   -672   -462  A    S  
ATOM   1853  N   HIS C 909      47.196  32.271 158.645  1.00 68.75      A    N  
ANISOU 1853  N   HIS C 909     9145   8586   8391   -315  -1049   -799  A    N  
ATOM   1854  CA  HIS C 909      47.573  32.319 160.058  1.00 76.39      A    C  
ANISOU 1854  CA  HIS C 909    10259   9606   9158   -451  -1219   -908  A    C  
ATOM   1855  C   HIS C 909      48.552  33.452 160.342  1.00 79.72      A    C  
ANISOU 1855  C   HIS C 909    10744   9867   9677   -622  -1396   -993  A    C  
ATOM   1856  O   HIS C 909      49.539  33.279 161.060  1.00 79.05      A    O  
ANISOU 1856  O   HIS C 909    10650   9835   9549   -795  -1628   -959  A    O  
ATOM   1857  CB  HIS C 909      48.167  30.981 160.510  1.00 79.89      A    C  
ANISOU 1857  CB  HIS C 909    10598  10235   9523   -506  -1343   -746  A    C  
ATOM   1858  CG  HIS C 909      47.164  29.872 160.578  1.00 83.52      A    C  
ANISOU 1858  CG  HIS C 909    11054  10847   9832   -379  -1191   -698  A    C  
ATOM   1859  CD2 HIS C 909      46.117  29.666 161.411  1.00 85.48      A    C  
ANISOU 1859  CD2 HIS C 909    11459  11190   9830   -329  -1096   -808  A    C  
ATOM   1860  ND1 HIS C 909      47.172  28.807 159.702  1.00 83.52      A    N  
ANISOU 1860  ND1 HIS C 909    10879  10908   9948   -298  -1105   -517  A    N  
ATOM   1861  CE1 HIS C 909      46.175  27.991 159.994  1.00 81.78      A    C  
ANISOU 1861  CE1 HIS C 909    10703  10808   9561   -219   -986   -516  A    C  
ATOM   1862  NE2 HIS C 909      45.518  28.489 161.026  1.00 83.57      A    N  
ANISOU 1862  NE2 HIS C 909    11116  11066   9571   -231   -973   -680  A    N  
ATOM   1863  N   THR C 910      48.210  34.629 159.815  1.00 79.78      A    N  
ANISOU 1863  N   THR C 910    10810   9675   9827   -582  -1297  -1088  A    N  
ATOM   1864  CA  THR C 910      48.983  35.832 160.032  1.00 82.63      A    C  
ANISOU 1864  CA  THR C 910    11264   9849  10282   -753  -1445  -1195  A    C  
ATOM   1865  C   THR C 910      48.729  36.417 161.390  1.00 86.86      A    C  
ANISOU 1865  C   THR C 910    12102  10351  10551   -845  -1501  -1451  A    C  
ATOM   1866  O   THR C 910      47.744  36.122 162.024  1.00 88.84      A    O  
ANISOU 1866  O   THR C 910    12513  10626  10616   -710  -1319  -1587  A    O  
ATOM   1867  CB  THR C 910      48.683  36.936 159.018  1.00 81.26      A    C  
ANISOU 1867  CB  THR C 910    11073   9441  10361   -684  -1311  -1205  A    C  
ATOM   1868  CG2 THR C 910      49.520  36.767 157.816  1.00 79.33      A    C  
ANISOU 1868  CG2 THR C 910    10562   9194  10387   -691  -1326   -962  A    C  
ATOM   1869  OG1 THR C 910      47.314  36.889 158.645  1.00 79.93      A    O  
ANISOU 1869  OG1 THR C 910    10961   9260  10148   -462  -1062  -1254  A    O  
ATOM   1870  N   SER C 911      49.637  37.274 161.813  1.00 90.25      A    N  
ANISOU 1870  N   SER C 911    12601  10736  10952  -1088  -1759  -1507  A    N  
ATOM   1871  CA  SER C 911      49.567  37.898 163.119  1.00 94.84      A    C  
ANISOU 1871  CA  SER C 911    13514  11186  11336  -1232  -1829  -1789  A    C  
ATOM   1872  C   SER C 911      50.159  39.284 163.080  1.00 99.48      A    C  
ANISOU 1872  C   SER C 911    14145  11470  12182  -1314  -1833  -1873  A    C  
ATOM   1873  O   SER C 911      51.007  39.590 162.259  1.00100.67      A    O  
ANISOU 1873  O   SER C 911    14099  11532  12619  -1194  -1710  -1725  A    O  
ATOM   1874  CB  SER C 911      50.312  37.061 164.155  1.00 95.71      A    C  
ANISOU 1874  CB  SER C 911    13695  11447  11222  -1485  -2147  -1795  A    C  
ATOM   1875  OG  SER C 911      51.660  36.886 163.792  1.00 96.36      A    O  
ANISOU 1875  OG  SER C 911    13542  11516  11553  -1669  -2401  -1612  A    O  
ATOM   1876  N   GLN C 912      49.702  40.124 163.991  1.00104.18      A    N  
ANISOU 1876  N   GLN C 912    15009  11906  12669  -1526  -1973  -2102  A    N  
ATOM   1877  CA  GLN C 912      50.232  41.456 164.130  1.00106.90      A    C  
ANISOU 1877  CA  GLN C 912    15377  11961  13280  -1668  -2039  -2153  A    C  
ATOM   1878  C   GLN C 912      51.745  41.423 164.105  1.00105.91      A    C  
ANISOU 1878  C   GLN C 912    15338  11828  13076  -2030  -2402  -2220  A    C  
ATOM   1879  O   GLN C 912      52.375  42.195 163.413  1.00109.44      A    O  
ANISOU 1879  O   GLN C 912    15880  12024  13680  -2230  -2513  -2321  A    O  
ATOM   1880  CB  GLN C 912      49.750  42.037 165.450  1.00111.87      A    C  
ANISOU 1880  CB  GLN C 912    16268  12299  13938  -1541  -1783  -2387  A    C  
ATOM   1881  N   GLY C 913      52.326  40.515 164.865  1.00103.53      A    N  
ANISOU 1881  N   GLY C 913    14978  11811  12550  -2127  -2610  -2129  A    N  
ATOM   1882  CA  GLY C 913      53.762  40.444 164.977  1.00106.52      A    C  
ANISOU 1882  CA  GLY C 913    15188  12280  13006  -2427  -2993  -1980  A    C  
ATOM   1883  C   GLY C 913      54.434  40.213 163.650  1.00105.79      A    C  
ANISOU 1883  C   GLY C 913    14664  12204  13326  -2331  -2952  -1656  A    C  
ATOM   1884  O   GLY C 913      55.633  40.409 163.505  1.00106.24      A    O  
ANISOU 1884  O   GLY C 913    14507  12253  13608  -2544  -3196  -1497  A    O  
ATOM   1885  N   ASP C 914      53.650  39.774 162.677  1.00105.01      A    N  
ANISOU 1885  N   ASP C 914    14444  12131  13323  -2019  -2638  -1558  A    N  
ATOM   1886  CA  ASP C 914      54.146  39.415 161.353  1.00104.13      A    C  
ANISOU 1886  CA  ASP C 914    14000  11986  13579  -1905  -2524  -1299  A    C  
ATOM   1887  C   ASP C 914      52.965  39.525 160.396  1.00 85.19      A    C  
ANISOU 1887  C   ASP C 914    11644   9519  11206  -1592  -2159  -1329  A    C  
ATOM   1888  O   ASP C 914      52.197  38.580 160.239  1.00 84.62      A    O  
ANISOU 1888  O   ASP C 914    11506   9636  11011  -1395  -2020  -1250  A    O  
ATOM   1889  CB  ASP C 914      54.700  37.992 161.368  1.00103.70      A    C  
ANISOU 1889  CB  ASP C 914    13613  12190  13598  -1903  -2648  -1001  A    C  
ATOM   1890  CG  ASP C 914      55.295  37.584 160.046  1.00102.16      A    C  
ANISOU 1890  CG  ASP C 914    13110  11981  13725  -1744  -2462   -748  A    C  
ATOM   1891  OD1 ASP C 914      55.255  38.397 159.107  1.00100.56      A    O  
ANISOU 1891  OD1 ASP C 914    12924  11572  13712  -1688  -2298   -775  A    O  
ATOM   1892  OD2 ASP C 914      55.793  36.446 159.951  1.00102.38      A    O1-
ANISOU 1892  OD2 ASP C 914    12887  12192  13823  -1683  -2479   -516  A    O1-
ATOM   1893  N   PRO C 915      52.822  40.764 159.751  1.00 81.84      A    N  
ANISOU 1893  N   PRO C 915    11327   8819  10949  -1556  -2016  -1430  A    N  
ATOM   1894  CA  PRO C 915      51.517  40.936 159.109  1.00 75.76      A    C  
ANISOU 1894  CA  PRO C 915    10633   7944  10210  -1285  -1702  -1477  A    C  
ATOM   1895  C   PRO C 915      51.486  40.644 157.633  1.00 69.59      A    C  
ANISOU 1895  C   PRO C 915     9585   7183   9673  -1118  -1540  -1219  A    C  
ATOM   1896  O   PRO C 915      50.757  41.272 156.913  1.00 70.71      A    O  
ANISOU 1896  O   PRO C 915     9774   7185   9908   -948  -1331  -1227  A    O  
ATOM   1897  CB  PRO C 915      51.250  42.406 159.330  1.00 78.46      A    C  
ANISOU 1897  CB  PRO C 915    11221   7951  10638  -1371  -1675  -1689  A    C  
ATOM   1898  CG  PRO C 915      52.562  43.043 159.075  1.00 80.68      A    C  
ANISOU 1898  CG  PRO C 915    11401   8139  11113  -1665  -1932  -1618  A    C  
ATOM   1899  CD  PRO C 915      53.616  42.057 159.460  1.00 80.99      A    C  
ANISOU 1899  CD  PRO C 915    11299   8466  11009  -1812  -2184  -1515  A    C  
ATOM   1900  N   ILE C 916      52.274  39.690 157.198  1.00 63.79      A    N  
ANISOU 1900  N   ILE C 916     8584   6617   9037  -1163  -1629   -989  A    N  
ATOM   1901  CA  ILE C 916      52.367  39.381 155.776  1.00 60.12      A    C  
ANISOU 1901  CA  ILE C 916     7894   6167   8782  -1033  -1470   -755  A    C  
ATOM   1902  C   ILE C 916      51.962  37.942 155.485  1.00 56.09      A    C  
ANISOU 1902  C   ILE C 916     7253   5913   8145   -873  -1377   -626  A    C  
ATOM   1903  O   ILE C 916      52.491  37.003 156.096  1.00 57.09      A    O  
ANISOU 1903  O   ILE C 916     7293   6216   8184   -942  -1512   -569  A    O  
ATOM   1904  CB  ILE C 916      53.794  39.607 155.253  1.00 62.61      A    C  
ANISOU 1904  CB  ILE C 916     7991   6415   9381  -1211  -1590   -571  A    C  
ATOM   1905  CG1 ILE C 916      54.252  41.040 155.544  1.00 66.78      A    C  
ANISOU 1905  CG1 ILE C 916     8650   6671  10053  -1406  -1699   -695  A    C  
ATOM   1906  CG2 ILE C 916      53.873  39.280 153.772  1.00 59.06      A    C  
ANISOU 1906  CG2 ILE C 916     7344   5982   9114  -1072  -1391   -337  A    C  
ATOM   1907  CD1 ILE C 916      53.308  42.105 155.065  1.00 66.25      A    C  
ANISOU 1907  CD1 ILE C 916     8772   6369  10032  -1277  -1505   -805  A    C  
ATOM   1908  N   GLY C 917      51.021  37.775 154.558  1.00 51.45      A    N  
ANISOU 1908  N   GLY C 917     6657   5340   7553   -670  -1158   -571  A    N  
ATOM   1909  CA  GLY C 917      50.587  36.453 154.133  1.00 50.45      A    C  
ANISOU 1909  CA  GLY C 917     6422   5426   7320   -532  -1055   -454  A    C  
ATOM   1910  C   GLY C 917      50.651  36.248 152.631  1.00 51.97      A    C  
ANISOU 1910  C   GLY C 917     6473   5610   7664   -439   -896   -260  A    C  
ATOM   1911  O   GLY C 917      50.754  37.211 151.854  1.00 51.23      A    O  
ANISOU 1911  O   GLY C 917     6381   5348   7736   -440   -832   -215  A    O  
ATOM   1912  N   LEU C 918      50.601  34.984 152.216  1.00 45.50      A    N  
ANISOU 1912  N   LEU C 918     5547   4963   6778   -366   -824   -144  A    N  
ATOM   1913  CA  LEU C 918      50.590  34.648 150.801  1.00 44.27      A    C  
ANISOU 1913  CA  LEU C 918     5298   4817   6705   -282   -658     21  A    C  
ATOM   1914  C   LEU C 918      49.331  33.869 150.503  1.00 43.96      A    C  
ANISOU 1914  C   LEU C 918     5321   4914   6470   -140   -540      1  A    C  
ATOM   1915  O   LEU C 918      48.892  33.045 151.310  1.00 40.57      A    O  
ANISOU 1915  O   LEU C 918     4923   4616   5875   -118   -577    -68  A    O  
ATOM   1916  CB  LEU C 918      51.821  33.832 150.406  1.00 44.27      A    C  
ANISOU 1916  CB  LEU C 918     5113   4869   6838   -340   -652    191  A    C  
ATOM   1917  CG  LEU C 918      53.196  34.441 150.720  1.00 45.86      A    C  
ANISOU 1917  CG  LEU C 918     5192   4968   7267   -502   -787    253  A    C  
ATOM   1918  CD1 LEU C 918      54.283  33.428 150.436  1.00 43.73      A    C  
ANISOU 1918  CD1 LEU C 918     4710   4778   7126   -520   -759    437  A    C  
ATOM   1919  CD2 LEU C 918      53.444  35.729 149.943  1.00 47.93      A    C  
ANISOU 1919  CD2 LEU C 918     5461   5038   7713   -548   -735    293  A    C  
ATOM   1920  N   ILE C 919      48.747  34.138 149.347  1.00 39.82      A    N  
ANISOU 1920  N   ILE C 919     4811   4359   5961    -56   -409     75  A    N  
ATOM   1921  CA  ILE C 919      47.521  33.475 148.966  1.00 40.02      A    C  
ANISOU 1921  CA  ILE C 919     4881   4513   5812     54   -320     73  A    C  
ATOM   1922  C   ILE C 919      47.534  33.171 147.478  1.00 40.83      A    C  
ANISOU 1922  C   ILE C 919     4950   4634   5930     83   -193    227  A    C  
ATOM   1923  O   ILE C 919      48.042  33.962 146.679  1.00 40.67      A    O  
ANISOU 1923  O   ILE C 919     4911   4494   6047     60   -152    320  A    O  
ATOM   1924  CB  ILE C 919      46.298  34.327 149.346  1.00 40.61      A    C  
ANISOU 1924  CB  ILE C 919     5054   4546   5830    141   -318    -35  A    C  
ATOM   1925  CG1 ILE C 919      45.025  33.498 149.274  1.00 38.51      A    C  
ANISOU 1925  CG1 ILE C 919     4801   4447   5384    234   -258    -43  A    C  
ATOM   1926  CG2 ILE C 919      46.195  35.558 148.458  1.00 49.04      A    C  
ANISOU 1926  CG2 ILE C 919     6139   5451   7042    174   -270     38  A    C  
ATOM   1927  CD1 ILE C 919      43.835  34.238 149.769  1.00 43.48      A    C  
ANISOU 1927  CD1 ILE C 919     5492   5049   5979    334   -237   -135  A    C  
ATOM   1928  N   LEU C 920      47.026  31.993 147.115  1.00 36.39      A    N  
ANISOU 1928  N   LEU C 920     4392   4216   5217    117   -129    253  A    N  
ATOM   1929  CA  LEU C 920      46.945  31.599 145.712  1.00 36.90      A    C  
ANISOU 1929  CA  LEU C 920     4470   4312   5238    128     -8    375  A    C  
ATOM   1930  C   LEU C 920      45.611  31.949 145.058  1.00 36.40      A    C  
ANISOU 1930  C   LEU C 920     4469   4300   5060    191      5    398  A    C  
ATOM   1931  O   LEU C 920      44.550  31.932 145.697  1.00 32.53      A    O  
ANISOU 1931  O   LEU C 920     3993   3880   4485    244    -47    319  A    O  
ATOM   1932  CB  LEU C 920      47.163  30.093 145.562  1.00 35.32      A    C  
ANISOU 1932  CB  LEU C 920     4265   4218   4938    111     63    390  A    C  
ATOM   1933  CG  LEU C 920      48.544  29.572 145.923  1.00 38.52      A    C  
ANISOU 1933  CG  LEU C 920     4577   4579   5479     66     82    429  A    C  
ATOM   1934  CD1 LEU C 920      48.465  28.080 146.197  1.00 34.99      A    C  
ANISOU 1934  CD1 LEU C 920     4138   4228   4929     76    127    413  A    C  
ATOM   1935  CD2 LEU C 920      49.538  29.887 144.810  1.00 38.88      A    C  
ANISOU 1935  CD2 LEU C 920     4582   4530   5661     41    209    560  A    C  
ATOM   1936  N   LEU C 921      45.686  32.245 143.769  1.00 36.70      A    N  
ANISOU 1936  N   LEU C 921     4535   4311   5098    184     79    525  A    N  
ATOM   1937  CA  LEU C 921      44.530  32.202 142.894  1.00 39.49      A    C  
ANISOU 1937  CA  LEU C 921     4941   4758   5304    216     84    593  A    C  
ATOM   1938  C   LEU C 921      44.720  31.001 141.986  1.00 42.26      A    C  
ANISOU 1938  C   LEU C 921     5354   5204   5499    152    177    637  A    C  
ATOM   1939  O   LEU C 921      45.767  30.856 141.351  1.00 39.91      A    O  
ANISOU 1939  O   LEU C 921     5074   4843   5247    109    286    699  A    O  
ATOM   1940  CB  LEU C 921      44.387  33.486 142.064  1.00 40.86      A    C  
ANISOU 1940  CB  LEU C 921     5130   4833   5563    246     85    721  A    C  
ATOM   1941  CG  LEU C 921      43.552  34.625 142.634  1.00 44.46      A    C  
ANISOU 1941  CG  LEU C 921     5560   5216   6119    341      9    699  A    C  
ATOM   1942  CD1 LEU C 921      43.618  35.867 141.744  1.00 41.58      A    C  
ANISOU 1942  CD1 LEU C 921     5212   4717   5869    369     25    856  A    C  
ATOM   1943  CD2 LEU C 921      42.118  34.148 142.794  1.00 46.40      A    C  
ANISOU 1943  CD2 LEU C 921     5786   5621   6223    401    -42    681  A    C  
ATOM   1944  N   GLY C 922      43.714  30.140 141.928  1.00 39.80      A    N  
ANISOU 1944  N   GLY C 922     5079   5035   5009    142    149    603  A    N  
ATOM   1945  CA  GLY C 922      43.781  28.980 141.065  1.00 38.51      A    C  
ANISOU 1945  CA  GLY C 922     5013   4944   4676     65    236    620  A    C  
ATOM   1946  C   GLY C 922      42.523  28.825 140.235  1.00 35.22      A    C  
ANISOU 1946  C   GLY C 922     4662   4659   4063     27    173    676  A    C  
ATOM   1947  O   GLY C 922      41.427  29.159 140.673  1.00 32.04      A    O  
ANISOU 1947  O   GLY C 922     4189   4331   3653     69     57    675  A    O  
ATOM   1948  N   GLU C 923      42.700  28.339 139.016  1.00 34.91      A    N  
ANISOU 1948  N   GLU C 923     4756   4646   3863    -59    252    733  A    N  
ATOM   1949  CA  GLU C 923      41.580  27.959 138.193  1.00 35.61      A    C  
ANISOU 1949  CA  GLU C 923     4929   4877   3725   -140    172    780  A    C  
ATOM   1950  C   GLU C 923      41.266  26.524 138.564  1.00 36.25      A    C  
ANISOU 1950  C   GLU C 923     5061   5025   3688   -216    190    657  A    C  
ATOM   1951  O   GLU C 923      42.152  25.668 138.606  1.00 37.21      A    O  
ANISOU 1951  O   GLU C 923     5259   5070   3810   -241    335    582  A    O  
ATOM   1952  CB  GLU C 923      41.897  28.098 136.703  1.00 38.13      A    C  
ANISOU 1952  CB  GLU C 923     5410   5196   3883   -221    245    889  A    C  
ATOM   1953  CG  GLU C 923      40.758  27.601 135.819  1.00 41.37      A    C  
ANISOU 1953  CG  GLU C 923     5931   5770   4019   -346    132    934  A    C  
ATOM   1954  CD  GLU C 923      41.092  27.626 134.344  1.00 47.13      A    C  
ANISOU 1954  CD  GLU C 923     6869   6510   4529   -450    208   1027  A    C  
ATOM   1955  OE1 GLU C 923      41.961  28.431 133.945  1.00 47.78      A    O  
ANISOU 1955  OE1 GLU C 923     6964   6488   4702   -397    316   1116  A    O  
ATOM   1956  OE2 GLU C 923      40.482  26.840 133.582  1.00 47.82      A    O1-
ANISOU 1956  OE2 GLU C 923     7117   6710   4341   -600    161   1011  A    O1-
ATOM   1957  N   VAL C 924      40.008  26.275 138.876  1.00 36.95      A    N  
ANISOU 1957  N   VAL C 924     5092   5245   3703   -243     51    650  A    N  
ATOM   1958  CA  VAL C 924      39.591  24.965 139.352  1.00 34.62      A    C  
ANISOU 1958  CA  VAL C 924     4826   5008   3318   -321     54    543  A    C  
ATOM   1959  C   VAL C 924      38.470  24.460 138.447  1.00 38.56      A    C  
ANISOU 1959  C   VAL C 924     5409   5653   3589   -472    -56    587  A    C  
ATOM   1960  O   VAL C 924      37.465  25.140 138.225  1.00 35.93      A    O  
ANISOU 1960  O   VAL C 924     4976   5435   3241   -467   -211    696  A    O  
ATOM   1961  CB  VAL C 924      39.127  25.019 140.842  1.00 39.68      A    C  
ANISOU 1961  CB  VAL C 924     5296   5675   4104   -228     -7    484  A    C  
ATOM   1962  CG1 VAL C 924      38.874  23.634 141.371  1.00 33.45      A    C  
ANISOU 1962  CG1 VAL C 924     4545   4922   3241   -308     21    388  A    C  
ATOM   1963  CG2 VAL C 924      40.167  25.733 141.710  1.00 35.69      A    C  
ANISOU 1963  CG2 VAL C 924     4716   5040   3806   -101     52    451  A    C  
ATOM   1964  N   ALA C 925      38.664  23.280 137.880  1.00 37.90      A    N  
ANISOU 1964  N   ALA C 925     5513   5556   3332   -612     24    509  A    N  
ATOM   1965  CA  ALA C 925      37.658  22.723 136.998  1.00 42.04      A    C  
ANISOU 1965  CA  ALA C 925     6148   6212   3614   -798    -95    533  A    C  
ATOM   1966  C   ALA C 925      36.683  21.933 137.859  1.00 41.88      A    C  
ANISOU 1966  C   ALA C 925     6020   6280   3612   -855   -189    479  A    C  
ATOM   1967  O   ALA C 925      36.968  20.799 138.231  1.00 40.07      A    O  
ANISOU 1967  O   ALA C 925     5883   5979   3362   -914    -87    359  A    O  
ATOM   1968  CB  ALA C 925      38.305  21.846 135.930  1.00 42.01      A    C  
ANISOU 1968  CB  ALA C 925     6438   6131   3391   -942     51    456  A    C  
ATOM   1969  N   LEU C 926      35.547  22.544 138.189  1.00 42.72      A    N  
ANISOU 1969  N   LEU C 926     5923   6531   3778   -826   -367    581  A    N  
ATOM   1970  CA  LEU C 926      34.658  21.993 139.213  1.00 43.31      A    C  
ANISOU 1970  CA  LEU C 926     5841   6688   3928   -837   -428    551  A    C  
ATOM   1971  C   LEU C 926      33.672  20.965 138.659  1.00 42.00      A    C  
ANISOU 1971  C   LEU C 926     5743   6643   3572  -1078   -547    550  A    C  
ATOM   1972  O   LEU C 926      33.230  20.069 139.383  1.00 42.03      A    O  
ANISOU 1972  O   LEU C 926     5703   6665   3601  -1142   -538    485  A    O  
ATOM   1973  CB  LEU C 926      33.880  23.117 139.900  1.00 40.97      A    C  
ANISOU 1973  CB  LEU C 926     5277   6480   3811   -678   -525    662  A    C  
ATOM   1974  CG  LEU C 926      34.697  24.097 140.743  1.00 42.63      A    C  
ANISOU 1974  CG  LEU C 926     5410   6562   4225   -456   -420    635  A    C  
ATOM   1975  CD1 LEU C 926      33.822  25.293 141.087  1.00 40.26      A    C  
ANISOU 1975  CD1 LEU C 926     4892   6333   4074   -314   -510    755  A    C  
ATOM   1976  CD2 LEU C 926      35.266  23.413 142.020  1.00 35.04      A    C  
ANISOU 1976  CD2 LEU C 926     4448   5517   3347   -403   -298    494  A    C  
ATOM   1977  N   GLY C 927      33.303  21.115 137.390  1.00 41.83      A    N  
ANISOU 1977  N   GLY C 927     5829   6708   3357  -1225   -671    632  A    N  
ATOM   1978  CA  GLY C 927      32.321  20.228 136.773  1.00 41.67      A    C  
ANISOU 1978  CA  GLY C 927     5878   6816   3138  -1490   -829    640  A    C  
ATOM   1979  C   GLY C 927      31.020  20.182 137.558  1.00 45.95      A    C  
ANISOU 1979  C   GLY C 927     6130   7517   3810  -1502   -979    729  A    C  
ATOM   1980  O   GLY C 927      30.565  21.218 138.051  1.00 48.75      A    O  
ANISOU 1980  O   GLY C 927     6226   7947   4351  -1321  -1035    858  A    O  
ATOM   1981  N   ASN C 928      30.435  18.992 137.693  1.00 42.62      A    N  
ANISOU 1981  N   ASN C 928     5751   7133   3309  -1710  -1021    660  A    N  
ATOM   1982  CA  ASN C 928      29.208  18.828 138.470  1.00 46.91      A    C  
ANISOU 1982  CA  ASN C 928     6010   7827   3987  -1739  -1137    749  A    C  
ATOM   1983  C   ASN C 928      29.494  18.882 139.977  1.00 45.09      A    C  
ANISOU 1983  C   ASN C 928     5629   7516   3989  -1515   -957    689  A    C  
ATOM   1984  O   ASN C 928      30.157  17.993 140.522  1.00 42.81      A    O  
ANISOU 1984  O   ASN C 928     5484   7084   3696  -1530   -799    543  A    O  
ATOM   1985  CB  ASN C 928      28.506  17.506 138.136  1.00 49.51      A    C  
ANISOU 1985  CB  ASN C 928     6441   8210   4162  -2060  -1240    699  A    C  
ATOM   1986  CG  ASN C 928      27.799  17.533 136.787  1.00 63.13      A    C  
ANISOU 1986  CG  ASN C 928     8236  10091   5661  -2318  -1499    803  A    C  
ATOM   1987  ND2 ASN C 928      26.531  17.918 136.790  1.00 73.17      A    N  
ANISOU 1987  ND2 ASN C 928     9202  11585   7013  -2376  -1728   1003  A    N  
ATOM   1988  OD1 ASN C 928      28.388  17.218 135.761  1.00 65.21      A    O  
ANISOU 1988  OD1 ASN C 928     8821  10278   5677  -2463  -1489    713  A    O  
ATOM   1989  N   MET C 929      28.971  19.921 140.627  1.00 42.66      A    N  
ANISOU 1989  N   MET C 929     5040   7296   3873  -1313   -982    810  A    N  
ATOM   1990  CA  MET C 929      29.148  20.147 142.061  1.00 45.29      A    C  
ANISOU 1990  CA  MET C 929     5237   7573   4400  -1100   -824    760  A    C  
ATOM   1991  C   MET C 929      28.158  19.386 142.937  1.00 45.00      A    C  
ANISOU 1991  C   MET C 929     5030   7639   4431  -1178   -823    782  A    C  
ATOM   1992  O   MET C 929      26.943  19.477 142.765  1.00 44.49      A    O  
ANISOU 1992  O   MET C 929     4746   7750   4410  -1257   -962    927  A    O  
ATOM   1993  CB  MET C 929      29.033  21.641 142.360  1.00 47.21      A    C  
ANISOU 1993  CB  MET C 929     5290   7836   4813   -846   -819    861  A    C  
ATOM   1994  CG  MET C 929      30.025  22.480 141.561  1.00 48.28      A    C  
ANISOU 1994  CG  MET C 929     5578   7859   4909   -763   -808    858  A    C  
ATOM   1995  SD  MET C 929      30.061  24.203 142.078  1.00 45.56      A    S  
ANISOU 1995  SD  MET C 929     5051   7467   4792   -458   -762    943  A    S  
ATOM   1996  CE  MET C 929      28.376  24.699 141.709  1.00 43.94      A    C  
ANISOU 1996  CE  MET C 929     4541   7480   4673   -466   -947   1186  A    C  
ATOM   1997  N   TYR C 930      28.700  18.637 143.884  1.00 41.92      A    N  
ANISOU 1997  N   TYR C 930     4728   7141   4060  -1153   -666    658  A    N  
ATOM   1998  CA  TYR C 930      27.911  18.014 144.935  1.00 37.88      A    C  
ANISOU 1998  CA  TYR C 930     4060   6705   3627  -1183   -616    680  A    C  
ATOM   1999  C   TYR C 930      27.753  19.047 146.057  1.00 40.55      A    C  
ANISOU 1999  C   TYR C 930     4201   7075   4131   -913   -511    713  A    C  
ATOM   2000  O   TYR C 930      28.717  19.353 146.771  1.00 35.89      A    O  
ANISOU 2000  O   TYR C 930     3713   6358   3567   -751   -380    611  A    O  
ATOM   2001  CB  TYR C 930      28.596  16.724 145.420  1.00 35.19      A    C  
ANISOU 2001  CB  TYR C 930     3927   6224   3221  -1281   -494    549  A    C  
ATOM   2002  CG  TYR C 930      27.866  15.968 146.517  1.00 36.18      A    C  
ANISOU 2002  CG  TYR C 930     3924   6411   3412  -1330   -427    579  A    C  
ATOM   2003  CD1 TYR C 930      26.487  15.821 146.487  1.00 38.93      A    C  
ANISOU 2003  CD1 TYR C 930     4042   6941   3810  -1457   -526    709  A    C  
ATOM   2004  CD2 TYR C 930      28.565  15.362 147.554  1.00 38.58      A    C  
ANISOU 2004  CD2 TYR C 930     4332   6597   3730  -1262   -268    499  A    C  
ATOM   2005  CE1 TYR C 930      25.818  15.109 147.474  1.00 44.11      A    C  
ANISOU 2005  CE1 TYR C 930     4576   7653   4529  -1512   -445    750  A    C  
ATOM   2006  CE2 TYR C 930      27.899  14.656 148.564  1.00 39.76      A    C  
ANISOU 2006  CE2 TYR C 930     4378   6805   3925  -1313   -196    543  A    C  
ATOM   2007  CZ  TYR C 930      26.531  14.540 148.512  1.00 42.90      A    C  
ANISOU 2007  CZ  TYR C 930     4551   7376   4371  -1438   -273    664  A    C  
ATOM   2008  OH  TYR C 930      25.854  13.835 149.484  1.00 47.20      A    O  
ANISOU 2008  OH  TYR C 930     4986   7982   4967  -1498   -185    723  A    O  
ATOM   2009  N   GLU C 931      26.549  19.601 146.199  1.00 38.46      A    N  
ANISOU 2009  N   GLU C 931     3658   6972   3981   -869   -567    858  A    N  
ATOM   2010  CA  GLU C 931      26.345  20.732 147.104  1.00 40.19      A    C  
ANISOU 2010  CA  GLU C 931     3709   7203   4358   -598   -450    887  A    C  
ATOM   2011  C   GLU C 931      25.962  20.278 148.522  1.00 40.95      A    C  
ANISOU 2011  C   GLU C 931     3720   7333   4506   -544   -282    854  A    C  
ATOM   2012  O   GLU C 931      24.972  19.585 148.710  1.00 39.45      A    O  
ANISOU 2012  O   GLU C 931     3372   7272   4344   -673   -296    945  A    O  
ATOM   2013  CB  GLU C 931      25.272  21.681 146.534  1.00 43.85      A    C  
ANISOU 2013  CB  GLU C 931     3902   7806   4952   -531   -562   1079  A    C  
ATOM   2014  CG  GLU C 931      25.620  22.195 145.116  1.00 51.63      A    C  
ANISOU 2014  CG  GLU C 931     4979   8773   5866   -585   -739   1140  A    C  
ATOM   2015  CD  GLU C 931      24.778  23.398 144.658  1.00 57.61      A    C  
ANISOU 2015  CD  GLU C 931     5480   9629   6782   -446   -833   1346  A    C  
ATOM   2016  OE1 GLU C 931      23.655  23.595 145.167  1.00 60.78      A    O  
ANISOU 2016  OE1 GLU C 931     5587  10158   7347   -375   -809   1480  A    O  
ATOM   2017  OE2 GLU C 931      25.247  24.149 143.772  1.00 61.96      A    O1-
ANISOU 2017  OE2 GLU C 931     6116  10123   7304   -402   -921   1392  A    O1-
ATOM   2018  N   LEU C 932      26.766  20.672 149.510  1.00 40.41      A    N  
ANISOU 2018  N   LEU C 932     3763   7151   4441   -368   -128    732  A    N  
ATOM   2019  CA  LEU C 932      26.552  20.272 150.900  1.00 39.78      A    C  
ANISOU 2019  CA  LEU C 932     3656   7096   4363   -315     40    691  A    C  
ATOM   2020  C   LEU C 932      26.338  21.476 151.825  1.00 40.84      A    C  
ANISOU 2020  C   LEU C 932     3697   7227   4596    -58    189    669  A    C  
ATOM   2021  O   LEU C 932      26.779  22.598 151.538  1.00 40.96      A    O  
ANISOU 2021  O   LEU C 932     3743   7153   4666     92    175    636  A    O  
ATOM   2022  CB  LEU C 932      27.742  19.446 151.388  1.00 37.05      A    C  
ANISOU 2022  CB  LEU C 932     3567   6618   3891   -371     89    559  A    C  
ATOM   2023  CG  LEU C 932      27.931  18.128 150.634  1.00 39.26      A    C  
ANISOU 2023  CG  LEU C 932     3966   6868   4084   -615     -2    563  A    C  
ATOM   2024  CD1 LEU C 932      29.171  17.438 151.125  1.00 35.31      A    C  
ANISOU 2024  CD1 LEU C 932     3698   6216   3503   -621     64    456  A    C  
ATOM   2025  CD2 LEU C 932      26.705  17.209 150.811  1.00 44.09      A    C  
ANISOU 2025  CD2 LEU C 932     4423   7615   4714   -786     -5    668  A    C  
ATOM   2026  N   LYS C 933      25.671  21.236 152.946  1.00 40.54      A    N  
ANISOU 2026  N   LYS C 933     3561   7270   4573    -13    348    684  A    N  
ATOM   2027  CA  LYS C 933      25.337  22.303 153.880  1.00 42.70      A    C  
ANISOU 2027  CA  LYS C 933     3761   7538   4924    224    529    653  A    C  
ATOM   2028  C   LYS C 933      26.001  22.093 155.245  1.00 45.10      A    C  
ANISOU 2028  C   LYS C 933     4265   7782   5089    277    684    507  A    C  
ATOM   2029  O   LYS C 933      25.894  22.941 156.141  1.00 44.61      A    O  
ANISOU 2029  O   LYS C 933     4220   7691   5039    459    851    435  A    O  
ATOM   2030  CB  LYS C 933      23.828  22.395 154.052  1.00 42.57      A    C  
ANISOU 2030  CB  LYS C 933     3430   7688   5056    265    621    815  A    C  
ATOM   2031  CG  LYS C 933      23.077  22.724 152.767  1.00 47.45      A    C  
ANISOU 2031  CG  LYS C 933     3815   8391   5825    223    447    993  A    C  
ATOM   2032  CD  LYS C 933      21.604  22.966 153.053  1.00 49.21      A    C  
ANISOU 2032  CD  LYS C 933     3683   8775   6241    304    557   1176  A    C  
ATOM   2033  CE  LYS C 933      20.830  23.280 151.777  1.00 56.06      A    C  
ANISOU 2033  CE  LYS C 933     4291   9748   7262    250    346   1390  A    C  
ATOM   2034  NZ  LYS C 933      19.400  23.604 152.121  1.00 59.68      A    N1+
ANISOU 2034  NZ  LYS C 933     4358  10363   7955    362    470   1594  A    N1+
ATOM   2035  N   HIS C 934      26.661  20.950 155.402  1.00 39.80      A    N  
ANISOU 2035  N   HIS C 934     3752   7088   4284    115    631    472  A    N  
ATOM   2036  CA  HIS C 934      27.342  20.628 156.650  1.00 41.78      A    C  
ANISOU 2036  CA  HIS C 934     4193   7295   4386    139    738    369  A    C  
ATOM   2037  C   HIS C 934      28.557  19.808 156.295  1.00 45.70      A    C  
ANISOU 2037  C   HIS C 934     4887   7686   4793      9    604    325  A    C  
ATOM   2038  O   HIS C 934      28.637  19.267 155.183  1.00 41.41      A    O  
ANISOU 2038  O   HIS C 934     4328   7120   4286   -121    476    375  A    O  
ATOM   2039  CB  HIS C 934      26.447  19.841 157.619  1.00 40.72      A    C  
ANISOU 2039  CB  HIS C 934     3974   7293   4203     88    895    444  A    C  
ATOM   2040  CG  HIS C 934      25.126  20.494 157.875  1.00 48.91      A    C  
ANISOU 2040  CG  HIS C 934     4769   8450   5366    208   1052    523  A    C  
ATOM   2041  CD2 HIS C 934      23.946  20.394 157.221  1.00 48.26      A    C  
ANISOU 2041  CD2 HIS C 934     4403   8489   5446    162   1035    682  A    C  
ATOM   2042  ND1 HIS C 934      24.921  21.398 158.899  1.00 51.50      A    N  
ANISOU 2042  ND1 HIS C 934     5125   8774   5669    403   1260    443  A    N  
ATOM   2043  CE1 HIS C 934      23.672  21.826 158.860  1.00 49.87      A    C  
ANISOU 2043  CE1 HIS C 934     4653   8671   5625    497   1392    554  A    C  
ATOM   2044  NE2 HIS C 934      23.056  21.225 157.858  1.00 50.45      A    N  
ANISOU 2044  NE2 HIS C 934     4515   8832   5821    350   1246    714  A    N  
ATOM   2045  N   ALA C 935      29.486  19.714 157.246  1.00 42.17      A    N  
ANISOU 2045  N   ALA C 935     4626   7174   4225     43    639    237  A    N  
ATOM   2046  CA  ALA C 935      30.685  18.925 157.083  1.00 41.90      A    C  
ANISOU 2046  CA  ALA C 935     4757   7034   4128    -52    538    216  A    C  
ATOM   2047  C   ALA C 935      30.308  17.503 156.745  1.00 38.71      A    C  
ANISOU 2047  C   ALA C 935     4328   6660   3719   -228    523    317  A    C  
ATOM   2048  O   ALA C 935      29.351  16.974 157.282  1.00 40.84      A    O  
ANISOU 2048  O   ALA C 935     4506   7039   3972   -280    617    392  A    O  
ATOM   2049  CB  ALA C 935      31.550  18.966 158.370  1.00 46.17      A    C  
ANISOU 2049  CB  ALA C 935     5466   7543   4534      2    573    148  A    C  
ATOM   2050  N   SER C 936      31.082  16.887 155.858  1.00 36.98      A    N  
ANISOU 2050  N   SER C 936     4200   6329   3522   -323    422    316  A    N  
ATOM   2051  CA  SER C 936      30.849  15.509 155.475  1.00 38.02      A    C  
ANISOU 2051  CA  SER C 936     4355   6440   3651   -501    412    387  A    C  
ATOM   2052  C   SER C 936      32.161  14.883 155.036  1.00 39.40      A    C  
ANISOU 2052  C   SER C 936     4704   6443   3824   -537    361    356  A    C  
ATOM   2053  O   SER C 936      32.755  15.313 154.041  1.00 40.50      A    O  
ANISOU 2053  O   SER C 936     4884   6500   4006   -520    293    306  A    O  
ATOM   2054  CB  SER C 936      29.804  15.426 154.345  1.00 40.66      A    C  
ANISOU 2054  CB  SER C 936     4555   6843   4052   -621    352    437  A    C  
ATOM   2055  OG  SER C 936      29.522  14.076 154.036  1.00 38.32      A    O  
ANISOU 2055  OG  SER C 936     4302   6514   3745   -821    344    491  A    O  
ATOM   2056  N   HIS C 937      32.605  13.854 155.752  1.00 37.70      A    N  
ANISOU 2056  N   HIS C 937     4585   6170   3571   -582    407    402  A    N  
ATOM   2057  CA  HIS C 937      33.934  13.301 155.509  1.00 39.85      A    C  
ANISOU 2057  CA  HIS C 937     5000   6271   3872   -575    383    395  A    C  
ATOM   2058  C   HIS C 937      33.935  12.351 154.311  1.00 44.35      A    C  
ANISOU 2058  C   HIS C 937     5643   6718   4492   -718    382    395  A    C  
ATOM   2059  O   HIS C 937      34.081  11.137 154.460  1.00 46.77      A    O  
ANISOU 2059  O   HIS C 937     6036   6923   4810   -808    435    448  A    O  
ATOM   2060  CB  HIS C 937      34.457  12.604 156.764  1.00 39.46      A    C  
ANISOU 2060  CB  HIS C 937     5020   6199   3772   -550    423    470  A    C  
ATOM   2061  CG  HIS C 937      34.401  13.461 157.987  1.00 38.76      A    C  
ANISOU 2061  CG  HIS C 937     4905   6237   3586   -440    427    457  A    C  
ATOM   2062  CD2 HIS C 937      33.766  13.288 159.172  1.00 42.31      A    C  
ANISOU 2062  CD2 HIS C 937     5344   6808   3925   -442    499    511  A    C  
ATOM   2063  ND1 HIS C 937      35.060  14.673 158.077  1.00 40.22      A    N  
ANISOU 2063  ND1 HIS C 937     5093   6422   3765   -320    364    370  A    N  
ATOM   2064  CE1 HIS C 937      34.837  15.205 159.268  1.00 44.89      A    C  
ANISOU 2064  CE1 HIS C 937     5697   7121   4237   -259    391    354  A    C  
ATOM   2065  NE2 HIS C 937      34.058  14.384 159.953  1.00 46.01      A    N  
ANISOU 2065  NE2 HIS C 937     5832   7344   4304   -325    481    440  A    N  
ATOM   2066  N   ILE C 938      33.771  12.939 153.132  1.00 42.43      A    N  
ANISOU 2066  N   ILE C 938     5380   6476   4268   -742    326    335  A    N  
ATOM   2067  CA  ILE C 938      33.676  12.212 151.863  1.00 47.98      A    C  
ANISOU 2067  CA  ILE C 938     6177   7079   4974   -897    316    308  A    C  
ATOM   2068  C   ILE C 938      34.907  11.355 151.587  1.00 44.74      A    C  
ANISOU 2068  C   ILE C 938     5943   6451   4606   -892    387    291  A    C  
ATOM   2069  O   ILE C 938      36.045  11.828 151.703  1.00 39.06      A    O  
ANISOU 2069  O   ILE C 938     5247   5658   3934   -750    398    279  A    O  
ATOM   2070  CB  ILE C 938      33.470  13.190 150.674  1.00 59.70      A    C  
ANISOU 2070  CB  ILE C 938     7625   8613   6445   -898    232    258  A    C  
ATOM   2071  CG1 ILE C 938      31.998  13.572 150.536  1.00 63.73      A    C  
ANISOU 2071  CG1 ILE C 938     7965   9312   6937   -977    160    305  A    C  
ATOM   2072  CG2 ILE C 938      33.939  12.594 149.365  1.00 60.76      A    C  
ANISOU 2072  CG2 ILE C 938     7932   8603   6553  -1014    239    203  A    C  
ATOM   2073  CD1 ILE C 938      31.673  14.934 151.084  1.00 65.03      A    C  
ANISOU 2073  CD1 ILE C 938     7964   9607   7136   -805    141    321  A    C  
ATOM   2074  N   SER C 939      34.673  10.090 151.244  1.00 38.96      A    N  
ANISOU 2074  N   SER C 939     5326   5605   3872  -1049    443    298  A    N  
ATOM   2075  CA  SER C 939      35.727   9.233 150.731  1.00 43.15      A    C  
ANISOU 2075  CA  SER C 939     6040   5898   4458  -1050    541    272  A    C  
ATOM   2076  C   SER C 939      35.703   9.249 149.203  1.00 45.37      A    C  
ANISOU 2076  C   SER C 939     6448   6105   4685  -1162    540    168  A    C  
ATOM   2077  O   SER C 939      36.747   9.176 148.562  1.00 52.01      A    O  
ANISOU 2077  O   SER C 939     7412   6786   5562  -1096    624    122  A    O  
ATOM   2078  CB  SER C 939      35.581   7.806 151.252  1.00 54.74      A    C  
ANISOU 2078  CB  SER C 939     7600   7235   5964  -1149    631    333  A    C  
ATOM   2079  OG  SER C 939      36.184   7.687 152.534  1.00 66.26      A    O  
ANISOU 2079  OG  SER C 939     9004   8692   7481  -1006    659    442  A    O  
ATOM   2080  N   LYS C 940      34.508   9.359 148.634  1.00 45.83      A    N  
ANISOU 2080  N   LYS C 940     6470   6291   4651  -1333    443    145  A    N  
ATOM   2081  CA  LYS C 940      34.321   9.323 147.180  1.00 51.07      A    C  
ANISOU 2081  CA  LYS C 940     7273   6914   5216  -1484    409     55  A    C  
ATOM   2082  C   LYS C 940      33.103  10.148 146.795  1.00 47.86      A    C  
ANISOU 2082  C   LYS C 940     6705   6746   4733  -1576    236     84  A    C  
ATOM   2083  O   LYS C 940      32.061  10.032 147.437  1.00 46.68      A    O  
ANISOU 2083  O   LYS C 940     6398   6737   4601  -1648    174    156  A    O  
ATOM   2084  CB  LYS C 940      34.134   7.883 146.688  1.00 55.85      A    C  
ANISOU 2084  CB  LYS C 940     8100   7336   5786  -1701    486     -3  A    C  
ATOM   2085  CG  LYS C 940      34.151   7.736 145.175  1.00 60.60      A    C  
ANISOU 2085  CG  LYS C 940     8919   7857   6249  -1865    477   -121  A    C  
ATOM   2086  CD  LYS C 940      33.894   6.296 144.761  1.00 64.87      A    C  
ANISOU 2086  CD  LYS C 940     9705   8197   6747  -2102    556   -200  A    C  
ATOM   2087  CE  LYS C 940      32.455   5.903 145.037  0.91 65.95      A    C  
ANISOU 2087  CE  LYS C 940     9728   8479   6851  -2340    406   -147  A    C  
ATOM   2088  NZ  LYS C 940      31.506   6.698 144.200  0.75 64.91      A    N1+
ANISOU 2088  NZ  LYS C 940     9499   8582   6581  -2487    190   -143  A    N1+
ATOM   2089  N   LEU C 941      33.224  10.970 145.755  1.00 43.17      A    N  
ANISOU 2089  N   LEU C 941     6140   6198   4064  -1571    165     48  A    N  
ATOM   2090  CA  LEU C 941      32.077  11.728 145.263  1.00 43.16      A    C  
ANISOU 2090  CA  LEU C 941     5984   6415   4001  -1660    -13    103  A    C  
ATOM   2091  C   LEU C 941      30.978  10.795 144.810  1.00 46.39      A    C  
ANISOU 2091  C   LEU C 941     6431   6867   4329  -1954   -105    106  A    C  
ATOM   2092  O   LEU C 941      31.257   9.666 144.448  1.00 44.22      A    O  
ANISOU 2092  O   LEU C 941     6386   6414   4000  -2108    -28     23  A    O  
ATOM   2093  CB  LEU C 941      32.474  12.647 144.110  1.00 38.98      A    C  
ANISOU 2093  CB  LEU C 941     5520   5903   3388  -1625    -71     78  A    C  
ATOM   2094  CG  LEU C 941      33.326  13.828 144.587  1.00 40.39      A    C  
ANISOU 2094  CG  LEU C 941     5595   6080   3669  -1350    -23    101  A    C  
ATOM   2095  CD1 LEU C 941      33.903  14.572 143.387  1.00 40.55      A    C  
ANISOU 2095  CD1 LEU C 941     5723   6071   3611  -1327    -41     80  A    C  
ATOM   2096  CD2 LEU C 941      32.496  14.751 145.485  1.00 42.64      A    C  
ANISOU 2096  CD2 LEU C 941     5603   6553   4047  -1233   -105    195  A    C  
ATOM   2097  N   PRO C 942      29.722  11.262 144.854  1.00 47.20      A    N  
ANISOU 2097  N   PRO C 942     6300   7194   4441  -2032   -264    210  A    N  
ATOM   2098  CA  PRO C 942      28.640  10.506 144.221  1.00 49.39      A    C  
ANISOU 2098  CA  PRO C 942     6593   7539   4635  -2349   -402    229  A    C  
ATOM   2099  C   PRO C 942      28.893  10.401 142.725  1.00 50.75      A    C  
ANISOU 2099  C   PRO C 942     7016   7649   4615  -2524   -486    139  A    C  
ATOM   2100  O   PRO C 942      29.547  11.295 142.153  1.00 47.96      A    O  
ANISOU 2100  O   PRO C 942     6713   7296   4212  -2379   -484    123  A    O  
ATOM   2101  CB  PRO C 942      27.387  11.346 144.509  1.00 50.09      A    C  
ANISOU 2101  CB  PRO C 942     6327   7902   4803  -2333   -556    390  A    C  
ATOM   2102  CG  PRO C 942      27.758  12.167 145.733  1.00 49.88      A    C  
ANISOU 2102  CG  PRO C 942     6127   7905   4919  -2012   -426    432  A    C  
ATOM   2103  CD  PRO C 942      29.231  12.453 145.570  1.00 45.35      A    C  
ANISOU 2103  CD  PRO C 942     5769   7149   4314  -1835   -309    320  A    C  
ATOM   2104  N   LYS C 943      28.392   9.333 142.106  1.00 50.81      A    N  
ANISOU 2104  N   LYS C 943     7198   7600   4509  -2841   -551     80  A    N  
ATOM   2105  CA  LYS C 943      28.567   9.127 140.673  1.00 56.19      A    C  
ANISOU 2105  CA  LYS C 943     8168   8221   4962  -3050   -629    -25  A    C  
ATOM   2106  C   LYS C 943      28.112  10.358 139.898  1.00 56.06      A    C  
ANISOU 2106  C   LYS C 943     8004   8436   4860  -3031   -840     83  A    C  
ATOM   2107  O   LYS C 943      27.016  10.873 140.116  1.00 53.21      A    O  
ANISOU 2107  O   LYS C 943     7331   8312   4574  -3066  -1028    245  A    O  
ATOM   2108  CB  LYS C 943      27.794   7.889 140.194  1.00 57.38      A    C  
ANISOU 2108  CB  LYS C 943     8484   8319   4998  -3442   -726    -88  A    C  
ATOM   2109  CG  LYS C 943      28.290   6.578 140.804  1.00 61.99      A    C  
ANISOU 2109  CG  LYS C 943     9270   8623   5660  -3483   -504   -200  A    C  
ATOM   2110  CD  LYS C 943      27.287   5.437 140.571  1.00 66.75      A    C  
ANISOU 2110  CD  LYS C 943     9957   9199   6204  -3881   -624   -226  A    C  
ATOM   2111  CE  LYS C 943      26.074   5.536 141.512  1.00 68.24      A    C  
ANISOU 2111  CE  LYS C 943     9742   9616   6569  -3929   -757    -32  A    C  
ATOM   2112  N   GLY C 944      28.971  10.839 139.008  1.00 54.43      A    N  
ANISOU 2112  N   GLY C 944     8011   8157   4513  -2960   -793     13  A    N  
ATOM   2113  CA  GLY C 944      28.613  11.951 138.154  1.00 54.35      A    C  
ANISOU 2113  CA  GLY C 944     7908   8343   4398  -2957   -989    124  A    C  
ATOM   2114  C   GLY C 944      29.029  13.306 138.697  1.00 49.88      A    C  
ANISOU 2114  C   GLY C 944     7102   7846   4003  -2604   -938    232  A    C  
ATOM   2115  O   GLY C 944      28.951  14.297 137.972  1.00 53.13      A    O  
ANISOU 2115  O   GLY C 944     7467   8375   4346  -2559  -1060    326  A    O  
ATOM   2116  N   LYS C 945      29.467  13.351 139.955  1.00 42.98      A    N  
ANISOU 2116  N   LYS C 945     6094   6894   3343  -2369   -766    222  A    N  
ATOM   2117  CA  LYS C 945      29.937  14.595 140.577  1.00 44.39      A    C  
ANISOU 2117  CA  LYS C 945     6078   7105   3684  -2046   -702    294  A    C  
ATOM   2118  C   LYS C 945      31.444  14.706 140.457  1.00 44.51      A    C  
ANISOU 2118  C   LYS C 945     6307   6911   3692  -1883   -498    182  A    C  
ATOM   2119  O   LYS C 945      32.141  13.685 140.492  1.00 42.67      A    O  
ANISOU 2119  O   LYS C 945     6296   6490   3427  -1938   -341     57  A    O  
ATOM   2120  CB  LYS C 945      29.543  14.663 142.065  1.00 40.62      A    C  
ANISOU 2120  CB  LYS C 945     5337   6678   3420  -1891   -640    349  A    C  
ATOM   2121  CG  LYS C 945      28.039  14.674 142.301  1.00 42.74      A    C  
ANISOU 2121  CG  LYS C 945     5330   7164   3745  -2011   -807    489  A    C  
ATOM   2122  CD  LYS C 945      27.379  15.909 141.702  1.00 44.21      A    C  
ANISOU 2122  CD  LYS C 945     5312   7536   3951  -1951   -985    644  A    C  
ATOM   2123  CE  LYS C 945      25.911  15.951 142.061  1.00 47.46      A    C  
ANISOU 2123  CE  LYS C 945     5394   8163   4474  -2032  -1125    811  A    C  
ATOM   2124  NZ  LYS C 945      25.322  17.254 141.701  1.00 50.49      A    N1+
ANISOU 2124  NZ  LYS C 945     5532   8708   4942  -1898  -1260    989  A    N1+
ATOM   2125  N   HIS C 946      31.942  15.939 140.330  1.00 42.09      A    N  
ANISOU 2125  N   HIS C 946     5922   6629   3443  -1680   -493    240  A    N  
ATOM   2126  CA  HIS C 946      33.369  16.178 140.149  1.00 39.95      A    C  
ANISOU 2126  CA  HIS C 946     5815   6179   3187  -1530   -312    163  A    C  
ATOM   2127  C   HIS C 946      33.975  17.053 141.238  1.00 36.83      A    C  
ANISOU 2127  C   HIS C 946     5235   5753   3004  -1253   -232    194  A    C  
ATOM   2128  O   HIS C 946      35.201  17.199 141.318  1.00 37.56      A    O  
ANISOU 2128  O   HIS C 946     5417   5697   3158  -1124    -83    143  A    O  
ATOM   2129  CB  HIS C 946      33.612  16.821 138.789  1.00 44.74      A    C  
ANISOU 2129  CB  HIS C 946     6562   6808   3631  -1581   -365    194  A    C  
ATOM   2130  CG  HIS C 946      32.988  16.072 137.663  1.00 46.29      A    C  
ANISOU 2130  CG  HIS C 946     6964   7053   3572  -1876   -475    162  A    C  
ATOM   2131  CD2 HIS C 946      33.239  14.838 137.169  1.00 46.39      A    C  
ANISOU 2131  CD2 HIS C 946     7268   6932   3427  -2071   -378     18  A    C  
ATOM   2132  ND1 HIS C 946      31.960  16.589 136.906  1.00 49.04      A    N  
ANISOU 2132  ND1 HIS C 946     7234   7603   3795  -2014   -720    287  A    N  
ATOM   2133  CE1 HIS C 946      31.608  15.707 135.988  1.00 51.34      A    C  
ANISOU 2133  CE1 HIS C 946     7768   7900   3840  -2304   -793    217  A    C  
ATOM   2134  NE2 HIS C 946      32.368  14.636 136.127  1.00 49.57      A    N  
ANISOU 2134  NE2 HIS C 946     7785   7461   3589  -2344   -576     40  A    N  
ATOM   2135  N   SER C 947      33.125  17.617 142.089  1.00 36.61      A    N  
ANISOU 2135  N   SER C 947     4954   5862   3094  -1169   -322    277  A    N  
ATOM   2136  CA  SER C 947      33.601  18.460 143.190  1.00 35.23      A    C  
ANISOU 2136  CA  SER C 947     4630   5660   3096   -929   -254    287  A    C  
ATOM   2137  C   SER C 947      32.525  18.594 144.248  1.00 35.95      A    C  
ANISOU 2137  C   SER C 947     4492   5886   3281   -885   -303    344  A    C  
ATOM   2138  O   SER C 947      31.354  18.271 144.007  1.00 36.81      A    O  
ANISOU 2138  O   SER C 947     4505   6132   3348  -1023   -412    412  A    O  
ATOM   2139  CB  SER C 947      33.982  19.856 142.686  1.00 32.79      A    C  
ANISOU 2139  CB  SER C 947     4278   5350   2832   -792   -287    346  A    C  
ATOM   2140  OG  SER C 947      32.857  20.452 142.050  1.00 38.20      A    O  
ANISOU 2140  OG  SER C 947     4841   6193   3479   -846   -449    467  A    O  
ATOM   2141  N   VAL C 948      32.925  19.082 145.414  1.00 34.46      A    N  
ANISOU 2141  N   VAL C 948     4218   5662   3215   -702   -222    320  A    N  
ATOM   2142  CA  VAL C 948      31.972  19.493 146.437  1.00 33.52      A    C  
ANISOU 2142  CA  VAL C 948     3888   5664   3184   -615   -230    370  A    C  
ATOM   2143  C   VAL C 948      31.897  21.009 146.465  1.00 32.49      A    C  
ANISOU 2143  C   VAL C 948     3638   5552   3154   -432   -254    417  A    C  
ATOM   2144  O   VAL C 948      32.935  21.674 146.396  1.00 34.34      A    O  
ANISOU 2144  O   VAL C 948     3957   5667   3425   -327   -216    370  A    O  
ATOM   2145  CB  VAL C 948      32.375  18.973 147.832  1.00 34.65      A    C  
ANISOU 2145  CB  VAL C 948     4045   5758   3362   -548   -114    306  A    C  
ATOM   2146  CG1 VAL C 948      31.639  19.727 148.921  1.00 36.74      A    C  
ANISOU 2146  CG1 VAL C 948     4130   6122   3709   -408    -81    335  A    C  
ATOM   2147  CG2 VAL C 948      32.093  17.477 147.957  1.00 36.92      A    C  
ANISOU 2147  CG2 VAL C 948     4403   6042   3582   -725    -88    297  A    C  
ATOM   2148  N   LYS C 949      30.687  21.556 146.536  1.00 33.11      A    N  
ANISOU 2148  N   LYS C 949     3512   5769   3298   -395   -312    519  A    N  
ATOM   2149  CA  LYS C 949      30.503  22.933 146.979  1.00 35.87      A    C  
ANISOU 2149  CA  LYS C 949     3734   6113   3784   -183   -281    551  A    C  
ATOM   2150  C   LYS C 949      29.830  22.991 148.348  1.00 37.63      A    C  
ANISOU 2150  C   LYS C 949     3821   6397   4081    -78   -172    534  A    C  
ATOM   2151  O   LYS C 949      28.681  22.570 148.500  1.00 39.77      A    O  
ANISOU 2151  O   LYS C 949     3928   6811   4373   -138   -184    622  A    O  
ATOM   2152  CB  LYS C 949      29.670  23.749 145.987  1.00 40.82      A    C  
ANISOU 2152  CB  LYS C 949     4216   6829   4465   -168   -403    708  A    C  
ATOM   2153  CG  LYS C 949      29.426  25.181 146.470  1.00 43.73      A    C  
ANISOU 2153  CG  LYS C 949     4452   7159   5006     71   -345    748  A    C  
ATOM   2154  CD  LYS C 949      28.777  26.056 145.382  1.00 51.83      A    C  
ANISOU 2154  CD  LYS C 949     5347   8243   6103    105   -473    933  A    C  
ATOM   2155  CE  LYS C 949      28.651  27.501 145.867  1.00 54.95      A    C  
ANISOU 2155  CE  LYS C 949     5639   8546   6695    361   -386    963  A    C  
ATOM   2156  NZ  LYS C 949      28.019  28.401 144.863  1.00 61.15      A    N1+
ANISOU 2156  NZ  LYS C 949     6281   9372   7579    421   -505   1175  A    N1+
ATOM   2157  N   GLY C 950      30.550  23.515 149.337  1.00 34.99      A    N  
ANISOU 2157  N   GLY C 950     3560   5958   3778     65    -64    425  A    N  
ATOM   2158  CA  GLY C 950      29.966  23.789 150.644  1.00 31.98      A    C  
ANISOU 2158  CA  GLY C 950     3087   5621   3442    186     63    394  A    C  
ATOM   2159  C   GLY C 950      29.228  25.122 150.527  1.00 36.73      A    C  
ANISOU 2159  C   GLY C 950     3531   6232   4194    360     89    464  A    C  
ATOM   2160  O   GLY C 950      29.815  26.135 150.164  1.00 37.26      A    O  
ANISOU 2160  O   GLY C 950     3657   6177   4325    460     69    441  A    O  
ATOM   2161  N   LEU C 951      27.941  25.124 150.827  1.00 41.35      A    N  
ANISOU 2161  N   LEU C 951     3903   6951   4856    401    143    564  A    N  
ATOM   2162  CA  LEU C 951      27.117  26.315 150.625  1.00 45.18      A    C  
ANISOU 2162  CA  LEU C 951     4199   7446   5521    579    175    671  A    C  
ATOM   2163  C   LEU C 951      27.172  27.258 151.809  1.00 47.11      A    C  
ANISOU 2163  C   LEU C 951     4480   7586   5834    796    375    555  A    C  
ATOM   2164  O   LEU C 951      26.745  26.899 152.896  1.00 49.52      A    O  
ANISOU 2164  O   LEU C 951     4763   7950   6102    826    527    501  A    O  
ATOM   2165  CB  LEU C 951      25.672  25.920 150.375  1.00 43.82      A    C  
ANISOU 2165  CB  LEU C 951     3743   7470   5435    532    148    858  A    C  
ATOM   2166  CG  LEU C 951      25.383  25.076 149.140  1.00 44.53      A    C  
ANISOU 2166  CG  LEU C 951     3782   7681   5458    296    -72    988  A    C  
ATOM   2167  CD1 LEU C 951      23.866  24.873 149.002  1.00 44.34      A    C  
ANISOU 2167  CD1 LEU C 951     3428   7858   5560    261   -108   1195  A    C  
ATOM   2168  CD2 LEU C 951      25.968  25.738 147.900  1.00 47.24      A    C  
ANISOU 2168  CD2 LEU C 951     4211   7945   5793    291   -228   1035  A    C  
ATOM   2169  N   GLY C 952      27.676  28.470 151.597  1.00 42.64      A    N  
ANISOU 2169  N   GLY C 952     3983   6857   5361    938    385    515  A    N  
ATOM   2170  CA  GLY C 952      27.807  29.425 152.686  1.00 44.24      A    C  
ANISOU 2170  CA  GLY C 952     4271   6923   5616   1127    574    374  A    C  
ATOM   2171  C   GLY C 952      26.621  30.364 152.876  1.00 49.54      A    C  
ANISOU 2171  C   GLY C 952     4732   7594   6496   1346    727    472  A    C  
ATOM   2172  O   GLY C 952      25.765  30.493 151.997  1.00 51.86      A    O  
ANISOU 2172  O   GLY C 952     4788   7982   6934   1370    648    685  A    O  
ATOM   2173  N   LYS C 953      26.564  31.014 154.036  1.00 53.82      A    N  
ANISOU 2173  N   LYS C 953     5366   8030   7054   1505    949    322  A    N  
ATOM   2174  CA  LYS C 953      25.560  32.046 154.310  1.00 57.45      A    C  
ANISOU 2174  CA  LYS C 953     5663   8431   7734   1754   1151    386  A    C  
ATOM   2175  C   LYS C 953      25.815  33.282 153.448  1.00 58.43      A    C  
ANISOU 2175  C   LYS C 953     5784   8368   8051   1880   1085    453  A    C  
ATOM   2176  O   LYS C 953      24.880  34.004 153.088  1.00 60.54      A    O  
ANISOU 2176  O   LYS C 953     5826   8619   8557   2063   1159    623  A    O  
ATOM   2177  CB  LYS C 953      25.573  32.451 155.788  1.00 60.01      A    C  
ANISOU 2177  CB  LYS C 953     6160   8654   7986   1881   1428    166  A    C  
ATOM   2178  CG  LYS C 953      24.836  31.529 156.746  0.91 63.93      A    C  
ANISOU 2178  CG  LYS C 953     6582   9338   8368   1848   1592    160  A    C  
ATOM   2179  CD  LYS C 953      25.021  32.010 158.188  0.39 67.12      A    C  
ANISOU 2179  CD  LYS C 953     7232   9625   8647   1959   1860    -83  A    C  
ATOM   2180  CE  LYS C 953      24.154  31.244 159.187  0.77 70.16      A    C  
ANISOU 2180  CE  LYS C 953     7535  10191   8932   1962   2083    -70  A    C  
ATOM   2181  NZ  LYS C 953      23.154  32.131 159.876  1.00 75.97      A    N1+
ANISOU 2181  NZ  LYS C 953     8186  10858   9821   2230   2440    -89  A    N1+
ATOM   2182  N   THR C 954      27.089  33.520 153.136  1.00 55.15      A    N  
ANISOU 2182  N   THR C 954     5605   7804   7544   1785    952    336  A    N  
ATOM   2183  CA  THR C 954      27.512  34.688 152.360  1.00 55.23      A    C  
ANISOU 2183  CA  THR C 954     5655   7611   7718   1879    892    387  A    C  
ATOM   2184  C   THR C 954      28.171  34.268 151.045  1.00 54.11      A    C  
ANISOU 2184  C   THR C 954     5519   7525   7515   1698    627    512  A    C  
ATOM   2185  O   THR C 954      28.918  33.297 150.997  1.00 46.90      A    O  
ANISOU 2185  O   THR C 954     4723   6692   6403   1499    515    436  A    O  
ATOM   2186  CB  THR C 954      28.507  35.573 153.155  1.00 73.29      A    C  
ANISOU 2186  CB  THR C 954     8237   9631   9980   1931    995    133  A    C  
ATOM   2187  CG2 THR C 954      28.844  36.847 152.396  1.00 72.00      A    C  
ANISOU 2187  CG2 THR C 954     8104   9232  10022   2038    960    199  A    C  
ATOM   2188  OG1 THR C 954      27.947  35.916 154.427  1.00 76.49      A    O  
ANISOU 2188  OG1 THR C 954     8694   9980  10390   2080   1259    -18  A    O  
ATOM   2189  N   THR C 955      27.908  35.017 149.982  1.00 55.81      A    N  
ANISOU 2189  N   THR C 955     5619   7687   7901   1776    541    709  A    N  
ATOM   2190  CA  THR C 955      28.413  34.658 148.668  1.00 54.24      A    C  
ANISOU 2190  CA  THR C 955     5429   7553   7625   1610    309    846  A    C  
ATOM   2191  C   THR C 955      28.647  35.917 147.829  1.00 52.87      A    C  
ANISOU 2191  C   THR C 955     5264   7194   7631   1723    267    975  A    C  
ATOM   2192  O   THR C 955      27.947  36.917 148.000  1.00 53.95      A    O  
ANISOU 2192  O   THR C 955     5285   7218   7994   1943    385   1059  A    O  
ATOM   2193  CB  THR C 955      27.431  33.705 147.951  1.00 59.17      A    C  
ANISOU 2193  CB  THR C 955     5826   8455   8202   1499    171   1056  A    C  
ATOM   2194  CG2 THR C 955      26.108  34.426 147.588  1.00 61.26      A    C  
ANISOU 2194  CG2 THR C 955     5794   8771   8711   1685    189   1311  A    C  
ATOM   2195  OG1 THR C 955      28.037  33.188 146.766  1.00 62.65      A    O  
ANISOU 2195  OG1 THR C 955     6347   8961   8498   1300    -38   1136  A    O  
ATOM   2196  N   PRO C 956      29.655  35.887 146.946  1.00 50.94      A    N  
ANISOU 2196  N   PRO C 956     5161   6900   7295   1583    124    996  A    N  
ATOM   2197  CA  PRO C 956      29.822  37.023 146.030  1.00 52.27      A    C  
ANISOU 2197  CA  PRO C 956     5325   6910   7623   1673     73   1163  A    C  
ATOM   2198  C   PRO C 956      28.553  37.254 145.218  1.00 56.89      A    C  
ANISOU 2198  C   PRO C 956     5643   7633   8339   1768    -11   1471  A    C  
ATOM   2199  O   PRO C 956      27.961  36.291 144.733  1.00 59.82      A    O  
ANISOU 2199  O   PRO C 956     5886   8259   8584   1636   -145   1588  A    O  
ATOM   2200  CB  PRO C 956      30.985  36.591 145.130  1.00 46.90      A    C  
ANISOU 2200  CB  PRO C 956     4811   6237   6770   1465    -69   1161  A    C  
ATOM   2201  CG  PRO C 956      31.796  35.650 146.006  1.00 47.13      A    C  
ANISOU 2201  CG  PRO C 956     4993   6293   6621   1329    -25    904  A    C  
ATOM   2202  CD  PRO C 956      30.767  34.918 146.852  1.00 46.72      A    C  
ANISOU 2202  CD  PRO C 956     4807   6412   6531   1360     40    860  A    C  
ATOM   2203  N   ASP C 957      28.135  38.510 145.112  1.00 56.40      A    N  
ANISOU 2203  N   ASP C 957     5498   7395   8538   1989     64   1604  A    N  
