CNRS Nantes University UFIP UFIP
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***  2xoa  ***

elNémo ID: 190111112151107769

Job options:

ID        	=	 190111112151107769
JOBID     	=	 2xoa
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 2xoa
CRYST1  170.800  170.800  301.200  90.00  90.00 120.00 H 3 2        18          
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      0.005855  0.003380  0.000000        0.00000                         
SCALE2      0.000000  0.006761  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003320        0.00000                         
ATOM      1  N   GLN A  12      24.008  -5.667  99.326  1.00 61.80           N  
ANISOU    1  N   GLN A  12     7225   9716   6539   1712   -276   -274       N  
ATOM      2  CA  GLN A  12      24.920  -5.413  98.147  1.00 62.64           C  
ANISOU    2  CA  GLN A  12     7346   9942   6514   1838   -236   -257       C  
ATOM      3  C   GLN A  12      26.258  -4.710  98.461  1.00 60.48           C  
ANISOU    3  C   GLN A  12     7118   9563   6298   1875    -89   -205       C  
ATOM      4  O   GLN A  12      27.314  -5.292  98.287  1.00 60.37           O  
ANISOU    4  O   GLN A  12     7166   9524   6248   1886   -102   -302       O  
ATOM      5  CB  GLN A  12      24.151  -4.663  97.064  1.00 65.19           C  
ANISOU    5  CB  GLN A  12     7576  10471   6721   1950   -223   -124       C  
ATOM      6  CG  GLN A  12      24.372  -5.150  95.630  1.00 70.78           C  
ANISOU    6  CG  GLN A  12     8281  11383   7230   2043   -302   -184       C  
ATOM      7  CD  GLN A  12      24.203  -6.673  95.462  1.00 75.60           C  
ANISOU    7  CD  GLN A  12     8937  12009   7778   1959   -475   -402       C  
ATOM      8  OE1 GLN A  12      23.732  -7.142  94.424  1.00 77.24           O  
ANISOU    8  OE1 GLN A  12     9111  12407   7830   1996   -580   -463       O  
ATOM      9  NE2 GLN A  12      24.631  -7.442  96.471  1.00 75.17           N  
ANISOU    9  NE2 GLN A  12     8962  11756   7844   1848   -499   -521       N  
ATOM     10  N   PHE A  13      26.207  -3.473  98.934  1.00 58.82           N  
ANISOU   10  N   PHE A  13     6875   9291   6184   1891     54    -58       N  
ATOM     11  CA  PHE A  13      27.399  -2.698  99.245  1.00 57.87           C  
ANISOU   11  CA  PHE A  13     6784   9074   6130   1909    203     -7       C  
ATOM     12  C   PHE A  13      27.544  -2.419 100.750  1.00 56.23           C  
ANISOU   12  C   PHE A  13     6601   8671   6092   1794    267    -19       C  
ATOM     13  O   PHE A  13      26.613  -2.652 101.490  1.00 56.29           O  
ANISOU   13  O   PHE A  13     6595   8626   6165   1718    216    -34       O  
ATOM     14  CB  PHE A  13      27.366  -1.394  98.452  1.00 59.18           C  
ANISOU   14  CB  PHE A  13     6897   9324   6263   2029    344    175       C  
ATOM     15  CG  PHE A  13      27.286  -1.599  96.962  1.00 61.59           C  
ANISOU   15  CG  PHE A  13     7175   9842   6384   2154    290    199       C  
ATOM     16  CD1 PHE A  13      28.330  -2.238  96.270  1.00 61.82           C  
ANISOU   16  CD1 PHE A  13     7249   9932   6308   2197    255    104       C  
ATOM     17  CD2 PHE A  13      26.161  -1.156  96.240  1.00 63.99           C  
ANISOU   17  CD2 PHE A  13     7402  10301   6610   2237    275    319       C  
ATOM     18  CE1 PHE A  13      28.255  -2.438  94.870  1.00 64.36           C  
ANISOU   18  CE1 PHE A  13     7548  10465   6442   2317    207    119       C  
ATOM     19  CE2 PHE A  13      26.073  -1.333  94.838  1.00 64.06           C  
ANISOU   19  CE2 PHE A  13     7378  10534   6427   2358    221    342       C  
ATOM     20  CZ  PHE A  13      27.114  -1.976  94.155  1.00 65.31           C  
ANISOU   20  CZ  PHE A  13     7589  10749   6475   2395    187    237       C  
ATOM     21  N   LEU A  14      28.716  -1.966 101.196  1.00 54.74           N  
ANISOU   21  N   LEU A  14     6442   8389   5966   1777    375    -22       N  
ATOM     22  CA  LEU A  14      28.967  -1.607 102.583  1.00 52.90           C  
ANISOU   22  CA  LEU A  14     6229   7993   5879   1670    445    -38       C  
ATOM     23  C   LEU A  14      29.130  -0.116 102.700  1.00 53.59           C  
ANISOU   23  C   LEU A  14     6287   8026   6047   1692    632     95       C  
ATOM     24  O   LEU A  14      29.731   0.514 101.839  1.00 54.21           O  
ANISOU   24  O   LEU A  14     6352   8162   6083   1777    725    171       O  
ATOM     25  CB  LEU A  14      30.254  -2.259 103.098  1.00 52.15           C  
ANISOU   25  CB  LEU A  14     6183   7837   5796   1620    422   -157       C  
ATOM     26  CG  LEU A  14      30.291  -3.770 103.321  1.00 52.14           C  
ANISOU   26  CG  LEU A  14     6228   7832   5752   1581    261   -300       C  
ATOM     27  CD1 LEU A  14      31.696  -4.210 103.715  1.00 53.28           C  
ANISOU   27  CD1 LEU A  14     6408   7933   5903   1565    270   -384       C  
ATOM     28  CD2 LEU A  14      29.271  -4.212 104.374  1.00 49.75           C  
ANISOU   28  CD2 LEU A  14     5932   7445   5526   1482    192   -331       C  
ATOM     29  N   ARG A  15      28.637   0.458 103.793  1.00 54.05           N  
ANISOU   29  N   ARG A  15     6342   7965   6229   1613    699    121       N  
ATOM     30  CA  ARG A  15      28.641   1.914 103.953  1.00 55.20           C  
ANISOU   30  CA  ARG A  15     6468   8037   6470   1629    891    245       C  
ATOM     31  C   ARG A  15      29.118   2.309 105.330  1.00 54.94           C  
ANISOU   31  C   ARG A  15     6462   7849   6566   1505    971    184       C  
ATOM     32  O   ARG A  15      28.974   1.535 106.292  1.00 54.37           O  
ANISOU   32  O   ARG A  15     6412   7729   6515   1413    875     79       O  
ATOM     33  CB  ARG A  15      27.249   2.489 103.741  1.00 55.73           C  
ANISOU   33  CB  ARG A  15     6489   8131   6553   1685    922    372       C  
ATOM     34  CG  ARG A  15      26.727   2.378 102.322  1.00 58.68           C  
ANISOU   34  CG  ARG A  15     6819   8682   6794   1820    869    462       C  
ATOM     35  CD  ARG A  15      25.178   2.451 102.261  1.00 61.25           C  
ANISOU   35  CD  ARG A  15     7087   9071   7114   1855    823    545       C  
ATOM     36  NE  ARG A  15      24.737   2.513 100.866  1.00 66.16           N  
ANISOU   36  NE  ARG A  15     7654   9884   7599   1994    789    646       N  
ATOM     37  CZ  ARG A  15      24.378   1.466 100.115  1.00 67.91           C  
ANISOU   37  CZ  ARG A  15     7855  10266   7681   2018    614    575       C  
ATOM     38  NH1 ARG A  15      24.383   0.227 100.618  1.00 65.77           N  
ANISOU   38  NH1 ARG A  15     7618   9970   7400   1912    460    405       N  
ATOM     39  NH2 ARG A  15      24.010   1.660  98.842  1.00 69.04           N  
ANISOU   39  NH2 ARG A  15     7943  10600   7690   2151    598    675       N  
ATOM     40  N   THR A  16      29.690   3.511 105.438  1.00 55.27           N  
ANISOU   40  N   THR A  16     6501   7810   6690   1499   1152    247       N  
ATOM     41  CA  THR A  16      30.094   3.988 106.748  1.00 54.68           C  
ANISOU   41  CA  THR A  16     6447   7595   6733   1374   1238    181       C  
ATOM     42  C   THR A  16      28.855   3.991 107.639  1.00 54.67           C  
ANISOU   42  C   THR A  16     6447   7532   6792   1328   1216    186       C  
ATOM     43  O   THR A  16      27.740   4.262 107.174  1.00 55.37           O  
ANISOU   43  O   THR A  16     6510   7655   6875   1404   1225    294       O  
ATOM     44  CB  THR A  16      30.789   5.341 106.704  1.00 54.94           C  
ANISOU   44  CB  THR A  16     6477   7540   6859   1363   1448    243       C  
ATOM     45  OG1 THR A  16      29.911   6.319 106.133  1.00 56.52           O  
ANISOU   45  OG1 THR A  16     6660   7719   7097   1456   1572    403       O  
ATOM     46  CG2 THR A  16      32.045   5.238 105.861  1.00 54.67           C  
ANISOU   46  CG2 THR A  16     6434   7577   6763   1402   1462    233       C  
ATOM     47  N   ASP A  17      29.069   3.633 108.901  1.00 53.57           N  
ANISOU   47  N   ASP A  17     6333   7321   6700   1209   1181     73       N  
ATOM     48  CA  ASP A  17      28.010   3.389 109.883  1.00 53.76           C  
ANISOU   48  CA  ASP A  17     6362   7296   6768   1152   1138     54       C  
ATOM     49  C   ASP A  17      27.340   2.029 109.869  1.00 51.37           C  
ANISOU   49  C   ASP A  17     6058   7069   6390   1154    946      9       C  
ATOM     50  O   ASP A  17      26.717   1.670 110.840  1.00 51.17           O  
ANISOU   50  O   ASP A  17     6041   7000   6401   1085    903    -29       O  
ATOM     51  CB  ASP A  17      27.012   4.557 109.954  1.00 55.45           C  
ANISOU   51  CB  ASP A  17     6559   7442   7069   1188   1286    174       C  
ATOM     52  CG  ASP A  17      27.736   5.895 110.166  1.00 62.45           C  
ANISOU   52  CG  ASP A  17     7461   8214   8053   1159   1494    197       C  
ATOM     53  OD1 ASP A  17      28.124   6.163 111.333  1.00 66.30           O  
ANISOU   53  OD1 ASP A  17     7975   8607   8610   1043   1549    101       O  
ATOM     54  OD2 ASP A  17      27.994   6.636 109.155  1.00 69.71           O  
ANISOU   54  OD2 ASP A  17     8367   9146   8975   1248   1600    302       O  
ATOM     55  N   ASP A  18      27.483   1.240 108.816  1.00 50.32           N  
ANISOU   55  N   ASP A  18     5918   7046   6156   1225    832      4       N  
ATOM     56  CA  ASP A  18      27.122  -0.167 108.947  1.00 49.13           C  
ANISOU   56  CA  ASP A  18     5781   6940   5946   1198    653    -78       C  
ATOM     57  C   ASP A  18      27.926  -0.830 110.065  1.00 48.00           C  
ANISOU   57  C   ASP A  18     5679   6734   5824   1101    608   -196       C  
ATOM     58  O   ASP A  18      29.041  -0.442 110.371  1.00 48.22           O  
ANISOU   58  O   ASP A  18     5719   6733   5870   1073    677   -234       O  
ATOM     59  CB  ASP A  18      27.317  -0.911 107.639  1.00 49.40           C  
ANISOU   59  CB  ASP A  18     5811   7095   5864   1284    548    -89       C  
ATOM     60  CG  ASP A  18      26.445  -0.377 106.546  1.00 53.28           C  
ANISOU   60  CG  ASP A  18     6252   7679   6313   1384    571     29       C  
ATOM     61  OD1 ASP A  18      25.598   0.504 106.878  1.00 55.21           O  
ANISOU   61  OD1 ASP A  18     6465   7885   6629   1388    664    125       O  
ATOM     62  OD2 ASP A  18      26.586  -0.816 105.362  1.00 55.41           O  
ANISOU   62  OD2 ASP A  18     6513   8068   6473   1465    501     29       O  
ATOM     63  N   GLU A  19      27.363  -1.844 110.675  1.00 47.24           N  
ANISOU   63  N   GLU A  19     5600   6626   5725   1051    492   -250       N  
ATOM     64  CA  GLU A  19      28.085  -2.610 111.660  1.00 47.27           C  
ANISOU   64  CA  GLU A  19     5641   6588   5733    979    437   -347       C  
ATOM     65  C   GLU A  19      28.547  -3.938 111.029  1.00 46.24           C  
ANISOU   65  C   GLU A  19     5539   6510   5520   1017    299   -416       C  
ATOM     66  O   GLU A  19      27.769  -4.610 110.309  1.00 45.98           O  
ANISOU   66  O   GLU A  19     5504   6520   5445   1050    206   -413       O  
ATOM     67  CB  GLU A  19      27.142  -2.831 112.819  1.00 47.56           C  
ANISOU   67  CB  GLU A  19     5682   6563   5826    901    420   -349       C  
ATOM     68  CG  GLU A  19      27.726  -3.338 114.084  1.00 52.92           C  
ANISOU   68  CG  GLU A  19     6393   7196   6520    823    397   -423       C  
ATOM     69  CD  GLU A  19      26.712  -3.215 115.250  1.00 62.19           C  
ANISOU   69  CD  GLU A  19     7564   8311   7756    751    421   -403       C  
ATOM     70  OE1 GLU A  19      26.007  -2.157 115.344  1.00 65.26           O  
ANISOU   70  OE1 GLU A  19     7925   8673   8198    750    527   -339       O  
ATOM     71  OE2 GLU A  19      26.623  -4.177 116.068  1.00 64.66           O  
ANISOU   71  OE2 GLU A  19     7902   8603   8062    704    342   -444       O  
ATOM     72  N   VAL A  20      29.799  -4.318 111.273  1.00 44.45           N  
ANISOU   72  N   VAL A  20     5336   6284   5269   1013    288   -483       N  
ATOM     73  CA  VAL A  20      30.356  -5.489 110.593  1.00 44.07           C  
ANISOU   73  CA  VAL A  20     5319   6280   5145   1067    180   -546       C  
ATOM     74  C   VAL A  20      31.130  -6.430 111.534  1.00 44.55           C  
ANISOU   74  C   VAL A  20     5416   6304   5206   1031    122   -620       C  
ATOM     75  O   VAL A  20      31.532  -6.035 112.629  1.00 44.44           O  
ANISOU   75  O   VAL A  20     5393   6259   5234    969    175   -626       O  
ATOM     76  CB  VAL A  20      31.371  -5.065 109.470  1.00 44.65           C  
ANISOU   76  CB  VAL A  20     5378   6429   5159   1152    228   -538       C  
ATOM     77  CG1 VAL A  20      30.730  -4.191 108.405  1.00 42.52           C  
ANISOU   77  CG1 VAL A  20     5074   6213   4871   1212    286   -451       C  
ATOM     78  CG2 VAL A  20      32.630  -4.378 110.077  1.00 42.94           C  
ANISOU   78  CG2 VAL A  20     5142   6201   4971   1121    325   -551       C  
ATOM     79  N   VAL A  21      31.362  -7.656 111.090  1.00 44.42           N  
ANISOU   79  N   VAL A  21     5440   6297   5140   1074     20   -676       N  
ATOM     80  CA  VAL A  21      32.352  -8.525 111.711  1.00 44.55           C  
ANISOU   80  CA  VAL A  21     5487   6296   5143   1079    -21   -733       C  
ATOM     81  C   VAL A  21      33.464  -8.795 110.693  1.00 45.82           C  
ANISOU   81  C   VAL A  21     5653   6523   5232   1174    -27   -768       C  
ATOM     82  O   VAL A  21      33.272  -8.606 109.467  1.00 46.60           O  
ANISOU   82  O   VAL A  21     5747   6675   5284   1234    -27   -760       O  
ATOM     83  CB  VAL A  21      31.761  -9.844 112.208  1.00 44.82           C  
ANISOU   83  CB  VAL A  21     5576   6260   5193   1054   -120   -768       C  
ATOM     84  CG1 VAL A  21      30.816  -9.575 113.348  1.00 43.14           C  
ANISOU   84  CG1 VAL A  21     5353   5991   5049    962   -103   -728       C  
ATOM     85  CG2 VAL A  21      31.035 -10.556 111.104  1.00 44.71           C  
ANISOU   85  CG2 VAL A  21     5591   6250   5148   1089   -198   -798       C  
ATOM     86  N   LEU A  22      34.643  -9.149 111.187  1.00 45.34           N  
ANISOU   86  N   LEU A  22     5593   6477   5158   1193    -24   -800       N  
ATOM     87  CA  LEU A  22      35.788  -9.425 110.297  1.00 46.03           C  
ANISOU   87  CA  LEU A  22     5679   6633   5180   1289    -22   -831       C  
ATOM     88  C   LEU A  22      36.050 -10.889 110.454  1.00 46.32           C  
ANISOU   88  C   LEU A  22     5776   6628   5195   1335   -111   -886       C  
ATOM     89  O   LEU A  22      36.462 -11.372 111.548  1.00 45.34           O  
ANISOU   89  O   LEU A  22     5658   6474   5096   1313   -128   -891       O  
ATOM     90  CB  LEU A  22      37.023  -8.601 110.665  1.00 46.29           C  
ANISOU   90  CB  LEU A  22     5647   6727   5213   1282     65   -819       C  
ATOM     91  CG  LEU A  22      36.978  -7.164 110.136  1.00 48.00           C  
ANISOU   91  CG  LEU A  22     5811   6980   5447   1261    174   -767       C  
ATOM     92  CD1 LEU A  22      38.300  -6.479 110.356  1.00 49.12           C  
ANISOU   92  CD1 LEU A  22     5889   7184   5590   1251    257   -770       C  
ATOM     93  CD2 LEU A  22      36.788  -7.265 108.673  1.00 53.52           C  
ANISOU   93  CD2 LEU A  22     6526   7723   6084   1352    164   -756       C  
ATOM     94  N   GLN A  23      35.728 -11.595 109.384  1.00 46.42           N  
ANISOU   94  N   GLN A  23     5835   6638   5163   1397   -166   -927       N  
ATOM     95  CA  GLN A  23      35.765 -13.025 109.379  1.00 48.05           C  
ANISOU   95  CA  GLN A  23     6116   6779   5361   1437   -246   -988       C  
ATOM     96  C   GLN A  23      36.882 -13.591 108.462  1.00 48.92           C  
ANISOU   96  C   GLN A  23     6248   6941   5399   1559   -247  -1040       C  
ATOM     97  O   GLN A  23      37.169 -13.059 107.368  1.00 48.85           O  
ANISOU   97  O   GLN A  23     6214   7019   5327   1615   -213  -1042       O  
ATOM     98  CB  GLN A  23      34.391 -13.554 108.977  1.00 48.77           C  
ANISOU   98  CB  GLN A  23     6253   6809   5467   1394   -314  -1018       C  
ATOM     99  CG  GLN A  23      34.303 -15.053 108.836  1.00 52.09           C  
ANISOU   99  CG  GLN A  23     6761   7141   5889   1424   -389  -1095       C  
ATOM    100  CD  GLN A  23      32.916 -15.537 108.475  1.00 56.74           C  
ANISOU  100  CD  GLN A  23     7383   7675   6499   1358   -457  -1134       C  
ATOM    101  OE1 GLN A  23      32.008 -15.512 109.308  1.00 63.17           O  
ANISOU  101  OE1 GLN A  23     8190   8428   7385   1264   -470  -1097       O  
ATOM    102  NE2 GLN A  23      32.750 -16.016 107.253  1.00 57.49           N  
ANISOU  102  NE2 GLN A  23     7512   7800   6531   1403   -500  -1213       N  
ATOM    103  N   CYS A  24      37.498 -14.665 108.931  1.00 49.48           N  
ANISOU  103  N   CYS A  24     6364   6958   5477   1607   -278  -1071       N  
ATOM    104  CA  CYS A  24      38.500 -15.387 108.180  1.00 51.94           C  
ANISOU  104  CA  CYS A  24     6706   7299   5729   1731   -279  -1123       C  
ATOM    105  C   CYS A  24      38.248 -16.860 108.412  1.00 53.80           C  
ANISOU  105  C   CYS A  24     7040   7408   5994   1758   -341  -1178       C  
ATOM    106  O   CYS A  24      37.380 -17.210 109.193  1.00 53.42           O  
ANISOU  106  O   CYS A  24     7022   7262   6012   1675   -376  -1164       O  
ATOM    107  CB  CYS A  24      39.899 -14.996 108.620  1.00 51.04           C  
ANISOU  107  CB  CYS A  24     6523   7273   5599   1783   -221  -1084       C  
ATOM    108  SG  CYS A  24      40.274 -15.503 110.271  1.00 53.71           S  
ANISOU  108  SG  CYS A  24     6852   7562   5994   1756   -235  -1042       S  
ATOM    109  N   SER A  25      38.943 -17.726 107.677  1.00 57.21           N  
ANISOU  109  N   SER A  25     7525   7832   6380   1872   -347  -1241       N  
ATOM    110  CA  SER A  25      38.775 -19.161 107.860  1.00 60.28           C  
ANISOU  110  CA  SER A  25     8018   8079   6807   1906   -389  -1297       C  
ATOM    111  C   SER A  25      40.071 -19.884 107.935  1.00 62.67           C  
ANISOU  111  C   SER A  25     8339   8383   7089   2043   -359  -1301       C  
ATOM    112  O   SER A  25      41.103 -19.415 107.471  1.00 63.41           O  
ANISOU  112  O   SER A  25     8375   8599   7120   2127   -314  -1289       O  
ATOM    113  CB  SER A  25      37.856 -19.811 106.834  1.00 61.05           C  
ANISOU  113  CB  SER A  25     8198   8110   6887   1889   -441  -1403       C  
ATOM    114  OG  SER A  25      37.878 -19.122 105.617  1.00 62.88           O  
ANISOU  114  OG  SER A  25     8396   8467   7029   1918   -431  -1436       O  
ATOM    115  N   ALA A  26      39.989 -21.029 108.578  1.00 65.74           N  
ANISOU  115  N   ALA A  26     8806   8633   7539   2064   -378  -1306       N  
ATOM    116  CA  ALA A  26      41.116 -21.858 108.863  1.00 69.28           C  
ANISOU  116  CA  ALA A  26     9279   9059   7986   2201   -348  -1291       C  
ATOM    117  C   ALA A  26      40.598 -23.227 108.611  1.00 72.67           C  
ANISOU  117  C   ALA A  26     9844   9301   8464   2225   -372  -1368       C  
ATOM    118  O   ALA A  26      39.419 -23.505 108.800  1.00 72.37           O  
ANISOU  118  O   ALA A  26     9859   9151   8487   2112   -412  -1395       O  
ATOM    119  CB  ALA A  26      41.542 -21.714 110.298  1.00 68.23           C  
ANISOU  119  CB  ALA A  26     9084   8949   7891   2190   -335  -1178       C  
ATOM    120  N   THR A  27      41.481 -24.082 108.127  1.00 77.79           N  
ANISOU  120  N   THR A  27    10549   9916   9090   2373   -340  -1412       N  
ATOM    121  CA  THR A  27      41.096 -25.443 107.844  1.00 82.14           C  
ANISOU  121  CA  THR A  27    11242  10271   9696   2406   -346  -1498       C  
ATOM    122  C   THR A  27      41.686 -26.241 108.974  1.00 84.21           C  
ANISOU  122  C   THR A  27    11529  10442  10026   2490   -312  -1403       C  
ATOM    123  O   THR A  27      42.878 -26.178 109.228  1.00 84.34           O  
ANISOU  123  O   THR A  27    11486  10555  10003   2619   -271  -1335       O  
ATOM    124  CB  THR A  27      41.517 -25.897 106.421  1.00 83.65           C  
ANISOU  124  CB  THR A  27    11498  10469   9815   2511   -328  -1631       C  
ATOM    125  OG1 THR A  27      41.735 -27.315 106.414  1.00 86.82           O  
ANISOU  125  OG1 THR A  27    12030  10683  10276   2605   -298  -1686       O  
ATOM    126  CG2 THR A  27      42.775 -25.137 105.921  1.00 83.43           C  
ANISOU  126  CG2 THR A  27    11371  10644   9685   2631   -282  -1596       C  
ATOM    127  N   VAL A  28      40.807 -26.913 109.703  1.00 87.10           N  
ANISOU  127  N   VAL A  28    11967  10636  10490   2408   -330  -1384       N  
ATOM    128  CA  VAL A  28      41.183 -27.637 110.907  1.00 90.05           C  
ANISOU  128  CA  VAL A  28    12363  10919  10931   2474   -298  -1269       C  
ATOM    129  C   VAL A  28      40.407 -28.964 111.035  1.00 92.80           C  
ANISOU  129  C   VAL A  28    12862  11003  11394   2449   -288  -1313       C  
ATOM    130  O   VAL A  28      39.162 -28.992 111.021  1.00 92.73           O  
ANISOU  130  O   VAL A  28    12892  10900  11442   2291   -327  -1363       O  
ATOM    131  CB  VAL A  28      41.134 -26.714 112.156  1.00 88.77           C  
ANISOU  131  CB  VAL A  28    12082  10883  10764   2398   -314  -1131       C  
ATOM    132  CG1 VAL A  28      40.413 -27.370 113.349  1.00 89.50           C  
ANISOU  132  CG1 VAL A  28    12226  10824  10954   2337   -314  -1046       C  
ATOM    133  CG2 VAL A  28      42.569 -26.265 112.514  1.00 89.67           C  
ANISOU  133  CG2 VAL A  28    12085  11183  10801   2530   -281  -1045       C  
ATOM    134  N   LEU A  29      41.186 -30.050 111.132  1.00 95.90           N  
ANISOU  134  N   LEU A  29    13336  11281  11822   2610   -227  -1294       N  
ATOM    135  CA  LEU A  29      40.706 -31.432 110.973  1.00 98.82           C  
ANISOU  135  CA  LEU A  29    13869  11378  12301   2622   -193  -1362       C  
ATOM    136  C   LEU A  29      39.972 -31.631 109.626  1.00 99.37           C  
ANISOU  136  C   LEU A  29    14020  11373  12362   2535   -223  -1566       C  
ATOM    137  O   LEU A  29      38.843 -32.137 109.574  1.00 99.71           O  
ANISOU  137  O   LEU A  29    14144  11251  12491   2397   -245  -1641       O  
ATOM    138  CB  LEU A  29      39.864 -31.869 112.189  1.00 99.47           C  
ANISOU  138  CB  LEU A  29    13985  11312  12497   2524   -190  -1257       C  
ATOM    139  CG  LEU A  29      40.674 -32.275 113.436  1.00101.76           C  
ANISOU  139  CG  LEU A  29    14253  11600  12810   2663   -135  -1069       C  
ATOM    140  CD1 LEU A  29      41.038 -31.074 114.343  1.00101.30           C  
ANISOU  140  CD1 LEU A  29    14028  11795  12667   2640   -172   -935       C  
ATOM    141  CD2 LEU A  29      39.928 -33.357 114.236  1.00104.68           C  
ANISOU  141  CD2 LEU A  29    14737  11714  13322   2623    -94  -1006       C  
ATOM    142  N   LYS A  30      40.639 -31.213 108.545  1.00 99.34           N  
ANISOU  142  N   LYS A  30    13986  11510  12248   2617   -223  -1654       N  
ATOM    143  CA  LYS A  30      40.075 -31.202 107.176  1.00 99.65           C  
ANISOU  143  CA  LYS A  30    14076  11549  12237   2550   -259  -1846       C  
ATOM    144  C   LYS A  30      38.616 -30.659 107.076  1.00 98.36           C  
ANISOU  144  C   LYS A  30    13885  11397  12090   2326   -341  -1899       C  
ATOM    145  O   LYS A  30      37.787 -31.176 106.324  1.00 99.64           O  
ANISOU  145  O   LYS A  30    14129  11455  12272   2235   -371  -2054       O  
ATOM    146  CB  LYS A  30      40.242 -32.579 106.495  1.00102.14           C  
ANISOU  146  CB  LYS A  30    14558  11649  12603   2638   -204  -1987       C  
ATOM    147  N   GLU A  31      38.320 -29.614 107.845  1.00 95.89           N  
ANISOU  147  N   GLU A  31    13449  11217  11765   2240   -376  -1773       N  
ATOM    148  CA  GLU A  31      37.011 -28.931 107.799  1.00 93.71           C  
ANISOU  148  CA  GLU A  31    13123  10986  11496   2046   -447  -1797       C  
ATOM    149  C   GLU A  31      37.254 -27.432 107.927  1.00 90.40           C  
ANISOU  149  C   GLU A  31    12553  10807  10987   2030   -466  -1704       C  
ATOM    150  O   GLU A  31      38.177 -27.023 108.649  1.00 89.64           O  
ANISOU  150  O   GLU A  31    12390  10797  10873   2116   -429  -1582       O  
ATOM    151  CB  GLU A  31      36.086 -29.420 108.932  1.00 93.91           C  
ANISOU  151  CB  GLU A  31    13181  10847  11655   1926   -452  -1726       C  
ATOM    152  N   GLN A  32      36.459 -26.620 107.226  1.00 87.62           N  
ANISOU  152  N   GLN A  32    12146  10567  10579   1924   -519  -1760       N  
ATOM    153  CA  GLN A  32      36.558 -25.168 107.409  1.00 84.44           C  
ANISOU  153  CA  GLN A  32    11607  10364  10111   1895   -525  -1664       C  
ATOM    154  C   GLN A  32      36.026 -24.718 108.773  1.00 80.85           C  
ANISOU  154  C   GLN A  32    11095   9893   9733   1794   -529  -1534       C  
ATOM    155  O   GLN A  32      34.955 -25.139 109.231  1.00 80.96           O  
ANISOU  155  O   GLN A  32    11144   9787   9831   1677   -557  -1538       O  
ATOM    156  CB  GLN A  32      35.896 -24.366 106.268  1.00 84.93           C  
ANISOU  156  CB  GLN A  32    11622  10561  10088   1831   -569  -1739       C  
ATOM    157  CG  GLN A  32      36.571 -24.497 104.860  1.00 89.27           C  
ANISOU  157  CG  GLN A  32    12202  11195  10523   1946   -559  -1852       C  
ATOM    158  CD  GLN A  32      38.100 -24.237 104.854  1.00 92.49           C  
ANISOU  158  CD  GLN A  32    12573  11696  10874   2107   -491  -1792       C  
ATOM    159  OE1 GLN A  32      38.896 -25.121 105.217  1.00 94.67           O  
ANISOU  159  OE1 GLN A  32    12911  11873  11188   2212   -452  -1789       O  
ATOM    160  NE2 GLN A  32      38.505 -23.032 104.421  1.00 91.00           N  
ANISOU  160  NE2 GLN A  32    12281  11698  10597   2131   -473  -1740       N  
ATOM    161  N   LEU A  33      36.811 -23.883 109.432  1.00 76.81           N  
ANISOU  161  N   LEU A  33    10491   9503   9189   1839   -495  -1422       N  
ATOM    162  CA  LEU A  33      36.373 -23.227 110.643  1.00 72.95           C  
ANISOU  162  CA  LEU A  33     9934   9039   8745   1745   -494  -1308       C  
ATOM    163  C   LEU A  33      36.323 -21.743 110.343  1.00 69.11           C  
ANISOU  163  C   LEU A  33     9335   8730   8193   1699   -491  -1280       C  
ATOM    164  O   LEU A  33      37.310 -21.162 109.923  1.00 68.14           O  
ANISOU  164  O   LEU A  33     9159   8733   7998   1783   -459  -1272       O  
ATOM    165  CB  LEU A  33      37.338 -23.524 111.786  1.00 73.54           C  
ANISOU  165  CB  LEU A  33     9994   9108   8838   1830   -454  -1204       C  
ATOM    166  CG  LEU A  33      36.994 -23.053 113.207  1.00 75.42           C  
ANISOU  166  CG  LEU A  33    10174   9364   9117   1748   -449  -1087       C  
ATOM    167  CD1 LEU A  33      35.638 -23.604 113.717  1.00 78.84           C  
ANISOU  167  CD1 LEU A  33    10667   9644   9646   1626   -474  -1080       C  
ATOM    168  CD2 LEU A  33      38.120 -23.427 114.168  1.00 76.80           C  
ANISOU  168  CD2 LEU A  33    10331   9567   9282   1860   -414   -994       C  
ATOM    169  N   LYS A  34      35.158 -21.137 110.517  1.00 65.57           N  
ANISOU  169  N   LYS A  34     8852   8288   7774   1569   -517  -1263       N  
ATOM    170  CA  LYS A  34      35.048 -19.706 110.371  1.00 61.94           C  
ANISOU  170  CA  LYS A  34     8290   7974   7269   1526   -499  -1220       C  
ATOM    171  C   LYS A  34      35.322 -19.060 111.716  1.00 58.87           C  
ANISOU  171  C   LYS A  34     7837   7621   6909   1490   -462  -1113       C  
ATOM    172  O   LYS A  34      34.951 -19.587 112.752  1.00 58.73           O  
ANISOU  172  O   LYS A  34     7846   7513   6955   1446   -469  -1069       O  
ATOM    173  CB  LYS A  34      33.674 -19.318 109.837  1.00 62.29           C  
ANISOU  173  CB  LYS A  34     8321   8023   7324   1419   -538  -1249       C  
ATOM    174  CG  LYS A  34      33.332 -19.859 108.476  1.00 64.95           C  
ANISOU  174  CG  LYS A  34     8709   8357   7613   1442   -582  -1365       C  
ATOM    175  CD  LYS A  34      32.220 -19.032 107.861  1.00 70.24           C  
ANISOU  175  CD  LYS A  34     9319   9112   8256   1360   -611  -1366       C  
ATOM    176  CE  LYS A  34      31.412 -19.805 106.778  1.00 75.18           C  
ANISOU  176  CE  LYS A  34     9995   9713   8855   1331   -681  -1491       C  
ATOM    177  NZ  LYS A  34      30.146 -19.072 106.383  1.00 75.05           N  
ANISOU  177  NZ  LYS A  34     9907   9784   8824   1240   -718  -1475       N  
ATOM    178  N   LEU A  35      35.988 -17.920 111.689  1.00 56.05           N  
ANISOU  178  N   LEU A  35     7394   7398   6503   1506   -418  -1076       N  
ATOM    179  CA  LEU A  35      36.378 -17.219 112.897  1.00 54.03           C  
ANISOU  179  CA  LEU A  35     7069   7198   6261   1469   -380   -996       C  
ATOM    180  C   LEU A  35      36.262 -15.701 112.703  1.00 52.89           C  
ANISOU  180  C   LEU A  35     6837   7162   6095   1410   -333   -971       C  
ATOM    181  O   LEU A  35      36.554 -15.208 111.621  1.00 52.98           O  
ANISOU  181  O   LEU A  35     6828   7244   6060   1452   -315   -999       O  
ATOM    182  CB  LEU A  35      37.808 -17.547 113.252  1.00 53.95           C  
ANISOU  182  CB  LEU A  35     7040   7245   6215   1573   -357   -978       C  
ATOM    183  CG  LEU A  35      38.203 -19.006 113.415  1.00 54.97           C  
ANISOU  183  CG  LEU A  35     7252   7274   6360   1667   -381   -989       C  
ATOM    184  CD1 LEU A  35      39.466 -19.225 112.619  1.00 55.20           C  
ANISOU  184  CD1 LEU A  35     7272   7375   6327   1803   -360  -1022       C  
ATOM    185  CD2 LEU A  35      38.416 -19.349 114.847  1.00 54.35           C  
ANISOU  185  CD2 LEU A  35     7163   7178   6309   1662   -377   -909       C  
ATOM    186  N   CYS A  36      35.868 -14.974 113.752  1.00 50.84           N  
ANISOU  186  N   CYS A  36     6532   6914   5871   1319   -306   -916       N  
ATOM    187  CA  CYS A  36      35.684 -13.541 113.683  1.00 49.80           C  
ANISOU  187  CA  CYS A  36     6328   6857   5738   1258   -248   -891       C  
ATOM    188  C   CYS A  36      36.666 -12.848 114.599  1.00 47.60           C  
ANISOU  188  C   CYS A  36     5979   6661   5445   1242   -195   -864       C  
ATOM    189  O   CYS A  36      36.961 -13.323 115.690  1.00 46.55           O  
ANISOU  189  O   CYS A  36     5848   6521   5317   1235   -210   -843       O  
ATOM    190  CB  CYS A  36      34.273 -13.173 114.147  1.00 49.88           C  
ANISOU  190  CB  CYS A  36     6340   6809   5805   1153   -251   -860       C  
ATOM    191  SG  CYS A  36      32.941 -13.636 113.004  1.00 60.07           S  
ANISOU  191  SG  CYS A  36     7676   8041   7108   1142   -309   -893       S  
ATOM    192  N   LEU A  37      37.164 -11.702 114.161  1.00 46.54           N  
ANISOU  192  N   LEU A  37     5781   6611   5293   1233   -129   -863       N  
ATOM    193  CA  LEU A  37      38.005 -10.876 115.006  1.00 45.72           C  
ANISOU  193  CA  LEU A  37     5601   6589   5183   1190    -72   -852       C  
ATOM    194  C   LEU A  37      37.199 -10.391 116.242  1.00 45.60           C  
ANISOU  194  C   LEU A  37     5577   6537   5211   1078    -53   -827       C  
ATOM    195  O   LEU A  37      36.079  -9.871 116.108  1.00 44.06           O  
ANISOU  195  O   LEU A  37     5397   6285   5060   1020    -32   -810       O  
ATOM    196  CB  LEU A  37      38.513  -9.707 114.167  1.00 45.78           C  
ANISOU  196  CB  LEU A  37     5549   6666   5179   1189      8   -855       C  
ATOM    197  CG  LEU A  37      39.614  -8.804 114.716  1.00 47.29           C  
ANISOU  197  CG  LEU A  37     5652   6954   5363   1146     78   -864       C  
ATOM    198  CD1 LEU A  37      40.882  -9.595 114.822  1.00 50.64           C  
ANISOU  198  CD1 LEU A  37     6048   7460   5734   1229     42   -881       C  
ATOM    199  CD2 LEU A  37      39.851  -7.670 113.770  1.00 48.57           C  
ANISOU  199  CD2 LEU A  37     5770   7149   5533   1138    168   -856       C  
ATOM    200  N   ALA A  38      37.783 -10.577 117.430  1.00 45.75           N  
ANISOU  200  N   ALA A  38     5568   6603   5213   1057    -60   -824       N  
ATOM    201  CA  ALA A  38      37.172 -10.249 118.718  1.00 45.49           C  
ANISOU  201  CA  ALA A  38     5528   6555   5202    962    -45   -806       C  
ATOM    202  C   ALA A  38      38.168  -9.549 119.645  1.00 46.63           C  
ANISOU  202  C   ALA A  38     5592   6817   5310    914     -3   -829       C  
ATOM    203  O   ALA A  38      39.383  -9.773 119.542  1.00 48.62           O  
ANISOU  203  O   ALA A  38     5797   7165   5513    971    -15   -845       O  
ATOM    204  CB  ALA A  38      36.660 -11.495 119.383  1.00 44.76           C  
ANISOU  204  CB  ALA A  38     5497   6397   5114    987   -114   -773       C  
ATOM    205  N   ALA A  39      37.657  -8.722 120.555  1.00 46.22           N  
ANISOU  205  N   ALA A  39     5519   6765   5278    809     46   -835       N  
ATOM    206  CA  ALA A  39      38.443  -8.148 121.653  1.00 46.31           C  
ANISOU  206  CA  ALA A  39     5459   6891   5247    743     76   -871       C  
ATOM    207  C   ALA A  39      37.522  -7.698 122.794  1.00 46.38           C  
ANISOU  207  C   ALA A  39     5482   6869   5272    644    107   -870       C  
ATOM    208  O   ALA A  39      36.378  -7.300 122.555  1.00 46.13           O  
ANISOU  208  O   ALA A  39     5493   6733   5302    607    143   -851       O  
ATOM    209  CB  ALA A  39      39.239  -6.983 121.157  1.00 46.52           C  
ANISOU  209  CB  ALA A  39     5415   6979   5281    698    155   -922       C  
ATOM    210  N   GLU A  40      38.003  -7.752 124.032  1.00 46.24           N  
ANISOU  210  N   GLU A  40     5424   6953   5192    608     95   -887       N  
ATOM    211  CA  GLU A  40      37.196  -7.291 125.109  1.00 45.53           C  
ANISOU  211  CA  GLU A  40     5346   6846   5106    518    132   -894       C  
ATOM    212  C   GLU A  40      37.378  -5.806 125.281  1.00 46.71           C  
ANISOU  212  C   GLU A  40     5447   7024   5278    405    234   -973       C  
ATOM    213  O   GLU A  40      36.401  -5.102 125.509  1.00 45.66           O  
ANISOU  213  O   GLU A  40     5344   6808   5198    338    301   -979       O  
ATOM    214  CB  GLU A  40      37.473  -8.007 126.391  1.00 45.73           C  
ANISOU  214  CB  GLU A  40     5359   6969   5048    529     78   -873       C  
ATOM    215  CG  GLU A  40      36.410  -7.691 127.449  1.00 45.86           C  
ANISOU  215  CG  GLU A  40     5406   6951   5070    449    115   -865       C  
ATOM    216  CD  GLU A  40      35.058  -8.385 127.193  1.00 46.82           C  
ANISOU  216  CD  GLU A  40     5611   6921   5259    481     96   -784       C  
ATOM    217  OE1 GLU A  40      35.058  -9.519 126.658  1.00 47.87           O  
ANISOU  217  OE1 GLU A  40     5783   7001   5402    572     27   -726       O  
ATOM    218  OE2 GLU A  40      33.992  -7.826 127.578  1.00 44.88           O  
ANISOU  218  OE2 GLU A  40     5389   6608   5055    412    152   -781       O  