ATOM   2204  CA  ASP C 957      26.964  38.883 144.330  1.00 60.40      A    C  
ANISOU 2204  CA  ASP C 957     5727   8011   9213   2106    -25   1940  A    C  
ATOM   2205  C   ASP C 957      27.079  38.327 142.911  1.00 62.99      A    C  
ANISOU 2205  C   ASP C 957     6039   8537   9358   1895   -298   2155  A    C  
ATOM   2206  O   ASP C 957      27.898  38.794 142.127  1.00 61.35      A    O  
ANISOU 2206  O   ASP C 957     5988   8213   9109   1839   -373   2210  A    O  
ATOM   2207  CB  ASP C 957      26.820  40.405 144.304  1.00 61.72      A    C  
ANISOU 2207  CB  ASP C 957     5867   7893   9690   2369     96   2051  A    C  
ATOM   2208  CG  ASP C 957      25.440  40.856 143.887  1.00 68.36      A    C  
ANISOU 2208  CG  ASP C 957     6370   8824  10779   2564     70   2388  A    C  
ATOM   2209  OD1 ASP C 957      24.760  40.103 143.158  1.00 70.25      A    O  
ANISOU 2209  OD1 ASP C 957     6410   9360  10922   2441   -138   2607  A    O  
ATOM   2210  OD2 ASP C 957      25.039  41.972 144.285  1.00 69.17      A    O1-
ANISOU 2210  OD2 ASP C 957     6406   8691  11183   2839    256   2439  A    O1-
ATOM   2211  N   PRO C 958      26.248  37.325 142.578  1.00 69.55      A    N  
ANISOU 2211  N   PRO C 958     6692   9664  10070   1764   -443   2276  A    N  
ATOM   2212  CA  PRO C 958      26.297  36.598 141.302  1.00 71.63      A    C  
ANISOU 2212  CA  PRO C 958     6977  10142  10098   1518   -706   2438  A    C  
ATOM   2213  C   PRO C 958      26.135  37.540 140.122  1.00 75.18      A    C  
ANISOU 2213  C   PRO C 958     7368  10555  10641   1582   -851   2754  A    C  
ATOM   2214  O   PRO C 958      26.610  37.254 139.014  1.00 74.71      A    O  
ANISOU 2214  O   PRO C 958     7445  10579  10362   1390  -1028   2848  A    O  
ATOM   2215  CB  PRO C 958      25.097  35.646 141.384  1.00 74.36      A    C  
ANISOU 2215  CB  PRO C 958     7069  10777  10406   1429   -807   2542  A    C  
ATOM   2216  CG  PRO C 958      24.735  35.594 142.825  1.00 74.09      A    C  
ANISOU 2216  CG  PRO C 958     6951  10684  10516   1584   -563   2356  A    C  
ATOM   2217  CD  PRO C 958      25.071  36.939 143.371  1.00 73.80      A    C  
ANISOU 2217  CD  PRO C 958     6974  10346  10720   1856   -357   2299  A    C  
ATOM   2218  N   SER C 959      25.443  38.648 140.381  1.00 76.32      A    N  
ANISOU 2218  N   SER C 959     7316  10573  11111   1859   -760   2923  A    N  
ATOM   2219  CA  SER C 959      25.268  39.735 139.422  1.00 79.29      A    C  
ANISOU 2219  CA  SER C 959     7622  10860  11644   1979   -862   3244  A    C  
ATOM   2220  C   SER C 959      26.579  40.289 138.859  1.00 78.63      A    C  
ANISOU 2220  C   SER C 959     7843  10563  11468   1916   -852   3183  A    C  
ATOM   2221  O   SER C 959      26.636  40.721 137.711  1.00 80.71      A    O  
ANISOU 2221  O   SER C 959     8122  10852  11693   1876  -1015   3453  A    O  
ATOM   2222  CB  SER C 959      24.494  40.877 140.075  1.00 79.85      A    C  
ANISOU 2222  CB  SER C 959     7522  10729  12089   2284   -663   3301  A    C  
ATOM   2223  OG  SER C 959      24.594  42.045 139.284  1.00 84.45      A    O  
ANISOU 2223  OG  SER C 959     8158  11132  12798   2364   -693   3488  A    O  
ATOM   2224  N   ALA C 960      27.628  40.295 139.672  1.00 71.60      A    N  
ANISOU 2224  N   ALA C 960     7189   9471  10546   1903   -664   2848  A    N  
ATOM   2225  CA  ALA C 960      28.871  40.935 139.266  1.00 68.39      A    C  
ANISOU 2225  CA  ALA C 960     7035   8833  10116   1863   -625   2795  A    C  
ATOM   2226  C   ALA C 960      29.940  39.922 138.863  1.00 62.93      A    C  
ANISOU 2226  C   ALA C 960     6575   8246   9087   1581   -689   2625  A    C  
ATOM   2227  O   ALA C 960      31.109  40.269 138.754  1.00 62.16      A    O  
ANISOU 2227  O   ALA C 960     6688   7965   8966   1527   -618   2518  A    O  
ATOM   2228  CB  ALA C 960      29.390  41.827 140.377  1.00 68.95      A    C  
ANISOU 2228  CB  ALA C 960     7209   8568  10420   2041   -380   2568  A    C  
ATOM   2229  N   ASN C 961      29.544  38.674 138.637  1.00 60.11      A    N  
ANISOU 2229  N   ASN C 961     6177   8173   8489   1399   -813   2606  A    N  
ATOM   2230  CA  ASN C 961      30.492  37.686 138.152  1.00 60.65      A    C  
ANISOU 2230  CA  ASN C 961     6468   8330   8246   1144   -859   2466  A    C  
ATOM   2231  C   ASN C 961      30.955  38.085 136.758  1.00 62.81      A    C  
ANISOU 2231  C   ASN C 961     6864   8603   8398   1050   -972   2687  A    C  
ATOM   2232  O   ASN C 961      30.175  38.604 135.954  1.00 67.96      A    O  
ANISOU 2232  O   ASN C 961     7390   9339   9093   1098  -1120   2995  A    O  
ATOM   2233  CB  ASN C 961      29.878  36.284 138.138  1.00 62.54      A    C  
ANISOU 2233  CB  ASN C 961     6648   8851   8261    964   -968   2413  A    C  
ATOM   2234  N   ILE C 962      32.231  37.881 136.472  1.00 56.21      A    N  
ANISOU 2234  N   ILE C 962     6266   7670   7419    923   -897   2551  A    N  
ATOM   2235  CA  ILE C 962      32.692  38.075 135.113  1.00 59.41      A    C  
ANISOU 2235  CA  ILE C 962     6814   8106   7651    804   -982   2748  A    C  
ATOM   2236  C   ILE C 962      33.280  36.771 134.628  1.00 58.27      A    C  
ANISOU 2236  C   ILE C 962     6861   8114   7164    554   -995   2604  A    C  
ATOM   2237  O   ILE C 962      33.644  35.899 135.431  1.00 54.53      A    O  
ANISOU 2237  O   ILE C 962     6427   7645   6646    499   -901   2337  A    O  
ATOM   2238  CB  ILE C 962      33.742  39.206 134.987  1.00 59.91      A    C  
ANISOU 2238  CB  ILE C 962     6997   7885   7880    887   -849   2777  A    C  
ATOM   2239  CG1 ILE C 962      34.984  38.885 135.830  1.00 56.18      A    C  
ANISOU 2239  CG1 ILE C 962     6659   7254   7433    842   -667   2458  A    C  
ATOM   2240  CG2 ILE C 962      33.122  40.574 135.333  1.00 56.28      A    C  
ANISOU 2240  CG2 ILE C 962     6375   7239   7768   1138   -831   2946  A    C  
ATOM   2241  CD1 ILE C 962      36.182  39.771 135.520  1.00 57.92      A    C  
ANISOU 2241  CD1 ILE C 962     7014   7230   7763    846   -553   2489  A    C  
ATOM   2242  N   SER C 963      33.358  36.638 133.311  1.00 58.09      A    N  
ANISOU 2242  N   SER C 963     6968   8209   6895    405  -1103   2786  A    N  
ATOM   2243  CA  SER C 963      33.928  35.450 132.708  1.00 64.79      A    C  
ANISOU 2243  CA  SER C 963     8038   9178   7403    168  -1090   2656  A    C  
ATOM   2244  C   SER C 963      35.214  35.808 131.967  1.00 64.33      A    C  
ANISOU 2244  C   SER C 963     8205   8979   7257    114   -950   2675  A    C  
ATOM   2245  O   SER C 963      35.233  36.724 131.158  1.00 63.09      A    O  
ANISOU 2245  O   SER C 963     8076   8784   7112    147   -997   2924  A    O  
ATOM   2246  CB  SER C 963      32.915  34.798 131.762  1.00 72.76      A    C  
ANISOU 2246  CB  SER C 963     9050  10468   8128     -9  -1328   2821  A    C  
ATOM   2247  OG  SER C 963      33.359  33.520 131.346  1.00 78.20      A    O  
ANISOU 2247  OG  SER C 963     9965  11255   8492   -240  -1296   2640  A    O  
ATOM   2248  N   LEU C 964      36.295  35.098 132.275  1.00 64.34      A    N  
ANISOU 2248  N   LEU C 964     8352   8900   7195     39   -769   2430  A    N  
ATOM   2249  CA  LEU C 964      37.563  35.275 131.572  1.00 62.80      A    C  
ANISOU 2249  CA  LEU C 964     8358   8587   6916    -26   -604   2439  A    C  
ATOM   2250  C   LEU C 964      37.848  34.012 130.770  1.00 66.59      A    C  
ANISOU 2250  C   LEU C 964     9067   9210   7026   -241   -566   2347  A    C  
ATOM   2251  O   LEU C 964      38.282  33.000 131.324  1.00 63.78      A    O  
ANISOU 2251  O   LEU C 964     8759   8842   6633   -293   -456   2105  A    O  
ATOM   2252  CB  LEU C 964      38.704  35.573 132.549  1.00 57.19      A    C  
ANISOU 2252  CB  LEU C 964     7615   7641   6472     71   -404   2256  A    C  
ATOM   2253  CG  LEU C 964      38.600  36.909 133.289  1.00 54.64      A    C  
ANISOU 2253  CG  LEU C 964     7129   7127   6506    263   -408   2322  A    C  
ATOM   2254  CD1 LEU C 964      39.750  37.111 134.276  1.00 50.75      A    C  
ANISOU 2254  CD1 LEU C 964     6622   6418   6241    311   -242   2121  A    C  
ATOM   2255  CD2 LEU C 964      38.536  38.056 132.277  1.00 53.10      A    C  
ANISOU 2255  CD2 LEU C 964     6965   6871   6340    298   -450   2623  A    C  
ATOM   2256  N   ASP C 965      37.580  34.089 129.468  1.00 69.03      A    N  
ANISOU 2256  N   ASP C 965     9528   9644   7055   -365   -658   2546  A    N  
ATOM   2257  CA  ASP C 965      37.618  32.944 128.556  1.00 72.67      A    C  
ANISOU 2257  CA  ASP C 965    10245  10258   7108   -592   -654   2476  A    C  
ATOM   2258  C   ASP C 965      37.053  31.658 129.163  1.00 67.30      A    C  
ANISOU 2258  C   ASP C 965     9543   9687   6342   -684   -713   2252  A    C  
ATOM   2259  O   ASP C 965      37.778  30.682 129.341  1.00 64.85      A    O  
ANISOU 2259  O   ASP C 965     9377   9318   5946   -756   -531   2023  A    O  
ATOM   2260  CB  ASP C 965      39.044  32.682 128.074  1.00 79.03      A    C  
ANISOU 2260  CB  ASP C 965    11283  10931   7812   -647   -364   2377  A    C  
ATOM   2261  CG  ASP C 965      39.086  32.220 126.623  1.00 87.56      A    C  
ANISOU 2261  CG  ASP C 965    12679  12145   8447   -856   -357   2458  A    C  
ATOM   2262  OD1 ASP C 965      38.594  32.969 125.746  1.00 90.81      A    O  
ANISOU 2262  OD1 ASP C 965    13129  12651   8722   -891   -513   2728  A    O  
ATOM   2263  OD2 ASP C 965      39.584  31.101 126.363  1.00 88.94      A    O1-
ANISOU 2263  OD2 ASP C 965    13072  12324   8398   -985   -195   2256  A    O1-
ATOM   2264  N   GLY C 966      35.762  31.662 129.476  1.00 63.88      A    N  
ANISOU 2264  N   GLY C 966     8918   9403   5950   -678   -958   2334  A    N  
ATOM   2265  CA  GLY C 966      35.120  30.484 130.029  1.00 63.35      A    C  
ANISOU 2265  CA  GLY C 966     8813   9447   5812   -780  -1029   2154  A    C  
ATOM   2266  C   GLY C 966      35.416  30.204 131.499  1.00 56.50      A    C  
ANISOU 2266  C   GLY C 966     7785   8450   5234   -637   -891   1934  A    C  
ATOM   2267  O   GLY C 966      34.951  29.200 132.050  1.00 54.61      A    O  
ANISOU 2267  O   GLY C 966     7513   8283   4954   -714   -924   1783  A    O  
ATOM   2268  N   VAL C 967      36.190  31.078 132.140  1.00 52.46      A    N  
ANISOU 2268  N   VAL C 967     7183   7745   5003   -445   -744   1919  A    N  
ATOM   2269  CA  VAL C 967      36.473  30.931 133.565  1.00 48.75      A    C  
ANISOU 2269  CA  VAL C 967     6569   7159   4793   -314   -637   1727  A    C  
ATOM   2270  C   VAL C 967      35.730  31.997 134.375  1.00 50.02      A    C  
ANISOU 2270  C   VAL C 967     6471   7287   5245   -118   -725   1826  A    C  
ATOM   2271  O   VAL C 967      35.938  33.190 134.163  1.00 47.82      A    O  
ANISOU 2271  O   VAL C 967     6151   6899   5120      0   -715   1974  A    O  
ATOM   2272  CB  VAL C 967      37.980  31.024 133.872  1.00 49.72      A    C  
ANISOU 2272  CB  VAL C 967     6785   7077   5030   -259   -400   1597  A    C  
ATOM   2273  CG1 VAL C 967      38.217  30.919 135.387  1.00 45.94      A    C  
ANISOU 2273  CG1 VAL C 967     6158   6498   4800   -138   -332   1416  A    C  
ATOM   2274  CG2 VAL C 967      38.746  29.934 133.130  1.00 49.63      A    C  
ANISOU 2274  CG2 VAL C 967     7022   7074   4763   -422   -261   1492  A    C  
ATOM   2275  N   ASP C 968      34.869  31.561 135.297  1.00 46.48      A    N  
ANISOU 2275  N   ASP C 968     5859   6921   4880    -81   -788   1747  A    N  
ATOM   2276  CA  ASP C 968      34.123  32.491 136.143  1.00 49.17      A    C  
ANISOU 2276  CA  ASP C 968     5961   7223   5497    118   -828   1817  A    C  
ATOM   2277  C   ASP C 968      34.980  33.114 137.248  1.00 44.98      A    C  
ANISOU 2277  C   ASP C 968     5411   6467   5214    276   -658   1664  A    C  
ATOM   2278  O   ASP C 968      35.707  32.420 137.958  1.00 45.18      A    O  
ANISOU 2278  O   ASP C 968     5503   6436   5226    241   -547   1453  A    O  
ATOM   2279  CB  ASP C 968      32.919  31.789 136.777  1.00 50.83      A    C  
ANISOU 2279  CB  ASP C 968     6001   7603   5711     99   -924   1787  A    C  
ATOM   2280  N   VAL C 969      34.889  34.431 137.383  1.00 44.73      A    N  
ANISOU 2280  N   VAL C 969     5289   6299   5407    443   -648   1779  A    N  
ATOM   2281  CA  VAL C 969      35.518  35.139 138.490  1.00 43.84      A    C  
ANISOU 2281  CA  VAL C 969     5155   5968   5534    584   -515   1634  A    C  
ATOM   2282  C   VAL C 969      34.425  35.832 139.293  1.00 44.50      A    C  
ANISOU 2282  C   VAL C 969     5048   6031   5828    770   -530   1672  A    C  
ATOM   2283  O   VAL C 969      33.867  36.832 138.850  1.00 43.96      A    O  
ANISOU 2283  O   VAL C 969     4892   5913   5898    887   -578   1877  A    O  
ATOM   2284  CB  VAL C 969      36.555  36.176 138.018  1.00 45.87      A    C  
ANISOU 2284  CB  VAL C 969     5512   6014   5904    615   -443   1705  A    C  
ATOM   2285  CG1 VAL C 969      37.415  36.650 139.199  1.00 45.49      A    C  
ANISOU 2285  CG1 VAL C 969     5479   5748   6058    689   -319   1505  A    C  
ATOM   2286  CG2 VAL C 969      37.431  35.601 136.912  1.00 46.86      A    C  
ANISOU 2286  CG2 VAL C 969     5808   6186   5811    444   -419   1746  A    C  
ATOM   2287  N   PRO C 970      34.092  35.274 140.469  1.00 46.48      A    N  
ANISOU 2287  N   PRO C 970     5234   6322   6106    803   -476   1488  A    N  
ATOM   2288  CA  PRO C 970      33.028  35.780 141.345  1.00 48.29      A    C  
ANISOU 2288  CA  PRO C 970     5287   6543   6519    982   -444   1496  A    C  
ATOM   2289  C   PRO C 970      33.524  36.924 142.211  1.00 55.09      A    C  
ANISOU 2289  C   PRO C 970     6189   7134   7607   1142   -308   1384  A    C  
ATOM   2290  O   PRO C 970      33.723  36.751 143.418  1.00 57.31      A    O  
ANISOU 2290  O   PRO C 970     6503   7357   7916   1175   -208   1164  A    O  
ATOM   2291  CB  PRO C 970      32.691  34.572 142.206  1.00 46.30      A    C  
ANISOU 2291  CB  PRO C 970     5002   6442   6149    910   -420   1326  A    C  
ATOM   2292  CG  PRO C 970      34.027  33.880 142.362  1.00 42.65      A    C  
ANISOU 2292  CG  PRO C 970     4733   5921   5553    770   -371   1141  A    C  
ATOM   2293  CD  PRO C 970      34.744  34.076 141.030  1.00 41.31      A    C  
ANISOU 2293  CD  PRO C 970     4677   5718   5300    673   -425   1271  A    C  
ATOM   2294  N   LEU C 971      33.740  38.080 141.607  1.00 57.23      A    N  
ANISOU 2294  N   LEU C 971     6479   7236   8028   1226   -309   1532  A    N  
ATOM   2295  CA  LEU C 971      34.336  39.176 142.350  1.00 60.34      A    C  
ANISOU 2295  CA  LEU C 971     6952   7340   8633   1341   -184   1412  A    C  
ATOM   2296  C   LEU C 971      33.289  40.195 142.808  1.00 60.48      A    C  
ANISOU 2296  C   LEU C 971     6841   7240   8899   1580   -109   1489  A    C  
ATOM   2297  O   LEU C 971      33.608  41.345 143.081  1.00 63.16      A    O  
ANISOU 2297  O   LEU C 971     7247   7306   9446   1694    -17   1464  A    O  
ATOM   2298  CB  LEU C 971      35.433  39.843 141.514  1.00 60.12      A    C  
ANISOU 2298  CB  LEU C 971     7055   7145   8645   1273   -195   1499  A    C  
ATOM   2299  CG  LEU C 971      35.202  40.008 140.016  1.00 61.71      A    C  
ANISOU 2299  CG  LEU C 971     7230   7436   8780   1233   -305   1800  A    C  
ATOM   2300  CD1 LEU C 971      34.183  41.087 139.729  1.00 64.68      A    C  
ANISOU 2300  CD1 LEU C 971     7472   7734   9371   1430   -326   2036  A    C  
ATOM   2301  CD2 LEU C 971      36.522  40.311 139.342  1.00 62.89      A    C  
ANISOU 2301  CD2 LEU C 971     7538   7453   8906   1115   -279   1826  A    C  
ATOM   2302  N   GLY C 972      32.040  39.759 142.904  1.00 58.97      A    N  
ANISOU 2302  N   GLY C 972     6462   7244   8702   1654   -137   1583  A    N  
ATOM   2303  CA  GLY C 972      31.008  40.581 143.508  1.00 60.15      A    C  
ANISOU 2303  CA  GLY C 972     6465   7292   9098   1900    -22   1635  A    C  
ATOM   2304  C   GLY C 972      31.222  40.708 145.007  1.00 58.59      A    C  
ANISOU 2304  C   GLY C 972     6369   6947   8948   1972    168   1323  A    C  
ATOM   2305  O   GLY C 972      31.795  39.825 145.647  1.00 52.42      A    O  
ANISOU 2305  O   GLY C 972     5694   6250   7974   1827    173   1103  A    O  
ATOM   2306  N   THR C 973      30.777  41.822 145.573  1.00 61.53      A    N  
ANISOU 2306  N   THR C 973     6722   7084   9570   2196    330   1307  A    N  
ATOM   2307  CA  THR C 973      30.818  42.001 147.016  1.00 61.78      A    C  
ANISOU 2307  CA  THR C 973     6868   6978   9628   2275    528   1011  A    C  
ATOM   2308  C   THR C 973      29.899  40.967 147.674  1.00 60.70      A    C  
ANISOU 2308  C   THR C 973     6584   7108   9371   2284    573    964  A    C  
ATOM   2309  O   THR C 973      28.929  40.506 147.064  1.00 56.53      A    O  
ANISOU 2309  O   THR C 973     5815   6805   8859   2311    491   1198  A    O  
ATOM   2310  CB  THR C 973      30.385  43.423 147.417  1.00 66.22      A    C  
ANISOU 2310  CB  THR C 973     7447   7218  10494   2534    723   1013  A    C  
ATOM   2311  CG2 THR C 973      31.224  44.464 146.693  1.00 66.38      A    C  
ANISOU 2311  CG2 THR C 973     7599   6964  10659   2520    675   1097  A    C  
ATOM   2312  OG1 THR C 973      29.014  43.621 147.059  1.00 71.15      A    O  
ANISOU 2312  OG1 THR C 973     7792   7938  11305   2744    764   1278  A    O  
ATOM   2313  N   GLY C 974      30.199  40.605 148.916  1.00 62.28      A    N  
ANISOU 2313  N   GLY C 974     6928   7288   9448   2246    694    675  A    N  
ATOM   2314  CA  GLY C 974      29.415  39.604 149.631  1.00 62.45      A    C  
ANISOU 2314  CA  GLY C 974     6836   7551   9343   2239    758    621  A    C  
ATOM   2315  C   GLY C 974      27.976  39.970 149.972  1.00 67.83      A    C  
ANISOU 2315  C   GLY C 974     7288   8261  10223   2485    937    740  A    C  
ATOM   2316  O   GLY C 974      27.706  40.930 150.700  1.00 68.60      A    O  
ANISOU 2316  O   GLY C 974     7449   8127  10489   2688   1164    635  A    O  
ATOM   2317  N   ILE C 975      27.043  39.189 149.438  1.00 69.39      A    N  
ANISOU 2317  N   ILE C 975     7215   8740  10409   2459    841    963  A    N  
ATOM   2318  CA  ILE C 975      25.628  39.329 149.761  1.00 72.47      A    C  
ANISOU 2318  CA  ILE C 975     7327   9215  10991   2669    999   1108  A    C  
ATOM   2319  C   ILE C 975      25.123  38.052 150.426  1.00 69.59      A    C  
ANISOU 2319  C   ILE C 975     6872   9125  10445   2556   1030   1042  A    C  
ATOM   2320  O   ILE C 975      25.827  37.038 150.455  1.00 67.14      A    O  
ANISOU 2320  O   ILE C 975     6698   8943   9870   2314    895    923  A    O  
ATOM   2321  CB  ILE C 975      24.775  39.621 148.506  1.00 73.75      A    C  
ANISOU 2321  CB  ILE C 975     7183   9483  11357   2748    844   1497  A    C  
ATOM   2322  CG1 ILE C 975      24.762  38.408 147.572  1.00 69.96      A    C  
ANISOU 2322  CG1 ILE C 975     6603   9318  10661   2478    550   1646  A    C  
ATOM   2323  CG2 ILE C 975      25.299  40.848 147.777  1.00 73.94      A    C  
ANISOU 2323  CG2 ILE C 975     7302   9238  11554   2849    802   1597  A    C  
ATOM   2324  CD1 ILE C 975      23.784  38.535 146.418  1.00 72.52      A    C  
ANISOU 2324  CD1 ILE C 975     6608   9807  11139   2517    366   2037  A    C  
ATOM   2325  N   SER C 976      23.906  38.106 150.957  1.00 69.43      A    N  
ANISOU 2325  N   SER C 976     6614   9183  10585   2736   1222   1132  A    N  
ATOM   2326  CA  SER C 976      23.278  36.945 151.585  1.00 70.12      A    C  
ANISOU 2326  CA  SER C 976     6576   9530  10538   2642   1275   1109  A    C  
ATOM   2327  C   SER C 976      22.874  35.904 150.534  1.00 68.60      A    C  
ANISOU 2327  C   SER C 976     6158   9636  10271   2429    985   1354  A    C  
ATOM   2328  O   SER C 976      22.173  36.223 149.581  1.00 70.17      A    O  
ANISOU 2328  O   SER C 976     6095   9910  10656   2488    855   1649  A    O  
ATOM   2329  CB  SER C 976      22.055  37.379 152.403  1.00 74.07      A    C  
ANISOU 2329  CB  SER C 976     6860  10021  11263   2910   1593   1163  A    C  
ATOM   2330  OG  SER C 976      21.723  36.415 153.388  1.00 73.79      A    O  
ANISOU 2330  OG  SER C 976     6820  10158  11058   2830   1731   1040  A    O  
ATOM   2331  N   SER C 977      23.318  34.661 150.709  1.00 64.76      A    N  
ANISOU 2331  N   SER C 977     5784   9312   9512   2174    878   1237  A    N  
ATOM   2332  CA  SER C 977      23.036  33.603 149.737  1.00 63.50      A    C  
ANISOU 2332  CA  SER C 977     5475   9406   9246   1936    607   1422  A    C  
ATOM   2333  C   SER C 977      21.596  33.095 149.777  1.00 70.65      A    C  
ANISOU 2333  C   SER C 977     6006  10553  10284   1952    628   1646  A    C  
ATOM   2334  O   SER C 977      21.139  32.438 148.836  1.00 72.33      A    O  
ANISOU 2334  O   SER C 977     6043  10971  10467   1772    382   1853  A    O  
ATOM   2335  CB  SER C 977      23.963  32.418 149.963  1.00 57.35      A    C  
ANISOU 2335  CB  SER C 977     4942   8689   8158   1672    517   1222  A    C  
ATOM   2336  OG  SER C 977      23.424  31.573 150.964  1.00 54.32      A    O  
ANISOU 2336  OG  SER C 977     4495   8439   7704   1634    661   1150  A    O  
ATOM   2337  N   GLY C 978      20.898  33.367 150.877  1.00 71.26      A    N  
ANISOU 2337  N   GLY C 978     5971  10608  10496   2150    924   1600  A    N  
ATOM   2338  CA  GLY C 978      19.549  32.869 151.063  1.00 74.35      A    C  
ANISOU 2338  CA  GLY C 978     5990  11226  11032   2171    988   1808  A    C  
ATOM   2339  C   GLY C 978      19.452  31.360 151.244  1.00 73.83      A    C  
ANISOU 2339  C   GLY C 978     5918  11388  10746   1881    889   1774  A    C  
ATOM   2340  O   GLY C 978      18.362  30.789 151.140  1.00 73.36      A    O  
ANISOU 2340  O   GLY C 978     5530  11548  10795   1821    860   1985  A    O  
ATOM   2341  N   VAL C 979      20.578  30.701 151.516  1.00 67.83      A    N  
ANISOU 2341  N   VAL C 979     5505  10570   9695   1698    836   1527  A    N  
ATOM   2342  CA  VAL C 979      20.540  29.251 151.666  1.00 69.36      A    C  
ANISOU 2342  CA  VAL C 979     5717  10946   9690   1426    747   1499  A    C  
ATOM   2343  C   VAL C 979      20.029  28.861 153.051  1.00 75.59      A    C  
ANISOU 2343  C   VAL C 979     6467  11788  10466   1494   1043   1410  A    C  
ATOM   2344  O   VAL C 979      20.299  29.545 154.035  1.00 77.89      A    O  
ANISOU 2344  O   VAL C 979     6912  11927  10757   1693   1303   1235  A    O  
ATOM   2345  CB  VAL C 979      21.918  28.598 151.439  1.00 62.46      A    C  
ANISOU 2345  CB  VAL C 979     5208   9992   8531   1212    592   1296  A    C  
ATOM   2346  CG1 VAL C 979      21.855  27.139 151.821  1.00 58.26      A    C  
ANISOU 2346  CG1 VAL C 979     4710   9605   7822    973    567   1253  A    C  
ATOM   2347  CG2 VAL C 979      22.352  28.746 149.989  1.00 60.15      A    C  
ANISOU 2347  CG2 VAL C 979     4951   9687   8215   1096    304   1402  A    C  
ATOM   2348  N   ASP C 981      19.362  26.018 154.951  1.00 64.43      A    N  
ANISOU 2348  N   ASP C 981     5048  10701   8729   1117   1269   1326  A    N  
ATOM   2349  CA  ASP C 981      19.840  25.731 156.303  1.00 65.12      A    C  
ANISOU 2349  CA  ASP C 981     5388  10730   8623   1149   1507   1117  A    C  
ATOM   2350  C   ASP C 981      21.290  25.244 156.329  1.00 63.86      A    C  
ANISOU 2350  C   ASP C 981     5618  10452   8194    997   1358    909  A    C  
ATOM   2351  O   ASP C 981      21.538  24.041 156.224  1.00 62.60      A    O  
ANISOU 2351  O   ASP C 981     5526  10366   7895    762   1234    918  A    O  
ATOM   2352  CB  ASP C 981      18.955  24.680 156.958  1.00 64.40      A    C  
ANISOU 2352  CB  ASP C 981     5120  10827   8520   1031   1639   1225  A    C  
ATOM   2353  N   THR C 982      22.237  26.170 156.483  1.00 65.38      A    N  
ANISOU 2353  N   THR C 982     6057  10453   8333   1132   1377    731  A    N  
ATOM   2354  CA  THR C 982      23.662  25.838 156.451  1.00 62.63      A    C  
ANISOU 2354  CA  THR C 982     6040   9986   7771   1006   1228    558  A    C  
ATOM   2355  C   THR C 982      24.416  26.210 157.714  1.00 62.91      A    C  
ANISOU 2355  C   THR C 982     6362   9902   7638   1097   1397    333  A    C  
ATOM   2356  O   THR C 982      24.045  27.139 158.424  1.00 66.46      A    O  
ANISOU 2356  O   THR C 982     6821  10287   8144   1299   1622    261  A    O  
ATOM   2357  CB  THR C 982      24.393  26.533 155.273  1.00 81.28      A    C  
ANISOU 2357  CB  THR C 982     8464  12219  10200   1014   1015    556  A    C  
ATOM   2358  CG2 THR C 982      24.167  25.789 154.007  1.00 81.31      A    C  
ANISOU 2358  CG2 THR C 982     8334  12331  10230    820    773    720  A    C  
ATOM   2359  OG1 THR C 982      23.903  27.873 155.117  1.00 82.00      A    O  
ANISOU 2359  OG1 THR C 982     8434  12226  10497   1249   1114    599  A    O  
ATOM   2360  N   SER C 983      25.509  25.503 157.961  1.00 58.49      A    N  
ANISOU 2360  N   SER C 983     6045   9304   6872    944   1283    225  A    N  
ATOM   2361  CA  SER C 983      26.399  25.864 159.040  1.00 58.85      A    C  
ANISOU 2361  CA  SER C 983     6383   9242   6736    989   1367     21  A    C  
ATOM   2362  C   SER C 983      27.642  26.580 158.562  1.00 58.96      A    C  
ANISOU 2362  C   SER C 983     6578   9073   6751    994   1199    -93  A    C  
ATOM   2363  O   SER C 983      28.459  26.979 159.352  1.00 61.47      A    O  
ANISOU 2363  O   SER C 983     7138   9286   6932   1007   1215   -261  A    O  
ATOM   2364  CB  SER C 983      26.803  24.648 159.811  1.00 60.42      A    C  
ANISOU 2364  CB  SER C 983     6714   9526   6715    824   1354      5  A    C  
ATOM   2365  OG  SER C 983      27.286  23.696 158.929  1.00 63.50      A    O  
ANISOU 2365  OG  SER C 983     7087   9934   7107    641   1132     90  A    O  
ATOM   2366  N   LEU C 984      27.777  26.747 157.260  1.00 56.92      A    N  
ANISOU 2366  N   LEU C 984     6205   8784   6639    966   1029      8  A    N  
ATOM   2367  CA  LEU C 984      28.929  27.436 156.703  1.00 52.16      A    C  
ANISOU 2367  CA  LEU C 984     5751   8013   6056    960    878    -70  A    C  
ATOM   2368  C   LEU C 984      28.692  28.930 156.528  1.00 52.81      A    C  
ANISOU 2368  C   LEU C 984     5813   7950   6303   1157    963   -108  A    C  
ATOM   2369  O   LEU C 984      27.661  29.351 156.063  1.00 51.48      A    O  
ANISOU 2369  O   LEU C 984     5426   7822   6313   1269   1023     26  A    O  
ATOM   2370  CB  LEU C 984      29.329  26.843 155.354  1.00 49.37      A    C  
ANISOU 2370  CB  LEU C 984     5327   7686   5744    819    666     54  A    C  
ATOM   2371  CG  LEU C 984      29.595  25.387 155.020  1.00 50.90      A    C  
ANISOU 2371  CG  LEU C 984     5567   7960   5812    613    553     93  A    C  
ATOM   2372  CD1 LEU C 984      30.823  25.303 154.144  1.00 52.40      A    C  
ANISOU 2372  CD1 LEU C 984     5859   8043   6007    530    385     88  A    C  
ATOM   2373  CD2 LEU C 984      29.797  24.534 156.225  1.00 51.03      A    C  
ANISOU 2373  CD2 LEU C 984     5732   7997   5661    562    623      0  A    C  
ATOM   2374  N   LEU C 985      29.691  29.708 156.880  1.00 49.91      A    N  
ANISOU 2374  N   LEU C 985     5668   7405   5890   1192    960   -277  A    N  
ATOM   2375  CA  LEU C 985      29.671  31.128 156.706  1.00 53.05      A    C  
ANISOU 2375  CA  LEU C 985     6091   7613   6451   1358   1027   -328  A    C  
ATOM   2376  C   LEU C 985      29.967  31.511 155.272  1.00 51.22      A    C  
ANISOU 2376  C   LEU C 985     5763   7316   6381   1344    853   -192  A    C  
ATOM   2377  O   LEU C 985      29.356  32.412 154.729  1.00 52.03      A    O  
ANISOU 2377  O   LEU C 985     5734   7350   6684   1493    901    -94  A    O  
ATOM   2378  CB  LEU C 985      30.715  31.751 157.601  1.00 55.60      A    C  
ANISOU 2378  CB  LEU C 985     6704   7762   6659   1351   1051   -560  A    C  
ATOM   2379  CG  LEU C 985      30.209  32.821 158.528  1.00 64.93      A    C  
ANISOU 2379  CG  LEU C 985     7992   8807   7871   1530   1291   -711  A    C  
ATOM   2380  CD1 LEU C 985      29.246  32.192 159.507  1.00 65.85      A    C  
ANISOU 2380  CD1 LEU C 985     8026   9088   7908   1601   1516   -695  A    C  
ATOM   2381  CD2 LEU C 985      31.346  33.495 159.252  1.00 68.29      A    C  
ANISOU 2381  CD2 LEU C 985     8734   9072   8142   1455   1253   -947  A    C  
ATOM   2382  N   TYR C 986      30.926  30.822 154.672  1.00 46.40      A    N  
ANISOU 2382  N   TYR C 986     5224   6722   5683   1171    663   -176  A    N  
ATOM   2383  CA  TYR C 986      31.347  31.094 153.305  1.00 46.85      A    C  
ANISOU 2383  CA  TYR C 986     5234   6723   5843   1130    507    -58  A    C  
ATOM   2384  C   TYR C 986      31.290  29.845 152.457  1.00 45.87      A    C  
ANISOU 2384  C   TYR C 986     5027   6764   5639    965    373     71  A    C  
ATOM   2385  O   TYR C 986      31.380  28.733 152.982  1.00 42.81      A    O  
ANISOU 2385  O   TYR C 986     4675   6482   5109    853    374     33  A    O  
ATOM   2386  CB  TYR C 986      32.772  31.651 153.271  1.00 47.52      A    C  
ANISOU 2386  CB  TYR C 986     5515   6621   5919   1081    428   -173  A    C  
ATOM   2387  CG  TYR C 986      32.918  32.940 154.034  1.00 54.72      A    C  
ANISOU 2387  CG  TYR C 986     6547   7336   6909   1212    541   -318  A    C  
ATOM   2388  CD1 TYR C 986      32.253  34.080 153.620  1.00 57.50      A    C  
ANISOU 2388  CD1 TYR C 986     6818   7570   7461   1382    623   -253  A    C  
ATOM   2389  CD2 TYR C 986      33.719  33.016 155.166  1.00 57.22      A    C  
ANISOU 2389  CD2 TYR C 986     7069   7574   7097   1159    561   -517  A    C  
ATOM   2390  CE1 TYR C 986      32.370  35.264 154.314  1.00 65.63      A    C  
ANISOU 2390  CE1 TYR C 986     7983   8383   8571   1503    749   -401  A    C  
ATOM   2391  CE2 TYR C 986      33.850  34.200 155.865  1.00 63.09      A    C  
ANISOU 2391  CE2 TYR C 986     7959   8120   7891   1253    662   -675  A    C  
ATOM   2392  CZ  TYR C 986      33.170  35.323 155.433  1.00 67.48      A    C  
ANISOU 2392  CZ  TYR C 986     8448   8535   8657   1429    770   -627  A    C  
ATOM   2393  OH  TYR C 986      33.285  36.510 156.116  1.00 72.11      A    O  
ANISOU 2393  OH  TYR C 986     9205   8889   9305   1525    893   -797  A    O  
ATOM   2394  N   ASN C 987      31.158  30.028 151.145  1.00 40.08      A    N  
ANISOU 2394  N   ASN C 987     4202   6040   4986    940    260    221  A    N  
ATOM   2395  CA  ASN C 987      31.265  28.899 150.234  1.00 38.58      A    C  
ANISOU 2395  CA  ASN C 987     3993   5971   4693    760    128    313  A    C  
ATOM   2396  C   ASN C 987      32.633  28.235 150.339  1.00 40.11      A    C  
ANISOU 2396  C   ASN C 987     4378   6096   4766    633     84    203  A    C  
ATOM   2397  O   ASN C 987      33.641  28.891 150.609  1.00 40.84      A    O  
ANISOU 2397  O   ASN C 987     4593   6036   4888    670     91    108  A    O  
ATOM   2398  CB  ASN C 987      31.023  29.334 148.784  1.00 33.78      A    C  
ANISOU 2398  CB  ASN C 987     3305   5373   4158    746      8    484  A    C  
ATOM   2399  CG  ASN C 987      29.608  29.845 148.559  1.00 39.17      A    C  
ANISOU 2399  CG  ASN C 987     3751   6152   4978    859     18    649  A    C  
ATOM   2400  ND2 ASN C 987      29.482  30.859 147.707  1.00 40.96      A    N  
ANISOU 2400  ND2 ASN C 987     3920   6310   5332    949    -38    780  A    N  
ATOM   2401  OD1 ASN C 987      28.644  29.344 149.149  1.00 38.01      A    O  
ANISOU 2401  OD1 ASN C 987     3464   6141   4837    868     82    677  A    O  
ATOM   2402  N   GLU C 988      32.667  26.928 150.135  1.00 38.30      A    N  
ANISOU 2402  N   GLU C 988     4166   5970   4418    482     40    223  A    N  
ATOM   2403  CA  GLU C 988      33.933  26.235 149.976  1.00 34.76      A    C  
ANISOU 2403  CA  GLU C 988     3869   5450   3887    372      2    163  A    C  
ATOM   2404  C   GLU C 988      33.825  25.351 148.770  1.00 33.83      A    C  
ANISOU 2404  C   GLU C 988     3757   5396   3700    227    -72    252  A    C  
ATOM   2405  O   GLU C 988      32.736  24.904 148.425  1.00 37.49      A    O  
ANISOU 2405  O   GLU C 988     4115   5991   4137    168   -105    337  A    O  
ATOM   2406  CB  GLU C 988      34.279  25.419 151.220  1.00 40.80      A    C  
ANISOU 2406  CB  GLU C 988     4705   6235   4563    339     58     67  A    C  
ATOM   2407  CG  GLU C 988      34.495  26.275 152.441  1.00 49.26      A    C  
ANISOU 2407  CG  GLU C 988     5822   7241   5653    454    123    -44  A    C  
ATOM   2408  CD  GLU C 988      34.984  25.471 153.625  1.00 53.87      A    C  
ANISOU 2408  CD  GLU C 988     6499   7851   6118    403    148   -119  A    C  
ATOM   2409  OE1 GLU C 988      35.663  24.445 153.403  1.00 53.94      A    O  
ANISOU 2409  OE1 GLU C 988     6557   7860   6077    297    101    -91  A    O  
ATOM   2410  OE2 GLU C 988      34.654  25.849 154.771  1.00 53.08      A    O1-
ANISOU 2410  OE2 GLU C 988     6429   7770   5970    472    225   -198  A    O1-
ATOM   2411  N   TYR C 989      34.958  25.101 148.128  1.00 32.78      A    N  
ANISOU 2411  N   TYR C 989     3750   5167   3539    161    -94    233  A    N  
ATOM   2412  CA  TYR C 989      34.994  24.288 146.922  1.00 31.70      A    C  
ANISOU 2412  CA  TYR C 989     3674   5060   3310     18   -139    290  A    C  
ATOM   2413  C   TYR C 989      36.092  23.263 147.062  1.00 33.31      A    C  
ANISOU 2413  C   TYR C 989     4013   5182   3463    -58    -84    221  A    C  
ATOM   2414  O   TYR C 989      37.229  23.624 147.383  1.00 33.90      A    O  
ANISOU 2414  O   TYR C 989     4139   5140   3602      2    -50    175  A    O  
ATOM   2415  CB  TYR C 989      35.253  25.159 145.690  1.00 31.17      A    C  
ANISOU 2415  CB  TYR C 989     3630   4943   3268     31   -189    369  A    C  
ATOM   2416  CG  TYR C 989      34.226  26.241 145.480  1.00 36.56      A    C  
ANISOU 2416  CG  TYR C 989     4169   5687   4034    126   -246    471  A    C  
ATOM   2417  CD1 TYR C 989      34.323  27.461 146.144  1.00 35.88      A    C  
ANISOU 2417  CD1 TYR C 989     4029   5511   4092    293   -205    449  A    C  
ATOM   2418  CD2 TYR C 989      33.175  26.050 144.597  1.00 36.25      A    C  
ANISOU 2418  CD2 TYR C 989     4052   5786   3937     45   -346    599  A    C  
ATOM   2419  CE1 TYR C 989      33.383  28.460 145.930  1.00 38.08      A    C  
ANISOU 2419  CE1 TYR C 989     4171   5818   4478    404   -234    558  A    C  
ATOM   2420  CE2 TYR C 989      32.234  27.031 144.380  1.00 42.53      A    C  
ANISOU 2420  CE2 TYR C 989     4685   6639   4836    147   -404    730  A    C  
ATOM   2421  CZ  TYR C 989      32.341  28.236 145.045  1.00 42.33      A    C  
ANISOU 2421  CZ  TYR C 989     4601   6505   4977    341   -334    712  A    C  
ATOM   2422  OH  TYR C 989      31.397  29.206 144.808  1.00 43.54      A    O  
ANISOU 2422  OH  TYR C 989     4588   6692   5263    463   -371    857  A    O  
ATOM   2423  N   ILE C 990      35.777  21.997 146.815  1.00 33.70      A    N  
ANISOU 2423  N   ILE C 990     4113   5279   3413   -191    -77    222  A    N  
ATOM   2424  CA  ILE C 990      36.766  20.946 147.018  1.00 35.04      A    C  
ANISOU 2424  CA  ILE C 990     4404   5351   3560   -242     -2    169  A    C  
ATOM   2425  C   ILE C 990      36.810  20.006 145.818  1.00 36.87      A    C  
ANISOU 2425  C   ILE C 990     4768   5554   3688   -391     17    175  A    C  
ATOM   2426  O   ILE C 990      35.774  19.562 145.338  1.00 34.38      A    O  
ANISOU 2426  O   ILE C 990     4446   5337   3282   -512    -42    203  A    O  
ATOM   2427  CB  ILE C 990      36.486  20.121 148.300  1.00 35.00      A    C  
ANISOU 2427  CB  ILE C 990     4369   5386   3544   -248     31    142  A    C  
ATOM   2428  CG1 ILE C 990      36.294  21.032 149.523  1.00 33.00      A    C  
ANISOU 2428  CG1 ILE C 990     4018   5175   3346   -117     23    119  A    C  
ATOM   2429  CG2 ILE C 990      37.630  19.148 148.572  1.00 29.31      A    C  
ANISOU 2429  CG2 ILE C 990     3756   4543   2837   -268    104    118  A    C  
ATOM   2430  CD1 ILE C 990      34.853  21.380 149.810  1.00 33.02      A    C  
ANISOU 2430  CD1 ILE C 990     3889   5319   3338    -99      6    153  A    C  
ATOM   2431  N   VAL C 991      38.013  19.709 145.335  1.00 33.67      A    N  
ANISOU 2431  N   VAL C 991     4485   5010   3297   -390    105    149  A    N  
ATOM   2432  CA  VAL C 991      38.159  18.712 144.284  1.00 35.19      A    C  
ANISOU 2432  CA  VAL C 991     4849   5142   3380   -527    170    126  A    C  
ATOM   2433  C   VAL C 991      39.032  17.604 144.815  1.00 35.68      A    C  
ANISOU 2433  C   VAL C 991     4990   5071   3497   -518    298     86  A    C  
ATOM   2434  O   VAL C 991      39.798  17.825 145.758  1.00 32.67      A    O  
ANISOU 2434  O   VAL C 991     4529   4643   3243   -398    321     97  A    O  
ATOM   2435  CB  VAL C 991      38.777  19.301 143.000  1.00 32.56      A    C  
ANISOU 2435  CB  VAL C 991     4616   4750   3004   -532    207    144  A    C  
ATOM   2436  CG1 VAL C 991      37.764  20.261 142.313  1.00 30.50      A    C  
ANISOU 2436  CG1 VAL C 991     4292   4629   2669   -565     62    216  A    C  
ATOM   2437  CG2 VAL C 991      40.132  19.969 143.301  1.00 30.84      A    C  
ANISOU 2437  CG2 VAL C 991     4359   4415   2945   -387    290    156  A    C  
ATOM   2438  N   TYR C 992      38.948  16.432 144.196  1.00 35.20      A    N  
ANISOU 2438  N   TYR C 992     5091   4940   3344   -648    375     45  A    N  
ATOM   2439  CA  TYR C 992      39.558  15.235 144.763  1.00 35.13      A    C  
ANISOU 2439  CA  TYR C 992     5151   4795   3401   -641    499     23  A    C  
ATOM   2440  C   TYR C 992      40.545  14.560 143.797  1.00 35.55      A    C  
ANISOU 2440  C   TYR C 992     5399   4659   3450   -660    685    -19  A    C  
ATOM   2441  O   TYR C 992      41.037  13.467 144.057  1.00 36.49      A    O  
ANISOU 2441  O   TYR C 992     5602   4631   3630   -657    817    -34  A    O  
ATOM   2442  CB  TYR C 992      38.443  14.259 145.210  1.00 34.58      A    C  
ANISOU 2442  CB  TYR C 992     5096   4784   3261   -776    453     11  A    C  
ATOM   2443  CG  TYR C 992      37.546  14.901 146.256  1.00 35.24      A    C  
ANISOU 2443  CG  TYR C 992     4977   5045   3366   -732    320     61  A    C  
ATOM   2444  CD1 TYR C 992      36.482  15.721 145.881  1.00 37.17      A    C  
ANISOU 2444  CD1 TYR C 992     5124   5455   3545   -775    190     85  A    C  
ATOM   2445  CD2 TYR C 992      37.798  14.735 147.615  1.00 33.07      A    C  
ANISOU 2445  CD2 TYR C 992     4611   4773   3180   -635    334     94  A    C  
ATOM   2446  CE1 TYR C 992      35.681  16.341 146.811  1.00 35.55      A    C  
ANISOU 2446  CE1 TYR C 992     4734   5394   3379   -710    111    129  A    C  
ATOM   2447  CE2 TYR C 992      36.995  15.355 148.576  1.00 36.02      A    C  
ANISOU 2447  CE2 TYR C 992     4828   5304   3554   -587    248    125  A    C  
ATOM   2448  CZ  TYR C 992      35.934  16.156 148.169  1.00 36.49      A    C  
ANISOU 2448  CZ  TYR C 992     4790   5508   3567   -617    154    136  A    C  
ATOM   2449  OH  TYR C 992      35.127  16.770 149.095  1.00 32.48      A    O  
ANISOU 2449  OH  TYR C 992     4127   5138   3075   -551    109    166  A    O  
ATOM   2450  N   ASP C 993      40.840  15.227 142.689  1.00 34.27      A    N  
ANISOU 2450  N   ASP C 993     5311   4491   3220   -669    714    -29  A    N  
ATOM   2451  CA  ASP C 993      41.900  14.789 141.795  1.00 35.94      A    C  
ANISOU 2451  CA  ASP C 993     5695   4525   3438   -654    928    -63  A    C  
ATOM   2452  C   ASP C 993      42.826  15.992 141.618  1.00 34.02      A    C  
ANISOU 2452  C   ASP C 993     5339   4280   3305   -516    949      4  A    C  
ATOM   2453  O   ASP C 993      42.343  17.099 141.368  1.00 33.25      A    O  
ANISOU 2453  O   ASP C 993     5166   4312   3153   -521    809     39  A    O  
ATOM   2454  CB  ASP C 993      41.351  14.300 140.447  1.00 36.69      A    C  
ANISOU 2454  CB  ASP C 993     6047   4601   3291   -842    971   -147  A    C  
ATOM   2455  CG  ASP C 993      42.430  13.676 139.574  1.00 36.61      A    C  
ANISOU 2455  CG  ASP C 993     6256   4380   3274   -824   1249   -205  A    C  
ATOM   2456  OD1 ASP C 993      43.365  14.403 139.174  1.00 35.28      A    O  
ANISOU 2456  OD1 ASP C 993     6052   4173   3180   -709   1352   -156  A    O  
ATOM   2457  OD2 ASP C 993      42.353  12.454 139.295  1.00 39.96      A    O1-
ANISOU 2457  OD2 ASP C 993     6891   4663   3630   -924   1382   -298  A    O1-
ATOM   2458  N   ILE C 994      44.138  15.801 141.777  1.00 33.60      A    N  
ANISOU 2458  N   ILE C 994     5256   4079   3432   -392   1120     40  A    N  
ATOM   2459  CA  ILE C 994      45.045  16.966 141.788  1.00 34.32      A    C  
ANISOU 2459  CA  ILE C 994     5199   4172   3669   -272   1120    120  A    C  
ATOM   2460  C   ILE C 994      45.160  17.668 140.449  1.00 37.62      A    C  
ANISOU 2460  C   ILE C 994     5730   4594   3969   -315   1187    123  A    C  
ATOM   2461  O   ILE C 994      45.494  18.860 140.395  1.00 38.60      A    O  
ANISOU 2461  O   ILE C 994     5735   4761   4170   -256   1125    193  A    O  
ATOM   2462  CB  ILE C 994      46.466  16.602 142.255  1.00 37.91      A    C  
ANISOU 2462  CB  ILE C 994     5555   4478   4372   -137   1278    188  A    C  
ATOM   2463  CG1 ILE C 994      47.050  15.474 141.405  1.00 43.67      A    C  
ANISOU 2463  CG1 ILE C 994     6477   5023   5092   -142   1562    151  A    C  
ATOM   2464  CG2 ILE C 994      46.437  16.276 143.764  1.00 40.15      A    C  
ANISOU 2464  CG2 ILE C 994     5677   4795   4782    -79   1147    230  A    C  
ATOM   2465  CD1 ILE C 994      48.539  15.265 141.617  1.00 48.65      A    C  
ANISOU 2465  CD1 ILE C 994     6983   5502   5999     12   1752    252  A    C  
ATOM   2466  N   ALA C 995      44.849  16.957 139.371  1.00 39.96      A    N  
ANISOU 2466  N   ALA C 995     6275   4846   4063   -433   1307     49  A    N  
ATOM   2467  CA  ALA C 995      44.959  17.539 138.032  1.00 39.35      A    C  
ANISOU 2467  CA  ALA C 995     6346   4779   3826   -491   1382     57  A    C  
ATOM   2468  C   ALA C 995      43.828  18.528 137.722  1.00 37.27      A    C  
ANISOU 2468  C   ALA C 995     6051   4707   3403   -576   1132     95  A    C  
ATOM   2469  O   ALA C 995      43.876  19.205 136.709  1.00 37.95      A    O  
ANISOU 2469  O   ALA C 995     6229   4826   3364   -615   1150    140  A    O  
ATOM   2470  CB  ALA C 995      44.997  16.427 136.981  1.00 42.91      A    C  
ANISOU 2470  CB  ALA C 995     7114   5114   4076   -607   1596    -50  A    C  
ATOM   2471  N   GLN C 996      42.814  18.605 138.587  1.00 37.29      A    N  
ANISOU 2471  N   GLN C 996     5919   4835   3416   -597    912     94  A    N  
ATOM   2472  CA  GLN C 996      41.716  19.571 138.405  1.00 37.66      A    C  
ANISOU 2472  CA  GLN C 996     5885   5057   3365   -645    680    156  A    C  
ATOM   2473  C   GLN C 996      42.070  21.006 138.805  1.00 37.64      A    C  
ANISOU 2473  C   GLN C 996     5685   5079   3539   -504    606    254  A    C  
ATOM   2474  O   GLN C 996      41.224  21.906 138.761  1.00 34.53      A    O  
ANISOU 2474  O   GLN C 996     5199   4804   3116   -504    433    321  A    O  
ATOM   2475  CB  GLN C 996      40.476  19.135 139.195  1.00 37.74      A    C  
ANISOU 2475  CB  GLN C 996     5805   5188   3346   -710    504    130  A    C  
ATOM   2476  CG  GLN C 996      39.630  18.040 138.498  1.00 37.53      A    C  
ANISOU 2476  CG  GLN C 996     5977   5197   3085   -921    480     59  A    C  
ATOM   2477  CD  GLN C 996      38.594  17.418 139.452  1.00 40.33      A    C  
ANISOU 2477  CD  GLN C 996     6219   5638   3466   -979    351     38  A    C  
ATOM   2478  NE2 GLN C 996      37.405  18.034 139.531  1.00 36.32      A    N  
ANISOU 2478  NE2 GLN C 996     5565   5315   2920  -1023    140    113  A    N  
ATOM   2479  OE1 GLN C 996      38.871  16.408 140.113  1.00 36.82      A    O  
ANISOU 2479  OE1 GLN C 996     5807   5092   3090   -978    452    -26  A    O  
ATOM   2480  N   VAL C 997      43.325  21.220 139.173  1.00 35.37      A    N  
ANISOU 2480  N   VAL C 997     5327   4666   3446   -387    739    271  A    N  
ATOM   2481  CA  VAL C 997      43.757  22.521 139.655  1.00 35.52      A    C  
ANISOU 2481  CA  VAL C 997     5169   4678   3651   -274    670    347  A    C  
ATOM   2482  C   VAL C 997      44.899  23.082 138.818  1.00 36.21      A    C  
ANISOU 2482  C   VAL C 997     5294   4661   3804   -241    828    419  A    C  
ATOM   2483  O   VAL C 997      45.853  22.361 138.500  1.00 38.09      A    O  
ANISOU 2483  O   VAL C 997     5605   4789   4080   -231   1035    403  A    O  
ATOM   2484  CB  VAL C 997      44.230  22.451 141.112  1.00 35.23      A    C  
ANISOU 2484  CB  VAL C 997     4961   4602   3822   -177    634    322  A    C  
ATOM   2485  CG1 VAL C 997      44.802  23.815 141.541  1.00 36.95      A    C  
ANISOU 2485  CG1 VAL C 997     5028   4784   4226    -89    569    383  A    C  
ATOM   2486  CG2 VAL C 997      43.086  21.995 142.040  1.00 30.30      A    C  
ANISOU 2486  CG2 VAL C 997     4288   4088   3137   -201    493    265  A    C  
ATOM   2487  N   ASN C 998      44.799  24.362 138.468  1.00 35.29      A    N  
ANISOU 2487  N   ASN C 998     5122   4569   3718   -217    748    509  A    N  
ATOM   2488  CA  ASN C 998      45.876  25.063 137.753  1.00 41.64      A    C  
ANISOU 2488  CA  ASN C 998     5935   5275   4613   -187    890    601  A    C  
ATOM   2489  C   ASN C 998      46.177  26.391 138.453  1.00 40.33      A    C  
ANISOU 2489  C   ASN C 998     5578   5069   4676   -105    778    666  A    C  
ATOM   2490  O   ASN C 998      45.344  27.299 138.450  1.00 40.79      A    O  
ANISOU 2490  O   ASN C 998     5604   5186   4709    -96    624    708  A    O  
ATOM   2491  CB  ASN C 998      45.483  25.295 136.290  1.00 42.15      A    C  
ANISOU 2491  CB  ASN C 998     6190   5389   4436   -276    932    667  A    C  
ATOM   2492  CG  ASN C 998      46.653  25.728 135.417  1.00 44.73      A    C  
ANISOU 2492  CG  ASN C 998     6570   5611   4815   -261   1147    759  A    C  
ATOM   2493  ND2 ASN C 998      46.334  26.404 134.333  1.00 43.95      A    N  
ANISOU 2493  ND2 ASN C 998     6589   5560   4550   -318   1135    862  A    N  
ATOM   2494  OD1 ASN C 998      47.821  25.466 135.713  1.00 45.33      A    O  
ANISOU 2494  OD1 ASN C 998     6569   5570   5083   -200   1320    758  A    O  
ATOM   2495  N   LEU C 999      47.339  26.486 139.096  1.00 38.42      A    N  
ANISOU 2495  N   LEU C 999     5208   4723   4668    -49    848    676  A    N  
ATOM   2496  CA  LEU C 999      47.672  27.689 139.846  1.00 39.79      A    C  
ANISOU 2496  CA  LEU C 999     5221   4842   5057     -1    730    713  A    C  
ATOM   2497  C   LEU C 999      47.937  28.828 138.879  1.00 40.03      A    C  
ANISOU 2497  C   LEU C 999     5276   4815   5118    -13    775    838  A    C  
ATOM   2498  O   LEU C 999      48.654  28.637 137.904  1.00 41.67      A    O  
ANISOU 2498  O   LEU C 999     5554   4977   5301    -39    963    912  A    O  
ATOM   2499  CB  LEU C 999      48.888  27.463 140.732  1.00 38.28      A    C  
ANISOU 2499  CB  LEU C 999     4880   4565   5099     30    767    709  A    C  
ATOM   2500  CG  LEU C 999      48.729  26.363 141.764  1.00 39.00      A    C  
ANISOU 2500  CG  LEU C 999     4939   4704   5176     47    718    616  A    C  
ATOM   2501  CD1 LEU C 999      49.929  26.358 142.696  1.00 40.10      A    C  
ANISOU 2501  CD1 LEU C 999     4904   4772   5560     72    700    649  A    C  
ATOM   2502  CD2 LEU C 999      47.436  26.563 142.532  1.00 36.14      A    C  
ANISOU 2502  CD2 LEU C 999     4589   4443   4700     50    528    528  A    C  
ATOM   2503  N   LYS C1000      47.360  29.999 139.133  1.00 35.91      A    N  
ANISOU 2503  N   LYS C1000     4706   4285   4653     12    625    868  A    N  
ATOM   2504  CA  LYS C1000      47.516  31.125 138.201  1.00 39.02      A    C  
ANISOU 2504  CA  LYS C1000     5131   4614   5079      3    658   1009  A    C  
ATOM   2505  C   LYS C1000      48.296  32.301 138.796  1.00 40.57      A    C  
ANISOU 2505  C   LYS C1000     5195   4662   5558     22    617   1049  A    C  
ATOM   2506  O   LYS C1000      49.171  32.885 138.135  1.00 40.58      A    O  
ANISOU 2506  O   LYS C1000     5182   4564   5672     -6    730   1170  A    O  
ATOM   2507  CB  LYS C1000      46.146  31.624 137.724  1.00 41.30      A    C  
ANISOU 2507  CB  LYS C1000     5492   4993   5206     13    529   1059  A    C  
ATOM   2508  CG  LYS C1000      45.172  30.552 137.274  1.00 44.89      A    C  
ANISOU 2508  CG  LYS C1000     6063   5609   5384    -34    503   1014  A    C  
ATOM   2509  CD  LYS C1000      45.706  29.767 136.095  1.00 49.59      A    C  
ANISOU 2509  CD  LYS C1000     6824   6222   5796   -117    685   1048  A    C  
ATOM   2510  CE  LYS C1000      45.759  30.609 134.843  1.00 53.70      A    C  
ANISOU 2510  CE  LYS C1000     7443   6732   6228   -150    729   1220  A    C  
ATOM   2511  NZ  LYS C1000      46.149  29.806 133.652  1.00 55.16      A    N1+
ANISOU 2511  NZ  LYS C1000     7837   6949   6173   -242    918   1236  A    N1+
ATOM   2512  N   TYR C1001      47.981  32.648 140.041  1.00 36.97      A    N  
ANISOU 2512  N   TYR C1001     4654   4185   5209     58    464    944  A    N  
ATOM   2513  CA  TYR C1001      48.579  33.814 140.680  1.00 39.29      A    C  
ANISOU 2513  CA  TYR C1001     4854   4327   5746     53    396    951  A    C  
ATOM   2514  C   TYR C1001      48.929  33.537 142.117  1.00 41.26      A    C  
ANISOU 2514  C   TYR C1001     5015   4567   6096     45    292    811  A    C  
ATOM   2515  O   TYR C1001      48.263  32.758 142.780  1.00 39.06      A    O  
ANISOU 2515  O   TYR C1001     4754   4399   5689     75    233    702  A    O  
ATOM   2516  CB  TYR C1001      47.629  35.018 140.632  1.00 39.99      A    C  
ANISOU 2516  CB  TYR C1001     4982   4358   5855    106    299    979  A    C  
ATOM   2517  CG  TYR C1001      47.257  35.429 139.238  1.00 45.00      A    C  
ANISOU 2517  CG  TYR C1001     5700   5004   6394    110    366   1152  A    C  
ATOM   2518  CD1 TYR C1001      48.092  36.250 138.491  1.00 49.38      A    C  
ANISOU 2518  CD1 TYR C1001     6254   5427   7081     69    457   1302  A    C  
ATOM   2519  CD2 TYR C1001      46.071  34.995 138.662  1.00 47.41      A    C  
ANISOU 2519  CD2 TYR C1001     6084   5459   6471    141    329   1181  A    C  
ATOM   2520  CE1 TYR C1001      47.753  36.635 137.201  1.00 51.05      A    C  
ANISOU 2520  CE1 TYR C1001     6561   5658   7179     68    516   1480  A    C  
ATOM   2521  CE2 TYR C1001      45.725  35.370 137.370  1.00 49.07      A    C  
ANISOU 2521  CE2 TYR C1001     6381   5699   6565    128    363   1358  A    C  
ATOM   2522  CZ  TYR C1001      46.571  36.188 136.646  1.00 50.32      A    C  
ANISOU 2522  CZ  TYR C1001     6556   5726   6836     96    460   1508  A    C  
ATOM   2523  OH  TYR C1001      46.241  36.563 135.365  1.00 55.09      A    O  
ANISOU 2523  OH  TYR C1001     7263   6367   7301     78    492   1701  A    O  
ATOM   2524  N   LEU C1002      49.975  34.202 142.588  1.00 42.62      A    N  
ANISOU 2524  N   LEU C1002     5093   4610   6493    -11    261    827  A    N  
ATOM   2525  CA  LEU C1002      50.342  34.204 143.991  1.00 40.11      A    C  
ANISOU 2525  CA  LEU C1002     4703   4269   6267    -46    119    705  A    C  
ATOM   2526  C   LEU C1002      50.345  35.661 144.403  1.00 40.25      A    C  
ANISOU 2526  C   LEU C1002     4736   4122   6435    -77     21    673  A    C  
ATOM   2527  O   LEU C1002      50.988  36.486 143.745  1.00 35.84      A    O  
ANISOU 2527  O   LEU C1002     4147   3431   6039   -126     74    790  A    O  
ATOM   2528  CB  LEU C1002      51.718  33.559 144.218  1.00 41.80      A    C  
ANISOU 2528  CB  LEU C1002     4776   4481   6626   -112    152    763  A    C  
ATOM   2529  CG  LEU C1002      52.171  33.180 145.637  1.00 48.61      A    C  
ANISOU 2529  CG  LEU C1002     5554   5375   7539   -159     -8    669  A    C  
ATOM   2530  CD1 LEU C1002      53.505  32.448 145.570  1.00 46.14      A    C  
ANISOU 2530  CD1 LEU C1002     5070   5071   7389   -201     53    790  A    C  
ATOM   2531  CD2 LEU C1002      52.317  34.388 146.551  1.00 58.40      A    C  
ANISOU 2531  CD2 LEU C1002     6799   6496   8893   -239   -185    582  A    C  
ATOM   2532  N   LEU C1003      49.620  35.969 145.476  1.00 36.35      A    N  
ANISOU 2532  N   LEU C1003     4302   3623   5886    -49   -102    516  A    N  
ATOM   2533  CA  LEU C1003      49.566  37.314 146.006  1.00 38.87      A    C  
ANISOU 2533  CA  LEU C1003     4672   3760   6338    -76   -184    445  A    C  
ATOM   2534  C   LEU C1003      50.281  37.402 147.343  1.00 41.17      A    C  
ANISOU 2534  C   LEU C1003     4940   4009   6695   -186   -333    311  A    C  
ATOM   2535  O   LEU C1003      50.103  36.545 148.219  1.00 39.94      A    O  
ANISOU 2535  O   LEU C1003     4786   3989   6401   -182   -400    211  A    O  
ATOM   2536  CB  LEU C1003      48.117  37.779 146.181  1.00 42.51      A    C  
ANISOU 2536  CB  LEU C1003     5244   4216   6690     50   -184    362  A    C  
ATOM   2537  CG  LEU C1003      47.302  38.262 144.972  1.00 43.82      A    C  
ANISOU 2537  CG  LEU C1003     5445   4361   6843    149    -92    506  A    C  
ATOM   2538  CD1 LEU C1003      46.989  37.112 144.011  1.00 43.83      A    C  
ANISOU 2538  CD1 LEU C1003     5423   4565   6665    177    -15    615  A    C  
ATOM   2539  CD2 LEU C1003      46.014  38.937 145.458  1.00 40.58      A    C  
ANISOU 2539  CD2 LEU C1003     5109   3902   6408    274   -110    419  A    C  
ATOM   2540  N   LYS C1004      51.081  38.449 147.494  1.00 40.21      A    N  
ANISOU 2540  N   LYS C1004     4804   3698   6776   -300   -395    318  A    N  
ATOM   2541  CA  LYS C1004      51.620  38.831 148.784  1.00 41.32      A    C  
ANISOU 2541  CA  LYS C1004     4967   3766   6966   -431   -570    170  A    C  
ATOM   2542  C   LYS C1004      50.705  39.890 149.387  1.00 43.89      A    C  
ANISOU 2542  C   LYS C1004     5481   3937   7256   -388   -594     -6  A    C  
ATOM   2543  O   LYS C1004      50.535  40.982 148.814  1.00 45.82      A    O  
ANISOU 2543  O   LYS C1004     5782   3984   7642   -368   -532     36  A    O  
ATOM   2544  CB  LYS C1004      53.055  39.350 148.637  0.88 44.57      A    C  
ANISOU 2544  CB  LYS C1004     5248   4051   7633   -611   -636    277  A    C  
ATOM   2545  CG  LYS C1004      53.734  39.791 149.920  0.92 50.40      A    C  
ANISOU 2545  CG  LYS C1004     6005   4715   8429   -795   -856    140  A    C  
ATOM   2546  CD  LYS C1004      55.178  40.257 149.625  1.00 55.24      A    C  
ANISOU 2546  CD  LYS C1004     6440   5217   9330   -987   -921    290  A    C  
ATOM   2547  CE  LYS C1004      55.869  40.812 150.860  1.00 60.78      A    C  
ANISOU 2547  CE  LYS C1004     7169   5833  10093  -1212  -1177    158  A    C  
ATOM   2548  NZ  LYS C1004      57.144  41.505 150.505  0.81 65.89      A    N1+
ANISOU 2548  NZ  LYS C1004     7647   6334  11053  -1415  -1241    306  A    N1+
ATOM   2549  N   LEU C1005      50.108  39.570 150.529  1.00 40.63      A    N  
ANISOU 2549  N   LEU C1005     5172   3605   6660   -363   -665   -192  A    N  
ATOM   2550  CA  LEU C1005      49.153  40.479 151.163  1.00 48.12      A    C  
ANISOU 2550  CA  LEU C1005     6312   4412   7558   -294   -643   -376  A    C  
ATOM   2551  C   LEU C1005      49.661  41.043 152.479  1.00 51.33      A    C  
ANISOU 2551  C   LEU C1005     6851   4703   7950   -458   -799   -583  A    C  
ATOM   2552  O   LEU C1005      50.336  40.346 153.250  1.00 52.69      A    O  
ANISOU 2552  O   LEU C1005     6980   5008   8030   -585   -946   -619  A    O  
ATOM   2553  CB  LEU C1005      47.825  39.773 151.427  1.00 50.04      A    C  
ANISOU 2553  CB  LEU C1005     6606   4829   7579   -117   -555   -442  A    C  
ATOM   2554  CG  LEU C1005      47.116  39.104 150.256  1.00 53.30      A    C  
ANISOU 2554  CG  LEU C1005     6916   5388   7949     30   -428   -266  A    C  