ATOM    219  N   GLY A  41      38.615  -5.323 125.135  1.00 47.82           N  
ANISOU  219  N   GLY A  41     5511   7273   5385    385    253  -1035       N  
ATOM    220  CA  GLY A  41      38.911  -3.898 125.316  1.00 48.45           C  
ANISOU  220  CA  GLY A  41     5541   7375   5494    264    360  -1123       C  
ATOM    221  C   GLY A  41      39.326  -3.645 126.745  1.00 50.09           C  
ANISOU  221  C   GLY A  41     5697   7713   5622    175    359  -1194       C  
ATOM    222  O   GLY A  41      40.531  -3.615 127.067  1.00 51.28           O  
ANISOU  222  O   GLY A  41     5761   8021   5703    155    334  -1249       O  
ATOM    223  N   PHE A  42      38.347  -3.489 127.626  1.00 50.31           N  
ANISOU  223  N   PHE A  42     5771   7695   5649    125    384  -1193       N  
ATOM    224  CA  PHE A  42      38.678  -3.261 129.021  1.00 51.96           C  
ANISOU  224  CA  PHE A  42     5935   8041   5767     43    383  -1264       C  
ATOM    225  C   PHE A  42      39.289  -4.537 129.549  1.00 51.91           C  
ANISOU  225  C   PHE A  42     5899   8174   5650    135    262  -1207       C  
ATOM    226  O   PHE A  42      38.826  -5.638 129.207  1.00 50.59           O  
ANISOU  226  O   PHE A  42     5790   7937   5494    247    195  -1100       O  
ATOM    227  CB  PHE A  42      37.449  -2.887 129.853  1.00 52.49           C  
ANISOU  227  CB  PHE A  42     6062   8030   5851    -18    440  -1268       C  
ATOM    228  CG  PHE A  42      36.593  -1.830 129.227  1.00 55.12           C  
ANISOU  228  CG  PHE A  42     6442   8192   6308    -69    560  -1283       C  
ATOM    229  CD1 PHE A  42      35.357  -2.174 128.614  1.00 55.98           C  
ANISOU  229  CD1 PHE A  42     6626   8148   6496     -2    562  -1182       C  
ATOM    230  CD2 PHE A  42      36.995  -0.493 129.238  1.00 55.98           C  
ANISOU  230  CD2 PHE A  42     6519   8294   6459   -182    674  -1396       C  
ATOM    231  CE1 PHE A  42      34.530  -1.191 128.036  1.00 52.84           C  
ANISOU  231  CE1 PHE A  42     6264   7606   6208    -33    675  -1180       C  
ATOM    232  CE2 PHE A  42      36.182   0.492 128.646  1.00 55.69           C  
ANISOU  232  CE2 PHE A  42     6529   8088   6543   -213    799  -1393       C  
ATOM    233  CZ  PHE A  42      34.951   0.132 128.037  1.00 55.27           C  
ANISOU  233  CZ  PHE A  42     6545   7898   6559   -130    796  -1278       C  
ATOM    234  N   GLY A  43      40.321  -4.396 130.381  1.00 52.23           N  
ANISOU  234  N   GLY A  43     5848   8412   5584     89    236  -1277       N  
ATOM    235  CA  GLY A  43      41.024  -5.570 130.876  1.00 52.47           C  
ANISOU  235  CA  GLY A  43     5837   8597   5502    192    125  -1212       C  
ATOM    236  C   GLY A  43      41.976  -6.212 129.856  1.00 52.27           C  
ANISOU  236  C   GLY A  43     5773   8602   5487    303     71  -1166       C  
ATOM    237  O   GLY A  43      42.941  -6.862 130.243  1.00 54.06           O  
ANISOU  237  O   GLY A  43     5925   9000   5614    370     -2  -1143       O  
ATOM    238  N   ASN A  44      41.737  -6.042 128.556  1.00 50.96           N  
ANISOU  238  N   ASN A  44     5652   8283   5429    333    107  -1150       N  
ATOM    239  CA  ASN A  44      42.575  -6.701 127.544  1.00 50.09           C  
ANISOU  239  CA  ASN A  44     5514   8193   5323    449     60  -1106       C  
ATOM    240  C   ASN A  44      42.338  -6.153 126.156  1.00 49.30           C  
ANISOU  240  C   ASN A  44     5451   7950   5332    447    123  -1114       C  
ATOM    241  O   ASN A  44      41.304  -6.429 125.548  1.00 48.09           O  
ANISOU  241  O   ASN A  44     5393   7630   5249    488    129  -1059       O  
ATOM    242  CB  ASN A  44      42.333  -8.211 127.549  1.00 49.81           C  
ANISOU  242  CB  ASN A  44     5541   8123   5260    600    -28   -988       C  
ATOM    243  CG  ASN A  44      43.274  -8.988 126.597  1.00 49.10           C  
ANISOU  243  CG  ASN A  44     5427   8065   5165    735    -74   -947       C  
ATOM    244  OD1 ASN A  44      44.005  -8.437 125.775  1.00 49.23           O  
ANISOU  244  OD1 ASN A  44     5386   8115   5204    724    -41   -995       O  
ATOM    245  ND2 ASN A  44      43.220 -10.278 126.713  1.00 44.59           N  
ANISOU  245  ND2 ASN A  44     4903   7474   4567    865   -141   -855       N  
ATOM    246  N   ARG A  45      43.320  -5.406 125.657  1.00 49.23           N  
ANISOU  246  N   ARG A  45     5357   8018   5332    402    169  -1179       N  
ATOM    247  CA  ARG A  45      43.219  -4.768 124.364  1.00 48.38           C  
ANISOU  247  CA  ARG A  45     5269   7795   5317    399    242  -1184       C  
ATOM    248  C   ARG A  45      43.436  -5.702 123.198  1.00 49.42           C  
ANISOU  248  C   ARG A  45     5434   7886   5457    549    191  -1110       C  
ATOM    249  O   ARG A  45      43.133  -5.311 122.064  1.00 50.14           O  
ANISOU  249  O   ARG A  45     5561   7872   5619    566    244  -1096       O  
ATOM    250  CB  ARG A  45      44.252  -3.638 124.242  1.00 49.03           C  
ANISOU  250  CB  ARG A  45     5244   7973   5411    293    320  -1276       C  
ATOM    251  CG  ARG A  45      44.233  -2.607 125.384  1.00 48.12           C  
ANISOU  251  CG  ARG A  45     5085   7913   5285    124    381  -1382       C  
ATOM    252  CD  ARG A  45      42.956  -1.726 125.290  1.00 46.51           C  
ANISOU  252  CD  ARG A  45     4975   7516   5181     48    482  -1391       C  
ATOM    253  NE  ARG A  45      43.108  -0.636 126.207  1.00 45.60           N  
ANISOU  253  NE  ARG A  45     4816   7445   5066   -116    562  -1511       N  
ATOM    254  CZ  ARG A  45      42.728  -0.671 127.483  1.00 43.86           C  
ANISOU  254  CZ  ARG A  45     4603   7281   4781   -176    539  -1556       C  
ATOM    255  NH1 ARG A  45      42.121  -1.742 127.982  1.00 41.44           N  
ANISOU  255  NH1 ARG A  45     4348   6984   4412    -83    445  -1474       N  
ATOM    256  NH2 ARG A  45      42.982   0.374 128.260  1.00 38.71           N  
ANISOU  256  NH2 ARG A  45     3905   6679   4125   -334    618  -1687       N  
ATOM    257  N   LEU A  46      43.985  -6.901 123.422  1.00 49.69           N  
ANISOU  257  N   LEU A  46     5455   8004   5420    664     98  -1062       N  
ATOM    258  CA  LEU A  46      44.410  -7.725 122.286  1.00 49.99           C  
ANISOU  258  CA  LEU A  46     5514   8019   5462    807     63  -1012       C  
ATOM    259  C   LEU A  46      43.258  -8.444 121.618  1.00 48.40           C  
ANISOU  259  C   LEU A  46     5441   7638   5311    880     36   -953       C  
ATOM    260  O   LEU A  46      42.464  -9.085 122.278  1.00 48.37           O  
ANISOU  260  O   LEU A  46     5502   7572   5304    891     -8   -915       O  
ATOM    261  CB  LEU A  46      45.471  -8.763 122.675  1.00 51.23           C  
ANISOU  261  CB  LEU A  46     5612   8323   5532    920    -15   -978       C  
ATOM    262  CG  LEU A  46      46.852  -8.264 123.118  1.00 56.11           C  
ANISOU  262  CG  LEU A  46     6076   9158   6084    878     -6  -1029       C  
ATOM    263  CD1 LEU A  46      47.714  -9.443 123.595  1.00 60.24           C  
ANISOU  263  CD1 LEU A  46     6548   9823   6516   1016    -91   -970       C  
ATOM    264  CD2 LEU A  46      47.559  -7.513 121.996  1.00 59.50           C  
ANISOU  264  CD2 LEU A  46     6446   9605   6556    860     63  -1069       C  
ATOM    265  N   CYS A  47      43.213  -8.383 120.293  1.00 47.55           N  
ANISOU  265  N   CYS A  47     5363   7458   5244    935     61   -946       N  
ATOM    266  CA  CYS A  47      42.301  -9.201 119.528  1.00 46.16           C  
ANISOU  266  CA  CYS A  47     5296   7141   5100   1016     22   -903       C  
ATOM    267  C   CYS A  47      42.597 -10.682 119.633  1.00 45.94           C  
ANISOU  267  C   CYS A  47     5308   7114   5032   1145    -61   -862       C  
ATOM    268  O   CYS A  47      43.736 -11.076 119.890  1.00 46.39           O  
ANISOU  268  O   CYS A  47     5300   7293   5032   1211    -83   -858       O  
ATOM    269  CB  CYS A  47      42.376  -8.792 118.104  1.00 45.72           C  
ANISOU  269  CB  CYS A  47     5249   7050   5073   1052     66   -911       C  
ATOM    270  SG  CYS A  47      41.672  -7.212 117.897  1.00 50.29           S  
ANISOU  270  SG  CYS A  47     5816   7572   5720    923    172   -930       S  
ATOM    271  N   PHE A  48      41.557 -11.490 119.449  1.00 44.98           N  
ANISOU  271  N   PHE A  48     5292   6854   4945   1179   -102   -831       N  
ATOM    272  CA  PHE A  48      41.684 -12.943 119.352  1.00 44.87           C  
ANISOU  272  CA  PHE A  48     5341   6792   4916   1304   -167   -794       C  
ATOM    273  C   PHE A  48      40.619 -13.390 118.376  1.00 44.43           C  
ANISOU  273  C   PHE A  48     5387   6580   4913   1322   -183   -799       C  
ATOM    274  O   PHE A  48      39.980 -12.552 117.704  1.00 43.10           O  
ANISOU  274  O   PHE A  48     5222   6375   4777   1258   -147   -823       O  
ATOM    275  CB  PHE A  48      41.530 -13.639 120.699  1.00 44.97           C  
ANISOU  275  CB  PHE A  48     5367   6813   4908   1306   -206   -743       C  
ATOM    276  CG  PHE A  48      40.174 -13.450 121.354  1.00 46.63           C  
ANISOU  276  CG  PHE A  48     5630   6923   5163   1204   -202   -726       C  
ATOM    277  CD1 PHE A  48      39.903 -12.311 122.129  1.00 45.91           C  
ANISOU  277  CD1 PHE A  48     5485   6891   5068   1079   -159   -748       C  
ATOM    278  CD2 PHE A  48      39.170 -14.418 121.210  1.00 47.49           C  
ANISOU  278  CD2 PHE A  48     5842   6879   5324   1230   -237   -691       C  
ATOM    279  CE1 PHE A  48      38.664 -12.155 122.760  1.00 47.36           C  
ANISOU  279  CE1 PHE A  48     5714   6989   5291    996   -149   -728       C  
ATOM    280  CE2 PHE A  48      37.924 -14.261 121.812  1.00 46.64           C  
ANISOU  280  CE2 PHE A  48     5773   6688   5260   1137   -230   -669       C  
ATOM    281  CZ  PHE A  48      37.668 -13.140 122.603  1.00 46.17           C  
ANISOU  281  CZ  PHE A  48     5657   6695   5190   1027   -186   -682       C  
ATOM    282  N   LEU A  49      40.416 -14.694 118.251  1.00 44.47           N  
ANISOU  282  N   LEU A  49     5474   6494   4929   1409   -234   -778       N  
ATOM    283  CA  LEU A  49      39.466 -15.101 117.248  1.00 44.55           C  
ANISOU  283  CA  LEU A  49     5571   6373   4983   1415   -253   -803       C  
ATOM    284  C   LEU A  49      38.406 -15.924 117.871  1.00 45.22           C  
ANISOU  284  C   LEU A  49     5735   6330   5118   1383   -289   -771       C  
ATOM    285  O   LEU A  49      38.685 -16.866 118.638  1.00 46.23           O  
ANISOU  285  O   LEU A  49     5891   6433   5243   1438   -312   -727       O  
ATOM    286  CB  LEU A  49      40.143 -15.836 116.080  1.00 45.59           C  
ANISOU  286  CB  LEU A  49     5739   6494   5090   1542   -266   -838       C  
ATOM    287  CG  LEU A  49      41.040 -14.948 115.202  1.00 46.41           C  
ANISOU  287  CG  LEU A  49     5768   6718   5149   1570   -221   -869       C  
ATOM    288  CD1 LEU A  49      42.028 -15.765 114.462  1.00 49.02           C  
ANISOU  288  CD1 LEU A  49     6113   7072   5439   1714   -228   -889       C  
ATOM    289  CD2 LEU A  49      40.253 -14.046 114.244  1.00 43.31           C  
ANISOU  289  CD2 LEU A  49     5379   6305   4774   1506   -193   -897       C  
ATOM    290  N   GLU A  50      37.180 -15.562 117.532  1.00 44.98           N  
ANISOU  290  N   GLU A  50     5734   6222   5134   1298   -289   -785       N  
ATOM    291  CA  GLU A  50      36.003 -16.220 118.069  1.00 46.13           C  
ANISOU  291  CA  GLU A  50     5943   6245   5338   1243   -318   -757       C  
ATOM    292  C   GLU A  50      35.474 -17.137 116.990  1.00 46.74           C  
ANISOU  292  C   GLU A  50     6103   6208   5447   1280   -358   -802       C  
ATOM    293  O   GLU A  50      35.079 -16.695 115.909  1.00 45.54           O  
ANISOU  293  O   GLU A  50     5948   6063   5291   1265   -361   -850       O  
ATOM    294  CB  GLU A  50      34.934 -15.186 118.540  1.00 45.48           C  
ANISOU  294  CB  GLU A  50     5826   6165   5289   1116   -288   -739       C  
ATOM    295  CG  GLU A  50      33.643 -15.805 119.131  1.00 47.05           C  
ANISOU  295  CG  GLU A  50     6078   6247   5552   1050   -310   -703       C  
ATOM    296  CD  GLU A  50      33.818 -16.476 120.518  1.00 51.13           C  
ANISOU  296  CD  GLU A  50     6610   6750   6066   1057   -312   -637       C  
ATOM    297  OE1 GLU A  50      34.897 -16.337 121.184  1.00 51.57           O  
ANISOU  297  OE1 GLU A  50     6623   6910   6062   1104   -299   -616       O  
ATOM    298  OE2 GLU A  50      32.846 -17.155 120.951  1.00 50.92           O  
ANISOU  298  OE2 GLU A  50     6633   6617   6096   1015   -327   -600       O  
ATOM    299  N   PRO A  51      35.505 -18.437 117.258  1.00 48.68           N  
ANISOU  299  N   PRO A  51     6423   6351   5720   1334   -386   -789       N  
ATOM    300  CA  PRO A  51      35.008 -19.344 116.235  1.00 49.95           C  
ANISOU  300  CA  PRO A  51     6669   6395   5916   1357   -421   -853       C  
ATOM    301  C   PRO A  51      33.506 -19.192 116.149  1.00 50.95           C  
ANISOU  301  C   PRO A  51     6809   6450   6101   1235   -441   -863       C  
ATOM    302  O   PRO A  51      32.852 -19.093 117.182  1.00 50.22           O  
ANISOU  302  O   PRO A  51     6704   6328   6049   1159   -431   -801       O  
ATOM    303  CB  PRO A  51      35.350 -20.722 116.778  1.00 50.56           C  
ANISOU  303  CB  PRO A  51     6823   6362   6026   1431   -427   -822       C  
ATOM    304  CG  PRO A  51      35.597 -20.558 118.231  1.00 50.07           C  
ANISOU  304  CG  PRO A  51     6719   6348   5958   1420   -405   -723       C  
ATOM    305  CD  PRO A  51      35.996 -19.125 118.463  1.00 49.25           C  
ANISOU  305  CD  PRO A  51     6507   6413   5793   1378   -381   -717       C  
ATOM    306  N   THR A  52      32.969 -19.186 114.929  1.00 52.70           N  
ANISOU  306  N   THR A  52     7049   6655   6320   1220   -469   -939       N  
ATOM    307  CA  THR A  52      31.526 -19.054 114.732  1.00 53.53           C  
ANISOU  307  CA  THR A  52     7152   6713   6474   1107   -496   -951       C  
ATOM    308  C   THR A  52      30.910 -20.244 114.009  1.00 55.06           C  
ANISOU  308  C   THR A  52     7428   6783   6709   1093   -546  -1031       C  
ATOM    309  O   THR A  52      29.694 -20.344 113.910  1.00 55.92           O  
ANISOU  309  O   THR A  52     7534   6845   6866    993   -575  -1046       O  
ATOM    310  CB  THR A  52      31.194 -17.800 113.907  1.00 53.29           C  
ANISOU  310  CB  THR A  52     7049   6801   6399   1080   -487   -967       C  
ATOM    311  OG1 THR A  52      31.870 -17.884 112.649  1.00 54.73           O  
ANISOU  311  OG1 THR A  52     7246   7034   6515   1167   -500  -1038       O  
ATOM    312  CG2 THR A  52      31.608 -16.503 114.649  1.00 49.89           C  
ANISOU  312  CG2 THR A  52     6537   6473   5947   1065   -425   -896       C  
ATOM    313  N   SER A  53      31.734 -21.138 113.486  1.00 56.14           N  
ANISOU  313  N   SER A  53     7634   6869   6827   1191   -553  -1089       N  
ATOM    314  CA  SER A  53      31.223 -22.305 112.755  1.00 57.66           C  
ANISOU  314  CA  SER A  53     7916   6933   7060   1176   -593  -1187       C  
ATOM    315  C   SER A  53      30.288 -23.262 113.532  1.00 57.29           C  
ANISOU  315  C   SER A  53     7925   6717   7124   1084   -600  -1166       C  
ATOM    316  O   SER A  53      29.380 -23.817 112.956  1.00 59.10           O  
ANISOU  316  O   SER A  53     8191   6869   7397   1004   -639  -1247       O  
ATOM    317  CB  SER A  53      32.389 -23.107 112.172  1.00 59.49           C  
ANISOU  317  CB  SER A  53     8220   7128   7256   1312   -581  -1248       C  
ATOM    318  OG  SER A  53      32.907 -22.452 111.021  1.00 63.00           O  
ANISOU  318  OG  SER A  53     8628   7707   7602   1374   -587  -1309       O  
ATOM    319  N   ASN A  54      30.509 -23.485 114.819  1.00 55.31           N  
ANISOU  319  N   ASN A  54     7681   6415   6918   1092   -562  -1059       N  
ATOM    320  CA  ASN A  54      29.695 -24.469 115.552  1.00 53.99           C  
ANISOU  320  CA  ASN A  54     7575   6078   6860   1016   -556  -1027       C  
ATOM    321  C   ASN A  54      28.466 -23.785 116.308  1.00 52.72           C  
ANISOU  321  C   ASN A  54     7340   5949   6742    877   -557   -955       C  
ATOM    322  O   ASN A  54      27.994 -24.269 117.359  1.00 51.43           O  
ANISOU  322  O   ASN A  54     7198   5692   6653    827   -530   -873       O  
ATOM    323  CB  ASN A  54      30.658 -25.210 116.484  1.00 53.89           C  
ANISOU  323  CB  ASN A  54     7618   5993   6866   1124   -507   -941       C  
ATOM    324  CG  ASN A  54      30.046 -26.394 117.172  1.00 54.30           C  
ANISOU  324  CG  ASN A  54     7752   5847   7034   1077   -483   -899       C  
ATOM    325  OD1 ASN A  54      30.375 -26.658 118.314  1.00 55.72           O  
ANISOU  325  OD1 ASN A  54     7940   6000   7232   1120   -441   -778       O  
ATOM    326  ND2 ASN A  54      29.169 -27.112 116.506  1.00 53.09           N  
ANISOU  326  ND2 ASN A  54     7657   5559   6957    988   -507   -995       N  
ATOM    327  N   ALA A  55      27.960 -22.668 115.745  1.00 50.73           N  
ANISOU  327  N   ALA A  55     7003   5832   6442    824   -581   -980       N  
ATOM    328  CA  ALA A  55      26.882 -21.876 116.362  1.00 49.53           C  
ANISOU  328  CA  ALA A  55     6771   5729   6318    714   -573   -913       C  
ATOM    329  C   ALA A  55      25.633 -22.682 116.726  1.00 50.12           C  
ANISOU  329  C   ALA A  55     6869   5672   6500    594   -586   -906       C  
ATOM    330  O   ALA A  55      25.050 -22.452 117.773  1.00 50.40           O  
ANISOU  330  O   ALA A  55     6871   5699   6578    532   -553   -812       O  
ATOM    331  CB  ALA A  55      26.523 -20.676 115.532  1.00 47.77           C  
ANISOU  331  CB  ALA A  55     6463   5654   6034    694   -592   -944       C  
ATOM    332  N   GLN A  56      25.277 -23.670 115.920  1.00 51.22           N  
ANISOU  332  N   GLN A  56     7071   5706   6685    559   -626  -1008       N  
ATOM    333  CA  GLN A  56      24.115 -24.510 116.200  1.00 52.80           C  
ANISOU  333  CA  GLN A  56     7293   5771   6999    431   -635  -1015       C  
ATOM    334  C   GLN A  56      24.241 -25.264 117.528  1.00 53.68           C  
ANISOU  334  C   GLN A  56     7463   5744   7191    435   -573   -905       C  
ATOM    335  O   GLN A  56      23.226 -25.569 118.172  1.00 55.29           O  
ANISOU  335  O   GLN A  56     7651   5872   7483    324   -557   -852       O  
ATOM    336  CB  GLN A  56      23.844 -25.493 115.044  1.00 54.73           C  
ANISOU  336  CB  GLN A  56     7602   5918   7273    392   -686  -1169       C  
ATOM    337  N   ASN A  57      25.469 -25.560 117.945  1.00 52.61           N  
ANISOU  337  N   ASN A  57     7385   5583   7021    566   -536   -860       N  
ATOM    338  CA  ASN A  57      25.671 -26.266 119.195  1.00 53.08           C  
ANISOU  338  CA  ASN A  57     7497   5530   7140    592   -476   -741       C  
ATOM    339  C   ASN A  57      26.085 -25.331 120.319  1.00 51.34           C  
ANISOU  339  C   ASN A  57     7208   5449   6851    637   -439   -613       C  
ATOM    340  O   ASN A  57      25.645 -25.496 121.446  1.00 51.01           O  
ANISOU  340  O   ASN A  57     7161   5369   6852    597   -396   -502       O  
ATOM    341  CB  ASN A  57      26.748 -27.365 119.060  1.00 53.78           C  
ANISOU  341  CB  ASN A  57     7698   5493   7243    718   -450   -757       C  
ATOM    342  CG  ASN A  57      26.321 -28.503 118.145  1.00 57.22           C  
ANISOU  342  CG  ASN A  57     8226   5747   7769    667   -467   -883       C  
ATOM    343  OD1 ASN A  57      27.018 -28.820 117.169  1.00 56.79           O  
ANISOU  343  OD1 ASN A  57     8225   5677   7677    746   -486   -993       O  
ATOM    344  ND2 ASN A  57      25.182 -29.135 118.457  1.00 57.35           N  
ANISOU  344  ND2 ASN A  57     8263   5624   7905    529   -455   -875       N  
ATOM    345  N   VAL A  58      27.000 -24.419 120.009  1.00 49.58           N  
ANISOU  345  N   VAL A  58     6937   5381   6519    723   -450   -633       N  
ATOM    346  CA  VAL A  58      27.559 -23.529 120.982  1.00 48.39           C  
ANISOU  346  CA  VAL A  58     6724   5370   6294    766   -417   -539       C  
ATOM    347  C   VAL A  58      27.480 -22.108 120.404  1.00 47.05           C  
ANISOU  347  C   VAL A  58     6462   5364   6053    739   -435   -588       C  
ATOM    348  O   VAL A  58      28.136 -21.784 119.405  1.00 47.68           O  
ANISOU  348  O   VAL A  58     6535   5507   6077    799   -460   -667       O  
ATOM    349  CB  VAL A  58      28.988 -23.972 121.380  1.00 49.09           C  
ANISOU  349  CB  VAL A  58     6851   5474   6327    915   -395   -496       C  
ATOM    350  CG1 VAL A  58      29.619 -23.023 122.405  1.00 47.05           C  
ANISOU  350  CG1 VAL A  58     6516   5384   5979    950   -367   -413       C  
ATOM    351  CG2 VAL A  58      28.930 -25.366 121.982  1.00 50.49           C  
ANISOU  351  CG2 VAL A  58     7122   5475   6588    944   -363   -427       C  
ATOM    352  N   PRO A  59      26.631 -21.265 120.998  1.00 45.61           N  
ANISOU  352  N   PRO A  59     6210   5243   5878    651   -415   -539       N  
ATOM    353  CA  PRO A  59      26.528 -19.930 120.421  1.00 44.64           C  
ANISOU  353  CA  PRO A  59     6006   5255   5699    632   -418   -578       C  
ATOM    354  C   PRO A  59      27.824 -19.158 120.683  1.00 44.21           C  
ANISOU  354  C   PRO A  59     5921   5326   5553    720   -391   -567       C  
ATOM    355  O   PRO A  59      28.361 -19.226 121.769  1.00 44.07           O  
ANISOU  355  O   PRO A  59     5903   5332   5508    751   -360   -500       O  
ATOM    356  CB  PRO A  59      25.359 -19.322 121.169  1.00 43.62           C  
ANISOU  356  CB  PRO A  59     5819   5146   5609    530   -387   -515       C  
ATOM    357  CG  PRO A  59      25.212 -20.114 122.396  1.00 43.48           C  
ANISOU  357  CG  PRO A  59     5841   5047   5632    515   -356   -427       C  
ATOM    358  CD  PRO A  59      25.766 -21.453 122.174  1.00 45.01           C  
ANISOU  358  CD  PRO A  59     6126   5119   5858    574   -378   -443       C  
ATOM    359  N   PRO A  60      28.364 -18.479 119.678  1.00 44.44           N  
ANISOU  359  N   PRO A  60     5921   5438   5528    763   -403   -633       N  
ATOM    360  CA  PRO A  60      29.596 -17.727 119.950  1.00 44.57           C  
ANISOU  360  CA  PRO A  60     5897   5572   5464    831   -372   -625       C  
ATOM    361  C   PRO A  60      29.295 -16.392 120.657  1.00 45.69           C  
ANISOU  361  C   PRO A  60     5964   5810   5588    767   -319   -589       C  
ATOM    362  O   PRO A  60      28.149 -15.937 120.652  1.00 46.61           O  
ANISOU  362  O   PRO A  60     6054   5908   5746    688   -307   -575       O  
ATOM    363  CB  PRO A  60      30.119 -17.445 118.571  1.00 44.37           C  
ANISOU  363  CB  PRO A  60     5867   5594   5400    887   -393   -704       C  
ATOM    364  CG  PRO A  60      28.838 -17.417 117.679  1.00 44.11           C  
ANISOU  364  CG  PRO A  60     5832   5518   5411    816   -425   -742       C  
ATOM    365  CD  PRO A  60      27.897 -18.369 118.285  1.00 44.19           C  
ANISOU  365  CD  PRO A  60     5884   5406   5499    749   -443   -713       C  
ATOM    366  N   ASP A  61      30.328 -15.757 121.201  1.00 45.55           N  
ANISOU  366  N   ASP A  61     5908   5895   5506    803   -285   -581       N  
ATOM    367  CA  ASP A  61      30.220 -14.543 121.939  1.00 44.89           C  
ANISOU  367  CA  ASP A  61     5762   5895   5401    744   -227   -563       C  
ATOM    368  C   ASP A  61      30.339 -13.350 120.957  1.00 44.82           C  
ANISOU  368  C   ASP A  61     5704   5945   5380    738   -196   -611       C  
ATOM    369  O   ASP A  61      31.410 -12.763 120.774  1.00 45.51           O  
ANISOU  369  O   ASP A  61     5757   6117   5417    775   -172   -641       O  
ATOM    370  CB  ASP A  61      31.317 -14.592 123.019  1.00 45.39           C  
ANISOU  370  CB  ASP A  61     5807   6042   5397    781   -212   -539       C  
ATOM    371  CG  ASP A  61      31.253 -13.443 124.012  1.00 47.01           C  
ANISOU  371  CG  ASP A  61     5955   6336   5572    711   -149   -533       C  
ATOM    372  OD1 ASP A  61      30.288 -12.650 123.976  1.00 50.18           O  
ANISOU  372  OD1 ASP A  61     6338   6715   6015    638   -108   -534       O  
ATOM    373  OD2 ASP A  61      32.180 -13.323 124.846  1.00 47.10           O  
ANISOU  373  OD2 ASP A  61     5935   6446   5514    730   -139   -530       O  
ATOM    374  N   LEU A  62      29.228 -12.981 120.329  1.00 44.60           N  
ANISOU  374  N   LEU A  62     5668   5879   5399    694   -192   -610       N  
ATOM    375  CA  LEU A  62      29.222 -11.975 119.269  1.00 44.49           C  
ANISOU  375  CA  LEU A  62     5615   5913   5377    704   -162   -638       C  
ATOM    376  C   LEU A  62      29.261 -10.504 119.663  1.00 44.14           C  
ANISOU  376  C   LEU A  62     5513   5926   5330    662    -71   -627       C  
ATOM    377  O   LEU A  62      29.707  -9.666 118.877  1.00 44.10           O  
ANISOU  377  O   LEU A  62     5479   5968   5309    688    -31   -646       O  
ATOM    378  CB  LEU A  62      28.022 -12.177 118.375  1.00 44.91           C  
ANISOU  378  CB  LEU A  62     5671   5921   5470    684   -198   -636       C  
ATOM    379  CG  LEU A  62      28.190 -13.271 117.328  1.00 50.09           C  
ANISOU  379  CG  LEU A  62     6376   6543   6114    737   -278   -685       C  
ATOM    380  CD1 LEU A  62      27.069 -13.104 116.355  1.00 54.61           C  
ANISOU  380  CD1 LEU A  62     6925   7117   6706    711   -304   -692       C  
ATOM    381  CD2 LEU A  62      29.549 -13.247 116.545  1.00 51.76           C  
ANISOU  381  CD2 LEU A  62     6596   6811   6260    829   -281   -733       C  
ATOM    382  N   ALA A  63      28.764 -10.162 120.841  1.00 44.10           N  
ANISOU  382  N   ALA A  63     5497   5914   5345    598    -27   -596       N  
ATOM    383  CA  ALA A  63      28.771  -8.779 121.276  1.00 43.99           C  
ANISOU  383  CA  ALA A  63     5438   5939   5335    553     71   -598       C  
ATOM    384  C   ALA A  63      30.128  -8.142 121.080  1.00 45.03           C  
ANISOU  384  C   ALA A  63     5544   6143   5422    577    107   -646       C  
ATOM    385  O   ALA A  63      30.212  -6.966 120.702  1.00 46.74           O  
ANISOU  385  O   ALA A  63     5727   6375   5655    561    187   -657       O  
ATOM    386  CB  ALA A  63      28.428  -8.698 122.695  1.00 43.88           C  
ANISOU  386  CB  ALA A  63     5425   5926   5323    493    105   -578       C  
ATOM    387  N   ILE A  64      31.197  -8.884 121.345  1.00 44.26           N  
ANISOU  387  N   ILE A  64     5456   6089   5271    616     56   -670       N  
ATOM    388  CA  ILE A  64      32.517  -8.286 121.231  1.00 43.77           C  
ANISOU  388  CA  ILE A  64     5353   6112   5165    631     91   -716       C  
ATOM    389  C   ILE A  64      33.271  -8.502 119.887  1.00 43.46           C  
ANISOU  389  C   ILE A  64     5313   6094   5107    713     63   -736       C  
ATOM    390  O   ILE A  64      34.475  -8.157 119.785  1.00 43.14           O  
ANISOU  390  O   ILE A  64     5231   6132   5027    732     85   -771       O  
ATOM    391  CB  ILE A  64      33.406  -8.671 122.420  1.00 44.80           C  
ANISOU  391  CB  ILE A  64     5467   6319   5235    624     71   -731       C  
ATOM    392  CG1 ILE A  64      33.744 -10.173 122.399  1.00 43.04           C  
ANISOU  392  CG1 ILE A  64     5285   6084   4984    707    -23   -704       C  
ATOM    393  CG2 ILE A  64      32.763  -8.129 123.715  1.00 43.99           C  
ANISOU  393  CG2 ILE A  64     5356   6220   5138    536    122   -725       C  
ATOM    394  CD1 ILE A  64      34.717 -10.561 123.445  1.00 43.90           C  
ANISOU  394  CD1 ILE A  64     5367   6289   5022    724    -44   -703       C  
ATOM    395  N   CYS A  65      32.558  -9.059 118.905  1.00 41.30           N  
ANISOU  395  N   CYS A  65     5076   5761   4855    756     16   -718       N  
ATOM    396  CA  CYS A  65      32.988  -9.131 117.533  1.00 42.05           C  
ANISOU  396  CA  CYS A  65     5173   5874   4929    829      0   -736       C  
ATOM    397  C   CYS A  65      32.513  -7.972 116.628  1.00 42.72           C  
ANISOU  397  C   CYS A  65     5228   5964   5038    821     70   -718       C  
ATOM    398  O   CYS A  65      33.018  -7.834 115.526  1.00 43.81           O  
ANISOU  398  O   CYS A  65     5357   6140   5148    883     75   -728       O  
ATOM    399  CB  CYS A  65      32.505 -10.437 116.901  1.00 41.54           C  
ANISOU  399  CB  CYS A  65     5167   5752   4863    881    -93   -740       C  
ATOM    400  SG  CYS A  65      33.117 -11.928 117.757  1.00 45.14           S  
ANISOU  400  SG  CYS A  65     5671   6180   5299    920   -164   -746       S  
ATOM    401  N   CYS A  66      31.542  -7.170 117.066  1.00 42.63           N  
ANISOU  401  N   CYS A  66     5201   5918   5077    756    128   -684       N  
ATOM    402  CA  CYS A  66      30.927  -6.129 116.242  1.00 42.82           C  
ANISOU  402  CA  CYS A  66     5200   5938   5131    763    199   -646       C  
ATOM    403  C   CYS A  66      31.773  -4.887 116.173  1.00 41.56           C  
ANISOU  403  C   CYS A  66     5002   5811   4980    749    311   -653       C  
ATOM    404  O   CYS A  66      32.205  -4.372 117.207  1.00 41.98           O  
ANISOU  404  O   CYS A  66     5038   5866   5048    682    368   -681       O  
ATOM    405  CB  CYS A  66      29.565  -5.739 116.829  1.00 42.84           C  
ANISOU  405  CB  CYS A  66     5199   5888   5192    705    231   -600       C  
ATOM    406  SG  CYS A  66      28.412  -7.093 116.708  1.00 48.96           S  
ANISOU  406  SG  CYS A  66     6007   6623   5973    708    110   -586       S  
ATOM    407  N   PHE A  67      31.955  -4.384 114.969  1.00 40.22           N  
ANISOU  407  N   PHE A  67     4815   5666   4799    808    348   -628       N  
ATOM    408  CA  PHE A  67      32.657  -3.151 114.753  1.00 40.76           C  
ANISOU  408  CA  PHE A  67     4847   5750   4890    796    471   -622       C  
ATOM    409  C   PHE A  67      31.754  -2.286 113.909  1.00 42.06           C  
ANISOU  409  C   PHE A  67     5002   5890   5090    830    544   -543       C  
ATOM    410  O   PHE A  67      30.949  -2.806 113.112  1.00 42.65           O  
ANISOU  410  O   PHE A  67     5086   5979   5138    890    475   -505       O  
ATOM    411  CB  PHE A  67      33.991  -3.407 114.021  1.00 40.33           C  
ANISOU  411  CB  PHE A  67     4776   5767   4779    853    456   -653       C  
ATOM    412  CG  PHE A  67      35.059  -4.026 114.900  1.00 39.16           C  
ANISOU  412  CG  PHE A  67     4618   5660   4598    825    409   -721       C  
ATOM    413  CD1 PHE A  67      35.113  -5.408 115.088  1.00 37.59           C  
ANISOU  413  CD1 PHE A  67     4455   5472   4354    866    287   -745       C  
ATOM    414  CD2 PHE A  67      35.991  -3.213 115.579  1.00 38.13           C  
ANISOU  414  CD2 PHE A  67     4441   5561   4485    754    492   -760       C  
ATOM    415  CE1 PHE A  67      36.082  -5.993 115.925  1.00 37.55           C  
ANISOU  415  CE1 PHE A  67     4437   5516   4316    856    246   -789       C  
ATOM    416  CE2 PHE A  67      36.978  -3.790 116.408  1.00 36.91           C  
ANISOU  416  CE2 PHE A  67     4262   5473   4287    733    441   -817       C  
ATOM    417  CZ  PHE A  67      37.008  -5.178 116.589  1.00 37.10           C  
ANISOU  417  CZ  PHE A  67     4320   5514   4261    792    319   -823       C  
ATOM    418  N   THR A  68      31.897  -0.976 114.079  1.00 43.13           N  
ANISOU  418  N   THR A  68     5114   5991   5284    792    686   -520       N  
ATOM    419  CA  THR A  68      31.235   0.007 113.255  1.00 44.58           C  
ANISOU  419  CA  THR A  68     5283   6150   5506    839    786   -429       C  
ATOM    420  C   THR A  68      32.193   0.647 112.260  1.00 45.60           C  
ANISOU  420  C   THR A  68     5389   6313   5622    890    867   -404       C  
ATOM    421  O   THR A  68      33.305   1.061 112.622  1.00 46.63           O  
ANISOU  421  O   THR A  68     5503   6444   5769    837    931   -457       O  
ATOM    422  CB  THR A  68      30.551   1.066 114.171  1.00 44.97           C  
ANISOU  422  CB  THR A  68     5331   6109   5647    768    910   -408       C  
ATOM    423  OG1 THR A  68      29.316   0.509 114.636  1.00 47.54           O  
ANISOU  423  OG1 THR A  68     5669   6416   5978    762    838   -386       O  
ATOM    424  CG2 THR A  68      30.216   2.358 113.437  1.00 45.00           C  
ANISOU  424  CG2 THR A  68     5319   6069   5709    814   1062   -313       C  
ATOM    425  N   LEU A  69      31.766   0.743 111.006  1.00 46.78           N  
ANISOU  425  N   LEU A  69     5531   6504   5738    990    868   -322       N  
ATOM    426  CA  LEU A  69      32.521   1.471 110.000  1.00 47.97           C  
ANISOU  426  CA  LEU A  69     5660   6687   5880   1049    967   -271       C  
ATOM    427  C   LEU A  69      32.405   2.975 110.241  1.00 49.28           C  
ANISOU  427  C   LEU A  69     5813   6760   6150   1012   1157   -210       C  
ATOM    428  O   LEU A  69      31.602   3.629 109.643  1.00 50.51           O  
ANISOU  428  O   LEU A  69     5963   6898   6330   1077   1230   -102       O  
ATOM    429  CB  LEU A  69      32.046   1.083 108.585  1.00 47.93           C  
ANISOU  429  CB  LEU A  69     5651   6771   5791   1176    906   -198       C  
ATOM    430  CG  LEU A  69      32.476  -0.324 108.082  1.00 47.21           C  
ANISOU  430  CG  LEU A  69     5577   6769   5592   1222    744   -272       C  
ATOM    431  CD1 LEU A  69      31.684  -0.803 106.882  1.00 44.92           C  
ANISOU  431  CD1 LEU A  69     5287   6565   5215   1325    663   -223       C  
ATOM    432  CD2 LEU A  69      33.932  -0.359 107.721  1.00 44.36           C  
ANISOU  432  CD2 LEU A  69     5205   6453   5195   1241    774   -312       C  
ATOM    433  N   GLU A  70      33.217   3.532 111.114  1.00 51.14           N  
ANISOU  433  N   GLU A  70     6044   6940   6448    908   1243   -279       N  
ATOM    434  CA  GLU A  70      33.182   4.963 111.366  1.00 54.31           C  
ANISOU  434  CA  GLU A  70     6441   7234   6959    860   1437   -240       C  
ATOM    435  C   GLU A  70      33.447   5.831 110.164  1.00 56.17           C  
ANISOU  435  C   GLU A  70     6660   7466   7215    942   1568   -128       C  
ATOM    436  O   GLU A  70      32.865   6.880 110.000  1.00 57.20           O  
ANISOU  436  O   GLU A  70     6798   7510   7426    964   1715    -36       O  
ATOM    437  CB  GLU A  70      34.265   5.311 112.342  1.00 54.73           C  
ANISOU  437  CB  GLU A  70     6482   7256   7057    728   1494   -357       C  
ATOM    438  CG  GLU A  70      33.979   4.912 113.691  1.00 58.95           C  
ANISOU  438  CG  GLU A  70     7032   7770   7597    634   1430   -452       C  
ATOM    439  CD  GLU A  70      33.409   6.049 114.482  1.00 65.88           C  
ANISOU  439  CD  GLU A  70     7929   8522   8582    556   1582   -456       C  
ATOM    440  OE1 GLU A  70      34.177   7.032 114.782  1.00 66.85           O  