ATOM   2555  CD1 LEU C1005      46.092  38.141 150.813  1.00 56.16      A    C  
ANISOU 2555  CD1 LEU C1005     7296   5957   8084    133   -396   -342  A    C  
ATOM   2556  CD2 LEU C1005      46.460  40.130 149.357  1.00 52.24      A    C  
ANISOU 2556  CD2 LEU C1005     6812   5094   7944    143   -322   -178  A    C  
ATOM   2557  N   LYS C1006      49.304  42.297 152.735  1.00 51.26      A    N  
ANISOU 2557  N   LYS C1006     7014   4439   8022   -454   -765   -715  A    N  
ATOM   2558  CA  LYS C1006      49.526  42.931 154.025  1.00 57.35      A    C  
ANISOU 2558  CA  LYS C1006     7986   5073   8731   -598   -885   -963  A    C  
ATOM   2559  C   LYS C1006      48.254  42.936 154.883  1.00 58.94      A    C  
ANISOU 2559  C   LYS C1006     8386   5297   8712   -445   -779  -1174  A    C  
ATOM   2560  O   LYS C1006      47.229  43.494 154.497  1.00 56.07      A    O  
ANISOU 2560  O   LYS C1006     8086   4819   8400   -251   -597  -1183  A    O  
ATOM   2561  CB  LYS C1006      50.029  44.363 153.823  1.00 63.24      A    C  
ANISOU 2561  CB  LYS C1006     8828   5477   9721   -716   -901  -1000  A    C  
ATOM   2562  CG  LYS C1006      50.064  45.217 155.083  1.00 69.59      A    C  
ANISOU 2562  CG  LYS C1006     9909   6076  10455   -855   -987  -1295  A    C  
ATOM   2563  CD  LYS C1006      50.977  44.618 156.143  1.00 73.37      A    C  
ANISOU 2563  CD  LYS C1006    10391   6711  10775  -1098  -1239  -1387  A    C  
ATOM   2564  CE  LYS C1006      51.193  45.592 157.307  1.00 77.00      A    C  
ANISOU 2564  CE  LYS C1006    11152   6938  11166  -1300  -1357  -1681  A    C  
ATOM   2565  N   PHE C1007      48.328  42.316 156.054  1.00 64.18      A    N  
ANISOU 2565  N   PHE C1007     9137   6112   9136   -530   -887  -1324  A    N  
ATOM   2566  CA  PHE C1007      47.213  42.331 156.993  1.00 67.20      A    C  
ANISOU 2566  CA  PHE C1007     9724   6516   9293   -408   -774  -1535  A    C  
ATOM   2567  C   PHE C1007      47.328  43.516 157.947  1.00 75.22      A    C  
ANISOU 2567  C   PHE C1007    11036   7257  10286   -528   -801  -1808  A    C  
ATOM   2568  O   PHE C1007      48.225  43.556 158.796  1.00 78.18      A    O  
ANISOU 2568  O   PHE C1007    11512   7629  10564   -774  -1013  -1925  A    O  
ATOM   2569  CB  PHE C1007      47.155  41.029 157.782  1.00 65.46      A    C  
ANISOU 2569  CB  PHE C1007     9474   6602   8795   -433   -854  -1550  A    C  
ATOM   2570  CG  PHE C1007      46.689  39.856 156.984  1.00 63.73      A    C  
ANISOU 2570  CG  PHE C1007     9029   6627   8557   -279   -770  -1338  A    C  
ATOM   2571  CD1 PHE C1007      47.530  39.245 156.063  1.00 61.54      A    C  
ANISOU 2571  CD1 PHE C1007     8521   6442   8418   -334   -847  -1111  A    C  
ATOM   2572  CD2 PHE C1007      45.416  39.344 157.165  1.00 65.95      A    C  
ANISOU 2572  CD2 PHE C1007     9334   7043   8683    -88   -604  -1368  A    C  
ATOM   2573  CE1 PHE C1007      47.109  38.152 155.331  1.00 58.29      A    C  
ANISOU 2573  CE1 PHE C1007     7942   6235   7971   -210   -763   -940  A    C  
ATOM   2574  CE2 PHE C1007      44.991  38.243 156.434  1.00 66.42      A    C  
ANISOU 2574  CE2 PHE C1007     9200   7319   8719     21   -545  -1181  A    C  
ATOM   2575  CZ  PHE C1007      45.842  37.646 155.518  1.00 61.08      A    C  
ANISOU 2575  CZ  PHE C1007     8330   6716   8162    -44   -626   -979  A    C  
ATOM   2576  N   ASN C1008      46.469  44.504 157.814  1.00 80.28      A    N  
ANISOU 2576  N   ASN C1008    11819   7663  11021   -358   -589  -1904  A    N  
ATOM   2577  CA  ASN C1008      46.590  45.673 158.651  1.00 87.23      A    C  
ANISOU 2577  CA  ASN C1008    13011   8220  11913   -445   -560  -2175  A    C  
ATOM   2578  C   ASN C1008      45.567  45.648 159.754  1.00 92.31      A    C  
ANISOU 2578  C   ASN C1008    13889   8870  12316   -291   -367  -2412  A    C  
ATOM   2579  O   ASN C1008      44.383  45.853 159.519  1.00 91.51      A    O  
ANISOU 2579  O   ASN C1008    13749   8749  12273    -12   -117  -2368  A    O  
ATOM   2580  CB  ASN C1008      46.457  46.923 157.817  1.00 89.52      A    C  
ANISOU 2580  CB  ASN C1008    13309   8169  12534   -364   -436  -2108  A    C  
ATOM   2581  CG  ASN C1008      47.747  47.296 157.142  1.00 92.64      A    C  
ANISOU 2581  CG  ASN C1008    13605   8439  13155   -609   -634  -1985  A    C  
ATOM   2582  ND2 ASN C1008      47.685  47.548 155.850  1.00 89.62      A    N  
ANISOU 2582  ND2 ASN C1008    13014   8012  13027   -507   -564  -1720  A    N  
ATOM   2583  OD1 ASN C1008      48.788  47.369 157.779  1.00 96.98      A    O  
ANISOU 2583  OD1 ASN C1008    14255   8947  13648   -895   -851  -2111  A    O  
ATOM   2584  N   PHE C1009      46.034  45.375 160.967  1.00 98.89      A    N  
ANISOU 2584  N   PHE C1009    14959   9739  12877   -486   -491  -2648  A    N  
ATOM   2585  CA  PHE C1009      45.145  45.182 162.100  1.00105.56      A    C  
ANISOU 2585  CA  PHE C1009    16078  10583  13448   -387   -311  -2905  A    C  
ATOM   2586  C   PHE C1009      44.835  46.451 162.889  1.00107.50      A    C  
ANISOU 2586  C   PHE C1009    16632  10398  13813   -361   -139  -3150  A    C  
ATOM   2587  O   PHE C1009      43.721  46.966 162.840  1.00110.45      A    O  
ANISOU 2587  O   PHE C1009    17162  10529  14276   -608   -304  -3265  A    O  
ATOM   2588  CB  PHE C1009      45.700  44.104 163.022  1.00111.25      A    C  
ANISOU 2588  CB  PHE C1009    16954  11520  13796   -627   -526  -3049  A    C  
ATOM   2589  CG  PHE C1009      44.737  42.996 163.274  1.00113.09      A    C  
ANISOU 2589  CG  PHE C1009    17222  12027  13722   -467   -369  -3088  A    C  
ATOM   2590  CD1 PHE C1009      43.401  43.275 163.510  1.00116.64      A    C  
ANISOU 2590  CD1 PHE C1009    18008  12515  13796   -577   -363  -3357  A    C  
ATOM   2591  CD2 PHE C1009      45.152  41.685 163.257  1.00109.43      A    C  
ANISOU 2591  CD2 PHE C1009    16448  11809  13323   -246   -259  -2836  A    C  
ATOM   2592  CE1 PHE C1009      42.489  42.274 163.740  1.00115.50      A    C  
ANISOU 2592  CE1 PHE C1009    17879  12637  13369   -438   -209  -3363  A    C  
ATOM   2593  CE2 PHE C1009      44.243  40.667 163.484  1.00109.32      A    C  
ANISOU 2593  CE2 PHE C1009    16444  12044  13050   -119   -121  -2849  A    C  
ATOM   2594  CZ  PHE C1009      42.911  40.965 163.728  1.00112.23      A    C  
ANISOU 2594  CZ  PHE C1009    17132  12444  13067   -209    -89  -3101  A    C  
TER   
HETATM 2595  C1  GOL C1101      47.731  23.305 151.145  1.00 52.40      E    C  
HETATM 2596  O1  GOL C1101      47.846  24.598 151.694  1.00 52.05      E    O  
HETATM 2597  C2  GOL C1101      48.326  22.372 152.158  1.00 55.26      E    C  
HETATM 2598  O2  GOL C1101      49.696  22.362 151.841  1.00 63.84      E    O  
HETATM 2599  C3  GOL C1101      48.061  22.983 153.529  1.00 60.26      E    C  
HETATM 2600  O3  GOL C1101      48.953  22.509 154.517  1.00 62.27      E    O  
HETATM 2601  C1  GOL C1102      55.099  17.400 138.293  1.00 80.30      F    C  
HETATM 2602  O1  GOL C1102      55.381  18.245 139.393  1.00 75.89      F    O  
HETATM 2603  C2  GOL C1102      53.625  17.523 137.923  1.00 83.13      F    C  
HETATM 2604  O2  GOL C1102      53.412  17.187 136.570  1.00 86.59      F    O  
HETATM 2605  C3  GOL C1102      53.216  18.967 138.160  1.00 80.67      F    C  
HETATM 2606  O3  GOL C1102      52.252  19.363 137.209  1.00 79.77      F    O  
HETATM 2607  C   ACT C1103      41.415  27.803 151.738  1.00 61.75      G    C  
HETATM 2608  O   ACT C1103      41.760  28.888 151.225  1.00 57.58      G    O  
HETATM 2609  CH3 ACT C1103      42.442  26.786 152.152  1.00 60.93      G    C  
HETATM 2610  OXT ACT C1103      40.179  27.632 151.896  1.00 62.50      G    O  
HETATM 2611  O   HOH C1201      49.104  12.108 178.965  1.00 52.05      L    O  
HETATM 2612  O   HOH C1202      27.354  15.521 156.956  1.00 57.36      L    O  
HETATM 2613  O   HOH C1203      34.014  17.315 167.537  1.00 42.57      L    O  
HETATM 2614  O   HOH C1204      23.097  18.583 150.478  1.00 48.89      L    O  
HETATM 2615  O   HOH C1205      28.070  12.886 156.126  1.00 58.31      L    O  
HETATM 2616  O   HOH C1206      35.124  11.803 168.714  1.00 46.50      L    O  
HETATM 2617  O   HOH C1207      40.093  20.437 166.651  1.00 42.31      L    O  
HETATM 2618  O   HOH C1208      31.705  38.540 131.673  1.00 53.85      L    O  
HETATM 2619  O   HOH C1209      18.996  20.617 153.003  1.00 56.80      L    O  
HETATM 2620  O   HOH C1210      23.114  18.109 146.647  1.00 68.52      L    O  
HETATM 2621  O   HOH C1211      30.019  40.740 133.644  1.00 57.37      L    O  
HETATM 2622  O   HOH C1212      35.239  15.467 168.761  1.00 46.65      L    O  
HETATM 2623  O   HOH C1213      38.778  11.571 151.300  1.00 43.55      L    O  
HETATM 2624  O   HOH C1214      46.504  20.490 136.733  1.00 38.23      L    O  
HETATM 2625  O   HOH C1215      48.472  22.753 141.849  1.00 32.11      L    O  
HETATM 2626  O   HOH C1216      40.536   7.552 156.759  0.47 22.99      L    O  
HETATM 2627  O   HOH C1217      43.190   6.594 156.371  0.53 27.24      L    O  
HETATM 2628  O   HOH C1218      37.358  15.818 142.208  1.00 36.04      L    O  
HETATM 2629  O   HOH C1219      43.522  22.154 150.456  1.00 29.18      L    O  
HETATM 2630  O   HOH C1220      24.319  18.432 144.695  1.00 45.76      L    O  
HETATM 2631  O   HOH C1221      46.913  20.326 142.157  1.00 31.12      L    O  
HETATM 2632  O   HOH C1222      46.062  24.078 130.435  0.86 44.81      L    O  
HETATM 2633  O   HOH C1223      43.531  16.664 151.634  1.00 32.98      L    O  
HETATM 2634  O   HOH C1224      56.770  24.499 151.822  1.00 52.26      L    O  
HETATM 2635  O   HOH C1225      48.347  26.261 156.261  0.90 42.63      L    O  
HETATM 2636  O   HOH C1226      34.416  31.491 150.101  1.00 36.79      L    O  
HETATM 2637  O   HOH C1227      39.249  20.687 157.235  1.00 43.49      L    O  
HETATM 2638  O   HOH C1228      37.574  10.600 146.131  0.73 37.76      L    O  
HETATM 2639  O   HOH C1229      31.341  32.749 150.041  1.00 44.63      L    O  
HETATM 2640  O   HOH C1230      49.221  20.911 149.277  1.00 47.37      L    O  
HETATM 2641  O   HOH C1231      31.844  11.010 139.898  1.00 50.17      L    O  
HETATM 2642  O   HOH C1232      57.547  27.631 152.098  1.00 54.99      L    O  
HETATM 2643  O   HOH C1233      50.775  26.755 137.595  1.00 43.12      L    O  
HETATM 2644  O   HOH C1234      43.993  10.132 150.489  1.00 50.79      L    O  
HETATM 2645  O   HOH C1235      49.971  18.872 142.282  1.00 37.63      L    O  
HETATM 2646  O   HOH C1236      52.400  20.378 148.218  1.00 57.63      L    O  
HETATM 2647  O   HOH C1237      53.717  24.824 157.604  1.00 46.56      L    O  
HETATM 2648  O   HOH C1238      61.920  28.112 139.318  1.00 47.67      L    O  
HETATM 2649  O   HOH C1239      35.886  10.999 144.206  1.00 45.23      L    O  
HETATM 2650  O   HOH C1240      50.567  33.074 154.259  1.00 41.76      L    O  
HETATM 2651  O   HOH C1241      50.926  16.006 139.311  1.00 59.87      L    O  
HETATM 2652  O   HOH C1242      56.867  23.435 139.824  1.00 51.29      L    O  
HETATM 2653  O   HOH C1243      48.124  17.916 171.316  1.00 60.84      L    O  
HETATM 2654  O   HOH C1244      52.505  17.399 133.001  1.00 51.46      L    O  
HETATM 2655  O   HOH C1245      36.155   8.143 164.103  1.00 45.62      L    O  
HETATM 2656  O   HOH C1246      57.532  15.780 152.994  1.00 55.30      L    O  
HETATM 2657  O   HOH C1247      46.203   3.112 159.991  1.00 51.63      L    O  
HETATM 2658  O   HOH C1248      65.810  22.981 164.396  1.00 48.66      L    O  
HETATM 2659  O   HOH C1249      43.327   2.377 160.542  1.00 55.64      L    O  
HETATM 2660  O   HOH C1250      52.319   4.257 162.260  1.00 47.63      L    O  
HETATM 2661  O   HOH C1251      40.540  11.609 148.600  1.00 45.76      L    O  
HETATM 2662  O   HOH C1252      41.164  11.586 146.078  1.00 50.26      L    O  
HETATM 2663  O   HOH C1253      40.055  22.484 155.672  1.00 62.86      L    O  
HETATM 2664  O   HOH C1254      26.033  29.678 149.041  1.00 51.03      L    O  
HETATM 2665  O   HOH C1255      34.141   8.561 154.670  1.00 50.03      L    O  
HETATM 2666  O   HOH C1256      32.996  27.573 155.099  1.00 62.19      L    O  
HETATM 2667  O   HOH C1257      54.305  16.281 149.477  1.00 47.27      L    O  
HETATM 2668  O   HOH C1258      49.692   2.611 162.296  1.00 48.01      L    O  
HETATM 2669  O   HOH C1259      49.717  21.140 170.111  1.00 65.70      L    O  
HETATM 2670  O   HOH C1260      30.582   9.925 156.174  1.00 64.68      L    O  
HETATM 2671  O   HOH C1261      52.340  43.183 141.414  1.00 61.80      L    O  
HETATM 2672  O   HOH C1262      46.168  15.288 132.660  1.00 50.15      L    O  
HETATM 2673  O   HOH C1263      41.586   7.099 152.475  1.00 52.84      L    O  
HETATM 2674  O   HOH C1264      50.245  18.928 153.025  1.00 51.14      L    O  
HETATM 2675  O   HOH C1265      67.905  21.768 161.730  1.00 57.73      L    O  
HETATM 2676  O   HOH C1266      30.813  12.294 157.678  1.00 45.64      L    O  
HETATM 2677  O   HOH C1267      59.667  29.253 155.050  1.00 50.13      L    O  
HETATM 2678  O   HOH C1268      56.176  14.637 150.761  1.00 47.22      L    O  
HETATM 2679  O   HOH C1269      51.838  42.428 134.076  1.00 63.81      L    O  
HETATM 2680  O   HOH C1270      22.374  31.619 146.782  1.00 67.79      L    O  
HETATM 2681  O   HOH C1271      61.568  38.720 152.288  1.00 55.15      L    O  
HETATM 2682  O   HOH C1272      70.065  20.192 158.672  1.00 72.81      L    O  
HETATM 2683  O   HOH C1273      57.974  15.323 148.696  1.00 64.89      L    O  
HETATM 2684  O   HOH C1274      56.201   3.781 170.237  1.00 54.22      L    O  
HETATM 2685  O   HOH C1275      45.019   0.116 166.281  1.00 54.80      L    O  
HETATM 2686  O   HOH C1276      58.853  39.522 136.189  1.00 54.80      L    O  
HETATM 2687  O   HOH C1277      48.430  45.541 142.831  1.00 60.64      L    O  
HETATM 2688  O   HOH C1278      62.955  44.952 140.802  1.00 69.50      L    O  
HETATM 2689  O   HOH C1279      44.778  18.945 152.864  1.00 59.09      L    O  
HETATM 2690  O   HOH C1280      45.504  34.863 159.335  1.00 59.07      L    O  
HETATM 2691  O   HOH C1281      25.395  37.716 154.511  1.00 65.93      L    O  
HETATM 2692  O   HOH C1282      45.394  21.347 156.228  1.00 59.19      L    O  
HETATM 2693  O   HOH C1283      49.170  28.997 134.995  1.00 54.50      L    O  
HETATM 2694  O   HOH C1284      61.618  30.922 134.729  1.00 68.68      L    O  
HETATM 2695  O   HOH C1285      53.824   3.581 164.555  1.00 65.47      L    O  
HETATM 2696  O   HOH C1286      51.116   6.437 150.925  1.00 64.45      L    O  
HETATM 2697  O   HOH C1287      68.358  20.770 143.761  1.00 65.52      L    O  
HETATM 2698  O   HOH C1288      50.286  26.845 134.252  1.00 62.37      L    O  
HETATM 2699  O   HOH C1289      41.483  45.384 149.442  1.00 64.01      L    O  
HETATM 2700  O   HOH C1290      51.701  14.030 141.415  1.00 69.30      L    O  
CONECT 2595 2596 2597
CONECT 2596 2595
CONECT 2597 2595 2598 2599
CONECT 2598 2597
CONECT 2599 2597 2600
CONECT 2600 2599
CONECT 2601 2602 2603
CONECT 2602 2601
CONECT 2603 2601 2604 2605
CONECT 2604 2603
CONECT 2605 2603 2606
CONECT 2606 2605
CONECT 2607 2608 2609 2610
CONECT 2608 2607
CONECT 2609 2607
CONECT 2610 2607
END


A second structure was input as follows:


HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       16-SEP-15   XXXX              
TITLE     CRYSTAL STRUCTURE OF CONSTITUTIVELY ACTIVE PARP-1                     
KEYWDS    ADP-RIBOSYL TRANSFERASE, PARP-1, TRANSFERASE-TRANSFERASE INHIBITOR    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.LANGELIER,J.M.PASCAL                                              
JRNL        AUTH   J.M.DAWICKI-MCKENNA,M.F.LANGELIER,J.E.DENIZIO,A.A.RICCIO,    
JRNL        AUTH 2 C.D.CAO,K.R.KARCH,M.MCCAULEY,J.D.STEFFEN,B.E.BLACK,          
JRNL        AUTH 3 J.M.PASCAL                                                   
JRNL        TITL   PARP-1 ACTIVATION REQUIRES LOCAL UNFOLDING OF AN             
JRNL        TITL 2 AUTOINHIBITORY DOMAIN.                                       
JRNL        REF    MOL.CELL                      V.  60   755 2015              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   26626480                                                     
JRNL        DOI    10.1016/J.MOLCEL.2015.10.013                                 
SEQRES   1 A  271  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  271  LEU VAL PRO ARG GLY SER HIS MET THR LYS SER LYS LEU          
SEQRES   3 A  271  PRO LYS PRO VAL GLN ASP LEU ILE LYS MET ILE PHE GLY          
SEQRES   4 A  271  SER GLY SER GLY SER GLY GLY ASP PRO ILE ASP VAL ASN          
SEQRES   5 A  271  TYR GLU LYS LEU LYS THR ASP ILE LYS VAL VAL ASP ARG          
SEQRES   6 A  271  ASP SER GLU GLU ALA GLU ILE ILE ARG LYS TYR VAL LYS          
SEQRES   7 A  271  ASN THR HIS ALA THR THR HIS ASN ALA TYR ASP LEU GLU          
SEQRES   8 A  271  VAL ILE ASP ILE PHE LYS ILE GLU ARG GLU GLY GLU CYS          
SEQRES   9 A  271  GLN ARG TYR LYS PRO PHE LYS GLN LEU HIS ASN ARG ARG          
SEQRES  10 A  271  LEU LEU TRP HIS GLY SER ARG THR THR ASN PHE ALA GLY          
SEQRES  11 A  271  ILE LEU SER GLN GLY LEU ARG ILE ALA PRO PRO GLU ALA          
SEQRES  12 A  271  PRO VAL THR GLY TYR MET PHE GLY LYS GLY ILE TYR PHE          
SEQRES  13 A  271  ALA ASP MET VAL SER LYS SER ALA ASN TYR CYS HIS THR          
SEQRES  14 A  271  SER GLN GLY ASP PRO ILE GLY LEU ILE LEU LEU GLY GLU          
SEQRES  15 A  271  VAL ALA LEU GLY ASN MET TYR GLU LEU LYS HIS ALA SER          
SEQRES  16 A  271  HIS ILE SER LYS LEU PRO LYS GLY LYS HIS SER VAL LYS          
SEQRES  17 A  271  GLY LEU GLY LYS THR THR PRO ASP PRO SER ALA ASN ILE          
SEQRES  18 A  271  SER LEU ASP GLY VAL ASP VAL PRO LEU GLY THR GLY ILE          
SEQRES  19 A  271  SER SER GLY VAL ASN ASP THR SER LEU LEU TYR ASN GLU          
SEQRES  20 A  271  TYR ILE VAL TYR ASP ILE ALA GLN VAL ASN LEU LYS TYR          
SEQRES  21 A  271  LEU LEU LYS LEU LYS PHE ASN PHE LYS THR SER                  
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     09L 4-(3-{[4-(CYCLOPROPYLCARBONYL)PIPERAZIN-1-YL]CARBONYL}-          
HETNAM   2 09L  4-FLUOROBENZYL)PHTHALAZIN-1(2H)-ONE                             
HETNAM     SO4 SULFATE ION                                                      
HETSYN     1PE PEG400                                                           
HETSYN     09L OLAPARIB                                                         
FORMUL   2  1PE    C10 H22 O6                                                   
FORMUL   3  09L    C24 H23 F N4 O3                                              
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   6  HOH   *27(H2 O)                                                     
HELIX    1 AA1 PRO A  768  GLY A  780  1                                  13    
HELIX    2 AA2 PRO A  789  LYS A  796  1                                   8    
HELIX    3 AA3 SER A  808  THR A  821  1                                  14    
HELIX    4 AA4 GLY A  843  LYS A  849  1                                   7    
HELIX    5 AA5 PRO A  850  LYS A  852  5                                   3    
HELIX    6 AA6 ARG A  865  THR A  867  5                                   3    
HELIX    7 AA7 ASN A  868  GLY A  876  1                                   9    
HELIX    8 AA8 MET A  900  ASN A  906  1                                   7    
HELIX    9 AA9 TYR A  907  HIS A  909  5                                   3    
HELIX   10 AB1 PRO A  958  ASN A  961  5                                   4    
HELIX   11 AB2 ASP A  993  ALA A  995  5                                   3    
SHEET    1 AA1 5 THR A 799  VAL A 803  0                                        
SHEET    2 AA1 5 ASP A 830  ARG A 841 -1  O  LYS A 838   N  LYS A 802           
SHEET    3 AA1 5 VAL A 997  ASN A1008 -1  O  LYS A1006   N  GLU A 832           
SHEET    4 AA1 5 ILE A 916  ALA A 925 -1  N  ILE A 919   O  LEU A1003           
SHEET    5 AA1 5 ARG A 857  GLY A 863 -1  N  ARG A 858   O  VAL A 924           
SHEET    1 AA2 4 ILE A 895  PHE A 897  0                                        
SHEET    2 AA2 4 GLU A 988  VAL A 991 -1  O  TYR A 989   N  PHE A 897           
SHEET    3 AA2 4 SER A 947  GLY A 950 -1  N  GLY A 950   O  GLU A 988           
SHEET    4 AA2 4 MET A 929  LEU A 932  1  N  LEU A 932   O  LYS A 949           
SHEET    1 AA3 3 GLY A 974  SER A 976  0                                        
SHEET    2 AA3 3 GLY A 952  PRO A 956 -1  N  THR A 955   O  ILE A 975           
SHEET    3 AA3 3 LEU A 984  TYR A 986  1  O  LEU A 985   N  THR A 954           
SHEET    1 AA4 2 ILE A 962  LEU A 964  0                                        
SHEET    2 AA4 2 VAL A 967  VAL A 969 -1  O  VAL A 967   N  LEU A 964           
SSBOND   1 CYS A  845    CYS A  845                          1555   7555  2.06  
SITE     1 AC1  4 ARG A 865  ASN A 906  TYR A 907  HIS A 909                    
SITE     1 AC2 12 HIS A 862  GLY A 863  LEU A 877  ARG A 878                    
SITE     2 AC2 12 TYR A 889  GLY A 894  ILE A 895  TYR A 896                    
SITE     3 AC2 12 PHE A 897  SER A 904  TYR A 907  GLU A 988                    
SITE     1 AC3  4 LYS A 903  LEU A 984  LEU A 985  TYR A 986                    
SITE     1 AC4  3 ARG A 858  MET A 929  LYS A 949                               
CRYST1   93.405   93.405  134.197  90.00  90.00 120.00 P 61 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010706  0.006181  0.000000        0.00000                         
SCALE2      0.000000  0.012362  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007452        0.00000                         
MODEL        1                                                                  
ATOM      1  N   SER A 765      26.799  56.739  16.552  1.00 90.23           N  
ANISOU    1  N   SER A 765     8444   9430  16409  -2070    378  -2266       N  
ATOM      2  CA  SER A 765      26.238  55.363  16.406  1.00 86.07           C  
ANISOU    2  CA  SER A 765     8093   9225  15384  -1807    308  -2009       C  
ATOM      3  C   SER A 765      27.121  54.476  15.555  1.00 85.76           C  
ANISOU    3  C   SER A 765     7838   9234  15513  -1722    435  -1700       C  
ATOM      4  O   SER A 765      27.343  54.769  14.389  1.00 84.88           O  
ANISOU    4  O   SER A 765     7715   8873  15662  -1702    810  -1479       O  
ATOM      5  CB  SER A 765      24.861  55.417  15.760  1.00 82.68           C  
ANISOU    5  CB  SER A 765     8055   8702  14655  -1607    556  -1831       C  
ATOM      6  OG  SER A 765      24.428  54.118  15.389  1.00 79.28           O  
ANISOU    6  OG  SER A 765     7761   8522  13839  -1376    549  -1565       O  
ATOM      7  N   LYS A 766      27.593  53.379  16.134  1.00 86.94           N  
ANISOU    7  N   LYS A 766     7827   9701  15505  -1665    141  -1673       N  
ATOM      8  CA  LYS A 766      28.401  52.396  15.403  1.00 88.71           C  
ANISOU    8  CA  LYS A 766     7833   9976  15897  -1557    263  -1396       C  
ATOM      9  C   LYS A 766      27.534  51.455  14.529  1.00 83.52           C  
ANISOU    9  C   LYS A 766     7479   9379  14874  -1292    500  -1107       C  
ATOM     10  O   LYS A 766      28.036  50.839  13.587  1.00 83.90           O  
ANISOU   10  O   LYS A 766     7426   9377  15072  -1201    753   -882       O  
ATOM     11  CB  LYS A 766      29.309  51.627  16.394  1.00 93.45           C  
ANISOU   11  CB  LYS A 766     8095  10861  16551  -1598   -161  -1465       C  
ATOM     12  CG  LYS A 766      29.556  50.136  16.139  1.00 94.23           C  
ANISOU   12  CG  LYS A 766     8106  11153  16544  -1380   -185  -1189       C  
ATOM     13  CD  LYS A 766      28.305  49.273  16.373  1.00 91.87           C  
ANISOU   13  CD  LYS A 766     8190  11063  15654  -1165   -259  -1090       C  
ATOM     14  CE  LYS A 766      28.579  48.034  17.221  1.00 93.23           C  
ANISOU   14  CE  LYS A 766     8220  11548  15655  -1056   -625   -992       C  
ATOM     15  NZ  LYS A 766      29.781  47.265  16.790  1.00 95.63           N  
ANISOU   15  NZ  LYS A 766     8124  11824  16385  -1000   -578   -803       N  
ATOM     16  N   LEU A 767      26.240  51.358  14.834  1.00 78.61           N  
ANISOU   16  N   LEU A 767     7218   8860  13790  -1180    430  -1136       N  
ATOM     17  CA  LEU A 767      25.317  50.464  14.116  1.00 73.49           C  
ANISOU   17  CA  LEU A 767     6856   8289  12777   -949    599   -902       C  
ATOM     18  C   LEU A 767      25.359  50.604  12.588  1.00 71.20           C  
ANISOU   18  C   LEU A 767     6647   7781  12624   -893   1043   -667       C  
ATOM     19  O   LEU A 767      25.553  51.694  12.072  1.00 72.65           O  
ANISOU   19  O   LEU A 767     6815   7708  13077  -1010   1260   -669       O  
ATOM     20  CB  LEU A 767      23.870  50.702  14.586  1.00 71.37           C  
ANISOU   20  CB  LEU A 767     6941   8084  12090   -878    511   -992       C  
ATOM     21  CG  LEU A 767      23.500  50.238  16.002  1.00 70.77           C  
ANISOU   21  CG  LEU A 767     6899   8296  11691   -874    123  -1165       C  
ATOM     22  CD1 LEU A 767      22.094  50.696  16.358  1.00 68.15           C  
ANISOU   22  CD1 LEU A 767     6896   7964  11033   -826    130  -1275       C  
ATOM     23  CD2 LEU A 767      23.644  48.726  16.143  1.00 69.07           C  
ANISOU   23  CD2 LEU A 767     6632   8331  11278   -719    -11   -982       C  
ATOM     24  N   PRO A 768      25.150  49.496  11.858  1.00 68.02           N  
ANISOU   24  N   PRO A 768     6345   7479  12020   -720   1186   -465       N  
ATOM     25  CA  PRO A 768      25.149  49.583  10.392  1.00 67.39           C  
ANISOU   25  CA  PRO A 768     6381   7240  11981   -675   1607   -255       C  
ATOM     26  C   PRO A 768      24.023  50.452   9.854  1.00 65.62           C  
ANISOU   26  C   PRO A 768     6489   6887  11554   -655   1750   -188       C  
ATOM     27  O   PRO A 768      22.979  50.549  10.480  1.00 64.55           O  
ANISOU   27  O   PRO A 768     6548   6833  11145   -600   1548   -274       O  
ATOM     28  CB  PRO A 768      24.959  48.125   9.943  1.00 65.77           C  
ANISOU   28  CB  PRO A 768     6256   7209  11524   -495   1664   -128       C  
ATOM     29  CG  PRO A 768      25.302  47.282  11.133  1.00 65.78           C  
ANISOU   29  CG  PRO A 768     6055   7406  11531   -462   1304   -228       C  
ATOM     30  CD  PRO A 768      24.962  48.110  12.333  1.00 66.29           C  
ANISOU   30  CD  PRO A 768     6129   7513  11543   -570    983   -424       C  
ATOM     31  N   LYS A 769      24.226  51.055   8.690  1.00 66.70           N  
ANISOU   31  N   LYS A 769     6683   6828  11828   -693   2105    -11       N  
ATOM     32  CA  LYS A 769      23.251  51.998   8.143  1.00 66.92           C  
ANISOU   32  CA  LYS A 769     6989   6705  11733   -677   2234    104       C  
ATOM     33  C   LYS A 769      21.841  51.408   8.015  1.00 62.68           C  
ANISOU   33  C   LYS A 769     6774   6340  10700   -499   2127    171       C  
ATOM     34  O   LYS A 769      20.894  51.985   8.536  1.00 62.33           O  
ANISOU   34  O   LYS A 769     6866   6257  10559   -476   1978    100       O  
ATOM     35  CB  LYS A 769      23.735  52.591   6.809  1.00 70.41           C  
ANISOU   35  CB  LYS A 769     7456   6944  12351   -733   2649    353       C  
ATOM     36  CG  LYS A 769      22.701  53.429   6.059  1.00 71.48           C  
ANISOU   36  CG  LYS A 769     7894   6945  12320   -684   2789    566       C  
ATOM     37  CD  LYS A 769      23.349  54.200   4.910  1.00 75.68           C  
ANISOU   37  CD  LYS A 769     8414   7250  13091   -778   3193    824       C  
ATOM     38  CE  LYS A 769      22.325  54.826   3.964  1.00 76.28           C  
ANISOU   38  CE  LYS A 769     8812   7243  12926   -697   3335   1128       C  
ATOM     39  NZ  LYS A 769      21.283  55.627   4.673  1.00 75.50           N  
ANISOU   39  NZ  LYS A 769     8806   7019  12861   -658   3105   1056       N  
ATOM     40  N   PRO A 770      21.690  50.264   7.331  1.00 59.90           N  
ANISOU   40  N   PRO A 770     6529   6164  10065   -382   2213    286       N  
ATOM     41  CA  PRO A 770      20.345  49.685   7.252  1.00 56.38           C  
ANISOU   41  CA  PRO A 770     6358   5878   9183   -234   2088    326       C  
ATOM     42  C   PRO A 770      19.641  49.584   8.598  1.00 53.82           C  
ANISOU   42  C   PRO A 770     6036   5655   8757   -200   1749    129       C  
ATOM     43  O   PRO A 770      18.428  49.790   8.680  1.00 52.08           O  
ANISOU   43  O   PRO A 770     6017   5457   8313   -122   1662    147       O  
ATOM     44  CB  PRO A 770      20.604  48.288   6.691  1.00 55.81           C  
ANISOU   44  CB  PRO A 770     6300   5980   8923   -150   2177    369       C  
ATOM     45  CG  PRO A 770      21.834  48.449   5.854  1.00 58.54           C  
ANISOU   45  CG  PRO A 770     6496   6210   9533   -236   2500    459       C  
ATOM     46  CD  PRO A 770      22.658  49.530   6.494  1.00 60.85           C  
ANISOU   46  CD  PRO A 770     6539   6315  10266   -384   2469    379       C  
ATOM     47  N   VAL A 771      20.396  49.267   9.644  1.00 53.80           N  
ANISOU   47  N   VAL A 771     5803   5724   8913   -261   1559    -48       N  
ATOM     48  CA  VAL A 771      19.822  49.123  10.975  1.00 52.28           C  
ANISOU   48  CA  VAL A 771     5620   5666   8578   -245   1247   -235       C  
ATOM     49  C   VAL A 771      19.419  50.493  11.490  1.00 53.70           C  
ANISOU   49  C   VAL A 771     5837   5676   8890   -337   1207   -370       C  
ATOM     50  O   VAL A 771      18.326  50.662  12.011  1.00 52.75           O  
ANISOU   50  O   VAL A 771     5876   5596   8567   -278   1097   -446       O  
ATOM     51  CB  VAL A 771      20.792  48.440  11.960  1.00 52.74           C  
ANISOU   51  CB  VAL A 771     5419   5871   8746   -293   1027   -359       C  
ATOM     52  CG1 VAL A 771      20.206  48.405  13.360  1.00 51.71           C  
ANISOU   52  CG1 VAL A 771     5329   5900   8418   -299    715   -544       C  
ATOM     53  CG2 VAL A 771      21.095  47.024  11.498  1.00 51.72           C  
ANISOU   53  CG2 VAL A 771     5250   5874   8527   -177   1080   -225       C  
ATOM     54  N   GLN A 772      20.285  51.482  11.319  1.00 56.66           N  
ANISOU   54  N   GLN A 772     6053   5835   9640   -483   1326   -405       N  
ATOM     55  CA  GLN A 772      19.941  52.853  11.694  1.00 58.38           C  
ANISOU   55  CA  GLN A 772     6299   5824  10058   -578   1339   -538       C  
ATOM     56  C   GLN A 772      18.706  53.364  10.959  1.00 58.07           C  
ANISOU   56  C   GLN A 772     6517   5654   9890   -462   1488   -362       C  
ATOM     57  O   GLN A 772      17.882  54.053  11.550  1.00 59.25           O  
ANISOU   57  O   GLN A 772     6754   5712  10045   -454   1420   -496       O  
ATOM     58  CB  GLN A 772      21.102  53.792  11.420  1.00 61.37           C  
ANISOU   58  CB  GLN A 772     6457   5949  10911   -759   1494   -562       C  
ATOM     59  CG  GLN A 772      22.365  53.475  12.201  1.00 62.88           C  
ANISOU   59  CG  GLN A 772     6337   6243  11312   -898   1315   -752       C  
ATOM     60  CD  GLN A 772      23.430  54.518  11.971  1.00 66.23           C  
ANISOU   60  CD  GLN A 772     6522   6385  12258  -1099   1470   -801       C  
ATOM     61  OE1 GLN A 772      24.584  54.204  11.694  1.00 67.30           O  
ANISOU   61  OE1 GLN A 772     6401   6524  12644  -1173   1534   -750       O  
ATOM     62  NE2 GLN A 772      23.035  55.776  12.054  1.00 68.15           N  
ANISOU   62  NE2 GLN A 772     6831   6351  12710  -1186   1558   -894       N  
ATOM     63  N   ASP A 773      18.580  53.031   9.675  1.00 58.23           N  
ANISOU   63  N   ASP A 773     6653   5673   9797   -373   1690    -66       N  
ATOM     64  CA  ASP A 773      17.415  53.442   8.876  1.00 58.14           C  
ANISOU   64  CA  ASP A 773     6877   5577   9637   -255   1794    153       C  
ATOM     65  C   ASP A 773      16.148  52.813   9.406  1.00 55.30           C  
ANISOU   65  C   ASP A 773     6664   5409   8935   -117   1593     84       C  
ATOM     66  O   ASP A 773      15.103  53.444   9.431  1.00 54.77           O  
ANISOU   66  O   ASP A 773     6711   5235   8862    -47   1583    119       O  
ATOM     67  CB  ASP A 773      17.579  53.045   7.409  1.00 58.87           C  
ANISOU   67  CB  ASP A 773     7079   5707   9582   -203   2017    469       C  
ATOM     68  CG  ASP A 773      18.726  53.778   6.719  1.00 62.70           C  
ANISOU   68  CG  ASP A 773     7441   5973  10409   -335   2289    597       C  
ATOM     69  OD1 ASP A 773      19.002  54.943   7.071  1.00 64.93           O  
ANISOU   69  OD1 ASP A 773     7617   5984  11066   -443   2338    536       O  
ATOM     70  OD2 ASP A 773      19.353  53.185   5.813  1.00 64.33           O  
ANISOU   70  OD2 ASP A 773     7652   6265  10523   -340   2478    749       O  
ATOM     71  N   LEU A 774      16.252  51.554   9.811  1.00 53.56           N  
ANISOU   71  N   LEU A 774     6423   5455   8470    -75   1452      1       N  
ATOM     72  CA  LEU A 774      15.127  50.828  10.395  1.00 51.81           C  
ANISOU   72  CA  LEU A 774     6318   5426   7940     40   1273    -67       C  
ATOM     73  C   LEU A 774      14.697  51.451  11.723  1.00 52.58           C  
ANISOU   73  C   LEU A 774     6383   5485   8108      0   1128   -328       C  
ATOM     74  O   LEU A 774      13.509  51.641  11.970  1.00 51.72           O  
ANISOU   74  O   LEU A 774     6390   5371   7887     86   1091   -348       O  
ATOM     75  CB  LEU A 774      15.515  49.371  10.609  1.00 50.28           C  
ANISOU   75  CB  LEU A 774     6078   5483   7543     75   1174    -91       C  
ATOM     76  CG  LEU A 774      14.507  48.455  11.279  1.00 48.34           C  
ANISOU   76  CG  LEU A 774     5924   5439   7002    177   1002   -153       C  
ATOM     77  CD1 LEU A 774      13.306  48.310  10.376  1.00 48.38           C  
ANISOU   77  CD1 LEU A 774     6115   5453   6815    291   1063     14       C  
ATOM     78  CD2 LEU A 774      15.121  47.096  11.565  1.00 47.34           C  
ANISOU   78  CD2 LEU A 774     5709   5503   6773    196    919   -163       C  
ATOM     79  N   ILE A 775      15.667  51.769  12.573  1.00 54.23           N  
ANISOU   79  N   ILE A 775     6426   5674   8504   -141   1051   -542       N  
ATOM     80  CA  ILE A 775      15.371  52.392  13.857  1.00 55.56           C  
ANISOU   80  CA  ILE A 775     6576   5824   8710   -213    923   -841       C  
ATOM     81  C   ILE A 775      14.613  53.685  13.622  1.00 56.32           C  
ANISOU   81  C   ILE A 775     6749   5625   9024   -201   1070   -853       C  
ATOM     82  O   ILE A 775      13.601  53.943  14.264  1.00 56.52           O  
ANISOU   82  O   ILE A 775     6865   5647   8963   -147   1035   -991       O  
ATOM     83  CB  ILE A 775      16.649  52.701  14.671  1.00 58.43           C  
ANISOU   83  CB  ILE A 775     6731   6192   9277   -402    808  -1076       C  
ATOM     84  CG1 ILE A 775      17.422  51.422  15.023  1.00 57.82           C  
ANISOU   84  CG1 ILE A 775     6538   6402   9028   -399    630  -1047       C  
ATOM     85  CG2 ILE A 775      16.305  53.438  15.960  1.00 60.64           C  
ANISOU   85  CG2 ILE A 775     7024   6455   9561   -500    692  -1428       C  
ATOM     86  CD1 ILE A 775      16.730  50.520  16.022  1.00 56.59           C  
ANISOU   86  CD1 ILE A 775     6477   6532   8491   -324    426  -1127       C  
ATOM     87  N   LYS A 776      15.104  54.496  12.695  1.00 58.25           N  
ANISOU   87  N   LYS A 776     6950   5606   9575   -248   1257   -693       N  
ATOM     88  CA  LYS A 776      14.443  55.760  12.359  1.00 60.68           C  
ANISOU   88  CA  LYS A 776     7314   5584  10156   -224   1414   -639       C  
ATOM     89  C   LYS A 776      13.012  55.530  11.901  1.00 58.04           C  
ANISOU   89  C   LYS A 776     7148   5292   9611    -27   1423   -442       C  
ATOM     90  O   LYS A 776      12.101  56.228  12.310  1.00 58.72           O  
ANISOU   90  O   LYS A 776     7272   5222   9816     27   1448   -537       O  
ATOM     91  CB  LYS A 776      15.206  56.492  11.254  1.00 64.18           C  
ANISOU   91  CB  LYS A 776     7698   5762  10922   -289   1631   -395       C  
ATOM     92  CG  LYS A 776      16.513  57.139  11.699  1.00 68.11           C  
ANISOU   92  CG  LYS A 776     7990   6095  11793   -507   1667   -606       C  
ATOM     93  CD  LYS A 776      17.360  57.583  10.508  1.00 71.13           C  
ANISOU   93  CD  LYS A 776     8307   6270  12449   -569   1910   -313       C  
ATOM     94  CE  LYS A 776      16.727  58.738   9.740  1.00 74.11           C  
ANISOU   94  CE  LYS A 776     8778   6290  13088   -514   2125    -64       C  
ATOM     95  NZ  LYS A 776      17.252  58.815   8.347  1.00 76.17           N  
ANISOU   95  NZ  LYS A 776     9068   6469  13405   -511   2364    344       N  
ATOM     96  N   MET A 777      12.843  54.529  11.050  1.00 56.26           N  
ANISOU   96  N   MET A 777     7006   5277   9094     72   1404   -186       N  
ATOM     97  CA  MET A 777      11.552  54.166  10.470  1.00 55.22           C  
ANISOU   97  CA  MET A 777     7014   5226   8740    245   1378     22       C  
ATOM     98  C   MET A 777      10.464  53.836  11.493  1.00 52.91           C  
ANISOU   98  C   MET A 777     6753   5054   8296    322   1249   -181       C  
ATOM     99  O   MET A 777       9.315  54.221  11.310  1.00 51.98           O  
ANISOU   99  O   MET A 777     6686   4843   8220    441   1266    -87       O  
ATOM    100  CB  MET A 777      11.750  52.976   9.515  1.00 54.72           C  
ANISOU  100  CB  MET A 777     7025   5407   8359    293   1363    240       C  
ATOM    101  CG  MET A 777      10.473  52.394   8.938  1.00 54.63           C  
ANISOU  101  CG  MET A 777     7143   5537   8076    444   1290    418       C  
ATOM    102  SD  MET A 777      10.764  51.544   7.377  1.00 55.97           S  
ANISOU  102  SD  MET A 777     7430   5876   7958    468   1355    713       S  
ATOM    103  CE  MET A 777      12.210  50.579   7.790  1.00 55.91           C  
ANISOU  103  CE  MET A 777     7316   6009   7918    357   1381    528       C  
ATOM    104  N   ILE A 778      10.823  53.129  12.559  1.00 52.15           N  
ANISOU  104  N   ILE A 778     6615   5165   8033    258   1126   -435       N  
ATOM    105  CA  ILE A 778       9.828  52.633  13.499  1.00 51.79           C  
ANISOU  105  CA  ILE A 778     6614   5280   7780    326   1028   -597       C  
ATOM    106  C   ILE A 778       9.675  53.469  14.769  1.00 54.02           C  
ANISOU  106  C   ILE A 778     6864   5459   8202    250   1041   -941       C  
ATOM    107  O   ILE A 778       8.836  53.162  15.613  1.00 52.94           O  
ANISOU  107  O   ILE A 778     6771   5446   7896    296   1003  -1094       O  
ATOM    108  CB  ILE A 778      10.072  51.150  13.839  1.00 50.63           C  
ANISOU  108  CB  ILE A 778     6479   5462   7293    332    889   -604       C  
ATOM    109  CG1 ILE A 778      11.215  50.970  14.834  1.00 51.64           C  
ANISOU  109  CG1 ILE A 778     6513   5702   7405    191    787   -827       C  
ATOM    110  CG2 ILE A 778      10.321  50.360  12.557  1.00 49.77           C  
ANISOU  110  CG2 ILE A 778     6405   5430   7075    387    912   -322       C  
ATOM    111  CD1 ILE A 778      11.727  49.545  14.896  1.00 50.48           C  
ANISOU  111  CD1 ILE A 778     6341   5820   7017    206    668   -743       C  
ATOM    112  N   PHE A 779      10.458  54.539  14.887  1.00 56.76           N  
ANISOU  112  N   PHE A 779     7134   5568   8864    124   1116  -1076       N  
ATOM    113  CA  PHE A 779      10.280  55.486  15.973  1.00 59.12           C  
ANISOU  113  CA  PHE A 779     7410   5715   9337     37   1161  -1436       C  
ATOM    114  C   PHE A 779       9.806  56.845  15.475  1.00 63.55           C  
ANISOU  114  C   PHE A 779     7951   5857  10335     77   1358  -1388       C  
ATOM    115  O   PHE A 779       8.869  57.394  16.044  1.00 67.11           O  
ANISOU  115  O   PHE A 779     8425   6178  10892    133   1443  -1563       O  
ATOM    116  CB  PHE A 779      11.567  55.603  16.785  1.00 59.92           C  
ANISOU  116  CB  PHE A 779     7418   5888   9461   -173   1058  -1722       C  
ATOM    117  CG  PHE A 779      11.800  54.439  17.707  1.00 57.62           C  
ANISOU  117  CG  PHE A 779     7145   5997   8750   -206    849  -1840       C  
ATOM    118  CD1 PHE A 779      11.131  54.358  18.919  1.00 57.69           C  
ANISOU  118  CD1 PHE A 779     7233   6159   8526   -220    805  -2119       C  
ATOM    119  CD2 PHE A 779      12.678  53.422  17.363  1.00 55.49           C  
ANISOU  119  CD2 PHE A 779     6813   5942   8329   -219    718  -1657       C  
ATOM    120  CE1 PHE A 779      11.329  53.289  19.773  1.00 56.65           C  
ANISOU  120  CE1 PHE A 779     7130   6400   7993   -248    615  -2177       C  
ATOM    121  CE2 PHE A 779      12.882  52.347  18.213  1.00 54.56           C  
ANISOU  121  CE2 PHE A 779     6699   6167   7861   -234    522  -1719       C  
ATOM    122  CZ  PHE A 779      12.205  52.281  19.419  1.00 55.40           C  
ANISOU  122  CZ  PHE A 779     6898   6436   7713   -250    461  -1960       C  
ATOM    123  N   GLY A 780      10.453  57.397  14.444  1.00 66.76           N  
ANISOU  123  N   GLY A 780     8309   6039  11016     50   1451  -1146       N  
ATOM    124  CA  GLY A 780      10.015  58.659  13.797  1.00 70.68           C  
ANISOU  124  CA  GLY A 780     8786   6112  11957    108   1643   -992       C  
ATOM    125  C   GLY A 780      10.000  59.912  14.673  1.00 76.23           C  
ANISOU  125  C   GLY A 780     9422   6476  13063      6   1771  -1364       C  
ATOM    126  O   GLY A 780       9.586  59.865  15.831  1.00 77.87           O  
ANISOU  126  O   GLY A 780     9650   6780  13156    -26   1737  -1741       O  
ATOM    127  N   SER A 781      10.414  61.047  14.110  1.00 81.07           N  
ANISOU  127  N   SER A 781     9964   6680  14157    -46   1941  -1259       N  
ATOM    128  CA  SER A 781      10.584  62.287  14.876  1.00 86.12           C  
ANISOU  128  CA  SER A 781    10524   6943  15255   -180   2084  -1641       C  
ATOM    129  C   SER A 781       9.285  63.005  15.215  1.00 90.10           C  
ANISOU  129  C   SER A 781    11045   7178  16011    -33   2230  -1741       C  
ATOM    130  O   SER A 781       8.250  62.361  15.409  1.00 87.74           O  
ANISOU  130  O   SER A 781    10813   7100  15421    128   2168  -1701       O  
ATOM    131  N   GLY A 782       9.364  64.338  15.331  1.00 96.11           N  
ANISOU  131  N   GLY A 782    11723   7440  17353    -98   2440  -1894       N  
ATOM    132  CA  GLY A 782       8.193  65.218  15.530  1.00100.77           C  
ANISOU  132  CA  GLY A 782    12289   7657  18340     52   2637  -1960       C  
ATOM    133  C   GLY A 782       7.415  65.137  16.848  1.00103.24           C  
ANISOU  133  C   GLY A 782    12639   8076  18511     54   2670  -2475       C  
ATOM    134  O   GLY A 782       6.765  64.123  17.132  1.00100.57           O  
ANISOU  134  O   GLY A 782    12378   8140  17693    159   2541  -2454       O  
ATOM    135  N   SER A 783       7.467  66.216  17.637  1.00110.21           N  
ANISOU  135  N   SER A 783    13468   8583  19823    -67   2869  -2942       N  
ATOM    136  CA  SER A 783       6.651  66.377  18.868  1.00113.73           C  
ANISOU  136  CA  SER A 783    13953   9041  20218    -65   2990  -3466       C  
ATOM    137  C   SER A 783       7.398  66.128  20.170  1.00115.38           C  
ANISOU  137  C   SER A 783    14233   9545  20062   -343   2889  -4083       C  
ATOM    138  O   SER A 783       7.950  67.055  20.783  1.00117.21           O  
ANISOU  138  O   SER A 783    14423   9489  20622   -555   3009  -4549       O  
ATOM    139  N   GLY A 784       7.343  64.870  20.608  1.00112.91           N  
ANISOU  139  N   GLY A 784    14024   9803  19071   -338   2666  -4083       N  
ATOM    140  CA  GLY A 784       8.328  64.279  21.512  1.00112.50           C  
ANISOU  140  CA  GLY A 784    14034  10168  18541   -588   2438  -4436       C  
ATOM    141  C   GLY A 784       9.136  63.315  20.658  1.00108.69           C  
ANISOU  141  C   GLY A 784    13527   9983  17786   -575   2179  -3966       C  
ATOM    142  O   GLY A 784       9.236  62.118  20.954  1.00103.61           O  
ANISOU  142  O   GLY A 784    12957   9828  16579   -565   1960  -3892       O  
ATOM    143  N   SER A 785       9.665  63.859  19.562  1.00109.83           N  
ANISOU  143  N   SER A 785    13567   9800  18361   -564   2239  -3632       N  
ATOM    144  CA  SER A 785      10.469  63.125  18.581  1.00106.90           C  
ANISOU  144  CA  SER A 785    13160   9622  17833   -553   2071  -3178       C  
ATOM    145  C   SER A 785      11.702  63.899  18.122  1.00108.80           C  
ANISOU  145  C   SER A 785    13264   9561  18510   -744   2117  -3168       C  
ATOM    146  O   SER A 785      12.607  63.318  17.514  1.00108.48           O  
ANISOU  146  O   SER A 785    13173   9700  18344   -794   1990  -2903       O  
ATOM    147  N   GLY A 786      11.732  65.209  18.380  1.00111.26           N  
ANISOU  147  N   GLY A 786    13505   9391  19376   -849   2326  -3451       N  
ATOM    148  CA  GLY A 786      12.979  65.966  18.380  1.00113.20           C  
ANISOU  148  CA  GLY A 786    13605   9376  20029  -1111   2355  -3635       C  
ATOM    149  C   GLY A 786      13.746  65.588  19.636  1.00112.93           C  
ANISOU  149  C   GLY A 786    13555   9696  19656  -1367   2117  -4178       C  
ATOM    150  O   GLY A 786      13.736  66.328  20.622  1.00115.92           O  
ANISOU  150  O   GLY A 786    13929   9919  20197  -1541   2174  -4736       O  
ATOM    151  N   GLY A 787      14.395  64.421  19.595  1.00108.06           N  
ANISOU  151  N   GLY A 787    12930   9560  18565  -1388   1846  -4010       N  
ATOM    152  CA  GLY A 787      15.050  63.820  20.767  1.00106.74           C  
ANISOU  152  CA  GLY A 787    12754   9831  17968  -1588   1553  -4420       C  
ATOM    153  C   GLY A 787      15.183  62.301  20.667  1.00100.45           C  
ANISOU  153  C   GLY A 787    12007   9581  16577  -1472   1295  -4109       C  
ATOM    154  O   GLY A 787      14.570  61.672  19.797  1.00 96.16           O  
ANISOU  154  O   GLY A 787    11538   9099  15897  -1230   1357  -3646       O  
ATOM    155  N   ASP A 788      15.981  61.723  21.571  1.00 98.82           N  
ANISOU  155  N   ASP A 788    11751   9763  16033  -1649    998  -4369       N  
ATOM    156  CA  ASP A 788      16.290  60.268  21.623  1.00 92.55           C  
ANISOU  156  CA  ASP A 788    10966   9477  14719  -1568    728  -4108       C  
ATOM    157  C   ASP A 788      17.183  59.778  20.485  1.00 87.32           C  
ANISOU  157  C   ASP A 788    10145   8799  14233  -1526    704  -3662       C  
ATOM    158  O   ASP A 788      16.695  59.519  19.386  1.00 83.14           O  
ANISOU  158  O   ASP A 788     9673   8157  13758  -1321    876  -3236       O  
ATOM    159  CB  ASP A 788      15.028  59.400  21.696  1.00 89.30           C  
ANISOU  159  CB  ASP A 788    10765   9309  13854  -1319    757  -3913       C  
ATOM    160  CG  ASP A 788      14.488  59.289  23.100  1.00 91.19           C  
ANISOU  160  CG  ASP A 788    11148   9820  13677  -1390    662  -4334       C  
ATOM    161  OD1 ASP A 788      13.919  60.285  23.598  1.00 93.87           O  
ANISOU  161  OD1 ASP A 788    11554   9909  14200  -1453    850  -4706       O  
ATOM    162  OD2 ASP A 788      14.640  58.206  23.701  1.00 89.92           O  
ANISOU  162  OD2 ASP A 788    11035  10115  13014  -1384    417  -4287       O  
ATOM    163  N   PRO A 789      18.494  59.635  20.751  1.00 86.48           N  
ANISOU  163  N   PRO A 789     9828   8820  14208  -1726    491  -3768       N  
ATOM    164  CA  PRO A 789      19.401  59.179  19.701  1.00 83.86           C  
ANISOU  164  CA  PRO A 789     9321   8463  14078  -1696    509  -3375       C  
ATOM    165  C   PRO A 789      19.201  57.720  19.303  1.00 79.00           C  
ANISOU  165  C   PRO A 789     8775   8203  13038  -1480    410  -2989       C  
ATOM    166  O   PRO A 789      18.506  56.964  19.984  1.00 77.05           O  
ANISOU  166  O   PRO A 789     8682   8269  12322  -1380    267  -3031       O  
ATOM    167  CB  PRO A 789      20.790  59.387  20.309  1.00 87.34           C  
ANISOU  167  CB  PRO A 789     9490   8976  14717  -1974    275  -3652       C  
ATOM    168  CG  PRO A 789      20.569  59.388  21.774  1.00 89.99           C  
ANISOU  168  CG  PRO A 789     9908   9592  14691  -2104     12  -4110       C  
ATOM    169  CD  PRO A 789      19.212  59.979  21.990  1.00 90.02           C  
ANISOU  169  CD  PRO A 789    10174   9418  14611  -2003    239  -4269       C  
ATOM    170  N   ILE A 790      19.838  57.351  18.197  1.00 76.87           N  
ANISOU  170  N   ILE A 790     8386   7863  12956  -1421    513  -2626       N  
ATOM    171  CA  ILE A 790      19.659  56.050  17.562  1.00 72.89           C  
ANISOU  171  CA  ILE A 790     7945   7606  12143  -1214    498  -2248       C  
ATOM    172  C   ILE A 790      19.914  54.908  18.544  1.00 71.34           C  
ANISOU  172  C   ILE A 790     7714   7847  11542  -1211    167  -2328       C  
ATOM    173  O   ILE A 790      19.056  54.057  18.745  1.00 69.27           O  
ANISOU  173  O   ILE A 790     7630   7810  10877  -1047    113  -2220       O  
ATOM    174  CB  ILE A 790      20.584  55.925  16.316  1.00 73.34           C  
ANISOU  174  CB  ILE A 790     7838   7516  12512  -1211    674  -1929       C  
ATOM    175  CG1 ILE A 790      20.147  56.906  15.210  1.00 73.94           C  
ANISOU  175  CG1 ILE A 790     8007   7194  12893  -1169   1019  -1734       C  
ATOM    176  CG2 ILE A 790      20.624  54.500  15.773  1.00 70.03           C  
ANISOU  176  CG2 ILE A 790     7445   7366  11796  -1035    640  -1616       C  
ATOM    177  CD1 ILE A 790      18.743  56.683  14.674  1.00 71.03           C  
ANISOU  177  CD1 ILE A 790     7914   6830  12245   -939   1137  -1512       C  
ATOM    178  N   ASP A 791      21.080  54.913  19.173  1.00 73.28           N  
ANISOU  178  N   ASP A 791     7719   8206  11916  -1396    -62  -2506       N  
ATOM    179  CA  ASP A 791      21.488  53.812  20.036  1.00 72.65           C  
ANISOU  179  CA  ASP A 791     7565   8540  11498  -1391   -402  -2510       C  
ATOM    180  C   ASP A 791      20.575  53.599  21.242  1.00 71.67           C  
ANISOU  180  C   ASP A 791     7662   8685  10882  -1375   -580  -2727       C  
ATOM    181  O   ASP A 791      20.433  52.472  21.710  1.00 70.49           O  
ANISOU  181  O   ASP A 791     7560   8867  10355  -1272   -770  -2586       O  
ATOM    182  CB  ASP A 791      22.926  54.025  20.514  1.00 76.93           C  
ANISOU  182  CB  ASP A 791     7772   9139  12318  -1614   -645  -2676       C  
ATOM    183  CG  ASP A 791      23.950  53.932  19.379  1.00 77.85           C  
ANISOU  183  CG  ASP A 791     7625   9057  12894  -1613   -476  -2416       C  
ATOM    184  OD1 ASP A 791      25.115  54.347  19.611  1.00 81.51           O  
ANISOU  184  OD1 ASP A 791     7778   9474  13716  -1815   -608  -2561       O  
ATOM    185  OD2 ASP A 791      23.602  53.442  18.272  1.00 74.58           O  
ANISOU  185  OD2 ASP A 791     7309   8546  12481  -1423   -210  -2082       O  
ATOM    186  N   VAL A 792      19.966  54.666  21.748  1.00 72.45           N  
ANISOU  186  N   VAL A 792     7894   8631  11002  -1478   -493  -3065       N  
ATOM    187  CA  VAL A 792      19.121  54.558  22.935  1.00 72.79           C  
ANISOU  187  CA  VAL A 792     8151   8926  10580  -1487   -616  -3317       C  
ATOM    188  C   VAL A 792      17.803  53.903  22.560  1.00 68.59           C  
ANISOU  188  C   VAL A 792     7861   8432   9768  -1232   -432  -3064       C  
ATOM    189  O   VAL A 792      17.296  53.059  23.299  1.00 67.36           O  
ANISOU  189  O   VAL A 792     7835   8602   9156  -1161   -569  -3035       O  
ATOM    190  CB  VAL A 792      18.882  55.930  23.601  1.00 76.37           C  
ANISOU  190  CB  VAL A 792     8664   9176  11177  -1684   -540  -3809       C  
ATOM    191  CG1 VAL A 792      17.880  55.822  24.743  1.00 77.12           C  
ANISOU  191  CG1 VAL A 792     9011   9517  10771  -1676   -583  -4071       C  
ATOM    192  CG2 VAL A 792      20.195  56.488  24.117  1.00 80.76           C  
ANISOU  192  CG2 VAL A 792     8969   9745  11969  -1969   -778  -4105       C  
ATOM    193  N   ASN A 793      17.265  54.297  21.406  1.00 66.59           N  
ANISOU  193  N   ASN A 793     7656   7849   9794  -1104   -131  -2865       N  
ATOM    194  CA  ASN A 793      16.063  53.668  20.844  1.00 63.10           C  
ANISOU  194  CA  ASN A 793     7401   7423   9151   -864     30  -2590       C  
ATOM    195  C   ASN A 793      16.286  52.219  20.470  1.00 60.01           C  
ANISOU  195  C   ASN A 793     6980   7284   8534   -728    -82  -2241       C  
ATOM    196  O   ASN A 793      15.377  51.404  20.575  1.00 57.93           O  
ANISOU  196  O   ASN A 793     6865   7185   7961   -578    -71  -2103       O  
ATOM    197  CB  ASN A 793      15.553  54.434  19.617  1.00 62.34           C  
ANISOU  197  CB  ASN A 793     7339   6934   9413   -769    333  -2420       C  
ATOM    198  CG  ASN A 793      14.766  55.679  19.991  1.00 65.19           C  
ANISOU  198  CG  ASN A 793     7791   7025   9950   -811    504  -2707       C  
ATOM    199  OD1 ASN A 793      14.617  56.018  21.169  1.00 67.72           O  
ANISOU  199  OD1 ASN A 793     8161   7447  10123   -929    423  -3085       O  
ATOM    200  ND2 ASN A 793      14.260  56.373  18.984  1.00 65.25           N  
ANISOU  200  ND2 ASN A 793     7824   6687  10280   -715    749  -2527       N  
ATOM    201  N   TYR A 794      17.494  51.899  20.027  1.00 60.38           N  
ANISOU  201  N   TYR A 794     6820   7341   8779   -781   -169  -2106       N  
ATOM    202  CA  TYR A 794      17.832  50.528  19.686  1.00 58.63           C  
ANISOU  202  CA  TYR A 794     6539   7324   8412   -657   -260  -1800       C  
ATOM    203  C   TYR A 794      17.794  49.646  20.925  1.00 59.29           C  
ANISOU  203  C   TYR A 794     6650   7778   8098   -660   -541  -1849       C  
ATOM    204  O   TYR A 794      17.131  48.617  20.942  1.00 56.68           O  
ANISOU  204  O   TYR A 794     6435   7604   7495   -507   -543  -1652       O  
ATOM    205  CB  TYR A 794      19.212  50.471  19.039  1.00 59.85           C  
ANISOU  205  CB  TYR A 794     6429   7389   8921   -727   -271  -1685       C  
ATOM    206  CG  TYR A 794      19.716  49.075  18.817  1.00 58.56           C  
ANISOU  206  CG  TYR A 794     6160   7419   8670   -612   -369  -1415       C  
ATOM    207  CD1 TYR A 794      19.305  48.338  17.718  1.00 55.85           C  
ANISOU  207  CD1 TYR A 794     5901   7009   8307   -439   -161  -1139       C  
ATOM    208  CD2 TYR A 794      20.600  48.487  19.711  1.00 60.90           C  
ANISOU  208  CD2 TYR A 794     6265   7960   8913   -677   -677  -1441       C  
ATOM    209  CE1 TYR A 794      19.770  47.050  17.508  1.00 55.23           C  
ANISOU  209  CE1 TYR A 794     5720   7067   8196   -335   -219   -922       C  
ATOM    210  CE2 TYR A 794      21.071  47.201  19.511  1.00 60.12           C  
ANISOU  210  CE2 TYR A 794     6044   7997   8799   -555   -752  -1176       C  
ATOM    211  CZ  TYR A 794      20.651  46.490  18.409  1.00 56.99           C  
ANISOU  211  CZ  TYR A 794     5737   7495   8421   -384   -503   -932       C  
ATOM    212  OH  TYR A 794      21.113  45.221  18.213  1.00 56.14           O  
ANISOU  212  OH  TYR A 794     5506   7482   8342   -265   -547   -702       O  
ATOM    213  N   GLU A 795      18.499  50.067  21.963  1.00 63.40           N  
ANISOU  213  N   GLU A 795     7066   8438   8584   -844   -782  -2109       N  
ATOM    214  CA  GLU A 795      18.513  49.334  23.225  1.00 66.20           C  
ANISOU  214  CA  GLU A 795     7457   9176   8516   -870  -1077  -2151       C  
ATOM    215  C   GLU A 795      17.090  49.179  23.767  1.00 64.29           C  
ANISOU  215  C   GLU A 795     7509   9041   7876   -781   -970  -2208       C  
ATOM    216  O   GLU A 795      16.789  48.223  24.467  1.00 64.14           O  
ANISOU  216  O   GLU A 795     7573   9314   7482   -716  -1111  -2082       O  
ATOM    217  CB  GLU A 795      19.464  50.018  24.227  1.00 72.00           C  
ANISOU  217  CB  GLU A 795     8046  10045   9266  -1118  -1363  -2475       C  
ATOM    218  CG  GLU A 795      19.204  49.726  25.690  1.00 76.03           C  
ANISOU  218  CG  GLU A 795     8687  10947   9251  -1198  -1633  -2641       C  
ATOM    219  CD  GLU A 795      18.023  50.522  26.222  1.00 78.76           C  
ANISOU  219  CD  GLU A 795     9314  11246   9364  -1240  -1439  -2966       C  
ATOM    220  OE1 GLU A 795      18.063  51.775  26.141  1.00 82.33           O  
ANISOU  220  OE1 GLU A 795     9755  11441  10083  -1383  -1311  -3304       O  
ATOM    221  OE2 GLU A 795      17.049  49.899  26.712  1.00 78.79           O  
ANISOU  221  OE2 GLU A 795     9536  11442   8956  -1129  -1389  -2882       O  
ATOM    222  N   LYS A 796      16.216  50.111  23.412  1.00 63.26           N  
ANISOU  222  N   LYS A 796     7516   8654   7865   -770   -702  -2371       N  
ATOM    223  CA  LYS A 796      14.798  50.055  23.783  1.00 62.02           C  
ANISOU  223  CA  LYS A 796     7601   8538   7425   -671   -542  -2424       C  
ATOM    224  C   LYS A 796      14.041  48.850  23.238  1.00 57.62           C  
ANISOU  224  C   LYS A 796     7124   8050   6719   -456   -456  -2060       C  
ATOM    225  O   LYS A 796      13.019  48.452  23.786  1.00 56.88           O  
ANISOU  225  O   LYS A 796     7193   8093   6324   -385   -396  -2060       O  
ATOM    226  CB  LYS A 796      14.105  51.305  23.262  1.00 62.61           C  
ANISOU  226  CB  LYS A 796     7742   8251   7795   -673   -258  -2608       C  
ATOM    227  CG  LYS A 796      12.906  51.755  24.061  1.00 63.90           C  
ANISOU  227  CG  LYS A 796     8100   8435   7740   -667   -115  -2865       C  
ATOM    228  CD  LYS A 796      12.594  53.212  23.751  1.00 65.96           C  
ANISOU  228  CD  LYS A 796     8363   8308   8391   -722    115  -3124       C  
ATOM    229  CE  LYS A 796      13.694  54.150  24.227  1.00 69.60           C  
ANISOU  229  CE  LYS A 796     8706   8693   9044   -966     -3  -3469       C  
ATOM    230  NZ  LYS A 796      13.219  55.555  24.217  1.00 72.13           N  
ANISOU  230  NZ  LYS A 796     9059   8638   9707  -1029    244  -3789       N  
ATOM    231  N   LEU A 797      14.527  48.300  22.136  1.00 55.36           N  
ANISOU  231  N   LEU A 797     6718   7652   6661   -363   -426  -1772       N  
ATOM    232  CA  LEU A 797      13.891  47.161  21.480  1.00 52.17           C  
ANISOU  232  CA  LEU A 797     6375   7280   6168   -177   -338  -1456       C  
ATOM    233  C   LEU A 797      14.183  45.814  22.155  1.00 52.34           C  
ANISOU  233  C   LEU A 797     6368   7597   5920   -133   -541  -1269       C  
ATOM    234  O   LEU A 797      13.528  44.814  21.851  1.00 49.36           O  
ANISOU  234  O   LEU A 797     6058   7258   5436      4   -471  -1046       O  
ATOM    235  CB  LEU A 797      14.341  47.100  20.013  1.00 50.27           C  
ANISOU  235  CB  LEU A 797     6033   6809   6255   -111   -205  -1251       C  
ATOM    236  CG  LEU A 797      14.004  48.316  19.148  1.00 50.32           C  
ANISOU  236  CG  LEU A 797     6074   6507   6539   -124     11  -1325       C  
ATOM    237  CD1 LEU A 797      14.618  48.196  17.763  1.00 49.31           C  
ANISOU  237  CD1 LEU A 797     5854   6208   6672    -81    134  -1105       C  
ATOM    238  CD2 LEU A 797      12.493  48.491  19.039  1.00 49.30           C  
ANISOU  238  CD2 LEU A 797     6122   6313   6295    -14    166  -1326       C  
ATOM    239  N   LYS A 798      15.181  45.783  23.044  1.00 55.89           N  
ANISOU  239  N   LYS A 798     6704   8244   6286   -254   -802  -1348       N  
ATOM    240  CA  LYS A 798      15.565  44.565  23.755  1.00 56.39           C  
ANISOU  240  CA  LYS A 798     6719   8590   6117   -213  -1030  -1133       C  
ATOM    241  C   LYS A 798      15.742  43.418  22.765  1.00 53.67           C  
ANISOU  241  C   LYS A 798     6279   8145   5967    -50   -952   -793       C  
ATOM    242  O   LYS A 798      15.307  42.302  23.011  1.00 52.30           O  
ANISOU  242  O   LYS A 798     6162   8091   5617     58   -971   -572       O  
ATOM    243  CB  LYS A 798      14.491  44.215  24.784  1.00 57.41           C  
ANISOU  243  CB  LYS A 798     7067   8942   5801   -192  -1027  -1157       C  
ATOM    244  CG  LYS A 798      14.030  45.377  25.649  1.00 59.66           C  
ANISOU  244  CG  LYS A 798     7496   9286   5883   -337   -999  -1541       C  
ATOM    245  CD  LYS A 798      15.172  45.932  26.474  1.00 63.91           C  
ANISOU  245  CD  LYS A 798     7922   9998   6360   -533  -1291  -1756       C  
ATOM    246  CE  LYS A 798      14.697  46.907  27.548  1.00 66.90           C  
ANISOU  246  CE  LYS A 798     8476  10499   6442   -695  -1279  -2170       C  
ATOM    247  NZ  LYS A 798      15.879  47.531  28.209  1.00 70.87           N  
ANISOU  247  NZ  LYS A 798     8845  11143   6938   -913  -1581  -2421       N  
ATOM    248  N   THR A 799      16.381  43.728  21.641  1.00 53.55           N  
ANISOU  248  N   THR A 799     6125   7896   6325    -44   -838   -768       N  
ATOM    249  CA  THR A 799      16.458  42.850  20.457  1.00 52.18           C  
ANISOU  249  CA  THR A 799     5895   7573   6359     95   -677   -522       C  
ATOM    250  C   THR A 799      17.872  42.992  19.868  1.00 53.87           C  
ANISOU  250  C   THR A 799     5847   7678   6943     47   -706   -488       C  
ATOM    251  O   THR A 799      18.444  44.086  19.866  1.00 55.50           O  
ANISOU  251  O   THR A 799     5966   7801   7318    -87   -724   -675       O  
ATOM    252  CB  THR A 799      15.391  43.260  19.378  1.00 49.34           C  
ANISOU  252  CB  THR A 799     5705   6998   6040    161   -387   -545       C  
ATOM    253  OG1 THR A 799      14.069  43.122  19.903  1.00 47.95           O  
ANISOU  253  OG1 THR A 799     5730   6909   5580    208   -346   -575       O  
ATOM    254  CG2 THR A 799      15.470  42.422  18.112  1.00 47.51           C  
ANISOU  254  CG2 THR A 799     5442   6634   5975    275   -219   -343       C  
ATOM    255  N   ASP A 800      18.447  41.886  19.403  1.00 54.44           N  
ANISOU  255  N   ASP A 800     5776   7733   7175    150   -694   -261       N  
ATOM    256  CA  ASP A 800      19.688  41.940  18.631  1.00 56.09           C  
ANISOU  256  CA  ASP A 800     5732   7798   7781    129   -631   -216       C  
ATOM    257  C   ASP A 800      19.275  41.983  17.173  1.00 52.99           C  
ANISOU  257  C   ASP A 800     5448   7177   7507    195   -287   -179       C  
ATOM    258  O   ASP A 800      18.472  41.166  16.738  1.00 50.74           O  
ANISOU  258  O   ASP A 800     5311   6879   7087    313   -166    -71       O  
ATOM    259  CB  ASP A 800      20.566  40.714  18.892  1.00 58.70           C  
ANISOU  259  CB  ASP A 800     5827   8210   8265    216   -777      5       C  
ATOM    260  CG  ASP A 800      21.959  40.843  18.263  1.00 62.55           C  
ANISOU  260  CG  ASP A 800     5995   8561   9207    181   -725     29       C  
ATOM    261  OD1 ASP A 800      22.820  41.530  18.853  1.00 66.98           O  
ANISOU  261  OD1 ASP A 800     6354   9190   9905     48   -935    -74       O  
ATOM    262  OD2 ASP A 800      22.208  40.255  17.184  1.00 62.33           O  
ANISOU  262  OD2 ASP A 800     5909   8361   9412    276   -464    135       O  
ATOM    263  N   ILE A 801      19.808  42.937  16.419  1.00 53.16           N  
ANISOU  263  N   ILE A 801     5401   7026   7771    109   -132   -265       N  
ATOM    264  CA  ILE A 801      19.481  43.062  15.000  1.00 51.25           C  
ANISOU  264  CA  ILE A 801     5275   6595   7600    156    189   -210       C  
ATOM    265  C   ILE A 801      20.772  43.028  14.193  1.00 53.21           C  
ANISOU  265  C   ILE A 801     5286   6711   8218    126    348   -152       C  
ATOM    266  O   ILE A 801      21.680  43.803  14.448  1.00 55.18           O  
ANISOU  266  O   ILE A 801     5338   6913   8716      4    288   -234       O  
ATOM    267  CB  ILE A 801      18.684  44.351  14.717  1.00 49.97           C  
ANISOU  267  CB  ILE A 801     5304   6322   7357     91    295   -327       C  
ATOM    268  CG1 ILE A 801      17.532  44.482  15.718  1.00 48.82           C  
ANISOU  268  CG1 ILE A 801     5338   6307   6902    106    138   -424       C  
ATOM    269  CG2 ILE A 801      18.140  44.362  13.292  1.00 48.29           C  
ANISOU  269  CG2 ILE A 801     5254   5971   7121    157    580   -220       C  
ATOM    270  CD1 ILE A 801      16.633  45.668  15.462  1.00 48.25           C  
ANISOU  270  CD1 ILE A 801     5439   6101   6790     73    253   -528       C  
ATOM    271  N   LYS A 802      20.855  42.089  13.251  1.00 53.60           N  
ANISOU  271  N   LYS A 802     5344   6701   8319    230    558    -29       N  
ATOM    272  CA  LYS A 802      21.987  41.991  12.329  1.00 55.56           C  
ANISOU  272  CA  LYS A 802     5393   6811   8906    215    795     19       C  
ATOM    273  C   LYS A 802      21.481  41.972  10.903  1.00 53.05           C  
ANISOU  273  C   LYS A 802     5294   6384   8477    251   1139     59       C  
ATOM    274  O   LYS A 802      20.433  41.409  10.626  1.00 51.72           O  
ANISOU  274  O   LYS A 802     5359   6267   8023    334   1164     82       O  
ATOM    275  CB  LYS A 802      22.771  40.709  12.566  1.00 58.18           C  
ANISOU  275  CB  LYS A 802     5483   7176   9446    311    746    118       C  
ATOM    276  CG  LYS A 802      23.495  40.637  13.892  1.00 62.13           C  
ANISOU  276  CG  LYS A 802     5715   7804  10088    277    386    129       C  
ATOM    277  CD  LYS A 802      24.390  39.406  13.927  1.00 66.05           C  
ANISOU  277  CD  LYS A 802     5925   8281  10889    391    379    275       C  
ATOM    278  CE  LYS A 802      24.605  38.896  15.347  1.00 69.22           C  
ANISOU  278  CE  LYS A 802     6166   8875  11256    421    -39    370       C  
ATOM    279  NZ  LYS A 802      25.101  39.963  16.267  1.00 72.15           N  
ANISOU  279  NZ  LYS A 802     6400   9369  11642    258   -341    257       N  
ATOM    280  N   VAL A 803      22.239  42.573  10.000  1.00 53.49           N  
ANISOU  280  N   VAL A 803     5269   6301   8753    178   1401     73       N  
ATOM    281  CA  VAL A 803      21.913  42.530   8.585  1.00 52.45           C  
ANISOU  281  CA  VAL A 803     5344   6095   8489    199   1741    129       C  
ATOM    282  C   VAL A 803      22.332  41.187   8.006  1.00 52.87           C  
ANISOU  282  C   VAL A 803     5330   6145   8613    294   1928    150       C  
ATOM    283  O   VAL A 803      23.490  40.781   8.112  1.00 55.26           O  
ANISOU  283  O   VAL A 803     5335   6387   9273    298   1997    157       O  
ATOM    284  CB  VAL A 803      22.604  43.657   7.793  1.00 53.71           C  
ANISOU  284  CB  VAL A 803     5453   6105   8849     81   1999    163       C  
ATOM    285  CG1 VAL A 803      22.258  43.558   6.311  1.00 53.69           C  
ANISOU  285  CG1 VAL A 803     5693   6070   8633    100   2347    246       C  
ATOM    286  CG2 VAL A 803      22.187  45.010   8.346  1.00 53.58           C  
ANISOU  286  CG2 VAL A 803     5495   6040   8823    -13   1839    127       C  
ATOM    287  N   VAL A 804      21.375  40.500   7.401  1.00 51.15           N  
ANISOU  287  N   VAL A 804     5372   5978   8084    367   2010    148       N  
ATOM    288  CA  VAL A 804      21.656  39.303   6.638  1.00 51.42           C  
ANISOU  288  CA  VAL A 804     5398   5978   8160    439   2254    124       C  
ATOM    289  C   VAL A 804      22.332  39.746   5.348  1.00 54.45           C  
ANISOU  289  C   VAL A 804     5807   6273   8609    368   2652    130       C  
ATOM    290  O   VAL A 804      21.804  40.575   4.611  1.00 53.60           O  
ANISOU  290  O   VAL A 804     5935   6183   8245    304   2757    172       O  
ATOM    291  CB  VAL A 804      20.362  38.533   6.326  1.00 49.08           C  
ANISOU  291  CB  VAL A 804     5387   5763   7496    504   2217     86       C  
ATOM    292  CG1 VAL A 804      20.619  37.387   5.366  1.00 50.71           C  
ANISOU  292  CG1 VAL A 804     5623   5913   7730    550   2518      9       C  
ATOM    293  CG2 VAL A 804      19.738  38.020   7.610  1.00 47.30           C  
ANISOU  293  CG2 VAL A 804     5124   5616   7230    572   1872    101       C  
ATOM    294  N   ASP A 805      23.515  39.206   5.094  1.00 58.77           N  
ANISOU  294  N   ASP A 805     6096   6720   9514    384   2882    109       N  
ATOM    295  CA  ASP A 805      24.244  39.503   3.873  1.00 63.10           C  
ANISOU  295  CA  ASP A 805     6649   7184  10142    317   3321    108       C  
ATOM    296  C   ASP A 805      23.394  39.161   2.646  1.00 63.61           C  
ANISOU  296  C   ASP A 805     7095   7321   9750    316   3556     60       C  
ATOM    297  O   ASP A 805      22.830  38.073   2.558  1.00 61.99           O  
ANISOU  297  O   ASP A 805     7001   7158   9395    393   3532    -37       O  
ATOM    298  CB  ASP A 805      25.555  38.716   3.850  1.00 66.85           C  
ANISOU  298  CB  ASP A 805     6764   7533  11102    363   3543     68       C  
ATOM    299  CG  ASP A 805      26.502  39.186   2.764  1.00 71.99           C  
ANISOU  299  CG  ASP A 805     7345   8082  11924    276   4015     74       C  
ATOM    300  OD1 ASP A 805      26.202  40.194   2.096  1.00 73.56           O  
ANISOU  300  OD1 ASP A 805     7769   8308  11869    172   4147    141       O  
ATOM    301  OD2 ASP A 805      27.558  38.541   2.570  1.00 76.66           O  
ANISOU  301  OD2 ASP A 805     7646   8556  12925    316   4276     28       O  
ATOM    302  N   ARG A 806      23.306  40.099   1.706  1.00 66.23           N  
ANISOU  302  N   ARG A 806     7626   7670   9867    220   3771    137       N  
ATOM    303  CA  ARG A 806      22.534  39.896   0.483  1.00 69.03           C  
ANISOU  303  CA  ARG A 806     8354   8135   9736    198   3970    113       C  
ATOM    304  C   ARG A 806      22.948  38.623  -0.281  1.00 70.31           C  
ANISOU  304  C   ARG A 806     8527   8282   9903    231   4311    -64       C  
ATOM    305  O   ARG A 806      22.110  37.952  -0.874  1.00 69.12           O  
ANISOU  305  O   ARG A 806     8647   8238   9374    242   4329   -174       O  
ATOM    306  CB  ARG A 806      22.658  41.117  -0.437  1.00 74.01           C  
ANISOU  306  CB  ARG A 806     9150   8773  10197     87   4200    275       C  
ATOM    307  CG  ARG A 806      21.620  41.123  -1.557  1.00 78.25           C  
ANISOU  307  CG  ARG A 806    10108   9480  10142     59   4268    309       C  
ATOM    308  CD  ARG A 806      21.965  42.022  -2.745  1.00 84.06           C  
ANISOU  308  CD  ARG A 806    11021  10235  10682    -46   4620    482       C  
ATOM    309  NE  ARG A 806      21.348  41.501  -3.970  1.00 89.21           N  
ANISOU  309  NE  ARG A 806    12034  11081  10779    -76   4789    431       N  
ATOM    310  CZ  ARG A 806      20.040  41.538  -4.256  1.00 90.69           C  
ANISOU  310  CZ  ARG A 806    12516  11445  10495    -64   4518    478       C  
ATOM    311  NH1 ARG A 806      19.160  42.100  -3.423  1.00 88.76           N  
ANISOU  311  NH1 ARG A 806    12252  11191  10278    -10   4094    588       N  
ATOM    312  NH2 ARG A 806      19.603  41.009  -5.397  1.00 93.97           N  
ANISOU  312  NH2 ARG A 806    13240  12055  10407   -112   4675    400       N  
ATOM    313  N   ASP A 807      24.239  38.300  -0.250  1.00 72.16           N  
ANISOU  313  N   ASP A 807     8448   8371  10598    243   4580   -109       N  
ATOM    314  CA  ASP A 807      24.784  37.122  -0.937  1.00 74.18           C  
ANISOU  314  CA  ASP A 807     8660   8559  10963    282   4963   -298       C  
ATOM    315  C   ASP A 807      24.625  35.787  -0.207  1.00 70.26           C  
ANISOU  315  C   ASP A 807     8013   7992  10691    413   4789   -428       C  
ATOM    316  O   ASP A 807      24.985  34.751  -0.745  1.00 72.04           O  
ANISOU  316  O   ASP A 807     8206   8127  11037    454   5103   -607       O  
ATOM    317  CB  ASP A 807      26.267  37.346  -1.192  1.00 79.37           C  
ANISOU  317  CB  ASP A 807     8993   9061  12100    252   5352   -278       C  
ATOM    318  CG  ASP A 807      26.517  38.508  -2.115  1.00 84.03           C  
ANISOU  318  CG  ASP A 807     9745   9693  12486    115   5646   -151       C  
ATOM    319  OD1 ASP A 807      25.962  38.485  -3.234  1.00 87.70           O  
ANISOU  319  OD1 ASP A 807    10591  10292  12440     54   5877   -193       O  
ATOM    320  OD2 ASP A 807      27.262  39.442  -1.732  1.00 87.04           O  
ANISOU  320  OD2 ASP A 807     9876   9980  13215     58   5642     -5       O  
ATOM    321  N   SER A 808      24.104  35.806   1.011  1.00 65.19           N  
ANISOU  321  N   SER A 808     7278   7374  10115    475   4318   -338       N  
ATOM    322  CA  SER A 808      24.000  34.595   1.819  1.00 62.93           C  
ANISOU  322  CA  SER A 808     6826   7010  10075    602   4137   -395       C  
ATOM    323  C   SER A 808      22.984  33.621   1.236  1.00 61.79           C  
ANISOU  323  C   SER A 808     6980   6906   9591    617   4195   -570       C  
ATOM    324  O   SER A 808      22.146  33.997   0.418  1.00 60.29           O  
ANISOU  324  O   SER A 808     7141   6861   8904    530   4236   -623       O  
ATOM    325  CB  SER A 808      23.610  34.949   3.262  1.00 59.76           C  
ANISOU  325  CB  SER A 808     6301   6666   9738    643   3622   -239       C  
ATOM    326  OG  SER A 808      22.291  35.475   3.346  1.00 56.36           O  
ANISOU  326  OG  SER A 808     6190   6394   8829    599   3364   -212       O  
ATOM    327  N   GLU A 809      23.063  32.363   1.655  1.00 62.12           N  
ANISOU  327  N   GLU A 809     6869   6812   9919    725   4188   -652       N  
ATOM    328  CA  GLU A 809      22.038  31.408   1.278  1.00 61.92           C  
ANISOU  328  CA  GLU A 809     7095   6800   9630    730   4191   -827       C  
ATOM    329  C   GLU A 809      20.752  31.712   2.030  1.00 58.58           C  
ANISOU  329  C   GLU A 809     6838   6528   8889    723   3732   -718       C  
ATOM    330  O   GLU A 809      19.674  31.564   1.466  1.00 57.68           O  
ANISOU  330  O   GLU A 809     7025   6523   8366    661   3694   -833       O  
ATOM    331  CB  GLU A 809      22.472  29.958   1.503  1.00 63.60           C  
ANISOU  331  CB  GLU A 809     7089   6776  10299    847   4345   -940       C  
ATOM    332  CG  GLU A 809      21.612  28.992   0.697  1.00 64.38           C  
ANISOU  332  CG  GLU A 809     7467   6852  10141    806   4508  -1215       C  
ATOM    333  CD  GLU A 809      21.804  27.541   1.070  1.00 66.20           C  
ANISOU  333  CD  GLU A 809     7498   6814  10839    924   4602  -1310       C  
ATOM    334  OE1 GLU A 809      20.900  26.974   1.721  1.00 64.61           O  
ANISOU  334  OE1 GLU A 809     7345   6597  10604    958   4321  -1270       O  
ATOM    335  OE2 GLU A 809      22.845  26.962   0.701  1.00 69.49           O  
ANISOU  335  OE2 GLU A 809     7700   7017  11685    986   4980  -1419       O  
ATOM    336  N   GLU A 810      20.878  32.126   3.294  1.00 57.85           N  
ANISOU  336  N   GLU A 810     6541   6449   8987    780   3392   -510       N  
ATOM    337  CA  GLU A 810      19.753  32.656   4.084  1.00 56.17           C  
ANISOU  337  CA  GLU A 810     6469   6389   8484    766   2985   -397       C  
ATOM    338  C   GLU A 810      18.934  33.676   3.295  1.00 54.15           C  
ANISOU  338  C   GLU A 810     6527   6300   7745    656   2976   -414       C  
ATOM    339  O   GLU A 810      17.706  33.626   3.269  1.00 51.90           O  
ANISOU  339  O   GLU A 810     6459   6119   7140    635   2795   -439       O  
ATOM    340  CB  GLU A 810      20.269  33.373   5.343  1.00 58.10           C  
ANISOU  340  CB  GLU A 810     6470   6660   8944    797   2696   -199       C  
ATOM    341  CG  GLU A 810      20.383  32.556   6.630  1.00 59.94           C  
ANISOU  341  CG  GLU A 810     6476   6840   9456    906   2445    -83       C  
ATOM    342  CD  GLU A 810      20.698  33.448   7.846  1.00 61.09           C  
ANISOU  342  CD  GLU A 810     6458   7088   9664    896   2110     80       C  
ATOM    343  OE1 GLU A 810      21.715  34.201   7.802  1.00 63.19           O  
ANISOU  343  OE1 GLU A 810     6538   7335  10134    853   2166    109       O  
ATOM    344  OE2 GLU A 810      19.930  33.409   8.842  1.00 58.18           O  
ANISOU  344  OE2 GLU A 810     6146   6822   9138    918   1804    163       O  
ATOM    345  N   ALA A 811      19.641  34.626   2.691  1.00 54.72           N  
ANISOU  345  N   ALA A 811     6598   6387   7804    590   3164   -372       N  
ATOM    346  CA  ALA A 811      19.021  35.682   1.907  1.00 54.43           C  
ANISOU  346  CA  ALA A 811     6836   6488   7355    494   3176   -327       C  
ATOM    347  C   ALA A 811      18.339  35.134   0.665  1.00 55.52           C  
ANISOU  347  C   ALA A 811     7274   6714   7106    440   3358   -485       C  
ATOM    348  O   ALA A 811      17.249  35.563   0.316  1.00 55.13           O  
ANISOU  348  O   ALA A 811     7469   6811   6664    395   3191   -452       O  
ATOM    349  CB  ALA A 811      20.063  36.707   1.508  1.00 56.44           C  
ANISOU  349  CB  ALA A 811     6997   6701   7743    432   3394   -230       C  
ATOM    350  N   GLU A 812      19.001  34.198  -0.003  1.00 57.97           N  
ANISOU  350  N   GLU A 812     7551   6934   7541    440   3700   -666       N  
ATOM    351  CA  GLU A 812      18.443  33.528  -1.166  1.00 59.79           C  
ANISOU  351  CA  GLU A 812     8060   7246   7411    371   3892   -883       C  
ATOM    352  C   GLU A 812      17.167  32.751  -0.843  1.00 57.65           C  
ANISOU  352  C   GLU A 812     7901   7020   6981    385   3609   -984       C  
ATOM    353  O   GLU A 812      16.188  32.826  -1.578  1.00 57.85           O  
ANISOU  353  O   GLU A 812     8203   7213   6562    303   3530  -1057       O  
ATOM    354  CB  GLU A 812      19.460  32.561  -1.734  1.00 63.55           C  
ANISOU  354  CB  GLU A 812     8427   7564   8154    382   4331  -1099       C  
ATOM    355  CG  GLU A 812      19.062  32.015  -3.084  1.00 67.52           C  
ANISOU  355  CG  GLU A 812     9243   8169   8240    276   4602  -1366       C  
ATOM    356  CD  GLU A 812      19.232  33.031  -4.185  1.00 70.80           C  
ANISOU  356  CD  GLU A 812     9900   8771   8228    160   4809  -1291       C  
ATOM    357  OE1 GLU A 812      19.747  34.131  -3.895  1.00 70.73           O  
ANISOU  357  OE1 GLU A 812     9782   8760   8329    168   4782  -1033       O  
ATOM    358  OE2 GLU A 812      18.878  32.715  -5.346  1.00 75.17           O  
ANISOU  358  OE2 GLU A 812    10754   9469   8338     53   5009  -1491       O  
ATOM    359  N   ILE A 813      17.181  31.991   0.244  1.00 55.66           N  
ANISOU  359  N   ILE A 813     7426   6622   7099    485   3454   -974       N  
ATOM    360  CA  ILE A 813      15.993  31.246   0.651  1.00 53.70           C  
ANISOU  360  CA  ILE A 813     7252   6389   6762    496   3204  -1044       C  
ATOM    361  C   ILE A 813      14.834  32.195   0.901  1.00 50.49           C  
ANISOU  361  C   ILE A 813     6998   6175   6011    462   2855   -893       C  
ATOM    362  O   ILE A 813      13.718  31.948   0.457  1.00 50.08           O  
ANISOU  362  O   ILE A 813     7136   6231   5658    401   2731   -991       O  
ATOM    363  CB  ILE A 813      16.257  30.386   1.898  1.00 52.96           C  
ANISOU  363  CB  ILE A 813     6881   6106   7135    617   3091   -979       C  
ATOM    364  CG1 ILE A 813      17.183  29.231   1.529  1.00 56.24           C  
ANISOU  364  CG1 ILE A 813     7153   6295   7920    661   3443  -1157       C  
ATOM    365  CG2 ILE A 813      14.964  29.797   2.452  1.00 51.30           C  
ANISOU  365  CG2 ILE A 813     6738   5915   6835    621   2819   -992       C  
ATOM    366  CD1 ILE A 813      17.773  28.524   2.724  1.00 56.58           C  
ANISOU  366  CD1 ILE A 813     6870   6135   8491    802   3360  -1013       C  
ATOM    367  N   ILE A 814      15.111  33.293   1.588  1.00 48.46           N  
ANISOU  367  N   ILE A 814     6641   5948   5824    496   2705   -669       N  
ATOM    368  CA  ILE A 814      14.076  34.256   1.920  1.00 46.30           C  
ANISOU  368  CA  ILE A 814     6474   5813   5302    481   2401   -523       C  
ATOM    369  C   ILE A 814      13.535  34.970   0.674  1.00 47.99           C  
ANISOU  369  C   ILE A 814     6958   6193   5082    389   2443   -515       C  
ATOM    370  O   ILE A 814      12.334  35.129   0.527  1.00 48.33           O  
ANISOU  370  O   ILE A 814     7140   6358   4864    366   2222   -498       O  
ATOM    371  CB  ILE A 814      14.588  35.255   2.964  1.00 44.64           C  
ANISOU  371  CB  ILE A 814     6087   5568   5303    528   2262   -328       C  
ATOM    372  CG1 ILE A 814      14.825  34.525   4.292  1.00 43.35           C  
ANISOU  372  CG1 ILE A 814     5694   5307   5469    615   2123   -304       C  
ATOM    373  CG2 ILE A 814      13.593  36.389   3.143  1.00 43.32           C  
ANISOU  373  CG2 ILE A 814     6040   5514   4902    511   2020   -196       C  
ATOM    374  CD1 ILE A 814      15.747  35.236   5.255  1.00 43.18           C  
ANISOU  374  CD1 ILE A 814     5453   5243   5710    645   2041   -171       C  
ATOM    375  N   ARG A 815      14.408  35.385  -0.229  1.00 50.35           N  
ANISOU  375  N   ARG A 815     7320   6502   5305    337   2728   -510       N  
ATOM    376  CA  ARG A 815      13.961  36.027  -1.462  1.00 52.42           C  
ANISOU  376  CA  ARG A 815     7857   6942   5117    247   2781   -465       C  
ATOM    377  C   ARG A 815      13.123  35.093  -2.320  1.00 54.55           C  
ANISOU  377  C   ARG A 815     8337   7340   5050    176   2772   -686       C  
ATOM    378  O   ARG A 815      12.206  35.525  -3.007  1.00 55.73           O  
ANISOU  378  O   ARG A 815     8697   7680   4797    116   2613   -627       O  
ATOM    379  CB  ARG A 815      15.150  36.522  -2.278  1.00 54.93           C  
ANISOU  379  CB  ARG A 815     8205   7240   5425    195   3152   -422       C  
ATOM    380  CG  ARG A 815      15.774  37.793  -1.732  1.00 54.21           C  
ANISOU  380  CG  ARG A 815     7968   7064   5564    220   3134   -173       C  
ATOM    381  CD  ARG A 815      16.524  38.537  -2.814  1.00 56.76           C  
ANISOU  381  CD  ARG A 815     8412   7424   5731    138   3463    -64       C  
ATOM    382  NE  ARG A 815      17.595  37.704  -3.327  1.00 59.99           N  
ANISOU  382  NE  ARG A 815     8757   7761   6275    112   3867   -258       N  
ATOM    383  CZ  ARG A 815      18.797  37.564  -2.763  1.00 60.49           C  
ANISOU  383  CZ  ARG A 815     8522   7635   6826    151   4052   -282       C  
ATOM    384  NH1 ARG A 815      19.692  36.773  -3.330  1.00 62.33           N  
ANISOU  384  NH1 ARG A 815     8697   7796   7189    136   4445   -466       N  
ATOM    385  NH2 ARG A 815      19.113  38.208  -1.639  1.00 59.07           N  
ANISOU  385  NH2 ARG A 815     8091   7338   7012    203   3846   -136       N  
ATOM    386  N   LYS A 816      13.452  33.811  -2.291  1.00 56.14           N  
ANISOU  386  N   LYS A 816     8467   7427   5435    178   2938   -941       N  
ATOM    387  CA  LYS A 816      12.690  32.814  -3.027  1.00 58.68           C  
ANISOU  387  CA  LYS A 816     8963   7833   5496     93   2938  -1212       C  
ATOM    388  C   LYS A 816      11.315  32.669  -2.375  1.00 56.15           C  
ANISOU  388  C   LYS A 816     8624   7564   5145    111   2533  -1174       C  
ATOM    389  O   LYS A 816      10.304  32.527  -3.055  1.00 57.05           O  
ANISOU  389  O   LYS A 816     8918   7851   4907     21   2374  -1268       O  
ATOM    390  CB  LYS A 816      13.438  31.481  -3.031  1.00 61.30           C  
ANISOU  390  CB  LYS A 816     9182   7961   6146    105   3242  -1495       C  
ATOM    391  CG  LYS A 816      13.190  30.633  -4.263  1.00 66.98           C  
ANISOU  391  CG  LYS A 816    10136   8765   6548    -27   3446  -1843       C  
ATOM    392  CD  LYS A 816      14.128  29.426  -4.327  1.00 70.41           C  
ANISOU  392  CD  LYS A 816    10441   8946   7366     -4   3835  -2126       C  
ATOM    393  CE  LYS A 816      15.522  29.777  -4.838  1.00 73.04           C  
ANISOU  393  CE  LYS A 816    10735   9223   7793      7   4266  -2115       C  
ATOM    394  NZ  LYS A 816      15.678  29.539  -6.300  1.00 77.97           N  
ANISOU  394  NZ  LYS A 816    11650   9993   7980   -141   4611  -2403       N  
ATOM    395  N   TYR A 817      11.293  32.733  -1.048  1.00 52.93           N  
ANISOU  395  N   TYR A 817     7989   7019   5102    220   2367  -1030       N  
ATOM    396  CA  TYR A 817      10.056  32.621  -0.289  1.00 51.21           C  
ANISOU  396  CA  TYR A 817     7722   6828   4908    247   2031   -977       C  
ATOM    397  C   TYR A 817       9.132  33.765  -0.698  1.00 51.73           C  
ANISOU  397  C   TYR A 817     7928   7098   4627    216   1788   -802       C  
ATOM    398  O   TYR A 817       7.974  33.543  -1.018  1.00 51.81           O  
ANISOU  398  O   TYR A 817     8022   7228   4436    162   1579   -863       O  
ATOM    399  CB  TYR A 817      10.367  32.657   1.216  1.00 48.20           C  
ANISOU  399  CB  TYR A 817     7093   6290   4928    366   1936   -824       C  
ATOM    400  CG  TYR A 817       9.300  32.117   2.159  1.00 46.69           C  
ANISOU  400  CG  TYR A 817     6812   6066   4860    399   1696   -813       C  
ATOM    401  CD1 TYR A 817       8.011  31.800   1.722  1.00 47.54           C  
ANISOU  401  CD1 TYR A 817     7024   6276   4761    326   1529   -913       C  
ATOM    402  CD2 TYR A 817       9.573  31.976   3.520  1.00 44.70           C  
ANISOU  402  CD2 TYR A 817     6362   5697   4923    495   1626   -686       C  
ATOM    403  CE1 TYR A 817       7.047  31.332   2.609  1.00 45.95           C  
ANISOU  403  CE1 TYR A 817     6717   6031   4710    350   1343   -890       C  
ATOM    404  CE2 TYR A 817       8.616  31.516   4.408  1.00 43.27           C  
ANISOU  404  CE2 TYR A 817     6109   5493   4837    520   1444   -650       C  
ATOM    405  CZ  TYR A 817       7.358  31.199   3.944  1.00 43.97           C  
ANISOU  405  CZ  TYR A 817     6289   5657   4758    449   1321   -753       C  
ATOM    406  OH  TYR A 817       6.409  30.743   4.811  1.00 43.02           O  
ANISOU  406  OH  TYR A 817     6079   5502   4762    466   1175   -714       O  
ATOM    407  N   VAL A 818       9.670  34.982  -0.721  1.00 52.92           N  
ANISOU  407  N   VAL A 818     8088   7273   4745    248   1824   -581       N  
ATOM    408  CA  VAL A 818       8.913  36.173  -1.116  1.00 54.14           C  
ANISOU  408  CA  VAL A 818     8359   7579   4632    240   1622   -365       C  
ATOM    409  C   VAL A 818       8.434  36.100  -2.561  1.00 59.06           C  
ANISOU  409  C   VAL A 818     9235   8420   4784    129   1620   -426       C  
ATOM    410  O   VAL A 818       7.263  36.349  -2.858  1.00 60.41           O  
ANISOU  410  O   VAL A 818     9477   8741   4733    107   1341   -357       O  
ATOM    411  CB  VAL A 818       9.760  37.455  -0.976  1.00 53.44           C  
ANISOU  411  CB  VAL A 818     8235   7430   4639    280   1729   -129       C  
ATOM    412  CG1 VAL A 818       9.057  38.644  -1.620  1.00 54.27           C  
ANISOU  412  CG1 VAL A 818     8483   7669   4468    269   1573    113       C  
ATOM    413  CG2 VAL A 818      10.047  37.750   0.489  1.00 51.26           C  
ANISOU  413  CG2 VAL A 818     7724   6988   4765    373   1648    -59       C  
ATOM    414  N   LYS A 819       9.359  35.778  -3.455  1.00 62.89           N  
ANISOU  414  N   LYS A 819     9847   8932   5116     56   1934   -550       N  
ATOM    415  CA  LYS A 819       9.102  35.810  -4.883  1.00 67.85           C  
ANISOU  415  CA  LYS A 819    10752   9799   5228    -64   1978   -600       C  
ATOM    416  C   LYS A 819       7.970  34.835  -5.243  1.00 71.08           C  
ANISOU  416  C   LYS A 819    11239  10340   5427   -151   1759   -848       C  
ATOM    417  O   LYS A 819       6.984  35.211  -5.890  1.00 71.98           O  
ANISOU  417  O   LYS A 819    11491  10682   5173   -208   1488   -759       O  
ATOM    418  CB  LYS A 819      10.409  35.491  -5.619  1.00 70.00           C  
ANISOU  418  CB  LYS A 819    11118  10041   5437   -125   2429   -744       C  
ATOM    419  CG  LYS A 819      10.380  35.621  -7.130  1.00 74.82           C  
ANISOU  419  CG  LYS A 819    12049  10917   5460   -263   2559   -783       C  
ATOM    420  CD  LYS A 819       9.902  34.337  -7.793  1.00 77.87           C  
ANISOU  420  CD  LYS A 819    12577  11416   5592   -387   2573  -1189       C  
ATOM    421  CE  LYS A 819      10.819  33.888  -8.922  1.00 82.40           C  
ANISOU  421  CE  LYS A 819    13363  12069   5874   -506   3023  -1430       C  
ATOM    422  NZ  LYS A 819      11.028  34.950  -9.939  1.00 85.97           N  
ANISOU  422  NZ  LYS A 819    14068  12766   5827   -570   3112  -1162       N  
ATOM    423  N   ASN A 820       8.099  33.598  -4.771  1.00 73.72           N  
ANISOU  423  N   ASN A 820    11457  10513   6040   -157   1858  -1142       N  
ATOM    424  CA  ASN A 820       7.173  32.518  -5.135  1.00 77.74           C  
ANISOU  424  CA  ASN A 820    12024  11097   6417   -265   1715  -1442       C  
ATOM    425  C   ASN A 820       5.773  32.644  -4.520  1.00 77.83           C  
ANISOU  425  C   ASN A 820    11916  11153   6501   -238   1292  -1335       C  
ATOM    426  O   ASN A 820       4.771  32.389  -5.197  1.00 79.37           O  
ANISOU  426  O   ASN A 820    12214  11543   6400   -350   1058  -1448       O  
ATOM    427  CB  ASN A 820       7.788  31.144  -4.795  1.00 78.06           C  
ANISOU  427  CB  ASN A 820    11955  10891   6810   -273   1990  -1772       C  
ATOM    428  CG  ASN A 820       8.948  30.765  -5.722  1.00 80.60           C  
ANISOU  428  CG  ASN A 820    12423  11200   6999   -342   2426  -1992       C  
ATOM    429  OD1 ASN A 820       8.966  31.124  -6.897  1.00 84.41           O  
ANISOU  429  OD1 ASN A 820    13163  11924   6984   -455   2497  -2036       O  
ATOM    430  ND2 ASN A 820       9.911  30.022  -5.195  1.00 79.78           N  
ANISOU  430  ND2 ASN A 820    12150  10817   7343   -273   2728  -2122       N  
ATOM    431  N   THR A 821       5.706  33.047  -3.252  1.00 77.07           N  
ANISOU  431  N   THR A 821    11598  10890   6793    -99   1197  -1126       N  
ATOM    432  CA  THR A 821       4.430  33.125  -2.529  1.00 77.32           C  
ANISOU  432  CA  THR A 821    11485  10929   6963    -61    860  -1035       C  
ATOM    433  C   THR A 821       3.742  34.502  -2.698  1.00 79.69           C  
ANISOU  433  C   THR A 821    11814  11390   7075    -10    597   -712       C  
ATOM    434  O   THR A 821       3.414  35.188  -1.728  1.00 77.61           O  
ANISOU  434  O   THR A 821    11390  11034   7062    104    478   -502       O  
ATOM    435  CB  THR A 821       4.603  32.720  -1.035  1.00 73.40           C  
ANISOU  435  CB  THR A 821    10746  10180   6960     50    905  -1006       C  
ATOM    436  OG1 THR A 821       5.430  33.665  -0.329  1.00 68.71           O  
ANISOU  436  OG1 THR A 821    10078   9497   6529    168    996   -769       O  
ATOM    437  CG2 THR A 821       5.204  31.298  -0.926  1.00 72.85           C  
ANISOU  437  CG2 THR A 821    10634   9930   7114     10   1147  -1290       C  
ATOM    438  N   HIS A 822       3.479  34.867  -3.950  1.00 87.14           N  
ANISOU  438  N   HIS A 822    12962  12576   7570   -101    506   -678       N  
ATOM    439  CA  HIS A 822       3.024  36.214  -4.290  1.00 89.97           C  
ANISOU  439  CA  HIS A 822    13368  13074   7742    -46    300   -325       C  
ATOM    440  C   HIS A 822       2.252  36.237  -5.628  1.00 90.49           C  
ANISOU  440  C   HIS A 822    13628  13458   7295   -170     63   -325       C  
ATOM    441  O   HIS A 822       2.788  35.897  -6.685  1.00 87.87           O  
ANISOU  441  O   HIS A 822    13531  13283   6570   -293    221   -470       O  
ATOM    442  CB  HIS A 822       4.252  37.144  -4.301  1.00 92.76           C  
ANISOU  442  CB  HIS A 822    13784  13338   8119     20    572   -116       C  
ATOM    443  CG  HIS A 822       4.073  38.401  -5.096  1.00 99.89           C  
ANISOU  443  CG  HIS A 822    14825  14398   8728     34    463    227       C  
ATOM    444  ND1 HIS A 822       3.644  39.583  -4.531  1.00100.01           N  
ANISOU  444  ND1 HIS A 822    14715  14324   8958    161    301    552       N  
ATOM    445  CD2 HIS A 822       4.287  38.665  -6.409  1.00104.43           C  
ANISOU  445  CD2 HIS A 822    15657  15202   8817    -59    511    310       C  
ATOM    446  CE1 HIS A 822       3.587  40.517  -5.464  1.00103.10           C  
ANISOU  446  CE1 HIS A 822    15265  14862   9046    153    242    847       C  
ATOM    447  NE2 HIS A 822       3.973  39.986  -6.612  1.00105.61           N  
ANISOU  447  NE2 HIS A 822    15824  15391   8909     18    361    722       N  
ATOM    448  N   HIS A 826      -0.611  37.829 -10.012  1.00116.95           N  
ANISOU  448  N   HIS A 826    17586  18099   8750   -477  -1136    295       N  
ATOM    449  CA  HIS A 826      -1.880  38.257  -9.438  1.00117.69           C  
ANISOU  449  CA  HIS A 826    17392  18159   9163   -369  -1550    509       C  
ATOM    450  C   HIS A 826      -2.143  39.758  -9.709  1.00119.32           C  
ANISOU  450  C   HIS A 826    17596  18424   9315   -222  -1737   1086       C  
ATOM    451  O   HIS A 826      -2.378  40.121 -10.861  1.00123.46           O  
ANISOU  451  O   HIS A 826    18325  19272   9310   -296  -1948   1295       O  
ATOM    452  CB  HIS A 826      -1.953  37.888  -7.942  1.00114.14           C  
ANISOU  452  CB  HIS A 826    16637  17342   9388   -257  -1422    356       C  
ATOM    453  CG  HIS A 826      -3.097  38.529  -7.213  1.00115.52           C  
ANISOU  453  CG  HIS A 826    16506  17426   9961   -112  -1738    613       C  
ATOM    454  ND1 HIS A 826      -4.359  38.645  -7.759  1.00118.90           N  
ANISOU  454  ND1 HIS A 826    16837  18087  10253   -146  -2198    733       N  
ATOM    455  CD2 HIS A 826      -3.162  39.110  -5.990  1.00112.64           C  
ANISOU  455  CD2 HIS A 826    15904  16765  10129     65  -1650    764       C  
ATOM    456  CE1 HIS A 826      -5.152  39.265  -6.903  1.00116.62           C  
ANISOU  456  CE1 HIS A 826    16246  17627  10437     17  -2355    954       C  
ATOM    457  NE2 HIS A 826      -4.451  39.559  -5.823  1.00113.73           N  
ANISOU  457  NE2 HIS A 826    15806  16941  10464    142  -2016    963       N  
ATOM    458  N   ASN A 827      -2.064  40.616  -8.679  1.00115.89           N  
ANISOU  458  N   ASN A 827    16947  17676   9408    -24  -1646   1339       N  
ATOM    459  CA  ASN A 827      -2.589  42.005  -8.719  1.00115.98           C  
ANISOU  459  CA  ASN A 827    16860  17659   9547    140  -1864   1868       C  
ATOM    460  C   ASN A 827      -2.391  42.798  -7.405  1.00109.72           C  
ANISOU  460  C   ASN A 827    15824  16460   9402    337  -1679   2011       C  
ATOM    461  O   ASN A 827      -2.263  42.210  -6.325  1.00105.88           O  
ANISOU  461  O   ASN A 827    15175  15756   9295    357  -1518   1714       O  
ATOM    462  CB  ASN A 827      -4.095  42.012  -9.064  1.00119.19           C  
ANISOU  462  CB  ASN A 827    17094  18279   9912    143  -2400   1997       C  
ATOM    463  CG  ASN A 827      -4.387  42.468 -10.487  1.00125.84           C  
ANISOU  463  CG  ASN A 827    18160  19507  10144     74  -2699   2320       C  
ATOM    464  OD1 ASN A 827      -3.488  42.623 -11.315  1.00128.40           O  
ANISOU  464  OD1 ASN A 827    18810  19980   9993     -8  -2487   2395       O  
ATOM    465  ND2 ASN A 827      -5.663  42.685 -10.776  1.00129.44           N  
ANISOU  465  ND2 ASN A 827    18430  20139  10610    107  -3197   2527       N  
ATOM    466  N   ALA A 828      -2.390  44.132  -7.532  1.00108.44           N  
ANISOU  466  N   ALA A 828    15647  16205   9347    475  -1712   2473       N  
ATOM    467  CA  ALA A 828      -2.309  45.118  -6.421  1.00102.42           C  
ANISOU  467  CA  ALA A 828    14666  15065   9183    661  -1571   2650       C  
ATOM    468  C   ALA A 828      -0.952  45.853  -6.376  1.00100.66           C  
ANISOU  468  C   ALA A 828    14594  14648   9004    679  -1173   2782       C  
ATOM    469  O   ALA A 828      -0.875  47.033  -6.733  1.00102.50           O  
ANISOU  469  O   ALA A 828    14859  14798   9289    769  -1175   3204       O  
ATOM    470  CB  ALA A 828      -2.661  44.510  -5.059  1.00 96.79           C  
ANISOU  470  CB  ALA A 828    13691  14140   8943    703  -1518   2311       C  
ATOM    471  N   TYR A 829       0.102  45.154  -5.945  1.00 97.06           N  
ANISOU  471  N   TYR A 829    14209  14106   8562    595   -836   2437       N  
ATOM    472  CA  TYR A 829       1.468  45.712  -5.844  1.00 93.15           C  
ANISOU  472  CA  TYR A 829    13817  13424   8149    590   -444   2502       C  
ATOM    473  C   TYR A 829       2.534  44.645  -6.112  1.00 89.18           C  
ANISOU  473  C   TYR A 829    13482  13014   7386    441   -152   2153       C  
ATOM    474  O   TYR A 829       2.241  43.454  -6.139  1.00 88.39           O  
ANISOU  474  O   TYR A 829    13392  13056   7136    356   -225   1818       O  
ATOM    475  CB  TYR A 829       1.713  46.345  -4.459  1.00 90.05           C  
ANISOU  475  CB  TYR A 829    13191  12660   8364    710   -299   2473       C  
ATOM    476  CG  TYR A 829       1.280  45.487  -3.278  1.00 86.57           C  
ANISOU  476  CG  TYR A 829    12546  12136   8208    729   -349   2109       C  
ATOM    477  CD1 TYR A 829       1.941  44.296  -2.966  1.00 84.20           C  
ANISOU  477  CD1 TYR A 829    12281  11870   7838    630   -176   1735       C  
ATOM    478  CD2 TYR A 829       0.212  45.875  -2.468  1.00 85.48           C  
ANISOU  478  CD2 TYR A 829    12174  11872   8431    851   -547   2159       C  
ATOM    479  CE1 TYR A 829       1.540  43.516  -1.892  1.00 81.73           C  
ANISOU  479  CE1 TYR A 829    11793  11480   7781    649   -216   1456       C  
ATOM    480  CE2 TYR A 829      -0.192  45.104  -1.393  1.00 82.35           C  
ANISOU  480  CE2 TYR A 829    11606  11412   8270    860   -563   1855       C  
ATOM    481  CZ  TYR A 829       0.472  43.929  -1.107  1.00 81.15           C  
ANISOU  481  CZ  TYR A 829    11508  11305   8018    758   -405   1521       C  
ATOM    482  OH  TYR A 829       0.063  43.166  -0.037  1.00 79.52           O  
ANISOU  482  OH  TYR A 829    11138  11031   8042    769   -416   1267       O  
ATOM    483  N   ASP A 830       3.775  45.088  -6.284  1.00 86.61           N  
ANISOU  483  N   ASP A 830    13264  12578   7066    412    196   2229       N  
ATOM    484  CA  ASP A 830       4.904  44.198  -6.532  1.00 83.42           C  
ANISOU  484  CA  ASP A 830    12986  12218   6492    290    528   1926       C  
ATOM    485  C   ASP A 830       5.846  44.286  -5.330  1.00 77.51           C  
ANISOU  485  C   ASP A 830    12044  11151   6252    340    788   1775       C  
ATOM    486  O   ASP A 830       6.257  45.383  -4.937  1.00 76.84           O  
ANISOU  486  O   ASP A 830    11878  10852   6465    406    889   2004       O  
ATOM    487  CB  ASP A 830       5.629  44.641  -7.806  1.00 88.34           C  
ANISOU  487  CB  ASP A 830    13883  12995   6684    202    746   2153       C  
ATOM    488  CG  ASP A 830       5.799  43.521  -8.813  1.00 91.46           C  
ANISOU  488  CG  ASP A 830    14519  13694   6538     44    830   1882       C  
ATOM    489  OD1 ASP A 830       6.070  42.378  -8.388  1.00 90.44           O  
ANISOU  489  OD1 ASP A 830    14325  13527   6508     -5    939   1459       O  
ATOM    490  OD2 ASP A 830       5.668  43.792 -10.032  1.00 94.59           O  
ANISOU  490  OD2 ASP A 830    15173  14363   6404    -32    794   2095       O  
ATOM    491  N   LEU A 831       6.176  43.146  -4.733  1.00 72.23           N  
ANISOU  491  N   LEU A 831    11294  10447   5703    304    882   1397       N  
ATOM    492  CA  LEU A 831       7.067  43.140  -3.578  1.00 67.29           C  
ANISOU  492  CA  LEU A 831    10476   9560   5528    346   1083   1259       C  
ATOM    493  C   LEU A 831       8.509  42.960  -4.013  1.00 66.69           C  
ANISOU  493  C   LEU A 831    10476   9445   5415    267   1469   1186       C  
ATOM    494  O   LEU A 831       8.807  42.159  -4.885  1.00 67.51           O  
ANISOU  494  O   LEU A 831    10743   9712   5194    173   1613   1032       O  
ATOM    495  CB  LEU A 831       6.688  42.046  -2.588  1.00 64.32           C  
ANISOU  495  CB  LEU A 831     9942   9141   5355    367    977    948       C  
ATOM    496  CG  LEU A 831       5.379  42.261  -1.832  1.00 63.78           C  
ANISOU  496  CG  LEU A 831     9729   9047   5457    456    658    997       C  
ATOM    497  CD1 LEU A 831       5.027  41.003  -1.053  1.00 62.29           C  
ANISOU  497  CD1 LEU A 831     9422   8848   5397    448    597    696       C  
ATOM    498  CD2 LEU A 831       5.454  43.463  -0.900  1.00 62.13           C  
ANISOU  498  CD2 LEU A 831     9369   8618   5620    556    654   1172       C  
ATOM    499  N   GLU A 832       9.396  43.699  -3.361  1.00 65.21           N  
ANISOU  499  N   GLU A 832    10152   9032   5593    299   1642   1269       N  
ATOM    500  CA  GLU A 832      10.804  43.728  -3.689  1.00 65.80           C  
ANISOU  500  CA  GLU A 832    10238   9030   5733    232   2017   1243       C  
ATOM    501  C   GLU A 832      11.524  43.898  -2.357  1.00 61.35           C  
ANISOU  501  C   GLU A 832     9403   8218   5687    277   2067   1139       C  
ATOM    502  O   GLU A 832      11.192  44.807  -1.595  1.00 59.68           O  
ANISOU  502  O   GLU A 832     9075   7865   5736    337   1918   1265       O  
ATOM    503  CB  GLU A 832      11.048  44.910  -4.626  1.00 71.27           C  
ANISOU  503  CB  GLU A 832    11081   9733   6262    199   2150   1599       C  
ATOM    504  CG  GLU A 832      12.301  44.836  -5.485  1.00 76.70           C  
ANISOU  504  CG  GLU A 832    11875  10442   6825     97   2572   1605       C  
ATOM    505  CD  GLU A 832      13.427  45.733  -4.985  1.00 78.43           C  
ANISOU  505  CD  GLU A 832    11912  10388   7497     90   2817   1721       C  
ATOM    506  OE1 GLU A 832      13.614  45.833  -3.744  1.00 75.71           O  
ANISOU  506  OE1 GLU A 832    11316   9847   7603    143   2715   1599       O  
ATOM    507  OE2 GLU A 832      14.130  46.326  -5.843  1.00 81.85           O  
ANISOU  507  OE2 GLU A 832    12458  10815   7824     18   3116   1931       O  
ATOM    508  N   VAL A 833      12.467  43.011  -2.048  1.00 58.53           N  
ANISOU  508  N   VAL A 833     8938   7811   5489    249   2262    902       N  
ATOM    509  CA  VAL A 833      13.156  43.062  -0.757  1.00 55.42           C  
ANISOU  509  CA  VAL A 833     8277   7223   5555    286   2260    802       C  
ATOM    510  C   VAL A 833      14.280  44.082  -0.775  1.00 56.45           C  
ANISOU  510  C   VAL A 833     8310   7189   5947    241   2487    943       C  
ATOM    511  O   VAL A 833      15.047  44.123  -1.707  1.00 59.55           O  
ANISOU  511  O   VAL A 833     8784   7601   6241    172   2784    999       O  
ATOM    512  CB  VAL A 833      13.737  41.696  -0.352  1.00 54.42           C  
ANISOU  512  CB  VAL A 833     8030   7090   5554    290   2349    531       C  
ATOM    513  CG1 VAL A 833      14.464  41.802   0.983  1.00 52.24           C  
ANISOU  513  CG1 VAL A 833     7476   6650   5722    326   2302    472       C  
ATOM    514  CG2 VAL A 833      12.632  40.654  -0.260  1.00 53.61           C  
ANISOU  514  CG2 VAL A 833     8001   7111   5256    322   2137    380       C  
ATOM    515  N   ILE A 834      14.370  44.902   0.265  1.00 55.93           N  
ANISOU  515  N   ILE A 834     8069   6959   6221    266   2362    982       N  
ATOM    516  CA  ILE A 834      15.393  45.944   0.356  1.00 57.65           C  
ANISOU  516  CA  ILE A 834     8162   6988   6753    206   2550   1094       C  
ATOM    517  C   ILE A 834      16.460  45.537   1.354  1.00 57.40           C  
ANISOU  517  C   ILE A 834     7854   6855   7101    187   2586    898       C  
ATOM    518  O   ILE A 834      17.642  45.605   1.054  1.00 59.01           O  
ANISOU  518  O   ILE A 834     7942   6976   7500    120   2849    900       O  
ATOM    519  CB  ILE A 834      14.790  47.273   0.833  1.00 57.37           C  
ANISOU  519  CB  ILE A 834     8108   6808   6880    229   2388   1254       C  
ATOM    520  CG1 ILE A 834      13.757  47.780  -0.164  1.00 59.34           C  
ANISOU  520  CG1 ILE A 834     8598   7142   6804    263   2331   1512       C  
ATOM    521  CG2 ILE A 834      15.871  48.320   1.025  1.00 58.73           C  
ANISOU  521  CG2 ILE A 834     8123   6750   7439    147   2579   1329       C  
ATOM    522  CD1 ILE A 834      12.797  48.776   0.451  1.00 59.40           C  
ANISOU  522  CD1 ILE A 834     8573   7022   6974    333   2102   1622       C  
ATOM    523  N   ASP A 835      16.024  45.148   2.552  1.00 56.11           N  
ANISOU  523  N   ASP A 835     7574   6702   7041    244   2315    747       N  
ATOM    524  CA  ASP A 835      16.914  44.693   3.623  1.00 56.00           C  
ANISOU  524  CA  ASP A 835     7298   6633   7345    237   2268    583       C  
ATOM    525  C   ASP A 835      16.287  43.509   4.343  1.00 51.38           C  
ANISOU  525  C   ASP A 835     6701   6167   6652    318   2054    439       C  
ATOM    526  O   ASP A 835      15.067  43.472   4.551  1.00 48.57           O  
ANISOU  526  O   ASP A 835     6475   5886   6093    371   1861    445       O  
ATOM    527  CB  ASP A 835      17.125  45.788   4.678  1.00 59.22           C  
ANISOU  527  CB  ASP A 835     7546   6903   8050    197   2125    567       C  
ATOM    528  CG  ASP A 835      17.823  47.020   4.135  1.00 64.00           C  
ANISOU  528  CG  ASP A 835     8116   7335   8866    103   2336    703       C  
ATOM    529  OD1 ASP A 835      17.253  48.125   4.299  1.00 67.37           O  
ANISOU  529  OD1 ASP A 835     8600   7651   9344     92   2260    786       O  
ATOM    530  OD2 ASP A 835      18.932  46.892   3.555  1.00 68.50           O  
ANISOU  530  OD2 ASP A 835     8586   7855   9583     39   2597    731       O  
ATOM    531  N   ILE A 836      17.139  42.572   4.747  1.00 49.55           N  
ANISOU  531  N   ILE A 836     6290   5934   6602    330   2097    331       N  
ATOM    532  CA  ILE A 836      16.737  41.424   5.548  1.00 46.77           C  
ANISOU  532  CA  ILE A 836     5886   5659   6226    406   1913    227       C  
ATOM    533  C   ILE A 836      17.513  41.472   6.851  1.00 45.82           C  
ANISOU  533  C   ILE A 836     5502   5498   6406    402   1756    183       C  
ATOM    534  O   ILE A 836      18.743  41.443   6.838  1.00 47.15           O  
ANISOU  534  O   ILE A 836     5464   5594   6855    368   1879    178       O  
ATOM    535  CB  ILE A 836      17.040  40.097   4.827  1.00 47.15           C  
ANISOU  535  CB  ILE A 836     5951   5729   6232    437   2103    154       C  
ATOM    536  CG1 ILE A 836      16.379  40.070   3.446  1.00 47.79           C  
ANISOU  536  CG1 ILE A 836     6306   5883   5967    410   2262    171       C  
ATOM    537  CG2 ILE A 836      16.562  38.923   5.663  1.00 45.64           C  
ANISOU  537  CG2 ILE A 836     5705   5581   6053    516   1920     79       C  
ATOM    538  CD1 ILE A 836      16.757  38.871   2.605  1.00 49.20           C  
ANISOU  538  CD1 ILE A 836     6523   6072   6095    412   2507     48       C  
ATOM    539  N   PHE A 837      16.797  41.549   7.967  1.00 43.73           N  
ANISOU  539  N   PHE A 837     5239   5296   6079    431   1486    151       N  
ATOM    540  CA  PHE A 837      17.419  41.584   9.285  1.00 44.30           C  
ANISOU  540  CA  PHE A 837     5095   5384   6351    417   1289    106       C  
ATOM    541  C   PHE A 837      17.170  40.289  10.036  1.00 44.34           C  
ANISOU  541  C   PHE A 837     5051   5483   6311    502   1142    100       C  
ATOM    542  O   PHE A 837      16.041  39.800  10.103  1.00 43.41           O  
ANISOU  542  O   PHE A 837     5094   5430   5969    555   1077     99       O  
ATOM    543  CB  PHE A 837      16.870  42.737  10.122  1.00 44.01           C  
ANISOU  543  CB  PHE A 837     5099   5354   6268    368   1109     59       C  
ATOM    544  CG  PHE A 837      16.990  44.077   9.460  1.00 45.52           C  
ANISOU  544  CG  PHE A 837     5340   5412   6542    291   1247     86       C  
ATOM    545  CD1 PHE A 837      18.182  44.778   9.509  1.00 47.51           C  
ANISOU  545  CD1 PHE A 837     5402   5556   7093    192   1318     67       C  
ATOM    546  CD2 PHE A 837      15.915  44.624   8.772  1.00 45.14           C  
ANISOU  546  CD2 PHE A 837     5511   5337   6303    317   1304    154       C  
ATOM    547  CE1 PHE A 837      18.298  46.005   8.897  1.00 49.23           C  
ANISOU  547  CE1 PHE A 837     5661   5619   7423    116   1470    117       C  
ATOM    548  CE2 PHE A 837      16.025  45.844   8.142  1.00 46.63           C  
ANISOU  548  CE2 PHE A 837     5744   5382   6590    257   1438    231       C  
ATOM    549  CZ  PHE A 837      17.215  46.542   8.212  1.00 48.77           C  
ANISOU  549  CZ  PHE A 837     5838   5524   7165    154   1534    213       C  
ATOM    550  N   LYS A 838      18.226  39.741  10.618  1.00 46.15           N  
ANISOU  550  N   LYS A 838     5039   5710   6784    514   1084    116       N  
ATOM    551  CA  LYS A 838      18.086  38.640  11.553  1.00 46.32           C  
ANISOU  551  CA  LYS A 838     4986   5813   6799    593    904    161       C  
ATOM    552  C   LYS A 838      17.882  39.225  12.948  1.00 46.25           C  
ANISOU  552  C   LYS A 838     4945   5929   6697    552    610    141       C  
ATOM    553  O   LYS A 838      18.674  40.048  13.398  1.00 48.36           O  
ANISOU  553  O   LYS A 838     5065   6201   7109    468    517     96       O  
ATOM    554  CB  LYS A 838      19.327  37.755  11.505  1.00 48.61           C  
ANISOU  554  CB  LYS A 838     5012   6036   7420    641    971    221       C  
ATOM    555  CG  LYS A 838      19.133  36.415  12.177  1.00 49.37           C  
ANISOU  555  CG  LYS A 838     5049   6167   7542    749    852    316       C  
ATOM    556  CD  LYS A 838      20.319  35.495  11.937  1.00 52.34           C  
ANISOU  556  CD  LYS A 838     5153   6424   8307    820    969    385       C  
ATOM    557  CE  LYS A 838      19.908  34.036  12.087  1.00 53.18           C  
ANISOU  557  CE  LYS A 838     5268   6478   8457    940    986    469       C  
ATOM    558  NZ  LYS A 838      21.065  33.139  11.837  1.00 56.05           N  
ANISOU  558  NZ  LYS A 838     5346   6686   9264   1027   1125    536       N  
ATOM    559  N   ILE A 839      16.817  38.808  13.624  1.00 44.96           N  
ANISOU  559  N   ILE A 839     4921   5868   6291    597    480    157       N  
ATOM    560  CA  ILE A 839      16.498  39.334  14.945  1.00 45.27           C  
ANISOU  560  CA  ILE A 839     4975   6050   6175    553    239    115       C  
ATOM    561  C   ILE A 839      16.471  38.253  16.012  1.00 46.64           C  
ANISOU  561  C   ILE A 839     5085   6355   6279    617     55    236       C  
ATOM    562  O   ILE A 839      16.028  37.141  15.757  1.00 46.57           O  
ANISOU  562  O   ILE A 839     5119   6314   6260    707    130    337       O  
ATOM    563  CB  ILE A 839      15.152  40.087  14.951  1.00 43.42           C  
ANISOU  563  CB  ILE A 839     4974   5830   5693    534    264     24       C  
ATOM    564  CG1 ILE A 839      13.999  39.172  14.543  1.00 41.14           C  
ANISOU  564  CG1 ILE A 839     4836   5543   5251    621    347     87       C  
ATOM    565  CG2 ILE A 839      15.227  41.300  14.024  1.00 43.28           C  
ANISOU  565  CG2 ILE A 839     5006   5677   5762    471    414    -51       C  
ATOM    566  CD1 ILE A 839      12.647  39.818  14.698  1.00 39.99           C  
ANISOU  566  CD1 ILE A 839     4867   5423   4902    616    346     17       C  
ATOM    567  N   GLU A 840      16.970  38.591  17.198  1.00 49.44           N  
ANISOU  567  N   GLU A 840     5338   6857   6588    560   -187    227       N  