ANISOU  440  OE1 GLU A  70     8040   8584   8777    466   1726   -507       O  
ATOM    441  OE2 GLU A  70      32.192   5.922 114.797  1.00 68.47           O  
ANISOU  441  OE2 GLU A  70     8282   8813   8922    583   1559   -413       O  
ATOM    442  N   GLN A  71      34.386   5.415 109.339  1.00 57.96           N  
ANISOU  442  N   GLN A  71     6866   7787   7370    992   1527   -132       N  
ATOM    443  CA  GLN A  71      35.027   6.324 108.436  1.00 59.92           C  
ANISOU  443  CA  GLN A  71     7093   8026   7649   1035   1677    -51       C  
ATOM    444  C   GLN A  71      35.690   5.526 107.334  1.00 60.20           C  
ANISOU  444  C   GLN A  71     7110   8200   7565   1134   1583    -37       C  
ATOM    445  O   GLN A  71      36.318   4.486 107.588  1.00 59.18           O  
ANISOU  445  O   GLN A  71     6974   8146   7364   1113   1447   -140       O  
ATOM    446  CB  GLN A  71      36.084   7.034 109.239  1.00 61.30           C  
ANISOU  446  CB  GLN A  71     7249   8130   7913    895   1793   -140       C  
ATOM    447  CG  GLN A  71      36.480   8.355 108.704  1.00 67.65           C  
ANISOU  447  CG  GLN A  71     8041   8851   8812    893   2009    -55       C  
ATOM    448  CD  GLN A  71      35.649   9.466 109.256  1.00 71.75           C  
ANISOU  448  CD  GLN A  71     8592   9210   9459    849   2166    -12       C  
ATOM    449  OE1 GLN A  71      35.083  10.257 108.500  1.00 75.85           O  
ANISOU  449  OE1 GLN A  71     9123   9671  10023    941   2296    134       O  
ATOM    450  NE2 GLN A  71      35.571   9.547 110.576  1.00 72.35           N  
ANISOU  450  NE2 GLN A  71     8683   9217   9589    716   2162   -136       N  
ATOM    451  N   SER A  72      35.526   6.009 106.110  1.00 62.08           N  
ANISOU  451  N   SER A  72     7338   8473   7776   1250   1661     95       N  
ATOM    452  CA  SER A  72      36.129   5.409 104.929  1.00 63.64           C  
ANISOU  452  CA  SER A  72     7520   8807   7855   1358   1599    121       C  
ATOM    453  C   SER A  72      36.662   6.508 104.001  1.00 66.04           C  
ANISOU  453  C   SER A  72     7798   9101   8192   1415   1788    247       C  
ATOM    454  O   SER A  72      35.877   7.189 103.316  1.00 66.84           O  
ANISOU  454  O   SER A  72     7904   9189   8302   1508   1877    392       O  
ATOM    455  CB  SER A  72      35.109   4.543 104.212  1.00 63.24           C  
ANISOU  455  CB  SER A  72     7486   8855   7688   1474   1452    160       C  
ATOM    456  OG  SER A  72      35.671   3.888 103.092  1.00 65.15           O  
ANISOU  456  OG  SER A  72     7718   9234   7802   1577   1385    165       O  
ATOM    457  N   LEU A  73      37.989   6.675 103.987  1.00 67.33           N  
ANISOU  457  N   LEU A  73     7929   9277   8374   1362   1852    199       N  
ATOM    458  CA  LEU A  73      38.639   7.795 103.297  1.00 69.96           C  
ANISOU  458  CA  LEU A  73     8235   9578   8768   1382   2055    306       C  
ATOM    459  C   LEU A  73      39.587   7.384 102.184  1.00 72.11           C  
ANISOU  459  C   LEU A  73     8474   9991   8932   1477   2041    336       C  
ATOM    460  O   LEU A  73      40.293   6.377 102.300  1.00 71.72           O  
ANISOU  460  O   LEU A  73     8409  10036   8803   1467   1908    224       O  
ATOM    461  CB  LEU A  73      39.461   8.619 104.289  1.00 69.69           C  
ANISOU  461  CB  LEU A  73     8178   9420   8880   1211   2190    227       C  
ATOM    462  CG  LEU A  73      38.731   9.311 105.428  1.00 69.12           C  
ANISOU  462  CG  LEU A  73     8138   9187   8937   1099   2260    192       C  
ATOM    463  CD1 LEU A  73      39.711  10.154 106.242  1.00 66.39           C  
ANISOU  463  CD1 LEU A  73     7763   8739   8723    925   2404    101       C  
ATOM    464  CD2 LEU A  73      37.581  10.156 104.863  1.00 69.81           C  
ANISOU  464  CD2 LEU A  73     8259   9193   9071   1200   2381    362       C  
ATOM    465  N   SER A  74      39.641   8.194 101.132  1.00 75.16           N  
ANISOU  465  N   SER A  74     8850  10389   9321   1572   2192    493       N  
ATOM    466  CA  SER A  74      40.779   8.165 100.215  1.00 78.42           C  
ANISOU  466  CA  SER A  74     9221  10904   9672   1630   2248    529       C  
ATOM    467  C   SER A  74      42.060   8.550 100.972  1.00 79.65           C  
ANISOU  467  C   SER A  74     9327  10998   9938   1471   2337    430       C  
ATOM    468  O   SER A  74      42.012   9.220 102.006  1.00 80.02           O  
ANISOU  468  O   SER A  74     9376  10902  10125   1326   2416    375       O  
ATOM    469  CB  SER A  74      40.560   9.125  99.048  1.00 79.93           C  
ANISOU  469  CB  SER A  74     9407  11100   9862   1753   2423    734       C  
ATOM    470  OG  SER A  74      40.942  10.439  99.412  1.00 82.44           O  
ANISOU  470  OG  SER A  74     9712  11257  10356   1655   2650    792       O  
ATOM    471  N   VAL A  75      43.202   8.121 100.464  1.00 81.61           N  
ANISOU  471  N   VAL A  75     9527  11363  10118   1497   2323    401       N  
ATOM    472  CA  VAL A  75      44.468   8.311 101.178  1.00 83.06           C  
ANISOU  472  CA  VAL A  75     9645  11528  10384   1348   2377    294       C  
ATOM    473  C   VAL A  75      44.941   9.763 101.156  1.00 84.85           C  
ANISOU  473  C   VAL A  75     9838  11630  10769   1255   2628    372       C  
ATOM    474  O   VAL A  75      45.652  10.202 102.061  1.00 84.70           O  
ANISOU  474  O   VAL A  75     9775  11544  10865   1084   2691    270       O  
ATOM    475  CB  VAL A  75      45.556   7.397 100.606  1.00 83.83           C  
ANISOU  475  CB  VAL A  75     9691  11799  10361   1416   2292    247       C  
ATOM    476  CG1 VAL A  75      45.986   7.872  99.181  1.00 84.40           C  
ANISOU  476  CG1 VAL A  75     9740  11946  10384   1543   2431    404       C  
ATOM    477  CG2 VAL A  75      46.741   7.261 101.613  1.00 84.84           C  
ANISOU  477  CG2 VAL A  75     9744  11941  10553   1258   2278    101       C  
ATOM    478  N   ARG A  76      44.553  10.488 100.110  1.00 86.84           N  
ANISOU  478  N   ARG A  76    10111  11860  11025   1370   2771    554       N  
ATOM    479  CA  ARG A  76      44.739  11.929 100.061  1.00 89.21           C  
ANISOU  479  CA  ARG A  76    10401  12003  11491   1298   3028    655       C  
ATOM    480  C   ARG A  76      43.866  12.573 101.155  1.00 89.40           C  
ANISOU  480  C   ARG A  76    10476  11837  11654   1182   3075    611       C  
ATOM    481  O   ARG A  76      44.331  13.439 101.911  1.00 90.45           O  
ANISOU  481  O   ARG A  76    10590  11826  11948   1012   3219    549       O  
ATOM    482  CB  ARG A  76      44.398  12.485  98.667  1.00 90.49           C  
ANISOU  482  CB  ARG A  76    10580  12193  11609   1476   3163    883       C  
ATOM    483  N   ALA A  77      42.616  12.130 101.264  1.00 88.51           N  
ANISOU  483  N   ALA A  77    10425  11727  11479   1268   2952    630       N  
ATOM    484  CA  ALA A  77      41.745  12.614 102.334  1.00 88.41           C  
ANISOU  484  CA  ALA A  77    10460  11549  11582   1170   2979    580       C  
ATOM    485  C   ALA A  77      42.269  12.232 103.725  1.00 87.86           C  
ANISOU  485  C   ALA A  77    10369  11456  11557    979   2885    361       C  
ATOM    486  O   ALA A  77      42.019  12.949 104.696  1.00 88.48           O  
ANISOU  486  O   ALA A  77    10469  11379  11770    845   2977    297       O  
ATOM    487  CB  ALA A  77      40.294  12.133 102.138  1.00 87.29           C  
ANISOU  487  CB  ALA A  77    10374  11440  11353   1305   2855    649       C  
ATOM    488  N   LEU A  78      42.987  11.115 103.824  1.00 87.20           N  
ANISOU  488  N   LEU A  78    10243  11530  11359    974   2708    249       N  
ATOM    489  CA  LEU A  78      43.553  10.704 105.098  1.00 87.18           C  
ANISOU  489  CA  LEU A  78    10208  11535  11380    811   2613     55       C  
ATOM    490  C   LEU A  78      44.755  11.549 105.496  1.00 90.35           C  
ANISOU  490  C   LEU A  78    10540  11886  11903    642   2770    -13       C  
ATOM    491  O   LEU A  78      44.797  12.079 106.609  1.00 90.38           O  
ANISOU  491  O   LEU A  78    10543  11785  12013    474   2822   -127       O  
ATOM    492  CB  LEU A  78      43.897   9.216 105.106  1.00 85.14           C  
ANISOU  492  CB  LEU A  78     9930  11457  10965    872   2379    -31       C  
ATOM    493  CG  LEU A  78      44.429   8.597 106.404  1.00 82.06           C  
ANISOU  493  CG  LEU A  78     9504  11107  10568    736   2253   -215       C  
ATOM    494  CD1 LEU A  78      43.526   8.876 107.574  1.00 81.34           C  
ANISOU  494  CD1 LEU A  78     9463  10894  10549    636   2241   -282       C  
ATOM    495  CD2 LEU A  78      44.574   7.129 106.238  1.00 77.66           C  
ANISOU  495  CD2 LEU A  78     8945  10704   9859    838   2039   -261       C  
ATOM    496  N   GLN A  79      45.724  11.691 104.590  1.00 93.93           N  
ANISOU  496  N   GLN A  79    10933  12416  12339    682   2850     53       N  
ATOM    497  CA  GLN A  79      46.922  12.479 104.873  1.00 97.62           C  
ANISOU  497  CA  GLN A  79    11319  12848  12923    517   3004     -8       C  
ATOM    498  C   GLN A  79      46.552  13.920 105.185  1.00100.03           C  
ANISOU  498  C   GLN A  79    11662  12927  13417    405   3238     29       C  
ATOM    499  O   GLN A  79      47.187  14.555 106.028  1.00100.84           O  
ANISOU  499  O   GLN A  79    11722  12955  13640    205   3331    -96       O  
ATOM    500  CB  GLN A  79      47.908  12.424 103.713  1.00 99.01           C  
ANISOU  500  CB  GLN A  79    11427  13142  13050    601   3068     87       C  
ATOM    501  CG  GLN A  79      48.750  11.145 103.648  1.00100.30           C  
ANISOU  501  CG  GLN A  79    11522  13524  13064    650   2875      1       C  
ATOM    502  CD  GLN A  79      49.555  11.044 102.347  1.00104.10           C  
ANISOU  502  CD  GLN A  79    11949  14128  13478    772   2940    116       C  
ATOM    503  OE1 GLN A  79      49.983  12.061 101.778  1.00106.17           O  
ANISOU  503  OE1 GLN A  79    12180  14321  13838    741   3153    217       O  
ATOM    504  NE2 GLN A  79      49.763   9.811 101.871  1.00104.01           N  
ANISOU  504  NE2 GLN A  79    11929  14292  13298    914   2766    103       N  
ATOM    505  N   GLU A  80      45.508  14.417 104.519  1.00101.99           N  
ANISOU  505  N   GLU A  80    11991  13072  13690    536   3332    196       N  
ATOM    506  CA  GLU A  80      44.998  15.769 104.752  1.00105.02           C  
ANISOU  506  CA  GLU A  80    12427  13221  14255    463   3565    255       C  
ATOM    507  C   GLU A  80      44.584  15.918 106.212  1.00105.11           C  
ANISOU  507  C   GLU A  80    12470  13125  14342    299   3528     80       C  
ATOM    508  O   GLU A  80      44.997  16.866 106.893  1.00106.63           O  
ANISOU  508  O   GLU A  80    12652  13170  14690    115   3691    -10       O  
ATOM    509  CB  GLU A  80      43.823  16.084 103.803  1.00105.65           C  
ANISOU  509  CB  GLU A  80    12583  13244  14315    668   3634    477       C  
ATOM    510  CG  GLU A  80      43.033  17.399 104.080  1.00108.93           C  
ANISOU  510  CG  GLU A  80    13070  13406  14912    633   3865    557       C  
ATOM    511  CD  GLU A  80      43.655  18.656 103.433  1.00113.75           C  
ANISOU  511  CD  GLU A  80    13668  13875  15677    602   4159    684       C  
ATOM    512  OE1 GLU A  80      43.198  19.783 103.769  1.00114.46           O  
ANISOU  512  OE1 GLU A  80    13815  13732  15941    544   4372    725       O  
ATOM    513  OE2 GLU A  80      44.589  18.519 102.597  1.00114.03           O  
ANISOU  513  OE2 GLU A  80    13639  14023  15663    637   4186    745       O  
ATOM    514  N   MET A  81      43.794  14.965 106.690  1.00104.16           N  
ANISOU  514  N   MET A  81    12386  13082  14108    361   3317     26       N  
ATOM    515  CA  MET A  81      43.257  15.024 108.043  1.00104.33           C  
ANISOU  515  CA  MET A  81    12444  13017  14179    232   3272   -122       C  
ATOM    516  C   MET A  81      44.314  14.776 109.121  1.00104.38           C  
ANISOU  516  C   MET A  81    12378  13094  14189     31   3202   -341       C  
ATOM    517  O   MET A  81      44.283  15.401 110.187  1.00104.86           O  
ANISOU  517  O   MET A  81    12451  13040  14352   -138   3277   -472       O  
ATOM    518  CB  MET A  81      42.102  14.035 108.200  1.00102.90           C  
ANISOU  518  CB  MET A  81    12317  12908  13874    360   3068   -104       C  
ATOM    519  CG  MET A  81      41.511  14.044 109.584  1.00104.04           C  
ANISOU  519  CG  MET A  81    12499  12975  14058    241   3020   -245       C  
ATOM    520  SD  MET A  81      41.156  12.375 110.124  1.00106.81           S  
ANISOU  520  SD  MET A  81    12845  13510  14226    296   2706   -334       S  
ATOM    521  CE  MET A  81      39.339  12.386 110.106  1.00103.87           C  
ANISOU  521  CE  MET A  81    12565  13046  13854    424   2688   -221       C  
ATOM    522  N   LEU A  82      45.242  13.865 108.843  1.00104.14           N  
ANISOU  522  N   LEU A  82    12267  13260  14041     55   3059   -380       N  
ATOM    523  CA  LEU A  82      46.281  13.520 109.805  1.00104.53           C  
ANISOU  523  CA  LEU A  82    12229  13417  14070   -111   2973   -572       C  
ATOM    524  C   LEU A  82      47.210  14.684 110.124  1.00107.03           C  
ANISOU  524  C   LEU A  82    12485  13642  14541   -316   3177   -654       C  
ATOM    525  O   LEU A  82      47.744  14.765 111.228  1.00107.19           O  
ANISOU  525  O   LEU A  82    12453  13692  14584   -499   3147   -836       O  
ATOM    526  CB  LEU A  82      47.080  12.303 109.337  1.00103.50           C  
ANISOU  526  CB  LEU A  82    12025  13517  13785    -17   2793   -575       C  
ATOM    527  CG  LEU A  82      46.430  10.943 109.577  1.00100.95           C  
ANISOU  527  CG  LEU A  82    11742  13307  13309    107   2549   -591       C  
ATOM    528  CD1 LEU A  82      47.257   9.834 108.971  1.00 99.39           C  
ANISOU  528  CD1 LEU A  82    11480  13310  12975    214   2407   -580       C  
ATOM    529  CD2 LEU A  82      46.227  10.701 111.068  1.00100.60           C  
ANISOU  529  CD2 LEU A  82    11701  13262  13260    -27   2450   -755       C  
ATOM    530  N   ALA A  83      47.385  15.589 109.161  1.00109.42           N  
ANISOU  530  N   ALA A  83    12793  13834  14947   -287   3386   -518       N  
ATOM    531  CA  ALA A  83      48.201  16.799 109.359  1.00112.61           C  
ANISOU  531  CA  ALA A  83    13148  14116  15525   -485   3613   -580       C  
ATOM    532  C   ALA A  83      47.389  17.995 109.916  1.00114.13           C  
ANISOU  532  C   ALA A  83    13436  14040  15889   -583   3811   -598       C  
ATOM    533  O   ALA A  83      47.770  19.156 109.748  1.00116.15           O  
ANISOU  533  O   ALA A  83    13689  14129  16313   -697   4053   -584       O  
ATOM    534  CB  ALA A  83      48.968  17.175 108.059  1.00113.53           C  
ANISOU  534  CB  ALA A  83    13211  14251  15676   -418   3758   -426       C  
ATOM    535  N   ASN A  84      46.277  17.688 110.585  1.00113.67           N  
ANISOU  535  N   ASN A  84    13462  13938  15789   -538   3712   -630       N  
ATOM    536  CA  ASN A  84      45.485  18.672 111.316  1.00115.06           C  
ANISOU  536  CA  ASN A  84    13728  13881  16108   -632   3870   -679       C  
ATOM    537  C   ASN A  84      45.347  18.274 112.788  1.00114.78           C  
ANISOU  537  C   ASN A  84    13691  13898  16024   -772   3728   -901       C  
ATOM    538  O   ASN A  84      45.205  17.089 113.114  1.00113.32           O  
ANISOU  538  O   ASN A  84    13485  13898  15675   -702   3485   -940       O  
ATOM    539  CB  ASN A  84      44.094  18.828 110.686  1.00114.71           C  
ANISOU  539  CB  ASN A  84    13795  13718  16072   -423   3919   -477       C  
ATOM    540  CG  ASN A  84      44.050  19.903 109.606  1.00116.46           C  
ANISOU  540  CG  ASN A  84    14049  13769  16431   -351   4182   -281       C  
ATOM    541  OD1 ASN A  84      44.767  19.837 108.607  1.00116.14           O  
ANISOU  541  OD1 ASN A  84    13951  13810  16366   -288   4216   -173       O  
ATOM    542  ND2 ASN A  84      43.187  20.895 109.802  1.00117.88           N  
ANISOU  542  ND2 ASN A  84    14323  13711  16755   -349   4376   -226       N  
ATOM    543  N   GLY A  97      25.952  11.306 105.581  1.00 83.33           N  
ANISOU  543  N   GLY A  97    10007  10785  10869   1804   2303   1106       N  
ATOM    544  CA  GLY A  97      27.231  10.637 105.329  1.00 82.72           C  
ANISOU  544  CA  GLY A  97     9944  10766  10719   1737   2211    985       C  
ATOM    545  C   GLY A  97      27.180   9.115 105.519  1.00 81.20           C  
ANISOU  545  C   GLY A  97     9741  10708  10403   1684   1950    841       C  
ATOM    546  O   GLY A  97      27.723   8.552 106.516  1.00 80.42           O  
ANISOU  546  O   GLY A  97     9672  10556  10327   1543   1877    671       O  
ATOM    547  N   HIS A  98      26.499   8.439 104.594  1.00 79.93           N  
ANISOU  547  N   HIS A  98     9536  10722  10112   1795   1812    906       N  
ATOM    548  CA  HIS A  98      26.672   7.003 104.481  1.00 77.77           C  
ANISOU  548  CA  HIS A  98     9259  10575   9715   1758   1582    773       C  
ATOM    549  C   HIS A  98      27.441   6.757 103.173  1.00 76.69           C  
ANISOU  549  C   HIS A  98     9111  10574   9455   1852   1552    808       C  
ATOM    550  O   HIS A  98      26.863   6.358 102.148  1.00 77.28           O  
ANISOU  550  O   HIS A  98     9146  10814   9405   1966   1459    879       O  
ATOM    551  CB  HIS A  98      25.336   6.253 104.576  1.00 78.04           C  
ANISOU  551  CB  HIS A  98     9256  10701   9696   1776   1428    775       C  
ATOM    552  CG  HIS A  98      24.677   6.370 105.913  1.00 79.97           C  
ANISOU  552  CG  HIS A  98     9513  10820  10051   1677   1450    727       C  
ATOM    553  ND1 HIS A  98      25.366   6.724 107.057  1.00 82.43           N  
ANISOU  553  ND1 HIS A  98     9877  10972  10472   1553   1539    630       N  
ATOM    554  CD2 HIS A  98      23.389   6.183 106.297  1.00 83.24           C  
ANISOU  554  CD2 HIS A  98     9889  11257  10480   1682   1397    762       C  
ATOM    555  CE1 HIS A  98      24.529   6.759 108.085  1.00 81.30           C  
ANISOU  555  CE1 HIS A  98     9735  10757  10401   1492   1544    607       C  
ATOM    556  NE2 HIS A  98      23.323   6.437 107.651  1.00 81.97           N  
ANISOU  556  NE2 HIS A  98     9765  10945  10436   1570   1462    691       N  
ATOM    557  N   ARG A  99      28.744   7.064 103.215  1.00 74.06           N  
ANISOU  557  N   ARG A  99     8807  10175   9157   1805   1641    761       N  
ATOM    558  CA  ARG A  99      29.640   6.846 102.080  1.00 71.84           C  
ANISOU  558  CA  ARG A  99     8518  10011   8768   1883   1628    782       C  
ATOM    559  C   ARG A  99      29.802   5.349 101.872  1.00 68.77           C  
ANISOU  559  C   ARG A  99     8134   9750   8244   1869   1401    643       C  
ATOM    560  O   ARG A  99      30.125   4.643 102.810  1.00 66.98           O  
ANISOU  560  O   ARG A  99     7935   9466   8049   1753   1312    494       O  
ATOM    561  CB  ARG A  99      31.014   7.511 102.326  1.00 72.24           C  
ANISOU  561  CB  ARG A  99     8589   9953   8905   1813   1780    751       C  
ATOM    562  N   THR A 100      29.528   4.874 100.661  1.00 67.33           N  
ANISOU  562  N   THR A 100     7926   9742   7913   1990   1313    693       N  
ATOM    563  CA  THR A 100      29.907   3.511 100.242  1.00 65.58           C  
ANISOU  563  CA  THR A 100     7720   9641   7558   1991   1125    558       C  
ATOM    564  C   THR A 100      31.430   3.306 100.275  1.00 63.90           C  
ANISOU  564  C   THR A 100     7534   9400   7344   1952   1157    469       C  
ATOM    565  O   THR A 100      32.173   4.220  99.952  1.00 64.14           O  
ANISOU  565  O   THR A 100     7556   9401   7415   1982   1317    553       O  
ATOM    566  CB  THR A 100      29.391   3.200  98.828  1.00 66.56           C  
ANISOU  566  CB  THR A 100     7809   9969   7513   2135   1049    631       C  
ATOM    567  OG1 THR A 100      27.964   3.277  98.844  1.00 67.55           O  
ANISOU  567  OG1 THR A 100     7894  10141   7632   2164    999    701       O  
ATOM    568  CG2 THR A 100      29.786   1.804  98.407  1.00 65.75           C  
ANISOU  568  CG2 THR A 100     7731   9972   7278   2131    868    475       C  
ATOM    569  N   LEU A 101      31.878   2.115 100.680  1.00 61.62           N  
ANISOU  569  N   LEU A 101     7275   9120   7017   1888   1011    307       N  
ATOM    570  CA  LEU A 101      33.303   1.819 100.779  1.00 60.10           C  
ANISOU  570  CA  LEU A 101     7099   8915   6821   1855   1027    219       C  
ATOM    571  C   LEU A 101      33.916   1.527  99.410  1.00 60.16           C  
ANISOU  571  C   LEU A 101     7099   9073   6685   1980   1015    244       C  
ATOM    572  O   LEU A 101      33.366   0.743  98.624  1.00 60.89           O  
ANISOU  572  O   LEU A 101     7197   9290   6647   2055    889    220       O  
ATOM    573  CB  LEU A 101      33.565   0.637 101.698  1.00 58.86           C  
ANISOU  573  CB  LEU A 101     6976   8715   6672   1761    884     52       C  
ATOM    574  CG  LEU A 101      33.020   0.539 103.119  1.00 59.03           C  
ANISOU  574  CG  LEU A 101     7014   8611   6805   1636    853     -6       C  
ATOM    575  CD1 LEU A 101      33.886  -0.427 103.931  1.00 57.38           C  
ANISOU  575  CD1 LEU A 101     6831   8368   6600   1560    765   -150       C  
ATOM    576  CD2 LEU A 101      32.927   1.877 103.806  1.00 57.92           C  
ANISOU  576  CD2 LEU A 101     6856   8355   6798   1575   1022     72       C  
ATOM    577  N   LEU A 102      35.055   2.150  99.122  1.00 58.98           N  
ANISOU  577  N   LEU A 102     6935   8918   6557   1996   1148    285       N  
ATOM    578  CA  LEU A 102      35.717   1.909  97.842  1.00 58.65           C  
ANISOU  578  CA  LEU A 102     6884   9023   6378   2118   1152    312       C  
ATOM    579  C   LEU A 102      37.017   1.191  98.064  1.00 57.59           C  
ANISOU  579  C   LEU A 102     6760   8894   6228   2083   1115    186       C  
ATOM    580  O   LEU A 102      37.721   1.450  99.049  1.00 56.81           O  
ANISOU  580  O   LEU A 102     6653   8688   6247   1974   1171    137       O  
ATOM    581  CB  LEU A 102      35.949   3.218  97.083  1.00 59.62           C  
ANISOU  581  CB  LEU A 102     6972   9164   6519   2196   1348    493       C  
ATOM    582  CG  LEU A 102      34.687   4.067  96.810  1.00 59.52           C  
ANISOU  582  CG  LEU A 102     6942   9148   6526   2256   1412    651       C  
ATOM    583  CD1 LEU A 102      35.069   5.322  96.060  1.00 59.17           C  
ANISOU  583  CD1 LEU A 102     6869   9109   6505   2341   1623    836       C  
ATOM    584  CD2 LEU A 102      33.583   3.310  96.055  1.00 57.62           C  
ANISOU  584  CD2 LEU A 102     6697   9066   6130   2350   1252    651       C  
ATOM    585  N   TYR A 103      37.348   0.269  97.168  1.00 57.16           N  
ANISOU  585  N   TYR A 103     6720   8971   6025   2177   1021    129       N  
ATOM    586  CA  TYR A 103      38.665  -0.341  97.270  1.00 56.37           C  
ANISOU  586  CA  TYR A 103     6622   8886   5908   2168   1009     29       C  
ATOM    587  C   TYR A 103      39.727   0.739  97.148  1.00 57.03           C  
ANISOU  587  C   TYR A 103     6656   8954   6059   2162   1196    121       C  
ATOM    588  O   TYR A 103      39.610   1.652  96.320  1.00 57.52           O  
ANISOU  588  O   TYR A 103     6693   9062   6100   2236   1321    264       O  
ATOM    589  CB  TYR A 103      38.860  -1.395  96.217  1.00 56.78           C  
ANISOU  589  CB  TYR A 103     6703   9082   5789   2285    904    -38       C  
ATOM    590  CG  TYR A 103      38.149  -2.679  96.519  1.00 54.18           C  
ANISOU  590  CG  TYR A 103     6429   8743   5416   2261    717   -176       C  
ATOM    591  CD1 TYR A 103      36.945  -2.980  95.882  1.00 51.46           C  
ANISOU  591  CD1 TYR A 103     6102   8474   4978   2309    624   -168       C  
ATOM    592  CD2 TYR A 103      38.674  -3.588  97.445  1.00 51.28           C  
ANISOU  592  CD2 TYR A 103     6091   8294   5101   2189    637   -308       C  
ATOM    593  CE1 TYR A 103      36.291  -4.156  96.126  1.00 49.39           C  
ANISOU  593  CE1 TYR A 103     5887   8196   4683   2274    460   -299       C  
ATOM    594  CE2 TYR A 103      38.019  -4.783  97.704  1.00 50.59           C  
ANISOU  594  CE2 TYR A 103     6059   8180   4982   2168    478   -427       C  
ATOM    595  CZ  TYR A 103      36.818  -5.054  97.033  1.00 49.35           C  
ANISOU  595  CZ  TYR A 103     5921   8089   4741   2203    393   -427       C  
ATOM    596  OH  TYR A 103      36.126  -6.212  97.292  1.00 48.62           O  
ANISOU  596  OH  TYR A 103     5881   7962   4630   2165    243   -548       O  
ATOM    597  N   GLY A 104      40.752   0.639  97.987  1.00 56.61           N  
ANISOU  597  N   GLY A 104     6581   8839   6087   2071   1219     42       N  
ATOM    598  CA  GLY A 104      41.772   1.663  98.047  1.00 57.82           C  
ANISOU  598  CA  GLY A 104     6677   8964   6327   2029   1395    109       C  
ATOM    599  C   GLY A 104      41.555   2.631  99.189  1.00 58.68           C  
ANISOU  599  C   GLY A 104     6770   8919   6608   1884   1490    126       C  
ATOM    600  O   GLY A 104      42.515   3.279  99.627  1.00 58.93           O  
ANISOU  600  O   GLY A 104     6752   8904   6734   1798   1607    123       O  
ATOM    601  N   HIS A 105      40.306   2.747  99.679  1.00 58.08           N  
ANISOU  601  N   HIS A 105     6730   8764   6573   1850   1443    140       N  
ATOM    602  CA  HIS A 105      40.034   3.544 100.875  1.00 57.65           C  
ANISOU  602  CA  HIS A 105     6670   8557   6676   1709   1520    132       C  
ATOM    603  C   HIS A 105      40.654   2.975 102.157  1.00 56.55           C  
ANISOU  603  C   HIS A 105     6523   8374   6591   1581   1442    -18       C  
ATOM    604  O   HIS A 105      40.874   1.755 102.282  1.00 55.54           O  
ANISOU  604  O   HIS A 105     6411   8309   6381   1606   1289   -118       O  
ATOM    605  CB  HIS A 105      38.541   3.631 101.111  1.00 58.61           C  
ANISOU  605  CB  HIS A 105     6831   8624   6815   1715   1471    173       C  
ATOM    606  CG  HIS A 105      37.847   4.681 100.302  1.00 62.69           C  
ANISOU  606  CG  HIS A 105     7342   9134   7344   1799   1605    345       C  
ATOM    607  ND1 HIS A 105      36.520   4.992 100.493  1.00 64.84           N  
ANISOU  607  ND1 HIS A 105     7633   9357   7648   1812   1597    410       N  
ATOM    608  CD2 HIS A 105      38.291   5.491  99.309  1.00 66.66           C  
ANISOU  608  CD2 HIS A 105     7818   9676   7832   1883   1755    477       C  
ATOM    609  CE1 HIS A 105      36.177   5.953  99.651  1.00 68.42           C  
ANISOU  609  CE1 HIS A 105     8071   9822   8104   1907   1736    578       C  
ATOM    610  NE2 HIS A 105      37.232   6.266  98.916  1.00 68.55           N  
ANISOU  610  NE2 HIS A 105     8064   9890   8092   1951   1835    624       N  
ATOM    611  N   ALA A 106      40.889   3.877 103.118  1.00 55.69           N  
ANISOU  611  N   ALA A 106     6390   8152   6618   1447   1553    -32       N  
ATOM    612  CA  ALA A 106      41.308   3.534 104.471  1.00 54.23           C  
ANISOU  612  CA  ALA A 106     6192   7924   6489   1313   1492   -164       C  
ATOM    613  C   ALA A 106      40.090   3.618 105.439  1.00 53.71           C  
ANISOU  613  C   ALA A 106     6172   7751   6484   1244   1450   -185       C  
ATOM    614  O   ALA A 106      39.327   4.598 105.431  1.00 53.90           O  
ANISOU  614  O   ALA A 106     6211   7682   6586   1230   1564   -101       O  
ATOM    615  CB  ALA A 106      42.401   4.449 104.934  1.00 53.58           C  
ANISOU  615  CB  ALA A 106     6046   7805   6506   1197   1637   -187       C  
ATOM    616  N   ILE A 107      39.927   2.590 106.275  1.00 52.20           N  
ANISOU  616  N   ILE A 107     6001   7572   6260   1208   1296   -288       N  
ATOM    617  CA  ILE A 107      38.792   2.523 107.159  1.00 50.74           C  
ANISOU  617  CA  ILE A 107     5857   7303   6119   1151   1246   -308       C  
ATOM    618  C   ILE A 107      39.154   2.601 108.627  1.00 50.17           C  
ANISOU  618  C   ILE A 107     5770   7179   6113   1008   1243   -411       C  
ATOM    619  O   ILE A 107      40.229   2.187 109.026  1.00 49.76           O  
ANISOU  619  O   ILE A 107     5680   7188   6038    968   1206   -491       O  
ATOM    620  CB  ILE A 107      37.905   1.306 106.891  1.00 49.65           C  
ANISOU  620  CB  ILE A 107     5766   7208   5890   1232   1075   -320       C  
ATOM    621  CG1 ILE A 107      38.659   0.006 107.143  1.00 47.42           C  
ANISOU  621  CG1 ILE A 107     5487   6996   5533   1245    936   -422       C  
ATOM    622  CG2 ILE A 107      37.385   1.380 105.502  1.00 50.47           C  
ANISOU  622  CG2 ILE A 107     5880   7371   5925   1361   1085   -221       C  
ATOM    623  CD1 ILE A 107      37.773  -1.208 106.935  1.00 43.00           C  
ANISOU  623  CD1 ILE A 107     4982   6455   4902   1307    777   -447       C  
ATOM    624  N   LEU A 108      38.223   3.159 109.407  1.00 49.08           N  
ANISOU  624  N   LEU A 108     5658   6938   6052    937   1286   -405       N  
ATOM    625  CA  LEU A 108      38.388   3.304 110.826  1.00 47.99           C  
ANISOU  625  CA  LEU A 108     5513   6753   5969    802   1288   -502       C  
ATOM    626  C   LEU A 108      37.301   2.460 111.445  1.00 47.23           C  
ANISOU  626  C   LEU A 108     5463   6638   5843    810   1158   -520       C  
ATOM    627  O   LEU A 108      36.116   2.723 111.209  1.00 48.42           O  
ANISOU  627  O   LEU A 108     5646   6731   6019    847   1177   -447       O  
ATOM    628  CB  LEU A 108      38.233   4.769 111.203  1.00 48.03           C  
ANISOU  628  CB  LEU A 108     5512   6642   6096    709   1475   -482       C  
ATOM    629  CG  LEU A 108      38.292   5.065 112.697  1.00 48.12           C  
ANISOU  629  CG  LEU A 108     5520   6601   6163    560   1495   -591       C  
ATOM    630  CD1 LEU A 108      39.682   4.852 113.300  1.00 49.46           C  
ANISOU  630  CD1 LEU A 108     5627   6857   6308    469   1468   -706       C  
ATOM    631  CD2 LEU A 108      37.819   6.468 112.948  1.00 46.83           C  
ANISOU  631  CD2 LEU A 108     5374   6296   6124    491   1683   -563       C  
ATOM    632  N   LEU A 109      37.683   1.452 112.223  1.00 46.08           N  
ANISOU  632  N   LEU A 109     5317   6546   5647    780   1032   -606       N  
ATOM    633  CA  LEU A 109      36.727   0.484 112.769  1.00 44.97           C  
ANISOU  633  CA  LEU A 109     5221   6391   5474    792    902   -620       C  
ATOM    634  C   LEU A 109      36.568   0.673 114.279  1.00 44.49           C  
ANISOU  634  C   LEU A 109     5161   6288   5455    673    911   -687       C  
ATOM    635  O   LEU A 109      37.503   0.377 115.032  1.00 43.71           O  
ANISOU  635  O   LEU A 109     5031   6248   5330    617    878   -765       O  
ATOM    636  CB  LEU A 109      37.175  -0.944 112.467  1.00 44.16           C  
ANISOU  636  CB  LEU A 109     5130   6371   5278    868    750   -653       C  
ATOM    637  CG  LEU A 109      36.950  -1.424 111.040  1.00 45.24           C  
ANISOU  637  CG  LEU A 109     5286   6547   5354    994    705   -599       C  
ATOM    638  CD1 LEU A 109      37.942  -2.560 110.651  1.00 46.74           C  
ANISOU  638  CD1 LEU A 109     5474   6824   5460   1066    607   -649       C  
ATOM    639  CD2 LEU A 109      35.540  -1.869 110.824  1.00 41.17           C  
ANISOU  639  CD2 LEU A 109     4817   5993   4832   1029    635   -560       C  
ATOM    640  N   ARG A 110      35.403   1.181 114.727  1.00 43.73           N  
ANISOU  640  N   ARG A 110     5094   6104   5416    638    959   -655       N  
ATOM    641  CA  ARG A 110      35.194   1.399 116.166  1.00 42.91           C  
ANISOU  641  CA  ARG A 110     4995   5964   5344    528    977   -721       C  
ATOM    642  C   ARG A 110      34.529   0.165 116.730  1.00 42.26           C  
ANISOU  642  C   ARG A 110     4946   5901   5211    549    832   -727       C  
ATOM    643  O   ARG A 110      33.562  -0.366 116.137  1.00 42.30           O  
ANISOU  643  O   ARG A 110     4980   5885   5206    621    770   -663       O  
ATOM    644  CB  ARG A 110      34.356   2.628 116.387  1.00 44.02           C  
ANISOU  644  CB  ARG A 110     5151   5996   5578    483   1122   -685       C  
ATOM    645  CG  ARG A 110      33.938   2.923 117.804  1.00 45.89           C  
ANISOU  645  CG  ARG A 110     5401   6187   5846    379   1155   -750       C  
ATOM    646  CD  ARG A 110      33.661   4.396 117.910  1.00 52.45           C  
ANISOU  646  CD  ARG A 110     6239   6909   6781    323   1343   -741       C  
ATOM    647  NE  ARG A 110      34.055   4.878 119.226  1.00 60.74           N  
ANISOU  647  NE  ARG A 110     7284   7947   7850    189   1400   -858       N  
ATOM    648  CZ  ARG A 110      33.815   6.098 119.702  1.00 63.19           C  
ANISOU  648  CZ  ARG A 110     7608   8151   8249    111   1565   -891       C  
ATOM    649  NH1 ARG A 110      33.172   6.987 118.958  1.00 65.11           N  
ANISOU  649  NH1 ARG A 110     7874   8283   8581    164   1699   -796       N  
ATOM    650  NH2 ARG A 110      34.211   6.414 120.933  1.00 62.34           N  
ANISOU  650  NH2 ARG A 110     7495   8054   8138    -17   1598  -1018       N  
ATOM    651  N   HIS A 111      35.083  -0.336 117.829  1.00 40.86           N  
ANISOU  651  N   HIS A 111     4758   5772   4996    489    775   -802       N  
ATOM    652  CA  HIS A 111      34.536  -1.512 118.501  1.00 40.43           C  
ANISOU  652  CA  HIS A 111     4734   5729   4897    503    650   -802       C  
ATOM    653  C   HIS A 111      33.182  -1.135 119.205  1.00 40.74           C  
ANISOU  653  C   HIS A 111     4804   5686   4989    456    692   -774       C  
ATOM    654  O   HIS A 111      33.126  -0.211 120.021  1.00 41.28           O  
ANISOU  654  O   HIS A 111     4864   5724   5095    371    792   -812       O  
ATOM    655  CB  HIS A 111      35.580  -1.948 119.499  1.00 39.36           C  
ANISOU  655  CB  HIS A 111     4569   5681   4705    456    603   -877       C  
ATOM    656  CG  HIS A 111      35.281  -3.207 120.237  1.00 38.59           C  
ANISOU  656  CG  HIS A 111     4501   5606   4556    479    482   -871       C  
ATOM    657  ND1 HIS A 111      35.207  -4.441 119.621  1.00 39.82           N  
ANISOU  657  ND1 HIS A 111     4688   5765   4677    574    373   -835       N  
ATOM    658  CD2 HIS A 111      35.161  -3.446 121.566  1.00 36.63           C  
ANISOU  658  CD2 HIS A 111     4254   5383   4280    420    460   -900       C  
ATOM    659  CE1 HIS A 111      35.007  -5.380 120.532  1.00 36.83           C  
ANISOU  659  CE1 HIS A 111     4333   5397   4265    572    295   -833       C  
ATOM    660  NE2 HIS A 111      34.992  -4.801 121.719  1.00 36.36           N  
ANISOU  660  NE2 HIS A 111     4252   5360   4203    484    344   -866       N  
ATOM    661  N   ALA A 112      32.107  -1.851 118.916  1.00 40.46           N  
ANISOU  661  N   ALA A 112     4802   5618   4955    507    620   -715       N  