ATOM    568  CA  GLU A 840      16.874  37.746  18.387  1.00 51.28           C  
ANISOU  568  CA  GLU A 840     5543   7265   6675    605   -399    369       C  
ATOM    569  C   GLU A 840      16.316  38.592  19.528  1.00 50.63           C  
ANISOU  569  C   GLU A 840     5590   7372   6275    510   -568    241       C  
ATOM    570  O   GLU A 840      17.048  39.366  20.142  1.00 53.06           O  
ANISOU  570  O   GLU A 840     5796   7773   6589    404   -744    133       O  
ATOM    571  CB  GLU A 840      18.256  37.246  18.805  1.00 56.58           C  
ANISOU  571  CB  GLU A 840     5924   7978   7592    621   -578    509       C  
ATOM    572  CG  GLU A 840      18.860  36.123  17.972  1.00 59.67           C  
ANISOU  572  CG  GLU A 840     6152   8194   8324    740   -423    666       C  
ATOM    573  CD  GLU A 840      19.989  35.410  18.723  1.00 66.31           C  
ANISOU  573  CD  GLU A 840     6700   9107   9388    793   -656    876       C  
ATOM    574  OE1 GLU A 840      21.181  35.570  18.351  1.00 69.68           O  
ANISOU  574  OE1 GLU A 840     6859   9449  10166    781   -652    874       O  
ATOM    575  OE2 GLU A 840      19.686  34.704  19.720  1.00 69.89           O  
ANISOU  575  OE2 GLU A 840     7176   9707   9670    846   -851   1063       O  
ATOM    576  N   ARG A 841      15.030  38.460  19.819  1.00 47.83           N  
ANISOU  576  N   ARG A 841     5447   7068   5655    538   -502    227       N  
ATOM    577  CA  ARG A 841      14.456  39.187  20.942  1.00 47.93           C  
ANISOU  577  CA  ARG A 841     5592   7261   5357    453   -615     88       C  
ATOM    578  C   ARG A 841      14.970  38.586  22.235  1.00 50.44           C  
ANISOU  578  C   ARG A 841     5841   7828   5494    440   -879    229       C  
ATOM    579  O   ARG A 841      15.026  37.370  22.361  1.00 50.55           O  
ANISOU  579  O   ARG A 841     5804   7865   5537    540   -910    487       O  
ATOM    580  CB  ARG A 841      12.939  39.099  20.931  1.00 45.80           C  
ANISOU  580  CB  ARG A 841     5535   6978   4887    497   -450     60       C  
ATOM    581  CG  ARG A 841      12.255  39.684  19.702  1.00 43.68           C  
ANISOU  581  CG  ARG A 841     5344   6496   4753    518   -227    -45       C  
ATOM    582  CD  ARG A 841      10.745  39.804  19.938  1.00 42.85           C  
ANISOU  582  CD  ARG A 841     5412   6409   4458    544   -111   -100       C  
ATOM    583  NE  ARG A 841      10.476  40.382  21.260  1.00 44.82           N  
ANISOU  583  NE  ARG A 841     5738   6836   4454    469   -195   -234       N  
ATOM    584  CZ  ARG A 841       9.991  39.735  22.324  1.00 45.18           C  
ANISOU  584  CZ  ARG A 841     5856   7071   4239    477   -239   -151       C  
ATOM    585  NH1 ARG A 841       9.632  38.457  22.278  1.00 44.34           N  
ANISOU  585  NH1 ARG A 841     5746   6977   4122    561   -207     83       N  
ATOM    586  NH2 ARG A 841       9.846  40.397  23.454  1.00 47.08           N  
ANISOU  586  NH2 ARG A 841     6181   7483   4222    388   -296   -316       N  
ATOM    587  N   GLU A 842      15.328  39.429  23.201  1.00 53.24           N  
ANISOU  587  N   GLU A 842     6200   8367   5661    311  -1073     63       N  
ATOM    588  CA  GLU A 842      15.777  38.942  24.500  1.00 56.98           C  
ANISOU  588  CA  GLU A 842     6635   9134   5879    279  -1363    197       C  
ATOM    589  C   GLU A 842      14.801  37.924  25.066  1.00 55.64           C  
ANISOU  589  C   GLU A 842     6624   9076   5437    370  -1306    418       C  
ATOM    590  O   GLU A 842      13.599  38.175  25.125  1.00 53.10           O  
ANISOU  590  O   GLU A 842     6509   8740   4927    368  -1110    306       O  
ATOM    591  CB  GLU A 842      15.921  40.075  25.506  1.00 61.56           C  
ANISOU  591  CB  GLU A 842     7285   9924   6182    102  -1536    -89       C  
ATOM    592  CG  GLU A 842      17.225  40.837  25.419  1.00 65.77           C  
ANISOU  592  CG  GLU A 842     7591  10441   6956    -18  -1730   -241       C  
ATOM    593  CD  GLU A 842      17.335  41.913  26.492  1.00 71.81           C  
ANISOU  593  CD  GLU A 842     8435  11423   7427   -217  -1915   -567       C  
ATOM    594  OE1 GLU A 842      18.463  42.433  26.706  1.00 76.58           O  
ANISOU  594  OE1 GLU A 842     8834  12083   8177   -345  -2154   -685       O  
ATOM    595  OE2 GLU A 842      16.297  42.232  27.133  1.00 73.65           O  
ANISOU  595  OE2 GLU A 842     8922  11766   7293   -255  -1813   -723       O  
ATOM    596  N   GLY A 843      15.339  36.771  25.453  1.00 56.39           N  
ANISOU  596  N   GLY A 843     6599   9261   5563    454  -1467    752       N  
ATOM    597  CA  GLY A 843      14.612  35.766  26.202  1.00 56.79           C  
ANISOU  597  CA  GLY A 843     6775   9447   5353    524  -1459   1019       C  
ATOM    598  C   GLY A 843      13.656  34.899  25.419  1.00 54.13           C  
ANISOU  598  C   GLY A 843     6507   8873   5186    646  -1164   1148       C  
ATOM    599  O   GLY A 843      13.106  33.953  25.974  1.00 54.64           O  
ANISOU  599  O   GLY A 843     6643   9004   5111    707  -1137   1405       O  
ATOM    600  N   GLU A 844      13.456  35.194  24.137  1.00 51.62           N  
ANISOU  600  N   GLU A 844     6165   8284   5162    673   -949    983       N  
ATOM    601  CA  GLU A 844      12.411  34.518  23.381  1.00 50.53           C  
ANISOU  601  CA  GLU A 844     6112   7946   5138    756   -683   1034       C  
ATOM    602  C   GLU A 844      12.784  33.074  23.055  1.00 50.98           C  
ANISOU  602  C   GLU A 844     6034   7860   5476    878   -661   1337       C  
ATOM    603  O   GLU A 844      11.954  32.174  23.173  1.00 51.19           O  
ANISOU  603  O   GLU A 844     6132   7831   5485    933   -537   1497       O  
ATOM    604  CB  GLU A 844      12.051  35.284  22.105  1.00 48.59           C  
ANISOU  604  CB  GLU A 844     5899   7489   5071    739   -486    777       C  
ATOM    605  CG  GLU A 844      10.590  35.108  21.706  1.00 47.55           C  
ANISOU  605  CG  GLU A 844     5920   7264   4882    765   -264    727       C  
ATOM    606  CD  GLU A 844      10.241  35.768  20.372  1.00 46.90           C  
ANISOU  606  CD  GLU A 844     5862   6987   4969    760   -104    531       C  
ATOM    607  OE1 GLU A 844      10.951  35.537  19.362  1.00 46.06           O  
ANISOU  607  OE1 GLU A 844     5657   6732   5113    790    -64    542       O  
ATOM    608  OE2 GLU A 844       9.235  36.514  20.333  1.00 47.13           O  
ANISOU  608  OE2 GLU A 844     6008   7016   4880    730    -10    377       O  
ATOM    609  N   CYS A 845      14.028  32.855  22.659  1.00 52.19           N  
ANISOU  609  N   CYS A 845     5972   7930   5926    918   -761   1411       N  
ATOM    610  CA  CYS A 845      14.493  31.516  22.355  1.00 53.87           C  
ANISOU  610  CA  CYS A 845     6025   7972   6471   1043   -725   1683       C  
ATOM    611  C   CYS A 845      14.396  30.608  23.575  1.00 55.92           C  
ANISOU  611  C   CYS A 845     6286   8385   6576   1095   -879   2036       C  
ATOM    612  O   CYS A 845      13.991  29.445  23.455  1.00 56.51           O  
ANISOU  612  O   CYS A 845     6350   8297   6824   1188   -748   2254       O  
ATOM    613  CB  CYS A 845      15.921  31.550  21.832  1.00 56.29           C  
ANISOU  613  CB  CYS A 845     6069   8179   7139   1077   -806   1693       C  
ATOM    614  SG  CYS A 845      16.598  29.906  21.515  1.00 61.88           S  
ANISOU  614  SG  CYS A 845     6539   8640   8332   1249   -745   2023       S  
ATOM    615  N   GLN A 846      14.741  31.153  24.741  1.00 57.65           N  
ANISOU  615  N   GLN A 846     6528   8915   6460   1024  -1149   2086       N  
ATOM    616  CA AGLN A 846      14.652  30.417  26.000  0.50 60.87           C  
ANISOU  616  CA AGLN A 846     6971   9536   6620   1056  -1322   2443       C  
ATOM    617  CA BGLN A 846      14.643  30.418  26.013  0.50 61.20           C  
ANISOU  617  CA BGLN A 846     7015   9581   6656   1055  -1323   2444       C  
ATOM    618  C   GLN A 846      13.188  30.106  26.341  1.00 60.29           C  
ANISOU  618  C   GLN A 846     7146   9482   6276   1040  -1102   2473       C  
ATOM    619  O   GLN A 846      12.881  29.043  26.870  1.00 61.82           O  
ANISOU  619  O   GLN A 846     7354   9669   6465   1112  -1079   2822       O  
ATOM    620  CB AGLN A 846      15.331  31.206  27.129  0.50 63.58           C  
ANISOU  620  CB AGLN A 846     7310  10253   6592    949  -1674   2426       C  
ATOM    621  CB BGLN A 846      15.301  31.212  27.155  0.50 64.28           C  
ANISOU  621  CB BGLN A 846     7407  10350   6667    947  -1673   2425       C  
ATOM    622  CG AGLN A 846      16.845  31.385  26.969  0.50 64.91           C  
ANISOU  622  CG AGLN A 846     7178  10428   7057    962  -1942   2460       C  
ATOM    623  CG BGLN A 846      14.893  30.816  28.571  0.50 67.68           C  
ANISOU  623  CG BGLN A 846     7992  11102   6619    923  -1827   2705       C  
ATOM    624  CD AGLN A 846      17.245  32.301  25.811  0.50 61.67           C  
ANISOU  624  CD AGLN A 846     6675   9813   6941    910  -1807   2085       C  
ATOM    625  CD BGLN A 846      15.267  29.393  28.931  0.50 70.53           C  
ANISOU  625  CD BGLN A 846     8212  11409   7176   1072  -1922   3235       C  
ATOM    626  OE1AGLN A 846      16.460  33.132  25.345  0.50 57.62           O  
ANISOU  626  OE1AGLN A 846     6350   9244   6297    829  -1601   1760       O  
ATOM    627  OE1BGLN A 846      16.442  29.047  28.997  0.50 72.71           O  
ANISOU  627  OE1BGLN A 846     8229  11689   7709   1142  -2180   3453       O  
ATOM    628  NE2AGLN A 846      18.474  32.140  25.336  0.50 62.51           N  
ANISOU  628  NE2AGLN A 846     6479   9800   7470    961  -1912   2153       N  
ATOM    629  NE2BGLN A 846      14.262  28.564  29.187  0.50 70.67           N  
ANISOU  629  NE2BGLN A 846     8382  11362   7106   1123  -1710   3460       N  
ATOM    630  N   ARG A 847      12.299  31.043  26.022  1.00 59.01           N  
ANISOU  630  N   ARG A 847     7159   9326   5935    949   -930   2122       N  
ATOM    631  CA  ARG A 847      10.851  30.882  26.184  1.00 59.81           C  
ANISOU  631  CA  ARG A 847     7460   9413   5851    928   -686   2091       C  
ATOM    632  C   ARG A 847      10.270  29.837  25.224  1.00 58.72           C  
ANISOU  632  C   ARG A 847     7269   8942   6097   1018   -439   2184       C  
ATOM    633  O   ARG A 847       9.311  29.140  25.549  1.00 58.09           O  
ANISOU  633  O   ARG A 847     7276   8828   5967   1031   -281   2338       O  
ATOM    634  CB  ARG A 847      10.163  32.234  25.938  1.00 59.25           C  
ANISOU  634  CB  ARG A 847     7530   9388   5592    825   -575   1675       C  
ATOM    635  CG  ARG A 847       8.645  32.252  26.105  1.00 59.65           C  
ANISOU  635  CG  ARG A 847     7753   9430   5478    800   -319   1600       C  
ATOM    636  CD  ARG A 847       8.058  33.640  25.873  1.00 58.67           C  
ANISOU  636  CD  ARG A 847     7731   9327   5231    718   -222   1205       C  
ATOM    637  NE  ARG A 847       7.820  33.914  24.460  1.00 57.22           N  
ANISOU  637  NE  ARG A 847     7483   8870   5386    750    -94   1026       N  
ATOM    638  CZ  ARG A 847       7.360  35.070  23.974  1.00 58.12           C  
ANISOU  638  CZ  ARG A 847     7648   8929   5505    706     -8    726       C  
ATOM    639  NH1 ARG A 847       7.096  36.088  24.791  1.00 58.64           N  
ANISOU  639  NH1 ARG A 847     7821   9161   5296    627    -12    530       N  
ATOM    640  NH2 ARG A 847       7.169  35.217  22.653  1.00 57.59           N  
ANISOU  640  NH2 ARG A 847     7527   8633   5720    741     86    624       N  
ATOM    641  N   TYR A 848      10.851  29.752  24.033  1.00 58.88           N  
ANISOU  641  N   TYR A 848     7149   8720   6502   1064   -393   2069       N  
ATOM    642  CA  TYR A 848      10.396  28.831  22.998  1.00 58.99           C  
ANISOU  642  CA  TYR A 848     7115   8416   6879   1126   -165   2079       C  
ATOM    643  C   TYR A 848      10.753  27.373  23.313  1.00 65.61           C  
ANISOU  643  C   TYR A 848     7829   9113   7983   1231   -166   2460       C  
ATOM    644  O   TYR A 848      10.103  26.465  22.814  1.00 66.32           O  
ANISOU  644  O   TYR A 848     7917   8963   8318   1263     37   2506       O  
ATOM    645  CB  TYR A 848      11.000  29.272  21.664  1.00 55.96           C  
ANISOU  645  CB  TYR A 848     6643   7855   6764   1129   -108   1821       C  
ATOM    646  CG  TYR A 848      10.554  28.521  20.425  1.00 53.88           C  
ANISOU  646  CG  TYR A 848     6359   7292   6820   1162    126   1727       C  
ATOM    647  CD1 TYR A 848       9.301  28.724  19.866  1.00 51.28           C  
ANISOU  647  CD1 TYR A 848     6163   6908   6409   1104    286   1533       C  
ATOM    648  CD2 TYR A 848      11.413  27.644  19.784  1.00 55.26           C  
ANISOU  648  CD2 TYR A 848     6367   7239   7388   1243    184   1808       C  
ATOM    649  CE1 TYR A 848       8.909  28.050  18.722  1.00 49.71           C  
ANISOU  649  CE1 TYR A 848     5950   6467   6470   1110    466   1417       C  
ATOM    650  CE2 TYR A 848      11.028  26.968  18.640  1.00 53.84           C  
ANISOU  650  CE2 TYR A 848     6186   6796   7474   1252    408   1669       C  
ATOM    651  CZ  TYR A 848       9.779  27.180  18.113  1.00 50.91           C  
ANISOU  651  CZ  TYR A 848     5966   6405   6970   1176    532   1468       C  
ATOM    652  OH  TYR A 848       9.426  26.500  16.977  1.00 49.96           O  
ANISOU  652  OH  TYR A 848     5846   6050   7086   1163    722   1308       O  
ATOM    653  N   LYS A 849      11.771  27.159  24.151  1.00 74.42           N  
ANISOU  653  N   LYS A 849     8831  10371   9071   1282   -404   2737       N  
ATOM    654  CA  LYS A 849      12.261  25.807  24.501  1.00 82.25           C  
ANISOU  654  CA  LYS A 849     9670  11218  10363   1405   -437   3158       C  
ATOM    655  C   LYS A 849      11.189  24.742  24.783  1.00 88.69           C  
ANISOU  655  C   LYS A 849    10571  11889  11236   1428   -232   3386       C  
ATOM    656  O   LYS A 849      11.326  23.608  24.309  1.00 93.02           O  
ANISOU  656  O   LYS A 849    10987  12115  12240   1521    -97   3549       O  
ATOM    657  CB  LYS A 849      13.218  25.855  25.698  1.00 85.24           C  
ANISOU  657  CB  LYS A 849     9962  11880  10546   1436   -778   3480       C  
ATOM    658  CG  LYS A 849      14.621  26.279  25.342  1.00 85.29           C  
ANISOU  658  CG  LYS A 849     9738  11890  10778   1469   -981   3410       C  
ATOM    659  CD  LYS A 849      15.491  26.313  26.579  1.00 89.31           C  
ANISOU  659  CD  LYS A 849    10149  12712  11071   1484  -1365   3736       C  
ATOM    660  CE  LYS A 849      16.826  26.966  26.280  1.00 89.61           C  
ANISOU  660  CE  LYS A 849     9948  12797  11302   1479  -1589   3605       C  
ATOM    661  NZ  LYS A 849      17.593  27.201  27.527  1.00 93.88           N  
ANISOU  661  NZ  LYS A 849    10410  13711  11549   1451  -2017   3855       N  
ATOM    662  N   PRO A 850      10.153  25.075  25.592  1.00 92.96           N  
ANISOU  662  N   PRO A 850    11318  12651  11350   1342   -190   3402       N  
ATOM    663  CA  PRO A 850       9.016  24.163  25.730  1.00 93.68           C  
ANISOU  663  CA  PRO A 850    11482  12580  11531   1339     54   3564       C  
ATOM    664  C   PRO A 850       8.554  23.530  24.401  1.00 91.96           C  
ANISOU  664  C   PRO A 850    11188  11957  11794   1352    311   3358       C  
ATOM    665  O   PRO A 850       8.354  22.307  24.342  1.00 91.38           O  
ANISOU  665  O   PRO A 850    11035  11611  12075   1408    454   3596       O  
ATOM    666  CB  PRO A 850       7.928  25.070  26.318  1.00 92.58           C  
ANISOU  666  CB  PRO A 850    11562  12713  10898   1217    123   3383       C  
ATOM    667  CG  PRO A 850       8.673  26.092  27.119  1.00 93.51           C  
ANISOU  667  CG  PRO A 850    11738  13204  10585   1177   -152   3345       C  
ATOM    668  CD  PRO A 850      10.101  26.135  26.619  1.00 94.45           C  
ANISOU  668  CD  PRO A 850    11658  13252  10974   1250   -371   3346       C  
ATOM    669  N   PHE A 851       8.438  24.349  23.351  1.00 87.62           N  
ANISOU  669  N   PHE A 851    10663  11370  11259   1296    360   2926       N  
ATOM    670  CA  PHE A 851       7.862  23.915  22.075  1.00 86.20           C  
ANISOU  670  CA  PHE A 851    10454  10880  11416   1273    582   2670       C  
ATOM    671  C   PHE A 851       8.861  23.594  20.960  1.00 83.42           C  
ANISOU  671  C   PHE A 851     9954  10285  11454   1336    607   2535       C  
ATOM    672  O   PHE A 851       8.452  23.172  19.886  1.00 80.28           O  
ANISOU  672  O   PHE A 851     9546   9643  11313   1307    789   2308       O  
ATOM    673  CB  PHE A 851       6.878  24.976  21.584  1.00 85.75           C  
ANISOU  673  CB  PHE A 851    10535  10942  11103   1165    642   2303       C  
ATOM    674  CG  PHE A 851       5.729  25.209  22.526  1.00 90.30           C  
ANISOU  674  CG  PHE A 851    11236  11696  11375   1100    701   2382       C  
ATOM    675  CD1 PHE A 851       4.562  24.455  22.421  1.00 91.23           C  
ANISOU  675  CD1 PHE A 851    11358  11647  11658   1057    907   2414       C  
ATOM    676  CD2 PHE A 851       5.814  26.172  23.530  1.00 92.62           C  
ANISOU  676  CD2 PHE A 851    11636  12320  11232   1072    570   2407       C  
ATOM    677  CE1 PHE A 851       3.501  24.670  23.289  1.00 92.92           C  
ANISOU  677  CE1 PHE A 851    11667  12018  11618    997   1001   2488       C  
ATOM    678  CE2 PHE A 851       4.754  26.386  24.404  1.00 93.48           C  
ANISOU  678  CE2 PHE A 851    11866  12594  11057   1011    673   2458       C  
ATOM    679  CZ  PHE A 851       3.596  25.637  24.282  1.00 93.09           C  
ANISOU  679  CZ  PHE A 851    11806  12372  11188    979    899   2510       C  
ATOM    680  N   LYS A 852      10.155  23.770  21.210  1.00 85.28           N  
ANISOU  680  N   LYS A 852    10069  10592  11741   1414    432   2663       N  
ATOM    681  CA  LYS A 852      11.175  23.618  20.155  1.00 88.61           C  
ANISOU  681  CA  LYS A 852    10337  10804  12524   1470    483   2508       C  
ATOM    682  C   LYS A 852      11.317  22.201  19.581  1.00 93.44           C  
ANISOU  682  C   LYS A 852    10814  11017  13671   1550    692   2593       C  
ATOM    683  O   LYS A 852      11.778  22.041  18.448  1.00 92.90           O  
ANISOU  683  O   LYS A 852    10674  10738  13884   1561    839   2344       O  
ATOM    684  CB  LYS A 852      12.546  24.101  20.650  1.00 90.05           C  
ANISOU  684  CB  LYS A 852    10372  11149  12690   1535    242   2653       C  
ATOM    685  N   GLN A 853      10.936  21.186  20.364  1.00100.47           N  
ANISOU  685  N   GLN A 853    11673  11794  14705   1599    724   2939       N  
ATOM    686  CA  GLN A 853      10.986  19.774  19.934  1.00101.87           C  
ANISOU  686  CA  GLN A 853    11718  11546  15443   1672    942   3042       C  
ATOM    687  C   GLN A 853       9.581  19.204  19.655  1.00100.29           C  
ANISOU  687  C   GLN A 853    11636  11176  15293   1567   1160   2918       C  
ATOM    688  O   GLN A 853       9.367  17.989  19.680  1.00100.75           O  
ANISOU  688  O   GLN A 853    11606  10902  15770   1605   1328   3086       O  
ATOM    689  CB  GLN A 853      11.705  18.929  20.991  1.00105.72           C  
ANISOU  689  CB  GLN A 853    12036  11964  16168   1820    826   3583       C  
ATOM    690  N   LEU A 854       8.631  20.097  19.387  1.00 96.79           N  
ANISOU  690  N   LEU A 854    11368  10944  14461   1434   1154   2627       N  
ATOM    691  CA  LEU A 854       7.276  19.719  19.003  1.00 95.25           C  
ANISOU  691  CA  LEU A 854    11259  10621  14309   1316   1332   2451       C  
ATOM    692  C   LEU A 854       7.235  19.704  17.477  1.00 90.31           C  
ANISOU  692  C   LEU A 854    10638   9812  13860   1249   1467   1989       C  
ATOM    693  O   LEU A 854       7.543  20.718  16.848  1.00 88.03           O  
ANISOU  693  O   LEU A 854    10416   9709  13322   1220   1386   1726       O  
ATOM    694  CB  LEU A 854       6.271  20.747  19.556  1.00 94.92           C  
ANISOU  694  CB  LEU A 854    11379  10920  13766   1220   1243   2397       C  
ATOM    695  CG  LEU A 854       4.764  20.493  19.413  1.00 95.55           C  
ANISOU  695  CG  LEU A 854    11518  10929  13854   1097   1394   2273       C  
ATOM    696  CD1 LEU A 854       4.344  19.243  20.181  1.00 98.62           C  
ANISOU  696  CD1 LEU A 854    11839  11099  14532   1113   1537   2632       C  
ATOM    697  CD2 LEU A 854       3.968  21.712  19.877  1.00 93.02           C  
ANISOU  697  CD2 LEU A 854    11330  10955  13056   1027   1306   2182       C  
ATOM    698  N  AHIS A 855       6.864  18.554  16.910  0.50 88.54           N  
ANISOU  698  N  AHIS A 855    10350   9228  14061   1216   1677   1896       N  
ATOM    699  N  BHIS A 855       6.864  18.573  16.878  0.50 88.81           N  
ANISOU  699  N  BHIS A 855    10387   9265  14091   1214   1677   1884       N  
ATOM    700  CA AHIS A 855       6.613  18.366  15.473  0.50 83.96           C  
ANISOU  700  CA AHIS A 855     9799   8471  13628   1116   1824   1430       C  
ATOM    701  CA BHIS A 855       6.873  18.464  15.420  0.50 84.01           C  
ANISOU  701  CA BHIS A 855     9798   8493  13627   1136   1811   1426       C  
ATOM    702  C  AHIS A 855       5.883  19.532  14.781  0.50 78.90           C  
ANISOU  702  C  AHIS A 855     9315   8117  12546    990   1727   1086       C  
ATOM    703  C  BHIS A 855       5.915  19.486  14.772  0.50 79.31           C  
ANISOU  703  C  BHIS A 855     9362   8155  12616    993   1733   1089       C  
ATOM    704  O  AHIS A 855       5.167  20.306  15.434  0.50 76.56           O  
ANISOU  704  O  AHIS A 855     9095   8085  11907    956   1598   1182       O  
ATOM    705  O  BHIS A 855       5.084  20.107  15.446  0.50 77.87           O  
ANISOU  705  O  BHIS A 855     9249   8204  12132    951   1623   1193       O  
ATOM    706  CB AHIS A 855       5.772  17.100  15.326  0.50 84.75           C  
ANISOU  706  CB AHIS A 855     9843   8219  14136   1040   2025   1399       C  
ATOM    707  CB BHIS A 855       6.536  17.039  14.971  0.50 85.46           C  
ANISOU  707  CB BHIS A 855     9892   8239  14337   1098   2053   1343       C  
ATOM    708  CG AHIS A 855       4.994  16.767  16.561  0.50 84.20           C  
ANISOU  708  CG AHIS A 855     9758   8174  14057   1038   2011   1784       C  
ATOM    709  CG BHIS A 855       7.385  16.549  13.838  0.50 84.83           C  
ANISOU  709  CG BHIS A 855     9752   7897  14579   1119   2226   1041       C  
ATOM    710  ND1AHIS A 855       5.482  15.933  17.545  0.50 86.60           N  
ANISOU  710  ND1AHIS A 855     9952   8305  14647   1161   2051   2248       N  
ATOM    711  ND1BHIS A 855       8.329  17.340  13.219  0.50 82.41           N  
ANISOU  711  ND1BHIS A 855     9471   7749  14088   1162   2182    868       N  
ATOM    712  CD2AHIS A 855       3.780  17.184  16.990  0.50 81.99           C  
ANISOU  712  CD2AHIS A 855     9557   8082  13511    933   1971   1795       C  
ATOM    713  CD2BHIS A 855       7.413  15.359  13.196  0.50 86.65           C  
ANISOU  713  CD2BHIS A 855     9901   7708  15313   1092   2475    857       C  
ATOM    714  CE1AHIS A 855       4.594  15.836  18.518  0.50 86.63           C  
ANISOU  714  CE1AHIS A 855     9991   8399  14525   1121   2052   2530       C  
ATOM    715  CE1BHIS A 855       8.911  16.655  12.253  0.50 83.85           C  
ANISOU  715  CE1BHIS A 855     9594   7638  14624   1166   2409    597       C  
ATOM    716  NE2AHIS A 855       3.552  16.584  18.206  0.50 84.15           N  
ANISOU  716  NE2AHIS A 855     9784   8297  13891    981   2018   2247       N  
ATOM    717  NE2BHIS A 855       8.373  15.449  12.217  0.50 86.88           N  
ANISOU  717  NE2BHIS A 855     9916   7665  15428   1124   2588    568       N  
ATOM    718  N   ASN A 856       6.064  19.655  13.462  1.00 75.76           N  
ANISOU  718  N   ASN A 856     8963   7662  12157    925   1800    696       N  
ATOM    719  CA  ASN A 856       5.331  20.655  12.672  1.00 68.89           C  
ANISOU  719  CA  ASN A 856     8235   7035  10903    806   1706    391       C  
ATOM    720  C   ASN A 856       5.675  22.113  13.025  1.00 62.42           C  
ANISOU  720  C   ASN A 856     7491   6562   9662    853   1516    474       C  
ATOM    721  O   ASN A 856       4.809  22.886  13.431  1.00 61.84           O  
ANISOU  721  O   ASN A 856     7484   6704   9307    809   1396    505       O  
ATOM    722  CB  ASN A 856       3.812  20.409  12.757  1.00 68.65           C  
ANISOU  722  CB  ASN A 856     8224   7000  10858    678   1697    325       C  
ATOM    723  CG  ASN A 856       3.037  21.166  11.700  1.00 68.30           C  
ANISOU  723  CG  ASN A 856     8288   7136  10527    551   1607    -16       C  
ATOM    724  OD1 ASN A 856       3.550  21.450  10.626  1.00 69.30           O  
ANISOU  724  OD1 ASN A 856     8489   7293  10548    523   1621   -272       O  
ATOM    725  ND2 ASN A 856       1.796  21.511  12.009  1.00 68.82           N  
ANISOU  725  ND2 ASN A 856     8356   7328  10464    475   1517     -1       N  
ATOM    726  N   ARG A 857       6.938  22.488  12.850  1.00 57.71           N  
ANISOU  726  N   ARG A 857     6868   5997   9062    938   1509    493       N  
ATOM    727  CA  ARG A 857       7.364  23.871  13.048  1.00 53.68           C  
ANISOU  727  CA  ARG A 857     6416   5773   8204    963   1349    525       C  
ATOM    728  C   ARG A 857       7.646  24.491  11.694  1.00 50.66           C  
ANISOU  728  C   ARG A 857     6125   5440   7683    903   1399    215       C  
ATOM    729  O   ARG A 857       8.325  23.890  10.879  1.00 51.30           O  
ANISOU  729  O   ARG A 857     6172   5344   7975    909   1564     65       O  
ATOM    730  CB  ARG A 857       8.608  23.939  13.905  1.00 55.59           C  
ANISOU  730  CB  ARG A 857     6540   6040   8540   1087   1281    794       C  
ATOM    731  CG  ARG A 857       8.724  22.777  14.864  1.00 58.97           C  
ANISOU  731  CG  ARG A 857     6843   6293   9270   1168   1310   1104       C  
ATOM    732  CD  ARG A 857       9.476  23.150  16.122  1.00 60.26           C  
ANISOU  732  CD  ARG A 857     6930   6630   9334   1263   1123   1443       C  
ATOM    733  NE  ARG A 857      10.763  23.765  15.843  1.00 60.61           N  
ANISOU  733  NE  ARG A 857     6891   6739   9398   1316   1059   1404       N  
ATOM    734  CZ  ARG A 857      11.840  23.108  15.426  1.00 63.00           C  
ANISOU  734  CZ  ARG A 857     7028   6825  10084   1403   1163   1429       C  
ATOM    735  NH1 ARG A 857      11.799  21.796  15.211  1.00 65.01           N  
ANISOU  735  NH1 ARG A 857     7191   6759  10748   1451   1344   1479       N  
ATOM    736  NH2 ARG A 857      12.968  23.781  15.218  1.00 63.16           N  
ANISOU  736  NH2 ARG A 857     6954   6926  10116   1439   1105   1394       N  
ATOM    737  N   ARG A 858       7.116  25.690  11.461  1.00 46.92           N  
ANISOU  737  N   ARG A 858     5767   5200   6861    848   1276    130       N  
ATOM    738  CA  ARG A 858       7.174  26.321  10.154  1.00 45.48           C  
ANISOU  738  CA  ARG A 858     5698   5090   6493    779   1311   -123       C  
ATOM    739  C   ARG A 858       7.630  27.755  10.238  1.00 43.25           C  
ANISOU  739  C   ARG A 858     5463   5013   5956    801   1200    -70       C  
ATOM    740  O   ARG A 858       7.313  28.471  11.200  1.00 41.40           O  
ANISOU  740  O   ARG A 858     5222   4915   5591    827   1058     81       O  
ATOM    741  CB  ARG A 858       5.801  26.306   9.497  1.00 45.97           C  
ANISOU  741  CB  ARG A 858     5856   5202   6407    665   1265   -304       C  
ATOM    742  CG  ARG A 858       5.220  24.923   9.407  1.00 48.47           C  
ANISOU  742  CG  ARG A 858     6118   5302   6995    612   1369   -390       C  
ATOM    743  CD  ARG A 858       4.086  24.848   8.422  1.00 49.69           C  
ANISOU  743  CD  ARG A 858     6356   5503   7021    472   1325   -647       C  
ATOM    744  NE  ARG A 858       3.419  23.562   8.550  1.00 52.34           N  
ANISOU  744  NE  ARG A 858     6611   5619   7657    406   1409   -715       N  
ATOM    745  CZ  ARG A 858       2.318  23.217   7.896  1.00 54.69           C  
ANISOU  745  CZ  ARG A 858     6926   5912   7939    266   1361   -934       C  
ATOM    746  NH1 ARG A 858       1.744  24.062   7.046  1.00 55.06           N  
ANISOU  746  NH1 ARG A 858     7075   6187   7658    188   1207  -1083       N  
ATOM    747  NH2 ARG A 858       1.787  22.015   8.091  1.00 57.45           N  
ANISOU  747  NH2 ARG A 858     7180   6024   8623    200   1458   -990       N  
ATOM    748  N   LEU A 859       8.344  28.170   9.195  1.00 42.41           N  
ANISOU  748  N   LEU A 859     5412   4918   5784    779   1292   -212       N  
ATOM    749  CA  LEU A 859       8.758  29.553   9.036  1.00 40.95           C  
ANISOU  749  CA  LEU A 859     5280   4894   5384    779   1222   -185       C  
ATOM    750  C   LEU A 859       7.643  30.278   8.287  1.00 39.69           C  
ANISOU  750  C   LEU A 859     5271   4868   4939    700   1139   -291       C  
ATOM    751  O   LEU A 859       7.411  30.004   7.108  1.00 41.00           O  
ANISOU  751  O   LEU A 859     5537   5029   5011    628   1217   -467       O  
ATOM    752  CB  LEU A 859      10.071  29.616   8.258  1.00 41.97           C  
ANISOU  752  CB  LEU A 859     5383   4958   5605    789   1395   -258       C  
ATOM    753  CG  LEU A 859      10.788  30.955   8.298  1.00 41.51           C  
ANISOU  753  CG  LEU A 859     5323   5014   5434    796   1349   -185       C  
ATOM    754  CD1 LEU A 859      11.254  31.273   9.720  1.00 41.58           C  
ANISOU  754  CD1 LEU A 859     5187   5058   5551    862   1195     10       C  
ATOM    755  CD2 LEU A 859      11.950  30.950   7.325  1.00 42.68           C  
ANISOU  755  CD2 LEU A 859     5452   5090   5674    785   1572   -280       C  
ATOM    756  N   LEU A 860       6.950  31.191   8.975  1.00 37.71           N  
ANISOU  756  N   LEU A 860     5032   4740   4554    712    978   -186       N  
ATOM    757  CA  LEU A 860       5.714  31.811   8.457  1.00 36.20           C  
ANISOU  757  CA  LEU A 860     4933   4657   4161    660    869   -239       C  
ATOM    758  C   LEU A 860       5.739  33.317   8.560  1.00 34.64           C  
ANISOU  758  C   LEU A 860     4776   4568   3817    682    782   -158       C  
ATOM    759  O   LEU A 860       6.417  33.862   9.407  1.00 32.31           O  
ANISOU  759  O   LEU A 860     4424   4276   3574    727    771    -67       O  
ATOM    760  CB  LEU A 860       4.505  31.326   9.255  1.00 35.64           C  
ANISOU  760  CB  LEU A 860     4804   4582   4155    657    787   -199       C  
ATOM    761  CG  LEU A 860       4.156  29.848   9.177  1.00 36.68           C  
ANISOU  761  CG  LEU A 860     4887   4580   4470    618    864   -275       C  
ATOM    762  CD1 LEU A 860       3.076  29.554  10.197  1.00 36.43           C  
ANISOU  762  CD1 LEU A 860     4775   4545   4519    621    807   -178       C  
ATOM    763  CD2 LEU A 860       3.716  29.464   7.772  1.00 37.70           C  
ANISOU  763  CD2 LEU A 860     5100   4708   4515    518    879   -492       C  
ATOM    764  N   TRP A 861       4.926  33.964   7.729  1.00 35.74           N  
ANISOU  764  N   TRP A 861     5001   4789   3788    646    705   -189       N  
ATOM    765  CA  TRP A 861       4.855  35.428   7.653  1.00 35.97           C  
ANISOU  765  CA  TRP A 861     5069   4882   3713    670    635   -100       C  
ATOM    766  C   TRP A 861       3.917  36.104   8.662  1.00 35.36           C  
ANISOU  766  C   TRP A 861     4927   4830   3677    715    526    -28       C  
ATOM    767  O   TRP A 861       2.832  35.606   8.959  1.00 36.29           O  
ANISOU  767  O   TRP A 861     4996   4961   3830    710    466    -46       O  
ATOM    768  CB  TRP A 861       4.388  35.847   6.270  1.00 36.87           C  
ANISOU  768  CB  TRP A 861     5300   5075   3631    623    590   -118       C  
ATOM    769  CG  TRP A 861       5.256  35.380   5.169  1.00 38.13           C  
ANISOU  769  CG  TRP A 861     5559   5238   3688    566    729   -206       C  
ATOM    770  CD1 TRP A 861       4.976  34.400   4.279  1.00 39.63           C  
ANISOU  770  CD1 TRP A 861     5820   5458   3779    491    759   -358       C  
ATOM    771  CD2 TRP A 861       6.541  35.893   4.819  1.00 38.61           C  
ANISOU  771  CD2 TRP A 861     5657   5268   3743    568    882   -170       C  
ATOM    772  NE1 TRP A 861       6.010  34.262   3.389  1.00 41.64           N  
ANISOU  772  NE1 TRP A 861     6171   5708   3941    450    943   -430       N  
ATOM    773  CE2 TRP A 861       6.986  35.169   3.704  1.00 41.08           C  
ANISOU  773  CE2 TRP A 861     6071   5599   3938    500   1027   -301       C  
ATOM    774  CE3 TRP A 861       7.364  36.889   5.345  1.00 37.93           C  
ANISOU  774  CE3 TRP A 861     5519   5135   3757    607    923    -59       C  
ATOM    775  CZ2 TRP A 861       8.220  35.413   3.102  1.00 42.57           C  
ANISOU  775  CZ2 TRP A 861     6304   5760   4110    482   1237   -303       C  
ATOM    776  CZ3 TRP A 861       8.583  37.126   4.750  1.00 38.79           C  
ANISOU  776  CZ3 TRP A 861     5654   5209   3874    582   1104    -54       C  
ATOM    777  CH2 TRP A 861       9.000  36.399   3.645  1.00 41.00           C  
ANISOU  777  CH2 TRP A 861     6029   5509   4040    526   1270   -164       C  
ATOM    778  N   HIS A 862       4.333  37.268   9.147  1.00 34.53           N  
ANISOU  778  N   HIS A 862     4815   4718   3587    749    521     33       N  
ATOM    779  CA  HIS A 862       3.454  38.131   9.897  1.00 33.83           C  
ANISOU  779  CA  HIS A 862     4683   4638   3533    790    453     68       C  
ATOM    780  C   HIS A 862       3.667  39.580   9.522  1.00 34.11           C  
ANISOU  780  C   HIS A 862     4754   4639   3566    808    445    125       C  
ATOM    781  O   HIS A 862       4.683  40.172   9.859  1.00 34.30           O  
ANISOU  781  O   HIS A 862     4777   4619   3635    801    501    124       O  
ATOM    782  CB  HIS A 862       3.679  37.975  11.392  1.00 33.80           C  
ANISOU  782  CB  HIS A 862     4612   4636   3592    809    477     56       C  
ATOM    783  CG  HIS A 862       2.660  38.695  12.217  1.00 34.15           C  
ANISOU  783  CG  HIS A 862     4618   4691   3666    843    455     49       C  
ATOM    784  ND1 HIS A 862       1.496  38.097  12.646  1.00 34.36           N  
ANISOU  784  ND1 HIS A 862     4588   4742   3723    852    453     47       N  
ATOM    785  CD2 HIS A 862       2.611  39.973  12.658  1.00 34.92           C  
ANISOU  785  CD2 HIS A 862     4711   4755   3798    866    463     29       C  
ATOM    786  CE1 HIS A 862       0.781  38.970  13.331  1.00 35.33           C  
ANISOU  786  CE1 HIS A 862     4674   4860   3890    887    473     26       C  
ATOM    787  NE2 HIS A 862       1.441  40.114  13.361  1.00 36.02           N  
ANISOU  787  NE2 HIS A 862     4798   4906   3982    898    479      4       N  
ATOM    788  N   GLY A 863       2.696  40.154   8.832  1.00 34.95           N  
ANISOU  788  N   GLY A 863     4875   4754   3649    831    368    186       N  
ATOM    789  CA  GLY A 863       2.729  41.561   8.514  1.00 36.14           C  
ANISOU  789  CA  GLY A 863     5045   4837   3847    864    362    280       C  
ATOM    790  C   GLY A 863       2.019  42.376   9.566  1.00 37.27           C  
ANISOU  790  C   GLY A 863     5099   4910   4150    923    359    259       C  
ATOM    791  O   GLY A 863       1.074  41.913  10.204  1.00 37.59           O  
ANISOU  791  O   GLY A 863     5066   4984   4233    946    333    210       O  
ATOM    792  N   SER A 864       2.480  43.604   9.737  1.00 38.62           N  
ANISOU  792  N   SER A 864     5274   4968   4430    939    411    283       N  
ATOM    793  CA  SER A 864       1.854  44.549  10.629  1.00 38.82           C  
ANISOU  793  CA  SER A 864     5225   4892   4633    991    443    233       C  
ATOM    794  C   SER A 864       2.234  45.946  10.174  1.00 40.40           C  
ANISOU  794  C   SER A 864     5441   4927   4980   1010    485    320       C  
ATOM    795  O   SER A 864       3.190  46.131   9.421  1.00 41.21           O  
ANISOU  795  O   SER A 864     5613   5010   5033    965    513    401       O  
ATOM    796  CB  SER A 864       2.343  44.305  12.050  1.00 38.97           C  
ANISOU  796  CB  SER A 864     5224   4939   4642    952    512     58       C  
ATOM    797  OG  SER A 864       1.663  45.144  12.975  1.00 41.59           O  
ANISOU  797  OG  SER A 864     5499   5188   5115    991    574    -40       O  
ATOM    798  N   ARG A 865       1.495  46.948  10.612  1.00 41.60           N  
ANISOU  798  N   ARG A 865     5520   4938   5346   1077    518    309       N  
ATOM    799  CA  ARG A 865       1.883  48.300  10.249  1.00 42.54           C  
ANISOU  799  CA  ARG A 865     5644   4853   5666   1094    581    395       C  
ATOM    800  C   ARG A 865       3.126  48.729  11.035  1.00 41.81           C  
ANISOU  800  C   ARG A 865     5570   4684   5629   1001    687    218       C  
ATOM    801  O   ARG A 865       3.319  48.358  12.191  1.00 40.54           O  
ANISOU  801  O   ARG A 865     5393   4596   5413    955    712      4       O  
ATOM    802  CB  ARG A 865       0.714  49.299  10.338  1.00 44.29           C  
ANISOU  802  CB  ARG A 865     5762   4898   6168   1209    594    459       C  
ATOM    803  CG  ARG A 865      -0.057  49.348  11.642  1.00 44.53           C  
ANISOU  803  CG  ARG A 865     5698   4897   6323   1242    676    236       C  
ATOM    804  CD  ARG A 865      -1.582  49.391  11.419  1.00 45.58           C  
ANISOU  804  CD  ARG A 865     5696   5005   6616   1366    621    347       C  
ATOM    805  NE  ARG A 865      -2.015  50.409  10.467  1.00 47.35           N  
ANISOU  805  NE  ARG A 865     5860   5048   7083   1468    569    601       N  
ATOM    806  CZ  ARG A 865      -3.265  50.577  10.045  1.00 48.80           C  
ANISOU  806  CZ  ARG A 865     5898   5195   7447   1588    475    766       C  
ATOM    807  NH1 ARG A 865      -3.535  51.535   9.175  1.00 51.28           N  
ANISOU  807  NH1 ARG A 865     6162   5342   7979   1685    412   1041       N  
ATOM    808  NH2 ARG A 865      -4.247  49.800  10.477  1.00 48.47           N  
ANISOU  808  NH2 ARG A 865     5744   5277   7393   1614    441    683       N  
ATOM    809  N   THR A 866       3.980  49.487  10.357  1.00 42.48           N  
ANISOU  809  N   THR A 866     5688   4637   5812    964    741    326       N  
ATOM    810  CA  THR A 866       5.220  50.001  10.918  1.00 42.48           C  
ANISOU  810  CA  THR A 866     5679   4543   5918    859    829    177       C  
ATOM    811  C   THR A 866       5.068  50.562  12.330  1.00 43.34           C  
ANISOU  811  C   THR A 866     5728   4568   6168    832    879   -103       C  
ATOM    812  O   THR A 866       5.904  50.312  13.193  1.00 43.54           O  
ANISOU  812  O   THR A 866     5745   4674   6123    732    872   -303       O  
ATOM    813  CB  THR A 866       5.782  51.081   9.993  1.00 44.21           C  
ANISOU  813  CB  THR A 866     5912   4548   6336    842    917    362       C  
ATOM    814  OG1 THR A 866       6.036  50.493   8.716  1.00 44.23           O  
ANISOU  814  OG1 THR A 866     5997   4672   6134    844    891    597       O  
ATOM    815  CG2 THR A 866       7.073  51.654  10.531  1.00 45.30           C  
ANISOU  815  CG2 THR A 866     6007   4565   6638    715   1009    198       C  
ATOM    816  N   THR A 867       3.992  51.291  12.582  1.00 44.14           N  
ANISOU  816  N   THR A 867     5785   4521   6462    920    929   -124       N  
ATOM    817  CA  THR A 867       3.811  51.912  13.887  1.00 45.51           C  
ANISOU  817  CA  THR A 867     5920   4601   6771    888   1021   -426       C  
ATOM    818  C   THR A 867       3.667  50.914  15.026  1.00 44.29           C  
ANISOU  818  C   THR A 867     5788   4702   6337    847    981   -633       C  
ATOM    819  O   THR A 867       3.685  51.297  16.182  1.00 45.51           O  
ANISOU  819  O   THR A 867     5942   4845   6503    789   1052   -910       O  
ATOM    820  CB  THR A 867       2.605  52.870  13.888  1.00 47.36           C  
ANISOU  820  CB  THR A 867     6080   4596   7315   1010   1120   -406       C  
ATOM    821  OG1 THR A 867       1.518  52.263  13.188  1.00 47.41           O  
ANISOU  821  OG1 THR A 867     6056   4702   7254   1136   1032   -171       O  
ATOM    822  CG2 THR A 867       2.964  54.155  13.194  1.00 49.31           C  
ANISOU  822  CG2 THR A 867     6298   4521   7913   1021   1202   -275       C  
ATOM    823  N   ASN A 868       3.522  49.637  14.704  1.00 42.72           N  
ANISOU  823  N   ASN A 868     5616   4731   5882    870    878   -499       N  
ATOM    824  CA  ASN A 868       3.434  48.600  15.730  1.00 42.29           C  
ANISOU  824  CA  ASN A 868     5586   4912   5570    834    843   -631       C  
ATOM    825  C   ASN A 868       4.763  47.902  16.040  1.00 42.44           C  
ANISOU  825  C   ASN A 868     5635   5091   5398    727    753   -668       C  
ATOM    826  O   ASN A 868       4.847  47.132  16.990  1.00 41.19           O  
ANISOU  826  O   ASN A 868     5496   5122   5031    689    712   -758       O  
ATOM    827  CB  ASN A 868       2.404  47.549  15.306  1.00 40.69           C  
ANISOU  827  CB  ASN A 868     5369   4835   5254    919    795   -472       C  
ATOM    828  CG  ASN A 868       1.008  48.113  15.227  1.00 41.70           C  
ANISOU  828  CG  ASN A 868     5422   4838   5581   1027    867   -450       C  
ATOM    829  OD1 ASN A 868       0.710  49.121  15.833  1.00 44.47           O  
ANISOU  829  OD1 ASN A 868     5740   5035   6119   1042    988   -604       O  
ATOM    830  ND2 ASN A 868       0.154  47.473  14.467  1.00 41.78           N  
ANISOU  830  ND2 ASN A 868     5389   4906   5580   1099    793   -270       N  
ATOM    831  N   PHE A 869       5.798  48.159  15.246  1.00 44.03           N  
ANISOU  831  N   PHE A 869     5827   5216   5687    681    728   -577       N  
ATOM    832  CA  PHE A 869       7.000  47.332  15.329  1.00 44.03           C  
ANISOU  832  CA  PHE A 869     5814   5360   5553    606    643   -561       C  
ATOM    833  C   PHE A 869       7.884  47.623  16.514  1.00 44.80           C  
ANISOU  833  C   PHE A 869     5878   5520   5623    491    591   -778       C  
ATOM    834  O   PHE A 869       8.602  46.741  16.955  1.00 45.13           O  
ANISOU  834  O   PHE A 869     5893   5736   5515    451    486   -767       O  
ATOM    835  CB  PHE A 869       7.793  47.355  14.033  1.00 44.47           C  
ANISOU  835  CB  PHE A 869     5859   5334   5702    597    664   -384       C  
ATOM    836  CG  PHE A 869       7.392  46.266  13.110  1.00 43.51           C  
ANISOU  836  CG  PHE A 869     5780   5312   5438    666    644   -202       C  
ATOM    837  CD1 PHE A 869       7.940  45.018  13.243  1.00 43.28           C  
ANISOU  837  CD1 PHE A 869     5734   5435   5272    651    592   -183       C  
ATOM    838  CD2 PHE A 869       6.404  46.467  12.173  1.00 44.52           C  
ANISOU  838  CD2 PHE A 869     5954   5382   5579    744    665    -60       C  
ATOM    839  CE1 PHE A 869       7.546  43.989  12.424  1.00 42.59           C  
ANISOU  839  CE1 PHE A 869     5688   5418   5075    699    590    -63       C  
ATOM    840  CE2 PHE A 869       6.000  45.445  11.341  1.00 43.79           C  
ANISOU  840  CE2 PHE A 869     5904   5398   5334    783    628     63       C  
ATOM    841  CZ  PHE A 869       6.575  44.203  11.464  1.00 43.12           C  
ANISOU  841  CZ  PHE A 869     5814   5444   5124    754    604     40       C  
ATOM    842  N   ALA A 870       7.823  48.837  17.042  1.00 46.05           N  
ANISOU  842  N   ALA A 870     6030   5535   5932    437    654   -978       N  
ATOM    843  CA  ALA A 870       8.549  49.139  18.265  1.00 47.23           C  
ANISOU  843  CA  ALA A 870     6159   5773   6011    305    583  -1237       C  
ATOM    844  C   ALA A 870       8.004  48.256  19.379  1.00 46.89           C  
ANISOU  844  C   ALA A 870     6179   5993   5642    317    523  -1304       C  
ATOM    845  O   ALA A 870       8.779  47.653  20.133  1.00 48.62           O  
ANISOU  845  O   ALA A 870     6383   6424   5665    241    376  -1342       O  
ATOM    846  CB  ALA A 870       8.421  50.605  18.626  1.00 49.19           C  
ANISOU  846  CB  ALA A 870     6401   5793   6492    240    693  -1484       C  
ATOM    847  N   GLY A 871       6.675  48.165  19.462  1.00 44.84           N  
ANISOU  847  N   GLY A 871     5976   5721   5340    415    636  -1289       N  
ATOM    848  CA  GLY A 871       6.018  47.368  20.487  1.00 43.92           C  
ANISOU  848  CA  GLY A 871     5923   5832   4932    428    634  -1331       C  
ATOM    849  C   GLY A 871       6.245  45.896  20.256  1.00 41.55           C  
ANISOU  849  C   GLY A 871     5614   5712   4459    470    522  -1083       C  
ATOM    850  O   GLY A 871       6.512  45.146  21.183  1.00 41.55           O  
ANISOU  850  O   GLY A 871     5644   5935   4205    429    436  -1080       O  
ATOM    851  N   ILE A 872       6.153  45.493  19.002  1.00 39.92           N  
ANISOU  851  N   ILE A 872     5369   5404   4393    549    527   -871       N  
ATOM    852  CA  ILE A 872       6.299  44.096  18.623  1.00 39.36           C  
ANISOU  852  CA  ILE A 872     5285   5449   4220    593    457   -659       C  
ATOM    853  C   ILE A 872       7.706  43.560  18.903  1.00 40.20           C  
ANISOU  853  C   ILE A 872     5339   5666   4269    528    317   -617       C  
ATOM    854  O   ILE A 872       7.865  42.405  19.285  1.00 40.62           O  
ANISOU  854  O   ILE A 872     5383   5862   4189    547    248   -493       O  
ATOM    855  CB  ILE A 872       5.995  43.896  17.124  1.00 37.81           C  
ANISOU  855  CB  ILE A 872     5071   5118   4175    667    495   -491       C  
ATOM    856  CG1 ILE A 872       4.491  44.012  16.869  1.00 37.51           C  
ANISOU  856  CG1 ILE A 872     5048   5024   4180    748    580   -468       C  
ATOM    857  CG2 ILE A 872       6.481  42.535  16.655  1.00 37.21           C  
ANISOU  857  CG2 ILE A 872     4974   5125   4039    685    437   -328       C  
ATOM    858  CD1 ILE A 872       4.096  43.980  15.408  1.00 36.43           C  
ANISOU  858  CD1 ILE A 872     4902   4782   4156    807    580   -314       C  
ATOM    859  N   LEU A 873       8.726  44.374  18.680  1.00 40.33           N  
ANISOU  859  N   LEU A 873     5297   5596   4428    456    278   -699       N  
ATOM    860  CA  LEU A 873      10.070  43.899  18.899  1.00 41.60           C  
ANISOU  860  CA  LEU A 873     5362   5850   4592    398    138   -653       C  
ATOM    861  C   LEU A 873      10.408  43.907  20.392  1.00 44.55           C  
ANISOU  861  C   LEU A 873     5741   6435   4750    312     -7   -782       C  
ATOM    862  O   LEU A 873      11.083  42.994  20.875  1.00 44.87           O  
ANISOU  862  O   LEU A 873     5720   6639   4687    309   -155   -660       O  
ATOM    863  CB  LEU A 873      11.085  44.700  18.079  1.00 41.96           C  
ANISOU  863  CB  LEU A 873     5315   5727   4899    341    160   -680       C  
ATOM    864  CG  LEU A 873      10.944  44.505  16.565  1.00 40.65           C  
ANISOU  864  CG  LEU A 873     5158   5408   4876    416    293   -511       C  
ATOM    865  CD1 LEU A 873      11.950  45.357  15.803  1.00 41.30           C  
ANISOU  865  CD1 LEU A 873     5158   5326   5207    348    355   -520       C  
ATOM    866  CD2 LEU A 873      11.090  43.037  16.175  1.00 39.84           C  
ANISOU  866  CD2 LEU A 873     5033   5394   4708    487    276   -334       C  
ATOM    867  N   SER A 874       9.932  44.905  21.135  1.00 46.36           N  
ANISOU  867  N   SER A 874     6045   6666   4903    245     33  -1023       N  
ATOM    868  CA  SER A 874      10.266  44.969  22.559  1.00 49.66           C  
ANISOU  868  CA  SER A 874     6496   7320   5053    138   -109  -1181       C  
ATOM    869  C   SER A 874       9.409  44.019  23.392  1.00 49.89           C  
ANISOU  869  C   SER A 874     6634   7563   4756    192    -95  -1079       C  
ATOM    870  O   SER A 874       9.926  43.353  24.271  1.00 50.49           O  
ANISOU  870  O   SER A 874     6710   7882   4590    151   -266  -1001       O  
ATOM    871  CB  SER A 874      10.175  46.396  23.088  1.00 51.68           C  
ANISOU  871  CB  SER A 874     6796   7494   5343     21    -52  -1530       C  
ATOM    872  OG  SER A 874       8.840  46.706  23.384  1.00 53.31           O  
ANISOU  872  OG  SER A 874     7127   7661   5465     73    145  -1639       O  
ATOM    873  N   GLN A 875       8.116  43.939  23.091  1.00 50.16           N  
ANISOU  873  N   GLN A 875     6746   7506   4806    283    105  -1051       N  
ATOM    874  CA  GLN A 875       7.185  43.055  23.806  1.00 51.28           C  
ANISOU  874  CA  GLN A 875     6979   7816   4690    331    172   -944       C  
ATOM    875  C   GLN A 875       6.901  41.727  23.090  1.00 48.58           C  
ANISOU  875  C   GLN A 875     6589   7440   4426    444    185   -632       C  
ATOM    876  O   GLN A 875       6.254  40.854  23.664  1.00 48.32           O  
ANISOU  876  O   GLN A 875     6609   7532   4216    477    234   -501       O  
ATOM    877  CB  GLN A 875       5.845  43.763  23.999  1.00 53.51           C  
ANISOU  877  CB  GLN A 875     7341   8008   4980    356    408  -1124       C  
ATOM    878  CG  GLN A 875       5.924  45.060  24.773  1.00 57.22           C  
ANISOU  878  CG  GLN A 875     7872   8479   5388    246    458  -1480       C  
ATOM    879  CD  GLN A 875       6.157  44.789  26.229  1.00 62.33           C  
ANISOU  879  CD  GLN A 875     8631   9445   5604    140    380  -1579       C  
ATOM    880  OE1 GLN A 875       7.276  44.922  26.725  1.00 65.59           O  
ANISOU  880  OE1 GLN A 875     9032  10008   5880     28    161  -1651       O  
ATOM    881  NE2 GLN A 875       5.107  44.354  26.922  1.00 64.72           N  
ANISOU  881  NE2 GLN A 875     9036   9874   5680    170    551  -1560       N  
ATOM    882  N   GLY A 876       7.342  41.574  21.842  1.00 46.38           N  
ANISOU  882  N   GLY A 876     6220   6988   4413    494    167   -526       N  
ATOM    883  CA  GLY A 876       6.985  40.379  21.053  1.00 44.86           C  
ANISOU  883  CA  GLY A 876     5992   6733   4316    587    209   -294       C  
ATOM    884  C   GLY A 876       5.532  40.425  20.600  1.00 43.16           C  
ANISOU  884  C   GLY A 876     5817   6417   4162    648    377   -307       C  
ATOM    885  O   GLY A 876       4.797  41.331  20.965  1.00 43.90           O  
ANISOU  885  O   GLY A 876     5956   6488   4235    635    475   -471       O  
ATOM    886  N   LEU A 877       5.106  39.458  19.803  1.00 42.20           N  
ANISOU  886  N   LEU A 877     5663   6225   4144    710    413   -149       N  
ATOM    887  CA  LEU A 877       3.697  39.374  19.430  1.00 41.81           C  
ANISOU  887  CA  LEU A 877     5619   6104   4162    757    538   -149       C  
ATOM    888  C   LEU A 877       2.901  38.871  20.614  1.00 44.35           C  
ANISOU  888  C   LEU A 877     5977   6555   4319    750    623   -122       C  
ATOM    889  O   LEU A 877       3.301  37.906  21.279  1.00 44.62           O  
ANISOU  889  O   LEU A 877     6023   6704   4224    737    581     19       O  
ATOM    890  CB  LEU A 877       3.496  38.434  18.253  1.00 40.15           C  
ANISOU  890  CB  LEU A 877     5362   5796   4095    797    534    -21       C  
ATOM    891  CG  LEU A 877       4.046  38.932  16.918  1.00 39.37           C  
ANISOU  891  CG  LEU A 877     5251   5578   4129    804    495    -41       C  
ATOM    892  CD1 LEU A 877       4.127  37.785  15.929  1.00 38.54           C  
ANISOU  892  CD1 LEU A 877     5123   5421   4100    819    491     56       C  
ATOM    893  CD2 LEU A 877       3.191  40.051  16.346  1.00 39.58           C  
ANISOU  893  CD2 LEU A 877     5283   5513   4242    828    537   -118       C  
ATOM    894  N   ARG A 878       1.762  39.511  20.865  1.00 46.75           N  
ANISOU  894  N   ARG A 878     6287   6829   4644    763    760   -235       N  
ATOM    895  CA  ARG A 878       0.945  39.189  22.037  1.00 49.21           C  
ANISOU  895  CA  ARG A 878     6638   7266   4791    747    900   -236       C  
ATOM    896  C   ARG A 878      -0.511  38.887  21.723  1.00 48.81           C  
ANISOU  896  C   ARG A 878     6509   7127   4908    794   1053   -203       C  
ATOM    897  O   ARG A 878      -1.038  39.230  20.659  1.00 48.25           O  
ANISOU  897  O   ARG A 878     6353   6905   5073    840   1039   -224       O  
ATOM    898  CB  ARG A 878       1.024  40.319  23.050  1.00 52.06           C  
ANISOU  898  CB  ARG A 878     7082   7715   4983    696    966   -462       C  
ATOM    899  CG  ARG A 878       2.354  40.354  23.778  1.00 55.24           C  
ANISOU  899  CG  ARG A 878     7560   8285   5142    620    804   -482       C  
ATOM    900  CD  ARG A 878       2.395  41.489  24.766  1.00 59.51           C  
ANISOU  900  CD  ARG A 878     8191   8917   5501    543    868   -761       C  
ATOM    901  NE  ARG A 878       2.337  42.765  24.068  1.00 61.14           N  
ANISOU  901  NE  ARG A 878     8351   8908   5970    556    908   -967       N  
ATOM    902  CZ  ARG A 878       1.995  43.923  24.626  1.00 66.06           C  
ANISOU  902  CZ  ARG A 878     9019   9488   6590    516   1044  -1254       C  
ATOM    903  NH1 ARG A 878       1.665  43.998  25.924  1.00 69.69           N  
ANISOU  903  NH1 ARG A 878     9591  10139   6747    447   1166  -1410       N  
ATOM    904  NH2 ARG A 878       1.982  45.018  23.874  1.00 66.78           N  
ANISOU  904  NH2 ARG A 878     9049   9338   6987    542   1076  -1384       N  
ATOM    905  N   ILE A 879      -1.139  38.230  22.687  1.00 49.06           N  
ANISOU  905  N   ILE A 879     6563   7268   4809    774   1193   -134       N  
ATOM    906  CA  ILE A 879      -2.507  37.776  22.581  1.00 49.29           C  
ANISOU  906  CA  ILE A 879     6492   7229   5007    799   1358    -85       C  
ATOM    907  C   ILE A 879      -3.402  38.896  23.051  1.00 50.28           C  
ANISOU  907  C   ILE A 879     6594   7330   5177    817   1548   -287       C  
ATOM    908  O   ILE A 879      -3.281  39.341  24.191  1.00 50.88           O  
ANISOU  908  O   ILE A 879     6780   7540   5010    775   1668   -404       O  
ATOM    909  CB  ILE A 879      -2.770  36.577  23.525  1.00 51.20           C  
ANISOU  909  CB  ILE A 879     6766   7589   5095    761   1474     99       C  
ATOM    910  CG1 ILE A 879      -1.840  35.396  23.224  1.00 50.03           C  
ANISOU  910  CG1 ILE A 879     6632   7442   4933    753   1312    318       C  
ATOM    911  CG2 ILE A 879      -4.229  36.155  23.455  1.00 52.51           C  
ANISOU  911  CG2 ILE A 879     6801   7670   5479    771   1674    135       C  
ATOM    912  CD1 ILE A 879      -2.227  34.591  22.010  1.00 48.94           C  
ANISOU  912  CD1 ILE A 879     6368   7122   5105    773   1265    394       C  
ATOM    913  N   ALA A 880      -4.319  39.333  22.198  1.00 49.89           N  
ANISOU  913  N   ALA A 880     6399   7117   5440    878   1578   -331       N  
ATOM    914  CA  ALA A 880      -5.293  40.343  22.591  1.00 52.12           C  
ANISOU  914  CA  ALA A 880     6611   7331   5860    918   1785   -505       C  
ATOM    915  C   ALA A 880      -5.963  39.998  23.929  1.00 55.29           C  
ANISOU  915  C   ALA A 880     7050   7863   6095    876   2067   -536       C  
ATOM    916  O   ALA A 880      -6.264  38.838  24.195  1.00 55.14           O  
ANISOU  916  O   ALA A 880     7014   7915   6020    842   2121   -358       O  
ATOM    917  CB  ALA A 880      -6.334  40.505  21.508  1.00 51.67           C  
ANISOU  917  CB  ALA A 880     6344   7098   6188    994   1757   -461       C  
ATOM    918  N   PRO A 881      -6.204  41.013  24.776  1.00 59.36           N  
ANISOU  918  N   PRO A 881     7619   8399   6535    873   2274   -769       N  
ATOM    919  CA  PRO A 881      -6.721  40.750  26.127  1.00 63.55           C  
ANISOU  919  CA  PRO A 881     8231   9092   6821    817   2572   -823       C  
ATOM    920  C   PRO A 881      -8.084  40.054  26.105  1.00 66.07           C  
ANISOU  920  C   PRO A 881     8364   9349   7391    845   2792   -700       C  
ATOM    921  O   PRO A 881      -8.850  40.262  25.163  1.00 65.24           O  
ANISOU  921  O   PRO A 881     8036   9047   7701    923   2758   -683       O  
ATOM    922  CB  PRO A 881      -6.849  42.153  26.731  1.00 65.58           C  
ANISOU  922  CB  PRO A 881     8541   9311   7063    820   2765  -1161       C  
ATOM    923  CG  PRO A 881      -7.049  43.038  25.551  1.00 63.92           C  
ANISOU  923  CG  PRO A 881     8163   8831   7293    922   2648  -1217       C  
ATOM    924  CD  PRO A 881      -6.187  42.455  24.469  1.00 59.97           C  
ANISOU  924  CD  PRO A 881     7663   8315   6805    925   2288   -997       C  
ATOM    925  N   PRO A 882      -8.399  39.260  27.151  1.00 69.65           N  
ANISOU  925  N   PRO A 882     8897   9971   7596    777   3016   -603       N  
ATOM    926  CA  PRO A 882      -9.600  38.415  27.153  1.00 71.19           C  
ANISOU  926  CA  PRO A 882     8906  10105   8038    780   3228   -446       C  
ATOM    927  C   PRO A 882     -10.886  39.219  27.069  1.00 73.66           C  
ANISOU  927  C   PRO A 882     8992  10254   8740    850   3493   -625       C  
ATOM    928  O   PRO A 882     -11.869  38.741  26.508  1.00 73.31           O  
ANISOU  928  O   PRO A 882     8693  10074   9084    880   3538   -514       O  
ATOM    929  CB  PRO A 882      -9.520  37.689  28.498  1.00 74.05           C  
ANISOU  929  CB  PRO A 882     9454  10704   7976    686   3459   -332       C  
ATOM    930  CG  PRO A 882      -8.757  38.617  29.376  1.00 75.99           C  
ANISOU  930  CG  PRO A 882     9946  11130   7796    646   3489   -566       C  
ATOM    931  CD  PRO A 882      -7.763  39.309  28.481  1.00 72.42           C  
ANISOU  931  CD  PRO A 882     9509  10582   7422    687   3127   -670       C  
ATOM    932  N   GLU A 883     -10.854  40.431  27.621  1.00 76.65           N  
ANISOU  932  N   GLU A 883     9449  10634   9040    873   3660   -910       N  
ATOM    933  CA  GLU A 883     -12.011  41.328  27.651  1.00 80.42           C  
ANISOU  933  CA  GLU A 883     9710  10932   9913    957   3952  -1108       C  
ATOM    934  C   GLU A 883     -12.455  41.883  26.280  1.00 78.66           C  
ANISOU  934  C   GLU A 883     9209  10441  10237   1082   3730  -1084       C  
ATOM    935  O   GLU A 883     -13.629  42.208  26.101  1.00 80.26           O  
ANISOU  935  O   GLU A 883     9133  10479  10881   1162   3921  -1121       O  
ATOM    936  CB  GLU A 883     -11.787  42.480  28.665  1.00 84.55           C  
ANISOU  936  CB  GLU A 883    10412  11510  10201    937   4217  -1458       C  
ATOM    937  CG  GLU A 883     -10.439  43.218  28.618  1.00 84.24           C  
ANISOU  937  CG  GLU A 883    10605  11520   9882    903   3953  -1614       C  
ATOM    938  CD  GLU A 883     -10.348  44.307  27.549  1.00 84.32           C  
ANISOU  938  CD  GLU A 883    10465  11246  10323   1014   3767  -1715       C  
ATOM    939  OE1 GLU A 883     -11.324  44.518  26.789  1.00 85.31           O  
ANISOU  939  OE1 GLU A 883    10305  11148  10961   1131   3803  -1647       O  
ATOM    940  OE2 GLU A 883      -9.281  44.966  27.469  1.00 83.11           O  
ANISOU  940  OE2 GLU A 883    10474  11097  10007    981   3576  -1847       O  
ATOM    941  N   ALA A 884     -11.538  41.997  25.321  1.00 75.57           N  
ANISOU  941  N   ALA A 884     8880  10011   9821   1099   3335  -1006       N  
ATOM    942  CA  ALA A 884     -11.884  42.573  24.011  1.00 74.47           C  
ANISOU  942  CA  ALA A 884     8515   9650  10128   1211   3106   -955       C  
ATOM    943  C   ALA A 884     -12.951  41.745  23.266  1.00 74.84           C  
ANISOU  943  C   ALA A 884     8270   9628  10536   1236   3036   -753       C  
ATOM    944  O   ALA A 884     -13.062  40.534  23.476  1.00 73.42           O  
ANISOU  944  O   ALA A 884     8101   9560  10232   1149   3054   -610       O  
ATOM    945  CB  ALA A 884     -10.639  42.743  23.148  1.00 71.48           C  
ANISOU  945  CB  ALA A 884     8290   9274   9595   1204   2726   -890       C  
ATOM    946  N   PRO A 885     -13.739  42.399  22.389  1.00 75.43           N  
ANISOU  946  N   PRO A 885     8068   9511  11079   1352   2944   -732       N  
ATOM    947  CA  PRO A 885     -14.806  41.684  21.699  1.00 74.66           C  
ANISOU  947  CA  PRO A 885     7661   9361  11344   1362   2853   -567       C  
ATOM    948  C   PRO A 885     -14.286  40.846  20.539  1.00 71.69           C  
ANISOU  948  C   PRO A 885     7322   9042  10871   1305   2435   -384       C  
ATOM    949  O   PRO A 885     -13.261  41.170  19.916  1.00 67.96           O  
ANISOU  949  O   PRO A 885     7038   8588  10195   1312   2177   -365       O  
ATOM    950  CB  PRO A 885     -15.722  42.804  21.194  1.00 77.44           C  
ANISOU  950  CB  PRO A 885     7710   9500  12212   1517   2865   -602       C  
ATOM    951  CG  PRO A 885     -14.954  44.084  21.358  1.00 78.19           C  
ANISOU  951  CG  PRO A 885     7987   9507  12213   1587   2896   -756       C  
ATOM    952  CD  PRO A 885     -13.573  43.756  21.843  1.00 75.84           C  
ANISOU  952  CD  PRO A 885     8079   9387  11349   1469   2847   -817       C  
ATOM    953  N   VAL A 886     -15.041  39.801  20.234  1.00 72.58           N  
ANISOU  953  N   VAL A 886     7240   9170  11167   1243   2391   -269       N  
ATOM    954  CA  VAL A 886     -14.570  38.694  19.407  1.00 70.12           C  
ANISOU  954  CA  VAL A 886     6994   8929  10719   1144   2089   -143       C  
ATOM    955  C   VAL A 886     -14.565  38.990  17.896  1.00 70.18           C  
ANISOU  955  C   VAL A 886     6901   8893  10869   1187   1677    -71       C  
ATOM    956  O   VAL A 886     -13.981  38.233  17.105  1.00 67.83           O  
ANISOU  956  O   VAL A 886     6710   8658  10401   1107   1418    -10       O  
ATOM    957  CB  VAL A 886     -15.395  37.420  19.726  1.00 71.45           C  
ANISOU  957  CB  VAL A 886     6989   9107  11049   1037   2231    -71       C  
ATOM    958  CG1 VAL A 886     -16.680  37.344  18.895  1.00 73.28           C  
ANISOU  958  CG1 VAL A 886     6824   9244  11776   1052   2092    -31       C  
ATOM    959  CG2 VAL A 886     -14.539  36.183  19.553  1.00 70.21           C  
ANISOU  959  CG2 VAL A 886     7036   9027  10614    915   2098     14       C  
ATOM    960  N   THR A 887     -15.215  40.084  17.499  1.00 72.40           N  
ANISOU  960  N   THR A 887     6979   9067  11462   1314   1628    -72       N  
ATOM    961  CA  THR A 887     -15.191  40.531  16.107  1.00 71.58           C  
ANISOU  961  CA  THR A 887     6802   8941  11452   1369   1236     33       C  
ATOM    962  C   THR A 887     -13.794  41.050  15.793  1.00 67.50           C  
ANISOU  962  C   THR A 887     6616   8457  10570   1380   1112     28       C  
ATOM    963  O   THR A 887     -13.152  41.691  16.636  1.00 66.37           O  
ANISOU  963  O   THR A 887     6652   8284  10278   1412   1329    -75       O  
ATOM    964  CB  THR A 887     -16.200  41.665  15.848  1.00 75.47           C  
ANISOU  964  CB  THR A 887     6986   9288  12402   1526   1228     78       C  
ATOM    965  OG1 THR A 887     -15.808  42.820  16.597  1.00 76.45           O  
ANISOU  965  OG1 THR A 887     7225   9300  12520   1630   1483    -26       O  
ATOM    966  CG2 THR A 887     -17.622  41.251  16.256  1.00 78.66           C  
ANISOU  966  CG2 THR A 887     7010   9639  13236   1525   1398     72       C  
ATOM    967  N   GLY A 888     -13.326  40.762  14.584  1.00 64.82           N  
ANISOU  967  N   GLY A 888     6355   8185  10087   1340    772    125       N  
ATOM    968  CA  GLY A 888     -11.958  41.073  14.199  1.00 61.14           C  
ANISOU  968  CA  GLY A 888     6192   7758   9278   1329    664    132       C  
ATOM    969  C   GLY A 888     -11.010  39.970  14.626  1.00 58.34           C  
ANISOU  969  C   GLY A 888     6068   7508   8588   1203    731     71       C  
ATOM    970  O   GLY A 888      -9.781  40.106  14.482  1.00 57.12           O  
ANISOU  970  O   GLY A 888     6155   7389   8157   1183    683     61       O  
ATOM    971  N   TYR A 889     -11.574  38.880  15.160  1.00 56.34           N  
ANISOU  971  N   TYR A 889     5721   7288   8397   1122    851     48       N  
ATOM    972  CA  TYR A 889     -10.805  37.680  15.487  1.00 52.81           C  
ANISOU  972  CA  TYR A 889     5449   6911   7702   1009    898     36       C  
ATOM    973  C   TYR A 889     -11.511  36.471  14.904  1.00 53.74           C  
ANISOU  973  C   TYR A 889     5410   7034   7973    906    787     60       C  
ATOM    974  O   TYR A 889     -12.248  35.764  15.581  1.00 54.61           O  
ANISOU  974  O   TYR A 889     5381   7117   8248    854    966     61       O  
ATOM    975  CB  TYR A 889     -10.617  37.543  16.985  1.00 51.83           C  
ANISOU  975  CB  TYR A 889     5415   6809   7468    999   1215     -4       C  
ATOM    976  CG  TYR A 889      -9.910  38.725  17.576  1.00 50.20           C  
ANISOU  976  CG  TYR A 889     5364   6603   7103   1071   1312    -79       C  
ATOM    977  CD1 TYR A 889     -10.605  39.680  18.302  1.00 51.86           C  
ANISOU  977  CD1 TYR A 889     5474   6753   7475   1147   1528   -166       C  
ATOM    978  CD2 TYR A 889      -8.553  38.907  17.389  1.00 47.27           C  
ANISOU  978  CD2 TYR A 889     5225   6277   6457   1058   1200    -86       C  
ATOM    979  CE1 TYR A 889      -9.961  40.780  18.837  1.00 51.24           C  
ANISOU  979  CE1 TYR A 889     5538   6654   7275   1196   1624   -279       C  
ATOM    980  CE2 TYR A 889      -7.901  40.000  17.930  1.00 46.98           C  
ANISOU  980  CE2 TYR A 889     5313   6230   6305   1102   1279   -180       C  
ATOM    981  CZ  TYR A 889      -8.617  40.934  18.642  1.00 48.35           C  
ANISOU  981  CZ  TYR A 889     5398   6337   6633   1166   1485   -286       C  
ATOM    982  OH  TYR A 889      -7.989  42.021  19.170  1.00 48.62           O  
ANISOU  982  OH  TYR A 889     5555   6339   6578   1193   1571   -421       O  
ATOM    983  N   MET A 890     -11.261  36.263  13.617  1.00 54.04           N  
ANISOU  983  N   MET A 890     5478   7107   7948    867    499     69       N  
ATOM    984  CA  MET A 890     -11.888  35.226  12.832  1.00 54.86           C  
ANISOU  984  CA  MET A 890     5440   7220   8181    752    333     45       C  
ATOM    985  C   MET A 890     -11.677  33.859  13.476  1.00 52.77           C  
ANISOU  985  C   MET A 890     5222   6916   7912    640    512     16       C  
ATOM    986  O   MET A 890     -12.557  33.005  13.436  1.00 54.24           O  
ANISOU  986  O   MET A 890     5211   7054   8343    544    524     -8       O  
ATOM    987  CB  MET A 890     -11.285  35.261  11.432  1.00 56.98           C  
ANISOU  987  CB  MET A 890     5841   7564   8245    718     32     31       C  
ATOM    988  CG  MET A 890     -12.078  34.526  10.375  1.00 62.79           C  
ANISOU  988  CG  MET A 890     6415   8343   9098    601   -220    -23       C  
ATOM    989  SD  MET A 890     -11.229  34.563   8.782  1.00 67.37           S  
ANISOU  989  SD  MET A 890     7220   9050   9325    547   -525    -60       S  
ATOM    990  CE  MET A 890     -12.611  34.344   7.648  1.00 71.57           C  
ANISOU  990  CE  MET A 890     7477   9682  10032    454   -889    -88       C  
ATOM    991  N   PHE A 891     -10.507  33.653  14.070  1.00 48.91           N  
ANISOU  991  N   PHE A 891     4975   6434   7174    649    645     34       N  
ATOM    992  CA  PHE A 891     -10.211  32.400  14.738  1.00 47.84           C  
ANISOU  992  CA  PHE A 891     4890   6246   7039    565    817     62       C  
ATOM    993  C   PHE A 891      -9.761  32.657  16.178  1.00 46.88           C  
ANISOU  993  C   PHE A 891     4886   6153   6770    625   1079    143       C  
ATOM    994  O   PHE A 891      -8.850  32.013  16.699  1.00 45.64           O  
ANISOU  994  O   PHE A 891     4889   5998   6452    604   1162    208       O  
ATOM    995  CB  PHE A 891      -9.162  31.627  13.938  1.00 46.52           C  
ANISOU  995  CB  PHE A 891     4891   6063   6720    503    688     18       C  
ATOM    996  CG  PHE A 891      -9.623  31.219  12.560  1.00 47.59           C  
ANISOU  996  CG  PHE A 891     4936   6193   6950    410    448    -97       C  
ATOM    997  CD1 PHE A 891     -10.442  30.117  12.384  1.00 49.16           C  
ANISOU  997  CD1 PHE A 891     4963   6305   7409    282    454   -159       C  
ATOM    998  CD2 PHE A 891      -9.222  31.930  11.431  1.00 47.59           C  
ANISOU  998  CD2 PHE A 891     5031   6283   6766    436    217   -147       C  
ATOM    999  CE1 PHE A 891     -10.857  29.735  11.119  1.00 50.70           C  
ANISOU  999  CE1 PHE A 891     5083   6519   7661    172    210   -305       C  
ATOM   1000  CE2 PHE A 891      -9.635  31.546  10.157  1.00 48.82           C  
ANISOU 1000  CE2 PHE A 891     5131   6478   6939    335    -18   -261       C  
ATOM   1001  CZ  PHE A 891     -10.455  30.447  10.004  1.00 50.15           C  
ANISOU 1001  CZ  PHE A 891     5128   6575   7349    198    -34   -358       C  
ATOM   1002  N   GLY A 892     -10.420  33.605  16.826  1.00 47.62           N  
ANISOU 1002  N   GLY A 892     4894   6272   6926    697   1209    136       N  
ATOM   1003  CA  GLY A 892     -10.172  33.882  18.230  1.00 48.08           C  
ANISOU 1003  CA  GLY A 892     5060   6384   6823    732   1474    175       C  
ATOM   1004  C   GLY A 892      -8.927  34.712  18.483  1.00 46.42           C  
ANISOU 1004  C   GLY A 892     5086   6253   6298    794   1426    145       C  
ATOM   1005  O   GLY A 892      -8.218  35.115  17.563  1.00 43.13           O  
ANISOU 1005  O   GLY A 892     4748   5833   5806    818   1211    109       O  
ATOM   1006  N   LYS A 893      -8.668  34.959  19.759  1.00 47.93           N  
ANISOU 1006  N   LYS A 893     5389   6523   6296    806   1636    155       N  
ATOM   1007  CA  LYS A 893      -7.599  35.858  20.164  1.00 48.27           C  
ANISOU 1007  CA  LYS A 893     5629   6649   6062    848   1604     90       C  
ATOM   1008  C   LYS A 893      -6.287  35.097  20.225  1.00 47.30           C  
ANISOU 1008  C   LYS A 893     5676   6583   5712    809   1493    187       C  
ATOM   1009  O   LYS A 893      -5.913  34.563  21.253  1.00 49.61           O  
ANISOU 1009  O   LYS A 893     6068   6968   5813    778   1606    282       O  
ATOM   1010  CB  LYS A 893      -7.923  36.521  21.518  1.00 50.47           C  
ANISOU 1010  CB  LYS A 893     5957   7010   6207    862   1870     14       C  
ATOM   1011  CG  LYS A 893      -9.326  37.121  21.600  1.00 52.16           C  
ANISOU 1011  CG  LYS A 893     5962   7142   6711    906   2053    -73       C  
ATOM   1012  CD  LYS A 893      -9.301  38.530  22.150  1.00 53.38           C  
ANISOU 1012  CD  LYS A 893     6170   7299   6810    967   2180   -260       C  
ATOM   1013  CE  LYS A 893     -10.701  39.055  22.399  1.00 56.32           C  
ANISOU 1013  CE  LYS A 893     6317   7577   7504   1021   2423   -344       C  
ATOM   1014  NZ  LYS A 893     -11.320  38.454  23.614  1.00 59.23           N  
ANISOU 1014  NZ  LYS A 893     6685   8035   7783    963   2765   -325       N  
ATOM   1015  N   GLY A 894      -5.594  35.042  19.101  1.00 45.78           N  
ANISOU 1015  N   GLY A 894     5508   6338   5546    815   1274    178       N  
ATOM   1016  CA  GLY A 894      -4.318  34.357  19.022  1.00 44.01           C  
ANISOU 1016  CA  GLY A 894     5407   6137   5175    793   1174    259       C  
ATOM   1017  C   GLY A 894      -3.330  35.180  18.226  1.00 42.35           C  
ANISOU 1017  C   GLY A 894     5275   5921   4891    824   1004    180       C  
ATOM   1018  O   GLY A 894      -3.526  36.374  18.017  1.00 42.49           O  
ANISOU 1018  O   GLY A 894     5287   5932   4924    863    984     79       O  
ATOM   1019  N   ILE A 895      -2.272  34.519  17.779  1.00 40.95           N  
ANISOU 1019  N   ILE A 895     5159   5726   4671    808    907    236       N  
ATOM   1020  CA  ILE A 895      -1.259  35.125  16.953  1.00 38.91           C  
ANISOU 1020  CA  ILE A 895     4965   5454   4364    824    776    180       C  
ATOM   1021  C   ILE A 895      -1.357  34.458  15.599  1.00 37.86           C  
ANISOU 1021  C   ILE A 895     4796   5234   4354    799    696    165       C  
ATOM   1022  O   ILE A 895      -1.193  33.238  15.493  1.00 37.85           O  
ANISOU 1022  O   ILE A 895     4776   5178   4423    765    719    216       O  
ATOM   1023  CB  ILE A 895       0.133  34.907  17.536  1.00 39.00           C  
ANISOU 1023  CB  ILE A 895     5057   5521   4237    823    745    241       C  
ATOM   1024  CG1 ILE A 895       0.187  35.455  18.960  1.00 41.16           C  
ANISOU 1024  CG1 ILE A 895     5383   5923   4332    822    807    240       C  
ATOM   1025  CG2 ILE A 895       1.170  35.624  16.694  1.00 38.60           C  
ANISOU 1025  CG2 ILE A 895     5048   5444   4171    832    643    177       C  
ATOM   1026  CD1 ILE A 895       1.447  35.057  19.692  1.00 42.54           C  
ANISOU 1026  CD1 ILE A 895     5612   6189   4361    811    740    339       C  
ATOM   1027  N   TYR A 896      -1.590  35.283  14.578  1.00 36.27           N  
ANISOU 1027  N   TYR A 896     4591   5015   4172    812    604     96       N  
ATOM   1028  CA  TYR A 896      -1.969  34.839  13.245  1.00 35.95           C  
ANISOU 1028  CA  TYR A 896     4524   4937   4197    775    509     57       C  
ATOM   1029  C   TYR A 896      -0.803  34.958  12.253  1.00 35.48           C  
ANISOU 1029  C   TYR A 896     4572   4872   4036    765    450     31       C  
ATOM   1030  O   TYR A 896      -0.175  36.005  12.135  1.00 35.47           O  
ANISOU 1030  O   TYR A 896     4630   4888   3957    800    429     39       O  
ATOM   1031  CB  TYR A 896      -3.100  35.714  12.720  1.00 36.11           C  
ANISOU 1031  CB  TYR A 896     4462   4968   4289    800    427     39       C  
ATOM   1032  CG  TYR A 896      -4.456  35.527  13.366  1.00 36.50           C  
ANISOU 1032  CG  TYR A 896     4356   5006   4503    801    489     46       C  
ATOM   1033  CD1 TYR A 896      -4.659  35.789  14.711  1.00 36.46           C  
ANISOU 1033  CD1 TYR A 896     4332   5014   4508    834    650     65       C  
ATOM   1034  CD2 TYR A 896      -5.555  35.144  12.601  1.00 37.15           C  
ANISOU 1034  CD2 TYR A 896     4305   5078   4731    761    388     24       C  
ATOM   1035  CE1 TYR A 896      -5.910  35.656  15.283  1.00 37.19           C  
ANISOU 1035  CE1 TYR A 896     4274   5091   4765    835    751     69       C  
ATOM   1036  CE2 TYR A 896      -6.800  35.002  13.166  1.00 38.22           C  
ANISOU 1036  CE2 TYR A 896     4262   5192   5067    760    457     33       C  
ATOM   1037  CZ  TYR A 896      -6.970  35.262  14.507  1.00 38.05           C  
ANISOU 1037  CZ  TYR A 896     4222   5167   5068    801    660     59       C  
ATOM   1038  OH  TYR A 896      -8.215  35.120  15.057  1.00 39.30           O  
ANISOU 1038  OH  TYR A 896     4193   5297   5439    797    773     66       O  
ATOM   1039  N   PHE A 897      -0.541  33.887  11.521  1.00 35.23           N  
ANISOU 1039  N   PHE A 897     4557   4800   4027    709    447    -13       N  
ATOM   1040  CA  PHE A 897       0.519  33.870  10.536  1.00 35.25           C  
ANISOU 1040  CA  PHE A 897     4658   4795   3940    691    440    -58       C  
ATOM   1041  C   PHE A 897      -0.019  33.449   9.173  1.00 36.18           C  
ANISOU 1041  C   PHE A 897     4802   4930   4015    618    362   -161       C  
ATOM   1042  O   PHE A 897      -1.140  32.949   9.083  1.00 37.49           O  
ANISOU 1042  O   PHE A 897     4884   5094   4264    573    303   -203       O  
ATOM   1043  CB  PHE A 897       1.587  32.899  10.985  1.00 34.82           C  
ANISOU 1043  CB  PHE A 897     4608   4667   3953    692    546    -43       C  
ATOM   1044  CG  PHE A 897       2.307  33.338  12.218  1.00 34.13           C  
ANISOU 1044  CG  PHE A 897     4508   4606   3854    749    576     59       C  
ATOM   1045  CD1 PHE A 897       1.815  33.014  13.471  1.00 34.09           C  
ANISOU 1045  CD1 PHE A 897     4448   4618   3886    766    607    143       C  
ATOM   1046  CD2 PHE A 897       3.486  34.073  12.123  1.00 33.44           C  
ANISOU 1046  CD2 PHE A 897     4461   4536   3707    772    574     69       C  
ATOM   1047  CE1 PHE A 897       2.482  33.416  14.609  1.00 34.15           C  
ANISOU 1047  CE1 PHE A 897     4462   4689   3823    802    610    225       C  
ATOM   1048  CE2 PHE A 897       4.167  34.473  13.259  1.00 33.18           C  
ANISOU 1048  CE2 PHE A 897     4406   4545   3654    804    567    138       C  
ATOM   1049  CZ  PHE A 897       3.660  34.144  14.508  1.00 33.90           C  
ANISOU 1049  CZ  PHE A 897     4463   4683   3734    817    572    211       C  
ATOM   1050  N   ALA A 898       0.775  33.661   8.125  1.00 35.63           N  
ANISOU 1050  N   ALA A 898     4844   4885   3807    595    365   -208       N  
ATOM   1051  CA  ALA A 898       0.448  33.163   6.782  1.00 37.34           C  
ANISOU 1051  CA  ALA A 898     5126   5148   3912    505    304   -336       C  
ATOM   1052  C   ALA A 898       1.643  32.440   6.153  1.00 38.04           C  
ANISOU 1052  C   ALA A 898     5311   5181   3959    464    453   -448       C  
ATOM   1053  O   ALA A 898       2.799  32.721   6.492  1.00 36.81           O  
ANISOU 1053  O   ALA A 898     5176   4980   3828    518    570   -387       O  
ATOM   1054  CB  ALA A 898       0.000  34.314   5.889  1.00 37.89           C  
ANISOU 1054  CB  ALA A 898     5258   5345   3793    510    154   -270       C  
ATOM   1055  N   ASP A 899       1.359  31.516   5.235  1.00 40.34           N  
ANISOU 1055  N   ASP A 899     5648   5473   4206    361    455   -631       N  
ATOM   1056  CA  ASP A 899       2.408  30.873   4.447  1.00 42.31           C  
ANISOU 1056  CA  ASP A 899     6000   5670   4404    313    626   -782       C  
ATOM   1057  C   ASP A 899       2.613  31.533   3.092  1.00 44.23           C  
ANISOU 1057  C   ASP A 899     6416   6073   4316    256    596   -833       C  
ATOM   1058  O   ASP A 899       3.416  31.055   2.298  1.00 46.37           O  
ANISOU 1058  O   ASP A 899     6793   6326   4499    201    763   -985       O  
ATOM   1059  CB  ASP A 899       2.183  29.350   4.304  1.00 44.34           C  
ANISOU 1059  CB  ASP A 899     6216   5789   4841    227    715   -994       C  
ATOM   1060  CG  ASP A 899       0.898  28.984   3.575  1.00 46.49           C  
ANISOU 1060  CG  ASP A 899     6495   6148   5019     98    544  -1157       C  
ATOM   1061  OD1 ASP A 899       0.269  29.855   2.954  1.00 47.66           O  
ANISOU 1061  OD1 ASP A 899     6699   6489   4918     74    349  -1111       O  
ATOM   1062  OD2 ASP A 899       0.516  27.799   3.625  1.00 48.24           O  
ANISOU 1062  OD2 ASP A 899     6649   6233   5445     17    596  -1325       O  
ATOM   1063  N   MET A 900       1.907  32.627   2.826  1.00 45.66           N  
ANISOU 1063  N   MET A 900     6623   6403   4322    272    403   -693       N  
ATOM   1064  CA  MET A 900       2.130  33.393   1.599  1.00 49.31           C  
ANISOU 1064  CA  MET A 900     7257   7027   4449    232    367   -660       C  
ATOM   1065  C   MET A 900       2.200  34.888   1.858  1.00 47.50           C  
ANISOU 1065  C   MET A 900     7023   6837   4186    332    296   -391       C  
ATOM   1066  O   MET A 900       1.238  35.492   2.313  1.00 48.12           O  
ANISOU 1066  O   MET A 900     7001   6938   4342    385    114   -262       O  
ATOM   1067  CB  MET A 900       1.070  33.048   0.540  1.00 54.84           C  
ANISOU 1067  CB  MET A 900     8026   7898   4911    110    162   -787       C  
ATOM   1068  CG  MET A 900       1.197  31.600   0.071  1.00 58.64           C  
ANISOU 1068  CG  MET A 900     8551   8326   5403    -17    279  -1112       C  
ATOM   1069  SD  MET A 900       0.241  31.125  -1.369  1.00 68.22           S  
ANISOU 1069  SD  MET A 900     9892   9771   6258   -210     63  -1347       S  
ATOM   1070  CE  MET A 900       1.100  31.964  -2.701  1.00 69.62           C  
ANISOU 1070  CE  MET A 900    10354  10166   5930   -244    145  -1284       C  
ATOM   1071  N   VAL A 901       3.348  35.478   1.532  1.00 46.66           N  
ANISOU 1071  N   VAL A 901     7013   6717   3995    352    464   -319       N  
ATOM   1072  CA  VAL A 901       3.658  36.869   1.884  1.00 45.45           C  
ANISOU 1072  CA  VAL A 901     6842   6536   3887    440    456    -84       C  
ATOM   1073  C   VAL A 901       2.594  37.891   1.452  1.00 46.39           C  
ANISOU 1073  C   VAL A 901     6978   6763   3884    467    224    105       C  
ATOM   1074  O   VAL A 901       2.375  38.878   2.137  1.00 44.48           O  
ANISOU 1074  O   VAL A 901     6645   6445   3810    557    173    267       O  
ATOM   1075  CB  VAL A 901       5.063  37.279   1.347  1.00 45.91           C  
ANISOU 1075  CB  VAL A 901     7006   6569   3866    425    691    -46       C  
ATOM   1076  CG1 VAL A 901       5.118  37.263  -0.175  1.00 48.59           C  
ANISOU 1076  CG1 VAL A 901     7554   7073   3832    331    727    -66       C  
ATOM   1077  CG2 VAL A 901       5.484  38.636   1.887  1.00 44.75           C  
ANISOU 1077  CG2 VAL A 901     6806   6338   3856    501    708    164       C  
ATOM   1078  N   SER A 902       1.936  37.647   0.323  1.00 49.82           N  
ANISOU 1078  N   SER A 902     7519   7372   4037    389     80     80       N  
ATOM   1079  CA  SER A 902       0.909  38.556  -0.184  1.00 51.70           C  
ANISOU 1079  CA  SER A 902     7753   7728   4160    421   -176    295       C  
ATOM   1080  C   SER A 902      -0.207  38.746   0.838  1.00 50.36           C  
ANISOU 1080  C   SER A 902     7360   7477   4297    506   -342    343       C  
ATOM   1081  O   SER A 902      -0.660  39.868   1.068  1.00 50.49           O  
ANISOU 1081  O   SER A 902     7300   7449   4434    605   -437    564       O  
ATOM   1082  CB  SER A 902       0.325  38.014  -1.482  1.00 55.40           C  
ANISOU 1082  CB  SER A 902     8355   8433   4262    300   -348    216       C  
ATOM   1083  OG  SER A 902      -0.402  36.826  -1.225  1.00 56.03           O  
ANISOU 1083  OG  SER A 902     8332   8520   4435    228   -442    -33       O  
ATOM   1084  N   LYS A 903      -0.635  37.645   1.453  1.00 49.07           N  
ANISOU 1084  N   LYS A 903     7085   7272   4284    467   -344    138       N  
ATOM   1085  CA  LYS A 903      -1.615  37.693   2.534  1.00 47.85           C  
ANISOU 1085  CA  LYS A 903     6715   7030   4434    537   -431    160       C  
ATOM   1086  C   LYS A 903      -1.118  38.586   3.664  1.00 44.99           C  
ANISOU 1086  C   LYS A 903     6289   6510   4294    654   -287    271       C  
ATOM   1087  O   LYS A 903      -1.783  39.552   4.028  1.00 44.95           O  
ANISOU 1087  O   LYS A 903     6179   6460   4437    744   -371    418       O  
ATOM   1088  CB  LYS A 903      -1.914  36.273   3.041  1.00 48.75           C  
ANISOU 1088  CB  LYS A 903     6743   7099   4678    463   -386    -68       C  
ATOM   1089  CG  LYS A 903      -2.795  36.145   4.288  1.00 48.82           C  
ANISOU 1089  CG  LYS A 903     6538   7007   5003    520   -397    -57       C  
ATOM   1090  CD  LYS A 903      -4.267  36.402   4.033  1.00 51.54           C  
ANISOU 1090  CD  LYS A 903     6722   7428   5432    524   -640      5       C  
ATOM   1091  CE  LYS A 903      -5.073  36.406   5.335  1.00 52.05           C  
ANISOU 1091  CE  LYS A 903     6570   7378   5827    591   -584     25       C  
ATOM   1092  NZ  LYS A 903      -6.372  37.162   5.233  1.00 53.82           N  
ANISOU 1092  NZ  LYS A 903     6601   7638   6207    654   -780    157       N  
ATOM   1093  N   SER A 904       0.053  38.268   4.209  1.00 42.69           N  
ANISOU 1093  N   SER A 904     6049   6130   4041    647    -76    188       N  
ATOM   1094  CA  SER A 904       0.609  39.028   5.326  1.00 40.29           C  
ANISOU 1094  CA  SER A 904     5688   5697   3922    729     43    248       C  
ATOM   1095  C   SER A 904       0.862  40.487   4.982  1.00 41.04           C  
ANISOU 1095  C   SER A 904     5827   5754   4011    786     36    430       C  
ATOM   1096  O   SER A 904       0.729  41.360   5.832  1.00 40.46           O  
ANISOU 1096  O   SER A 904     5670   5574   4129    859     63    483       O  
ATOM   1097  CB  SER A 904       1.911  38.402   5.802  1.00 39.29           C  
ANISOU 1097  CB  SER A 904     5597   5508   3820    701    230    146       C  
ATOM   1098  OG  SER A 904       1.664  37.308   6.667  1.00 39.43           O  
ANISOU 1098  OG  SER A 904     5527   5494   3958    690    258     37       O  
ATOM   1099  N   ALA A 905       1.222  40.752   3.732  1.00 42.54           N  
ANISOU 1099  N   ALA A 905     6156   6024   3983    746     19    521       N  
ATOM   1100  CA  ALA A 905       1.689  42.084   3.329  1.00 43.77           C  
ANISOU 1100  CA  ALA A 905     6371   6117   4140    788     60    723       C  
ATOM   1101  C   ALA A 905       0.589  43.164   3.296  1.00 44.66           C  
ANISOU 1101  C   ALA A 905     6395   6189   4384    883   -103    925       C  
ATOM   1102  O   ALA A 905       0.879  44.357   3.385  1.00 45.85           O  
ANISOU 1102  O   ALA A 905     6540   6206   4674    942    -43   1081       O  
ATOM   1103  CB  ALA A 905       2.377  41.994   1.975  1.00 45.95           C  
ANISOU 1103  CB  ALA A 905     6836   6507   4113    711    117    786       C  
ATOM   1104  N   ASN A 906      -0.664  42.746   3.160  1.00 44.95           N  
ANISOU 1104  N   ASN A 906     6340   6319   4418    897   -302    921       N  
ATOM   1105  CA  ASN A 906      -1.791  43.666   3.263  1.00 46.06           C  
ANISOU 1105  CA  ASN A 906     6336   6400   4764   1005   -455   1101       C  
ATOM   1106  C   ASN A 906      -1.969  44.265   4.654  1.00 44.71           C  
ANISOU 1106  C   ASN A 906     6012   6027   4948   1094   -332   1038       C  
ATOM   1107  O   ASN A 906      -2.582  45.319   4.796  1.00 46.06           O  
ANISOU 1107  O   ASN A 906     6075   6074   5351   1199   -372   1190       O  
ATOM   1108  CB  ASN A 906      -3.078  42.962   2.880  1.00 47.43           C  
ANISOU 1108  CB  ASN A 906     6402   6723   4896    986   -697   1081       C  
ATOM   1109  CG  ASN A 906      -3.085  42.515   1.439  1.00 49.96           C  
ANISOU 1109  CG  ASN A 906     6875   7270   4836    890   -867   1139       C  
ATOM   1110  OD1 ASN A 906      -2.702  43.267   0.527  1.00 51.19           O  
ANISOU 1110  OD1 ASN A 906     7167   7475   4806    900   -899   1361       O  
ATOM   1111  ND2 ASN A 906      -3.522  41.281   1.219  1.00 50.13           N  
ANISOU 1111  ND2 ASN A 906     6883   7430   4733    785   -964    936       N  
ATOM   1112  N   TYR A 907      -1.442  43.597   5.675  1.00 42.28           N  
ANISOU 1112  N   TYR A 907     5697   5687   4681   1052   -179    818       N  
ATOM   1113  CA  TYR A 907      -1.589  44.066   7.045  1.00 41.61           C  
ANISOU 1113  CA  TYR A 907     5497   5456   4856   1112    -55    721       C  
ATOM   1114  C   TYR A 907      -0.551  45.114   7.415  1.00 41.83           C  
ANISOU 1114  C   TYR A 907     5582   5329   4979   1124     96    733       C  
ATOM   1115  O   TYR A 907      -0.528  45.593   8.549  1.00 41.21           O  
ANISOU 1115  O   TYR A 907     5436   5135   5085   1153    208    618       O  
ATOM   1116  CB  TYR A 907      -1.556  42.877   8.001  1.00 39.96           C  
ANISOU 1116  CB  TYR A 907     5255   5305   4620   1058     17    515       C  
ATOM   1117  CG  TYR A 907      -2.765  41.996   7.813  1.00 41.00           C  
ANISOU 1117  CG  TYR A 907     5279   5533   4764   1046   -111    493       C  
ATOM   1118  CD1 TYR A 907      -4.003  42.351   8.353  1.00 41.93           C  
ANISOU 1118  CD1 TYR A 907     5215   5599   5118   1120   -140    512       C  
ATOM   1119  CD2 TYR A 907      -2.693  40.838   7.054  1.00 41.35           C  
ANISOU 1119  CD2 TYR A 907     5388   5706   4618    954   -191    440       C  
ATOM   1120  CE1 TYR A 907      -5.120  41.558   8.158  1.00 42.97           C  
ANISOU 1120  CE1 TYR A 907     5212   5810   5303   1097   -261    494       C  
ATOM   1121  CE2 TYR A 907      -3.807  40.036   6.864  1.00 42.32           C  
ANISOU 1121  CE2 TYR A 907     5394   5902   4782    920   -318    397       C  
ATOM   1122  CZ  TYR A 907      -5.011  40.402   7.415  1.00 43.43           C  
ANISOU 1122  CZ  TYR A 907     5337   5996   5168    989   -361    434       C  
ATOM   1123  OH  TYR A 907      -6.110  39.601   7.213  1.00 46.71           O  
ANISOU 1123  OH  TYR A 907     5605   6478   5663    943   -488    391       O  
ATOM   1124  N   CYS A 908       0.304  45.458   6.451  1.00 42.68           N  
ANISOU 1124  N   CYS A 908     5818   5442   4956   1088    111    860       N  
ATOM   1125  CA  CYS A 908       1.240  46.572   6.572  1.00 42.74           C  
ANISOU 1125  CA  CYS A 908     5863   5279   5095   1089    247    912       C  
ATOM   1126  C   CYS A 908       0.551  47.906   6.291  1.00 44.50           C  
ANISOU 1126  C   CYS A 908     6020   5333   5554   1191    211   1119       C  
ATOM   1127  O   CYS A 908       1.075  48.962   6.630  1.00 45.00           O  
ANISOU 1127  O   CYS A 908     6070   5192   5835   1205    336   1135       O  
ATOM   1128  CB  CYS A 908       2.399  46.398   5.583  1.00 43.15           C  
ANISOU 1128  CB  CYS A 908     6064   5393   4935   1007    312    993       C  
ATOM   1129  SG  CYS A 908       3.367  44.887   5.792  1.00 42.06           S  
ANISOU 1129  SG  CYS A 908     5982   5401   4595    903    390    772       S  
ATOM   1130  N   HIS A 909      -0.608  47.862   5.643  1.00 45.89           N  
ANISOU 1130  N   HIS A 909     6138   5581   5715   1261     32   1283       N  
ATOM   1131  CA  HIS A 909      -1.328  49.075   5.255  1.00 48.60           C  
ANISOU 1131  CA  HIS A 909     6395   5763   6308   1380    -31   1538       C  
ATOM   1132  C   HIS A 909      -0.428  50.143   4.642  1.00 51.12           C  
ANISOU 1132  C   HIS A 909     6817   5925   6681   1374     73   1748       C  
ATOM   1133  O   HIS A 909      -0.582  51.327   4.937  1.00 53.31           O  
ANISOU 1133  O   HIS A 909     7008   5939   7308   1458    152   1844       O  
ATOM   1134  CB  HIS A 909      -2.066  49.647   6.459  1.00 48.23           C  
ANISOU 1134  CB  HIS A 909     6163   5519   6642   1473     52   1402       C  
ATOM   1135  CG  HIS A 909      -3.237  48.828   6.869  1.00 47.47           C  
ANISOU 1135  CG  HIS A 909     5926   5547   6562   1505    -54   1297       C  
ATOM   1136  ND1 HIS A 909      -3.126  47.746   7.712  1.00 45.24           N  
ANISOU 1136  ND1 HIS A 909     5652   5389   6148   1426     10   1029       N  
ATOM   1137  CD2 HIS A 909      -4.540  48.908   6.525  1.00 49.42           C  
ANISOU 1137  CD2 HIS A 909     6004   5811   6962   1603   -222   1446       C  
ATOM   1138  CE1 HIS A 909      -4.316  47.200   7.880  1.00 45.76           C  
ANISOU 1138  CE1 HIS A 909     5566   5530   6290   1466    -87   1007       C  
ATOM   1139  NE2 HIS A 909      -5.192  47.891   7.175  1.00 48.34           N  
ANISOU 1139  NE2 HIS A 909     5770   5796   6798   1571   -234   1244       N  
ATOM   1140  N   THR A 910       0.497  49.726   3.783  1.00 52.03           N  
ANISOU 1140  N   THR A 910     7107   6181   6479   1274     99   1814       N  
ATOM   1141  CA  THR A 910       1.428  50.654   3.168  1.00 54.75           C  
ANISOU 1141  CA  THR A 910     7553   6386   6862   1249    235   2022       C  
ATOM   1142  C   THR A 910       0.731  51.322   2.002  1.00 58.94           C  
ANISOU 1142  C   THR A 910     8113   6930   7351   1333     79   2433       C  
ATOM   1143  O   THR A 910      -0.117  50.716   1.352  1.00 58.46           O  
ANISOU 1143  O   THR A 910     8062   7099   7050   1353   -149   2529       O  
ATOM   1144  CB  THR A 910       2.706  49.965   2.653  1.00 54.67           C  
ANISOU 1144  CB  THR A 910     7710   6521   6538   1110    362   1948       C  
ATOM   1145  OG1 THR A 910       2.414  49.275   1.439  1.00 57.96           O  
ANISOU 1145  OG1 THR A 910     8264   7206   6552   1078    226   2091       O  
ATOM   1146  CG2 THR A 910       3.266  48.975   3.670  1.00 50.93           C  
ANISOU 1146  CG2 THR A 910     7200   6110   6041   1037    441   1577       C  
ATOM   1147  N   SER A 911       1.123  52.567   1.746  1.00 63.19           N  
ANISOU 1147  N   SER A 911     8658   7218   8131   1372    199   2681       N  
ATOM   1148  CA  SER A 911       0.451  53.452   0.804  1.00 68.36           C  
ANISOU 1148  CA  SER A 911     9307   7808   8855   1482     65   3133       C  
ATOM   1149  C   SER A 911       1.339  53.746  -0.392  1.00 71.54           C  
ANISOU 1149  C   SER A 911     9923   8279   8980   1404    156   3439       C  
ATOM   1150  O   SER A 911       2.551  53.528  -0.345  1.00 71.45           O  
ANISOU 1150  O   SER A 911    10020   8264   8862   1277    382   3287       O  
ATOM   1151  CB  SER A 911       0.150  54.774   1.499  1.00 70.41           C  
ANISOU 1151  CB  SER A 911     9390   7656   9703   1603    173   3212       C  
ATOM   1152  OG  SER A 911       1.347  55.319   2.048  1.00 70.06           O  
ANISOU 1152  OG  SER A 911     9379   7372   9869   1513    461   3051       O  
ATOM   1153  N   GLN A 912       0.739  54.270  -1.453  1.00 75.57           N  
ANISOU 1153  N   GLN A 912    10482   8847   9384   1483    -15   3891       N  
ATOM   1154  CA  GLN A 912       1.507  54.742  -2.597  1.00 78.97           C  
ANISOU 1154  CA  GLN A 912    11119   9315   9568   1421     95   4256       C  
ATOM   1155  C   GLN A 912       2.456  55.876  -2.191  1.00 79.71           C  
ANISOU 1155  C   GLN A 912    11177   8999  10107   1408    419   4324       C  
ATOM   1156  O   GLN A 912       3.532  56.024  -2.772  1.00 80.30           O  
ANISOU 1156  O   GLN A 912    11412   9079  10018   1296    641   4436       O  
ATOM   1157  CB  GLN A 912       0.573  55.217  -3.703  1.00 84.25           C  
ANISOU 1157  CB  GLN A 912    11824  10106  10080   1528   -182   4779       C  
ATOM   1158  CG  GLN A 912      -0.339  54.132  -4.249  1.00 85.24           C  
ANISOU 1158  CG  GLN A 912    11987  10659   9739   1511   -532   4725       C  
ATOM   1159  CD  GLN A 912      -0.782  54.407  -5.677  1.00 92.24           C  
ANISOU 1159  CD  GLN A 912    13027  11800  10220   1533   -780   5245       C  
ATOM   1160  OE1 GLN A 912      -1.152  55.535  -6.032  1.00 97.50           O  
ANISOU 1160  OE1 GLN A 912    13629  12272  11144   1667   -848   5729       O  
ATOM   1161  NE2 GLN A 912      -0.742  53.376  -6.511  1.00 93.47           N  
ANISOU 1161  NE2 GLN A 912    13389  12391   9732   1398   -915   5153       N  
ATOM   1162  N   GLY A 913       2.052  56.659  -1.186  1.00 79.71           N  
ANISOU 1162  N   GLY A 913    10961   8642  10683   1513    462   4229       N  
ATOM   1163  CA  GLY A 913       2.846  57.780  -0.668  1.00 80.17           C  
ANISOU 1163  CA  GLY A 913    10951   8267  11243   1492    756   4229       C  
ATOM   1164  C   GLY A 913       4.078  57.379   0.125  1.00 76.98           C  
ANISOU 1164  C   GLY A 913    10558   7827  10861   1326    997   3780       C  
ATOM   1165  O   GLY A 913       5.130  57.985  -0.028  1.00 78.33           O  
ANISOU 1165  O   GLY A 913    10769   7800  11192   1230   1245   3852       O  
ATOM   1166  N   ASP A 914       3.946  56.377   0.993  1.00 73.60           N  
ANISOU 1166  N   ASP A 914    10076   7581  10305   1290    921   3337       N  
ATOM   1167  CA  ASP A 914       5.101  55.799   1.700  1.00 71.00           C  
ANISOU 1167  CA  ASP A 914     9755   7290   9930   1137   1092   2936       C  
ATOM   1168  C   ASP A 914       5.081  54.267   1.519  1.00 65.88           C  
ANISOU 1168  C   ASP A 914     9201   7053   8776   1082    965   2739       C  
ATOM   1169  O   ASP A 914       4.602  53.533   2.385  1.00 62.58           O  
ANISOU 1169  O   ASP A 914     8700   6739   8336   1101    856   2431       O  
ATOM   1170  CB  ASP A 914       5.113  56.206   3.190  1.00 71.20           C  
ANISOU 1170  CB  ASP A 914     9602   7062  10386   1137   1164   2555       C  
ATOM   1171  CG  ASP A 914       6.378  55.713   3.938  1.00 70.85           C  
ANISOU 1171  CG  ASP A 914     9546   7057  10316    974   1305   2179       C  
ATOM   1172  OD1 ASP A 914       7.437  55.511   3.287  1.00 72.17           O  
ANISOU 1172  OD1 ASP A 914     9799   7294  10327    864   1435   2265       O  
ATOM   1173  OD2 ASP A 914       6.309  55.526   5.181  1.00 68.89           O  
ANISOU 1173  OD2 ASP A 914     9193   6779  10202    956   1287   1807       O  
ATOM   1174  N   PRO A 915       5.613  53.786   0.383  1.00 64.36           N  
ANISOU 1174  N   PRO A 915     9187   7083   8184   1007   1007   2916       N  
ATOM   1175  CA  PRO A 915       5.417  52.413  -0.041  1.00 61.91           C  
ANISOU 1175  CA  PRO A 915     8983   7142   7396    966    881   2781       C  
ATOM   1176  C   PRO A 915       6.491  51.440   0.451  1.00 58.15           C  
ANISOU 1176  C   PRO A 915     8509   6758   6825    845   1033   2420       C  
ATOM   1177  O   PRO A 915       6.884  50.543  -0.286  1.00 57.94           O  
ANISOU 1177  O   PRO A 915     8618   6970   6426    771   1074   2387       O  
ATOM   1178  CB  PRO A 915       5.471  52.544  -1.557  1.00 64.99           C  
ANISOU 1178  CB  PRO A 915     9578   7701   7413    942    882   3164       C  
ATOM   1179  CG  PRO A 915       6.529  53.575  -1.759  1.00 67.24           C  
ANISOU 1179  CG  PRO A 915     9881   7725   7940    887   1168   3353       C  
ATOM   1180  CD  PRO A 915       6.427  54.526  -0.598  1.00 66.93           C  
ANISOU 1180  CD  PRO A 915     9631   7311   8486    949   1207   3252       C  
ATOM   1181  N   ILE A 916       6.949  51.616   1.685  1.00 55.41           N  
ANISOU 1181  N   ILE A 916     8009   6227   6817    826   1112   2150       N  
ATOM   1182  CA  ILE A 916       7.888  50.693   2.312  1.00 52.42           C  
ANISOU 1182  CA  ILE A 916     7587   5930   6398    733   1204   1825       C  
ATOM   1183  C   ILE A 916       7.175  50.008   3.474  1.00 48.71           C  
ANISOU 1183  C   ILE A 916     7009   5526   5970    782   1037   1542       C  
ATOM   1184  O   ILE A 916       6.417  50.650   4.194  1.00 47.62           O  
ANISOU 1184  O   ILE A 916     6776   5247   6069    856    956   1516       O  
ATOM   1185  CB  ILE A 916       9.146  51.418   2.836  1.00 53.26           C  
ANISOU 1185  CB  ILE A 916     7593   5801   6841    644   1417   1744       C  
ATOM   1186  CG1 ILE A 916       9.780  52.278   1.741  1.00 56.99           C  
ANISOU 1186  CG1 ILE A 916     8154   6154   7345    595   1618   2063       C  
ATOM   1187  CG2 ILE A 916      10.169  50.421   3.357  1.00 51.57           C  
ANISOU 1187  CG2 ILE A 916     7315   5695   6583    556   1489   1461       C  
ATOM   1188  CD1 ILE A 916      10.599  51.496   0.742  1.00 58.10           C  
ANISOU 1188  CD1 ILE A 916     8422   6495   7158    511   1779   2113       C  
ATOM   1189  N   GLY A 917       7.417  48.710   3.656  1.00 46.29           N  
ANISOU 1189  N   GLY A 917     6716   5417   5452    741   1011   1337       N  
ATOM   1190  CA  GLY A 917       6.702  47.941   4.670  1.00 43.91           C  
ANISOU 1190  CA  GLY A 917     6331   5199   5154    783    866   1113       C  
ATOM   1191  C   GLY A 917       7.592  46.976   5.407  1.00 42.30           C  
ANISOU 1191  C   GLY A 917     6069   5061   4940    719    923    869       C  
ATOM   1192  O   GLY A 917       8.635  46.588   4.904  1.00 43.20           O  
ANISOU 1192  O   GLY A 917     6216   5210   4988    650   1056    864       O  
ATOM   1193  N   LEU A 918       7.172  46.580   6.604  1.00 40.92           N  
ANISOU 1193  N   LEU A 918     5801   4906   4839    745    831    684       N  
ATOM   1194  CA  LEU A 918       7.909  45.606   7.388  1.00 39.20           C  
ANISOU 1194  CA  LEU A 918     5519   4764   4609    701    845    496       C  
ATOM   1195  C   LEU A 918       7.080  44.343   7.574  1.00 38.26           C  
ANISOU 1195  C   LEU A 918     5413   4801   4324    737    739    423       C  
ATOM   1196  O   LEU A 918       5.904  44.416   7.890  1.00 37.62           O  
ANISOU 1196  O   LEU A 918     5317   4736   4238    794    636    425       O  
ATOM   1197  CB  LEU A 918       8.288  46.201   8.739  1.00 39.20           C  
ANISOU 1197  CB  LEU A 918     5406   4668   4818    678    835    345       C  
ATOM   1198  CG  LEU A 918       9.271  47.381   8.696  1.00 40.94           C  
ANISOU 1198  CG  LEU A 918     5581   4709   5265    610    946    363       C  
ATOM   1199  CD1 LEU A 918       9.495  47.990  10.084  1.00 41.00           C  
ANISOU 1199  CD1 LEU A 918     5485   4637   5454    569    906    161       C  
ATOM   1200  CD2 LEU A 918      10.589  46.969   8.057  1.00 41.02           C  
ANISOU 1200  CD2 LEU A 918     5572   4739   5274    538   1067    400       C  
ATOM   1201  N   ILE A 919       7.699  43.187   7.337  1.00 39.10           N  
ANISOU 1201  N   ILE A 919     5529   4995   4331    703    785    362       N  
ATOM   1202  CA  ILE A 919       7.063  41.898   7.571  1.00 39.49           C  
ANISOU 1202  CA  ILE A 919     5573   5151   4277    721    712    281       C  
ATOM   1203  C   ILE A 919       8.033  41.013   8.325  1.00 39.31           C  
ANISOU 1203  C   ILE A 919     5465   5136   4334    701    759    183       C  
ATOM   1204  O   ILE A 919       9.228  41.030   8.049  1.00 39.76           O  
ANISOU 1204  O   ILE A 919     5492   5153   4462    664    869    183       O  
ATOM   1205  CB  ILE A 919       6.662  41.205   6.264  1.00 41.68           C  
ANISOU 1205  CB  ILE A 919     5963   5520   4352    702    718    313       C  
ATOM   1206  CG1 ILE A 919       5.845  42.155   5.392  1.00 45.18           C  
ANISOU 1206  CG1 ILE A 919     6489   5978   4699    722    644    466       C  
ATOM   1207  CG2 ILE A 919       5.798  39.989   6.549  1.00 40.99           C  
ANISOU 1207  CG2 ILE A 919     5852   5507   4213    711    630    217       C  
ATOM   1208  CD1 ILE A 919       5.241  41.515   4.153  1.00 47.47           C  
ANISOU 1208  CD1 ILE A 919     6895   6407   4731    690    585    489       C  
ATOM   1209  N   LEU A 920       7.507  40.251   9.281  1.00 38.54           N  
ANISOU 1209  N   LEU A 920     5313   5085   4244    728    679    124       N  
ATOM   1210  CA  LEU A 920       8.295  39.297  10.048  1.00 38.50           C  
ANISOU 1210  CA  LEU A 920     5219   5094   4313    725    692     81       C  
ATOM   1211  C   LEU A 920       8.238  37.915   9.431  1.00 38.82           C  
ANISOU 1211  C   LEU A 920     5279   5146   4324    727    747     58       C  
ATOM   1212  O   LEU A 920       7.260  37.553   8.755  1.00 38.01           O  
ANISOU 1212  O   LEU A 920     5253   5074   4114    722    727     39       O  
ATOM   1213  CB  LEU A 920       7.759  39.166  11.466  1.00 38.88           C  
ANISOU 1213  CB  LEU A 920     5213   5192   4367    749    593     59       C  
ATOM   1214  CG  LEU A 920       7.801  40.424  12.320  1.00 39.62           C  
ANISOU 1214  CG  LEU A 920     5286   5275   4492    736    548     19       C  
ATOM   1215  CD1 LEU A 920       6.684  40.381  13.346  1.00 39.42           C  
ANISOU 1215  CD1 LEU A 920     5266   5310   4400    763    494    -15       C  
ATOM   1216  CD2 LEU A 920       9.164  40.565  12.978  1.00 40.77           C  
ANISOU 1216  CD2 LEU A 920     5339   5426   4725    694    527     -6       C  
ATOM   1217  N   LEU A 921       9.304  37.157   9.680  1.00 38.37           N  
ANISOU 1217  N   LEU A 921     5134   5054   4390    730    812     50       N  
ATOM   1218  CA  LEU A 921       9.299  35.720   9.530  1.00 38.37           C  
ANISOU 1218  CA  LEU A 921     5108   5021   4447    745    868     19       C  
ATOM   1219  C   LEU A 921       9.543  35.133  10.901  1.00 37.14           C  
ANISOU 1219  C   LEU A 921     4832   4870   4408    787    787     87       C  
ATOM   1220  O   LEU A 921      10.562  35.397  11.523  1.00 36.50           O  
ANISOU 1220  O   LEU A 921     4645   4790   4430    797    758    134       O  
ATOM   1221  CB  LEU A 921      10.393  35.274   8.575  1.00 40.66           C  
ANISOU 1221  CB  LEU A 921     5382   5239   4827    729   1046    -26       C  
ATOM   1222  CG  LEU A 921      10.072  35.420   7.095  1.00 42.04           C  
ANISOU 1222  CG  LEU A 921     5712   5435   4825    676   1154   -102       C  
ATOM   1223  CD1 LEU A 921      11.317  35.148   6.275  1.00 43.83           C  
ANISOU 1223  CD1 LEU A 921     5916   5594   5142    656   1379   -154       C  
ATOM   1224  CD2 LEU A 921       8.967  34.446   6.702  1.00 43.13           C  
ANISOU 1224  CD2 LEU A 921     5926   5591   4867    657   1122   -193       C  
ATOM   1225  N   GLY A 922       8.587  34.357  11.385  1.00 37.39           N  
ANISOU 1225  N   GLY A 922     4875   4914   4418    804    742    105       N  
ATOM   1226  CA  GLY A 922       8.710  33.699  12.680  1.00 37.53           C  
ANISOU 1226  CA  GLY A 922     4801   4949   4509    843    675    212       C  
ATOM   1227  C   GLY A 922       8.659  32.197  12.544  1.00 37.70           C  
ANISOU 1227  C   GLY A 922     4775   4859   4689    868    755    243       C  
ATOM   1228  O   GLY A 922       7.985  31.667  11.668  1.00 36.74           O  
ANISOU 1228  O   GLY A 922     4715   4674   4570    837    832    143       O  
ATOM   1229  N   GLU A 923       9.406  31.519  13.405  1.00 39.55           N  
ANISOU 1229  N   GLU A 923     4891   5064   5071    920    728    383       N  
ATOM   1230  CA  GLU A 923       9.301  30.080  13.563  1.00 41.17           C  
ANISOU 1230  CA  GLU A 923     5031   5134   5474    958    799    465       C  
ATOM   1231  C   GLU A 923       8.098  29.855  14.471  1.00 41.66           C  
ANISOU 1231  C   GLU A 923     5140   5264   5425    948    738    556       C  
ATOM   1232  O   GLU A 923       8.061  30.354  15.598  1.00 41.19           O  
ANISOU 1232  O   GLU A 923     5080   5349   5221    958    623    672       O  
ATOM   1233  CB  GLU A 923      10.565  29.518  14.194  1.00 42.76           C  
ANISOU 1233  CB  GLU A 923     5068   5281   5897   1034    772    637       C  
ATOM   1234  CG  GLU A 923      10.610  28.005  14.219  1.00 45.81           C  
ANISOU 1234  CG  GLU A 923     5365   5466   6574   1090    879    736       C  
ATOM   1235  CD  GLU A 923      11.825  27.457  14.964  1.00 49.40           C  
ANISOU 1235  CD  GLU A 923     5625   5867   7278   1188    818    969       C  
ATOM   1236  OE1 GLU A 923      12.869  28.152  15.025  1.00 49.91           O  
ANISOU 1236  OE1 GLU A 923     5597   6009   7357   1202    741    979       O  
ATOM   1237  OE2 GLU A 923      11.736  26.318  15.490  1.00 51.72           O  
ANISOU 1237  OE2 GLU A 923     5839   6030   7782   1250    843   1161       O  
ATOM   1238  N   VAL A 924       7.103  29.135  13.962  1.00 42.05           N  
ANISOU 1238  N   VAL A 924     5226   5215   5533    912    824    481       N  
ATOM   1239  CA  VAL A 924       5.881  28.880  14.701  1.00 42.23           C  
ANISOU 1239  CA  VAL A 924     5271   5277   5494    891    807    555       C  
ATOM   1240  C   VAL A 924       5.787  27.385  14.977  1.00 44.26           C  
ANISOU 1240  C   VAL A 924     5450   5352   6013    910    904    680       C  
ATOM   1241  O   VAL A 924       5.853  26.571  14.056  1.00 45.29           O  
ANISOU 1241  O   VAL A 924     5556   5298   6352    889   1015    559       O  
ATOM   1242  CB  VAL A 924       4.634  29.367  13.929  1.00 41.40           C  
ANISOU 1242  CB  VAL A 924     5242   5208   5278    820    809    375       C  
ATOM   1243  CG1 VAL A 924       3.412  29.368  14.840  1.00 41.80           C  
ANISOU 1243  CG1 VAL A 924     5288   5324   5270    802    800    456       C  
ATOM   1244  CG2 VAL A 924       4.852  30.768  13.370  1.00 40.13           C  
ANISOU 1244  CG2 VAL A 924     5153   5166   4928    810    738    264       C  
ATOM   1245  N   ALA A 925       5.648  27.027  16.249  1.00 46.04           N  
ANISOU 1245  N   ALA A 925     5641   5623   6227    946    875    922       N  
ATOM   1246  CA  ALA A 925       5.502  25.626  16.645  1.00 48.63           C  
ANISOU 1246  CA  ALA A 925     5891   5761   6824    969    975   1105       C  
ATOM   1247  C   ALA A 925       4.016  25.253  16.660  1.00 48.66           C  
ANISOU 1247  C   ALA A 925     5918   5717   6851    890   1062   1058       C  
ATOM   1248  O   ALA A 925       3.316  25.443  17.658  1.00 48.65           O  
ANISOU 1248  O   ALA A 925     5942   5840   6702    879   1056   1205       O  
ATOM   1249  CB  ALA A 925       6.145  25.385  18.003  1.00 50.82           C  
ANISOU 1249  CB  ALA A 925     6120   6123   7064   1047    895   1442       C  
ATOM   1250  N   LEU A 926       3.553  24.710  15.538  1.00 48.30           N  
ANISOU 1250  N   LEU A 926     5859   5497   6995    823   1150    837       N  
ATOM   1251  CA  LEU A 926       2.128  24.501  15.292  1.00 47.45           C  
ANISOU 1251  CA  LEU A 926     5746   5354   6926    724   1198    722       C  
ATOM   1252  C   LEU A 926       1.597  23.242  15.958  1.00 49.90           C  
ANISOU 1252  C   LEU A 926     5971   5469   7519    705   1332    912       C  
ATOM   1253  O   LEU A 926       0.432  23.188  16.332  1.00 50.73           O  
ANISOU 1253  O   LEU A 926     6050   5596   7627    639   1376    936       O  
ATOM   1254  CB  LEU A 926       1.868  24.424  13.785  1.00 46.23           C  
ANISOU 1254  CB  LEU A 926     5613   5117   6833    638   1204    390       C  
ATOM   1255  CG  LEU A 926       2.158  25.711  13.016  1.00 43.58           C  
ANISOU 1255  CG  LEU A 926     5373   4976   6207    639   1084    221       C  
ATOM   1256  CD1 LEU A 926       2.302  25.479  11.526  1.00 43.53           C  
ANISOU 1256  CD1 LEU A 926     5413   4895   6229    567   1108    -62       C  
ATOM   1257  CD2 LEU A 926       1.055  26.712  13.293  1.00 43.32           C  
ANISOU 1257  CD2 LEU A 926     5359   5130   5967    611    985    212       C  
ATOM   1258  N   GLY A 927       2.442  22.225  16.091  1.00 51.95           N  
ANISOU 1258  N   GLY A 927     6167   5515   8056    764   1415   1058       N  
ATOM   1259  CA  GLY A 927       1.996  20.927  16.576  1.00 54.66           C  
ANISOU 1259  CA  GLY A 927     6419   5604   8744    745   1569   1245       C  
ATOM   1260  C   GLY A 927       0.823  20.355  15.787  1.00 55.46           C  
ANISOU 1260  C   GLY A 927     6475   5531   9066    599   1666    988       C  
ATOM   1261  O   GLY A 927       0.763  20.466  14.561  1.00 54.76           O  
ANISOU 1261  O   GLY A 927     6409   5406   8989    526   1640    640       O  
ATOM   1262  N   ASN A 928      -0.114  19.745  16.505  1.00 57.23           N  
ANISOU 1262  N   ASN A 928     6631   5659   9452    546   1775   1165       N  
ATOM   1263  CA  ASN A 928      -1.290  19.136  15.909  1.00 58.60           C  
ANISOU 1263  CA  ASN A 928     6721   5655   9888    391   1864    948       C  
ATOM   1264  C   ASN A 928      -2.264  20.262  15.590  1.00 55.44           C  
ANISOU 1264  C   ASN A 928     6349   5528   9186    319   1731    744       C  
ATOM   1265  O   ASN A 928      -2.744  20.951  16.489  1.00 54.19           O  
ANISOU 1265  O   ASN A 928     6206   5575   8805    350   1718    922       O  
ATOM   1266  CB  ASN A 928      -1.879  18.107  16.890  1.00 63.00           C  
ANISOU 1266  CB  ASN A 928     7177   6000  10758    365   2054   1262       C  
ATOM   1267  CG  ASN A 928      -2.965  17.232  16.274  1.00 66.68           C  
ANISOU 1267  CG  ASN A 928     7515   6197  11622    190   2172   1041       C  
ATOM   1268  OD1 ASN A 928      -3.491  17.524  15.204  1.00 67.75           O  
ANISOU 1268  OD1 ASN A 928     7639   6374  11728     76   2074    652       O  
ATOM   1269  ND2 ASN A 928      -3.320  16.157  16.968  1.00 70.12           N  
ANISOU 1269  ND2 ASN A 928     7848   6359  12434    160   2375   1303       N  
ATOM   1270  N   MET A 929      -2.513  20.480  14.301  1.00 53.97           N  