ATOM    662  CA  ALA A 112      30.805  -1.483 119.475  1.00 40.44           C  
ANISOU  662  CA  ALA A 112     4816   5547   5004    473    665   -677       C  
ATOM    663  C   ALA A 112      30.813  -1.525 120.979  1.00 41.23           C  
ANISOU  663  C   ALA A 112     4921   5653   5091    389    673   -730       C  
ATOM    664  O   ALA A 112      30.338  -0.596 121.625  1.00 43.55           O  
ANISOU  664  O   ALA A 112     5215   5900   5431    329    779   -740       O  
ATOM    665  CB  ALA A 112      29.728  -2.363 118.929  1.00 39.09           C  
ANISOU  665  CB  ALA A 112     4665   5358   4831    532    572   -613       C  
ATOM    666  N   HIS A 113      31.355  -2.582 121.574  1.00 41.63           N  
ANISOU  666  N   HIS A 113     4976   5764   5076    388    569   -761       N  
ATOM    667  CA  HIS A 113      31.277  -2.697 123.041  1.00 40.78           C  
ANISOU  667  CA  HIS A 113     4874   5681   4941    318    570   -798       C  
ATOM    668  C   HIS A 113      32.111  -1.661 123.759  1.00 41.39           C  
ANISOU  668  C   HIS A 113     4918   5799   5008    233    665   -885       C  
ATOM    669  O   HIS A 113      31.577  -0.941 124.562  1.00 42.46           O  
ANISOU  669  O   HIS A 113     5061   5902   5170    166    749   -910       O  
ATOM    670  CB  HIS A 113      31.619  -4.113 123.551  1.00 40.28           C  
ANISOU  670  CB  HIS A 113     4824   5675   4807    350    442   -792       C  
ATOM    671  CG  HIS A 113      31.866  -4.168 125.020  1.00 41.76           C  
ANISOU  671  CG  HIS A 113     5002   5923   4940    288    445   -831       C  
ATOM    672  ND1 HIS A 113      30.900  -3.831 125.957  1.00 44.30           N  
ANISOU  672  ND1 HIS A 113     5341   6212   5280    232    498   -821       N  
ATOM    673  CD2 HIS A 113      32.986  -4.455 125.723  1.00 41.88           C  
ANISOU  673  CD2 HIS A 113     4987   6050   4875    275    408   -882       C  
ATOM    674  CE1 HIS A 113      31.412  -3.938 127.173  1.00 41.38           C  
ANISOU  674  CE1 HIS A 113     4957   5930   4837    187    491   -867       C  
ATOM    675  NE2 HIS A 113      32.674  -4.316 127.063  1.00 42.10           N  
ANISOU  675  NE2 HIS A 113     5016   6115   4866    212    433   -902       N  
ATOM    676  N   SER A 114      33.410  -1.578 123.468  1.00 41.48           N  
ANISOU  676  N   SER A 114     4892   5885   4985    232    655   -937       N  
ATOM    677  CA  SER A 114      34.345  -0.767 124.253  1.00 42.15           C  
ANISOU  677  CA  SER A 114     4934   6035   5047    135    723  -1037       C  
ATOM    678  C   SER A 114      34.466   0.636 123.697  1.00 42.94           C  
ANISOU  678  C   SER A 114     5021   6065   5230     86    869  -1067       C  
ATOM    679  O   SER A 114      35.028   1.534 124.327  1.00 43.03           O  
ANISOU  679  O   SER A 114     5004   6097   5250    -16    958  -1160       O  
ATOM    680  CB  SER A 114      35.751  -1.437 124.274  1.00 41.92           C  
ANISOU  680  CB  SER A 114     4853   6140   4934    156    636  -1077       C  
ATOM    681  OG  SER A 114      36.387  -1.394 122.974  1.00 42.95           O  
ANISOU  681  OG  SER A 114     4964   6269   5088    218    637  -1055       O  
ATOM    682  N   ARG A 115      34.021   0.808 122.465  1.00 44.22           N  
ANISOU  682  N   ARG A 115     5201   6151   5450    159    896   -988       N  
ATOM    683  CA  ARG A 115      34.160   2.107 121.785  1.00 47.09           C  
ANISOU  683  CA  ARG A 115     5555   6440   5898    134   1044   -989       C  
ATOM    684  C   ARG A 115      35.602   2.510 121.493  1.00 47.44           C  
ANISOU  684  C   ARG A 115     5543   6550   5931     92   1077  -1056       C  
ATOM    685  O   ARG A 115      35.859   3.653 121.116  1.00 48.02           O  
ANISOU  685  O   ARG A 115     5605   6560   6080     47   1216  -1072       O  
ATOM    686  CB  ARG A 115      33.341   3.203 122.523  1.00 48.30           C  
ANISOU  686  CB  ARG A 115     5735   6492   6124     57   1183  -1014       C  
ATOM    687  CG  ARG A 115      31.846   2.806 122.496  1.00 54.11           C  
ANISOU  687  CG  ARG A 115     6513   7165   6881    123   1154   -919       C  
ATOM    688  CD  ARG A 115      30.882   3.903 122.883  1.00 66.80           C  
ANISOU  688  CD  ARG A 115     8148   8658   8574     88   1305   -908       C  
ATOM    689  NE  ARG A 115      30.635   4.871 121.807  1.00 75.57           N  
ANISOU  689  NE  ARG A 115     9263   9675   9777    136   1430   -836       N  
ATOM    690  CZ  ARG A 115      30.763   6.198 121.961  1.00 80.72           C  
ANISOU  690  CZ  ARG A 115     9924  10231  10514     76   1609   -875       C  
ATOM    691  NH1 ARG A 115      31.121   6.716 123.143  1.00 80.28           N  
ANISOU  691  NH1 ARG A 115     9875  10166  10461    -45   1678  -1001       N  
ATOM    692  NH2 ARG A 115      30.537   7.016 120.935  1.00 83.43           N  
ANISOU  692  NH2 ARG A 115    10272  10488  10940    137   1725   -787       N  
ATOM    693  N   MET A 116      36.538   1.562 121.649  1.00 47.78           N  
ANISOU  693  N   MET A 116     5549   6719   5885    113    957  -1088       N  
ATOM    694  CA  MET A 116      37.925   1.753 121.218  1.00 48.01           C  
ANISOU  694  CA  MET A 116     5511   6833   5896     95    969  -1134       C  
ATOM    695  C   MET A 116      38.055   1.384 119.730  1.00 47.67           C  
ANISOU  695  C   MET A 116     5474   6780   5858    217    943  -1046       C  
ATOM    696  O   MET A 116      37.091   0.866 119.127  1.00 47.31           O  
ANISOU  696  O   MET A 116     5481   6677   5816    309    895   -961       O  
ATOM    697  CB  MET A 116      38.847   0.906 122.067  1.00 48.34           C  
ANISOU  697  CB  MET A 116     5504   7028   5836     77    856  -1198       C  
ATOM    698  CG  MET A 116      38.741   1.225 123.530  1.00 48.76           C  
ANISOU  698  CG  MET A 116     5547   7118   5861    -37    873  -1286       C  
ATOM    699  SD  MET A 116      39.824   0.145 124.448  1.00 52.20           S  
ANISOU  699  SD  MET A 116     5915   7760   6160    -30    730  -1333       S  
ATOM    700  CE  MET A 116      39.392   0.391 126.172  1.00 44.34           C  
ANISOU  700  CE  MET A 116     4924   6813   5111   -142    738  -1416       C  
ATOM    701  N   TYR A 117      39.214   1.657 119.129  1.00 47.70           N  
ANISOU  701  N   TYR A 117     5419   6846   5858    215    976  -1068       N  
ATOM    702  CA  TYR A 117      39.378   1.450 117.676  1.00 47.41           C  
ANISOU  702  CA  TYR A 117     5387   6805   5822    329    973   -987       C  
ATOM    703  C   TYR A 117      40.350   0.345 117.333  1.00 47.46           C  
ANISOU  703  C   TYR A 117     5356   6936   5740    409    855   -993       C  
ATOM    704  O   TYR A 117      41.342   0.141 118.051  1.00 48.60           O  
ANISOU  704  O   TYR A 117     5437   7188   5840    358    821  -1064       O  
ATOM    705  CB  TYR A 117      39.800   2.723 116.998  1.00 48.03           C  
ANISOU  705  CB  TYR A 117     5436   6834   5980    288   1133   -976       C  
ATOM    706  CG  TYR A 117      38.825   3.833 117.191  1.00 49.50           C  
ANISOU  706  CG  TYR A 117     5665   6878   6264    232   1268   -955       C  
ATOM    707  CD1 TYR A 117      38.904   4.664 118.305  1.00 52.49           C  
ANISOU  707  CD1 TYR A 117     6033   7218   6692     89   1357  -1049       C  
ATOM    708  CD2 TYR A 117      37.796   4.051 116.268  1.00 51.21           C  
ANISOU  708  CD2 TYR A 117     5933   7007   6519    326   1308   -841       C  
ATOM    709  CE1 TYR A 117      37.989   5.693 118.490  1.00 54.21           C  
ANISOU  709  CE1 TYR A 117     6299   7293   7007     47   1494  -1029       C  
ATOM    710  CE2 TYR A 117      36.878   5.083 116.439  1.00 51.92           C  
ANISOU  710  CE2 TYR A 117     6059   6965   6702    292   1441   -807       C  
ATOM    711  CZ  TYR A 117      36.987   5.891 117.548  1.00 53.98           C  
ANISOU  711  CZ  TYR A 117     6317   7171   7021    155   1538   -901       C  
ATOM    712  OH  TYR A 117      36.094   6.893 117.732  1.00 57.70           O  
ANISOU  712  OH  TYR A 117     6831   7506   7589    129   1679   -870       O  
ATOM    713  N   LEU A 118      40.058  -0.381 116.253  1.00 46.84           N  
ANISOU  713  N   LEU A 118     5315   6851   5631    538    793   -921       N  
ATOM    714  CA  LEU A 118      40.892  -1.488 115.834  1.00 46.99           C  
ANISOU  714  CA  LEU A 118     5313   6970   5570    633    689   -924       C  
ATOM    715  C   LEU A 118      42.268  -0.967 115.395  1.00 48.75           C  
ANISOU  715  C   LEU A 118     5451   7283   5790    618    757   -950       C  
ATOM    716  O   LEU A 118      42.387  -0.172 114.447  1.00 48.73           O  
ANISOU  716  O   LEU A 118     5437   7249   5830    629    861   -910       O  
ATOM    717  CB  LEU A 118      40.232  -2.303 114.730  1.00 45.55           C  
ANISOU  717  CB  LEU A 118     5195   6755   5358    764    620   -858       C  
ATOM    718  CG  LEU A 118      41.088  -3.531 114.351  1.00 45.12           C  
ANISOU  718  CG  LEU A 118     5131   6790   5222    868    516   -870       C  
ATOM    719  CD1 LEU A 118      41.214  -4.500 115.516  1.00 43.42           C  
ANISOU  719  CD1 LEU A 118     4922   6608   4968    858    414   -906       C  
ATOM    720  CD2 LEU A 118      40.524  -4.237 113.138  1.00 43.47           C  
ANISOU  720  CD2 LEU A 118     4985   6551   4981    989    462   -825       C  
ATOM    721  N   SER A 119      43.309  -1.361 116.107  1.00 50.14           N  
ANISOU  721  N   SER A 119     5557   7575   5917    589    709  -1010       N  
ATOM    722  CA  SER A 119      44.605  -0.895 115.665  1.00 53.22           C  
ANISOU  722  CA  SER A 119     5854   8061   6307    572    772  -1032       C  
ATOM    723  C   SER A 119      45.723  -1.927 115.536  1.00 54.06           C  
ANISOU  723  C   SER A 119     5902   8312   6328    665    680  -1041       C  
ATOM    724  O   SER A 119      45.621  -3.083 115.956  1.00 52.66           O  
ANISOU  724  O   SER A 119     5754   8167   6087    739    561  -1037       O  
ATOM    725  CB  SER A 119      45.058   0.281 116.490  1.00 53.75           C  
ANISOU  725  CB  SER A 119     5851   8143   6429    404    875  -1109       C  
ATOM    726  OG  SER A 119      45.575  -0.204 117.698  1.00 57.75           O  
ANISOU  726  OG  SER A 119     6304   8763   6875    352    792  -1179       O  
ATOM    727  N   CYS A 120      46.778  -1.462 114.885  1.00 57.03           N  
ANISOU  727  N   CYS A 120     6194   8764   6709    665    751  -1044       N  
ATOM    728  CA  CYS A 120      48.025  -2.159 114.796  1.00 59.47           C  
ANISOU  728  CA  CYS A 120     6418   9228   6950    733    697  -1057       C  
ATOM    729  C   CYS A 120      48.861  -1.664 115.957  1.00 61.28           C  
ANISOU  729  C   CYS A 120     6532   9574   7177    594    711  -1139       C  
ATOM    730  O   CYS A 120      49.252  -0.502 115.997  1.00 61.86           O  
ANISOU  730  O   CYS A 120     6540   9649   7315    464    825  -1180       O  
ATOM    731  CB  CYS A 120      48.680  -1.828 113.469  1.00 60.03           C  
ANISOU  731  CB  CYS A 120     6452   9326   7030    798    779  -1014       C  
ATOM    732  SG  CYS A 120      50.091  -2.900 113.140  1.00 64.19           S  
ANISOU  732  SG  CYS A 120     6890  10036   7464    932    707  -1011       S  
ATOM    733  N   LEU A 121      49.092  -2.536 116.929  1.00 63.26           N  
ANISOU  733  N   LEU A 121     6759   9921   7355    618    597  -1164       N  
ATOM    734  CA  LEU A 121      49.836  -2.163 118.126  1.00 66.29           C  
ANISOU  734  CA  LEU A 121     7029  10446   7714    491    590  -1246       C  
ATOM    735  C   LEU A 121      51.327  -2.218 117.862  1.00 69.17           C  
ANISOU  735  C   LEU A 121     7246  10995   8039    510    596  -1262       C  
ATOM    736  O   LEU A 121      51.740  -2.732 116.855  1.00 70.12           O  
ANISOU  736  O   LEU A 121     7366  11134   8143    642    592  -1203       O  
ATOM    737  CB  LEU A 121      49.468  -3.082 119.290  1.00 65.65           C  
ANISOU  737  CB  LEU A 121     6978  10410   7558    520    468  -1250       C  
ATOM    738  CG  LEU A 121      47.985  -3.136 119.686  1.00 64.37           C  
ANISOU  738  CG  LEU A 121     6950  10079   7426    501    454  -1232       C  
ATOM    739  CD1 LEU A 121      47.784  -4.129 120.787  1.00 62.80           C  
ANISOU  739  CD1 LEU A 121     6768   9943   7148    544    338  -1221       C  
ATOM    740  CD2 LEU A 121      47.419  -1.777 120.067  1.00 62.82           C  
ANISOU  740  CD2 LEU A 121     6767   9792   7311    330    565  -1294       C  
ATOM    741  N   THR A 122      52.142  -1.694 118.766  1.00 72.96           N  
ANISOU  741  N   THR A 122     7595  11625   8501    376    606  -1346       N  
ATOM    742  CA  THR A 122      53.605  -1.689 118.577  1.00 76.36           C  
ANISOU  742  CA  THR A 122     7860  12256   8896    379    613  -1365       C  
ATOM    743  C   THR A 122      54.328  -2.756 119.397  1.00 78.21           C  
ANISOU  743  C   THR A 122     8007  12698   9012    465    481  -1360       C  
ATOM    744  O   THR A 122      55.552  -2.738 119.489  1.00 80.02           O  
ANISOU  744  O   THR A 122     8076  13128   9200    454    475  -1384       O  
ATOM    745  CB  THR A 122      54.231  -0.303 118.910  1.00 77.67           C  
ANISOU  745  CB  THR A 122     7906  12479   9126    159    726  -1470       C  
ATOM    746  OG1 THR A 122      54.015  -0.001 120.295  1.00 78.73           O  
ANISOU  746  OG1 THR A 122     8015  12669   9231     17    689  -1567       O  
ATOM    747  CG2 THR A 122      53.618   0.816 118.046  1.00 77.90           C  
ANISOU  747  CG2 THR A 122     8014  12299   9284     83    880  -1460       C  
ATOM    748  N   THR A 123      53.577  -3.669 120.000  1.00 78.99           N  
ANISOU  748  N   THR A 123     8203  12752   9056    552    381  -1321       N  
ATOM    749  CA  THR A 123      54.158  -4.786 120.744  1.00 81.40           C  
ANISOU  749  CA  THR A 123     8446  13234   9250    665    260  -1288       C  
ATOM    750  C   THR A 123      54.086  -6.083 119.926  1.00 82.41           C  
ANISOU  750  C   THR A 123     8657  13302   9352    897    205  -1181       C  
ATOM    751  O   THR A 123      53.431  -6.117 118.880  1.00 81.49           O  
ANISOU  751  O   THR A 123     8660  13006   9296    955    247  -1144       O  
ATOM    752  CB  THR A 123      53.410  -5.023 122.073  1.00 81.31           C  
ANISOU  752  CB  THR A 123     8485  13221   9188    614    189  -1308       C  
ATOM    753  OG1 THR A 123      52.015  -5.282 121.807  1.00 78.64           O  
ANISOU  753  OG1 THR A 123     8332  12644   8904    654    191  -1262       O  
ATOM    754  CG2 THR A 123      53.592  -3.825 123.028  1.00 81.64           C  
ANISOU  754  CG2 THR A 123     8433  13353   9232    387    235  -1433       C  
ATOM    755  N   SER A 124      54.725  -7.154 120.417  1.00 84.86           N  
ANISOU  755  N   SER A 124     8910  13761   9570   1032    113  -1131       N  
ATOM    756  CA  SER A 124      54.686  -8.443 119.712  1.00 86.19           C  
ANISOU  756  CA  SER A 124     9166  13864   9719   1255     67  -1037       C  
ATOM    757  C   SER A 124      54.605  -9.747 120.551  1.00 87.63           C  
ANISOU  757  C   SER A 124     9383  14089   9825   1396    -37   -965       C  
ATOM    758  O   SER A 124      54.934  -9.773 121.742  1.00 88.49           O  
ANISOU  758  O   SER A 124     9401  14358   9863   1352    -89   -973       O  
ATOM    759  CB  SER A 124      55.852  -8.525 118.714  1.00 86.99           C  
ANISOU  759  CB  SER A 124     9166  14075   9813   1352    109  -1018       C  
ATOM    760  OG  SER A 124      55.599  -9.530 117.745  1.00 86.19           O  
ANISOU  760  OG  SER A 124     9183  13848   9716   1543     97   -951       O  
ATOM    761  N   ARG A 125      54.179 -10.824 119.873  1.00 88.51           N  
ANISOU  761  N   ARG A 125     9627  14053   9950   1568    -59   -895       N  
ATOM    762  CA  ARG A 125      54.120 -12.208 120.399  1.00 89.81           C  
ANISOU  762  CA  ARG A 125     9847  14213  10063   1737   -137   -810       C  
ATOM    763  C   ARG A 125      52.946 -12.425 121.365  1.00 89.30           C  
ANISOU  763  C   ARG A 125     9892  14033  10004   1677   -181   -795       C  
ATOM    764  O   ARG A 125      51.832 -12.755 120.928  1.00 88.55           O  
ANISOU  764  O   ARG A 125     9958  13715   9971   1690   -176   -784       O  
ATOM    765  CB  ARG A 125      55.468 -12.674 121.008  1.00 91.59           C  
ANISOU  765  CB  ARG A 125     9904  14702  10194   1838   -178   -765       C  
ATOM    766  N   LYS A 130      61.077 -10.928 115.578  1.00 89.03           N  
ANISOU  766  N   LYS A 130     8975  14952   9901   2073    186   -810       N  
ATOM    767  CA  LYS A 130      60.592 -11.174 114.210  1.00 88.79           C  
ANISOU  767  CA  LYS A 130     9097  14730   9911   2173    245   -798       C  
ATOM    768  C   LYS A 130      59.524 -10.124 113.754  1.00 87.04           C  
ANISOU  768  C   LYS A 130     8986  14319   9768   1997    302   -853       C  
ATOM    769  O   LYS A 130      59.202  -9.175 114.506  1.00 87.15           O  
ANISOU  769  O   LYS A 130     8957  14339   9814   1795    307   -905       O  
ATOM    770  CB  LYS A 130      60.091 -12.628 114.039  1.00 88.95           C  
ANISOU  770  CB  LYS A 130     9283  14609   9906   2388    187   -743       C  
ATOM    771  N   LEU A 131      58.969 -10.291 112.547  1.00 84.63           N  
ANISOU  771  N   LEU A 131     8820  13849   9488   2077    348   -843       N  
ATOM    772  CA  LEU A 131      58.383  -9.135 111.871  1.00 82.84           C  
ANISOU  772  CA  LEU A 131     8635  13514   9326   1934    434   -875       C  
ATOM    773  C   LEU A 131      56.880  -8.793 112.176  1.00 80.57           C  
ANISOU  773  C   LEU A 131     8506  13018   9090   1819    411   -901       C  
ATOM    774  O   LEU A 131      56.191  -8.098 111.394  1.00 79.66           O  
ANISOU  774  O   LEU A 131     8468  12776   9022   1760    477   -907       O  
ATOM    775  CB  LEU A 131      58.700  -9.229 110.374  1.00 83.10           C  
ANISOU  775  CB  LEU A 131     8696  13529   9348   2060    513   -848       C  
ATOM    776  CG  LEU A 131      60.045  -8.614 109.882  1.00 85.62           C  
ANISOU  776  CG  LEU A 131     8828  14041   9663   2052    606   -836       C  
ATOM    777  CD1 LEU A 131      61.254  -8.717 110.846  1.00 85.52           C  
ANISOU  777  CD1 LEU A 131     8612  14266   9617   2036    572   -836       C  
ATOM    778  CD2 LEU A 131      60.438  -9.118 108.483  1.00 85.84           C  
ANISOU  778  CD2 LEU A 131     8893  14071   9650   2239    665   -798       C  
ATOM    779  N   ALA A 132      56.373  -9.256 113.316  1.00 78.12           N  
ANISOU  779  N   ALA A 132     8234  12680   8768   1792    322   -908       N  
ATOM    780  CA  ALA A 132      54.929  -9.246 113.492  1.00 75.27           C  
ANISOU  780  CA  ALA A 132     8036  12116   8446   1732    292   -919       C  
ATOM    781  C   ALA A 132      54.491  -8.256 114.563  1.00 73.36           C  
ANISOU  781  C   ALA A 132     7756  11874   8245   1525    298   -964       C  
ATOM    782  O   ALA A 132      55.133  -8.110 115.600  1.00 74.73           O  
ANISOU  782  O   ALA A 132     7808  12199   8388   1458    269   -986       O  
ATOM    783  CB  ALA A 132      54.405 -10.664 113.790  1.00 75.17           C  
ANISOU  783  CB  ALA A 132     8145  12015   8400   1877    195   -887       C  
ATOM    784  N   PHE A 133      53.414  -7.550 114.301  1.00 69.83           N  
ANISOU  784  N   PHE A 133     7406  11266   7859   1425    341   -980       N  
ATOM    785  CA  PHE A 133      52.841  -6.730 115.339  1.00 67.19           C  
ANISOU  785  CA  PHE A 133     7064  10902   7564   1245    347  -1025       C  
ATOM    786  C   PHE A 133      51.523  -7.298 115.803  1.00 64.49           C  
ANISOU  786  C   PHE A 133     6870  10404   7230   1257    279  -1011       C  
ATOM    787  O   PHE A 133      50.753  -7.896 115.014  1.00 63.08           O  
ANISOU  787  O   PHE A 133     6819  10087   7060   1356    260   -977       O  
ATOM    788  CB  PHE A 133      52.663  -5.300 114.848  1.00 67.21           C  
ANISOU  788  CB  PHE A 133     7045  10847   7645   1099    469  -1054       C  
ATOM    789  CG  PHE A 133      53.952  -4.546 114.705  1.00 68.64           C  
ANISOU  789  CG  PHE A 133     7060  11186   7834   1030    547  -1082       C  
ATOM    790  CD1 PHE A 133      54.811  -4.392 115.802  1.00 69.19           C  
ANISOU  790  CD1 PHE A 133     6985  11434   7870    940    516  -1135       C  
ATOM    791  CD2 PHE A 133      54.304  -3.970 113.483  1.00 68.60           C  
ANISOU  791  CD2 PHE A 133     7034  11163   7866   1049    652  -1055       C  
ATOM    792  CE1 PHE A 133      55.999  -3.673 115.675  1.00 70.99           C  
ANISOU  792  CE1 PHE A 133     7046  11816   8111    858    588  -1169       C  
ATOM    793  CE2 PHE A 133      55.498  -3.247 113.343  1.00 68.75           C  
ANISOU  793  CE2 PHE A 133     6893  11326   7904    973    735  -1078       C  
ATOM    794  CZ  PHE A 133      56.340  -3.092 114.434  1.00 70.13           C  
ANISOU  794  CZ  PHE A 133     6920  11673   8054    871    702  -1139       C  
ATOM    795  N   ASP A 134      51.274  -7.101 117.092  1.00 62.96           N  
ANISOU  795  N   ASP A 134     6652  10242   7029   1150    244  -1041       N  
ATOM    796  CA  ASP A 134      49.984  -7.390 117.709  1.00 60.10           C  
ANISOU  796  CA  ASP A 134     6412   9740   6683   1122    197  -1032       C  
ATOM    797  C   ASP A 134      48.903  -6.528 117.099  1.00 57.45           C  
ANISOU  797  C   ASP A 134     6164   9234   6428   1040    270  -1040       C  
ATOM    798  O   ASP A 134      49.106  -5.341 116.840  1.00 56.70           O  
ANISOU  798  O   ASP A 134     6016   9146   6383    930    367  -1073       O  
ATOM    799  CB  ASP A 134      50.041  -7.090 119.194  1.00 61.01           C  
ANISOU  799  CB  ASP A 134     6464   9949   6769   1004    168  -1072       C  
ATOM    800  CG  ASP A 134      50.771  -8.149 119.991  1.00 64.24           C  
ANISOU  800  CG  ASP A 134     6813  10509   7087   1106     75  -1040       C  
ATOM    801  OD1 ASP A 134      50.973  -9.267 119.471  1.00 66.96           O  
ANISOU  801  OD1 ASP A 134     7201  10836   7406   1277     29   -978       O  
ATOM    802  OD2 ASP A 134      51.130  -7.855 121.168  1.00 68.58           O  
ANISOU  802  OD2 ASP A 134     7271  11198   7587   1016     51  -1076       O  
ATOM    803  N   VAL A 135      47.755  -7.144 116.860  1.00 55.34           N  
ANISOU  803  N   VAL A 135     6031   8818   6177   1097    228  -1004       N  
ATOM    804  CA  VAL A 135      46.534  -6.408 116.589  1.00 53.77           C  
ANISOU  804  CA  VAL A 135     5914   8469   6048   1017    279  -1003       C  
ATOM    805  C   VAL A 135      45.600  -6.328 117.832  1.00 53.51           C  
ANISOU  805  C   VAL A 135     5924   8379   6030    922    250  -1016       C  
ATOM    806  O   VAL A 135      45.315  -7.334 118.503  1.00 54.05           O  
ANISOU  806  O   VAL A 135     6034   8442   6060    975    164   -994       O  
ATOM    807  CB  VAL A 135      45.813  -7.002 115.399  1.00 53.12           C  
ANISOU  807  CB  VAL A 135     5938   8272   5973   1130    259   -961       C  
ATOM    808  CG1 VAL A 135      44.457  -6.310 115.191  1.00 49.73           C  
ANISOU  808  CG1 VAL A 135     5585   7702   5608   1057    302   -948       C  
ATOM    809  CG2 VAL A 135      46.705  -6.884 114.167  1.00 51.36           C  
ANISOU  809  CG2 VAL A 135     5671   8113   5732   1212    308   -951       C  
ATOM    810  N   GLY A 136      45.139  -5.131 118.153  1.00 52.71           N  
ANISOU  810  N   GLY A 136     5812   8232   5985    785    333  -1049       N  
ATOM    811  CA  GLY A 136      44.121  -4.987 119.197  1.00 51.88           C  
ANISOU  811  CA  GLY A 136     5757   8057   5897    701    320  -1060       C  
ATOM    812  C   GLY A 136      43.556  -3.591 119.264  1.00 51.35           C  
ANISOU  812  C   GLY A 136     5693   7910   5907    569    435  -1092       C  
ATOM    813  O   GLY A 136      43.564  -2.863 118.274  1.00 51.79           O  
ANISOU  813  O   GLY A 136     5748   7913   6016    567    520  -1078       O  
ATOM    814  N   LEU A 137      43.095  -3.191 120.439  1.00 51.41           N  
ANISOU  814  N   LEU A 137     5703   7911   5920    463    448  -1133       N  
ATOM    815  CA  LEU A 137      42.274  -1.979 120.531  1.00 51.26           C  
ANISOU  815  CA  LEU A 137     5715   7777   5984    355    560  -1155       C  
ATOM    816  C   LEU A 137      43.013  -0.770 121.100  1.00 52.55           C  
ANISOU  816  C   LEU A 137     5796   8000   6173    206    660  -1250       C  
ATOM    817  O   LEU A 137      43.776  -0.846 122.056  1.00 51.89           O  
ANISOU  817  O   LEU A 137     5638   8052   6027    143    625  -1320       O  
ATOM    818  CB  LEU A 137      40.960  -2.251 121.276  1.00 50.22           C  
ANISOU  818  CB  LEU A 137     5665   7556   5862    340    530  -1132       C  
ATOM    819  CG  LEU A 137      40.011  -3.322 120.705  1.00 49.66           C  
ANISOU  819  CG  LEU A 137     5682   7400   5789    459    447  -1045       C  
ATOM    820  CD1 LEU A 137      38.812  -3.551 121.640  1.00 49.12           C  
ANISOU  820  CD1 LEU A 137     5673   7263   5729    424    424  -1028       C  
ATOM    821  CD2 LEU A 137      39.530  -2.938 119.321  1.00 48.19           C  
ANISOU  821  CD2 LEU A 137     5530   7117   5661    512    500   -994       C  
ATOM    822  N   GLN A 138      42.789   0.348 120.455  1.00 54.31           N  
ANISOU  822  N   GLN A 138     6029   8121   6487    152    790  -1251       N  
ATOM    823  CA  GLN A 138      43.401   1.569 120.865  1.00 58.10           C  
ANISOU  823  CA  GLN A 138     6442   8618   7014      2    907  -1344       C  
ATOM    824  C   GLN A 138      42.304   2.458 121.420  1.00 59.52           C  
ANISOU  824  C   GLN A 138     6690   8657   7268    -88   1004  -1369       C  
ATOM    825  O   GLN A 138      41.262   2.598 120.810  1.00 59.10           O  
ANISOU  825  O   GLN A 138     6717   8467   7272    -27   1043  -1288       O  
ATOM    826  CB  GLN A 138      44.006   2.228 119.657  1.00 58.06           C  
ANISOU  826  CB  GLN A 138     6402   8584   7073     14   1007  -1316       C  
ATOM    827  CG  GLN A 138      44.989   3.247 120.005  1.00 62.25           C  
ANISOU  827  CG  GLN A 138     6840   9170   7642   -136   1109  -1416       C  
ATOM    828  CD  GLN A 138      45.657   3.807 118.781  1.00 66.54           C  
ANISOU  828  CD  GLN A 138     7343   9693   8247   -116   1209  -1374       C  
ATOM    829  OE1 GLN A 138      45.030   4.518 117.984  1.00 67.98           O  
ANISOU  829  OE1 GLN A 138     7586   9726   8519    -97   1324  -1307       O  
ATOM    830  NE2 GLN A 138      46.943   3.493 118.618  1.00 67.25           N  
ANISOU  830  NE2 GLN A 138     7324   9942   8286   -113   1171  -1402       N  
ATOM    831  N   GLU A 139      42.582   3.076 122.562  1.00 62.83           N  
ANISOU  831  N   GLU A 139     7070   9122   7680   -233   1046  -1485       N  
ATOM    832  CA  GLU A 139      41.623   3.864 123.294  1.00 65.22           C  
ANISOU  832  CA  GLU A 139     7434   9308   8039   -323   1137  -1529       C  
ATOM    833  C   GLU A 139      41.219   5.171 122.584  1.00 66.38           C  
ANISOU  833  C   GLU A 139     7618   9277   8325   -370   1320  -1514       C  
ATOM    834  O   GLU A 139      40.235   5.764 122.950  1.00 66.76           O  
ANISOU  834  O   GLU A 139     7734   9198   8433   -404   1404  -1516       O  
ATOM    835  CB  GLU A 139      41.989   4.002 124.824  1.00 66.55           C  
ANISOU  835  CB  GLU A 139     7555   9596   8134   -457   1113  -1667       C  
ATOM    836  CG  GLU A 139      43.509   4.261 125.311  1.00 70.91           C  
ANISOU  836  CG  GLU A 139     7977  10337   8630   -574   1102  -1796       C  
ATOM    837  CD  GLU A 139      44.644   3.285 124.770  1.00 71.43           C  
ANISOU  837  CD  GLU A 139     7952  10573   8615   -475    980  -1747       C  
ATOM    838  OE1 GLU A 139      44.935   2.224 125.402  1.00 69.32           O  
ANISOU  838  OE1 GLU A 139     7650  10461   8226   -412    838  -1734       O  
ATOM    839  OE2 GLU A 139      45.276   3.637 123.736  1.00 70.10           O  
ANISOU  839  OE2 GLU A 139     7744  10384   8507   -462   1040  -1722       O  
ATOM    840  N   ASP A 140      41.933   5.597 121.547  1.00 67.92           N  
ANISOU  840  N   ASP A 140     7774   9460   8574   -357   1389  -1485       N  
ATOM    841  CA  ASP A 140      41.474   6.753 120.762  1.00 69.64           C  
ANISOU  841  CA  ASP A 140     8036   9500   8925   -370   1567  -1436       C  
ATOM    842  C   ASP A 140      42.032   6.754 119.334  1.00 70.70           C  
ANISOU  842  C   ASP A 140     8143   9636   9085   -278   1597  -1339       C  
ATOM    843  O   ASP A 140      43.119   6.230 119.072  1.00 71.52           O  
ANISOU  843  O   ASP A 140     8168   9880   9127   -263   1525  -1357       O  
ATOM    844  CB  ASP A 140      41.831   8.082 121.458  1.00 71.99           C  
ANISOU  844  CB  ASP A 140     8312   9732   9310   -558   1731  -1568       C  
ATOM    845  N   ALA A 141      41.295   7.385 118.419  1.00 70.85           N  
ANISOU  845  N   ALA A 141     8221   9505   9193   -213   1712  -1231       N  
ATOM    846  CA  ALA A 141      41.577   7.288 116.994  1.00 70.23           C  
ANISOU  846  CA  ALA A 141     8133   9431   9121    -94   1731  -1114       C  
ATOM    847  C   ALA A 141      42.546   8.332 116.480  1.00 71.63           C  
ANISOU  847  C   ALA A 141     8253   9578   9385   -175   1893  -1131       C  
ATOM    848  O   ALA A 141      42.345   8.879 115.392  1.00 72.03           O  
ANISOU  848  O   ALA A 141     8327   9542   9498   -103   2005  -1017       O  
ATOM    849  CB  ALA A 141      40.279   7.357 116.215  1.00 69.71           C  
ANISOU  849  CB  ALA A 141     8150   9249   9087     34   1761   -974       C  
ATOM    850  N   THR A 142      43.586   8.625 117.250  1.00 72.50           N  
ANISOU  850  N   THR A 142     8284   9765   9498   -327   1912  -1268       N  
ATOM    851  CA  THR A 142      44.623   9.538 116.770  1.00 74.26           C  
ANISOU  851  CA  THR A 142     8436   9974   9804   -419   2060  -1293       C  
ATOM    852  C   THR A 142      45.736   8.761 116.074  1.00 73.53           C  
ANISOU  852  C   THR A 142     8254  10056   9628   -346   1965  -1263       C  
ATOM    853  O   THR A 142      46.013   7.609 116.425  1.00 72.89           O  
ANISOU  853  O   THR A 142     8141  10129   9424   -288   1786  -1289       O  
ATOM    854  CB  THR A 142      45.233  10.398 117.921  1.00 76.51           C  
ANISOU  854  CB  THR A 142     8668  10254  10149   -646   2149  -1473       C  
ATOM    855  OG1 THR A 142      45.916   9.551 118.869  1.00 76.64           O  
ANISOU  855  OG1 THR A 142     8605  10473  10041   -698   1981  -1589       O  
ATOM    856  CG2 THR A 142      44.131  11.249 118.633  1.00 76.88           C  
ANISOU  856  CG2 THR A 142     8812  10113  10287   -720   2265  -1513       C  
ATOM    857  N   GLY A 143      46.366   9.381 115.081  1.00 73.55           N  
ANISOU  857  N   GLY A 143     8218  10032   9697   -341   2094  -1202       N  
ATOM    858  CA  GLY A 143      47.501   8.751 114.390  1.00 72.26           C  
ANISOU  858  CA  GLY A 143     7960  10035   9461   -276   2029  -1175       C  
ATOM    859  C   GLY A 143      47.127   7.770 113.296  1.00 70.19           C  
ANISOU  859  C   GLY A 143     7744   9818   9108    -57   1926  -1037       C  
ATOM    860  O   GLY A 143      45.997   7.743 112.820  1.00 69.39           O  
ANISOU  860  O   GLY A 143     7741   9609   9013     48   1932   -939       O  
ATOM    861  N   GLU A 144      48.078   6.948 112.882  1.00 69.37           N  
ANISOU  861  N   GLU A 144     7563   9880   8913     16   1832  -1033       N  
ATOM    862  CA  GLU A 144      47.852   6.139 111.690  1.00 67.27           C  
ANISOU  862  CA  GLU A 144     7339   9653   8568    218   1764   -911       C  
ATOM    863  C   GLU A 144      47.555   4.682 112.019  1.00 64.97           C  
ANISOU  863  C   GLU A 144     7080   9455   8150    328   1554   -928       C  
ATOM    864  O   GLU A 144      47.030   3.925 111.184  1.00 63.72           O  
ANISOU  864  O   GLU A 144     6986   9300   7925    489   1480   -845       O  
ATOM    865  CB  GLU A 144      49.027   6.292 110.719  1.00 68.09           C  
ANISOU  865  CB  GLU A 144     7354   9851   8668    253   1838   -866       C  
ATOM    866  N   ALA A 145      47.856   4.309 113.256  1.00 63.75           N  
ANISOU  866  N   ALA A 145     6884   9373   7964    238   1464  -1037       N  
ATOM    867  CA  ALA A 145      47.722   2.935 113.702  1.00 62.27           C  
ANISOU  867  CA  ALA A 145     6718   9278   7665    332   1277  -1054       C  
ATOM    868  C   ALA A 145      46.285   2.357 113.637  1.00 61.06           C  
ANISOU  868  C   ALA A 145     6693   9017   7490    426   1199   -998       C  
ATOM    869  O   ALA A 145      46.096   1.147 113.573  1.00 59.85           O  
ANISOU  869  O   ALA A 145     6575   8913   7252    541   1060   -980       O  
ATOM    870  CB  ALA A 145      48.292   2.800 115.082  1.00 62.23           C  
ANISOU  870  CB  ALA A 145     6638   9374   7631    211   1215  -1171       C  
ATOM    871  N   CYS A 146      45.278   3.209 113.644  1.00 60.83           N  
ANISOU  871  N   CYS A 146     6731   8840   7543    378   1293   -968       N  
ATOM    872  CA  CYS A 146      43.928   2.707 113.665  1.00 61.28           C  
ANISOU  872  CA  CYS A 146     6891   8811   7582    451   1220   -919       C  
ATOM    873  C   CYS A 146      43.286   2.785 112.284  1.00 60.35           C  
ANISOU  873  C   CYS A 146     6829   8635   7468    580   1259   -801       C  
ATOM    874  O   CYS A 146      42.078   2.596 112.131  1.00 60.87           O  
ANISOU  874  O   CYS A 146     6970   8623   7533    635   1225   -749       O  
ATOM    875  CB  CYS A 146      43.104   3.443 114.739  1.00 62.03           C  
ANISOU  875  CB  CYS A 146     7021   8797   7748    327   1277   -965       C  
ATOM    876  SG  CYS A 146      43.246   5.235 114.578  1.00 68.99           S  
ANISOU  876  SG  CYS A 146     7883   9558   8772    201   1513   -967       S  
ATOM    877  N   TRP A 147      44.099   3.033 111.266  1.00 60.08           N  
ANISOU  877  N   TRP A 147     6749   8653   7426    632   1326   -757       N  
ATOM    878  CA  TRP A 147      43.605   3.036 109.886  1.00 58.41           C  
ANISOU  878  CA  TRP A 147     6581   8420   7191    768   1355   -643       C  
ATOM    879  C   TRP A 147      44.035   1.813 109.057  1.00 57.12           C  
ANISOU  879  C   TRP A 147     6420   8374   6910    915   1234   -629       C  
ATOM    880  O   TRP A 147      45.145   1.296 109.215  1.00 56.63           O  
ANISOU  880  O   TRP A 147     6296   8418   6804    917   1190   -683       O  
ATOM    881  CB  TRP A 147      44.000   4.332 109.208  1.00 59.26           C  
ANISOU  881  CB  TRP A 147     6654   8480   7381    735   1547   -579       C  
ATOM    882  CG  TRP A 147      43.330   5.518 109.823  1.00 59.35           C  
ANISOU  882  CG  TRP A 147     6692   8345   7515    621   1680   -575       C  
ATOM    883  CD1 TRP A 147      43.789   6.278 110.855  1.00 60.34           C  
ANISOU  883  CD1 TRP A 147     6776   8424   7726    452   1763   -669       C  
ATOM    884  CD2 TRP A 147      42.078   6.087 109.433  1.00 58.55           C  
ANISOU  884  CD2 TRP A 147     6661   8125   7460    672   1749   -476       C  
ATOM    885  NE1 TRP A 147      42.912   7.298 111.127  1.00 59.58           N  
ANISOU  885  NE1 TRP A 147     6731   8171   7735    395   1891   -639       N  
ATOM    886  CE2 TRP A 147      41.853   7.204 110.260  1.00 60.45           C  
ANISOU  886  CE2 TRP A 147     6908   8237   7825    534   1887   -511       C  
ATOM    887  CE3 TRP A 147      41.124   5.765 108.456  1.00 56.98           C  
ANISOU  887  CE3 TRP A 147     6517   7928   7207    821   1710   -362       C  
ATOM    888  CZ2 TRP A 147      40.705   7.995 110.143  1.00 59.28           C  
ANISOU  888  CZ2 TRP A 147     6820   7950   7753    556   1992   -425       C  
ATOM    889  CZ3 TRP A 147      40.010   6.561 108.328  1.00 55.65           C  
ANISOU  889  CZ3 TRP A 147     6395   7644   7107    839   1806   -273       C  
ATOM    890  CH2 TRP A 147      39.804   7.652 109.166  1.00 56.50           C  
ANISOU  890  CH2 TRP A 147     6510   7614   7344    714   1947   -299       C  
ATOM    891  N   TRP A 148      43.141   1.355 108.185  1.00 55.10           N  
ANISOU  891  N   TRP A 148     6232   8102   6601   1036   1182   -561       N  
ATOM    892  CA  TRP A 148      43.381   0.147 107.435  1.00 54.47           C  
ANISOU  892  CA  TRP A 148     6173   8115   6409   1171   1064   -565       C  
ATOM    893  C   TRP A 148      42.925   0.371 106.021  1.00 54.90           C  
ANISOU  893  C   TRP A 148     6258   8182   6421   1289   1110   -468       C  
ATOM    894  O   TRP A 148      41.779   0.797 105.822  1.00 54.13           O  
ANISOU  894  O   TRP A 148     6206   8013   6348   1298   1132   -406       O  
ATOM    895  CB  TRP A 148      42.601  -1.023 108.029  1.00 53.56           C  
ANISOU  895  CB  TRP A 148     6122   7977   6250   1193    903   -615       C  
ATOM    896  CG  TRP A 148      42.944  -1.323 109.446  1.00 53.49           C  
ANISOU  896  CG  TRP A 148     6089   7967   6268   1093    849   -697       C  
ATOM    897  CD1 TRP A 148      42.412  -0.729 110.576  1.00 52.77           C  
ANISOU  897  CD1 TRP A 148     6000   7799   6250    968    879   -723       C  
ATOM    898  CD2 TRP A 148      43.908  -2.273 109.908  1.00 52.97           C  
ANISOU  898  CD2 TRP A 148     5988   7990   6148   1116    761   -761       C  
ATOM    899  NE1 TRP A 148      42.995  -1.259 111.704  1.00 52.73           N  
ANISOU  899  NE1 TRP A 148     5962   7843   6230    909    810   -800       N  
ATOM    900  CE2 TRP A 148      43.914  -2.210 111.326  1.00 52.36           C  
ANISOU  900  CE2 TRP A 148     5890   7899   6107   1002    736   -818       C  
ATOM    901  CE3 TRP A 148      44.765  -3.179 109.266  1.00 53.12           C  
ANISOU  901  CE3 TRP A 148     5991   8104   6087   1231    705   -771       C  
ATOM    902  CZ2 TRP A 148      44.736  -3.023 112.109  1.00 50.86           C  
ANISOU  902  CZ2 TRP A 148     5657   7796   5871   1005    652   -874       C  
ATOM    903  CZ3 TRP A 148      45.594  -3.992 110.052  1.00 53.11           C  
ANISOU  903  CZ3 TRP A 148     5951   8177   6052   1237    628   -827       C  
ATOM    904  CH2 TRP A 148      45.566  -3.904 111.461  1.00 52.48           C  
ANISOU  904  CH2 TRP A 148     5845   8091   6006   1125    601   -872       C  
ATOM    905  N   THR A 149      43.797   0.091 105.037  1.00 55.01           N  
ANISOU  905  N   THR A 149     6242   8297   6362   1387   1125   -448       N  
ATOM    906  CA  THR A 149      43.376   0.174 103.631  1.00 55.91           C  
ANISOU  906  CA  THR A 149     6387   8452   6406   1516   1155   -359       C  
ATOM    907  C   THR A 149      42.829  -1.153 103.163  1.00 54.57           C  
ANISOU  907  C   THR A 149     6283   8328   6122   1625    995   -400       C  
ATOM    908  O   THR A 149      43.259  -2.201 103.626  1.00 54.50           O  
ANISOU  908  O   THR A 149     6284   8345   6079   1633    887   -489       O  
ATOM    909  CB  THR A 149      44.478   0.657 102.672  1.00 56.88           C  
ANISOU  909  CB  THR A 149     6448   8661   6501   1574   1273   -302       C  
ATOM    910  OG1 THR A 149      45.724   0.040 103.028  1.00 62.98           O  
ANISOU  910  OG1 THR A 149     7166   9513   7252   1565   1235   -383       O  
ATOM    911  CG2 THR A 149      44.656   2.152 102.781  1.00 58.46           C  
ANISOU  911  CG2 THR A 149     6602   8792   6819   1482   1460   -227       C  
ATOM    912  N   MET A 150      41.848  -1.096 102.272  1.00 54.54           N  
ANISOU  912  N   MET A 150     6323   8333   6065   1704    983   -336       N  
ATOM    913  CA  MET A 150      41.226  -2.289 101.735  1.00 54.25           C  
ANISOU  913  CA  MET A 150     6349   8340   5921   1795    837   -383       C  
ATOM    914  C   MET A 150      41.697  -2.549 100.307  1.00 55.78           C  
ANISOU  914  C   MET A 150     6544   8659   5991   1937    851   -356       C  
ATOM    915  O   MET A 150      41.646  -1.652  99.456  1.00 56.10           O  
ANISOU  915  O   MET A 150     6559   8745   6013   1987    962   -249       O  
ATOM    916  CB  MET A 150      39.721  -2.120 101.720  1.00 53.48           C  
ANISOU  916  CB  MET A 150     6292   8192   5835   1783    796   -342       C  
ATOM    917  CG  MET A 150      39.069  -1.927 103.098  1.00 52.91           C  
ANISOU  917  CG  MET A 150     6228   7999   5876   1654    776   -368       C  
ATOM    918  SD  MET A 150      37.360  -1.456 102.841  1.00 54.19           S  
ANISOU  918  SD  MET A 150     6413   8126   6050   1661    770   -283       S  
ATOM    919  CE  MET A 150      37.544   0.251 102.288  1.00 52.60           C  
ANISOU  919  CE  MET A 150     6163   7916   5907   1679    981   -133       C  
ATOM    920  N   HIS A 151      42.114  -3.786 100.039  1.00 56.29           N  
ANISOU  920  N   HIS A 151     6642   8778   5968   2008    745   -450       N  
ATOM    921  CA  HIS A 151      42.549  -4.168  98.704  1.00 57.92           C  
ANISOU  921  CA  HIS A 151     6858   9108   6042   2147    750   -445       C  
ATOM    922  C   HIS A 151      41.833  -5.395  98.181  1.00 58.35           C  
ANISOU  922  C   HIS A 151     6991   9189   5990   2218    604   -533       C  
ATOM    923  O   HIS A 151      41.546  -6.325  98.941  1.00 58.13           O  
ANISOU  923  O   HIS A 151     7010   9086   5992   2173    493   -628       O  
ATOM    924  CB  HIS A 151      44.065  -4.346  98.679  1.00 57.95           C  
ANISOU  924  CB  HIS A 151     6812   9171   6036   2182    805   -472       C  
ATOM    925  CG  HIS A 151      44.788  -3.107  99.063  1.00 59.21           C  
ANISOU  925  CG  HIS A 151     6885   9316   6295   2103    955   -393       C  
ATOM    926  ND1 HIS A 151      45.270  -2.897 100.335  1.00 61.38           N  
ANISOU  926  ND1 HIS A 151     7116   9524   6683   1979    968   -430       N  
ATOM    927  CD2 HIS A 151      45.021  -1.963  98.377  1.00 62.02           C  
ANISOU  927  CD2 HIS A 151     7193   9709   6662   2120   1105   -277       C  
ATOM    928  CE1 HIS A 151      45.827  -1.698 100.400  1.00 62.39           C  
ANISOU  928  CE1 HIS A 151     7169   9648   6887   1915   1117   -357       C  
ATOM    929  NE2 HIS A 151      45.679  -1.106  99.228  1.00 62.54           N  
ANISOU  929  NE2 HIS A 151     7188   9719   6855   1998   1208   -258       N  
ATOM    930  N   PRO A 152      41.551  -5.400  96.874  1.00 59.76           N  
ANISOU  930  N   PRO A 152     7186   9479   6042   2329    608   -503       N  
ATOM    931  CA  PRO A 152      40.840  -6.462  96.177  1.00 60.79           C  
ANISOU  931  CA  PRO A 152     7386   9658   6054   2395    479   -593       C  
ATOM    932  C   PRO A 152      41.648  -7.727  96.201  1.00 61.73           C  
ANISOU  932  C   PRO A 152     7551   9774   6130   2446    411   -724       C  
ATOM    933  O   PRO A 152      42.861  -7.670  96.060  1.00 62.61           O  
ANISOU  933  O   PRO A 152     7628   9930   6230   2499    485   -716       O  
ATOM    934  CB  PRO A 152      40.749  -5.931  94.751  1.00 62.04           C  
ANISOU  934  CB  PRO A 152     7526   9969   6078   2512    540   -512       C  
ATOM    935  CG  PRO A 152      41.888  -4.946  94.638  1.00 61.94           C  
ANISOU  935  CG  PRO A 152     7443   9987   6105   2533    704   -406       C  
ATOM    936  CD  PRO A 152      41.925  -4.301  95.964  1.00 60.71           C  
ANISOU  936  CD  PRO A 152     7251   9692   6122   2394    751   -373       C  
ATOM    937  N   ALA A 153      40.992  -8.861  96.396  1.00 62.41           N  
ANISOU  937  N   ALA A 153     7711   9802   6198   2430    278   -840       N  
ATOM    938  CA  ALA A 153      41.710 -10.110  96.560  1.00 63.31           C  
ANISOU  938  CA  ALA A 153     7879   9880   6294   2475    221   -962       C  
ATOM    939  C   ALA A 153      41.769 -10.891  95.270  1.00 65.44           C  
ANISOU  939  C   ALA A 153     8206  10250   6408   2598    182  -1050       C  
ATOM    940  O   ALA A 153      42.210 -12.035  95.269  1.00 66.35           O  
ANISOU  940  O   ALA A 153     8385  10327   6500   2648    131  -1165       O  
ATOM    941  CB  ALA A 153      41.095 -10.936  97.639  1.00 62.46           C  
ANISOU  941  CB  ALA A 153     7825   9628   6279   2383    118  -1039       C  
ATOM    942  N   SER A 154      41.325 -10.273  94.178  1.00 67.09           N  
ANISOU  942  N   SER A 154     8395  10589   6508   2653    211   -993       N  
ATOM    943  CA  SER A 154      41.437 -10.851  92.841  1.00 69.39           C  
ANISOU  943  CA  SER A 154     8729  11010   6624   2778    188  -1068       C  
ATOM    944  C   SER A 154      41.342  -9.754  91.792  1.00 70.98           C  
ANISOU  944  C   SER A 154     8871  11377   6722   2849    276   -940       C  
ATOM    945  O   SER A 154      41.081  -8.587  92.101  1.00 70.54           O  
ANISOU  945  O   SER A 154     8747  11314   6739   2797    351   -796       O  
ATOM    946  CB  SER A 154      40.362 -11.923  92.584  1.00 69.86           C  
ANISOU  946  CB  SER A 154     8874  11042   6626   2752     44  -1214       C  
ATOM    947  OG  SER A 154      39.124 -11.330  92.176  1.00 70.96           O  
ANISOU  947  OG  SER A 154     8985  11257   6720   2714      5  -1157       O  
ATOM    948  N   LYS A 155      41.548 -10.143  90.536  1.00 73.62           N  
ANISOU  948  N   LYS A 155     9234  11858   6881   2973    273   -993       N  
ATOM    949  CA  LYS A 155      41.440  -9.224  89.413  1.00 75.24           C  
ANISOU  949  CA  LYS A 155     9389  12243   6958   3063    352   -871       C  
ATOM    950  C   LYS A 155      39.962  -8.869  89.149  1.00 75.84           C  
ANISOU  950  C   LYS A 155     9455  12372   6990   3020    277   -832       C  
ATOM    951  O   LYS A 155      39.675  -7.982  88.343  1.00 76.51           O  
ANISOU  951  O   LYS A 155     9488  12600   6982   3087    341   -701       O  
ATOM    952  CB  LYS A 155      42.136  -9.824  88.173  1.00 76.51           C  
ANISOU  952  CB  LYS A 155     9584  12556   6929   3215    368   -950       C  
ATOM    953  N   GLN A 156      39.035  -9.553  89.834  1.00 75.99           N  
ANISOU  953  N   GLN A 156     9516  12279   7077   2913    147   -935       N  
ATOM    954  CA  GLN A 156      37.586  -9.258  89.711  1.00 77.01           C  
ANISOU  954  CA  GLN A 156     9622  12456   7182   2859     69   -901       C  
ATOM    955  C   GLN A 156      37.146  -7.938  90.352  1.00 75.19           C  
ANISOU  955  C   GLN A 156     9314  12175   7078   2798    153   -711       C  
ATOM    956  O   GLN A 156      36.002  -7.550  90.201  1.00 75.70           O  
ANISOU  956  O   GLN A 156     9346  12295   7121   2774    110   -652       O  
ATOM    957  CB  GLN A 156      36.686 -10.427  90.194  1.00 77.25           C  
ANISOU  957  CB  GLN A 156     9716  12388   7245   2757    -92  -1074       C  
ATOM    958  CG  GLN A 156      36.185 -11.365  89.043  1.00 82.27           C  
ANISOU  958  CG  GLN A 156    10403  13169   7689   2811   -205  -1232       C  
ATOM    959  CD  GLN A 156      35.227 -10.658  88.019  1.00 88.64           C  
ANISOU  959  CD  GLN A 156    11141  14199   8338   2864   -226  -1142       C  
ATOM    960  OE1 GLN A 156      34.281  -9.941  88.414  1.00 89.56           O  
ANISOU  960  OE1 GLN A 156    11194  14314   8521   2801   -236  -1027       O  
ATOM    961  NE2 GLN A 156      35.475 -10.871  86.707  1.00 88.93           N  
ANISOU  961  NE2 GLN A 156    11190  14437   8161   2987   -230  -1192       N  
ATOM    962  N   ARG A 157      38.056  -7.252  91.039  1.00 73.62           N  
ANISOU  962  N   ARG A 157     9084  11879   7007   2775    277   -619       N  
ATOM    963  CA  ARG A 157      37.790  -5.952  91.655  1.00 72.35           C  
ANISOU  963  CA  ARG A 157     8859  11655   6977   2717    382   -448       C  
ATOM    964  C   ARG A 157      38.994  -5.051  91.450  1.00 72.96           C  
ANISOU  964  C   ARG A 157     8889  11753   7079   2773    554   -330       C  
ATOM    965  O   ARG A 157      40.102  -5.553  91.323  1.00 73.96           O  
ANISOU  965  O   ARG A 157     9032  11890   7180   2815    576   -398       O  
ATOM    966  CB  ARG A 157      37.581  -6.130  93.156  1.00 70.31           C  
ANISOU  966  CB  ARG A 157     8612  11196   6904   2570    344   -493       C  
ATOM    967  CG  ARG A 157      36.403  -6.982  93.549  1.00 67.96           C  
ANISOU  967  CG  ARG A 157     8356  10849   6617   2493    189   -600       C  
ATOM    968  CD  ARG A 157      35.064  -6.311  93.257  1.00 66.13           C  
ANISOU  968  CD  ARG A 157     8078  10686   6361   2485    171   -500       C  
ATOM    969  NE  ARG A 157      34.003  -7.137  93.822  1.00 65.66           N  
ANISOU  969  NE  ARG A 157     8047  10559   6340   2388     28   -606       N  
ATOM    970  CZ  ARG A 157      33.228  -7.962  93.124  1.00 66.27           C  
ANISOU  970  CZ  ARG A 157     8147  10736   6298   2402   -101   -710       C  
ATOM    971  NH1 ARG A 157      33.343  -8.055  91.807  1.00 67.10           N  
ANISOU  971  NH1 ARG A 157     8248  11028   6220   2517   -112   -722       N  
ATOM    972  NH2 ARG A 157      32.322  -8.692  93.748  1.00 64.94           N  
ANISOU  972  NH2 ARG A 157     8000  10485   6189   2295   -217   -804       N  
ATOM    973  N   SER A 158      38.803  -3.735  91.457  1.00 73.15           N  
ANISOU  973  N   SER A 158     8854  11774   7165   2770    682   -152       N  
ATOM    974  CA  SER A 158      39.907  -2.794  91.203  1.00 73.83           C  
ANISOU  974  CA  SER A 158     8890  11877   7283   2814    862    -29       C  
ATOM    975  C   SER A 158      39.856  -1.612  92.155  1.00 72.98           C  
ANISOU  975  C   SER A 158     8739  11624   7367   2709    984     89       C  
ATOM    976  O   SER A 158      38.785  -1.297  92.645  1.00 72.88           O  
ANISOU  976  O   SER A 158     8727  11545   7419   2649    951    124       O  
ATOM    977  CB  SER A 158      39.836  -2.267  89.756  1.00 75.75           C  
ANISOU  977  CB  SER A 158     9108  12313   7360   2966    936     96       C  
ATOM    978  OG  SER A 158      39.288  -3.219  88.844  1.00 76.98           O  
ANISOU  978  OG  SER A 158     9305  12622   7323   3052    798     -4       O  
ATOM    979  N   GLU A 159      40.984  -0.936  92.390  1.00 73.08           N  
ANISOU  979  N   GLU A 159     8709  11590   7467   2685   1131    148       N  
ATOM    980  CA  GLU A 159      40.991   0.307  93.181  1.00 73.38           C  
ANISOU  980  CA  GLU A 159     8706  11492   7684   2585   1273    260       C  
ATOM    981  C   GLU A 159      39.883   1.235  92.681  1.00 72.98           C  
ANISOU  981  C   GLU A 159     8644  11465   7621   2636   1337    421       C  
ATOM    982  O   GLU A 159      39.673   1.329  91.477  1.00 74.07           O  
ANISOU  982  O   GLU A 159     8775  11757   7610   2773   1355    507       O  
ATOM    983  CB  GLU A 159      42.345   1.033  93.138  1.00 74.35           C  
ANISOU  983  CB  GLU A 159     8773  11602   7873   2573   1446    323       C  
ATOM    984  CG  GLU A 159      43.534   0.263  93.814  1.00 80.26           C  
ANISOU  984  CG  GLU A 159     9511  12324   8661   2512   1400    178       C  
ATOM    985  CD  GLU A 159      43.880   0.711  95.281  1.00 86.35           C  
ANISOU  985  CD  GLU A 159    10251  12934   9625   2337   1440    138       C  
ATOM    986  OE1 GLU A 159      43.939   1.954  95.547  1.00 87.40           O  
ANISOU  986  OE1 GLU A 159    10343  12985   9879   2268   1597    245       O  
ATOM    987  OE2 GLU A 159      44.133  -0.191  96.150  1.00 86.47           O  
ANISOU  987  OE2 GLU A 159    10281  12908   9665   2273   1321     -2       O  
ATOM    988  N   GLY A 160      39.149   1.861  93.616  1.00 71.22           N  
ANISOU  988  N   GLY A 160     8418  11099   7545   2534   1365    460       N  
ATOM    989  CA  GLY A 160      38.089   2.816  93.309  1.00 69.98           C  
ANISOU  989  CA  GLY A 160     8245  10940   7404   2579   1441    624       C  
ATOM    990  C   GLY A 160      36.717   2.236  93.022  1.00 69.47           C  
ANISOU  990  C   GLY A 160     8197  10960   7237   2626   1285    605       C  
ATOM    991  O   GLY A 160      35.747   2.997  92.830  1.00 69.31           O  
ANISOU  991  O   GLY A 160     8155  10948   7232   2668   1338    745       O  
ATOM    992  N   GLU A 161      36.629   0.906  92.956  1.00 68.37           N  
ANISOU  992  N   GLU A 161     8094  10889   6996   2622   1099    437       N  
ATOM    993  CA  GLU A 161      35.335   0.219  92.868  1.00 68.85           C  
ANISOU  993  CA  GLU A 161     8168  11011   6980   2628    934    381       C  
ATOM    994  C   GLU A 161      34.706   0.037  94.255  1.00 66.71           C  
ANISOU  994  C   GLU A 161     7914  10570   6864   2480    870    307       C  
ATOM    995  O   GLU A 161      35.410   0.021  95.279  1.00 66.51           O  
ANISOU  995  O   GLU A 161     7903  10399   6968   2373    903    240       O  
ATOM    996  CB  GLU A 161      35.486  -1.142  92.199  1.00 69.46           C  
ANISOU  996  CB  GLU A 161     8284  11218   6890   2677    772    222       C  
ATOM    997  CG  GLU A 161      35.289  -1.085  90.699  1.00 75.55           C  
ANISOU  997  CG  GLU A 161     9035  12214   7456   2835    771    295       C  
ATOM    998  CD  GLU A 161      35.669  -2.378  89.974  1.00 80.60           C  
ANISOU  998  CD  GLU A 161     9720  12979   7927   2889    640    124       C  
ATOM    999  OE1 GLU A 161      35.547  -3.484  90.566  1.00 81.54           O  
ANISOU  999  OE1 GLU A 161     9889  13022   8072   2804    501    -57       O  
ATOM   1000  OE2 GLU A 161      36.082  -2.271  88.795  1.00 82.87           O  
ANISOU 1000  OE2 GLU A 161     9996  13437   8053   3022    685    175       O  
ATOM   1001  N   LYS A 162      33.391  -0.121  94.292  1.00 65.49           N  
ANISOU 1001  N   LYS A 162     7749  10447   6687   2474    776    319       N  
ATOM   1002  CA  LYS A 162      32.676  -0.351  95.563  1.00 62.84           C  
ANISOU 1002  CA  LYS A 162     7426   9965   6485   2342    710    253       C  
ATOM   1003  C   LYS A 162      32.985  -1.746  96.127  1.00 61.52           C  
ANISOU 1003  C   LYS A 162     7313   9750   6312   2260    556     50       C  
ATOM   1004  O   LYS A 162      33.027  -2.726  95.371  1.00 61.74           O  
ANISOU 1004  O   LYS A 162     7365   9891   6203   2313    441    -49       O  
ATOM   1005  CB  LYS A 162      31.173  -0.219  95.349  1.00 62.32           C  
ANISOU 1005  CB  LYS A 162     7323   9970   6384   2367    646    322       C  
ATOM   1006  CG  LYS A 162      30.718   1.131  94.845  1.00 62.45           C  
ANISOU 1006  CG  LYS A 162     7285  10031   6412   2461    797    538       C  
ATOM   1007  CD  LYS A 162      29.209   1.114  94.814  1.00 64.66           C  
ANISOU 1007  CD  LYS A 162     7520  10380   6667   2473    713    588       C  
ATOM   1008  CE  LYS A 162      28.655   1.919  93.682  1.00 69.51           C  
ANISOU 1008  CE  LYS A 162     8072  11164   7173   2630    783    779       C  
ATOM   1009  NZ  LYS A 162      28.335   3.262  94.200  1.00 73.13           N  
ANISOU 1009  NZ  LYS A 162     8505  11497   7783   2640    965    957       N  
ATOM   1010  N   VAL A 163      33.228  -1.827  97.436  1.00 59.81           N  
ANISOU 1010  N   VAL A 163     7116   9368   6241   2137    563    -12       N  
ATOM   1011  CA  VAL A 163      33.349  -3.113  98.103  1.00 59.32           C  
ANISOU 1011  CA  VAL A 163     7104   9245   6189   2060    424   -180       C  
ATOM   1012  C   VAL A 163      31.972  -3.769  98.177  1.00 59.95           C  
ANISOU 1012  C   VAL A 163     7189   9345   6245   2026    285   -225       C  
ATOM   1013  O   VAL A 163      30.997  -3.148  98.589  1.00 60.83           O  
ANISOU 1013  O   VAL A 163     7266   9423   6424   1990    310   -142       O  
ATOM   1014  CB  VAL A 163      33.935  -2.975  99.502  1.00 58.02           C  
ANISOU 1014  CB  VAL A 163     6951   8919   6175   1945    470   -219       C  
ATOM   1015  CG1 VAL A 163      34.108  -4.324 100.135  1.00 56.90           C  
ANISOU 1015  CG1 VAL A 163     6861   8722   6036   1887    335   -373       C  
ATOM   1016  CG2 VAL A 163      35.271  -2.273  99.460  1.00 58.71           C  
ANISOU 1016  CG2 VAL A 163     7018   8995   6294   1962    608   -178       C  
ATOM   1017  N   ARG A 164      31.888  -5.015  97.748  1.00 60.79           N  
ANISOU 1017  N   ARG A 164     7336   9506   6257   2037    146   -358       N  
ATOM   1018  CA  ARG A 164      30.632  -5.724  97.742  1.00 61.74           C  
ANISOU 1018  CA  ARG A 164     7456   9652   6350   1993     11   -418       C  
ATOM   1019  C   ARG A 164      30.567  -6.673  98.929  1.00 61.10           C  
ANISOU 1019  C   ARG A 164     7426   9418   6373   1873    -70   -538       C  
ATOM   1020  O   ARG A 164      31.543  -7.355  99.269  1.00 61.17           O  
ANISOU 1020  O   ARG A 164     7489   9357   6398   1862    -82   -630       O  
ATOM   1021  CB  ARG A 164      30.432  -6.470  96.423  1.00 63.39           C  
ANISOU 1021  CB  ARG A 164     7675  10028   6382   2074    -90   -494       C  
ATOM   1022  CG  ARG A 164      30.008  -5.557  95.281  1.00 67.13           C  
ANISOU 1022  CG  ARG A 164     8083  10684   6741   2188    -37   -357       C  
ATOM   1023  CD  ARG A 164      30.277  -6.122  93.911  1.00 76.36           C  
ANISOU 1023  CD  ARG A 164     9264  12034   7713   2293    -97   -425       C  
ATOM   1024  NE  ARG A 164      29.883  -5.193  92.831  1.00 85.42           N  
ANISOU 1024  NE  ARG A 164    10342  13373   8740   2415    -38   -272       N  
ATOM   1025  CZ  ARG A 164      30.598  -4.134  92.395  1.00 87.58           C  
ANISOU 1025  CZ  ARG A 164    10590  13685   9000   2513    117   -120       C  
ATOM   1026  NH1 ARG A 164      31.792  -3.813  92.939  1.00 83.73           N  
ANISOU 1026  NH1 ARG A 164    10133  13065   8614   2496    232   -107       N  
ATOM   1027  NH2 ARG A 164      30.101  -3.374  91.401  1.00 88.08           N  
ANISOU 1027  NH2 ARG A 164    10590  13930   8945   2631    161     27       N  
ATOM   1028  N   VAL A 165      29.418  -6.681  99.590  1.00 60.54           N  
ANISOU 1028  N   VAL A 165     7332   9296   6374   1790   -116   -522       N  
ATOM   1029  CA  VAL A 165      29.155  -7.670 100.613  1.00 59.43           C  
ANISOU 1029  CA  VAL A 165     7238   9026   6318   1680   -203   -627       C  
ATOM   1030  C   VAL A 165      29.469  -9.011  99.981  1.00 60.32           C  
ANISOU 1030  C   VAL A 165     7412   9167   6338   1701   -315   -780       C  
ATOM   1031  O   VAL A 165      29.015  -9.288  98.866  1.00 61.63           O  
ANISOU 1031  O   VAL A 165     7565   9468   6382   1753   -380   -815       O  
ATOM   1032  CB  VAL A 165      27.675  -7.633 101.049  1.00 58.92           C  
ANISOU 1032  CB  VAL A 165     7130   8951   6306   1603   -257   -595       C  
ATOM   1033  CG1 VAL A 165      27.363  -8.839 101.895  1.00 57.53           C  
ANISOU 1033  CG1 VAL A 165     7005   8657   6197   1497   -357   -713       C  
ATOM   1034  CG2 VAL A 165      27.363  -6.321 101.810  1.00 57.64           C  
ANISOU 1034  CG2 VAL A 165     6916   8734   6249   1582   -133   -451       C  
ATOM   1035  N   GLY A 166      30.257  -9.821 100.675  1.00 59.71           N  
ANISOU 1035  N   GLY A 166     7402   8971   6316   1667   -332   -870       N  
ATOM   1036  CA  GLY A 166      30.694 -11.115 100.146  1.00 60.28           C  
ANISOU 1036  CA  GLY A 166     7546   9040   6317   1696   -417  -1017       C  
ATOM   1037  C   GLY A 166      32.146 -11.130  99.668  1.00 60.31           C  
ANISOU 1037  C   GLY A 166     7578   9077   6260   1798   -354  -1036       C  
ATOM   1038  O   GLY A 166      32.736 -12.195  99.561  1.00 61.00           O  
ANISOU 1038  O   GLY A 166     7735   9120   6324   1823   -399  -1151       O  
ATOM   1039  N   ASP A 167      32.728  -9.966  99.369  1.00 59.61           N  
ANISOU 1039  N   ASP A 167     7436   9061   6152   1861   -242   -921       N  
ATOM   1040  CA  ASP A 167      34.078  -9.915  98.781  1.00 59.82           C  
ANISOU 1040  CA  ASP A 167     7474   9143   6111   1962   -176   -930       C  
ATOM   1041  C   ASP A 167      35.217 -10.352  99.745  1.00 59.44           C  
ANISOU 1041  C   ASP A 167     7457   8981   6145   1944   -147   -970       C  
ATOM   1042  O   ASP A 167      35.329  -9.845 100.865  1.00 58.39           O  
ANISOU 1042  O   ASP A 167     7298   8763   6126   1869    -99   -913       O  
ATOM   1043  CB  ASP A 167      34.388  -8.511  98.262  1.00 59.29           C  
ANISOU 1043  CB  ASP A 167     7336   9173   6017   2023    -50   -786       C  
ATOM   1044  CG  ASP A 167      33.623  -8.156  96.987  1.00 61.25           C  
ANISOU 1044  CG  ASP A 167     7554   9583   6136   2097    -68   -740       C  
ATOM   1045  OD1 ASP A 167      32.765  -8.953  96.505  1.00 62.43           O  
ANISOU 1045  OD1 ASP A 167     7727   9783   6212   2088   -187   -829       O  
ATOM   1046  OD2 ASP A 167      33.868  -7.038  96.469  1.00 60.46           O  
ANISOU 1046  OD2 ASP A 167     7400   9564   6007   2162     43   -610       O  
ATOM   1047  N   ASP A 168      36.072 -11.279  99.296  1.00 60.07           N  
ANISOU 1047  N   ASP A 168     7590   9072   6162   2018   -172  -1067       N  
ATOM   1048  CA  ASP A 168      37.327 -11.553 100.002  1.00 59.31           C  
ANISOU 1048  CA  ASP A 168     7502   8914   6120   2035   -127  -1081       C  
ATOM   1049  C   ASP A 168      38.163 -10.289  99.892  1.00 58.05           C  
ANISOU 1049  C   ASP A 168     7263   8829   5964   2066      1   -969       C  
ATOM   1050  O   ASP A 168      38.204  -9.672  98.822  1.00 58.88           O  
ANISOU 1050  O   ASP A 168     7340   9052   5982   2137     51   -918       O  
ATOM   1051  CB  ASP A 168      38.084 -12.686  99.332  1.00 60.40           C  
ANISOU 1051  CB  ASP A 168     7705   9070   6175   2136   -162  -1194       C  
ATOM   1052  CG  ASP A 168      37.393 -14.028  99.471  1.00 64.01           C  
ANISOU 1052  CG  ASP A 168     8251   9426   6643   2102   -274  -1320       C  
ATOM   1053  OD1 ASP A 168      36.656 -14.231 100.461  1.00 65.38           O  
ANISOU 1053  OD1 ASP A 168     8436   9488   6918   1996   -319  -1314       O  
ATOM   1054  OD2 ASP A 168      37.630 -14.913  98.602  1.00 70.30           O  
ANISOU 1054  OD2 ASP A 168     9112  10250   7350   2180   -311  -1429       O  
ATOM   1055  N   LEU A 169      38.806  -9.876 100.973  1.00 55.89           N  
ANISOU 1055  N   LEU A 169     6952   8494   5789   2010     57   -927       N  
ATOM   1056  CA  LEU A 169      39.697  -8.748 100.850  1.00 55.42           C  
ANISOU 1056  CA  LEU A 169     6818   8500   5740   2028    183   -838       C  
ATOM   1057  C   LEU A 169      40.928  -8.808 101.699  1.00 54.22           C  
ANISOU 1057  C   LEU A 169     6631   8325   5645   2012    225   -848       C  
ATOM   1058  O   LEU A 169      41.041  -9.629 102.599  1.00 53.89           O  
ANISOU 1058  O   LEU A 169     6620   8209   5648   1980    161   -906       O  
ATOM   1059  CB  LEU A 169      38.971  -7.434 101.110  1.00 55.88           C  
ANISOU 1059  CB  LEU A 169     6824   8543   5863   1952    256   -730       C  
ATOM   1060  CG  LEU A 169      37.863  -7.390 102.124  1.00 55.92           C  
ANISOU 1060  CG  LEU A 169     6843   8444   5960   1841    207   -726       C  
ATOM   1061  CD1 LEU A 169      38.504  -7.392 103.449  1.00 58.84           C  
ANISOU 1061  CD1 LEU A 169     7195   8737   6423   1762    226   -743       C  
ATOM   1062  CD2 LEU A 169      37.109  -6.117 101.896  1.00 57.02           C  
ANISOU 1062  CD2 LEU A 169     6938   8598   6127   1816    289   -614       C  
ATOM   1063  N   ILE A 170      41.846  -7.907 101.383  1.00 53.57           N  
ANISOU 1063  N   ILE A 170     6477   8317   5558   2037    339   -784       N  
ATOM   1064  CA  ILE A 170      43.127  -7.818 102.050  1.00 53.12           C  
ANISOU 1064  CA  ILE A 170     6362   8277   5544   2023    391   -788       C  
ATOM   1065  C   ILE A 170      43.106  -6.536 102.842  1.00 51.98           C  
ANISOU 1065  C   ILE A 170     6148   8099   5501   1903    483   -718       C  
ATOM   1066  O   ILE A 170      42.687  -5.500 102.314  1.00 53.04           O  
ANISOU 1066  O   ILE A 170     6261   8247   5646   1889    566   -639       O  
ATOM   1067  CB  ILE A 170      44.287  -7.780 100.991  1.00 54.37           C  
ANISOU 1067  CB  ILE A 170     6483   8557   5618   2142    463   -776       C  
ATOM   1068  CG1 ILE A 170      44.364  -9.105 100.243  1.00 54.45           C  
ANISOU 1068  CG1 ILE A 170     6570   8593   5526   2265    378   -864       C  
ATOM   1069  CG2 ILE A 170      45.636  -7.446 101.623  1.00 54.29           C  
ANISOU 1069  CG2 ILE A 170     6382   8589   5657   2117    535   -763       C  
ATOM   1070  CD1 ILE A 170      44.910 -10.239 101.070  1.00 57.09           C  
ANISOU 1070  CD1 ILE A 170     6931   8874   5886   2280    308   -940       C  
ATOM   1071  N   LEU A 171      43.537  -6.583 104.094  1.00 50.42           N  
ANISOU 1071  N   LEU A 171     5918   7861   5377   1819    473   -744       N  
ATOM   1072  CA  LEU A 171      43.549  -5.372 104.881  1.00 50.58           C  
ANISOU 1072  CA  LEU A 171     5876   7848   5492   1694    563   -699       C  
ATOM   1073  C   LEU A 171      44.950  -5.034 105.295  1.00 50.73           C  
ANISOU 1073  C   LEU A 171     5804   7938   5534   1667    631   -708       C  
ATOM   1074  O   LEU A 171      45.639  -5.881 105.871  1.00 50.64           O  
ANISOU 1074  O   LEU A 171     5779   7959   5504   1689    566   -762       O  
ATOM   1075  CB  LEU A 171      42.608  -5.478 106.112  1.00 49.89           C  
ANISOU 1075  CB  LEU A 171     5823   7657   5475   1587    502   -721       C  
ATOM   1076  CG  LEU A 171      41.107  -5.596 105.795  1.00 50.44           C  
ANISOU 1076  CG  LEU A 171     5963   7660   5542   1588    449   -701       C  
ATOM   1077  CD1 LEU A 171      40.308  -6.058 107.018  1.00 50.43           C  
ANISOU 1077  CD1 LEU A 171     5999   7567   5596   1503    370   -735       C  
ATOM   1078  CD2 LEU A 171      40.525  -4.296 105.186  1.00 50.40           C  
ANISOU 1078  CD2 LEU A 171     5936   7650   5564   1572    558   -611       C  
ATOM   1079  N   VAL A 172      45.361  -3.799 105.010  1.00 51.11           N  
ANISOU 1079  N   VAL A 172     5784   8010   5624   1620    765   -651       N  
ATOM   1080  CA  VAL A 172      46.722  -3.373 105.263  1.00 52.52           C  
ANISOU 1080  CA  VAL A 172     5859   8268   5826   1584    843   -659       C  
ATOM   1081  C   VAL A 172      46.767  -2.251 106.271  1.00 53.16           C  
ANISOU 1081  C   VAL A 172     5883   8300   6016   1419    926   -659       C  
ATOM   1082  O   VAL A 172      46.084  -1.240 106.091  1.00 53.95           O  
ANISOU 1082  O   VAL A 172     5998   8323   6176   1363   1017   -605       O  
ATOM   1083  CB  VAL A 172      47.449  -2.880 103.959  1.00 53.78           C  
ANISOU 1083  CB  VAL A 172     5975   8515   5945   1669    953   -596       C  
ATOM   1084  CG1 VAL A 172      48.811  -2.245 104.299  1.00 53.62           C  
ANISOU 1084  CG1 VAL A 172     5830   8572   5971   1599   1052   -600       C  
ATOM   1085  CG2 VAL A 172      47.616  -4.007 102.965  1.00 52.46           C  
ANISOU 1085  CG2 VAL A 172     5857   8418   5658   1835    880   -613       C  
ATOM   1086  N   SER A 173      47.609  -2.412 107.289  1.00 53.42           N  
ANISOU 1086  N   SER A 173     5845   8384   6069   1347    903   -721       N  
ATOM   1087  CA  SER A 173      47.811  -1.406 108.299  1.00 54.29           C  
ANISOU 1087  CA  SER A 173     5890   8468   6271   1181    977   -748       C  
ATOM   1088  C   SER A 173      48.416  -0.178 107.680  1.00 56.01           C  
ANISOU 1088  C   SER A 173     6037   8698   6545   1130   1143   -702       C  
ATOM   1089  O   SER A 173      49.438  -0.282 106.984  1.00 58.97           O  
ANISOU 1089  O   SER A 173     6346   9179   6883   1195   1182   -684       O  
ATOM   1090  CB  SER A 173      48.770  -1.930 109.344  1.00 54.53           C  
ANISOU 1090  CB  SER A 173     5840   8598   6282   1137    911   -822       C  
ATOM   1091  OG  SER A 173      49.279  -0.846 110.092  1.00 57.51           O  
ANISOU 1091  OG  SER A 173     6127   8988   6736    973   1005   -859       O  
ATOM   1092  N   VAL A 174      47.825   0.984 107.910  1.00 55.79           N  
ANISOU 1092  N   VAL A 174     6023   8563   6613   1020   1251   -678       N  
ATOM   1093  CA  VAL A 174      48.412   2.227 107.408  1.00 56.58           C  
ANISOU 1093  CA  VAL A 174     6057   8652   6789    956   1429   -632       C  
ATOM   1094  C   VAL A 174      49.743   2.550 108.140  1.00 58.77           C  
ANISOU 1094  C   VAL A 174     6204   9023   7104    831   1470   -711       C  
ATOM   1095  O   VAL A 174      50.691   3.085 107.532  1.00 60.56           O  
ANISOU 1095  O   VAL A 174     6347   9310   7354    819   1582   -681       O  
ATOM   1096  CB  VAL A 174      47.409   3.398 107.466  1.00 56.07           C  
ANISOU 1096  CB  VAL A 174     6047   8430   6827    878   1550   -581       C  
ATOM   1097  CG1 VAL A 174      48.076   4.727 107.188  1.00 54.97           C  
ANISOU 1097  CG1 VAL A 174     5840   8256   6792    782   1748   -547       C  
ATOM   1098  CG2 VAL A 174      46.276   3.162 106.469  1.00 54.36           C  
ANISOU 1098  CG2 VAL A 174     5929   8165   6562   1020   1526   -481       C  
ATOM   1099  N   SER A 175      49.838   2.179 109.413  1.00 58.33           N  
ANISOU 1099  N   SER A 175     6123   8995   7043    742   1377   -808       N  
ATOM   1100  CA  SER A 175      50.981   2.562 110.211  1.00 60.04           C  
ANISOU 1100  CA  SER A 175     6210   9311   7292    606   1409   -893       C  
ATOM   1101  C   SER A 175      52.218   1.683 109.952  1.00 61.51           C  
ANISOU 1101  C   SER A 175     6298   9684   7390    697   1339   -903       C  
ATOM   1102  O   SER A 175      53.327   2.185 109.920  1.00 62.77           O  
ANISOU 1102  O   SER A 175     6332   9941   7578    624   1418   -926       O  
ATOM   1103  CB  SER A 175      50.629   2.535 111.698  1.00 59.48           C  
ANISOU 1103  CB  SER A 175     6142   9224   7235    479   1337   -992       C  
ATOM   1104  OG  SER A 175      50.442   1.198 112.142  1.00 58.86           O  
ANISOU 1104  OG  SER A 175     6098   9212   7055    582   1164  -1008       O  
ATOM   1105  N   SER A 176      52.018   0.379 109.783  1.00 61.15           N  