ANISOU 1270  N   MET A 929     6172   5350   8981    228   1633    374       N  
ATOM   1271  CA  MET A 929      -3.346  21.603  13.855  1.00 51.67           C  
ANISOU 1271  CA  MET A 929     5895   5315   8419    179   1470    197       C  
ATOM   1272  C   MET A 929      -4.808  21.209  13.868  1.00 52.21           C  
ANISOU 1272  C   MET A 929     5811   5311   8715     41   1507    128       C  
ATOM   1273  O   MET A 929      -5.137  20.052  13.674  1.00 54.12           O  
ANISOU 1273  O   MET A 929     5953   5286   9322    -62   1622     64       O  
ATOM   1274  CB  MET A 929      -2.963  22.046  12.436  1.00 51.12           C  
ANISOU 1274  CB  MET A 929     5913   5323   8187    140   1325   -131       C  
ATOM   1275  CG  MET A 929      -1.493  22.397  12.283  1.00 50.49           C  
ANISOU 1275  CG  MET A 929     5959   5289   7935    260   1317    -94       C  
ATOM   1276  SD  MET A 929      -1.037  22.999  10.646  1.00 50.72           S  
ANISOU 1276  SD  MET A 929     6112   5435   7721    210   1194   -445       S  
ATOM   1277  CE  MET A 929      -0.929  21.456   9.733  1.00 53.51           C  
ANISOU 1277  CE  MET A 929     6432   5469   8430     84   1344   -727       C  
ATOM   1278  N   TYR A 930      -5.677  22.187  14.097  1.00 50.69           N  
ANISOU 1278  N   TYR A 930     5580   5337   8344     41   1418    135       N  
ATOM   1279  CA  TYR A 930      -7.118  21.994  14.025  1.00 51.87           C  
ANISOU 1279  CA  TYR A 930     5544   5449   8714    -86   1426     52       C  
ATOM   1280  C   TYR A 930      -7.532  22.697  12.763  1.00 51.36           C  
ANISOU 1280  C   TYR A 930     5471   5536   8507   -148   1176   -245       C  
ATOM   1281  O   TYR A 930      -7.370  23.907  12.665  1.00 49.61           O  
ANISOU 1281  O   TYR A 930     5329   5544   7976    -55   1044   -232       O  
ATOM   1282  CB  TYR A 930      -7.795  22.623  15.248  1.00 51.16           C  
ANISOU 1282  CB  TYR A 930     5396   5495   8545    -25   1531    294       C  
ATOM   1283  CG  TYR A 930      -9.281  22.338  15.424  1.00 52.62           C  
ANISOU 1283  CG  TYR A 930     5349   5614   9030   -146   1610    270       C  
ATOM   1284  CD1 TYR A 930      -9.824  21.078  15.137  1.00 54.66           C  
ANISOU 1284  CD1 TYR A 930     5452   5603   9712   -301   1703    194       C  
ATOM   1285  CD2 TYR A 930     -10.133  23.314  15.942  1.00 51.21           C  
ANISOU 1285  CD2 TYR A 930     5084   5616   8755   -106   1622    326       C  
ATOM   1286  CE1 TYR A 930     -11.169  20.821  15.328  1.00 56.03           C  
ANISOU 1286  CE1 TYR A 930     5383   5708  10198   -422   1783    178       C  
ATOM   1287  CE2 TYR A 930     -11.474  23.057  16.135  1.00 53.08           C  
ANISOU 1287  CE2 TYR A 930     5074   5785   9307   -211   1717    315       C  
ATOM   1288  CZ  TYR A 930     -11.986  21.810  15.829  1.00 55.59           C  
ANISOU 1288  CZ  TYR A 930     5231   5849  10039   -373   1791    247       C  
ATOM   1289  OH  TYR A 930     -13.326  21.557  16.022  1.00 57.66           O  
ANISOU 1289  OH  TYR A 930     5215   6036  10656   -490   1890    235       O  
ATOM   1290  N   GLU A 931      -8.049  21.948  11.795  1.00 53.88           N  
ANISOU 1290  N   GLU A 931     5696   5728   9047   -311   1106   -509       N  
ATOM   1291  CA  GLU A 931      -8.236  22.479  10.443  1.00 54.40           C  
ANISOU 1291  CA  GLU A 931     5796   5954   8917   -381    841   -797       C  
ATOM   1292  C   GLU A 931      -9.664  22.910  10.192  1.00 55.25           C  
ANISOU 1292  C   GLU A 931     5695   6177   9118   -471    671   -871       C  
ATOM   1293  O   GLU A 931     -10.569  22.113  10.290  1.00 57.56           O  
ANISOU 1293  O   GLU A 931     5786   6317   9765   -610    723   -937       O  
ATOM   1294  CB  GLU A 931      -7.778  21.453   9.419  1.00 56.76           C  
ANISOU 1294  CB  GLU A 931     6155   6083   9326   -513    842  -1091       C  
ATOM   1295  CG  GLU A 931      -6.371  20.966   9.727  1.00 56.78           C  
ANISOU 1295  CG  GLU A 931     6315   5931   9326   -407   1039   -995       C  
ATOM   1296  CD  GLU A 931      -5.644  20.426   8.518  1.00 59.57           C  
ANISOU 1296  CD  GLU A 931     6792   6201   9639   -488   1028  -1317       C  
ATOM   1297  OE1 GLU A 931      -6.308  19.892   7.601  1.00 63.45           O  
ANISOU 1297  OE1 GLU A 931     7226   6645  10235   -676    937  -1639       O  
ATOM   1298  OE2 GLU A 931      -4.398  20.530   8.485  1.00 59.81           O  
ANISOU 1298  OE2 GLU A 931     6971   6217   9536   -372   1118  -1266       O  
ATOM   1299  N   LEU A 932      -9.846  24.185   9.873  1.00 54.67           N  
ANISOU 1299  N   LEU A 932     5651   6358   8762   -387    472   -847       N  
ATOM   1300  CA  LEU A 932     -11.170  24.795   9.739  1.00 56.72           C  
ANISOU 1300  CA  LEU A 932     5685   6741   9124   -424    303   -856       C  
ATOM   1301  C   LEU A 932     -11.309  25.503   8.397  1.00 57.98           C  
ANISOU 1301  C   LEU A 932     5887   7116   9025   -457    -39  -1025       C  
ATOM   1302  O   LEU A 932     -10.348  26.095   7.899  1.00 56.85           O  
ANISOU 1302  O   LEU A 932     5976   7090   8532   -374   -106  -1026       O  
ATOM   1303  CB  LEU A 932     -11.404  25.817  10.852  1.00 54.84           C  
ANISOU 1303  CB  LEU A 932     5405   6593   8839   -257    418   -595       C  
ATOM   1304  CG  LEU A 932     -11.177  25.324  12.283  1.00 54.29           C  
ANISOU 1304  CG  LEU A 932     5344   6383   8901   -202    755   -378       C  
ATOM   1305  CD1 LEU A 932     -11.298  26.505  13.238  1.00 52.76           C  
ANISOU 1305  CD1 LEU A 932     5161   6328   8557    -45    846   -186       C  
ATOM   1306  CD2 LEU A 932     -12.143  24.198  12.647  1.00 56.48           C  
ANISOU 1306  CD2 LEU A 932     5385   6460   9615   -351    905   -385       C  
ATOM   1307  N   LYS A 933     -12.510  25.436   7.830  1.00 61.29           N  
ANISOU 1307  N   LYS A 933     6072   7591   9624   -583   -257  -1146       N  
ATOM   1308  CA  LYS A 933     -12.841  26.122   6.588  1.00 63.45           C  
ANISOU 1308  CA  LYS A 933     6348   8100   9656   -621   -628  -1260       C  
ATOM   1309  C   LYS A 933     -13.602  27.419   6.851  1.00 64.29           C  
ANISOU 1309  C   LYS A 933     6289   8358   9777   -479   -764  -1047       C  
ATOM   1310  O   LYS A 933     -13.830  28.198   5.928  1.00 65.98           O  
ANISOU 1310  O   LYS A 933     6509   8777   9781   -462  -1074  -1049       O  
ATOM   1311  CB  LYS A 933     -13.689  25.205   5.701  1.00 67.63           C  
ANISOU 1311  CB  LYS A 933     6704   8616  10374   -867   -842  -1548       C  
ATOM   1312  CG  LYS A 933     -12.929  23.994   5.183  1.00 68.61           C  
ANISOU 1312  CG  LYS A 933     7009   8591  10467  -1021   -736  -1826       C  
ATOM   1313  CD  LYS A 933     -13.829  22.845   4.768  1.00 72.42           C  
ANISOU 1313  CD  LYS A 933     7269   8944  11302  -1282   -821  -2114       C  
ATOM   1314  CE  LYS A 933     -12.984  21.629   4.409  1.00 73.60           C  
ANISOU 1314  CE  LYS A 933     7603   8877  11483  -1412   -632  -2390       C  
ATOM   1315  NZ  LYS A 933     -13.741  20.575   3.679  1.00 77.97           N  
ANISOU 1315  NZ  LYS A 933     7995   9333  12295  -1703   -769  -2771       N  
ATOM   1316  N   HIS A 934     -14.009  27.644   8.101  1.00 64.47           N  
ANISOU 1316  N   HIS A 934     6164   8276  10054   -377   -520   -859       N  
ATOM   1317  CA  HIS A 934     -14.813  28.816   8.460  1.00 65.02           C  
ANISOU 1317  CA  HIS A 934     6038   8438  10227   -240   -585   -683       C  
ATOM   1318  C   HIS A 934     -14.419  29.358   9.829  1.00 61.39           C  
ANISOU 1318  C   HIS A 934     5652   7905   9767    -70   -243   -485       C  
ATOM   1319  O   HIS A 934     -13.865  28.640  10.654  1.00 60.81           O  
ANISOU 1319  O   HIS A 934     5689   7704   9712    -85     39   -456       O  
ATOM   1320  CB  HIS A 934     -16.304  28.463   8.462  1.00 69.61           C  
ANISOU 1320  CB  HIS A 934     6216   8981  11251   -352   -681   -727       C  
ATOM   1321  CG  HIS A 934     -16.782  27.845   7.186  1.00 74.21           C  
ANISOU 1321  CG  HIS A 934     6698   9646  11853   -554  -1039   -954       C  
ATOM   1322  ND1 HIS A 934     -17.061  26.499   7.072  1.00 77.50           N  
ANISOU 1322  ND1 HIS A 934     7016   9915  12512   -773   -990  -1165       N  
ATOM   1323  CD2 HIS A 934     -17.017  28.383   5.965  1.00 76.69           C  
ANISOU 1323  CD2 HIS A 934     7003  10181  11955   -582  -1457  -1008       C  
ATOM   1324  CE1 HIS A 934     -17.461  26.236   5.839  1.00 80.47           C  
ANISOU 1324  CE1 HIS A 934     7327  10425  12820   -941  -1367  -1381       C  
ATOM   1325  NE2 HIS A 934     -17.440  27.361   5.147  1.00 80.51           N  
ANISOU 1325  NE2 HIS A 934     7392  10674  12523   -828  -1666  -1278       N  
ATOM   1326  N   ALA A 935     -14.729  30.628  10.062  1.00 59.97           N  
ANISOU 1326  N   ALA A 935     5405   7807   9573     87   -275   -349       N  
ATOM   1327  CA  ALA A 935     -14.381  31.303  11.307  1.00 57.05           C  
ANISOU 1327  CA  ALA A 935     5117   7395   9165    241     29   -207       C  
ATOM   1328  C   ALA A 935     -15.016  30.602  12.502  1.00 57.34           C  
ANISOU 1328  C   ALA A 935     4986   7301   9497    195    356   -165       C  
ATOM   1329  O   ALA A 935     -16.177  30.227  12.460  1.00 59.74           O  
ANISOU 1329  O   ALA A 935     4981   7554  10161    113    338   -194       O  
ATOM   1330  CB  ALA A 935     -14.833  32.751  11.249  1.00 57.21           C  
ANISOU 1330  CB  ALA A 935     5032   7485   9221    399    -64   -108       C  
ATOM   1331  N   SER A 936     -14.238  30.430  13.563  1.00 55.37           N  
ANISOU 1331  N   SER A 936     4938   7008   9090    243    649    -84       N  
ATOM   1332  CA  SER A 936     -14.709  29.830  14.809  1.00 55.92           C  
ANISOU 1332  CA  SER A 936     4908   6979   9357    211    999      3       C  
ATOM   1333  C   SER A 936     -15.028  30.903  15.841  1.00 55.86           C  
ANISOU 1333  C   SER A 936     4869   7020   9334    349   1228     87       C  
ATOM   1334  O   SER A 936     -15.946  30.743  16.636  1.00 58.44           O  
ANISOU 1334  O   SER A 936     4994   7292   9919    330   1483    135       O  
ATOM   1335  CB  SER A 936     -13.619  28.931  15.377  1.00 54.94           C  
ANISOU 1335  CB  SER A 936     5039   6797   9038    177   1170     71       C  
ATOM   1336  OG  SER A 936     -12.404  29.660  15.551  1.00 52.19           O  
ANISOU 1336  OG  SER A 936     4976   6549   8305    296   1145    107       O  
ATOM   1337  N   HIS A 937     -14.238  31.972  15.835  1.00 53.56           N  
ANISOU 1337  N   HIS A 937     4782   6819   8748    478   1166     89       N  
ATOM   1338  CA  HIS A 937     -14.324  33.054  16.806  1.00 54.29           C  
ANISOU 1338  CA  HIS A 937     4902   6948   8776    604   1389    119       C  
ATOM   1339  C   HIS A 937     -14.002  32.667  18.238  1.00 54.68           C  
ANISOU 1339  C   HIS A 937     5094   7011   8669    592   1749    194       C  
ATOM   1340  O   HIS A 937     -14.340  33.396  19.151  1.00 56.20           O  
ANISOU 1340  O   HIS A 937     5270   7232   8850    663   1994    187       O  
ATOM   1341  CB  HIS A 937     -15.696  33.721  16.773  1.00 57.74           C  
ANISOU 1341  CB  HIS A 937     5000   7344   9595    656   1426     98       C  
ATOM   1342  CG  HIS A 937     -15.988  34.401  15.485  1.00 59.42           C  
ANISOU 1342  CG  HIS A 937     5083   7575   9919    706   1057     71       C  
ATOM   1343  ND1 HIS A 937     -15.316  35.537  15.081  1.00 58.51           N  
ANISOU 1343  ND1 HIS A 937     5127   7502   9599    827    912     76       N  
ATOM   1344  CD2 HIS A 937     -16.862  34.100  14.496  1.00 62.06           C  
ANISOU 1344  CD2 HIS A 937     5145   7901  10533    643    788     57       C  
ATOM   1345  CE1 HIS A 937     -15.769  35.909  13.897  1.00 59.70           C  
ANISOU 1345  CE1 HIS A 937     5124   7675   9885    847    577     97       C  
ATOM   1346  NE2 HIS A 937     -16.706  35.054  13.520  1.00 62.23           N  
ANISOU 1346  NE2 HIS A 937     5182   7982  10481    735    478     79       N  
ATOM   1347  N   ILE A 938     -13.347  31.536  18.459  1.00 54.08           N  
ANISOU 1347  N   ILE A 938     5164   6916   8468    506   1791    271       N  
ATOM   1348  CA  ILE A 938     -13.067  31.124  19.827  1.00 53.98           C  
ANISOU 1348  CA  ILE A 938     5286   6937   8284    493   2111    396       C  
ATOM   1349  C   ILE A 938     -11.612  30.765  19.932  1.00 52.30           C  
ANISOU 1349  C   ILE A 938     5367   6776   7725    501   2019    465       C  
ATOM   1350  O   ILE A 938     -10.968  30.451  18.932  1.00 50.96           O  
ANISOU 1350  O   ILE A 938     5255   6567   7541    483   1768    420       O  
ATOM   1351  CB  ILE A 938     -13.985  29.979  20.297  1.00 56.21           C  
ANISOU 1351  CB  ILE A 938     5379   7111   8863    380   2346    501       C  
ATOM   1352  CG1 ILE A 938     -13.718  28.697  19.504  1.00 55.85           C  
ANISOU 1352  CG1 ILE A 938     5310   6935   8974    267   2183    524       C  
ATOM   1353  CG2 ILE A 938     -15.439  30.408  20.178  1.00 58.18           C  
ANISOU 1353  CG2 ILE A 938     5290   7309   9503    377   2435    424       C  
ATOM   1354  CD1 ILE A 938     -14.731  27.601  19.741  1.00 58.42           C  
ANISOU 1354  CD1 ILE A 938     5395   7105   9694    135   2380    597       C  
ATOM   1355  N   SER A 939     -11.099  30.839  21.154  1.00 53.03           N  
ANISOU 1355  N   SER A 939     5641   6970   7535    526   2225    570       N  
ATOM   1356  CA  SER A 939      -9.669  30.744  21.403  1.00 51.53           C  
ANISOU 1356  CA  SER A 939     5713   6864   7000    554   2123    642       C  
ATOM   1357  C   SER A 939      -9.329  29.410  22.019  1.00 52.44           C  
ANISOU 1357  C   SER A 939     5890   6935   7098    493   2244    870       C  
ATOM   1358  O   SER A 939      -8.191  29.184  22.434  1.00 52.19           O  
ANISOU 1358  O   SER A 939     6048   6975   6804    518   2186    988       O  
ATOM   1359  CB  SER A 939      -9.247  31.860  22.351  1.00 51.82           C  
ANISOU 1359  CB  SER A 939     5917   7073   6699    621   2218    593       C  
ATOM   1360  OG  SER A 939      -9.855  33.080  21.967  1.00 51.98           O  
ANISOU 1360  OG  SER A 939     5833   7084   6830    680   2196    402       O  
ATOM   1361  N   LYS A 940     -10.317  28.523  22.053  1.00 54.27           N  
ANISOU 1361  N   LYS A 940     5938   7034   7647    411   2405    946       N  
ATOM   1362  CA  LYS A 940     -10.239  27.296  22.821  1.00 56.30           C  
ANISOU 1362  CA  LYS A 940     6226   7223   7941    350   2600   1205       C  
ATOM   1363  C   LYS A 940     -10.249  26.097  21.891  1.00 55.94           C  
ANISOU 1363  C   LYS A 940     6059   6939   8254    271   2495   1216       C  
ATOM   1364  O   LYS A 940     -11.174  25.923  21.100  1.00 57.61           O  
ANISOU 1364  O   LYS A 940     6051   7025   8811    199   2454   1067       O  
ATOM   1365  CB  LYS A 940     -11.409  27.252  23.805  1.00 59.77           C  
ANISOU 1365  CB  LYS A 940     6553   7687   8468    304   2954   1297       C  
ATOM   1366  CG  LYS A 940     -11.228  28.183  24.999  1.00 61.12           C  
ANISOU 1366  CG  LYS A 940     6908   8102   8213    364   3129   1317       C  
ATOM   1367  CD  LYS A 940     -10.596  27.484  26.202  1.00 64.26           C  
ANISOU 1367  CD  LYS A 940     7515   8610   8290    346   3290   1627       C  
ATOM   1368  CE  LYS A 940      -9.392  26.590  25.861  1.00 63.63           C  
ANISOU 1368  CE  LYS A 940     7542   8452   8180    360   3057   1807       C  
ATOM   1369  NZ  LYS A 940      -8.937  25.760  27.018  1.00 66.79           N  
ANISOU 1369  NZ  LYS A 940     8096   8930   8351    345   3214   2182       N  
ATOM   1370  N   LEU A 941      -9.216  25.272  21.992  1.00 55.22           N  
ANISOU 1370  N   LEU A 941     6100   6781   8098    281   2447   1382       N  
ATOM   1371  CA  LEU A 941      -9.027  24.152  21.085  1.00 55.19           C  
ANISOU 1371  CA  LEU A 941     6011   6529   8428    214   2357   1353       C  
ATOM   1372  C   LEU A 941      -9.431  22.844  21.716  1.00 57.73           C  
ANISOU 1372  C   LEU A 941     6250   6651   9033    133   2609   1609       C  
ATOM   1373  O   LEU A 941      -9.398  22.727  22.930  1.00 60.17           O  
ANISOU 1373  O   LEU A 941     6646   7051   9165    159   2816   1889       O  
ATOM   1374  CB  LEU A 941      -7.559  24.053  20.714  1.00 53.83           C  
ANISOU 1374  CB  LEU A 941     6011   6361   8081    290   2164   1368       C  
ATOM   1375  CG  LEU A 941      -7.057  25.259  19.935  1.00 50.95           C  
ANISOU 1375  CG  LEU A 941     5725   6151   7479    356   1918   1122       C  
ATOM   1376  CD1 LEU A 941      -5.550  25.189  19.780  1.00 49.46           C  
ANISOU 1376  CD1 LEU A 941     5695   5982   7115    433   1777   1174       C  
ATOM   1377  CD2 LEU A 941      -7.763  25.338  18.587  1.00 50.51           C  
ANISOU 1377  CD2 LEU A 941     5523   6005   7662    283   1774    841       C  
ATOM   1378  N   PRO A 942      -9.802  21.845  20.894  1.00 58.40           N  
ANISOU 1378  N   PRO A 942     6174   6462   9554     25   2597   1516       N  
ATOM   1379  CA  PRO A 942      -9.996  20.494  21.420  1.00 61.18           C  
ANISOU 1379  CA  PRO A 942     6452   6559  10233    -50   2835   1776       C  
ATOM   1380  C   PRO A 942      -8.701  19.935  21.983  1.00 61.65           C  
ANISOU 1380  C   PRO A 942     6698   6584  10140     48   2841   2073       C  
ATOM   1381  O   PRO A 942      -7.635  20.479  21.719  1.00 59.85           O  
ANISOU 1381  O   PRO A 942     6622   6492   9626    153   2631   2008       O  
ATOM   1382  CB  PRO A 942     -10.427  19.695  20.192  1.00 61.63           C  
ANISOU 1382  CB  PRO A 942     6322   6331  10761   -185   2747   1512       C  
ATOM   1383  CG  PRO A 942     -11.014  20.706  19.278  1.00 60.05           C  
ANISOU 1383  CG  PRO A 942     6036   6292  10485   -206   2524   1161       C  
ATOM   1384  CD  PRO A 942     -10.180  21.934  19.474  1.00 57.15           C  
ANISOU 1384  CD  PRO A 942     5883   6218   9612    -49   2376   1160       C  
ATOM   1385  N   LYS A 943      -8.799  18.854  22.745  1.00 65.41           N  
ANISOU 1385  N   LYS A 943     7144   6870  10837     14   3081   2415       N  
ATOM   1386  CA  LYS A 943      -7.653  18.286  23.447  1.00 67.02           C  
ANISOU 1386  CA  LYS A 943     7500   7048  10916    119   3094   2786       C  
ATOM   1387  C   LYS A 943      -6.620  17.728  22.455  1.00 65.73           C  
ANISOU 1387  C   LYS A 943     7336   6660  10975    161   2908   2652       C  
ATOM   1388  O   LYS A 943      -6.973  17.029  21.500  1.00 65.97           O  
ANISOU 1388  O   LYS A 943     7221   6394  11447     59   2921   2419       O  
ATOM   1389  CB  LYS A 943      -8.122  17.195  24.419  1.00 71.79           C  
ANISOU 1389  CB  LYS A 943     8049   7461  11767     65   3413   3216       C  
ATOM   1390  CG  LYS A 943      -7.044  16.686  25.369  1.00 74.52           C  
ANISOU 1390  CG  LYS A 943     8552   7836  11926    186   3428   3698       C  
ATOM   1391  CD  LYS A 943      -7.213  15.195  25.677  1.00 79.51           C  
ANISOU 1391  CD  LYS A 943     9075   8069  13067    136   3674   4065       C  
ATOM   1392  CE  LYS A 943      -5.876  14.464  25.843  1.00 81.08           C  
ANISOU 1392  CE  LYS A 943     9341   8118  13345    273   3567   4393       C  
ATOM   1393  NZ  LYS A 943      -4.927  14.645  24.697  1.00 77.77           N  
ANISOU 1393  NZ  LYS A 943     8911   7618  13017    343   3291   4039       N  
ATOM   1394  N   GLY A 944      -5.349  18.060  22.680  1.00 64.17           N  
ANISOU 1394  N   GLY A 944     7294   6612  10474    302   2741   2773       N  
ATOM   1395  CA  GLY A 944      -4.263  17.590  21.825  1.00 63.21           C  
ANISOU 1395  CA  GLY A 944     7168   6293  10553    362   2597   2665       C  
ATOM   1396  C   GLY A 944      -4.102  18.357  20.523  1.00 60.19           C  
ANISOU 1396  C   GLY A 944     6793   5985  10089    343   2387   2182       C  
ATOM   1397  O   GLY A 944      -3.400  17.908  19.626  1.00 61.01           O  
ANISOU 1397  O   GLY A 944     6877   5896  10406    357   2318   2012       O  
ATOM   1398  N   LYS A 945      -4.754  19.508  20.408  1.00 57.78           N  
ANISOU 1398  N   LYS A 945     6516   5952   9486    313   2302   1969       N  
ATOM   1399  CA  LYS A 945      -4.558  20.407  19.283  1.00 54.30           C  
ANISOU 1399  CA  LYS A 945     6107   5634   8888    313   2087   1583       C  
ATOM   1400  C   LYS A 945      -3.869  21.636  19.833  1.00 52.86           C  
ANISOU 1400  C   LYS A 945     6078   5783   8223    428   1953   1645       C  
ATOM   1401  O   LYS A 945      -4.235  22.134  20.899  1.00 53.38           O  
ANISOU 1401  O   LYS A 945     6192   6045   8042    449   2029   1824       O  
ATOM   1402  CB  LYS A 945      -5.887  20.821  18.673  1.00 53.66           C  
ANISOU 1402  CB  LYS A 945     5910   5585   8891    192   2072   1303       C  
ATOM   1403  CG  LYS A 945      -6.705  19.672  18.133  1.00 55.97           C  
ANISOU 1403  CG  LYS A 945     6027   5567   9672     42   2185   1195       C  
ATOM   1404  CD  LYS A 945      -6.111  19.135  16.848  1.00 55.71           C  
ANISOU 1404  CD  LYS A 945     5996   5345   9824      0   2074    907       C  
ATOM   1405  CE  LYS A 945      -6.953  17.998  16.307  1.00 58.56           C  
ANISOU 1405  CE  LYS A 945     6180   5389  10679   -176   2181    746       C  
ATOM   1406  NZ  LYS A 945      -6.657  17.749  14.876  1.00 58.60           N  
ANISOU 1406  NZ  LYS A 945     6197   5293  10775   -258   2041    339       N  
ATOM   1407  N   HIS A 946      -2.872  22.122  19.109  1.00 51.53           N  
ANISOU 1407  N   HIS A 946     5983   5671   7924    490   1775   1482       N  
ATOM   1408  CA  HIS A 946      -2.048  23.216  19.581  1.00 50.45           C  
ANISOU 1408  CA  HIS A 946     5975   5808   7386    588   1640   1530       C  
ATOM   1409  C   HIS A 946      -2.174  24.455  18.722  1.00 47.83           C  
ANISOU 1409  C   HIS A 946     5680   5630   6860    580   1489   1214       C  
ATOM   1410  O   HIS A 946      -1.691  25.516  19.102  1.00 47.65           O  
ANISOU 1410  O   HIS A 946     5752   5825   6526    640   1394   1211       O  
ATOM   1411  CB  HIS A 946      -0.591  22.769  19.617  1.00 51.65           C  
ANISOU 1411  CB  HIS A 946     6161   5891   7573    683   1568   1677       C  
ATOM   1412  CG  HIS A 946      -0.372  21.519  20.400  1.00 55.19           C  
ANISOU 1412  CG  HIS A 946     6558   6157   8254    713   1698   2034       C  
ATOM   1413  ND1 HIS A 946      -0.834  21.364  21.690  1.00 57.99           N  
ANISOU 1413  ND1 HIS A 946     6943   6619   8470    714   1802   2354       N  
ATOM   1414  CD2 HIS A 946       0.248  20.359  20.078  1.00 57.77           C  
ANISOU 1414  CD2 HIS A 946     6804   6186   8958    745   1758   2137       C  
ATOM   1415  CE1 HIS A 946      -0.508  20.161  22.129  1.00 61.16           C  
ANISOU 1415  CE1 HIS A 946     7287   6803   9146    748   1904   2677       C  
ATOM   1416  NE2 HIS A 946       0.154  19.532  21.171  1.00 61.29           N  
ANISOU 1416  NE2 HIS A 946     7225   6554   9508    773   1879   2550       N  
ATOM   1417  N   SER A 947      -2.815  24.330  17.568  1.00 47.43           N  
ANISOU 1417  N   SER A 947     5557   5469   6994    499   1459    954       N  
ATOM   1418  CA  SER A 947      -2.962  25.457  16.663  1.00 46.03           C  
ANISOU 1418  CA  SER A 947     5414   5431   6644    494   1303    697       C  
ATOM   1419  C   SER A 947      -4.163  25.267  15.729  1.00 47.03           C  
ANISOU 1419  C   SER A 947     5423   5480   6964    382   1275    479       C  
ATOM   1420  O   SER A 947      -4.770  24.193  15.696  1.00 50.04           O  
ANISOU 1420  O   SER A 947     5695   5674   7643    294   1380    485       O  
ATOM   1421  CB  SER A 947      -1.689  25.617  15.835  1.00 44.70           C  
ANISOU 1421  CB  SER A 947     5332   5251   6399    540   1194    591       C  
ATOM   1422  OG  SER A 947      -1.451  24.440  15.089  1.00 45.87           O  
ANISOU 1422  OG  SER A 947     5434   5165   6826    488   1251    505       O  
ATOM   1423  N   VAL A 948      -4.490  26.320  14.982  1.00 44.68           N  
ANISOU 1423  N   VAL A 948     5139   5323   6513    381   1123    301       N  
ATOM   1424  CA  VAL A 948      -5.530  26.273  13.974  1.00 45.28           C  
ANISOU 1424  CA  VAL A 948     5104   5374   6726    279   1023     95       C  
ATOM   1425  C   VAL A 948      -4.920  26.571  12.620  1.00 44.44           C  
ANISOU 1425  C   VAL A 948     5094   5309   6481    263    854   -107       C  
ATOM   1426  O   VAL A 948      -4.126  27.508  12.469  1.00 42.64           O  
ANISOU 1426  O   VAL A 948     4989   5206   6004    348    783    -93       O  
ATOM   1427  CB  VAL A 948      -6.646  27.305  14.250  1.00 45.21           C  
ANISOU 1427  CB  VAL A 948     4995   5506   6676    297    980     98       C  
ATOM   1428  CG1 VAL A 948      -7.397  27.670  12.972  1.00 45.78           C  
ANISOU 1428  CG1 VAL A 948     4981   5627   6785    230    769   -103       C  
ATOM   1429  CG2 VAL A 948      -7.613  26.772  15.287  1.00 46.92           C  
ANISOU 1429  CG2 VAL A 948     5065   5652   7108    259   1175    232       C  
ATOM   1430  N   LYS A 949      -5.292  25.765  11.639  1.00 45.85           N  
ANISOU 1430  N   LYS A 949     5220   5382   6817    140    804   -305       N  
ATOM   1431  CA  LYS A 949      -5.013  26.094  10.272  1.00 45.93           C  
ANISOU 1431  CA  LYS A 949     5321   5477   6652     95    637   -520       C  
ATOM   1432  C   LYS A 949      -6.305  26.488   9.598  1.00 47.70           C  
ANISOU 1432  C   LYS A 949     5424   5809   6891      8    444   -640       C  
ATOM   1433  O   LYS A 949      -7.203  25.662   9.447  1.00 50.23           O  
ANISOU 1433  O   LYS A 949     5593   6028   7464   -118    437   -746       O  
ATOM   1434  CB  LYS A 949      -4.398  24.927   9.536  1.00 47.35           C  
ANISOU 1434  CB  LYS A 949     5554   5483   6951      6    710   -705       C  
ATOM   1435  CG  LYS A 949      -3.891  25.357   8.177  1.00 48.10           C  
ANISOU 1435  CG  LYS A 949     5794   5702   6777    -29    580   -916       C  
ATOM   1436  CD  LYS A 949      -3.589  24.173   7.299  1.00 50.83           C  
ANISOU 1436  CD  LYS A 949     6177   5883   7250   -157    656  -1188       C  
ATOM   1437  CE  LYS A 949      -2.953  24.622   6.007  1.00 51.60           C  
ANISOU 1437  CE  LYS A 949     6455   6127   7021   -189    575  -1385       C  
ATOM   1438  NZ  LYS A 949      -2.225  23.488   5.385  1.00 54.04           N  
ANISOU 1438  NZ  LYS A 949     6832   6240   7459   -269    752  -1633       N  
ATOM   1439  N   GLY A 950      -6.399  27.755   9.205  1.00 46.99           N  
ANISOU 1439  N   GLY A 950     5378   5912   6561     76    280   -609       N  
ATOM   1440  CA  GLY A 950      -7.460  28.204   8.309  1.00 48.79           C  
ANISOU 1440  CA  GLY A 950     5503   6268   6765      7     36   -709       C  
ATOM   1441  C   GLY A 950      -7.127  27.681   6.927  1.00 50.58           C  
ANISOU 1441  C   GLY A 950     5844   6531   6841   -119    -90   -949       C  
ATOM   1442  O   GLY A 950      -6.026  27.909   6.421  1.00 49.49           O  
ANISOU 1442  O   GLY A 950     5909   6435   6458    -82    -59   -980       O  
ATOM   1443  N   LEU A 951      -8.060  26.949   6.326  1.00 53.14           N  
ANISOU 1443  N   LEU A 951     6035   6836   7316   -281   -218  -1137       N  
ATOM   1444  CA  LEU A 951      -7.795  26.269   5.064  1.00 54.45           C  
ANISOU 1444  CA  LEU A 951     6317   7028   7343   -437   -313  -1426       C  
ATOM   1445  C   LEU A 951      -8.157  27.177   3.917  1.00 55.64           C  
ANISOU 1445  C   LEU A 951     6525   7454   7160   -464   -627  -1463       C  
ATOM   1446  O   LEU A 951      -9.324  27.521   3.745  1.00 57.47           O  
ANISOU 1446  O   LEU A 951     6565   7794   7474   -504   -863  -1434       O  
ATOM   1447  CB  LEU A 951      -8.585  24.966   4.983  1.00 57.19           C  
ANISOU 1447  CB  LEU A 951     6493   7206   8027   -627   -298  -1647       C  
ATOM   1448  CG  LEU A 951      -8.089  23.867   5.925  1.00 56.62           C  
ANISOU 1448  CG  LEU A 951     6397   6827   8290   -619     29  -1616       C  
ATOM   1449  CD1 LEU A 951      -9.157  22.795   6.103  1.00 59.68           C  
ANISOU 1449  CD1 LEU A 951     6547   7027   9101   -791     51  -1749       C  
ATOM   1450  CD2 LEU A 951      -6.786  23.275   5.414  1.00 56.23           C  
ANISOU 1450  CD2 LEU A 951     6566   6670   8127   -626    189  -1774       C  
ATOM   1451  N   GLY A 952      -7.153  27.566   3.136  1.00 55.45           N  
ANISOU 1451  N   GLY A 952     6752   7542   6773   -439   -625  -1504       N  
ATOM   1452  CA  GLY A 952      -7.360  28.449   1.982  1.00 57.15           C  
ANISOU 1452  CA  GLY A 952     7068   8035   6610   -461   -909  -1495       C  
ATOM   1453  C   GLY A 952      -7.554  27.696   0.689  1.00 60.24           C  
ANISOU 1453  C   GLY A 952     7551   8542   6794   -678  -1067  -1824       C  
ATOM   1454  O   GLY A 952      -7.351  26.490   0.648  1.00 61.00           O  
ANISOU 1454  O   GLY A 952     7658   8468   7050   -807   -910  -2095       O  
ATOM   1455  N   LYS A 953      -7.951  28.413  -0.363  1.00 63.58           N  
ANISOU 1455  N   LYS A 953     8043   9252   6861   -722  -1377  -1799       N  
ATOM   1456  CA  LYS A 953      -8.026  27.852  -1.729  1.00 68.37           C  
ANISOU 1456  CA  LYS A 953     8801  10047   7128   -939  -1553  -2118       C  
ATOM   1457  C   LYS A 953      -6.632  27.632  -2.324  1.00 68.25           C  
ANISOU 1457  C   LYS A 953     9113  10030   6789   -956  -1288  -2270       C  
ATOM   1458  O   LYS A 953      -6.376  26.620  -2.979  1.00 70.76           O  
ANISOU 1458  O   LYS A 953     9546  10316   7020  -1136  -1201  -2645       O  
ATOM   1459  CB  LYS A 953      -8.805  28.778  -2.661  1.00 71.63           C  
ANISOU 1459  CB  LYS A 953     9208  10805   7203   -964  -1982  -1979       C  
ATOM   1460  CG  LYS A 953     -10.295  28.824  -2.403  1.00 74.55           C  
ANISOU 1460  CG  LYS A 953     9228  11214   7881  -1002  -2302  -1914       C  
ATOM   1461  CD  LYS A 953     -11.024  29.473  -3.575  1.00 79.91           C  
ANISOU 1461  CD  LYS A 953     9911  12261   8187  -1076  -2777  -1840       C  
ATOM   1462  CE  LYS A 953     -12.531  29.242  -3.512  1.00 83.68           C  
ANISOU 1462  CE  LYS A 953    10010  12789   8993  -1174  -3130  -1871       C  
ATOM   1463  NZ  LYS A 953     -13.102  29.677  -2.202  1.00 81.17           N  
ANISOU 1463  NZ  LYS A 953     9375  12245   9221   -985  -3009  -1600       N  
ATOM   1464  N   THR A 954      -5.747  28.600  -2.098  1.00 65.51           N  
ANISOU 1464  N   THR A 954     8898   9702   6290   -773  -1146  -1992       N  
ATOM   1465  CA  THR A 954      -4.376  28.554  -2.580  1.00 65.52           C  
ANISOU 1465  CA  THR A 954     9173   9694   6027   -762   -867  -2079       C  
ATOM   1466  C   THR A 954      -3.387  28.175  -1.463  1.00 62.37           C  
ANISOU 1466  C   THR A 954     8732   8979   5987   -630   -488  -2027       C  
ATOM   1467  O   THR A 954      -3.502  28.619  -0.321  1.00 58.74           O  
ANISOU 1467  O   THR A 954     8112   8396   5810   -477   -454  -1768       O  
ATOM   1468  CB  THR A 954      -3.992  29.908  -3.200  1.00 65.91           C  
ANISOU 1468  CB  THR A 954     9396   9985   5659   -668   -968  -1798       C  
ATOM   1469  OG1 THR A 954      -4.715  30.077  -4.421  1.00 69.60           O  
ANISOU 1469  OG1 THR A 954     9956  10771   5715   -814  -1303  -1872       O  
ATOM   1470  CG2 THR A 954      -2.502  29.997  -3.495  1.00 65.46           C  
ANISOU 1470  CG2 THR A 954     9578   9882   5409   -627   -624  -1826       C  
ATOM   1471  N   THR A 955      -2.413  27.350  -1.830  1.00 64.04           N  
ANISOU 1471  N   THR A 955     9088   9070   6172   -694   -206  -2283       N  
ATOM   1472  CA  THR A 955      -1.415  26.824  -0.913  1.00 61.63           C  
ANISOU 1472  CA  THR A 955     8734   8467   6214   -584    136  -2256       C  
ATOM   1473  C   THR A 955      -0.081  26.766  -1.665  1.00 63.03           C  
ANISOU 1473  C   THR A 955     9135   8651   6162   -590    409  -2390       C  
ATOM   1474  O   THR A 955      -0.068  26.558  -2.885  1.00 66.41           O  
ANISOU 1474  O   THR A 955     9750   9245   6236   -742    391  -2651       O  
ATOM   1475  CB  THR A 955      -1.834  25.418  -0.421  1.00 62.59           C  
ANISOU 1475  CB  THR A 955     8698   8319   6764   -675    236  -2483       C  
ATOM   1476  OG1 THR A 955      -1.175  25.115   0.807  1.00 60.48           O  
ANISOU 1476  OG1 THR A 955     8312   7780   6885   -524    474  -2301       O  
ATOM   1477  CG2 THR A 955      -1.514  24.325  -1.456  1.00 66.40           C  
ANISOU 1477  CG2 THR A 955     9317   8740   7169   -862    383  -2933       C  
ATOM   1478  N   PRO A 956       1.046  26.955  -0.960  1.00 60.97           N  
ANISOU 1478  N   PRO A 956     8851   8224   6089   -434    663  -2220       N  
ATOM   1479  CA  PRO A 956       2.339  26.778  -1.629  1.00 62.54           C  
ANISOU 1479  CA  PRO A 956     9214   8387   6160   -440    967  -2365       C  
ATOM   1480  C   PRO A 956       2.530  25.320  -2.051  1.00 65.55           C  
ANISOU 1480  C   PRO A 956     9613   8569   6723   -568   1188  -2775       C  
ATOM   1481  O   PRO A 956       1.997  24.423  -1.400  1.00 66.71           O  
ANISOU 1481  O   PRO A 956     9594   8501   7251   -590   1177  -2850       O  
ATOM   1482  CB  PRO A 956       3.360  27.174  -0.555  1.00 59.30           C  
ANISOU 1482  CB  PRO A 956     8691   7807   6034   -245   1144  -2085       C  
ATOM   1483  CG  PRO A 956       2.591  27.906   0.487  1.00 56.69           C  
ANISOU 1483  CG  PRO A 956     8210   7514   5814   -145    901  -1776       C  
ATOM   1484  CD  PRO A 956       1.206  27.337   0.452  1.00 58.02           C  
ANISOU 1484  CD  PRO A 956     8298   7705   6039   -257    684  -1904       C  
ATOM   1485  N   ASP A 957       3.257  25.086  -3.136  1.00 68.02           N  
ANISOU 1485  N   ASP A 957    10125   8939   6778   -658   1407  -3043       N  
ATOM   1486  CA  ASP A 957       3.407  23.733  -3.658  1.00 71.70           C  
ANISOU 1486  CA  ASP A 957    10628   9212   7402   -798   1638  -3492       C  
ATOM   1487  C   ASP A 957       4.269  22.907  -2.706  1.00 70.55           C  
ANISOU 1487  C   ASP A 957    10291   8657   7856   -660   1949  -3455       C  
ATOM   1488  O   ASP A 957       5.452  23.195  -2.532  1.00 70.41           O  
ANISOU 1488  O   ASP A 957    10266   8559   7927   -527   2193  -3321       O  
ATOM   1489  CB  ASP A 957       4.026  23.744  -5.061  1.00 75.21           C  
ANISOU 1489  CB  ASP A 957    11352   9833   7388   -928   1840  -3802       C  
ATOM   1490  CG  ASP A 957       4.106  22.350  -5.686  1.00 79.52           C  
ANISOU 1490  CG  ASP A 957    11954  10183   8075  -1099   2090  -4342       C  
ATOM   1491  OD1 ASP A 957       3.446  21.410  -5.194  1.00 79.77           O  
ANISOU 1491  OD1 ASP A 957    11822   9979   8506  -1154   2031  -4491       O  
ATOM   1492  OD2 ASP A 957       4.834  22.190  -6.686  1.00 82.92           O  
ANISOU 1492  OD2 ASP A 957    12596  10681   8226  -1185   2373  -4631       O  
ATOM   1493  N   PRO A 958       3.681  21.871  -2.089  1.00 70.70           N  
ANISOU 1493  N   PRO A 958    10138   8411   8311   -694   1938  -3553       N  
ATOM   1494  CA  PRO A 958       4.436  21.092  -1.117  1.00 69.62           C  
ANISOU 1494  CA  PRO A 958     9806   7886   8761   -548   2198  -3443       C  
ATOM   1495  C   PRO A 958       5.669  20.399  -1.692  1.00 71.75           C  
ANISOU 1495  C   PRO A 958    10126   7936   9200   -537   2620  -3712       C  
ATOM   1496  O   PRO A 958       6.596  20.100  -0.951  1.00 71.41           O  
ANISOU 1496  O   PRO A 958     9922   7631   9578   -366   2831  -3527       O  
ATOM   1497  CB  PRO A 958       3.417  20.056  -0.635  1.00 70.99           C  
ANISOU 1497  CB  PRO A 958     9826   7833   9311   -640   2114  -3555       C  
ATOM   1498  CG  PRO A 958       2.447  19.939  -1.759  1.00 74.13           C  
ANISOU 1498  CG  PRO A 958    10373   8443   9348   -885   1935  -3935       C  
ATOM   1499  CD  PRO A 958       2.318  21.341  -2.260  1.00 72.52           C  
ANISOU 1499  CD  PRO A 958    10329   8673   8551   -870   1691  -3754       C  
ATOM   1500  N   SER A 959       5.690  20.149  -2.994  1.00 74.88           N  
ANISOU 1500  N   SER A 959    10736   8442   9270   -715   2745  -4145       N  
ATOM   1501  CA  SER A 959       6.847  19.511  -3.607  1.00 77.65           C  
ANISOU 1501  CA  SER A 959    11142   8585   9773   -712   3195  -4443       C  
ATOM   1502  C   SER A 959       8.064  20.443  -3.694  1.00 76.13           C  
ANISOU 1502  C   SER A 959    10990   8514   9420   -563   3369  -4206       C  
ATOM   1503  O   SER A 959       9.153  20.011  -4.053  1.00 77.85           O  
ANISOU 1503  O   SER A 959    11200   8541   9836   -520   3770  -4381       O  
ATOM   1504  CB  SER A 959       6.490  18.969  -4.997  1.00 82.55           C  
ANISOU 1504  CB  SER A 959    12008   9315  10042   -971   3299  -5021       C  
ATOM   1505  OG  SER A 959       6.217  20.016  -5.907  1.00 82.60           O  
ANISOU 1505  OG  SER A 959    12272   9794   9317  -1075   3104  -5019       O  
ATOM   1506  N   ALA A 960       7.888  21.720  -3.377  1.00 73.57           N  
ANISOU 1506  N   ALA A 960    10692   8484   8775   -489   3089  -3819       N  
ATOM   1507  CA  ALA A 960       9.022  22.652  -3.336  1.00 72.84           C  
ANISOU 1507  CA  ALA A 960    10600   8477   8597   -352   3236  -3562       C  
ATOM   1508  C   ALA A 960       9.440  23.009  -1.914  1.00 69.22           C  
ANISOU 1508  C   ALA A 960     9877   7876   8546   -137   3134  -3109       C  
ATOM   1509  O   ALA A 960      10.478  23.648  -1.718  1.00 67.80           O  
ANISOU 1509  O   ALA A 960     9634   7703   8423    -18   3264  -2902       O  
ATOM   1510  CB  ALA A 960       8.705  23.914  -4.121  1.00 72.68           C  
ANISOU 1510  CB  ALA A 960    10818   8880   7916   -433   3047  -3464       C  
ATOM   1511  N   ASN A 961       8.645  22.599  -0.930  1.00 68.29           N  
ANISOU 1511  N   ASN A 961     9606   7638   8702    -99   2907  -2963       N  
ATOM   1512  CA  ASN A 961       8.942  22.916   0.451  1.00 67.13           C  
ANISOU 1512  CA  ASN A 961     9237   7397   8871     84   2784  -2543       C  
ATOM   1513  C   ASN A 961      10.270  22.294   0.844  1.00 67.69           C  
ANISOU 1513  C   ASN A 961     9119   7165   9433    226   3093  -2496       C  
ATOM   1514  O   ASN A 961      10.555  21.141   0.519  1.00 68.98           O  
ANISOU 1514  O   ASN A 961     9234   7047   9927    204   3363  -2759       O  
ATOM   1515  CB  ASN A 961       7.826  22.448   1.399  1.00 68.29           C  
ANISOU 1515  CB  ASN A 961     9266   7459   9221     84   2541  -2414       C  
ATOM   1516  CG  ASN A 961       6.489  23.159   1.153  1.00 69.77           C  
ANISOU 1516  CG  ASN A 961     9577   7944   8988    -30   2207  -2406       C  
ATOM   1517  OD1 ASN A 961       6.392  24.154   0.395  1.00 70.79           O  
ANISOU 1517  OD1 ASN A 961     9877   8362   8658    -84   2105  -2417       O  
ATOM   1518  ND2 ASN A 961       5.439  22.646   1.798  1.00 69.75           N  
ANISOU 1518  ND2 ASN A 961     9472   7859   9171    -64   2042  -2363       N  
ATOM   1519  N   ILE A 962      11.087  23.092   1.518  1.00 66.03           N  
ANISOU 1519  N   ILE A 962     8789   7009   9288    368   3050  -2169       N  
ATOM   1520  CA  ILE A 962      12.378  22.647   2.006  1.00 67.46           C  
ANISOU 1520  CA  ILE A 962     8741   6935   9952    521   3278  -2052       C  
ATOM   1521  C   ILE A 962      12.399  22.840   3.518  1.00 65.80           C  
ANISOU 1521  C   ILE A 962     8323   6698   9980    666   3022  -1630       C  
ATOM   1522  O   ILE A 962      11.421  23.289   4.105  1.00 62.74           O  
ANISOU 1522  O   ILE A 962     7987   6473   9376    639   2726  -1474       O  
ATOM   1523  CB  ILE A 962      13.548  23.355   1.280  1.00 68.05           C  
ANISOU 1523  CB  ILE A 962     8845   7098   9912    537   3514  -2099       C  
ATOM   1524  CG1 ILE A 962      13.510  24.884   1.459  1.00 65.95           C  
ANISOU 1524  CG1 ILE A 962     8655   7149   9255    537   3274  -1845       C  
ATOM   1525  CG2 ILE A 962      13.505  23.020  -0.197  1.00 71.23           C  
ANISOU 1525  CG2 ILE A 962     9477   7531  10055    384   3804  -2534       C  
ATOM   1526  CD1 ILE A 962      14.518  25.434   2.447  1.00 64.40           C  
ANISOU 1526  CD1 ILE A 962     8214   6913   9340    685   3215  -1515       C  
ATOM   1527  N   SER A 963      13.510  22.468   4.135  1.00 69.40           N  
ANISOU 1527  N   SER A 963     8536   6949  10882    816   3142  -1452       N  
ATOM   1528  CA  SER A 963      13.615  22.370   5.574  1.00 69.79           C  
ANISOU 1528  CA  SER A 963     8378   6943  11196    952   2922  -1064       C  
ATOM   1529  C   SER A 963      14.949  22.964   6.008  1.00 71.77           C  
ANISOU 1529  C   SER A 963     8431   7219  11618   1076   2929   -840       C  
ATOM   1530  O   SER A 963      15.989  22.320   5.881  1.00 75.88           O  
ANISOU 1530  O   SER A 963     8755   7499  12575   1171   3168   -856       O  
ATOM   1531  CB  SER A 963      13.511  20.890   5.975  1.00 73.43           C  
ANISOU 1531  CB  SER A 963     8690   7045  12162   1013   3046  -1053       C  
ATOM   1532  OG  SER A 963      13.607  20.687   7.374  1.00 74.21           O  
ANISOU 1532  OG  SER A 963     8598   7093  12503   1146   2840   -641       O  
ATOM   1533  N   LEU A 964      14.925  24.218   6.453  1.00 72.04           N  
ANISOU 1533  N   LEU A 964     8507   7533  11332   1066   2683   -660       N  
ATOM   1534  CA  LEU A 964      15.998  24.753   7.283  1.00 73.54           C  
ANISOU 1534  CA  LEU A 964     8470   7760  11708   1176   2571   -384       C  
ATOM   1535  C   LEU A 964      15.900  24.035   8.627  1.00 76.58           C  
ANISOU 1535  C   LEU A 964     8676   8045  12373   1290   2374    -77       C  
ATOM   1536  O   LEU A 964      14.816  23.580   9.001  1.00 78.45           O  
ANISOU 1536  O   LEU A 964     9017   8276  12515   1258   2270    -47       O  
ATOM   1537  CB  LEU A 964      15.830  26.257   7.514  1.00 71.08           C  
ANISOU 1537  CB  LEU A 964     8264   7756  10986   1115   2340   -291       C  
ATOM   1538  CG  LEU A 964      16.219  27.216   6.392  1.00 73.14           C  
ANISOU 1538  CG  LEU A 964     8651   8134  11003   1026   2504   -469       C  
ATOM   1539  CD1 LEU A 964      16.064  28.682   6.816  1.00 70.28           C  
ANISOU 1539  CD1 LEU A 964     8352   8019  10330    983   2260   -331       C  
ATOM   1540  CD2 LEU A 964      17.649  26.933   5.946  1.00 76.80           C  
ANISOU 1540  CD2 LEU A 964     8907   8428  11846   1087   2794   -514       C  
ATOM   1541  N   ASP A 965      17.013  23.931   9.355  1.00 79.24           N  
ANISOU 1541  N   ASP A 965     8738   8313  13056   1418   2318    169       N  
ATOM   1542  CA  ASP A 965      16.984  23.435  10.736  1.00 79.51           C  
ANISOU 1542  CA  ASP A 965     8613   8324  13273   1526   2071    531       C  
ATOM   1543  C   ASP A 965      16.233  22.097  10.749  1.00 78.99           C  
ANISOU 1543  C   ASP A 965     8575   7999  13438   1548   2195    519       C  
ATOM   1544  O   ASP A 965      16.619  21.166  10.042  1.00 84.43           O  
ANISOU 1544  O   ASP A 965     9178   8385  14515   1586   2492    357       O  
ATOM   1545  CB  ASP A 965      16.312  24.490  11.626  1.00 77.40           C  
ANISOU 1545  CB  ASP A 965     8478   8389  12539   1463   1729    680       C  
ATOM   1546  CG  ASP A 965      16.551  25.902  11.120  1.00 77.76           C  
ANISOU 1546  CG  ASP A 965     8624   8660  12260   1370   1695    528       C  
ATOM   1547  OD1 ASP A 965      17.731  26.324  11.098  1.00 79.70           O  
ANISOU 1547  OD1 ASP A 965     8682   8909  12691   1409   1710    574       O  
ATOM   1548  OD2 ASP A 965      15.566  26.574  10.716  1.00 75.24           O  
ANISOU 1548  OD2 ASP A 965     8552   8494  11541   1259   1663    371       O  
ATOM   1549  N   GLY A 966      15.185  22.001  11.560  1.00 74.09           N  
ANISOU 1549  N   GLY A 966     8062   7477  12609   1518   1993    681       N  
ATOM   1550  CA  GLY A 966      14.076  21.090  11.300  1.00 72.53           C  
ANISOU 1550  CA  GLY A 966     7986   7105  12466   1456   2113    557       C  
ATOM   1551  C   GLY A 966      12.802  21.913  11.127  1.00 67.58           C  
ANISOU 1551  C   GLY A 966     7621   6746  11310   1306   1979    405       C  
ATOM   1552  O   GLY A 966      11.715  21.443  11.458  1.00 66.67           O  
ANISOU 1552  O   GLY A 966     7583   6597  11152   1255   1940    438       O  
ATOM   1553  N   VAL A 967      12.948  23.145  10.624  1.00 62.54           N  
ANISOU 1553  N   VAL A 967     7095   6356  10309   1241   1917    261       N  
ATOM   1554  CA  VAL A 967      11.830  24.067  10.397  1.00 58.47           C  
ANISOU 1554  CA  VAL A 967     6803   6091   9322   1117   1784    135       C  
ATOM   1555  C   VAL A 967      11.471  24.126   8.916  1.00 58.02           C  
ANISOU 1555  C   VAL A 967     6912   6019   9112    999   1962   -238       C  
ATOM   1556  O   VAL A 967      12.309  24.461   8.082  1.00 58.14           O  
ANISOU 1556  O   VAL A 967     6934   6033   9122    993   2113   -385       O  
ATOM   1557  CB  VAL A 967      12.176  25.500  10.841  1.00 55.79           C  
ANISOU 1557  CB  VAL A 967     6487   6033   8677   1119   1584    244       C  
ATOM   1558  CG1 VAL A 967      11.059  26.460  10.479  1.00 52.77           C  
ANISOU 1558  CG1 VAL A 967     6315   5863   7872   1008   1481    107       C  
ATOM   1559  CG2 VAL A 967      12.448  25.556  12.334  1.00 56.38           C  
ANISOU 1559  CG2 VAL A 967     6432   6191   8797   1205   1368    582       C  
ATOM   1560  N   ASP A 968      10.211  23.844   8.611  1.00 56.91           N  
ANISOU 1560  N   ASP A 968     6904   5892   8826    897   1933   -381       N  
ATOM   1561  CA  ASP A 968       9.718  23.821   7.247  1.00 58.07           C  
ANISOU 1561  CA  ASP A 968     7220   6060   8784    765   2050   -733       C  
ATOM   1562  C   ASP A 968       9.571  25.243   6.678  1.00 54.23           C  
ANISOU 1562  C   ASP A 968     6890   5868   7843    705   1932   -785       C  
ATOM   1563  O   ASP A 968       8.962  26.107   7.301  1.00 51.51           O  
ANISOU 1563  O   ASP A 968     6578   5712   7281    707   1712   -625       O  
ATOM   1564  CB  ASP A 968       8.380  23.081   7.231  1.00 61.79           C  
ANISOU 1564  CB  ASP A 968     7740   6460   9276    668   2004   -841       C  
ATOM   1565  CG  ASP A 968       7.730  23.051   5.858  1.00 67.50           C  
ANISOU 1565  CG  ASP A 968     8639   7248   9758    507   2059  -1215       C  
ATOM   1566  OD1 ASP A 968       8.261  22.354   4.940  1.00 72.20           O  
ANISOU 1566  OD1 ASP A 968     9264   7682  10485    463   2301  -1489       O  
ATOM   1567  OD2 ASP A 968       6.663  23.711   5.713  1.00 68.97           O  
ANISOU 1567  OD2 ASP A 968     8928   7650   9627    423   1855  -1235       O  
ATOM   1568  N   VAL A 969      10.157  25.482   5.503  1.00 52.99           N  
ANISOU 1568  N   VAL A 969     6830   5738   7564    654   2106   -998       N  
ATOM   1569  CA  VAL A 969       9.966  26.732   4.761  1.00 49.91           C  
ANISOU 1569  CA  VAL A 969     6612   5603   6746    583   2028  -1045       C  
ATOM   1570  C   VAL A 969       9.124  26.458   3.517  1.00 50.09           C  
ANISOU 1570  C   VAL A 969     6831   5699   6501    436   2065  -1341       C  
ATOM   1571  O   VAL A 969       9.622  25.912   2.539  1.00 51.16           O  
ANISOU 1571  O   VAL A 969     7037   5757   6645    379   2308  -1592       O  
ATOM   1572  CB  VAL A 969      11.301  27.346   4.325  1.00 50.39           C  
ANISOU 1572  CB  VAL A 969     6650   5680   6815    622   2203  -1029       C  
ATOM   1573  CG1 VAL A 969      11.075  28.727   3.740  1.00 49.18           C  
ANISOU 1573  CG1 VAL A 969     6661   5773   6252    561   2105   -995       C  
ATOM   1574  CG2 VAL A 969      12.257  27.415   5.501  1.00 50.20           C  
ANISOU 1574  CG2 VAL A 969     6393   5565   7116    755   2165   -773       C  
ATOM   1575  N   PRO A 970       7.833  26.830   3.557  1.00 48.91           N  
ANISOU 1575  N   PRO A 970     6761   5705   6115    370   1821  -1323       N  
ATOM   1576  CA  PRO A 970       6.915  26.520   2.467  1.00 50.37           C  
ANISOU 1576  CA  PRO A 970     7104   5982   6052    218   1784  -1592       C  
ATOM   1577  C   PRO A 970       7.015  27.561   1.368  1.00 50.67           C  
ANISOU 1577  C   PRO A 970     7338   6268   5645    154   1761  -1633       C  
ATOM   1578  O   PRO A 970       6.195  28.469   1.294  1.00 50.95           O  
ANISOU 1578  O   PRO A 970     7438   6506   5415    133   1519  -1510       O  
ATOM   1579  CB  PRO A 970       5.548  26.587   3.155  1.00 48.76           C  
ANISOU 1579  CB  PRO A 970     6840   5838   5846    200   1512  -1485       C  
ATOM   1580  CG  PRO A 970       5.720  27.674   4.166  1.00 45.83           C  
ANISOU 1580  CG  PRO A 970     6397   5556   5460    321   1379  -1163       C  
ATOM   1581  CD  PRO A 970       7.161  27.605   4.621  1.00 45.78           C  
ANISOU 1581  CD  PRO A 970     6301   5419   5673    428   1565  -1060       C  
ATOM   1582  N   LEU A 971       8.029  27.437   0.530  1.00 51.98           N  
ANISOU 1582  N   LEU A 971     7589   6407   5751    130   2031  -1783       N  
ATOM   1583  CA  LEU A 971       8.277  28.416  -0.514  1.00 52.75           C  
ANISOU 1583  CA  LEU A 971     7883   6733   5425     71   2061  -1782       C  
ATOM   1584  C   LEU A 971       7.953  27.861  -1.901  1.00 57.06           C  
ANISOU 1584  C   LEU A 971     8646   7388   5643    -96   2160  -2126       C  
ATOM   1585  O   LEU A 971       8.449  28.358  -2.925  1.00 58.37           O  
ANISOU 1585  O   LEU A 971     8998   7711   5467   -158   2308  -2184       O  
ATOM   1586  CB  LEU A 971       9.722  28.923  -0.431  1.00 52.39           C  
ANISOU 1586  CB  LEU A 971     7778   6618   5508    160   2308  -1658       C  
ATOM   1587  CG  LEU A 971      10.847  27.929  -0.187  1.00 53.01           C  
ANISOU 1587  CG  LEU A 971     7700   6425   6016    224   2623  -1776       C  
ATOM   1588  CD1 LEU A 971      10.842  26.824  -1.222  1.00 56.57           C  
ANISOU 1588  CD1 LEU A 971     8272   6800   6422    110   2874  -2168       C  
ATOM   1589  CD2 LEU A 971      12.162  28.668  -0.219  1.00 53.36           C  
ANISOU 1589  CD2 LEU A 971     7677   6455   6141    293   2823  -1633       C  
ATOM   1590  N   GLY A 972       7.116  26.827  -1.939  1.00 58.40           N  
ANISOU 1590  N   GLY A 972     8800   7482   5906   -184   2085  -2362       N  
ATOM   1591  CA  GLY A 972       6.558  26.384  -3.199  1.00 61.54           C  
ANISOU 1591  CA  GLY A 972     9408   8033   5939   -374   2084  -2706       C  
ATOM   1592  C   GLY A 972       5.743  27.516  -3.788  1.00 61.44           C  
ANISOU 1592  C   GLY A 972     9553   8374   5417   -434   1769  -2545       C  
ATOM   1593  O   GLY A 972       5.192  28.348  -3.067  1.00 58.87           O  
ANISOU 1593  O   GLY A 972     9124   8112   5129   -342   1504  -2226       O  
ATOM   1594  N   THR A 973       5.674  27.558  -5.107  1.00 65.18           N  
ANISOU 1594  N   THR A 973    10278   9078   5408   -587   1806  -2759       N  
ATOM   1595  CA  THR A 973       4.849  28.537  -5.786  1.00 65.88           C  
ANISOU 1595  CA  THR A 973    10522   9517   4992   -653   1482  -2597       C  
ATOM   1596  C   THR A 973       3.377  28.220  -5.486  1.00 65.82           C  
ANISOU 1596  C   THR A 973    10399   9562   5045   -718   1087  -2635       C  
ATOM   1597  O   THR A 973       3.008  27.053  -5.344  1.00 66.72           O  
ANISOU 1597  O   THR A 973    10432   9515   5402   -806   1118  -2942       O  
ATOM   1598  CB  THR A 973       5.152  28.553  -7.296  1.00 70.10           C  
ANISOU 1598  CB  THR A 973    11373  10313   4949   -819   1622  -2825       C  
ATOM   1599  OG1 THR A 973       4.673  29.775  -7.854  1.00 70.99           O  
ANISOU 1599  OG1 THR A 973    11628  10751   4593   -827   1349  -2517       O  
ATOM   1600  CG2 THR A 973       4.526  27.368  -8.015  1.00 73.77           C  
ANISOU 1600  CG2 THR A 973    11938  10825   5265  -1029   1590  -3310       C  
ATOM   1601  N   GLY A 974       2.554  29.259  -5.356  1.00 64.95           N  
ANISOU 1601  N   GLY A 974    10256   9645   4775   -668    737  -2316       N  
ATOM   1602  CA  GLY A 974       1.143  29.093  -5.001  1.00 64.62           C  
ANISOU 1602  CA  GLY A 974    10057   9650   4844   -709    362  -2303       C  
ATOM   1603  C   GLY A 974       0.373  28.246  -6.003  1.00 68.87           C  
ANISOU 1603  C   GLY A 974    10701  10353   5112   -940    205  -2686       C  
ATOM   1604  O   GLY A 974       0.336  28.559  -7.188  1.00 72.35           O  
ANISOU 1604  O   GLY A 974    11379  11094   5017  -1060    118  -2760       O  
ATOM   1605  N   ILE A 975      -0.225  27.158  -5.528  1.00 69.18           N  
ANISOU 1605  N   ILE A 975    10570  10198   5517  -1014    176  -2934       N  
ATOM   1606  CA  ILE A 975      -1.078  26.315  -6.363  1.00 73.46           C  
ANISOU 1606  CA  ILE A 975    11164  10868   5880  -1255     -9  -3329       C  
ATOM   1607  C   ILE A 975      -2.427  26.096  -5.692  1.00 73.15           C  
ANISOU 1607  C   ILE A 975    10845  10777   6170  -1279   -340  -3273       C  
ATOM   1608  O   ILE A 975      -2.622  26.456  -4.522  1.00 69.25           O  
ANISOU 1608  O   ILE A 975    10131  10113   6066  -1106   -355  -2961       O  
ATOM   1609  CB  ILE A 975      -0.435  24.944  -6.644  1.00 75.99           C  
ANISOU 1609  CB  ILE A 975    11555  10948   6368  -1382    352  -3815       C  
ATOM   1610  CG1 ILE A 975      -0.331  24.110  -5.353  1.00 73.36           C  
ANISOU 1610  CG1 ILE A 975    10952  10178   6743  -1279    545  -3802       C  
ATOM   1611  CG2 ILE A 975       0.926  25.128  -7.310  1.00 76.95           C  
ANISOU 1611  CG2 ILE A 975    11928  11104   6203  -1357    730  -3890       C  
ATOM   1612  CD1 ILE A 975      -0.315  22.614  -5.593  1.00 76.39           C  
ANISOU 1612  CD1 ILE A 975    11319  10301   7402  -1448    758  -4299       C  
ATOM   1613  N   SER A 976      -3.349  25.497  -6.439  1.00 77.42           N  
ANISOU 1613  N   SER A 976    11393  11470   6551  -1506   -594  -3591       N  
ATOM   1614  CA  SER A 976      -4.683  25.205  -5.939  1.00 78.09           C  
ANISOU 1614  CA  SER A 976    11192  11514   6962  -1566   -908  -3585       C  
ATOM   1615  C   SER A 976      -4.625  24.079  -4.905  1.00 77.04           C  
ANISOU 1615  C   SER A 976    10849  10945   7476  -1554   -638  -3732       C  
ATOM   1616  O   SER A 976      -3.971  23.063  -5.121  1.00 78.45           O  
ANISOU 1616  O   SER A 976    11119  10912   7776  -1646   -332  -4083       O  
ATOM   1617  CB  SER A 976      -5.595  24.819  -7.094  1.00 83.42           C  
ANISOU 1617  CB  SER A 976    11930  12479   7285  -1840  -1258  -3926       C  
ATOM   1618  OG  SER A 976      -6.938  24.821  -6.675  1.00 84.12           O  
ANISOU 1618  OG  SER A 976    11712  12589   7659  -1880  -1622  -3836       O  
ATOM   1619  N   SER A 977      -5.305  24.273  -3.780  1.00 75.04           N  
ANISOU 1619  N   SER A 977    10315  10550   7646  -1436   -733  -3448       N  
ATOM   1620  CA  SER A 977      -5.260  23.324  -2.668  1.00 74.00           C  
ANISOU 1620  CA  SER A 977     9981  10015   8120  -1397   -475  -3477       C  
ATOM   1621  C   SER A 977      -6.249  22.179  -2.799  1.00 78.76           C  
ANISOU 1621  C   SER A 977    10410  10483   9028  -1627   -577  -3824       C  
ATOM   1622  O   SER A 977      -6.129  21.183  -2.098  1.00 78.89           O  
ANISOU 1622  O   SER A 977    10299  10138   9536  -1639   -322  -3919       O  
ATOM   1623  CB  SER A 977      -5.547  24.048  -1.353  1.00 69.82           C  
ANISOU 1623  CB  SER A 977     9243   9404   7880  -1177   -495  -3018       C  
ATOM   1624  OG  SER A 977      -6.881  24.525  -1.304  1.00 69.99           O  
ANISOU 1624  OG  SER A 977     9065   9594   7931  -1216   -853  -2899       O  
ATOM   1625  N   GLY A 978      -7.250  22.337  -3.657  1.00 84.06           N  
ANISOU 1625  N   GLY A 978    11057  11441   9440  -1810   -965  -3987       N  
ATOM   1626  CA  GLY A 978      -8.296  21.329  -3.812  1.00 89.31           C  
ANISOU 1626  CA  GLY A 978    11521  12003  10409  -2055  -1116  -4326       C  
ATOM   1627  C   GLY A 978      -9.431  21.437  -2.805  1.00 89.49           C  
ANISOU 1627  C   GLY A 978    11176  11920  10904  -2005  -1270  -4063       C  
ATOM   1628  O   GLY A 978     -10.438  20.749  -2.936  1.00 93.45           O  
ANISOU 1628  O   GLY A 978    11463  12367  11673  -2212  -1444  -4300       O  
ATOM   1629  N   VAL A 979      -9.278  22.300  -1.805  1.00 87.41           N  
ANISOU 1629  N   VAL A 979    10832  11627  10751  -1743  -1192  -3593       N  
ATOM   1630  CA  VAL A 979     -10.295  22.483  -0.766  1.00 87.84           C  
ANISOU 1630  CA  VAL A 979    10551  11582  11241  -1673  -1272  -3324       C  
ATOM   1631  C   VAL A 979     -11.521  23.181  -1.359  1.00 91.91           C  
ANISOU 1631  C   VAL A 979    10897  12422  11600  -1751  -1751  -3277       C  
ATOM   1632  O   VAL A 979     -11.417  24.290  -1.889  1.00 91.52           O  
ANISOU 1632  O   VAL A 979    10972  12678  11124  -1651  -1972  -3081       O  
ATOM   1633  CB  VAL A 979      -9.750  23.311   0.424  1.00 83.13           C  
ANISOU 1633  CB  VAL A 979     9948  10901  10733  -1376  -1056  -2866       C  
ATOM   1634  CG1 VAL A 979     -10.857  23.621   1.430  1.00 82.50           C  
ANISOU 1634  CG1 VAL A 979     9541  10765  11040  -1307  -1129  -2602       C  
ATOM   1635  CG2 VAL A 979      -8.591  22.586   1.103  1.00 80.91           C  
ANISOU 1635  CG2 VAL A 979     9785  10303  10655  -1293   -623  -2869       C  
ATOM   1636  N   ASN A 980     -12.679  22.531  -1.250  1.00 96.71           N  
ANISOU 1636  N   ASN A 980    11201  12947  12594  -1927  -1907  -3433       N  
ATOM   1637  CA  ASN A 980     -13.898  22.994  -1.915  1.00101.01           C  
ANISOU 1637  CA  ASN A 980    11537  13791  13049  -2043  -2400  -3447       C  
ATOM   1638  C   ASN A 980     -14.565  24.144  -1.158  1.00 99.00           C  
ANISOU 1638  C   ASN A 980    11041  13616  12957  -1817  -2519  -2980       C  
ATOM   1639  O   ASN A 980     -14.529  25.298  -1.589  1.00 99.21           O  
ANISOU 1639  O   ASN A 980    11153  13923  12619  -1683  -2753  -2737       O  
ATOM   1640  CB  ASN A 980     -14.901  21.833  -2.093  1.00104.92           C  
ANISOU 1640  CB  ASN A 980    11757  14153  13955  -2339  -2526  -3818       C  
ATOM   1641  CG  ASN A 980     -14.336  20.668  -2.898  1.00108.13           C  
ANISOU 1641  CG  ASN A 980    12386  14460  14238  -2590  -2412  -4345       C  
ATOM   1642  OD1 ASN A 980     -15.000  19.645  -3.069  1.00112.64           O  
ANISOU 1642  OD1 ASN A 980    12768  14877  15154  -2850  -2466  -4701       O  
ATOM   1643  ND2 ASN A 980     -13.115  20.814  -3.397  1.00106.74           N  
ANISOU 1643  ND2 ASN A 980    12598  14353  13603  -2522  -2233  -4414       N  
ATOM   1644  N   ASP A 981     -15.149  23.815  -0.014  1.00 97.56           N  
ANISOU 1644  N   ASP A 981    10563  13166  13338  -1773  -2322  -2855       N  
ATOM   1645  CA  ASP A 981     -16.079  24.693   0.665  1.00 97.00           C  
ANISOU 1645  CA  ASP A 981    10180  13143  13529  -1621  -2437  -2512       C  
ATOM   1646  C   ASP A 981     -15.317  25.574   1.650  1.00 91.95           C  
ANISOU 1646  C   ASP A 981     9679  12426  12833  -1320  -2128  -2141       C  
ATOM   1647  O   ASP A 981     -15.178  25.219   2.820  1.00 90.96           O  
ANISOU 1647  O   ASP A 981     9482  12036  13042  -1242  -1765  -2031       O  
ATOM   1648  CB  ASP A 981     -17.135  23.825   1.370  1.00 99.49           C  
ANISOU 1648  CB  ASP A 981    10102  13214  14485  -1758  -2348  -2598       C  
ATOM   1649  CG  ASP A 981     -18.303  24.629   1.915  1.00100.40           C  
ANISOU 1649  CG  ASP A 981     9829  13391  14928  -1646  -2495  -2311       C  
ATOM   1650  OD1 ASP A 981     -19.420  24.494   1.368  1.00103.70           O  
ANISOU 1650  OD1 ASP A 981     9930  13926  15544  -1810  -2855  -2432       O  
ATOM   1651  OD2 ASP A 981     -18.105  25.384   2.892  1.00 97.05           O  
ANISOU 1651  OD2 ASP A 981     9401  12893  14579  -1400  -2248  -1983       O  
ATOM   1652  N   THR A 982     -14.814  26.719   1.183  1.00 89.54           N  
ANISOU 1652  N   THR A 982     9574  12351  12096  -1163  -2271  -1947       N  
ATOM   1653  CA  THR A 982     -14.012  27.597   2.051  1.00 84.03           C  
ANISOU 1653  CA  THR A 982     9021  11580  11325   -899  -1992  -1637       C  
ATOM   1654  C   THR A 982     -14.057  29.101   1.724  1.00 82.79           C  
ANISOU 1654  C   THR A 982     8899  11647  10909   -713  -2212  -1341       C  
ATOM   1655  O   THR A 982     -14.151  29.527   0.572  1.00 84.04           O  
ANISOU 1655  O   THR A 982     9147  12064  10721   -765  -2551  -1355       O  
ATOM   1656  CB  THR A 982     -12.540  27.128   2.113  1.00 81.55           C  
ANISOU 1656  CB  THR A 982     9060  11148  10775   -879  -1675  -1736       C  
ATOM   1657  OG1 THR A 982     -11.857  27.808   3.180  1.00 76.32           O  
ANISOU 1657  OG1 THR A 982     8476  10380  10143   -651  -1392  -1458       O  
ATOM   1658  CG2 THR A 982     -11.824  27.374   0.773  1.00 82.83           C  
ANISOU 1658  CG2 THR A 982     9527  11546  10395   -941  -1855  -1869       C  
ATOM   1659  N   SER A 983     -13.958  29.890   2.787  1.00 79.75           N  
ANISOU 1659  N   SER A 983     8455  11149  10695   -498  -1993  -1070       N  
ATOM   1660  CA  SER A 983     -14.064  31.339   2.733  1.00 79.50           C  
ANISOU 1660  CA  SER A 983     8407  11239  10559   -299  -2126   -773       C  
ATOM   1661  C   SER A 983     -12.731  31.999   2.374  1.00 76.46           C  
ANISOU 1661  C   SER A 983     8394  10921   9733   -197  -2034   -682       C  
ATOM   1662  O   SER A 983     -12.708  33.046   1.726  1.00 76.97           O  
ANISOU 1662  O   SER A 983     8522  11147   9574   -105  -2245   -490       O  
ATOM   1663  CB  SER A 983     -14.514  31.836   4.106  1.00 78.37           C  
ANISOU 1663  CB  SER A 983     8044  10914  10817   -133  -1874   -582       C  
ATOM   1664  OG  SER A 983     -15.205  30.800   4.793  1.00 79.60           O  
ANISOU 1664  OG  SER A 983     7967  10911  11366   -249  -1725   -716       O  
ATOM   1665  N   LEU A 984     -11.633  31.370   2.795  1.00 72.17           N  
ANISOU 1665  N   LEU A 984     8076  10241   9104   -214  -1716   -801       N  
ATOM   1666  CA  LEU A 984     -10.293  31.939   2.680  1.00 68.74           C  
ANISOU 1666  CA  LEU A 984     7952   9822   8342   -113  -1558   -716       C  
ATOM   1667  C   LEU A 984      -9.614  31.692   1.331  1.00 69.21           C  
ANISOU 1667  C   LEU A 984     8282  10056   7958   -234  -1684   -869       C  
ATOM   1668  O   LEU A 984      -9.598  30.570   0.833  1.00 70.64           O  
ANISOU 1668  O   LEU A 984     8509  10236   8095   -416  -1691  -1155       O  
ATOM   1669  CB  LEU A 984      -9.400  31.341   3.759  1.00 66.63           C  
ANISOU 1669  CB  LEU A 984     7772   9334   8207    -73  -1173   -763       C  
ATOM   1670  CG  LEU A 984      -9.902  31.358   5.195  1.00 65.33           C  
ANISOU 1670  CG  LEU A 984     7399   9001   8419     17   -973   -647       C  
ATOM   1671  CD1 LEU A 984      -8.882  30.679   6.092  1.00 63.19           C  
ANISOU 1671  CD1 LEU A 984     7259   8558   8192     38   -641   -676       C  
ATOM   1672  CD2 LEU A 984     -10.155  32.788   5.637  1.00 65.31           C  
ANISOU 1672  CD2 LEU A 984     7329   9036   8450    199  -1001   -402       C  
ATOM   1673  N   LEU A 985      -9.044  32.750   0.759  1.00 68.35           N  
ANISOU 1673  N   LEU A 985     8355  10084   7531   -138  -1752   -683       N  
ATOM   1674  CA  LEU A 985      -8.175  32.650  -0.413  1.00 69.52           C  
ANISOU 1674  CA  LEU A 985     8808  10393   7214   -229  -1777   -789       C  
ATOM   1675  C   LEU A 985      -6.870  31.952  -0.051  1.00 66.01           C  
ANISOU 1675  C   LEU A 985     8554   9778   6748   -242  -1401   -955       C  
ATOM   1676  O   LEU A 985      -6.327  31.179  -0.847  1.00 65.92           O  
ANISOU 1676  O   LEU A 985     8726   9818   6501   -383  -1342  -1207       O  
ATOM   1677  CB  LEU A 985      -7.822  34.046  -0.944  1.00 70.71           C  
ANISOU 1677  CB  LEU A 985     9092  10686   7086   -100  -1879   -483       C  
ATOM   1678  CG  LEU A 985      -8.924  34.886  -1.597  1.00 74.83           C  
ANISOU 1678  CG  LEU A 985     9474  11410   7546    -70  -2285   -255       C  
ATOM   1679  CD1 LEU A 985      -8.463  36.333  -1.765  1.00 74.79           C  
ANISOU 1679  CD1 LEU A 985     9575  11434   7407    104  -2283    106       C  
ATOM   1680  CD2 LEU A 985      -9.343  34.295  -2.937  1.00 79.14           C  
ANISOU 1680  CD2 LEU A 985    10110  12239   7718   -276  -2600   -434       C  
ATOM   1681  N   TYR A 986      -6.367  32.261   1.145  1.00 61.57           N  
ANISOU 1681  N   TYR A 986     7941   9019   6432    -92  -1150   -811       N  
ATOM   1682  CA  TYR A 986      -5.099  31.743   1.620  1.00 58.61           C  
ANISOU 1682  CA  TYR A 986     7705   8482   6083    -69   -820   -897       C  
ATOM   1683  C   TYR A 986      -5.209  31.163   3.018  1.00 54.82           C  
ANISOU 1683  C   TYR A 986     7055   7776   5997    -17   -627   -887       C  
ATOM   1684  O   TYR A 986      -5.950  31.661   3.859  1.00 53.23           O  
ANISOU 1684  O   TYR A 986     6674   7538   6011     68   -667   -729       O  
ATOM   1685  CB  TYR A 986      -4.055  32.858   1.665  1.00 58.18           C  
ANISOU 1685  CB  TYR A 986     7803   8443   5857     64   -702   -690       C  
ATOM   1686  CG  TYR A 986      -3.839  33.610   0.366  1.00 61.98           C  
ANISOU 1686  CG  TYR A 986     8472   9141   5937     36   -849   -616       C  
ATOM   1687  CD1 TYR A 986      -3.120  33.038  -0.679  1.00 64.78           C  
ANISOU 1687  CD1 TYR A 986     9046   9588   5977    -86   -770   -813       C  
ATOM   1688  CD2 TYR A 986      -4.318  34.907   0.200  1.00 62.64           C  
ANISOU 1688  CD2 TYR A 986     8516   9324   5961    138  -1037   -334       C  
ATOM   1689  CE1 TYR A 986      -2.908  33.725  -1.860  1.00 67.86           C  
ANISOU 1689  CE1 TYR A 986     9632  10200   5951   -120   -881   -722       C  
ATOM   1690  CE2 TYR A 986      -4.110  35.600  -0.977  1.00 65.66           C  
ANISOU 1690  CE2 TYR A 986     9077   9902   5968    117  -1167   -211       C  
ATOM   1691  CZ  TYR A 986      -3.405  35.007  -2.006  1.00 68.54           C  
ANISOU 1691  CZ  TYR A 986     9680  10391   5970    -17  -1090   -398       C  
ATOM   1692  OH  TYR A 986      -3.195  35.689  -3.191  1.00 72.06           O  
ANISOU 1692  OH  TYR A 986    10329  11060   5990    -49  -1200   -256       O  
ATOM   1693  N   ASN A 987      -4.417  30.127   3.260  1.00 53.92           N  
ANISOU 1693  N   ASN A 987     7007   7508   5972    -63   -396  -1042       N  
ATOM   1694  CA  ASN A 987      -4.184  29.605   4.599  1.00 51.22           C  
ANISOU 1694  CA  ASN A 987     6558   6957   5944      5   -179   -974       C  
ATOM   1695  C   ASN A 987      -3.872  30.669   5.632  1.00 48.21           C  
ANISOU 1695  C   ASN A 987     6153   6570   5592    172   -111   -718       C  
ATOM   1696  O   ASN A 987      -3.225  31.673   5.337  1.00 47.13           O  
ANISOU 1696  O   ASN A 987     6135   6519   5252    247   -127   -616       O  
ATOM   1697  CB  ASN A 987      -2.991  28.657   4.593  1.00 50.93           C  
ANISOU 1697  CB  ASN A 987     6633   6766   5949    -17     63  -1102       C  
ATOM   1698  CG  ASN A 987      -3.246  27.400   3.811  1.00 54.10           C  
ANISOU 1698  CG  ASN A 987     7043   7096   6414   -189     74  -1402       C  
ATOM   1699  OD1 ASN A 987      -4.377  26.917   3.725  1.00 55.66           O  
ANISOU 1699  OD1 ASN A 987     7102   7287   6756   -297    -57  -1503       O  
ATOM   1700  ND2 ASN A 987      -2.184  26.847   3.243  1.00 55.65           N  
ANISOU 1700  ND2 ASN A 987     7388   7221   6536   -222    249  -1567       N  
ATOM   1701  N   GLU A 988      -4.317  30.415   6.854  1.00 46.57           N  
ANISOU 1701  N   GLU A 988     5799   6254   5641    217    -16   -626       N  
ATOM   1702  CA  GLU A 988      -3.943  31.210   8.000  1.00 44.33           C  
ANISOU 1702  CA  GLU A 988     5505   5952   5384    353     88   -436       C  
ATOM   1703  C   GLU A 988      -3.561  30.231   9.094  1.00 43.34           C  
ANISOU 1703  C   GLU A 988     5340   5677   5447    360    289   -401       C  
ATOM   1704  O   GLU A 988      -4.077  29.117   9.134  1.00 43.89           O  
ANISOU 1704  O   GLU A 988     5321   5642   5710    272    333   -481       O  
ATOM   1705  CB  GLU A 988      -5.106  32.073   8.461  1.00 45.83           C  
ANISOU 1705  CB  GLU A 988     5545   6199   5667    408     -5   -329       C  
ATOM   1706  CG  GLU A 988      -5.705  32.970   7.382  1.00 48.77           C  
ANISOU 1706  CG  GLU A 988     5907   6706   5916    408   -242   -316       C  
ATOM   1707  CD  GLU A 988      -6.791  33.895   7.924  1.00 49.47           C  
ANISOU 1707  CD  GLU A 988     5814   6811   6170    494   -305   -191       C  
ATOM   1708  OE1 GLU A 988      -7.461  34.575   7.100  1.00 51.78           O  
ANISOU 1708  OE1 GLU A 988     6044   7199   6429    505   -523   -141       O  
ATOM   1709  OE2 GLU A 988      -6.966  33.936   9.169  1.00 47.09           O  
ANISOU 1709  OE2 GLU A 988     5431   6429   6030    551   -130   -137       O  
ATOM   1710  N   TYR A 989      -2.653  30.644   9.972  1.00 41.24           N  
ANISOU 1710  N   TYR A 989     5134   5400   5132    457    400   -272       N  
ATOM   1711  CA  TYR A 989      -2.180  29.782  11.052  1.00 41.08           C  
ANISOU 1711  CA  TYR A 989     5088   5267   5252    479    564   -182       C  
ATOM   1712  C   TYR A 989      -2.251  30.542  12.357  1.00 39.73           C  
ANISOU 1712  C   TYR A 989     4896   5160   5037    565    615    -22       C  
ATOM   1713  O   TYR A 989      -1.787  31.671  12.458  1.00 38.39           O  
ANISOU 1713  O   TYR A 989     4792   5080   4712    629    572      6       O  
ATOM   1714  CB  TYR A 989      -0.740  29.327  10.814  1.00 40.82           C  
ANISOU 1714  CB  TYR A 989     5153   5165   5191    500    644   -195       C  
ATOM   1715  CG  TYR A 989      -0.533  28.581   9.528  1.00 40.98           C  
ANISOU 1715  CG  TYR A 989     5220   5117   5233    412    645   -394       C  
ATOM   1716  CD1 TYR A 989      -0.312  29.264   8.345  1.00 41.00           C  
ANISOU 1716  CD1 TYR A 989     5329   5231   5017    385    554   -508       C  
ATOM   1717  CD2 TYR A 989      -0.527  27.192   9.501  1.00 42.49           C  
ANISOU 1717  CD2 TYR A 989     5359   5124   5659    350    758   -470       C  
ATOM   1718  CE1 TYR A 989      -0.106  28.583   7.155  1.00 42.84           C  
ANISOU 1718  CE1 TYR A 989     5633   5429   5212    289    575   -720       C  
ATOM   1719  CE2 TYR A 989      -0.323  26.500   8.316  1.00 44.02           C  
ANISOU 1719  CE2 TYR A 989     5607   5246   5870    255    786   -707       C  
ATOM   1720  CZ  TYR A 989      -0.118  27.204   7.149  1.00 43.96           C  
ANISOU 1720  CZ  TYR A 989     5724   5387   5590    220    693   -844       C  
ATOM   1721  OH  TYR A 989       0.061  26.544   5.973  1.00 46.37           O  
ANISOU 1721  OH  TYR A 989     6109   5654   5854    111    733  -1104       O  
ATOM   1722  N   ILE A 990      -2.835  29.916  13.366  1.00 40.25           N  
ANISOU 1722  N   ILE A 990     4876   5177   5241    556    723     72       N  
ATOM   1723  CA  ILE A 990      -3.099  30.618  14.599  1.00 39.03           C  
ANISOU 1723  CA  ILE A 990     4709   5107   5011    617    792    189       C  
ATOM   1724  C   ILE A 990      -2.648  29.779  15.776  1.00 38.96           C  
ANISOU 1724  C   ILE A 990     4714   5061   5027    630    930    357       C  
ATOM   1725  O   ILE A 990      -3.034  28.640  15.890  1.00 39.99           O  
ANISOU 1725  O   ILE A 990     4773   5071   5349    578   1016    410       O  
ATOM   1726  CB  ILE A 990      -4.586  30.956  14.733  1.00 39.75           C  
ANISOU 1726  CB  ILE A 990     4665   5219   5217    595    806    162       C  
ATOM   1727  CG1 ILE A 990      -5.087  31.735  13.506  1.00 39.39           C  
ANISOU 1727  CG1 ILE A 990     4584   5214   5166    589    627     40       C  
ATOM   1728  CG2 ILE A 990      -4.803  31.790  15.982  1.00 40.41           C  
ANISOU 1728  CG2 ILE A 990     4758   5393   5203    659    917    240       C  
ATOM   1729  CD1 ILE A 990      -5.557  30.895  12.339  1.00 40.18           C  
ANISOU 1729  CD1 ILE A 990     4620   5259   5386    488    517    -75       C  
ATOM   1730  N   VAL A 991      -1.801  30.360  16.615  1.00 38.22           N  
ANISOU 1730  N   VAL A 991     4709   5070   4743    692    935    447       N  
ATOM   1731  CA  VAL A 991      -1.429  29.790  17.897  1.00 39.28           C  
ANISOU 1731  CA  VAL A 991     4867   5233   4822    712   1031    646       C  
ATOM   1732  C   VAL A 991      -1.937  30.683  19.029  1.00 39.90           C  
ANISOU 1732  C   VAL A 991     4980   5473   4706    729   1101    673       C  
ATOM   1733  O   VAL A 991      -2.128  31.876  18.846  1.00 38.80           O  
ANISOU 1733  O   VAL A 991     4861   5406   4473    749   1056    533       O  
ATOM   1734  CB  VAL A 991       0.086  29.630  18.042  1.00 39.14           C  
ANISOU 1734  CB  VAL A 991     4915   5230   4723    759    958    733       C  
ATOM   1735  CG1 VAL A 991       0.586  28.550  17.106  1.00 39.50           C  
ANISOU 1735  CG1 VAL A 991     4917   5087   5001    747    960    716       C  
ATOM   1736  CG2 VAL A 991       0.818  30.941  17.790  1.00 38.41           C  
ANISOU 1736  CG2 VAL A 991     4893   5251   4449    790    842    614       C  
ATOM   1737  N   TYR A 992      -2.140  30.088  20.200  1.00 41.81           N  
ANISOU 1737  N   TYR A 992     5233   5760   4890    720   1230    856       N  
ATOM   1738  CA  TYR A 992      -2.809  30.751  21.315  1.00 42.61           C  
ANISOU 1738  CA  TYR A 992     5372   6012   4806    716   1361    866       C  
ATOM   1739  C   TYR A 992      -1.917  30.872  22.533  1.00 43.63           C  
ANISOU 1739  C   TYR A 992     5633   6323   4621    732   1348   1005       C  
ATOM   1740  O   TYR A 992      -2.390  31.178  23.610  1.00 45.87           O  
ANISOU 1740  O   TYR A 992     5976   6751   4700    713   1485   1040       O  
ATOM   1741  CB  TYR A 992      -4.105  29.999  21.640  1.00 44.05           C  
ANISOU 1741  CB  TYR A 992     5446   6117   5173    667   1563    950       C  
ATOM   1742  CG  TYR A 992      -5.025  29.956  20.437  1.00 43.93           C  
ANISOU 1742  CG  TYR A 992     5275   5950   5462    636   1528    790       C  
ATOM   1743  CD1 TYR A 992      -5.037  28.858  19.589  1.00 44.36           C  
ANISOU 1743  CD1 TYR A 992     5249   5828   5777    589   1482    805       C  
ATOM   1744  CD2 TYR A 992      -5.849  31.033  20.120  1.00 43.42           C  
ANISOU 1744  CD2 TYR A 992     5140   5921   5434    652   1524    615       C  
ATOM   1745  CE1 TYR A 992      -5.856  28.824  18.474  1.00 44.13           C  
ANISOU 1745  CE1 TYR A 992     5086   5698   5983    541   1410    638       C  
ATOM   1746  CE2 TYR A 992      -6.662  31.006  19.003  1.00 43.24           C  
ANISOU 1746  CE2 TYR A 992     4965   5792   5671    624   1440    495       C  
ATOM   1747  CZ  TYR A 992      -6.661  29.898  18.186  1.00 43.68           C  
ANISOU 1747  CZ  TYR A 992     4956   5710   5928    560   1370    500       C  
ATOM   1748  OH  TYR A 992      -7.465  29.846  17.073  1.00 44.75           O  
ANISOU 1748  OH  TYR A 992     4947   5772   6283    510   1253    364       O  
ATOM   1749  N   ASP A 993      -0.625  30.645  22.338  1.00 44.03           N  
ANISOU 1749  N   ASP A 993     5722   6375   4630    762   1182   1075       N  
ATOM   1750  CA  ASP A 993       0.381  30.733  23.391  1.00 46.83           C  
ANISOU 1750  CA  ASP A 993     6177   6917   4700    774   1096   1218       C  
ATOM   1751  C   ASP A 993       1.606  31.402  22.783  1.00 45.57           C  
ANISOU 1751  C   ASP A 993     6022   6766   4524    801    890   1093       C  
ATOM   1752  O   ASP A 993       2.154  30.912  21.795  1.00 43.88           O  
ANISOU 1752  O   ASP A 993     5737   6391   4544    828    821   1096       O  
ATOM   1753  CB  ASP A 993       0.741  29.332  23.912  1.00 49.40           C  
ANISOU 1753  CB  ASP A 993     6480   7196   5091    791   1116   1554       C  
ATOM   1754  CG  ASP A 993       1.706  29.360  25.110  1.00 52.78           C  
ANISOU 1754  CG  ASP A 993     7003   7858   5191    803    994   1758       C  
ATOM   1755  OD1 ASP A 993       2.426  30.372  25.317  1.00 53.02           O  
ANISOU 1755  OD1 ASP A 993     7094   8055   4995    795    840   1608       O  
ATOM   1756  OD2 ASP A 993       1.755  28.343  25.843  1.00 55.40           O  
ANISOU 1756  OD2 ASP A 993     7341   8204   5502    816   1040   2085       O  
ATOM   1757  N   ILE A 994       2.029  32.515  23.375  1.00 47.15           N  
ANISOU 1757  N   ILE A 994     6305   7145   4462    781    815    967       N  
ATOM   1758  CA  ILE A 994       3.170  33.297  22.864  1.00 46.55           C  
ANISOU 1758  CA  ILE A 994     6221   7076   4389    788    637    833       C  
ATOM   1759  C   ILE A 994       4.477  32.493  22.797  1.00 47.16           C  
ANISOU 1759  C   ILE A 994     6235   7133   4549    823    483   1028       C  
ATOM   1760  O   ILE A 994       5.351  32.799  21.973  1.00 48.16           O  
ANISOU 1760  O   ILE A 994     6301   7176   4819    839    384    941       O  
ATOM   1761  CB  ILE A 994       3.412  34.579  23.702  1.00 47.95           C  
ANISOU 1761  CB  ILE A 994     6491   7447   4278    738    587    655       C  
ATOM   1762  CG1 ILE A 994       3.734  34.235  25.172  1.00 51.18           C  
ANISOU 1762  CG1 ILE A 994     6988   8106   4351    703    540    819       C  
ATOM   1763  CG2 ILE A 994       2.201  35.497  23.620  1.00 47.15           C  
ANISOU 1763  CG2 ILE A 994     6421   7311   4181    723    757    434       C  
ATOM   1764  CD1 ILE A 994       4.149  35.420  26.022  1.00 52.69           C  
ANISOU 1764  CD1 ILE A 994     7279   8509   4231    628    459    609       C  
ATOM   1765  N   ALA A 995       4.602  31.479  23.659  1.00 47.66           N  
ANISOU 1765  N   ALA A 995     6300   7264   4545    840    477   1308       N  
ATOM   1766  CA  ALA A 995       5.778  30.617  23.694  1.00 48.03           C  
ANISOU 1766  CA  ALA A 995     6255   7272   4721    895    337   1544       C  
ATOM   1767  C   ALA A 995       5.898  29.682  22.472  1.00 46.83           C  
ANISOU 1767  C   ALA A 995     5985   6824   4982    948    411   1572       C  
ATOM   1768  O   ALA A 995       6.903  28.977  22.335  1.00 48.04           O  
ANISOU 1768  O   ALA A 995     6034   6891   5328   1008    328   1737       O  
ATOM   1769  CB  ALA A 995       5.779  29.798  24.980  1.00 50.68           C  
ANISOU 1769  CB  ALA A 995     6629   7756   4871    906    315   1881       C  
ATOM   1770  N   GLN A 996       4.882  29.657  21.606  1.00 44.35           N  
ANISOU 1770  N   GLN A 996     5679   6359   4812    925    565   1405       N  
ATOM   1771  CA  GLN A 996       4.919  28.862  20.375  1.00 43.22           C  
ANISOU 1771  CA  GLN A 996     5451   5957   5013    946    639   1356       C  
ATOM   1772  C   GLN A 996       5.505  29.642  19.203  1.00 41.18           C  
ANISOU 1772  C   GLN A 996     5182   5649   4815    941    588   1113       C  
ATOM   1773  O   GLN A 996       5.572  29.127  18.091  1.00 39.19           O  
ANISOU 1773  O   GLN A 996     4886   5214   4788    944    656   1020       O  
ATOM   1774  CB  GLN A 996       3.513  28.379  20.000  1.00 43.50           C  
ANISOU 1774  CB  GLN A 996     5488   5870   5167    902    803   1295       C  
ATOM   1775  CG  GLN A 996       2.899  27.376  20.973  1.00 46.04           C  
ANISOU 1775  CG  GLN A 996     5799   6170   5522    899    913   1558       C  
ATOM   1776  CD  GLN A 996       1.504  26.905  20.559  1.00 46.16           C  
ANISOU 1776  CD  GLN A 996     5777   6046   5713    837   1079   1478       C  
ATOM   1777  OE1 GLN A 996       0.528  27.156  21.250  1.00 47.60           O  
ANISOU 1777  OE1 GLN A 996     5989   6329   5767    799   1176   1507       O  
ATOM   1778  NE2 GLN A 996       1.410  26.228  19.424  1.00 46.48           N  
ANISOU 1778  NE2 GLN A 996     5744   5858   6055    817   1118   1357       N  
ATOM   1779  N   VAL A 997       5.918  30.885  19.457  1.00 41.60           N  
ANISOU 1779  N   VAL A 997     5281   5862   4661    923    485   1003       N  
ATOM   1780  CA  VAL A 997       6.436  31.783  18.421  1.00 40.09           C  
ANISOU 1780  CA  VAL A 997     5089   5631   4510    910    454    799       C  
ATOM   1781  C   VAL A 997       7.879  32.173  18.718  1.00 41.13           C  
ANISOU 1781  C   VAL A 997     5157   5832   4639    924    322    839       C  
ATOM   1782  O   VAL A 997       8.195  32.618  19.815  1.00 43.37           O  
ANISOU 1782  O   VAL A 997     5454   6290   4733    907    204    897       O  
ATOM   1783  CB  VAL A 997       5.614  33.087  18.347  1.00 39.35           C  
ANISOU 1783  CB  VAL A 997     5081   5619   4249    867    464    612       C  
ATOM   1784  CG1 VAL A 997       6.132  33.990  17.229  1.00 38.32           C  
ANISOU 1784  CG1 VAL A 997     4955   5428   4175    854    446    452       C  
ATOM   1785  CG2 VAL A 997       4.130  32.787  18.166  1.00 39.07           C  
ANISOU 1785  CG2 VAL A 997     5070   5537   4236    853    575    581       C  
ATOM   1786  N   ASN A 998       8.744  32.010  17.727  1.00 41.21           N  
ANISOU 1786  N   ASN A 998     5090   5711   4856    945    347    792       N  
ATOM   1787  CA  ASN A 998      10.106  32.484  17.808  1.00 42.37           C  
ANISOU 1787  CA  ASN A 998     5139   5896   5062    949    242    799       C  
ATOM   1788  C   ASN A 998      10.443  33.294  16.571  1.00 41.12           C  
ANISOU 1788  C   ASN A 998     4992   5652   4976    917    320    608       C  
ATOM   1789  O   ASN A 998      10.670  32.738  15.511  1.00 41.45           O  
ANISOU 1789  O   ASN A 998     5008   5546   5195    937    446    569       O  
ATOM   1790  CB  ASN A 998      11.059  31.304  17.940  1.00 44.59           C  
ANISOU 1790  CB  ASN A 998     5265   6084   5593   1023    223    998       C  
ATOM   1791  CG  ASN A 998      12.452  31.719  18.365  1.00 46.05           C  
ANISOU 1791  CG  ASN A 998     5301   6348   5846   1030     63   1059       C  
ATOM   1792  OD1 ASN A 998      13.405  30.979  18.162  1.00 47.83           O  
ANISOU 1792  OD1 ASN A 998     5356   6461   6354   1097     67   1180       O  
ATOM   1793  ND2 ASN A 998      12.574  32.893  18.969  1.00 46.33           N  
ANISOU 1793  ND2 ASN A 998     5379   6564   5658    958    -74    964       N  
ATOM   1794  N   LEU A 999      10.457  34.614  16.714  1.00 41.06           N  
ANISOU 1794  N   LEU A 999     5036   5735   4831    861    261    486       N  
ATOM   1795  CA  LEU A 999      10.712  35.514  15.592  1.00 40.54           C  
ANISOU 1795  CA  LEU A 999     4995   5588   4820    826    342    343       C  
ATOM   1796  C   LEU A 999      12.159  35.391  15.151  1.00 41.74           C  
ANISOU 1796  C   LEU A 999     5001   5669   5187    832    360    368       C  
ATOM   1797  O   LEU A 999      13.064  35.417  15.986  1.00 42.72           O  
ANISOU 1797  O   LEU A 999     4996   5864   5371    829    226    439       O  
ATOM   1798  CB  LEU A 999      10.427  36.958  15.994  1.00 40.87           C  
ANISOU 1798  CB  LEU A 999     5102   5705   4719    767    282    226       C  
ATOM   1799  CG  LEU A 999       8.993  37.257  16.449  1.00 40.58           C  
ANISOU 1799  CG  LEU A 999     5186   5726   4507    766    294    179       C  
ATOM   1800  CD1 LEU A 999       8.843  38.733  16.777  1.00 40.87           C  
ANISOU 1800  CD1 LEU A 999     5267   5787   4474    714    270     38       C  
ATOM   1801  CD2 LEU A 999       7.983  36.847  15.379  1.00 39.76           C  
ANISOU 1801  CD2 LEU A 999     5147   5530   4430    794    404    171       C  
ATOM   1802  N   LYS A1000      12.368  35.243  13.843  1.00 41.25           N  
ANISOU 1802  N   LYS A1000     4952   5480   5237    834    526    309       N  
ATOM   1803  CA  LYS A1000      13.702  35.018  13.283  1.00 42.04           C  
ANISOU 1803  CA  LYS A1000     4905   5488   5580    845    614    321       C  
ATOM   1804  C   LYS A1000      14.186  36.161  12.406  1.00 40.98           C  
ANISOU 1804  C   LYS A1000     4793   5315   5462    780    715    225       C  
ATOM   1805  O   LYS A1000      15.326  36.593  12.548  1.00 41.12           O  
ANISOU 1805  O   LYS A1000     4655   5315   5652    754    700    235       O  
ATOM   1806  CB  LYS A1000      13.728  33.717  12.466  1.00 43.71           C  
ANISOU 1806  CB  LYS A1000     5101   5563   5941    898    789    325       C  
ATOM   1807  CG  LYS A1000      13.449  32.452  13.261  1.00 45.75           C  
ANISOU 1807  CG  LYS A1000     5299   5796   6285    968    727    456       C  
ATOM   1808  CD  LYS A1000      14.178  32.492  14.587  1.00 48.86           C  
ANISOU 1808  CD  LYS A1000     5536   6289   6738    998    519    623       C  
ATOM   1809  CE  LYS A1000      14.530  31.116  15.097  1.00 52.39           C  
ANISOU 1809  CE  LYS A1000     5841   6648   7414   1093    504    815       C  
ATOM   1810  NZ  LYS A1000      15.876  30.671  14.633  1.00 56.02           N  
ANISOU 1810  NZ  LYS A1000     6078   6965   8241   1151    595    851       N  
ATOM   1811  N   TYR A1001      13.333  36.631  11.493  1.00 39.12           N  
ANISOU 1811  N   TYR A1001     4734   5064   5065    752    812    152       N  
ATOM   1812  CA  TYR A1001      13.713  37.685  10.564  1.00 39.17           C  
ANISOU 1812  CA  TYR A1001     4786   5024   5073    695    930    109       C  
ATOM   1813  C   TYR A1001      12.690  38.810  10.467  1.00 38.69           C  
ANISOU 1813  C   TYR A1001     4876   4997   4826    664    875     87       C  
ATOM   1814  O   TYR A1001      11.510  38.631  10.775  1.00 38.73           O  
ANISOU 1814  O   TYR A1001     4974   5057   4684    691    790     82       O  
ATOM   1815  CB  TYR A1001      13.928  37.118   9.170  1.00 39.61           C  
ANISOU 1815  CB  TYR A1001     4904   5009   5137    694   1158     74       C  
ATOM   1816  CG  TYR A1001      14.891  35.965   9.104  1.00 40.54           C  
ANISOU 1816  CG  TYR A1001     4866   5046   5491    737   1272     74       C  
ATOM   1817  CD1 TYR A1001      16.261  36.179   9.039  1.00 42.48           C  
ANISOU 1817  CD1 TYR A1001     4923   5224   5990    726   1368     94       C  
ATOM   1818  CD2 TYR A1001      14.431  34.658   9.070  1.00 40.22           C  
ANISOU 1818  CD2 TYR A1001     4844   4969   5469    788   1302     53       C  
ATOM   1819  CE1 TYR A1001      17.150  35.120   8.959  1.00 43.79           C  
ANISOU 1819  CE1 TYR A1001     4913   5291   6432    783   1489    102       C  
ATOM   1820  CE2 TYR A1001      15.307  33.594   8.986  1.00 41.61           C  
ANISOU 1820  CE2 TYR A1001     4862   5028   5919    841   1431     56       C  
ATOM   1821  CZ  TYR A1001      16.662  33.826   8.936  1.00 43.51           C  
ANISOU 1821  CZ  TYR A1001     4907   5205   6418    848   1524     85       C  
ATOM   1822  OH  TYR A1001      17.517  32.756   8.878  1.00 45.52           O  
ANISOU 1822  OH  TYR A1001     4972   5321   7000    919   1659     98       O  
ATOM   1823  N   LEU A1002      13.176  39.974  10.042  1.00 38.96           N  
ANISOU 1823  N   LEU A1002     4911   4976   4914    610    938     87       N  
ATOM   1824  CA  LEU A1002      12.350  41.135   9.762  1.00 38.52           C  
ANISOU 1824  CA  LEU A1002     4979   4901   4755    591    922     96       C  
ATOM   1825  C   LEU A1002      12.771  41.631   8.406  1.00 39.51           C  
ANISOU 1825  C   LEU A1002     5173   4957   4882    555   1108    157       C  
ATOM   1826  O   LEU A1002      13.943  41.870   8.186  1.00 40.54           O  
ANISOU 1826  O   LEU A1002     5199   5020   5181    508   1225    165       O  
ATOM   1827  CB  LEU A1002      12.591  42.223  10.809  1.00 39.69           C  
ANISOU 1827  CB  LEU A1002     5049   5023   5007    547    817     43       C  
ATOM   1828  CG  LEU A1002      11.789  43.523  10.702  1.00 40.30           C  
ANISOU 1828  CG  LEU A1002     5220   5027   5065    537    813     42       C  
ATOM   1829  CD1 LEU A1002      10.298  43.254  10.662  1.00 39.52           C  
ANISOU 1829  CD1 LEU A1002     5237   4985   4791    607    753     62       C  
ATOM   1830  CD2 LEU A1002      12.095  44.442  11.874  1.00 41.50           C  
ANISOU 1830  CD2 LEU A1002     5286   5145   5336    479    722    -76       C  
ATOM   1831  N   LEU A1003      11.826  41.751   7.489  1.00 39.50           N  
ANISOU 1831  N   LEU A1003     5336   4981   4688    571   1134    212       N  
ATOM   1832  CA  LEU A1003      12.119  42.180   6.137  1.00 41.64           C  
ANISOU 1832  CA  LEU A1003     5713   5226   4880    534   1306    301       C  
ATOM   1833  C   LEU A1003      11.604  43.584   5.917  1.00 42.95           C  
ANISOU 1833  C   LEU A1003     5948   5323   5045    528   1277    420       C  
ATOM   1834  O   LEU A1003      10.500  43.907   6.315  1.00 43.15           O  
ANISOU 1834  O   LEU A1003     6010   5364   5020    575   1126    433       O  
ATOM   1835  CB  LEU A1003      11.430  41.270   5.130  1.00 42.04           C  
ANISOU 1835  CB  LEU A1003     5916   5382   4674    546   1338    292       C  
ATOM   1836  CG  LEU A1003      12.165  40.003   4.739  1.00 42.64           C  
ANISOU 1836  CG  LEU A1003     5964   5473   4763    533   1491    186       C  
ATOM   1837  CD1 LEU A1003      12.248  39.026   5.905  1.00 41.07           C  
ANISOU 1837  CD1 LEU A1003     5615   5261   4728    581   1387     96       C  
ATOM   1838  CD2 LEU A1003      11.447  39.388   3.547  1.00 43.71           C  
ANISOU 1838  CD2 LEU A1003     6288   5712   4604    511   1536    151       C  
ATOM   1839  N   LYS A1004      12.396  44.406   5.248  1.00 44.98           N  
ANISOU 1839  N   LYS A1004     6212   5488   5388    473   1444    521       N  
ATOM   1840  CA  LYS A1004      11.958  45.722   4.830  1.00 45.52           C  
ANISOU 1840  CA  LYS A1004     6356   5459   5479    471   1453    684       C  
ATOM   1841  C   LYS A1004      11.683  45.625   3.339  1.00 46.89           C  
ANISOU 1841  C   LYS A1004     6720   5721   5374    464   1559    850       C  
ATOM   1842  O   LYS A1004      12.571  45.280   2.558  1.00 47.65           O  
ANISOU 1842  O   LYS A1004     6852   5844   5408    407   1769    866       O  
ATOM   1843  CB  LYS A1004      13.050  46.720   5.142  1.00 47.40           C  
ANISOU 1843  CB  LYS A1004     6466   5518   6025    397   1575    696       C  
ATOM   1844  CG  LYS A1004      12.776  48.151   4.732  1.00 50.28           C  
ANISOU 1844  CG  LYS A1004     6883   5715   6502    387   1629    880       C  
ATOM   1845  CD  LYS A1004      13.996  48.943   5.131  1.00 52.55           C  
ANISOU 1845  CD  LYS A1004     7008   5815   7141    287   1761    836       C  
ATOM   1846  CE  LYS A1004      13.933  50.394   4.744  1.00 55.69           C  
ANISOU 1846  CE  LYS A1004     7432   5986   7741    259   1864   1020       C  
ATOM   1847  NZ  LYS A1004      15.105  51.099   5.346  1.00 57.76           N  
ANISOU 1847  NZ  LYS A1004     7496   6052   8395    140   1963    909       N  
ATOM   1848  N   LEU A1005      10.443  45.903   2.957  1.00 47.76           N  
ANISOU 1848  N   LEU A1005     6946   5890   5309    521   1410    970       N  
ATOM   1849  CA  LEU A1005       9.955  45.624   1.609  1.00 50.37           C  
ANISOU 1849  CA  LEU A1005     7472   6376   5290    513   1426   1109       C  
ATOM   1850  C   LEU A1005       9.462  46.866   0.876  1.00 52.38           C  
ANISOU 1850  C   LEU A1005     7824   6575   5501    536   1405   1412       C  
ATOM   1851  O   LEU A1005       8.718  47.664   1.427  1.00 51.19           O  
ANISOU 1851  O   LEU A1005     7604   6309   5534    606   1262   1492       O  
ATOM   1852  CB  LEU A1005       8.807  44.624   1.684  1.00 49.92           C  
ANISOU 1852  CB  LEU A1005     7451   6484   5029    556   1214    996       C  
ATOM   1853  CG  LEU A1005       9.214  43.232   2.161  1.00 49.76           C  
ANISOU 1853  CG  LEU A1005     7368   6523   5016    534   1251    739       C  
ATOM   1854  CD1 LEU A1005       8.222  42.712   3.191  1.00 49.24           C  
ANISOU 1854  CD1 LEU A1005     7206   6476   5024    594   1037    621       C  
ATOM   1855  CD2 LEU A1005       9.348  42.259   1.008  1.00 51.17           C  
ANISOU 1855  CD2 LEU A1005     7696   6854   4889    475   1356    670       C  
ATOM   1856  N   LYS A1006       9.880  47.001  -0.377  1.00 55.57           N  
ANISOU 1856  N   LYS A1006     8390   7058   5663    480   1566   1588       N  
ATOM   1857  CA  LYS A1006       9.351  48.011  -1.272  1.00 58.53           C  
ANISOU 1857  CA  LYS A1006     8895   7430   5912    504   1531   1935       C  
ATOM   1858  C   LYS A1006       8.088  47.466  -1.917  1.00 59.37           C  
ANISOU 1858  C   LYS A1006     9130   7781   5646    542   1275   1991       C  
ATOM   1859  O   LYS A1006       8.086  46.366  -2.465  1.00 59.63           O  
ANISOU 1859  O   LYS A1006     9273   8030   5350    484   1281   1833       O  
ATOM   1860  CB  LYS A1006      10.375  48.345  -2.357  1.00 62.01           C  
ANISOU 1860  CB  LYS A1006     9474   7883   6204    412   1832   2118       C  
ATOM   1861  CG  LYS A1006       9.923  49.386  -3.377  1.00 66.35           C  
ANISOU 1861  CG  LYS A1006    10182   8442   6585    431   1818   2544       C  
ATOM   1862  CD  LYS A1006       9.505  50.685  -2.705  1.00 66.59           C  
ANISOU 1862  CD  LYS A1006    10070   8184   7047    517   1722   2734       C  
ATOM   1863  CE  LYS A1006       9.613  51.883  -3.639  1.00 71.16           C  
ANISOU 1863  CE  LYS A1006    10763   8657   7616    516   1843   3192       C  
ATOM   1864  NZ  LYS A1006       8.527  51.929  -4.652  1.00 74.05           N  
ANISOU 1864  NZ  LYS A1006    11310   9252   7570    576   1614   3506       N  
ATOM   1865  N   PHE A1007       7.017  48.243  -1.839  1.00 59.93           N  
ANISOU 1865  N   PHE A1007     9166   7800   5804    637   1051   2204       N  
ATOM   1866  CA  PHE A1007       5.777  47.932  -2.527  1.00 60.76           C  
ANISOU 1866  CA  PHE A1007     9360   8130   5594    675    772   2321       C  
ATOM   1867  C   PHE A1007       5.779  48.771  -3.801  1.00 65.78           C  
ANISOU 1867  C   PHE A1007    10177   8837   5977    665    795   2736       C  
ATOM   1868  O   PHE A1007       5.919  49.993  -3.740  1.00 66.71           O  
ANISOU 1868  O   PHE A1007    10249   8729   6368    721    864   3019       O  
ATOM   1869  CB  PHE A1007       4.562  48.307  -1.664  1.00 58.43           C  
ANISOU 1869  CB  PHE A1007     8879   7727   5594    800    513   2334       C  
ATOM   1870  CG  PHE A1007       4.339  47.417  -0.466  1.00 54.22           C  
ANISOU 1870  CG  PHE A1007     8192   7175   5234    809    464   1965       C  
ATOM   1871  CD1 PHE A1007       5.330  47.231   0.498  1.00 51.85           C  
ANISOU 1871  CD1 PHE A1007     7803   6729   5166    772    661   1728       C  
ATOM   1872  CD2 PHE A1007       3.111  46.802  -0.265  1.00 53.29           C  
ANISOU 1872  CD2 PHE A1007     8000   7181   5066    854    210   1880       C  
ATOM   1873  CE1 PHE A1007       5.109  46.427   1.616  1.00 48.07           C  
ANISOU 1873  CE1 PHE A1007     7196   6248   4817    784    607   1439       C  
ATOM   1874  CE2 PHE A1007       2.883  46.006   0.854  1.00 49.99           C  
ANISOU 1874  CE2 PHE A1007     7446   6737   4811    860    190   1580       C  
ATOM   1875  CZ  PHE A1007       3.884  45.817   1.793  1.00 47.41           C  
ANISOU 1875  CZ  PHE A1007     7062   6281   4671    828    388   1373       C  
ATOM   1876  N   ASN A1008       5.625  48.123  -4.950  1.00 69.50           N  
ANISOU 1876  N   ASN A1008    10861   9617   5926    588    743   2776       N  
ATOM   1877  CA  ASN A1008       5.548  48.832  -6.227  1.00 75.48           C  
ANISOU 1877  CA  ASN A1008    11826  10510   6342    570    733   3198       C  
ATOM   1878  C   ASN A1008       4.142  48.726  -6.807  1.00 79.36           C  
ANISOU 1878  C   ASN A1008    12356  11247   6547    621    317   3371       C  
ATOM   1879  O   ASN A1008       3.736  47.670  -7.285  1.00 80.23           O  
ANISOU 1879  O   ASN A1008    12569  11655   6260    540    170   3158       O  
ATOM   1880  CB  ASN A1008       6.597  48.286  -7.191  1.00 77.30           C  
ANISOU 1880  CB  ASN A1008    12297  10929   6142    421   1037   3128       C  
ATOM   1881  CG  ASN A1008       8.013  48.528  -6.695  1.00 75.76           C  
ANISOU 1881  CG  ASN A1008    12024  10476   6283    376   1448   3018       C  
ATOM   1882  OD1 ASN A1008       8.451  49.668  -6.579  1.00 77.09           O  
ANISOU 1882  OD1 ASN A1008    12137  10402   6751    407   1592   3294       O  
ATOM   1883  ND2 ASN A1008       8.731  47.455  -6.388  1.00 73.90           N  
ANISOU 1883  ND2 ASN A1008    11759  10274   6043    301   1631   2617       N  
ATOM   1884  N   PHE A1009       3.401  49.829  -6.744  1.00 82.61           N  
ANISOU 1884  N   PHE A1009    12663  11517   7206    753    126   3751       N  
ATOM   1885  CA  PHE A1009       1.972  49.836  -7.050  1.00 85.59           C  
ANISOU 1885  CA  PHE A1009    12977  12067   7474    835   -307   3928       C  
ATOM   1886  C   PHE A1009       1.734  50.048  -8.543  1.00 92.74           C  
ANISOU 1886  C   PHE A1009    14137  13297   7800    785   -463   4321       C  
ATOM   1887  O   PHE A1009       2.662  49.957  -9.346  1.00 95.51           O  
ANISOU 1887  O   PHE A1009    14744  13783   7761    664   -207   4375       O  
ATOM   1888  CB  PHE A1009       1.282  50.961  -6.263  1.00 85.61           C  
ANISOU 1888  CB  PHE A1009    12718  11734   8073   1021   -423   4166       C  
ATOM   1889  CG  PHE A1009       1.215  50.735  -4.777  1.00 81.28           C  
ANISOU 1889  CG  PHE A1009    11920  10927   8032   1073   -346   3779       C  
ATOM   1890  CD1 PHE A1009       0.114  50.108  -4.208  1.00 79.46           C  
ANISOU 1890  CD1 PHE A1009    11509  10771   7909   1126   -610   3570       C  
ATOM   1891  CD2 PHE A1009       2.229  51.193  -3.941  1.00 79.25           C  
ANISOU 1891  CD2 PHE A1009    11603  10360   8148   1063    -15   3638       C  
ATOM   1892  CE1 PHE A1009       0.036  49.915  -2.841  1.00 75.87           C  
ANISOU 1892  CE1 PHE A1009    10848  10101   7877   1169   -520   3240       C  
ATOM   1893  CE2 PHE A1009       2.156  51.004  -2.571  1.00 75.81           C  
ANISOU 1893  CE2 PHE A1009    10960   9726   8118   1102     35   3293       C  
ATOM   1894  CZ  PHE A1009       1.060  50.360  -2.019  1.00 74.27           C  
ANISOU 1894  CZ  PHE A1009    10616   9621   7982   1157   -204   3101       C  
ATOM   1895  N   LYS A1010       0.480  50.323  -8.905  1.00 97.12           N  
ANISOU 1895  N   LYS A1010    14613  13989   8296    876   -884   4600       N  
ATOM   1896  CA  LYS A1010       0.121  50.799 -10.236  1.00103.55           C  
ANISOU 1896  CA  LYS A1010    15631  15087   8626    866  -1101   5093       C  
ATOM   1897  C   LYS A1010      -0.326  52.253 -10.100  1.00106.40           C  
ANISOU 1897  C   LYS A1010    15826  15147   9452   1063  -1195   5645       C  
ATOM   1898  O   LYS A1010      -0.905  52.831 -11.024  1.00112.85           O  
ANISOU 1898  O   LYS A1010    16721  16138  10019   1117  -1466   6155       O  
ATOM   1899  CB  LYS A1010      -1.009  49.962 -10.851  1.00106.28           C  
ANISOU 1899  CB  LYS A1010    15995  15854   8529    810  -1571   5013       C  
ATOM   1900  CG  LYS A1010      -1.143  48.544 -10.317  1.00102.69           C  
ANISOU 1900  CG  LYS A1010    15478  15511   8026    697  -1588   4377       C  
ATOM   1901  CD  LYS A1010       0.060  47.676 -10.639  1.00101.67           C  
ANISOU 1901  CD  LYS A1010    15615  15502   7511    509  -1206   4003       C  
ATOM   1902  CE  LYS A1010       0.111  46.481  -9.701  1.00 97.22           C  
ANISOU 1902  CE  LYS A1010    14907  14853   7178    453  -1118   3405       C  
ATOM   1903  NZ  LYS A1010       0.715  45.293 -10.358  1.00 98.19           N  
ANISOU 1903  NZ  LYS A1010    15280  15240   6786    251   -952   3014       N  
TER    1904      LYS A1010                                                      
HETATM 1905  OH2 1PE A1101      -4.720  49.941  16.657  1.00 71.02           O  
ANISOU 1905  OH2 1PE A1101     8577   8076  10330   1470   1392   -631       O  
HETATM 1906  C12 1PE A1101      -3.460  50.399  16.184  1.00 68.56           C  
ANISOU 1906  C12 1PE A1101     8393   7710   9946   1403   1300   -598       C  
HETATM 1907  C22 1PE A1101      -2.910  49.511  15.123  1.00 66.33           C  
ANISOU 1907  C22 1PE A1101     8178   7594   9430   1367   1068   -356       C  
HETATM 1908  OH3 1PE A1101      -3.977  48.976  14.353  1.00 68.14           O  
ANISOU 1908  OH3 1PE A1101     8285   7875   9727   1453    950   -145       O  
HETATM 1909  C13 1PE A1101      -4.990  47.181  13.165  1.00 71.46           C  
ANISOU 1909  C13 1PE A1101     8616   8574   9960   1462    669    122       C  
HETATM 1910  C23 1PE A1101      -3.727  47.686  13.797  1.00 68.17           C  
ANISOU 1910  C23 1PE A1101     8354   8109   9438   1390    785    -34       C  
HETATM 1911  OH4 1PE A1101      -4.872  47.114  11.745  1.00 72.66           O  
ANISOU 1911  OH4 1PE A1101     8792   8764  10052   1474    450    361       O  
HETATM 1912  C14 1PE A1101      -5.923  45.081  11.018  1.00 75.91           C  
ANISOU 1912  C14 1PE A1101     9110   9469  10260   1408    213    438       C  
HETATM 1913  C24 1PE A1101      -4.634  45.798  11.259  1.00 73.36           C  
ANISOU 1913  C24 1PE A1101     8955   9063   9854   1384    321    386       C  
HETATM 1914  OH5 1PE A1101      -6.262  45.135   9.635  1.00 80.16           O  
ANISOU 1914  OH5 1PE A1101     9623  10061  10772   1430    -27    650       O  
HETATM 1915  C15 1PE A1101      -7.967  45.007   7.935  1.00 84.70           C  
ANISOU 1915  C15 1PE A1101     9957  10757  11469   1493   -451    953       C  
HETATM 1916  C25 1PE A1101      -7.569  44.643   9.335  1.00 82.46           C  
ANISOU 1916  C25 1PE A1101     9711  10418  11200   1455   -171    707       C  
HETATM 1917  OH6 1PE A1101      -7.017  44.501   6.998  1.00 84.83           O  
ANISOU 1917  OH6 1PE A1101    10202  10920  11109   1389   -558    987       O  
HETATM 1918  C16 1PE A1101      -6.326  44.243   4.711  1.00 82.76           C  
ANISOU 1918  C16 1PE A1101    10203  10918  10323   1284   -881   1221       C  
HETATM 1919  C26 1PE A1101      -7.481  44.473   5.648  1.00 85.30           C  
ANISOU 1919  C26 1PE A1101    10249  11118  11040   1381   -850   1185       C  
HETATM 1920  OH7 1PE A1101      -6.055  42.862   4.534  1.00 78.93           O  
ANISOU 1920  OH7 1PE A1101     9811  10593   9584   1141   -895   1022       O  
HETATM 1921  CAJ 09L A1102      -1.039  43.569  21.423  1.00 48.36           C  
ANISOU 1921  CAJ 09L A1102     6423   6689   5261    848   1245   -863       C  
HETATM 1922  CAK 09L A1102      -2.154  42.608  21.257  1.00 48.31           C  
ANISOU 1922  CAK 09L A1102     6331   6704   5319    898   1316   -712       C  
HETATM 1923  CAI 09L A1102      -1.449  43.140  20.036  1.00 46.60           C  
ANISOU 1923  CAI 09L A1102     6094   6351   5258    922   1144   -664       C  
HETATM 1924  CAL 09L A1102      -0.529  42.182  19.312  1.00 44.31           C  
ANISOU 1924  CAL 09L A1102     5833   6120   4883    895    962   -493       C  
HETATM 1925  OAB 09L A1102       0.568  41.902  19.760  1.00 44.98           O  
ANISOU 1925  OAB 09L A1102     5993   6307   4790    834    886   -496       O  
HETATM 1926  NAE 09L A1102      -0.966  41.654  18.155  1.00 42.05           N  
ANISOU 1926  NAE 09L A1102     5476   5768   4733    938    887   -350       N  
HETATM 1927  CAM 09L A1102      -2.223  41.910  17.441  1.00 40.90           C  
ANISOU 1927  CAM 09L A1102     5212   5517   4811   1007    909   -309       C  
HETATM 1928  CAO 09L A1102      -3.012  40.627  17.290  1.00 40.08           C  
ANISOU 1928  CAO 09L A1102     5035   5471   4723    999    906   -205       C  
HETATM 1929  CAN 09L A1102      -0.158  40.639  17.475  1.00 40.17           C  
ANISOU 1929  CAN 09L A1102     5266   5572   4424    909    761   -222       C  
HETATM 1930  CAP 09L A1102      -0.938  39.360  17.383  1.00 39.41           C  
ANISOU 1930  CAP 09L A1102     5113   5512   4346    909    779   -120       C  
HETATM 1931  NAF 09L A1102      -2.187  39.594  16.656  1.00 38.67           N  
ANISOU 1931  NAF 09L A1102     4912   5336   4441    954    782   -108       N  
HETATM 1932  CAQ 09L A1102      -2.422  38.900  15.527  1.00 37.80           C  
ANISOU 1932  CAQ 09L A1102     4761   5203   4398    946    675    -31       C  
HETATM 1933  OAC 09L A1102      -1.649  38.060  15.108  1.00 37.21           O  
ANISOU 1933  OAC 09L A1102     4742   5150   4246    905    616     11       O  
HETATM 1934  CAR 09L A1102      -3.660  39.189  14.739  1.00 37.58           C  
ANISOU 1934  CAR 09L A1102     4606   5119   4553    984    621     -7       C  
HETATM 1935  CAS 09L A1102      -3.486  39.576  13.412  1.00 36.49           C  
ANISOU 1935  CAS 09L A1102     4485   4951   4428    996    468     42       C  
HETATM 1936  CAU 09L A1102      -4.957  38.986  15.174  1.00 39.23           C  
ANISOU 1936  CAU 09L A1102     4670   5317   4918   1000    700    -13       C  
HETATM 1937  FAA 09L A1102      -5.172  38.693  16.473  1.00 39.32           F  
ANISOU 1937  FAA 09L A1102     4679   5368   4891    985    883    -49       F  
HETATM 1938  CAX 09L A1102      -6.042  39.094  14.346  1.00 40.25           C  
ANISOU 1938  CAX 09L A1102     4645   5407   5239   1027    601     26       C  
HETATM 1939  CAW 09L A1102      -5.837  39.456  13.027  1.00 39.80           C  
ANISOU 1939  CAW 09L A1102     4612   5342   5166   1038    405     85       C  
HETATM 1940  CAT 09L A1102      -4.564  39.722  12.548  1.00 37.75           C  
ANISOU 1940  CAT 09L A1102     4524   5093   4725   1023    353     96       C  
HETATM 1941  CAV 09L A1102      -4.358  40.236  11.140  1.00 37.88           C  
ANISOU 1941  CAV 09L A1102     4585   5111   4694   1035    178    183       C  
HETATM 1942  CAY 09L A1102      -3.126  39.684  10.459  1.00 36.91           C  
ANISOU 1942  CAY 09L A1102     4628   5039   4355    966    145    176       C  
HETATM 1943  CAZ 09L A1102      -3.130  38.360   9.810  1.00 37.44           C  
ANISOU 1943  CAZ 09L A1102     4719   5175   4331    879     81    133       C  
HETATM 1944  CBB 09L A1102      -4.256  37.541   9.782  1.00 38.76           C  
ANISOU 1944  CBB 09L A1102     4754   5364   4607    840     25     99       C  
HETATM 1945  CBE 09L A1102      -4.209  36.322   9.127  1.00 39.39           C  
ANISOU 1945  CBE 09L A1102     4862   5481   4623    741    -25     22       C  
HETATM 1946  CBF 09L A1102      -3.055  35.912   8.494  1.00 38.82           C  
ANISOU 1946  CBF 09L A1102     4949   5424   4376    694     -1    -23       C  
HETATM 1947  CBD 09L A1102      -1.924  36.708   8.522  1.00 37.66           C  
ANISOU 1947  CBD 09L A1102     4921   5263   4123    740     65     27       C  
HETATM 1948  CBA 09L A1102      -1.950  37.931   9.189  1.00 36.95           C  
ANISOU 1948  CBA 09L A1102     4802   5136   4101    826     97    106       C  
HETATM 1949  CBC 09L A1102      -0.764  38.786   9.239  1.00 36.17           C  
ANISOU 1949  CBC 09L A1102     4807   5002   3934    854    167    142       C  
HETATM 1950  OAD 09L A1102       0.336  38.439   8.824  1.00 37.06           O  
ANISOU 1950  OAD 09L A1102     5018   5120   3941    814    218    119       O  
HETATM 1951  NAH 09L A1102      -0.924  39.965   9.855  1.00 35.86           N  
ANISOU 1951  NAH 09L A1102     4728   4902   3995    923    198    184       N  
HETATM 1952  NAG 09L A1102      -2.084  40.441  10.470  1.00 36.84           N  
ANISOU 1952  NAG 09L A1102     4725   4991   4281    981    195    191       N  
HETATM 1953  S   SO4 A1103      -7.949  35.602   2.606  1.00 73.90           S  
HETATM 1954  O1  SO4 A1103      -7.243  36.558   1.716  1.00 71.50           O  
HETATM 1955  O2  SO4 A1103      -9.059  35.002   1.851  1.00 71.79           O  
HETATM 1956  O3  SO4 A1103      -7.058  34.503   3.063  1.00 74.50           O  
HETATM 1957  O4  SO4 A1103      -8.480  36.331   3.784  1.00 73.89           O  
HETATM 1958  S   SO4 A1104       0.327  20.765   5.271  1.00104.82           S  
HETATM 1959  O1  SO4 A1104       1.684  20.424   4.770  1.00103.42           O  
HETATM 1960  O2  SO4 A1104      -0.674  20.351   4.259  1.00104.36           O  
HETATM 1961  O3  SO4 A1104       0.057  20.066   6.551  1.00101.67           O  
HETATM 1962  O4  SO4 A1104       0.238  22.230   5.485  1.00102.76           O  
HETATM 1963  O   HOH A1201      16.648  49.602   6.571  1.00 43.97           O  
HETATM 1964  O   HOH A1202      -6.734  33.696  23.526  1.00 43.40           O  
HETATM 1965  O   HOH A1203     -10.382  28.745  17.036  1.00 51.03           O  
HETATM 1966  O   HOH A1204       6.858  37.074  19.290  1.00 34.10           O  
HETATM 1967  O   HOH A1205       2.915  50.443   8.092  1.00 43.94           O  
HETATM 1968  O   HOH A1206      -0.954  32.071   3.880  1.00 36.70           O  
HETATM 1969  O   HOH A1207      -1.976  30.000   1.429  1.00 56.53           O  
HETATM 1970  O   HOH A1208       6.895  51.273  15.792  1.00 44.03           O  
HETATM 1971  O   HOH A1209      12.595  42.091  23.033  1.00 48.68           O  
HETATM 1972  O   HOH A1210      13.389  36.527  18.664  1.00 43.91           O  
HETATM 1973  O   HOH A1211       8.990  32.167  22.669  1.00 43.41           O  
HETATM 1974  O   HOH A1212       1.184  42.014  27.788  1.00 59.09           O  
HETATM 1975  O   HOH A1213       2.814  53.739   4.500  1.00 46.57           O  
HETATM 1976  O   HOH A1214      16.918  51.581   3.268  1.00 53.63           O  
HETATM 1977  O   HOH A1215       4.717  47.866   7.834  1.00 32.30           O  
HETATM 1978  O   HOH A1216       5.349  38.228  23.175  1.00 39.02           O  
HETATM 1979  O   HOH A1217      20.297  39.076  15.475  1.00 46.48           O  
HETATM 1980  O   HOH A1218       5.012  50.278  18.635  1.00 44.90           O  
HETATM 1981  O   HOH A1219      -4.853  38.398  19.589  1.00 52.10           O  
HETATM 1982  O   HOH A1220      19.846  42.546   3.793  1.00 37.90           O  
HETATM 1983  O   HOH A1221      25.807  31.759   2.336  1.00 46.49           O  
HETATM 1984  O   HOH A1222       5.059  35.676  20.535  1.00 50.12           O  
HETATM 1985  O   HOH A1223      12.634  23.935  -3.786  1.00 57.99           O  
HETATM 1986  O   HOH A1224      -4.923  42.409  19.037  1.00 51.59           O  
HETATM 1987  O   HOH A1225       0.568  32.905  26.218  1.00 39.32           O  
HETATM 1988  O   HOH A1226     -15.028  24.296   9.615  1.00 45.65           O  
HETATM 1989  O   HOH A1227       2.460  52.543   9.891  1.00 37.15           O  
ENDMDL                                                                          
MASTER        0    0    0   11   14    0    6    6 1972    1    0   21          
END                                                                             



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