ANISOU 1105  N   SER A 176     6307   9683   7243    854   1198   -889       N  
ATOM   1106  CA  SER A 176      53.115  -0.558 109.771  1.00 61.80           C  
ANISOU 1106  CA  SER A 176     6304   9935   7242    947   1120   -906       C  
ATOM   1107  C   SER A 176      53.260  -1.218 108.398  1.00 63.11           C  
ANISOU 1107  C   SER A 176     6512  10129   7339   1140   1118   -832       C  
ATOM   1108  O   SER A 176      54.222  -1.943 108.134  1.00 63.87           O  
ANISOU 1108  O   SER A 176     6539  10361   7368   1242   1081   -832       O  
ATOM   1109  CB  SER A 176      52.845  -1.631 110.806  1.00 60.92           C  
ANISOU 1109  CB  SER A 176     6224   9852   7070    979    961   -954       C  
ATOM   1110  OG  SER A 176      51.969  -2.609 110.267  1.00 58.79           O  
ANISOU 1110  OG  SER A 176     6089   9501   6746   1131    875   -913       O  
ATOM   1111  N   GLU A 177      52.277  -0.995 107.535  1.00 63.48           N  
ANISOU 1111  N   GLU A 177     6671  10055   7393   1197   1156   -771       N  
ATOM   1112  CA  GLU A 177      52.280  -1.551 106.185  1.00 64.33           C  
ANISOU 1112  CA  GLU A 177     6831  10189   7424   1374   1157   -709       C  
ATOM   1113  C   GLU A 177      52.133  -3.072 106.114  1.00 63.33           C  
ANISOU 1113  C   GLU A 177     6774  10093   7197   1529   1007   -735       C  
ATOM   1114  O   GLU A 177      52.132  -3.631 105.035  1.00 64.66           O  
ANISOU 1114  O   GLU A 177     6991  10284   7291   1677    999   -704       O  
ATOM   1115  CB  GLU A 177      53.475  -1.033 105.359  1.00 65.85           C  
ANISOU 1115  CB  GLU A 177     6911  10494   7616   1397   1282   -666       C  
ATOM   1116  CG  GLU A 177      53.622   0.508 105.383  1.00 70.88           C  
ANISOU 1116  CG  GLU A 177     7484  11079   8369   1236   1451   -636       C  
ATOM   1117  CD  GLU A 177      54.292   1.122 104.128  1.00 77.83           C  
ANISOU 1117  CD  GLU A 177     8309  12013   9251   1291   1602   -548       C  
ATOM   1118  OE1 GLU A 177      55.340   0.588 103.647  1.00 78.58           O  
ANISOU 1118  OE1 GLU A 177     8324  12253   9281   1385   1600   -543       O  
ATOM   1119  OE2 GLU A 177      53.763   2.159 103.638  1.00 79.37           O  
ANISOU 1119  OE2 GLU A 177     8540  12103   9514   1244   1731   -476       O  
ATOM   1120  N   ARG A 178      51.965  -3.749 107.238  1.00 62.12           N  
ANISOU 1120  N   ARG A 178     6633   9931   7039   1498    894   -792       N  
ATOM   1121  CA  ARG A 178      51.655  -5.181 107.201  1.00 61.39           C  
ANISOU 1121  CA  ARG A 178     6628   9826   6870   1639    762   -812       C  
ATOM   1122  C   ARG A 178      50.155  -5.513 107.005  1.00 59.60           C  
ANISOU 1122  C   ARG A 178     6552   9453   6642   1659    700   -806       C  
ATOM   1123  O   ARG A 178      49.266  -4.644 107.044  1.00 59.09           O  
ANISOU 1123  O   ARG A 178     6522   9294   6634   1565    747   -783       O  
ATOM   1124  CB  ARG A 178      52.237  -5.880 108.432  1.00 61.87           C  
ANISOU 1124  CB  ARG A 178     6632   9959   6919   1623    674   -857       C  
ATOM   1125  CG  ARG A 178      53.395  -5.089 108.967  1.00 66.88           C  
ANISOU 1125  CG  ARG A 178     7102  10724   7584   1517    743   -873       C  
ATOM   1126  CD  ARG A 178      54.550  -5.821 109.647  1.00 72.16           C  
ANISOU 1126  CD  ARG A 178     7659  11554   8205   1567    682   -895       C  
ATOM   1127  NE  ARG A 178      55.667  -4.868 109.687  1.00 76.47           N  
ANISOU 1127  NE  ARG A 178     8039  12235   8783   1467    780   -903       N  
ATOM   1128  CZ  ARG A 178      56.765  -4.976 110.433  1.00 80.38           C  
ANISOU 1128  CZ  ARG A 178     8383  12902   9256   1437    758   -930       C  
ATOM   1129  NH1 ARG A 178      57.710  -4.040 110.358  1.00 82.06           N  
ANISOU 1129  NH1 ARG A 178     8443  13228   9506   1330    857   -943       N  
ATOM   1130  NH2 ARG A 178      56.937  -6.007 111.251  1.00 81.49           N  
ANISOU 1130  NH2 ARG A 178     8517  13107   9337   1512    642   -940       N  
ATOM   1131  N   TYR A 179      49.893  -6.795 106.786  1.00 58.35           N  
ANISOU 1131  N   TYR A 179     6478   9274   6420   1785    597   -828       N  
ATOM   1132  CA  TYR A 179      48.583  -7.293 106.450  1.00 56.17           C  
ANISOU 1132  CA  TYR A 179     6334   8878   6130   1819    530   -832       C  
ATOM   1133  C   TYR A 179      47.918  -7.752 107.722  1.00 55.19           C  
ANISOU 1133  C   TYR A 179     6251   8674   6045   1745    440   -862       C  
ATOM   1134  O   TYR A 179      48.559  -8.360 108.574  1.00 55.69           O  
ANISOU 1134  O   TYR A 179     6275   8783   6100   1756    390   -885       O  
ATOM   1135  CB  TYR A 179      48.730  -8.490 105.532  1.00 55.75           C  
ANISOU 1135  CB  TYR A 179     6350   8842   5990   1987    474   -856       C  
ATOM   1136  CG  TYR A 179      49.381  -8.170 104.208  1.00 57.83           C  
ANISOU 1136  CG  TYR A 179     6581   9197   6195   2082    559   -827       C  
ATOM   1137  CD1 TYR A 179      50.671  -8.656 103.865  1.00 55.58           C  
ANISOU 1137  CD1 TYR A 179     6232   9027   5858   2192    584   -835       C  
ATOM   1138  CD2 TYR A 179      48.707  -7.393 103.269  1.00 58.02           C  
ANISOU 1138  CD2 TYR A 179     6636   9202   6208   2074    620   -783       C  
ATOM   1139  CE1 TYR A 179      51.244  -8.348 102.631  1.00 54.33           C  
ANISOU 1139  CE1 TYR A 179     6044   8958   5641   2281    670   -804       C  
ATOM   1140  CE2 TYR A 179      49.273  -7.109 102.023  1.00 56.89           C  
ANISOU 1140  CE2 TYR A 179     6465   9151   5999   2170    703   -747       C  
ATOM   1141  CZ  TYR A 179      50.535  -7.578 101.714  1.00 58.31           C  
ANISOU 1141  CZ  TYR A 179     6584   9440   6130   2269    730   -759       C  
ATOM   1142  OH  TYR A 179      51.022  -7.234 100.455  1.00 60.67           O  
ANISOU 1142  OH  TYR A 179     6858   9832   6361   2362    821   -716       O  
ATOM   1143  N   LEU A 180      46.629  -7.463 107.862  1.00 53.54           N  
ANISOU 1143  N   LEU A 180     6116   8354   5874   1677    421   -854       N  
ATOM   1144  CA  LEU A 180      45.840  -8.105 108.907  1.00 51.91           C  
ANISOU 1144  CA  LEU A 180     5969   8061   5693   1631    329   -878       C  
ATOM   1145  C   LEU A 180      45.868  -9.595 108.592  1.00 51.48           C  
ANISOU 1145  C   LEU A 180     5992   7986   5583   1762    236   -908       C  
ATOM   1146  O   LEU A 180      45.500 -10.004 107.499  1.00 51.10           O  
ANISOU 1146  O   LEU A 180     6010   7914   5492   1847    222   -918       O  
ATOM   1147  CB  LEU A 180      44.395  -7.579 108.958  1.00 50.48           C  
ANISOU 1147  CB  LEU A 180     5852   7769   5560   1549    330   -859       C  
ATOM   1148  CG  LEU A 180      43.548  -8.211 110.070  1.00 49.76           C  
ANISOU 1148  CG  LEU A 180     5816   7590   5499   1495    243   -877       C  
ATOM   1149  CD1 LEU A 180      44.093  -7.799 111.435  1.00 45.00           C  
ANISOU 1149  CD1 LEU A 180     5140   7028   4930   1395    260   -888       C  
ATOM   1150  CD2 LEU A 180      42.060  -7.839 109.936  1.00 52.08           C  
ANISOU 1150  CD2 LEU A 180     6173   7783   5832   1438    238   -855       C  
ATOM   1151  N   HIS A 181      46.299 -10.388 109.558  1.00 51.15           N  
ANISOU 1151  N   HIS A 181     5942   7954   5541   1779    177   -923       N  
ATOM   1152  CA  HIS A 181      46.784 -11.722 109.256  1.00 52.24           C  
ANISOU 1152  CA  HIS A 181     6126   8093   5630   1923    122   -945       C  
ATOM   1153  C   HIS A 181      46.370 -12.767 110.288  1.00 52.66           C  
ANISOU 1153  C   HIS A 181     6241   8064   5703   1928     37   -950       C  
ATOM   1154  O   HIS A 181      46.401 -12.501 111.489  1.00 52.34           O  
ANISOU 1154  O   HIS A 181     6153   8043   5692   1844     26   -930       O  
ATOM   1155  CB  HIS A 181      48.310 -11.680 109.163  1.00 52.32           C  
ANISOU 1155  CB  HIS A 181     6029   8250   5602   1996    167   -936       C  
ATOM   1156  CG  HIS A 181      48.945 -13.035 109.059  1.00 52.92           C  
ANISOU 1156  CG  HIS A 181     6139   8334   5634   2153    121   -948       C  
ATOM   1157  ND1 HIS A 181      49.589 -13.636 110.121  1.00 51.63           N  
ANISOU 1157  ND1 HIS A 181     5929   8217   5469   2184     84   -929       N  
ATOM   1158  CD2 HIS A 181      49.006 -13.916 108.026  1.00 48.36           C  
ANISOU 1158  CD2 HIS A 181     5643   7721   5012   2292    111   -978       C  
ATOM   1159  CE1 HIS A 181      50.023 -14.828 109.744  1.00 49.13           C  
ANISOU 1159  CE1 HIS A 181     5666   7882   5120   2343     60   -937       C  
ATOM   1160  NE2 HIS A 181      49.672 -15.022 108.485  1.00 48.89           N  
ANISOU 1160  NE2 HIS A 181     5718   7795   5065   2406     77   -975       N  
ATOM   1161  N   LEU A 182      45.994 -13.949 109.807  1.00 53.74           N  
ANISOU 1161  N   LEU A 182     6485   8109   5824   2026    -16   -978       N  
ATOM   1162  CA  LEU A 182      45.646 -15.059 110.671  1.00 54.66           C  
ANISOU 1162  CA  LEU A 182     6671   8131   5966   2048    -83   -975       C  
ATOM   1163  C   LEU A 182      46.861 -15.938 110.851  1.00 56.76           C  
ANISOU 1163  C   LEU A 182     6909   8459   6197   2188    -85   -962       C  
ATOM   1164  O   LEU A 182      47.441 -16.414 109.866  1.00 58.47           O  
ANISOU 1164  O   LEU A 182     7148   8696   6373   2313    -65   -990       O  
ATOM   1165  CB  LEU A 182      44.506 -15.883 110.061  1.00 54.35           C  
ANISOU 1165  CB  LEU A 182     6768   7939   5943   2065   -133  -1019       C  
ATOM   1166  CG  LEU A 182      44.365 -17.354 110.500  1.00 53.96           C  
ANISOU 1166  CG  LEU A 182     6814   7770   5916   2140   -186  -1028       C  
ATOM   1167  CD1 LEU A 182      43.965 -17.504 111.972  1.00 52.33           C  
ANISOU 1167  CD1 LEU A 182     6603   7520   5762   2063   -216   -973       C  
ATOM   1168  CD2 LEU A 182      43.377 -18.070 109.612  1.00 53.67           C  
ANISOU 1168  CD2 LEU A 182     6902   7601   5890   2150   -222  -1097       C  
ATOM   1169  N   SER A 183      47.235 -16.186 112.098  1.00 57.83           N  
ANISOU 1169  N   SER A 183     6999   8631   6344   2179   -107   -917       N  
ATOM   1170  CA  SER A 183      48.438 -16.968 112.376  1.00 60.10           C  
ANISOU 1170  CA  SER A 183     7240   9000   6595   2321   -107   -886       C  
ATOM   1171  C   SER A 183      48.211 -18.332 113.033  1.00 61.83           C  
ANISOU 1171  C   SER A 183     7551   9105   6836   2409   -153   -855       C  
ATOM   1172  O   SER A 183      47.197 -18.570 113.671  1.00 62.21           O  
ANISOU 1172  O   SER A 183     7671   9036   6930   2331   -190   -844       O  
ATOM   1173  CB  SER A 183      49.392 -16.154 113.244  1.00 60.00           C  
ANISOU 1173  CB  SER A 183     7066   9175   6557   2270    -86   -847       C  
ATOM   1174  OG  SER A 183      50.193 -17.024 114.022  1.00 59.30           O  
ANISOU 1174  OG  SER A 183     6940   9152   6441   2383   -111   -795       O  
ATOM   1175  N   THR A 184      49.191 -19.218 112.883  1.00 64.28           N  
ANISOU 1175  N   THR A 184     7855   9452   7117   2578   -141   -833       N  
ATOM   1176  CA  THR A 184      49.273 -20.460 113.670  1.00 65.95           C  
ANISOU 1176  CA  THR A 184     8125   9585   7347   2684   -167   -776       C  
ATOM   1177  C   THR A 184      50.682 -21.072 113.758  1.00 66.55           C  
ANISOU 1177  C   THR A 184     8127   9784   7377   2869   -141   -723       C  
ATOM   1178  O   THR A 184      51.363 -20.968 114.774  1.00 66.60           O  
ANISOU 1178  O   THR A 184     8021   9933   7351   2887   -152   -648       O  
ATOM   1179  CB  THR A 184      48.294 -21.549 113.178  1.00 66.84           C  
ANISOU 1179  CB  THR A 184     8420   9459   7516   2720   -183   -819       C  
ATOM   1180  OG1 THR A 184      48.879 -22.832 113.472  1.00 70.29           O  
ANISOU 1180  OG1 THR A 184     8907   9838   7963   2892   -172   -769       O  
ATOM   1181  CG2 THR A 184      47.955 -21.414 111.641  1.00 65.88           C  
ANISOU 1181  CG2 THR A 184     8368   9279   7384   2722   -165   -924       C  
ATOM   1182  N   LEU A 189      45.158 -20.716 116.858  1.00 64.12           N  
ANISOU 1182  N   LEU A 189     8108   8957   7297   2268   -291   -681       N  
ATOM   1183  CA  LEU A 189      44.638 -19.692 115.952  1.00 62.83           C  
ANISOU 1183  CA  LEU A 189     7934   8802   7138   2158   -282   -761       C  
ATOM   1184  C   LEU A 189      44.702 -18.327 116.583  1.00 61.50           C  
ANISOU 1184  C   LEU A 189     7647   8778   6944   2027   -270   -752       C  
ATOM   1185  O   LEU A 189      44.058 -18.105 117.590  1.00 62.44           O  
ANISOU 1185  O   LEU A 189     7762   8880   7082   1931   -285   -717       O  
ATOM   1186  CB  LEU A 189      43.202 -19.989 115.544  1.00 62.09           C  
ANISOU 1186  CB  LEU A 189     7958   8521   7110   2075   -304   -804       C  
ATOM   1187  CG  LEU A 189      42.928 -20.998 114.412  1.00 64.50           C  
ANISOU 1187  CG  LEU A 189     8386   8680   7442   2157   -310   -871       C  
ATOM   1188  CD1 LEU A 189      44.157 -21.218 113.536  1.00 63.36           C  
ANISOU 1188  CD1 LEU A 189     8216   8617   7241   2306   -280   -901       C  
ATOM   1189  CD2 LEU A 189      42.441 -22.311 114.988  1.00 66.71           C  
ANISOU 1189  CD2 LEU A 189     8775   8785   7786   2195   -325   -838       C  
ATOM   1190  N   GLN A 190      45.479 -17.418 116.003  1.00 60.52           N  
ANISOU 1190  N   GLN A 190     7426   8789   6779   2021   -235   -784       N  
ATOM   1191  CA  GLN A 190      45.603 -16.064 116.520  1.00 59.32           C  
ANISOU 1191  CA  GLN A 190     7163   8763   6612   1889   -209   -789       C  
ATOM   1192  C   GLN A 190      45.587 -15.032 115.397  1.00 57.47           C  
ANISOU 1192  C   GLN A 190     6900   8554   6382   1837   -161   -842       C  
ATOM   1193  O   GLN A 190      45.414 -15.400 114.253  1.00 58.15           O  
ANISOU 1193  O   GLN A 190     7053   8571   6470   1904   -157   -873       O  
ATOM   1194  CB  GLN A 190      46.843 -15.957 117.389  1.00 60.96           C  
ANISOU 1194  CB  GLN A 190     7245   9156   6761   1926   -208   -752       C  
ATOM   1195  CG  GLN A 190      46.719 -16.771 118.692  1.00 66.41           C  
ANISOU 1195  CG  GLN A 190     7953   9840   7439   1957   -251   -682       C  
ATOM   1196  CD  GLN A 190      47.893 -16.544 119.631  1.00 73.33           C  
ANISOU 1196  CD  GLN A 190     8686  10937   8241   1980   -257   -645       C  
ATOM   1197  OE1 GLN A 190      49.037 -16.932 119.326  1.00 75.41           O  
ANISOU 1197  OE1 GLN A 190     8882  11310   8462   2107   -252   -626       O  
ATOM   1198  NE2 GLN A 190      47.622 -15.903 120.775  1.00 71.80           N  
ANISOU 1198  NE2 GLN A 190     8435  10819   8024   1857   -268   -640       N  
ATOM   1199  N   VAL A 191      45.724 -13.752 115.703  1.00 55.18           N  
ANISOU 1199  N   VAL A 191     6517   8357   6092   1718   -119   -854       N  
ATOM   1200  CA  VAL A 191      45.658 -12.730 114.672  1.00 53.86           C  
ANISOU 1200  CA  VAL A 191     6327   8202   5937   1670    -59   -886       C  
ATOM   1201  C   VAL A 191      46.847 -11.867 114.953  1.00 54.17           C  
ANISOU 1201  C   VAL A 191     6224   8409   5948   1633     -8   -892       C  
ATOM   1202  O   VAL A 191      47.176 -11.657 116.115  1.00 53.95           O  
ANISOU 1202  O   VAL A 191     6127   8464   5908   1571    -20   -885       O  
ATOM   1203  CB  VAL A 191      44.459 -11.754 114.874  1.00 53.63           C  
ANISOU 1203  CB  VAL A 191     6322   8094   5962   1522    -33   -894       C  
ATOM   1204  CG1 VAL A 191      44.094 -10.994 113.571  1.00 50.66           C  
ANISOU 1204  CG1 VAL A 191     5961   7688   5601   1511     22   -908       C  
ATOM   1205  CG2 VAL A 191      43.263 -12.462 115.472  1.00 54.79           C  
ANISOU 1205  CG2 VAL A 191     6567   8110   6142   1497    -91   -877       C  
ATOM   1206  N   ASP A 192      47.494 -11.361 113.912  1.00 53.54           N  
ANISOU 1206  N   ASP A 192     6097   8390   5857   1666     50   -906       N  
ATOM   1207  CA  ASP A 192      48.546 -10.369 114.107  1.00 54.21           C  
ANISOU 1207  CA  ASP A 192     6040   8627   5931   1602    113   -917       C  
ATOM   1208  C   ASP A 192      48.644  -9.559 112.837  1.00 53.34           C  
ANISOU 1208  C   ASP A 192     5917   8513   5835   1598    195   -923       C  
ATOM   1209  O   ASP A 192      47.820  -9.726 111.945  1.00 52.09           O  
ANISOU 1209  O   ASP A 192     5858   8248   5687   1637    194   -919       O  
ATOM   1210  CB  ASP A 192      49.881 -11.015 114.457  1.00 55.07           C  
ANISOU 1210  CB  ASP A 192     6054   8888   5982   1701     88   -903       C  
ATOM   1211  CG  ASP A 192      50.348 -12.019 113.388  1.00 59.88           C  
ANISOU 1211  CG  ASP A 192     6709   9487   6556   1885     78   -889       C  
ATOM   1212  OD1 ASP A 192      50.116 -11.795 112.166  1.00 61.72           O  
ANISOU 1212  OD1 ASP A 192     6990   9667   6795   1918    121   -902       O  
ATOM   1213  OD2 ASP A 192      50.959 -13.049 113.771  1.00 65.46           O  
ANISOU 1213  OD2 ASP A 192     7406  10243   7225   2007     33   -863       O  
ATOM   1214  N   ALA A 193      49.618  -8.660 112.779  1.00 53.51           N  
ANISOU 1214  N   ALA A 193     5814   8659   5859   1543    268   -932       N  
ATOM   1215  CA  ALA A 193      49.877  -7.928 111.557  1.00 54.09           C  
ANISOU 1215  CA  ALA A 193     5866   8744   5942   1554    359   -922       C  
ATOM   1216  C   ALA A 193      51.205  -8.479 110.981  1.00 55.98           C  
ANISOU 1216  C   ALA A 193     6028   9119   6124   1687    369   -913       C  
ATOM   1217  O   ALA A 193      52.242  -8.498 111.661  1.00 57.71           O  
ANISOU 1217  O   ALA A 193     6127   9478   6324   1675    364   -920       O  
ATOM   1218  CB  ALA A 193      49.970  -6.469 111.842  1.00 52.68           C  
ANISOU 1218  CB  ALA A 193     5608   8586   5824   1391    456   -935       C  
ATOM   1219  N   SER A 194      51.191  -8.920 109.733  1.00 56.22           N  
ANISOU 1219  N   SER A 194     6118   9122   6120   1815    383   -899       N  
ATOM   1220  CA  SER A 194      52.274  -9.746 109.242  1.00 57.02           C  
ANISOU 1220  CA  SER A 194     6178   9327   6160   1971    377   -892       C  
ATOM   1221  C   SER A 194      52.563  -9.460 107.794  1.00 57.44           C  
ANISOU 1221  C   SER A 194     6235   9406   6184   2049    455   -878       C  
ATOM   1222  O   SER A 194      51.794  -8.792 107.129  1.00 57.06           O  
ANISOU 1222  O   SER A 194     6242   9283   6156   2002    500   -868       O  
ATOM   1223  CB  SER A 194      51.889 -11.214 109.436  1.00 56.71           C  
ANISOU 1223  CB  SER A 194     6250   9208   6090   2097    278   -901       C  
ATOM   1224  OG  SER A 194      52.553 -12.047 108.533  1.00 59.93           O  
ANISOU 1224  OG  SER A 194     6676   9655   6442   2271    286   -901       O  
ATOM   1225  N   PHE A 195      53.676  -9.975 107.287  1.00 58.83           N  
ANISOU 1225  N   PHE A 195     6349   9697   6308   2181    477   -870       N  
ATOM   1226  CA  PHE A 195      53.956  -9.810 105.880  1.00 58.77           C  
ANISOU 1226  CA  PHE A 195     6352   9722   6258   2274    552   -855       C  
ATOM   1227  C   PHE A 195      53.286 -10.872 105.041  1.00 57.41           C  
ANISOU 1227  C   PHE A 195     6333   9452   6029   2415    499   -882       C  
ATOM   1228  O   PHE A 195      53.209 -10.727 103.819  1.00 57.20           O  
ANISOU 1228  O   PHE A 195     6344   9435   5955   2485    550   -878       O  
ATOM   1229  CB  PHE A 195      55.442  -9.686 105.637  1.00 60.70           C  
ANISOU 1229  CB  PHE A 195     6447  10142   6473   2337    620   -833       C  
ATOM   1230  CG  PHE A 195      55.990  -8.354 106.049  1.00 65.45           C  
ANISOU 1230  CG  PHE A 195     6901  10832   7134   2174    704   -814       C  
ATOM   1231  CD1 PHE A 195      55.470  -7.165 105.485  1.00 67.45           C  
ANISOU 1231  CD1 PHE A 195     7167  11029   7432   2067    796   -790       C  
ATOM   1232  CD2 PHE A 195      57.021  -8.260 107.015  1.00 68.83           C  
ANISOU 1232  CD2 PHE A 195     7174  11403   7574   2122    697   -819       C  
ATOM   1233  CE1 PHE A 195      55.995  -5.896 105.859  1.00 69.05           C  
ANISOU 1233  CE1 PHE A 195     7238  11293   7705   1905    892   -779       C  
ATOM   1234  CE2 PHE A 195      57.546  -6.992 107.410  1.00 69.30           C  
ANISOU 1234  CE2 PHE A 195     7092  11545   7695   1948    779   -821       C  
ATOM   1235  CZ  PHE A 195      57.034  -5.813 106.823  1.00 69.42           C  
ANISOU 1235  CZ  PHE A 195     7130  11477   7767   1836    882   -804       C  
ATOM   1236  N   MET A 196      52.783 -11.922 105.697  1.00 56.12           N  
ANISOU 1236  N   MET A 196     6259   9195   5870   2452    400   -912       N  
ATOM   1237  CA  MET A 196      51.853 -12.864 105.053  1.00 56.20           C  
ANISOU 1237  CA  MET A 196     6431   9073   5849   2536    342   -955       C  
ATOM   1238  C   MET A 196      50.423 -12.270 104.967  1.00 55.06           C  
ANISOU 1238  C   MET A 196     6366   8813   5739   2413    320   -961       C  
ATOM   1239  O   MET A 196      49.918 -11.686 105.946  1.00 53.73           O  
ANISOU 1239  O   MET A 196     6174   8605   5637   2273    304   -943       O  
ATOM   1240  CB  MET A 196      51.832 -14.203 105.792  1.00 56.22           C  
ANISOU 1240  CB  MET A 196     6501   9003   5858   2615    258   -979       C  
ATOM   1241  CG  MET A 196      53.085 -15.110 105.548  1.00 61.36           C  
ANISOU 1241  CG  MET A 196     7114   9740   6459   2797    278   -977       C  
ATOM   1242  SD  MET A 196      53.493 -15.367 103.774  1.00 66.27           S  
ANISOU 1242  SD  MET A 196     7781  10406   6992   2957    346  -1015       S  
ATOM   1243  CE  MET A 196      54.736 -14.048 103.734  1.00 66.69           C  
ANISOU 1243  CE  MET A 196     7626  10671   7042   2906    450   -946       C  
ATOM   1244  N   GLN A 197      49.801 -12.410 103.792  1.00 54.12           N  
ANISOU 1244  N   GLN A 197     6336   8657   5570   2470    323   -987       N  
ATOM   1245  CA  GLN A 197      48.386 -12.089 103.574  1.00 52.02           C  
ANISOU 1245  CA  GLN A 197     6154   8291   5322   2385    289   -995       C  
ATOM   1246  C   GLN A 197      47.386 -13.120 104.124  1.00 52.25           C  
ANISOU 1246  C   GLN A 197     6299   8177   5378   2369    182  -1045       C  
ATOM   1247  O   GLN A 197      47.701 -14.302 104.167  1.00 52.30           O  
ANISOU 1247  O   GLN A 197     6362   8144   5364   2469    139  -1090       O  
ATOM   1248  CB  GLN A 197      48.128 -11.922 102.100  1.00 50.99           C  
ANISOU 1248  CB  GLN A 197     6065   8200   5110   2461    325  -1004       C  
ATOM   1249  CG  GLN A 197      48.859 -10.765 101.532  1.00 48.17           C  
ANISOU 1249  CG  GLN A 197     5603   7964   4736   2457    441   -936       C  
ATOM   1250  CD  GLN A 197      48.697 -10.701 100.044  1.00 48.56           C  
ANISOU 1250  CD  GLN A 197     5693   8073   4685   2557    478   -937       C  
ATOM   1251  OE1 GLN A 197      48.239 -11.673  99.401  1.00 46.53           O  
ANISOU 1251  OE1 GLN A 197     5538   7784   4356   2645    412  -1009       O  
ATOM   1252  NE2 GLN A 197      49.068  -9.553  99.461  1.00 49.16           N  
ANISOU 1252  NE2 GLN A 197     5689   8239   4751   2542    589   -859       N  
ATOM   1253  N   THR A 198      46.197 -12.639 104.551  1.00 51.56           N  
ANISOU 1253  N   THR A 198     6240   8007   5342   2245    152  -1032       N  
ATOM   1254  CA  THR A 198      45.029 -13.463 104.913  1.00 50.98           C  
ANISOU 1254  CA  THR A 198     6274   7797   5298   2209     59  -1075       C  
ATOM   1255  C   THR A 198      43.829 -12.785 104.301  1.00 51.03           C  
ANISOU 1255  C   THR A 198     6307   7781   5299   2141     56  -1066       C  
ATOM   1256  O   THR A 198      43.724 -11.546 104.326  1.00 50.29           O  
ANISOU 1256  O   THR A 198     6145   7735   5229   2068    121  -1003       O  
ATOM   1257  CB  THR A 198      44.815 -13.571 106.467  1.00 50.80           C  
ANISOU 1257  CB  THR A 198     6236   7707   5358   2113     21  -1050       C  
ATOM   1258  OG1 THR A 198      45.853 -14.377 107.042  1.00 53.36           O  
ANISOU 1258  OG1 THR A 198     6541   8055   5678   2196     11  -1053       O  
ATOM   1259  CG2 THR A 198      43.464 -14.221 106.818  1.00 48.57           C  
ANISOU 1259  CG2 THR A 198     6055   7284   5117   2054    -60  -1079       C  
ATOM   1260  N   LEU A 199      42.927 -13.588 103.729  1.00 51.83           N  
ANISOU 1260  N   LEU A 199     6507   7815   5371   2165    -14  -1128       N  
ATOM   1261  CA  LEU A 199      41.686 -13.083 103.152  1.00 51.46           C  
ANISOU 1261  CA  LEU A 199     6482   7759   5310   2106    -34  -1121       C  
ATOM   1262  C   LEU A 199      40.643 -12.908 104.262  1.00 50.95           C  
ANISOU 1262  C   LEU A 199     6424   7595   5340   1974    -75  -1095       C  
ATOM   1263  O   LEU A 199      40.461 -13.808 105.103  1.00 50.29           O  
ANISOU 1263  O   LEU A 199     6390   7413   5306   1949   -134  -1128       O  
ATOM   1264  CB  LEU A 199      41.149 -14.041 102.093  1.00 52.31           C  
ANISOU 1264  CB  LEU A 199     6681   7853   5340   2175    -99  -1214       C  
ATOM   1265  CG  LEU A 199      41.997 -14.290 100.820  1.00 56.00           C  
ANISOU 1265  CG  LEU A 199     7159   8425   5694   2316    -63  -1256       C  
ATOM   1266  CD1 LEU A 199      41.208 -15.122  99.798  1.00 55.44           C  
ANISOU 1266  CD1 LEU A 199     7181   8343   5542   2354   -135  -1362       C  
ATOM   1267  CD2 LEU A 199      42.513 -12.992 100.170  1.00 54.88           C  
ANISOU 1267  CD2 LEU A 199     6925   8421   5505   2342     37  -1167       C  
ATOM   1268  N   TRP A 200      39.971 -11.758 104.251  1.00 49.58           N  
ANISOU 1268  N   TRP A 200     6203   7446   5190   1897    -35  -1029       N  
ATOM   1269  CA  TRP A 200      38.959 -11.464 105.230  1.00 49.41           C  
ANISOU 1269  CA  TRP A 200     6179   7341   5252   1778    -59   -998       C  
ATOM   1270  C   TRP A 200      37.623 -11.174 104.566  1.00 49.72           C  
ANISOU 1270  C   TRP A 200     6235   7381   5273   1748    -89   -987       C  
ATOM   1271  O   TRP A 200      37.573 -10.629 103.459  1.00 50.97           O  
ANISOU 1271  O   TRP A 200     6374   7631   5363   1803    -55   -963       O  
ATOM   1272  CB  TRP A 200      39.396 -10.262 106.026  1.00 48.83           C  
ANISOU 1272  CB  TRP A 200     6024   7291   5239   1707     29   -925       C  
ATOM   1273  CG  TRP A 200      40.535 -10.556 106.903  1.00 48.19           C  
ANISOU 1273  CG  TRP A 200     5913   7219   5179   1713     42   -937       C  
ATOM   1274  CD1 TRP A 200      41.840 -10.351 106.623  1.00 45.86           C  
ANISOU 1274  CD1 TRP A 200     5562   7013   4849   1775     99   -932       C  
ATOM   1275  CD2 TRP A 200      40.481 -11.091 108.232  1.00 48.97           C  
ANISOU 1275  CD2 TRP A 200     6023   7250   5332   1656     -3   -947       C  
ATOM   1276  NE1 TRP A 200      42.612 -10.738 107.673  1.00 47.29           N  
ANISOU 1276  NE1 TRP A 200     5714   7197   5057   1763     87   -942       N  
ATOM   1277  CE2 TRP A 200      41.810 -11.201 108.682  1.00 48.76           C  
ANISOU 1277  CE2 TRP A 200     5944   7289   5295   1694     24   -948       C  
ATOM   1278  CE3 TRP A 200      39.436 -11.486 109.093  1.00 48.13           C  
ANISOU 1278  CE3 TRP A 200     5963   7044   5281   1578    -61   -948       C  
ATOM   1279  CZ2 TRP A 200      42.136 -11.697 109.957  1.00 48.34           C  
ANISOU 1279  CZ2 TRP A 200     5881   7215   5272   1666     -9   -948       C  
ATOM   1280  CZ3 TRP A 200      39.759 -11.972 110.360  1.00 47.15           C  
ANISOU 1280  CZ3 TRP A 200     5836   6888   5192   1548    -86   -945       C  
ATOM   1281  CH2 TRP A 200      41.101 -12.083 110.772  1.00 48.76           C  
ANISOU 1281  CH2 TRP A 200     5987   7168   5372   1596    -63   -945       C  
ATOM   1282  N   ASN A 201      36.535 -11.583 105.199  1.00 49.18           N  
ANISOU 1282  N   ASN A 201     6201   7225   5261   1667   -155  -1000       N  
ATOM   1283  CA  ASN A 201      35.222 -11.093 104.772  1.00 49.22           C  
ANISOU 1283  CA  ASN A 201     6193   7245   5263   1622   -173   -968       C  
ATOM   1284  C   ASN A 201      34.753 -10.135 105.848  1.00 47.86           C  
ANISOU 1284  C   ASN A 201     5973   7028   5185   1524   -119   -888       C  
ATOM   1285  O   ASN A 201      34.703 -10.467 107.032  1.00 47.19           O  
ANISOU 1285  O   ASN A 201     5901   6859   5171   1457   -137   -895       O  
ATOM   1286  CB  ASN A 201      34.227 -12.224 104.579  1.00 49.63           C  
ANISOU 1286  CB  ASN A 201     6308   7241   5308   1597   -284  -1047       C  
ATOM   1287  CG  ASN A 201      34.450 -13.012 103.292  1.00 54.31           C  
ANISOU 1287  CG  ASN A 201     6948   7892   5793   1688   -333  -1138       C  
ATOM   1288  OD1 ASN A 201      35.255 -12.641 102.427  1.00 60.03           O  
ANISOU 1288  OD1 ASN A 201     7655   8716   6437   1781   -283  -1130       O  
ATOM   1289  ND2 ASN A 201      33.696 -14.084 103.135  1.00 56.83           N  
ANISOU 1289  ND2 ASN A 201     7328   8152   6111   1657   -426  -1229       N  
ATOM   1290  N   MET A 202      34.523  -8.911 105.450  1.00 48.02           N  
ANISOU 1290  N   MET A 202     5938   7106   5203   1524    -39   -807       N  
ATOM   1291  CA  MET A 202      33.874  -7.928 106.307  1.00 48.75           C  
ANISOU 1291  CA  MET A 202     5989   7151   5381   1437     21   -733       C  
ATOM   1292  C   MET A 202      32.340  -8.119 106.193  1.00 47.74           C  
ANISOU 1292  C   MET A 202     5868   7005   5264   1399    -44   -720       C  
ATOM   1293  O   MET A 202      31.704  -7.531 105.330  1.00 48.00           O  
ANISOU 1293  O   MET A 202     5870   7109   5260   1435    -25   -665       O  
ATOM   1294  CB  MET A 202      34.317  -6.534 105.873  1.00 49.25           C  
ANISOU 1294  CB  MET A 202     5995   7270   5446   1463    151   -648       C  
ATOM   1295  CG  MET A 202      34.195  -5.495 106.922  1.00 53.89           C  
ANISOU 1295  CG  MET A 202     6548   7796   6134   1374    244   -594       C  
ATOM   1296  SD  MET A 202      35.036  -4.035 106.323  1.00 64.50           S  
ANISOU 1296  SD  MET A 202     7835   9189   7484   1409    407   -513       S  
ATOM   1297  CE  MET A 202      36.493  -4.248 107.304  1.00 62.73           C  
ANISOU 1297  CE  MET A 202     7596   8949   7290   1357    426   -583       C  
ATOM   1298  N   ASN A 203      31.772  -8.980 107.033  1.00 46.99           N  
ANISOU 1298  N   ASN A 203     5809   6827   5219   1330   -120   -765       N  
ATOM   1299  CA  ASN A 203      30.358  -9.341 106.935  1.00 47.39           C  
ANISOU 1299  CA  ASN A 203     5861   6864   5282   1285   -192   -766       C  
ATOM   1300  C   ASN A 203      29.379  -8.388 107.649  1.00 46.12           C  
ANISOU 1300  C   ASN A 203     5649   6675   5198   1216   -136   -678       C  
ATOM   1301  O   ASN A 203      29.566  -8.048 108.817  1.00 45.27           O  
ANISOU 1301  O   ASN A 203     5540   6498   5164   1155    -84   -656       O  
ATOM   1302  CB  ASN A 203      30.152 -10.779 107.394  1.00 47.89           C  
ANISOU 1302  CB  ASN A 203     5986   6843   5365   1244   -295   -855       C  
ATOM   1303  CG  ASN A 203      30.622 -11.778 106.361  1.00 50.54           C  
ANISOU 1303  CG  ASN A 203     6374   7211   5617   1317   -363   -950       C  
ATOM   1304  OD1 ASN A 203      30.655 -11.484 105.166  1.00 54.02           O  
ANISOU 1304  OD1 ASN A 203     6796   7757   5971   1385   -362   -954       O  
ATOM   1305  ND2 ASN A 203      30.990 -12.963 106.811  1.00 53.06           N  
ANISOU 1305  ND2 ASN A 203     6760   7440   5959   1308   -415  -1025       N  
ATOM   1306  N   PRO A 204      28.329  -7.947 106.936  1.00 46.37           N  
ANISOU 1306  N   PRO A 204     5639   6774   5208   1231   -144   -626       N  
ATOM   1307  CA  PRO A 204      27.468  -6.925 107.553  1.00 45.06           C  
ANISOU 1307  CA  PRO A 204     5420   6584   5115   1186    -69   -529       C  
ATOM   1308  C   PRO A 204      26.648  -7.552 108.678  1.00 44.33           C  
ANISOU 1308  C   PRO A 204     5341   6404   5099   1087   -121   -552       C  
ATOM   1309  O   PRO A 204      26.134  -8.680 108.527  1.00 44.52           O  
ANISOU 1309  O   PRO A 204     5390   6418   5108   1058   -231   -618       O  
ATOM   1310  CB  PRO A 204      26.588  -6.467 106.391  1.00 44.73           C  
ANISOU 1310  CB  PRO A 204     5325   6658   5013   1248    -78   -466       C  
ATOM   1311  CG  PRO A 204      26.453  -7.721 105.541  1.00 46.05           C  
ANISOU 1311  CG  PRO A 204     5521   6883   5094   1266   -214   -567       C  
ATOM   1312  CD  PRO A 204      27.795  -8.409 105.630  1.00 46.96           C  
ANISOU 1312  CD  PRO A 204     5705   6952   5187   1286   -225   -656       C  
ATOM   1313  N   ILE A 205      26.612  -6.858 109.818  1.00 43.47           N  
ANISOU 1313  N   ILE A 205     5221   6225   5070   1032    -36   -506       N  
ATOM   1314  CA  ILE A 205      25.700  -7.191 110.896  1.00 43.14           C  
ANISOU 1314  CA  ILE A 205     5178   6112   5100    944    -59   -499       C  
ATOM   1315  C   ILE A 205      24.374  -6.411 110.738  1.00 44.20           C  
ANISOU 1315  C   ILE A 205     5244   6282   5266    940    -22   -409       C  
ATOM   1316  O   ILE A 205      23.288  -6.991 110.832  1.00 43.55           O  
ANISOU 1316  O   ILE A 205     5140   6203   5202    896    -93   -409       O  
ATOM   1317  CB  ILE A 205      26.351  -6.967 112.267  1.00 42.59           C  
ANISOU 1317  CB  ILE A 205     5134   5963   5087    888      5   -508       C  
ATOM   1318  CG1 ILE A 205      27.550  -7.890 112.424  1.00 41.23           C  
ANISOU 1318  CG1 ILE A 205     5016   5772   4879    902    -47   -587       C  
ATOM   1319  CG2 ILE A 205      25.351  -7.196 113.400  1.00 40.86           C  
ANISOU 1319  CG2 ILE A 205     4909   5680   4935    804     -3   -486       C  
ATOM   1320  CD1 ILE A 205      27.209  -9.357 112.388  1.00 43.80           C  
ANISOU 1320  CD1 ILE A 205     5387   6061   5196    885   -166   -646       C  
ATOM   1321  N   CYS A 206      24.460  -5.116 110.474  1.00 42.73           N  
ANISOU 1321  N   CYS A 206     4999   5837   5401    428    387   -170       N  
ATOM   1322  CA  CYS A 206      23.244  -4.354 110.180  1.00 46.33           C  
ANISOU 1322  CA  CYS A 206     5490   6278   5837    418    385   -102       C  
ATOM   1323  C   CYS A 206      23.604  -3.079 109.475  1.00 47.73           C  
ANISOU 1323  C   CYS A 206     5648   6481   6008    393    449    -21       C  
ATOM   1324  O   CYS A 206      24.745  -2.660 109.476  1.00 48.34           O  
ANISOU 1324  O   CYS A 206     5684   6571   6113    373    493    -16       O  
ATOM   1325  CB  CYS A 206      22.466  -3.984 111.457  1.00 45.17           C  
ANISOU 1325  CB  CYS A 206     5366   6043   5753    396    348    -91       C  
ATOM   1326  SG  CYS A 206      23.471  -2.901 112.456  1.00 50.06           S  
ANISOU 1326  SG  CYS A 206     5950   6610   6462    353    381    -75       S  
ATOM   1327  N   SER A 207      22.598  -2.468 108.885  1.00 50.14           N  
ANISOU 1327  N   SER A 207     5980   6792   6280    393    451     45       N  
ATOM   1328  CA  SER A 207      22.710  -1.147 108.279  1.00 52.50           C  
ANISOU 1328  CA  SER A 207     6268   7098   6580    367    505    140       C  
ATOM   1329  C   SER A 207      21.572  -0.304 108.886  1.00 54.10           C  
ANISOU 1329  C   SER A 207     6501   7222   6832    354    481    190       C  
ATOM   1330  O   SER A 207      21.076  -0.644 109.968  1.00 54.60           O  
ANISOU 1330  O   SER A 207     6581   7226   6940    355    436    145       O  
ATOM   1331  CB  SER A 207      22.600  -1.276 106.765  1.00 52.26           C  
ANISOU 1331  CB  SER A 207     6239   7169   6448    389    531    176       C  
ATOM   1332  OG  SER A 207      23.236  -0.184 106.164  1.00 51.15           O  
ANISOU 1332  OG  SER A 207     6072   7052   6310    361    595    259       O  
ATOM   1333  N   CYS A 208      21.164   0.785 108.246  1.00 56.34           N  
ANISOU 1333  N   CYS A 208     6790   7505   7110    344    510    284       N  
ATOM   1334  CA  CYS A 208      20.007   1.573 108.716  1.00 58.43           C  
ANISOU 1334  CA  CYS A 208     7082   7698   7420    340    485    330       C  
ATOM   1335  C   CYS A 208      18.783   0.700 109.132  1.00 56.75           C  
ANISOU 1335  C   CYS A 208     6901   7476   7185    369    421    280       C  
ATOM   1336  O   CYS A 208      18.232  -0.073 108.336  1.00 56.71           O  
ANISOU 1336  O   CYS A 208     6911   7535   7099    398    398    269       O  
ATOM   1337  CB  CYS A 208      19.594   2.567 107.606  1.00 60.04           C  
ANISOU 1337  CB  CYS A 208     7293   7928   7593    340    516    441       C  
ATOM   1338  SG  CYS A 208      21.017   3.594 106.986  1.00 69.94           S  
ANISOU 1338  SG  CYS A 208     8506   9200   8870    300    598    516       S  
ATOM   1339  N   CYS A 209      18.350   0.800 110.374  1.00 55.46           N  
ANISOU 1339  N   CYS A 209     6747   7237   7091    359    391    248       N  
ATOM   1340  CA  CYS A 209      17.098   0.127 110.715  1.00 55.24           C  
ANISOU 1340  CA  CYS A 209     6745   7200   7042    381    336    217       C  
ATOM   1341  C   CYS A 209      15.969   1.145 110.835  1.00 52.42           C  
ANISOU 1341  C   CYS A 209     6401   6797   6719    382    329    279       C  
ATOM   1342  O   CYS A 209      16.253   2.311 111.061  1.00 51.94           O  
ANISOU 1342  O   CYS A 209     6330   6685   6721    363    362    326       O  
ATOM   1343  CB  CYS A 209      17.249  -0.627 112.014  1.00 55.17           C  
ANISOU 1343  CB  CYS A 209     6737   7152   7075    372    303    137       C  
ATOM   1344  SG  CYS A 209      17.322   0.576 113.297  1.00 66.53           S  
ANISOU 1344  SG  CYS A 209     8166   8499   8615    341    317    149       S  
ATOM   1345  N   GLU A 210      14.717   0.701 110.666  1.00 49.65           N  
ANISOU 1345  N   GLU A 210     6070   6462   6332    406    287    277       N  
ATOM   1346  CA  GLU A 210      13.544   1.503 111.038  1.00 47.86           C  
ANISOU 1346  CA  GLU A 210     5851   6186   6147    413    272    317       C  
ATOM   1347  C   GLU A 210      13.571   1.878 112.521  1.00 44.49           C  
ANISOU 1347  C   GLU A 210     5418   5678   5807    391    269    277       C  
ATOM   1348  O   GLU A 210      13.534   1.002 113.383  1.00 41.57           O  
ANISOU 1348  O   GLU A 210     5051   5304   5439    386    241    208       O  
ATOM   1349  CB  GLU A 210      12.239   0.733 110.816  1.00 48.11           C  
ANISOU 1349  CB  GLU A 210     5898   6252   6130    438    221    301       C  
ATOM   1350  CG  GLU A 210      11.725   0.726 109.435  1.00 55.21           C  
ANISOU 1350  CG  GLU A 210     6803   7220   6953    463    215    354       C  
ATOM   1351  CD  GLU A 210      11.365   2.103 108.921  1.00 61.17           C  
ANISOU 1351  CD  GLU A 210     7556   7954   7732    471    238    452       C  
ATOM   1352  OE1 GLU A 210      10.523   2.797 109.543  1.00 62.44           O  
ANISOU 1352  OE1 GLU A 210     7715   8055   7954    476    226    472       O  
ATOM   1353  OE2 GLU A 210      11.950   2.475 107.882  1.00 64.34           O  
ANISOU 1353  OE2 GLU A 210     7955   8401   8091    473    270    510       O  
ATOM   1354  N   GLU A 211      13.594   3.177 112.797  1.00 43.22           N  
ANISOU 1354  N   GLU A 211     5249   5456   5716    380    296    322       N  
ATOM   1355  CA  GLU A 211      13.384   3.705 114.144  1.00 42.05           C  
ANISOU 1355  CA  GLU A 211     5095   5233   5648    366    292    286       C  
ATOM   1356  C   GLU A 211      12.314   2.928 114.891  1.00 40.11           C  
ANISOU 1356  C   GLU A 211     4858   4993   5387    378    247    235       C  
ATOM   1357  O   GLU A 211      11.185   2.767 114.417  1.00 38.87           O  
ANISOU 1357  O   GLU A 211     4709   4861   5197    403    222    260       O  
ATOM   1358  CB  GLU A 211      12.919   5.159 114.078  1.00 42.23           C  
ANISOU 1358  CB  GLU A 211     5113   5192   5738    369    313    349       C  
ATOM   1359  CG  GLU A 211      14.020   6.104 114.305  1.00 46.76           C  
ANISOU 1359  CG  GLU A 211     5671   5713   6381    338    354    363       C  
ATOM   1360  CD  GLU A 211      13.546   7.495 114.727  1.00 51.67           C  
ANISOU 1360  CD  GLU A 211     6288   6245   7098    338    367    395       C  
ATOM   1361  OE1 GLU A 211      12.900   8.164 113.873  1.00 53.27           O  
ANISOU 1361  OE1 GLU A 211     6497   6439   7304    360    371    476       O  
ATOM   1362  OE2 GLU A 211      13.869   7.922 115.877  1.00 48.64           O  
ANISOU 1362  OE2 GLU A 211     5894   5802   6787    316    372    338       O  
ATOM   1363  N   GLY A 212      12.663   2.479 116.079  1.00 38.68           N  
ANISOU 1363  N   GLY A 212     4674   4794   5231    359    236    167       N  
ATOM   1364  CA  GLY A 212      11.652   1.940 116.953  1.00 37.28           C  
ANISOU 1364  CA  GLY A 212     4500   4614   5050    364    200    126       C  
ATOM   1365  C   GLY A 212      11.512   0.462 116.822  1.00 36.25           C  
ANISOU 1365  C   GLY A 212     4381   4536   4855    368    165     91       C  
ATOM   1366  O   GLY A 212      10.822  -0.152 117.608  1.00 37.26           O  
ANISOU 1366  O   GLY A 212     4512   4666   4979    365    135     55       O  
ATOM   1367  N   TYR A 213      12.187  -0.148 115.869  1.00 35.51           N  
ANISOU 1367  N   TYR A 213     4292   4486   4714    374    167     97       N  
ATOM   1368  CA  TYR A 213      11.970  -1.564 115.675  1.00 34.86           C  
ANISOU 1368  CA  TYR A 213     4221   4447   4577    381    130     60       C  
ATOM   1369  C   TYR A 213      13.010  -2.437 116.308  1.00 34.01           C  
ANISOU 1369  C   TYR A 213     4112   4338   4473    366    122      4       C  
ATOM   1370  O   TYR A 213      14.185  -2.108 116.298  1.00 35.02           O  
ANISOU 1370  O   TYR A 213     4227   4459   4619    357    151      0       O  
ATOM   1371  CB  TYR A 213      11.822  -1.858 114.199  1.00 35.93           C  
ANISOU 1371  CB  TYR A 213     4364   4639   4650    404    128     90       C  
ATOM   1372  CG  TYR A 213      10.443  -1.495 113.713  1.00 34.67           C  
ANISOU 1372  CG  TYR A 213     4209   4492   4474    422    110    132       C  
ATOM   1373  CD1 TYR A 213      10.180  -0.206 113.225  1.00 34.75           C  
ANISOU 1373  CD1 TYR A 213     4212   4486   4504    433    137    199       C  
ATOM   1374  CD2 TYR A 213       9.418  -2.428 113.750  1.00 32.52           C  
ANISOU 1374  CD2 TYR A 213     3942   4242   4171    429     64    106       C  
ATOM   1375  CE1 TYR A 213       8.968   0.137 112.757  1.00 34.05           C  
ANISOU 1375  CE1 TYR A 213     4124   4411   4403    454    118    240       C  
ATOM   1376  CE2 TYR A 213       8.150  -2.102 113.297  1.00 34.50           C  
ANISOU 1376  CE2 TYR A 213     4190   4509   4408    446     45    142       C  
ATOM   1377  CZ  TYR A 213       7.936  -0.828 112.794  1.00 37.39           C  
ANISOU 1377  CZ  TYR A 213     4550   4865   4791    462     71    209       C  
ATOM   1378  OH  TYR A 213       6.680  -0.496 112.345  1.00 44.52           O  
ANISOU 1378  OH  TYR A 213     5447   5786   5684    484     49    247       O  
ATOM   1379  N   VAL A 214      12.570  -3.531 116.899  1.00 33.02           N  
ANISOU 1379  N   VAL A 214     3994   4216   4334    363     81    -36       N  
ATOM   1380  CA  VAL A 214      13.491  -4.506 117.466  1.00 33.32           C  
ANISOU 1380  CA  VAL A 214     4033   4254   4375    354     65    -84       C  
ATOM   1381  C   VAL A 214      14.351  -5.199 116.390  1.00 33.94           C  
ANISOU 1381  C   VAL A 214     4111   4370   4416    371     68    -99       C  
ATOM   1382  O   VAL A 214      13.821  -5.683 115.383  1.00 33.74           O  
ANISOU 1382  O   VAL A 214     4096   4380   4344    390     54    -94       O  
ATOM   1383  CB  VAL A 214      12.739  -5.529 118.327  1.00 32.93           C  
ANISOU 1383  CB  VAL A 214     3993   4195   4322    345     18   -113       C  
ATOM   1384  CG1 VAL A 214      13.702  -6.387 119.099  1.00 33.02           C  
ANISOU 1384  CG1 VAL A 214     4004   4197   4347    335      0   -154       C  
ATOM   1385  CG2 VAL A 214      11.821  -4.797 119.314  1.00 32.98           C  
ANISOU 1385  CG2 VAL A 214     3996   4178   4358    330     21   -100       C  
ATOM   1386  N   THR A 215      15.672  -5.204 116.584  1.00 33.91           N  
ANISOU 1386  N   THR A 215     4092   4364   4430    367     88   -120       N  
ATOM   1387  CA  THR A 215      16.557  -6.019 115.746  1.00 35.06           C  
ANISOU 1387  CA  THR A 215     4232   4546   4544    385     89   -149       C  
ATOM   1388  C   THR A 215      17.351  -7.019 116.572  1.00 35.09           C  
ANISOU 1388  C   THR A 215     4229   4533   4570    384     61   -201       C  
ATOM   1389  O   THR A 215      17.401  -6.918 117.810  1.00 35.40           O  
ANISOU 1389  O   THR A 215     4266   4537   4648    364     48   -209       O  
ATOM   1390  CB  THR A 215      17.633  -5.171 115.016  1.00 35.87           C  
ANISOU 1390  CB  THR A 215     4311   4672   4646    385    144   -125       C  
ATOM   1391  OG1 THR A 215      18.681  -4.831 115.945  1.00 38.51           O  
ANISOU 1391  OG1 THR A 215     4623   4977   5032    366    159   -143       O  
ATOM   1392  CG2 THR A 215      17.041  -3.917 114.438  1.00 34.65           C  
ANISOU 1392  CG2 THR A 215     4159   4519   4488    381    177    -60       C  
ATOM   1393  N   GLY A 216      18.064  -7.926 115.900  1.00 34.78           N  
ANISOU 1393  N   GLY A 216     4185   4522   4508    407     55   -238       N  
ATOM   1394  CA  GLY A 216      18.849  -8.901 116.627  1.00 33.84           C  
ANISOU 1394  CA  GLY A 216     4058   4384   4416    412     25   -285       C  
ATOM   1395  C   GLY A 216      20.042  -8.138 117.167  1.00 34.25           C  
ANISOU 1395  C   GLY A 216     4079   4430   4505    398     59   -283       C  
ATOM   1396  O   GLY A 216      20.368  -7.042 116.654  1.00 34.21           O  
ANISOU 1396  O   GLY A 216     4057   4441   4499    388    108   -251       O  
ATOM   1397  N   GLY A 217      20.676  -8.687 118.214  1.00 33.87           N  
ANISOU 1397  N   GLY A 217     4021   4357   4492    394     30   -313       N  
ATOM   1398  CA  GLY A 217      21.816  -8.047 118.829  1.00 34.06           C  
ANISOU 1398  CA  GLY A 217     4012   4377   4554    379     53   -318       C  
ATOM   1399  C   GLY A 217      21.516  -6.923 119.795  1.00 35.03           C  
ANISOU 1399  C   GLY A 217     4132   4472   4706    344     66   -293       C  
ATOM   1400  O   GLY A 217      22.427  -6.490 120.526  1.00 36.52           O  
ANISOU 1400  O   GLY A 217     4292   4652   4930    328     74   -306       O  
ATOM   1401  N   HIS A 218      20.248  -6.485 119.874  1.00 34.42           N  
ANISOU 1401  N   HIS A 218     4081   4379   4617    333     64   -263       N  
ATOM   1402  CA  HIS A 218      19.834  -5.485 120.827  1.00 33.26           C  
ANISOU 1402  CA  HIS A 218     3934   4206   4499    305     72   -248       C  
ATOM   1403  C   HIS A 218      19.841  -6.059 122.224  1.00 33.18           C  
ANISOU 1403  C   HIS A 218     3925   4180   4501    293     30   -274       C  
ATOM   1404  O   HIS A 218      19.505  -7.253 122.407  1.00 32.54           O  
ANISOU 1404  O   HIS A 218     3862   4101   4401    305    -12   -284       O  
ATOM   1405  CB  HIS A 218      18.457  -4.959 120.464  1.00 33.64           C  
ANISOU 1405  CB  HIS A 218     4004   4246   4530    304     80   -212       C  
ATOM   1406  CG  HIS A 218      18.489  -3.921 119.385  1.00 36.96           C  
ANISOU 1406  CG  HIS A 218     4419   4675   4951    307    127   -174       C  
ATOM   1407  ND1 HIS A 218      17.354  -3.291 118.914  1.00 38.68           N  
ANISOU 1407  ND1 HIS A 218     4653   4887   5159    311    137   -134       N  
ATOM   1408  CD2 HIS A 218      19.536  -3.361 118.726  1.00 37.24           C  
ANISOU 1408  CD2 HIS A 218     4430   4722   4997    305    168   -163       C  
ATOM   1409  CE1 HIS A 218      17.703  -2.384 118.015  1.00 40.61           C  
ANISOU 1409  CE1 HIS A 218     4885   5136   5407    312    180    -96       C  
ATOM   1410  NE2 HIS A 218      19.021  -2.413 117.880  1.00 41.41           N  
ANISOU 1410  NE2 HIS A 218     4963   5250   5520    305    201   -112       N  
ATOM   1411  N   VAL A 219      20.268  -5.225 123.189  1.00 31.71           N  
ANISOU 1411  N   VAL A 219     3721   3981   4347    269     41   -284       N  
ATOM   1412  CA  VAL A 219      20.126  -5.509 124.601  1.00 31.40           C  
ANISOU 1412  CA  VAL A 219     3683   3935   4311    253      6   -303       C  
ATOM   1413  C   VAL A 219      18.831  -4.820 125.108  1.00 31.55           C  
ANISOU 1413  C   VAL A 219     3720   3942   4327    237     12   -287       C  
ATOM   1414  O   VAL A 219      18.618  -3.636 124.842  1.00 32.62           O  
ANISOU 1414  O   VAL A 219     3848   4062   4485    229     50   -277       O  
ATOM   1415  CB  VAL A 219      21.351  -5.012 125.373  1.00 31.89           C  
ANISOU 1415  CB  VAL A 219     3712   3999   4407    236     10   -332       C  
ATOM   1416  CG1 VAL A 219      21.134  -5.196 126.865  1.00 28.21           C  
ANISOU 1416  CG1 VAL A 219     3247   3536   3934    218    -25   -350       C  
ATOM   1417  CG2 VAL A 219      22.675  -5.789 124.880  1.00 30.51           C  
ANISOU 1417  CG2 VAL A 219     3513   3842   4239    256      2   -350       C  
ATOM   1418  N   LEU A 220      17.972  -5.534 125.820  1.00 30.40           N  
ANISOU 1418  N   LEU A 220     3593   3802   4157    234    -22   -285       N  
ATOM   1419  CA  LEU A 220      16.662  -4.975 126.139  1.00 30.24           C  
ANISOU 1419  CA  LEU A 220     3584   3777   4128    224    -13   -271       C  
ATOM   1420  C   LEU A 220      16.086  -5.618 127.403  1.00 29.77           C  
ANISOU 1420  C   LEU A 220     3533   3733   4047    209    -48   -277       C  
ATOM   1421  O   LEU A 220      16.672  -6.578 127.907  1.00 29.25           O  
ANISOU 1421  O   LEU A 220     3467   3676   3969    207    -84   -284       O  
ATOM   1422  CB  LEU A 220      15.735  -5.257 124.945  1.00 30.70           C  
ANISOU 1422  CB  LEU A 220     3661   3836   4168    243     -9   -240       C  
ATOM   1423  CG  LEU A 220      15.610  -6.723 124.448  1.00 29.07           C  
ANISOU 1423  CG  LEU A 220     3472   3639   3934    258    -47   -236       C  
ATOM   1424  CD1 LEU A 220      15.046  -7.577 125.461  1.00 23.78           C  
ANISOU 1424  CD1 LEU A 220     2812   2973   3249    243    -86   -236       C  
ATOM   1425  CD2 LEU A 220      14.717  -6.857 123.248  1.00 29.41           C  
ANISOU 1425  CD2 LEU A 220     3530   3688   3957    274    -43   -213       C  
ATOM   1426  N   ARG A 221      14.926  -5.133 127.861  1.00 28.50           N  
ANISOU 1426  N   ARG A 221     3375   3576   3877    199    -39   -271       N  
ATOM   1427  CA  ARG A 221      14.158  -5.779 128.931  1.00 29.06           C  
ANISOU 1427  CA  ARG A 221     3454   3671   3918    183    -67   -267       C  
ATOM   1428  C   ARG A 221      12.802  -6.239 128.401  1.00 30.36           C  
ANISOU 1428  C   ARG A 221     3632   3839   4064    187    -73   -237       C  
ATOM   1429  O   ARG A 221      12.254  -5.589 127.488  1.00 31.92           O  
ANISOU 1429  O   ARG A 221     3831   4025   4274    202    -48   -226       O  
ATOM   1430  CB  ARG A 221      13.942  -4.855 130.113  1.00 27.52           C  
ANISOU 1430  CB  ARG A 221     3242   3491   3723    164    -50   -295       C  
ATOM   1431  CG  ARG A 221      15.196  -4.590 130.895  1.00 30.50           C  
ANISOU 1431  CG  ARG A 221     3603   3875   4109    153    -56   -329       C  
ATOM   1432  CD  ARG A 221      14.923  -3.777 132.118  1.00 33.21           C  
ANISOU 1432  CD  ARG A 221     3931   4241   4445    134    -45   -365       C  
ATOM   1433  NE  ARG A 221      16.112  -3.621 132.958  1.00 35.95           N  
ANISOU 1433  NE  ARG A 221     4260   4603   4795    121    -59   -401       N  
ATOM   1434  CZ  ARG A 221      17.037  -2.680 132.828  1.00 38.98           C  
ANISOU 1434  CZ  ARG A 221     4624   4965   5221    118    -38   -436       C  
ATOM   1435  NH1 ARG A 221      16.967  -1.775 131.872  1.00 40.80           N  
ANISOU 1435  NH1 ARG A 221     4852   5153   5498    127     -1   -433       N  
ATOM   1436  NH2 ARG A 221      18.070  -2.659 133.665  1.00 43.15           N  
ANISOU 1436  NH2 ARG A 221     5133   5516   5747    104    -59   -470       N  
ATOM   1437  N   LEU A 222      12.251  -7.311 128.995  1.00 30.61           N  
ANISOU 1437  N   LEU A 222     3674   3887   4068    173   -107   -221       N  
ATOM   1438  CA  LEU A 222      10.917  -7.849 128.663  1.00 30.62           C  
ANISOU 1438  CA  LEU A 222     3684   3896   4054    169   -118   -194       C  
ATOM   1439  C   LEU A 222       9.981  -7.611 129.857  1.00 31.91           C  
ANISOU 1439  C   LEU A 222     3837   4093   4197    145   -112   -192       C  
ATOM   1440  O   LEU A 222      10.199  -8.197 130.939  1.00 32.58           O  
ANISOU 1440  O   LEU A 222     3921   4198   4258    123   -134   -189       O  
ATOM   1441  CB  LEU A 222      11.021  -9.350 128.414  1.00 30.24           C  
ANISOU 1441  CB  LEU A 222     3654   3838   3997    166   -163   -175       C  
ATOM   1442  CG  LEU A 222      11.956  -9.754 127.259  1.00 31.78           C  
ANISOU 1442  CG  LEU A 222     3859   4007   4209    193   -171   -185       C  
ATOM   1443  CD1 LEU A 222      13.313 -10.159 127.758  1.00 26.64           C  
ANISOU 1443  CD1 LEU A 222     3205   3349   3567    196   -189   -200       C  
ATOM   1444  CD2 LEU A 222      11.329 -10.880 126.413  1.00 31.68           C  
ANISOU 1444  CD2 LEU A 222     3863   3982   4192    197   -203   -172       C  
ATOM   1445  N   PHE A 223       8.982  -6.737 129.678  1.00 31.67           N  
ANISOU 1445  N   PHE A 223     3792   4069   4171    150    -82   -195       N  
ATOM   1446  CA  PHE A 223       8.059  -6.318 130.721  1.00 32.24           C  
ANISOU 1446  CA  PHE A 223     3847   4178   4226    134    -67   -202       C  
ATOM   1447  C   PHE A 223       6.729  -7.033 130.614  1.00 34.14           C  
ANISOU 1447  C   PHE A 223     4084   4438   4448    121    -80   -171       C  
ATOM   1448  O   PHE A 223       6.170  -7.210 129.509  1.00 33.98           O  
ANISOU 1448  O   PHE A 223     4068   4402   4441    135    -85   -153       O  
ATOM   1449  CB  PHE A 223       7.798  -4.808 130.613  1.00 31.34           C  
ANISOU 1449  CB  PHE A 223     3714   4054   4140    152    -24   -231       C  
ATOM   1450  CG  PHE A 223       8.913  -3.981 131.132  1.00 33.17           C  
ANISOU 1450  CG  PHE A 223     3940   4273   4390    153     -7   -270       C  
ATOM   1451  CD1 PHE A 223       9.063  -3.782 132.488  1.00 31.48           C  
ANISOU 1451  CD1 PHE A 223     3713   4094   4153    134     -5   -302       C  
ATOM   1452  CD2 PHE A 223       9.897  -3.468 130.269  1.00 34.18           C  
ANISOU 1452  CD2 PHE A 223     4074   4359   4554    170      3   -275       C  
ATOM   1453  CE1 PHE A 223      10.123  -3.055 132.970  1.00 30.79           C  
ANISOU 1453  CE1 PHE A 223     3619   3997   4084    131      5   -344       C  
ATOM   1454  CE2 PHE A 223      10.981  -2.732 130.770  1.00 31.77           C  
ANISOU 1454  CE2 PHE A 223     3759   4041   4271    165     16   -312       C  
ATOM   1455  CZ  PHE A 223      11.078  -2.524 132.094  1.00 30.61           C  
ANISOU 1455  CZ  PHE A 223     3599   3925   4105    146     15   -349       C  
ATOM   1456  N   HIS A 224       6.186  -7.393 131.766  1.00 37.25           N  
ANISOU 1456  N   HIS A 224     4468   4876   4812     93    -84   -165       N  
ATOM   1457  CA  HIS A 224       4.918  -8.103 131.853  1.00 40.56           C  
ANISOU 1457  CA  HIS A 224     4877   5321   5213     71    -95   -133       C  
ATOM   1458  C   HIS A 224       3.923  -7.164 132.516  1.00 42.49           C  
ANISOU 1458  C   HIS A 224     5088   5608   5448     71    -56   -153       C  
ATOM   1459  O   HIS A 224       3.981  -6.932 133.710  1.00 44.36           O  
ANISOU 1459  O   HIS A 224     5313   5887   5656     54    -43   -170       O  
ATOM   1460  CB  HIS A 224       5.131  -9.390 132.658  1.00 40.26           C  
ANISOU 1460  CB  HIS A 224     4852   5300   5146     36   -130   -100       C  
ATOM   1461  CG  HIS A 224       3.870 -10.119 132.962  1.00 45.89           C  
ANISOU 1461  CG  HIS A 224     5551   6044   5841      3   -139    -63       C  
ATOM   1462  ND1 HIS A 224       3.009 -10.561 131.980  1.00 49.97           N  
ANISOU 1462  ND1 HIS A 224     6065   6543   6379      4   -152    -45       N  
ATOM   1463  CD2 HIS A 224       3.295 -10.452 134.140  1.00 50.54           C  
ANISOU 1463  CD2 HIS A 224     6124   6688   6393    -33   -135    -42       C  
ATOM   1464  CE1 HIS A 224       1.957 -11.134 132.537  1.00 50.71           C  
ANISOU 1464  CE1 HIS A 224     6140   6673   6454    -33   -155    -14       C  
ATOM   1465  NE2 HIS A 224       2.106 -11.079 133.846  1.00 53.16           N  
ANISOU 1465  NE2 HIS A 224     6442   7029   6728    -56   -143     -9       N  
ATOM   1466  N   GLY A 225       3.062  -6.541 131.737  1.00 44.71           N  
ANISOU 1466  N   GLY A 225     5353   5881   5753     93    -38   -156       N  
ATOM   1467  CA  GLY A 225       1.966  -5.690 132.305  1.00 46.95           C  
ANISOU 1467  CA  GLY A 225     5599   6205   6034     98     -3   -177       C  
ATOM   1468  C   GLY A 225       2.329  -4.315 132.861  1.00 48.37           C  
ANISOU 1468  C   GLY A 225     5764   6384   6229    120     35   -230       C  
ATOM   1469  O   GLY A 225       3.325  -3.704 132.428  1.00 50.25           O  
ANISOU 1469  O   GLY A 225     6020   6576   6498    141     40   -249       O  
ATOM   1470  N   GLU A 229       7.536  -4.533 136.222  1.00 38.43           N  
ANISOU 1470  N   GLU A 229     4556   5154   4891     64    -10   -327       N  
ATOM   1471  CA  GLU A 229       7.643  -6.026 136.214  1.00 40.27           C  
ANISOU 1471  CA  GLU A 229     4810   5396   5094     43    -52   -267       C  
ATOM   1472  C   GLU A 229       8.333  -6.679 135.010  1.00 38.60           C  
ANISOU 1472  C   GLU A 229     4624   5123   4920     58    -80   -237       C  
ATOM   1473  O   GLU A 229       7.828  -6.665 133.900  1.00 39.58           O  
ANISOU 1473  O   GLU A 229     4753   5211   5073     74    -74   -221       O  
ATOM   1474  CB  GLU A 229       6.298  -6.680 136.388  1.00 41.30           C  
ANISOU 1474  CB  GLU A 229     4933   5564   5197     23    -52   -227       C  
ATOM   1475  CG  GLU A 229       6.367  -8.083 136.949  1.00 47.75           C  
ANISOU 1475  CG  GLU A 229     5763   6405   5973    -10    -91   -170       C  
ATOM   1476  CD  GLU A 229       4.955  -8.601 137.458  1.00 58.39           C  
ANISOU 1476  CD  GLU A 229     7092   7808   7285    -41    -82   -133       C  
ATOM   1477  OE1 GLU A 229       4.421  -8.032 138.467  1.00 59.47           O  
ANISOU 1477  OE1 GLU A 229     7202   8013   7381    -53    -52   -159       O  
ATOM   1478  OE2 GLU A 229       4.403  -9.582 136.846  1.00 59.94           O  
ANISOU 1478  OE2 GLU A 229     7299   7980   7496    -55   -106    -82       O  
ATOM   1479  N   CYS A 230       9.480  -7.286 135.206  1.00 36.73           N  
ANISOU 1479  N   CYS A 230     4402   4876   4679     54   -111   -229       N  
ATOM   1480  CA  CYS A 230      10.204  -7.717 134.022  1.00 35.38           C  
ANISOU 1480  CA  CYS A 230     4248   4648   4545     74   -129   -216       C  
ATOM   1481  C   CYS A 230      10.849  -9.085 134.246  1.00 34.44           C  
ANISOU 1481  C   CYS A 230     4147   4524   4414     64   -179   -180       C  
ATOM   1482  O   CYS A 230      10.938  -9.563 135.382  1.00 33.33           O  
ANISOU 1482  O   CYS A 230     4006   4424   4236     42   -199   -165       O  
ATOM   1483  CB  CYS A 230      11.246  -6.667 133.649  1.00 34.68           C  
ANISOU 1483  CB  CYS A 230     4153   4532   4493     95   -108   -260       C  
ATOM   1484  SG  CYS A 230      12.464  -6.430 134.996  1.00 37.15           S  
ANISOU 1484  SG  CYS A 230     4452   4879   4783     80   -121   -296       S  
ATOM   1485  N   LEU A 231      11.270  -9.709 133.158  1.00 33.20           N  
ANISOU 1485  N   LEU A 231     4006   4320   4287     83   -198   -167       N  
ATOM   1486  CA  LEU A 231      11.862 -11.036 133.250  1.00 33.80           C  
ANISOU 1486  CA  LEU A 231     4099   4379   4365     80   -247   -137       C  
ATOM   1487  C   LEU A 231      13.309 -10.920 133.688  1.00 34.02           C  
ANISOU 1487  C   LEU A 231     4121   4408   4398     91   -261   -159       C  
ATOM   1488  O   LEU A 231      14.084 -10.087 133.146  1.00 34.53           O  
ANISOU 1488  O   LEU A 231     4173   4457   4488    111   -237   -197       O  
ATOM   1489  CB  LEU A 231      11.788 -11.680 131.887  1.00 33.72           C  
ANISOU 1489  CB  LEU A 231     4105   4321   4387    101   -259   -128       C  
ATOM   1490  CG  LEU A 231      12.081 -13.155 131.716  1.00 35.34           C  
ANISOU 1490  CG  LEU A 231     4329   4493   4607    101   -310    -99       C  
ATOM   1491  CD1 LEU A 231      10.836 -13.911 132.091  1.00 35.55           C  
ANISOU 1491  CD1 LEU A 231     4363   4527   4618     69   -328    -55       C  
ATOM   1492  CD2 LEU A 231      12.383 -13.378 130.231  1.00 37.49           C  
ANISOU 1492  CD2 LEU A 231     4610   4723   4912    133   -311   -120       C  
ATOM   1493  N   THR A 232      13.686 -11.733 134.663  1.00 33.52           N  
ANISOU 1493  N   THR A 232     4061   4364   4312     77   -300   -132       N  
ATOM   1494  CA  THR A 232      15.020 -11.644 135.224  1.00 33.67           C  
ANISOU 1494  CA  THR A 232     4068   4393   4331     86   -320   -152       C  
ATOM   1495  C   THR A 232      15.504 -12.950 135.841  1.00 34.70           C  
ANISOU 1495  C   THR A 232     4209   4521   4453     82   -378   -106       C  
ATOM   1496  O   THR A 232      14.732 -13.897 135.972  1.00 35.85           O  
ANISOU 1496  O   THR A 232     4373   4658   4590     66   -402    -56       O  
ATOM   1497  CB  THR A 232      15.058 -10.504 136.279  1.00 34.32           C  
ANISOU 1497  CB  THR A 232     4129   4533   4380     69   -294   -187       C  
ATOM   1498  OG1 THR A 232      16.406 -10.267 136.693  1.00 35.83           O  
ANISOU 1498  OG1 THR A 232     4303   4733   4576     78   -311   -217       O  
ATOM   1499  CG2 THR A 232      14.194 -10.806 137.459  1.00 29.38           C  
ANISOU 1499  CG2 THR A 232     3504   3962   3695     37   -302   -156       C  
ATOM   1500  N   ILE A 233      16.792 -13.031 136.155  1.00 34.49           N  
ANISOU 1500  N   ILE A 233     4170   4497   4436     98   -404   -121       N  
ATOM   1501  CA  ILE A 233      17.321 -14.101 137.036  1.00 35.32           C  
ANISOU 1501  CA  ILE A 233     4281   4613   4527     95   -463    -76       C  
ATOM   1502  C   ILE A 233      17.561 -13.468 138.410  1.00 36.84           C  
ANISOU 1502  C   ILE A 233     4454   4880   4662     73   -464    -86       C  
ATOM   1503  O   ILE A 233      17.577 -12.234 138.544  1.00 36.92           O  
ANISOU 1503  O   ILE A 233     4446   4921   4660     67   -422   -140       O  
ATOM   1504  CB  ILE A 233      18.655 -14.741 136.535  1.00 34.29           C  
ANISOU 1504  CB  ILE A 233     4144   4440   4444    133   -500    -85       C  
ATOM   1505  CG1 ILE A 233      19.804 -13.749 136.680  1.00 32.16           C  
ANISOU 1505  CG1 ILE A 233     3842   4198   4180    146   -485   -142       C  
ATOM   1506  CG2 ILE A 233      18.514 -15.201 135.088  1.00 30.67           C  
ANISOU 1506  CG2 ILE A 233     3699   3915   4038    159   -492    -94       C  
ATOM   1507  CD1 ILE A 233      21.155 -14.290 136.146  1.00 30.84           C  
ANISOU 1507  CD1 ILE A 233     3660   3997   4063    185   -515   -157       C  
ATOM   1508  N   SER A 234      17.734 -14.287 139.433  1.00 38.46           N  
ANISOU 1508  N   SER A 234     4664   5116   4832     60   -511    -34       N  
ATOM   1509  CA  SER A 234      17.894 -13.741 140.788  1.00 41.54           C  
ANISOU 1509  CA  SER A 234     5036   5591   5155     38   -515    -42       C  
ATOM   1510  C   SER A 234      19.240 -12.979 140.995  1.00 41.93           C  
ANISOU 1510  C   SER A 234     5055   5661   5214     56   -521   -105       C  
ATOM   1511  O   SER A 234      20.158 -13.041 140.186  1.00 40.52           O  
ANISOU 1511  O   SER A 234     4868   5434   5093     87   -529   -129       O  
ATOM   1512  CB  SER A 234      17.850 -14.890 141.746  1.00 41.48           C  
ANISOU 1512  CB  SER A 234     5042   5611   5109     22   -570     39       C  
ATOM   1513  OG  SER A 234      18.921 -15.740 141.320  1.00 47.23           O  
ANISOU 1513  OG  SER A 234     5772   6282   5890     57   -621     57       O  
ATOM   1514  N   ALA A 235      19.358 -12.298 142.118  1.00 45.17           N  
ANISOU 1514  N   ALA A 235     5447   6150   5565     36   -519   -131       N  
ATOM   1515  CA  ALA A 235      20.565 -11.507 142.414  1.00 47.32           C  
ANISOU 1515  CA  ALA A 235     5687   6449   5845     45   -525   -196       C  
ATOM   1516  C   ALA A 235      21.781 -12.350 142.719  1.00 49.31           C  
ANISOU 1516  C   ALA A 235     5927   6702   6107     67   -591   -167       C  
ATOM   1517  O   ALA A 235      21.666 -13.546 143.027  1.00 50.26           O  
ANISOU 1517  O   ALA A 235     6067   6817   6214     70   -638    -91       O  
ATOM   1518  CB  ALA A 235      20.278 -10.573 143.546  1.00 47.33           C  
ANISOU 1518  CB  ALA A 235     5670   6536   5777     17   -507   -240       C  
ATOM   1519  N   ALA A 236      22.960 -11.740 142.631  1.00 52.13           N  
ANISOU 1519  N   ALA A 236     6250   7064   6494     82   -597   -227       N  
ATOM   1520  CA  ALA A 236      24.215 -12.450 142.971  1.00 54.66           C  
ANISOU 1520  CA  ALA A 236     6549   7393   6826    106   -661   -207       C  
ATOM   1521  C   ALA A 236      24.159 -13.108 144.372  1.00 57.44           C  
ANISOU 1521  C   ALA A 236     6905   7820   7098     91   -718   -149       C  
ATOM   1522  O   ALA A 236      23.646 -12.506 145.351  1.00 57.67           O  
ANISOU 1522  O   ALA A 236     6932   7929   7052     58   -705   -165       O  
ATOM   1523  CB  ALA A 236      25.425 -11.547 142.823  1.00 53.87           C  
ANISOU 1523  CB  ALA A 236     6404   7303   6763    115   -655   -286       C  
ATOM   1524  N   ASP A 237      24.626 -14.365 144.409  1.00 60.08           N  
ANISOU 1524  N   ASP A 237     7249   8128   7452    116   -779    -78       N  
ATOM   1525  CA  ASP A 237      24.810 -15.213 145.623  1.00 63.81           C  
ANISOU 1525  CA  ASP A 237     7724   8659   7861    111   -848     -3       C  
ATOM   1526  C   ASP A 237      23.519 -15.886 146.101  1.00 65.48           C  
ANISOU 1526  C   ASP A 237     7976   8885   8019     81   -847     81       C  
ATOM   1527  O   ASP A 237      23.469 -16.490 147.186  1.00 66.48           O  
ANISOU 1527  O   ASP A 237     8108   9072   8079     67   -894    152       O  
ATOM   1528  CB  ASP A 237      25.592 -14.518 146.790  1.00 64.55           C  
ANISOU 1528  CB  ASP A 237     7779   8858   7890    100   -876    -46       C  
ATOM   1529  N   SER A 238      22.498 -15.833 145.252  1.00 66.42           N  
ANISOU 1529  N   SER A 238     8121   8947   8169     71   -794     80       N  
ATOM   1530  CA  SER A 238      21.261 -16.579 145.510  1.00 67.32           C  
ANISOU 1530  CA  SER A 238     8271   9059   8250     41   -792    162       C  
ATOM   1531  C   SER A 238      21.409 -18.110 145.466  1.00 67.52           C  
ANISOU 1531  C   SER A 238     8318   9023   8311     57   -856    262       C  
ATOM   1532  O   SER A 238      22.191 -18.667 144.680  1.00 66.98           O  
ANISOU 1532  O   SER A 238     8249   8877   8325     99   -886    258       O  
ATOM   1533  CB  SER A 238      20.146 -16.103 144.572  1.00 66.81           C  
ANISOU 1533  CB  SER A 238     8221   8949   8213     28   -723    130       C  
ATOM   1534  OG  SER A 238      19.676 -14.826 145.007  1.00 68.50           O  
ANISOU 1534  OG  SER A 238     8420   9235   8374      3   -669     64       O  
ATOM   1535  N   ASP A 239      20.631 -18.753 146.337  1.00 68.37           N  
ANISOU 1535  N   ASP A 239     8446   9172   8359     22   -875    352       N  
ATOM   1536  CA  ASP A 239      20.506 -20.222 146.444  1.00 69.22           C  
ANISOU 1536  CA  ASP A 239     8581   9223   8496     24   -934    464       C  
ATOM   1537  C   ASP A 239      20.166 -20.902 145.091  1.00 67.96           C  
ANISOU 1537  C   ASP A 239     8446   8935   8442     44   -926    465       C  
ATOM   1538  O   ASP A 239      20.547 -22.047 144.844  1.00 69.11           O  
ANISOU 1538  O   ASP A 239     8605   9003   8650     68   -982    523       O  
ATOM   1539  CB  ASP A 239      19.463 -20.581 147.536  1.00 69.96           C  
ANISOU 1539  CB  ASP A 239     8690   9390   8500    -30   -934    556       C  
ATOM   1540  N   ASP A 240      19.391 -20.187 144.278  1.00 65.91           N  
ANISOU 1540  N   ASP A 240     8189   8659   8195     32   -859    403       N  
ATOM   1541  CA  ASP A 240      19.267 -20.324 142.816  1.00 63.59           C  
ANISOU 1541  CA  ASP A 240     7906   8265   7991     58   -836    358       C  
ATOM   1542  C   ASP A 240      20.427 -20.874 141.997  1.00 61.61           C  
ANISOU 1542  C   ASP A 240     7649   7933   7827    114   -875    332       C  
ATOM   1543  O   ASP A 240      20.224 -21.555 140.970  1.00 60.58           O  
ANISOU 1543  O   ASP A 240     7536   7712   7770    133   -879    331       O  
ATOM   1544  CB  ASP A 240      19.065 -18.904 142.255  1.00 62.74           C  
ANISOU 1544  CB  ASP A 240     7780   8187   7872     56   -763    258       C  
ATOM   1545  CG  ASP A 240      17.722 -18.722 141.736  1.00 64.51           C  
ANISOU 1545  CG  ASP A 240     8021   8397   8095     27   -714    258       C  
ATOM   1546  OD1 ASP A 240      16.940 -19.673 141.875  1.00 69.44           O  
ANISOU 1546  OD1 ASP A 240     8668   8994   8723      3   -735    333       O  
ATOM   1547  OD2 ASP A 240      17.416 -17.661 141.192  1.00 68.05           O  
ANISOU 1547  OD2 ASP A 240     8458   8857   8542     28   -657    188       O  
ATOM   1548  N   GLN A 241      21.627 -20.468 142.405  1.00 59.40           N  
ANISOU 1548  N   GLN A 241     7339   7694   7537    142   -897    299       N  
ATOM   1549  CA  GLN A 241      22.810 -20.482 141.551  1.00 57.50           C  
ANISOU 1549  CA  GLN A 241     7076   7402   7369    196   -909    239       C  
ATOM   1550  C   GLN A 241      22.628 -19.587 140.292  1.00 54.75           C  
ANISOU 1550  C   GLN A 241     6721   7028   7054    204   -839    149       C  
ATOM   1551  O   GLN A 241      23.390 -19.668 139.341  1.00 54.18           O  
ANISOU 1551  O   GLN A 241     6635   6906   7045    246   -838    102       O  
ATOM   1552  CB  GLN A 241      23.284 -21.927 141.249  1.00 58.76           C  
ANISOU 1552  CB  GLN A 241     7248   7473   7603    235   -976    293       C  
ATOM   1553  N   ARG A 242      21.649 -18.689 140.345  1.00 52.05           N  
ANISOU 1553  N   ARG A 242     6385   6726   6664    165   -781    128       N  
ATOM   1554  CA  ARG A 242      21.319 -17.787 139.249  1.00 49.55           C  
ANISOU 1554  CA  ARG A 242     6066   6391   6371    168   -715     57       C  
ATOM   1555  C   ARG A 242      20.792 -18.507 138.001  1.00 48.87           C  
ANISOU 1555  C   ARG A 242     6004   6219   6344    184   -709     62       C  
ATOM   1556  O   ARG A 242      20.905 -17.977 136.904  1.00 49.54           O  
ANISOU 1556  O   ARG A 242     6083   6280   6462    203   -668      3       O  
ATOM   1557  CB  ARG A 242      22.512 -16.903 138.869  1.00 48.44           C  
ANISOU 1557  CB  ARG A 242     5888   6264   6253    196   -696    -19       C  
ATOM   1558  CG  ARG A 242      23.118 -16.121 140.003  1.00 47.24           C  
ANISOU 1558  CG  ARG A 242     5706   6193   6049    181   -704    -40       C  
ATOM   1559  CD  ARG A 242      22.649 -14.750 139.921  1.00 47.37           C  
ANISOU 1559  CD  ARG A 242     5713   6245   6040    155   -639    -98       C  
ATOM   1560  NE  ARG A 242      23.686 -13.860 139.462  1.00 46.81           N  
ANISOU 1560  NE  ARG A 242     5606   6176   6004    173   -617   -170       N  
ATOM   1561  CZ  ARG A 242      23.493 -12.612 139.037  1.00 43.91           C  
ANISOU 1561  CZ  ARG A 242     5227   5814   5642    159   -557   -229       C  
ATOM   1562  NH1 ARG A 242      22.304 -12.068 138.981  1.00 41.36           N  
ANISOU 1562  NH1 ARG A 242     4924   5496   5295    134   -513   -231       N  
ATOM   1563  NH2 ARG A 242      24.527 -11.891 138.679  1.00 45.87           N  
ANISOU 1563  NH2 ARG A 242     5440   6062   5927    171   -542   -286       N  
ATOM   1564  N   ARG A 243      20.228 -19.695 138.150  1.00 48.28           N  
ANISOU 1564  N   ARG A 243     5957   6102   6284    176   -749    130       N  
ATOM   1565  CA  ARG A 243      19.797 -20.496 136.992  1.00 48.67           C  
ANISOU 1565  CA  ARG A 243     6029   6067   6396    192   -753    128       C  
ATOM   1566  C   ARG A 243      18.300 -20.398 136.649  1.00 47.54           C  
ANISOU 1566  C   ARG A 243     5909   5919   6236    152   -717    143       C  
ATOM   1567  O   ARG A 243      17.893 -20.759 135.531  1.00 46.95           O  
ANISOU 1567  O   ARG A 243     5847   5786   6205    164   -708    120       O  
ATOM   1568  CB  ARG A 243      20.095 -21.981 137.206  1.00 49.24           C  
ANISOU 1568  CB  ARG A 243     6119   6075   6517    209   -825    189       C  
ATOM   1569  CG  ARG A 243      21.459 -22.252 137.627  1.00 54.42           C  
ANISOU 1569  CG  ARG A 243     6752   6733   7193    249   -871    188       C  
ATOM   1570  CD  ARG A 243      22.327 -22.527 136.454  1.00 61.93           C  
ANISOU 1570  CD  ARG A 243     7689   7624   8216    305   -874    125       C  
ATOM   1571  NE  ARG A 243      23.705 -22.327 136.842  1.00 69.06           N  
ANISOU 1571  NE  ARG A 243     8555   8556   9127    342   -899    102       N  
ATOM   1572  CZ  ARG A 243      24.745 -22.779 136.166  1.00 71.81           C  
ANISOU 1572  CZ  ARG A 243     8883   8861   9541    398   -920     62       C  
ATOM   1573  NH1 ARG A 243      24.567 -23.467 135.041  1.00 72.70           N  
ANISOU 1573  NH1 ARG A 243     9010   8897   9714    426   -920     34       N  
ATOM   1574  NH2 ARG A 243      25.959 -22.537 136.639  1.00 73.47           N  
ANISOU 1574  NH2 ARG A 243     9054   9109   9753    427   -943     45       N  
ATOM   1575  N   LEU A 244      17.491 -19.975 137.615  1.00 46.75           N  
ANISOU 1575  N   LEU A 244     5810   5883   6071    106   -700    179       N  
ATOM   1576  CA  LEU A 244      16.055 -19.920 137.413  1.00 45.86           C  
ANISOU 1576  CA  LEU A 244     5711   5772   5941     68   -668    198       C  
ATOM   1577  C   LEU A 244      15.644 -18.557 136.918  1.00 44.38           C  
ANISOU 1577  C   LEU A 244     5509   5624   5730     65   -601    133       C  
ATOM   1578  O   LEU A 244      16.335 -17.555 137.161  1.00 44.01           O  
ANISOU 1578  O   LEU A 244     5441   5621   5661     78   -577     86       O  
ATOM   1579  CB  LEU A 244      15.328 -20.239 138.701  1.00 46.64           C  
ANISOU 1579  CB  LEU A 244     5816   5922   5983     19   -682    276       C  
ATOM   1580  CG  LEU A 244      15.609 -21.600 139.362  1.00 49.09           C  
ANISOU 1580  CG  LEU A 244     6142   6197   6312     12   -751    362       C  
ATOM   1581  CD1 LEU A 244      14.775 -21.750 140.672  1.00 48.29           C  
ANISOU 1581  CD1 LEU A 244     6043   6167   6138    -44   -752    444       C  
ATOM   1582  CD2 LEU A 244      15.277 -22.712 138.413  1.00 48.14           C  
ANISOU 1582  CD2 LEU A 244     6045   5974   6272     20   -780    379       C  
ATOM   1583  N   VAL A 245      14.501 -18.525 136.237  1.00 42.78           N  
ANISOU 1583  N   VAL A 245     5316   5404   5535     48   -573    131       N  
ATOM   1584  CA  VAL A 245      13.950 -17.293 135.667  1.00 40.41           C  
ANISOU 1584  CA  VAL A 245     5003   5131   5218     48   -511     77       C  
ATOM   1585  C   VAL A 245      12.687 -16.822 136.383  1.00 39.64           C  
ANISOU 1585  C   VAL A 245     4900   5093   5070      5   -480    101       C  
ATOM   1586  O   VAL A 245      11.864 -17.646 136.752  1.00 39.72           O  
ANISOU 1586  O   VAL A 245     4920   5100   5072    -28   -499    159       O  
ATOM   1587  CB  VAL A 245      13.728 -17.465 134.150  1.00 39.85           C  
ANISOU 1587  CB  VAL A 245     4942   5002   5198     73   -502     44       C  
ATOM   1588  CG1 VAL A 245      13.345 -16.151 133.531  1.00 38.77           C  
ANISOU 1588  CG1 VAL A 245     4791   4891   5047     79   -443     -6       C  
ATOM   1589  CG2 VAL A 245      15.010 -17.975 133.520  1.00 39.62           C  
ANISOU 1589  CG2 VAL A 245     4915   4924   5215    117   -531     18       C  
ATOM   1590  N   TYR A 246      12.538 -15.500 136.553  1.00 38.47           N  
ANISOU 1590  N   TYR A 246     4731   4995   4890      5   -430     55       N  
ATOM   1591  CA  TYR A 246      11.433 -14.902 137.313  1.00 38.48           C  
ANISOU 1591  CA  TYR A 246     4719   5061   4840    -29   -394     63       C  
ATOM   1592  C   TYR A 246      10.818 -13.668 136.625  1.00 38.34           C  
ANISOU 1592  C   TYR A 246     4687   5052   4830    -17   -338      8       C  
ATOM   1593  O   TYR A 246      11.485 -13.000 135.827  1.00 37.68           O  
ANISOU 1593  O   TYR A 246     4600   4938   4778     15   -321    -40       O  
ATOM   1594  CB  TYR A 246      11.900 -14.463 138.720  1.00 38.49           C  
ANISOU 1594  CB  TYR A 246     4706   5137   4783    -43   -395     62       C  
ATOM   1595  CG  TYR A 246      12.563 -15.537 139.553  1.00 40.49           C  
ANISOU 1595  CG  TYR A 246     4970   5395   5019    -53   -452    121       C  
ATOM   1596  CD1 TYR A 246      11.828 -16.321 140.440  1.00 41.83           C  
ANISOU 1596  CD1 TYR A 246     5146   5601   5147    -93   -470    195       C  
ATOM   1597  CD2 TYR A 246      13.928 -15.789 139.434  1.00 42.19           C  
ANISOU 1597  CD2 TYR A 246     5188   5580   5263    -21   -488    108       C  
ATOM   1598  CE1 TYR A 246      12.444 -17.345 141.184  1.00 43.02           C  
ANISOU 1598  CE1 TYR A 246     5308   5751   5286   -101   -527    261       C  
ATOM   1599  CE2 TYR A 246      14.546 -16.798 140.170  1.00 43.62           C  
ANISOU 1599  CE2 TYR A 246     5377   5761   5434    -25   -546    167       C  
ATOM   1600  CZ  TYR A 246      13.805 -17.564 141.051  1.00 44.37           C  
ANISOU 1600  CZ  TYR A 246     5482   5888   5488    -64   -566    246       C  
ATOM   1601  OH  TYR A 246      14.439 -18.546 141.776  1.00 44.40           O  
ANISOU 1601  OH  TYR A 246     5495   5890   5485    -66   -626    313       O  
ATOM   1602  N   TYR A 247       9.549 -13.380 136.938  1.00 38.53           N  
ANISOU 1602  N   TYR A 247     4698   5114   4825    -43   -309     20       N  
ATOM   1603  CA  TYR A 247       8.963 -12.070 136.695  1.00 38.98           C  
ANISOU 1603  CA  TYR A 247     4736   5196   4880    -33   -255    -31       C  
ATOM   1604  C   TYR A 247       9.108 -11.350 138.007  1.00 39.51           C  
ANISOU 1604  C   TYR A 247     4784   5335   4893    -47   -236    -54       C  
ATOM   1605  O   TYR A 247       8.635 -11.845 139.040  1.00 40.94           O  
ANISOU 1605  O   TYR A 247     4960   5572   5024    -80   -245    -15       O  
ATOM   1606  CB  TYR A 247       7.476 -12.172 136.375  1.00 39.53           C  
ANISOU 1606  CB  TYR A 247     4797   5276   4949    -51   -235    -10       C  
ATOM   1607  CG  TYR A 247       7.205 -12.875 135.064  1.00 43.39           C  
ANISOU 1607  CG  TYR A 247     5301   5699   5484    -40   -256      7       C  
ATOM   1608  CD1 TYR A 247       7.122 -12.157 133.891  1.00 46.81           C  
ANISOU 1608  CD1 TYR A 247     5732   6101   5951     -8   -233    -31       C  
ATOM   1609  CD2 TYR A 247       7.082 -14.268 134.996  1.00 44.08           C  
ANISOU 1609  CD2 TYR A 247     5406   5756   5585    -61   -301     59       C  
ATOM   1610  CE1 TYR A 247       6.883 -12.789 132.698  1.00 52.37           C  
ANISOU 1610  CE1 TYR A 247     6451   6758   6690      3   -253    -21       C  
ATOM   1611  CE2 TYR A 247       6.847 -14.902 133.808  1.00 47.07           C  
ANISOU 1611  CE2 TYR A 247     5799   6077   6007    -51   -322     63       C  
ATOM   1612  CZ  TYR A 247       6.742 -14.165 132.664  1.00 51.29           C  
ANISOU 1612  CZ  TYR A 247     6329   6593   6564    -19   -298     20       C  
ATOM   1613  OH  TYR A 247       6.501 -14.766 131.447  1.00 56.67           O  
ANISOU 1613  OH  TYR A 247     7024   7228   7281     -7   -319     18       O  
ATOM   1614  N   GLU A 248       9.766 -10.205 138.016  1.00 37.61           N  
ANISOU 1614  N   GLU A 248     4531   5097   4661    -25   -211   -116       N  
ATOM   1615  CA  GLU A 248       9.920  -9.534 139.261  1.00 36.96           C  
ANISOU 1615  CA  GLU A 248     4430   5085   4529    -38   -196   -149       C  
ATOM   1616  C   GLU A 248       9.751  -8.028 139.051  1.00 36.58           C  
ANISOU 1616  C   GLU A 248     4361   5036   4502    -19   -146   -222       C  
ATOM   1617  O   GLU A 248      10.088  -7.521 138.000  1.00 35.86           O  
ANISOU 1617  O   GLU A 248     4274   4885   4467      8   -134   -245       O  
ATOM   1618  CB  GLU A 248      11.293  -9.934 139.835  1.00 37.52           C  
ANISOU 1618  CB  GLU A 248     4507   5162   4586    -36   -237   -146       C  
ATOM   1619  CG  GLU A 248      11.744  -9.181 141.072  1.00 39.76           C  
ANISOU 1619  CG  GLU A 248     4771   5518   4819    -46   -229   -192       C  
ATOM   1620  CD  GLU A 248      13.092  -9.644 141.622  1.00 43.94           C  
ANISOU 1620  CD  GLU A 248     5303   6059   5334    -44   -278   -184       C  
ATOM   1621  OE1 GLU A 248      13.581 -10.751 141.219  1.00 43.60           O  
ANISOU 1621  OE1 GLU A 248     5280   5972   5315    -37   -321   -129       O  
ATOM   1622  OE2 GLU A 248      13.667  -8.878 142.463  1.00 45.42           O  
ANISOU 1622  OE2 GLU A 248     5471   6297   5489    -47   -273   -238       O  
ATOM   1623  N   GLY A 249       9.214  -7.313 140.043  1.00 37.55           N  
ANISOU 1623  N   GLY A 249     4461   5226   4581    -31   -117   -258       N  
ATOM   1624  CA  GLY A 249       9.067  -5.864 139.954  1.00 38.65           C  
ANISOU 1624  CA  GLY A 249     4580   5359   4747    -12    -72   -334       C  
ATOM   1625  C   GLY A 249       9.960  -5.055 140.878  1.00 40.15           C  
ANISOU 1625  C   GLY A 249     4754   5583   4917    -13    -69   -401       C  
ATOM   1626  O   GLY A 249      10.799  -5.580 141.579  1.00 41.79           O  
ANISOU 1626  O   GLY A 249     4967   5824   5087    -27   -104   -390       O  
ATOM   1627  N   GLY A 250       9.787  -3.752 140.890  1.00 40.58           N  
ANISOU 1627  N   GLY A 250     4790   5630   5001      2    -31   -473       N  
ATOM   1628  CA  GLY A 250      10.501  -2.952 141.858  1.00 41.11           C  
ANISOU 1628  CA  GLY A 250     4838   5734   5047     -4    -27   -548       C  
ATOM   1629  C   GLY A 250      11.713  -2.399 141.164  1.00 41.41           C  
ANISOU 1629  C   GLY A 250     4880   5699   5153     11    -35   -577       C  
ATOM   1630  O   GLY A 250      11.674  -2.076 140.000  1.00 43.59           O  
ANISOU 1630  O   GLY A 250     5164   5900   5497     31    -20   -566       O  
ATOM   1631  N   ALA A 251      12.811  -2.356 141.865  1.00 41.58           N  
ANISOU 1631  N   ALA A 251     4895   5749   5155      0    -61   -609       N  
ATOM   1632  CA  ALA A 251      14.027  -1.782 141.364  1.00 41.55           C  
ANISOU 1632  CA  ALA A 251     4887   5687   5214      8    -68   -644       C  
ATOM   1633  C   ALA A 251      14.760  -2.663 140.312  1.00 40.92           C  
ANISOU 1633  C   ALA A 251     4827   5551   5169     18    -96   -579       C  
ATOM   1634  O   ALA A 251      15.667  -2.158 139.611  1.00 41.65           O  
ANISOU 1634  O   ALA A 251     4914   5587   5324     27    -92   -600       O  
ATOM   1635  CB  ALA A 251      14.953  -1.485 142.580  1.00 40.90           C  
ANISOU 1635  CB  ALA A 251     4784   5665   5091    -10    -92   -705       C  
ATOM   1636  N   VAL A 252      14.406  -3.949 140.201  1.00 40.12           N  
ANISOU 1636  N   VAL A 252     4746   5465   5033     16   -123   -505       N  
ATOM   1637  CA  VAL A 252      15.182  -4.843 139.325  1.00 40.08           C  
ANISOU 1637  CA  VAL A 252     4758   5413   5058     28   -154   -455       C  
ATOM   1638  C   VAL A 252      15.111  -4.290 137.896  1.00 39.65           C  
ANISOU 1638  C   VAL A 252     4708   5281   5076     50   -122   -456       C  
ATOM   1639  O   VAL A 252      16.104  -4.360 137.123  1.00 38.45           O  
ANISOU 1639  O   VAL A 252     4556   5085   4967     62   -130   -453       O  
ATOM   1640  CB  VAL A 252      14.790  -6.354 139.421  1.00 39.37           C  
ANISOU 1640  CB  VAL A 252     4690   5340   4928     22   -192   -376       C  
ATOM   1641  CG1 VAL A 252      13.304  -6.579 139.246  1.00 40.37           C  
ANISOU 1641  CG1 VAL A 252     4826   5475   5037     15   -169   -342       C  
ATOM   1642  CG2 VAL A 252      15.466  -7.144 138.370  1.00 41.38           C  
ANISOU 1642  CG2 VAL A 252     4959   5536   5226     41   -216   -339       C  
ATOM   1643  N   CYS A 253      13.977  -3.646 137.599  1.00 39.49           N  
ANISOU 1643  N   CYS A 253     4688   5250   5068     55    -83   -464       N  
ATOM   1644  C   CYS A 253      14.758  -2.010 135.923  1.00 39.32           C  
ANISOU 1644  C   CYS A 253     4656   5119   5165     81    -34   -502       C  
ATOM   1645  O   CYS A 253      14.751  -1.478 134.821  1.00 40.70           O  
ANISOU 1645  O   CYS A 253     4834   5240   5392     97     -9   -492       O  
ATOM   1646  CA ACYS A 253      13.689  -3.053 136.302  0.50 39.81           C  
ANISOU 1646  CA ACYS A 253     4733   5225   5169     76    -52   -458       C  
ATOM   1647  CB ACYS A 253      12.251  -2.453 136.329  0.50 40.40           C  
ANISOU 1647  CB ACYS A 253     4802   5307   5241     81    -17   -465       C  
ATOM   1648  SG ACYS A 253      10.845  -3.668 136.684  0.50 40.52           S  
ANISOU 1648  SG ACYS A 253     4827   5375   5192     69    -32   -407       S  
ATOM   1649  CA BCYS A 253      13.789  -3.134 136.232  0.50 39.35           C  
ANISOU 1649  CA BCYS A 253     4675   5164   5111     77    -55   -455       C  
ATOM   1650  CB BCYS A 253      12.362  -2.650 135.988  0.50 39.96           C  
ANISOU 1650  CB BCYS A 253     4752   5238   5192     85    -22   -451       C  
ATOM   1651  SG BCYS A 253      12.171  -0.965 136.474  0.50 37.92           S  
ANISOU 1651  SG BCYS A 253     4468   4971   4970     88     21   -528       S  
ATOM   1652  N   THR A 254      15.636  -1.676 136.862  1.00 39.24           N  
ANISOU 1652  N   THR A 254     4627   5136   5146     65    -47   -551       N  
ATOM   1653  CA  THR A 254      16.739  -0.781 136.521  1.00 39.94           C  
ANISOU 1653  CA  THR A 254     4698   5184   5295     64    -34   -590       C  
ATOM   1654  C   THR A 254      18.115  -1.381 136.860  1.00 40.41           C  
ANISOU 1654  C   THR A 254     4746   5264   5344     55    -73   -595       C  
ATOM   1655  O   THR A 254      19.132  -0.673 136.813  1.00 41.49           O  
ANISOU 1655  O   THR A 254     4859   5379   5525     47    -67   -635       O  
ATOM   1656  CB  THR A 254      16.639   0.592 137.219  1.00 40.75           C  
ANISOU 1656  CB  THR A 254     4778   5282   5424     53     -7   -667       C  
ATOM   1657  OG1 THR A 254      16.901   0.403 138.587  1.00 40.20           O  
ANISOU 1657  OG1 THR A 254     4695   5282   5298     34    -34   -708       O  
ATOM   1658  CG2 THR A 254      15.248   1.204 137.124  1.00 42.11           C  
ANISOU 1658  CG2 THR A 254     4954   5441   5603     65     28   -672       C  
ATOM   1659  N   HIS A 255      18.156  -2.650 137.255  1.00 39.64           N  
ANISOU 1659  N   HIS A 255     4661   5207   5193     55   -114   -555       N  
ATOM   1660  CA  HIS A 255      19.413  -3.331 137.500  1.00 39.13           C  
ANISOU 1660  CA  HIS A 255     4585   5160   5122     54   -155   -550       C  
ATOM   1661  C   HIS A 255      19.881  -4.167 136.302  1.00 38.14           C  
ANISOU 1661  C   HIS A 255     4472   4994   5027     77   -165   -502       C  
ATOM   1662  O   HIS A 255      19.071  -4.553 135.410  1.00 36.50           O  
ANISOU 1662  O   HIS A 255     4288   4757   4823     91   -151   -460       O  
ATOM   1663  CB  HIS A 255      19.275  -4.272 138.692  1.00 40.73           C  
ANISOU 1663  CB  HIS A 255     4794   5431   5251     44   -200   -530       C  
ATOM   1664  CG  HIS A 255      19.051  -3.580 140.005  1.00 44.64           C  
ANISOU 1664  CG  HIS A 255     5273   5987   5703     22   -199   -584       C  
ATOM   1665  ND1 HIS A 255      18.605  -4.252 141.133  1.00 47.75           N  
ANISOU 1665  ND1 HIS A 255     5672   6454   6017      9   -227   -564       N  
ATOM   1666  CD2 HIS A 255      19.200  -2.279 140.372  1.00 46.72           C  
ANISOU 1666  CD2 HIS A 255     5513   6250   5990     10   -171   -661       C  
ATOM   1667  CE1 HIS A 255      18.493  -3.393 142.133  1.00 47.48           C  
ANISOU 1667  CE1 HIS A 255     5618   6470   5951     -8   -216   -629       C  
ATOM   1668  NE2 HIS A 255      18.851  -2.192 141.699  1.00 46.98           N  
ANISOU 1668  NE2 HIS A 255     5537   6360   5953     -7   -184   -693       N  
ATOM   1669  N   ALA A 256      21.176  -4.512 136.311  1.00 36.79           N  
ANISOU 1669  N   ALA A 256     4280   4826   4871     81   -193   -510       N  
ATOM   1670  CA  ALA A 256      21.757  -5.202 135.161  1.00 35.12           C  
ANISOU 1670  CA  ALA A 256     4072   4579   4692    106   -197   -478       C  
ATOM   1671  C   ALA A 256      21.209  -6.629 135.051  1.00 35.20           C  
ANISOU 1671  C   ALA A 256     4113   4593   4670    121   -232   -422       C  
ATOM   1672  O   ALA A 256      21.103  -7.160 133.942  1.00 36.08           O  
ANISOU 1672  O   ALA A 256     4238   4668   4801    143   -226   -395       O  
ATOM   1673  CB  ALA A 256      23.306  -5.162 135.186  1.00 34.12           C  
ANISOU 1673  CB  ALA A 256     3908   4457   4597    108   -215   -506       C  
ATOM   1674  N   ARG A 257      20.806  -7.248 136.162  1.00 35.22           N  
ANISOU 1674  N   ARG A 257     4125   4636   4620    110   -268   -403       N  
ATOM   1675  CA  ARG A 257      20.376  -8.642 136.067  1.00 34.52           C  
ANISOU 1675  CA  ARG A 257     4064   4541   4511    121   -306   -345       C  
ATOM   1676  C   ARG A 257      19.132  -8.868 135.196  1.00 34.52           C  
ANISOU 1676  C   ARG A 257     4093   4509   4514    125   -281   -314       C  
ATOM   1677  O   ARG A 257      18.799 -10.002 134.885  1.00 34.55           O  
ANISOU 1677  O   ARG A 257     4118   4494   4515    134   -309   -272       O  
ATOM   1678  CB  ARG A 257      20.247  -9.316 137.444  1.00 35.08           C  
ANISOU 1678  CB  ARG A 257     4138   4664   4525    104   -351   -318       C  
ATOM   1679  CG  ARG A 257      19.169  -8.826 138.309  1.00 35.56           C  
ANISOU 1679  CG  ARG A 257     4206   4770   4536     76   -332   -321       C  
ATOM   1680  CD  ARG A 257      19.333  -9.122 139.855  1.00 37.94           C  
ANISOU 1680  CD  ARG A 257     4499   5146   4770     56   -371   -312       C  
ATOM   1681  NE  ARG A 257      18.011  -9.585 140.256  1.00 45.92           N  
ANISOU 1681  NE  ARG A 257     5532   6182   5735     37   -366   -266       N  
ATOM   1682  CZ  ARG A 257      17.174  -9.054 141.135  1.00 42.30           C  
ANISOU 1682  CZ  ARG A 257     5068   5782   5221     12   -344   -280       C  
ATOM   1683  NH1 ARG A 257      17.481  -8.048 141.904  1.00 43.75           N  
ANISOU 1683  NH1 ARG A 257     5228   6015   5381      1   -329   -343       N  
ATOM   1684  NH2 ARG A 257      16.008  -9.611 141.250  1.00 41.90           N  
ANISOU 1684  NH2 ARG A 257     5035   5744   5141     -3   -338   -231       N  
ATOM   1685  N   SER A 258      18.434  -7.822 134.762  1.00 34.19           N  
ANISOU 1685  N   SER A 258     4050   4456   4483    119   -232   -336       N  
ATOM   1686  CA  SER A 258      17.209  -8.092 133.971  1.00 33.47           C  
ANISOU 1686  CA  SER A 258     3983   4342   4391    124   -215   -304       C  
ATOM   1687  C   SER A 258      17.421  -7.772 132.496  1.00 32.39           C  
ANISOU 1687  C   SER A 258     3848   4161   4297    147   -186   -309       C  
ATOM   1688  O   SER A 258      16.459  -7.659 131.729  1.00 31.51           O  
ANISOU 1688  O   SER A 258     3751   4034   4189    152   -165   -293       O  
ATOM   1689  CB  SER A 258      16.034  -7.299 134.546  1.00 33.26           C  
ANISOU 1689  CB  SER A 258     3956   4342   4340    105   -185   -314       C  
ATOM   1690  OG  SER A 258      16.318  -5.915 134.548  1.00 34.86           O  
ANISOU 1690  OG  SER A 258     4139   4539   4569    103   -146   -362       O  
ATOM   1691  N   LEU A 259      18.690  -7.585 132.119  1.00 31.55           N  
ANISOU 1691  N   LEU A 259     3723   4043   4221    160   -185   -332       N  
ATOM   1692  CA  LEU A 259      19.055  -7.271 130.741  1.00 31.23           C  
ANISOU 1692  CA  LEU A 259     3679   3972   4216    180   -155   -335       C  
ATOM   1693  C   LEU A 259      19.317  -8.535 129.964  1.00 31.04           C  
ANISOU 1693  C   LEU A 259     3668   3932   4194    205   -183   -315       C  
ATOM   1694  O   LEU A 259      19.992  -9.457 130.473  1.00 30.67           O  
ANISOU 1694  O   LEU A 259     3618   3891   4145    212   -226   -313       O  
ATOM   1695  CB  LEU A 259      20.290  -6.398 130.701  1.00 31.85           C  
ANISOU 1695  CB  LEU A 259     3726   4049   4329    177   -134   -370       C  
ATOM   1696  CG  LEU A 259      20.057  -4.973 131.192  1.00 34.33           C  
ANISOU 1696  CG  LEU A 259     4025   4362   4656    155    -98   -398       C  
ATOM   1697  CD1 LEU A 259      21.379  -4.177 131.121  1.00 34.92           C  
ANISOU 1697  CD1 LEU A 259     4064   4430   4773    147    -81   -433       C  
ATOM   1698  CD2 LEU A 259      18.981  -4.328 130.338  1.00 33.18           C  
ANISOU 1698  CD2 LEU A 259     3895   4191   4519    160    -59   -379       C  
ATOM   1699  N   TRP A 260      18.808  -8.556 128.729  1.00 30.44           N  
ANISOU 1699  N   TRP A 260     3605   3837   4122    220   -161   -303       N  
ATOM   1700  CA  TRP A 260      18.915  -9.721 127.822  1.00 31.68           C  
ANISOU 1700  CA  TRP A 260     3777   3979   4282    246   -185   -294       C  
ATOM   1701  C   TRP A 260      19.339  -9.255 126.447  1.00 31.69           C  
ANISOU 1701  C   TRP A 260     3769   3975   4296    267   -147   -305       C  
ATOM   1702  O   TRP A 260      19.000  -8.112 126.053  1.00 32.97           O  
ANISOU 1702  O   TRP A 260     3926   4139   4462    258   -103   -300       O  
ATOM   1703  CB  TRP A 260      17.540 -10.422 127.682  1.00 30.76           C  
ANISOU 1703  CB  TRP A 260     3690   3854   4143    241   -204   -266       C  
ATOM   1704  CG  TRP A 260      17.032 -10.857 128.979  1.00 31.18           C  
ANISOU 1704  CG  TRP A 260     3751   3918   4177    217   -235   -247       C  
ATOM   1705  CD1 TRP A 260      16.296 -10.103 129.854  1.00 30.56           C  
ANISOU 1705  CD1 TRP A 260     3670   3863   4080    190   -218   -241       C  
ATOM   1706  CD2 TRP A 260      17.207 -12.149 129.597  1.00 29.06           C  
ANISOU 1706  CD2 TRP A 260     3494   3641   3907    216   -288   -228       C  
ATOM   1707  NE1 TRP A 260      15.986 -10.845 130.968  1.00 31.16           N  
ANISOU 1707  NE1 TRP A 260     3753   3955   4133    171   -255   -218       N  
ATOM   1708  CE2 TRP A 260      16.529 -12.103 130.846  1.00 30.31           C  
ANISOU 1708  CE2 TRP A 260     3655   3825   4036    184   -300   -204       C  
ATOM   1709  CE3 TRP A 260      17.836 -13.347 129.202  1.00 31.81           C  
ANISOU 1709  CE3 TRP A 260     3849   3962   4277    240   -328   -227       C  
ATOM   1710  CZ2 TRP A 260      16.482 -13.201 131.738  1.00 29.15           C  
ANISOU 1710  CZ2 TRP A 260     3519   3679   3879    172   -349   -170       C  
ATOM   1711  CZ3 TRP A 260      17.777 -14.471 130.073  1.00 31.29           C  
ANISOU 1711  CZ3 TRP A 260     3795   3884   4211    231   -381   -196       C  
ATOM   1712  CH2 TRP A 260      17.083 -14.377 131.334  1.00 32.70           C  
ANISOU 1712  CH2 TRP A 260     3978   4091   4356    195   -391   -162       C  
ATOM   1713  N   ARG A 261      20.066 -10.119 125.733  1.00 31.10           N  
ANISOU 1713  N   ARG A 261     3690   3896   4230    294   -162   -318       N  
ATOM   1714  CA  ARG A 261      20.523  -9.860 124.371  1.00 30.93           C  
ANISOU 1714  CA  ARG A 261     3658   3881   4211    316   -127   -329       C  
ATOM   1715  C   ARG A 261      19.851 -10.848 123.454  1.00 31.87           C  
ANISOU 1715  C   ARG A 261     3804   3994   4313    338   -146   -326       C  
ATOM   1716  O   ARG A 261      19.868 -12.072 123.704  1.00 33.05           O  
ANISOU 1716  O   ARG A 261     3965   4126   4468    349   -193   -334       O  
ATOM   1717  CB  ARG A 261      22.059  -9.967 124.254  1.00 30.76           C  
ANISOU 1717  CB  ARG A 261     3603   3871   4215    333   -123   -358       C  
ATOM   1718  CG  ARG A 261      22.644  -9.465 122.956  1.00 31.72           C  
ANISOU 1718  CG  ARG A 261     3705   4011   4336    349    -75   -366       C  
ATOM   1719  CD  ARG A 261      24.210  -9.344 122.894  1.00 37.81           C  
ANISOU 1719  CD  ARG A 261     4431   4801   5136    359    -60   -395       C  
ATOM   1720  NE  ARG A 261      24.642 -10.039 121.672  1.00 46.49           N  
ANISOU 1720  NE  ARG A 261     5522   5917   6223    395    -50   -415       N  
ATOM   1721  CZ  ARG A 261      24.883  -9.520 120.476  1.00 46.06           C  
ANISOU 1721  CZ  ARG A 261     5455   5892   6154    403      0   -412       C  
ATOM   1722  NH1 ARG A 261      24.856  -8.236 120.221  1.00 52.83           N  
ANISOU 1722  NH1 ARG A 261     6302   6759   7013    376     49   -385       N  
ATOM   1723  NH2 ARG A 261      25.206 -10.318 119.522  1.00 49.20           N  
ANISOU 1723  NH2 ARG A 261     5848   6311   6535    438      0   -439       N  
ATOM   1724  N   LEU A 262      19.240 -10.325 122.404  1.00 32.86           N  
ANISOU 1724  N   LEU A 262     3937   4131   4418    342   -114   -315       N  
ATOM   1725  CA  LEU A 262      18.550 -11.138 121.403  1.00 35.08           C  
ANISOU 1725  CA  LEU A 262     4240   4413   4676    361   -130   -319       C  
ATOM   1726  C   LEU A 262      19.521 -11.590 120.315  1.00 37.31           C  
ANISOU 1726  C   LEU A 262     4507   4714   4955    395   -119   -352       C  
ATOM   1727  O   LEU A 262      20.218 -10.753 119.701  1.00 37.28           O  
ANISOU 1727  O   LEU A 262     4481   4737   4947    400    -72   -352       O  
ATOM   1728  CB  LEU A 262      17.435 -10.340 120.766  1.00 33.96           C  
ANISOU 1728  CB  LEU A 262     4110   4285   4509    353   -103   -290       C  
ATOM   1729  CG  LEU A 262      16.304  -9.909 121.708  1.00 35.65           C  
ANISOU 1729  CG  LEU A 262     4335   4486   4725    324   -110   -263       C  
ATOM   1730  CD1 LEU A 262      15.081  -9.546 120.885  1.00 35.08           C  
ANISOU 1730  CD1 LEU A 262     4275   4426   4627    326    -99   -239       C  
ATOM   1731  CD2 LEU A 262      15.926 -10.980 122.738  1.00 33.04           C  
ANISOU 1731  CD2 LEU A 262     4018   4136   4401    310   -161   -264       C  
ATOM   1732  N   GLU A 263      19.545 -12.908 120.063  1.00 39.08           N  
ANISOU 1732  N   GLU A 263     4743   4923   5182    417   -160   -381       N  
ATOM   1733  CA  GLU A 263      20.531 -13.494 119.157  1.00 40.26           C  
ANISOU 1733  CA  GLU A 263     4876   5090   5333    455   -155   -425       C  
ATOM   1734  C   GLU A 263      19.918 -14.422 118.128  1.00 40.95           C  
ANISOU 1734  C   GLU A 263     4984   5180   5398    478   -177   -453       C  
ATOM   1735  O   GLU A 263      19.778 -15.630 118.382  1.00 42.83           O  
ANISOU 1735  O   GLU A 263     5236   5380   5659    489   -228   -477       O  
ATOM   1736  CB  GLU A 263      21.598 -14.220 119.973  1.00 40.03           C  
ANISOU 1736  CB  GLU A 263     4828   5036   5345    469   -187   -449       C  
ATOM   1737  CG  GLU A 263      22.199 -13.330 121.051  1.00 42.25           C  
ANISOU 1737  CG  GLU A 263     5087   5320   5646    444   -172   -427       C  
ATOM   1738  CD  GLU A 263      23.510 -13.871 121.578  1.00 47.82           C  
ANISOU 1738  CD  GLU A 263     5761   6019   6388    465   -194   -454       C  
ATOM   1739  OE1 GLU A 263      23.695 -15.140 121.615  1.00 45.23           O  
ANISOU 1739  OE1 GLU A 263     5440   5663   6081    493   -241   -478       O  
ATOM   1740  OE2 GLU A 263      24.367 -13.004 121.922  1.00 48.51           O  
ANISOU 1740  OE2 GLU A 263     5816   6129   6488    454   -164   -454       O  
ATOM   1741  N   PRO A 264      19.554 -13.880 116.952  1.00 40.87           N  
ANISOU 1741  N   PRO A 264     4974   5212   5342    484   -141   -450       N  
ATOM   1742  CA  PRO A 264      19.088 -14.712 115.829  1.00 41.34           C  
ANISOU 1742  CA  PRO A 264     5049   5288   5372    509   -159   -488       C  
ATOM   1743  C   PRO A 264      20.098 -15.815 115.416  1.00 42.72           C  
ANISOU 1743  C   PRO A 264     5209   5459   5564    550   -177   -556       C  
ATOM   1744  O   PRO A 264      21.266 -15.721 115.732  1.00 40.85           O  
ANISOU 1744  O   PRO A 264     4944   5225   5352    563   -162   -569       O  
ATOM   1745  CB  PRO A 264      18.921 -13.703 114.686  1.00 40.91           C  
ANISOU 1745  CB  PRO A 264     4986   5296   5260    512   -106   -468       C  
ATOM   1746  CG  PRO A 264      18.761 -12.394 115.349  1.00 39.98           C  
ANISOU 1746  CG  PRO A 264     4864   5175   5154    480    -73   -408       C  
ATOM   1747  CD  PRO A 264      19.583 -12.449 116.604  1.00 40.44           C  
ANISOU 1747  CD  PRO A 264     4907   5194   5263    469    -83   -411       C  
ATOM   1748  N   LEU A 265      19.622 -16.859 114.730  1.00 44.49           N  
ANISOU 1748  N   LEU A 265     5451   5676   5779    571   -213   -602       N  
ATOM   1749  CA  LEU A 265      20.460 -17.999 114.433  1.00 45.94           C  
ANISOU 1749  CA  LEU A 265     5623   5842   5990    612   -238   -673       C  
ATOM   1750  C   LEU A 265      21.229 -17.739 113.137  1.00 47.38           C  
ANISOU 1750  C   LEU A 265     5779   6101   6125    647   -189   -717       C  
ATOM   1751  O   LEU A 265      21.003 -18.398 112.142  1.00 49.25           O  
ANISOU 1751  O   LEU A 265     6022   6360   6332    674   -200   -773       O  
ATOM   1752  CB  LEU A 265      19.612 -19.277 114.339  1.00 45.48           C  
ANISOU 1752  CB  LEU A 265     5595   5733   5954    616   -302   -709       C  
ATOM   1753  CG  LEU A 265      18.654 -19.637 115.494  1.00 45.05           C  
ANISOU 1753  CG  LEU A 265     5568   5610   5940    576   -351   -661       C  
ATOM   1754  CD1 LEU A 265      18.033 -21.000 115.294  1.00 44.52           C  
ANISOU 1754  CD1 LEU A 265     5524   5487   5906    582   -413   -704       C  
ATOM   1755  CD2 LEU A 265      19.255 -19.613 116.857  1.00 41.67           C  
ANISOU 1755  CD2 LEU A 265     5132   5140   5562    564   -364   -623       C  
ATOM   1756  N   ARG A 266      22.145 -16.777 113.143  1.00 47.25           N  
ANISOU 1756  N   ARG A 266     5729   6126   6097    646   -133   -693       N  
ATOM   1757  CA  ARG A 266      22.817 -16.344 111.920  1.00 46.76           C  
ANISOU 1757  CA  ARG A 266     5638   6147   5981    670    -76   -718       C  
ATOM   1758  C   ARG A 266      23.936 -15.435 112.391  1.00 46.87           C  
ANISOU 1758  C   ARG A 266     5613   6179   6016    660    -29   -687       C  
ATOM   1759  O   ARG A 266      23.940 -15.003 113.538  1.00 45.61           O  
ANISOU 1759  O   ARG A 266     5455   5974   5899    630    -40   -643       O  
ATOM   1760  CB  ARG A 266      21.848 -15.574 111.024  1.00 46.87           C  
ANISOU 1760  CB  ARG A 266     5672   6216   5923    652    -48   -680       C  
ATOM   1761  N   ILE A 267      24.928 -15.189 111.540  1.00 47.86           N  
ANISOU 1761  N   ILE A 267     5700   6373   6113    683     23   -714       N  
ATOM   1762  CA  ILE A 267      26.005 -14.280 111.906  1.00 47.70           C  
ANISOU 1762  CA  ILE A 267     5635   6374   6114    668     72   -685       C  
ATOM   1763  C   ILE A 267      25.808 -13.019 111.071  1.00 48.45           C  
ANISOU 1763  C   ILE A 267     5726   6535   6149    643    137   -627       C  
ATOM   1764  O   ILE A 267      25.540 -11.952 111.608  1.00 49.45           O  
ANISOU 1764  O   ILE A 267     5857   6642   6289    602    156   -559       O  
ATOM   1765  CB  ILE A 267      27.417 -14.903 111.689  1.00 48.04           C  
ANISOU 1765  CB  ILE A 267     5628   6445   6182    711     85   -752       C  
ATOM   1766  CG1 ILE A 267      27.506 -16.258 112.367  1.00 48.78           C  
ANISOU 1766  CG1 ILE A 267     5731   6469   6334    744     13   -809       C  
ATOM   1767  CG2 ILE A 267      28.511 -14.010 112.258  1.00 46.09           C  
ANISOU 1767  CG2 ILE A 267     5332   6212   5970    689    125   -721       C  
ATOM   1768  CD1 ILE A 267      27.273 -16.236 113.885  1.00 50.54           C  
ANISOU 1768  CD1 ILE A 267     5971   6612   6620    714    -35   -765       C  
ATOM   1769  N   SER A 268      25.925 -13.143 109.759  1.00 48.51           N  
ANISOU 1769  N   SER A 268     5722   6619   6089    668    171   -654       N  
ATOM   1770  CA  SER A 268      25.617 -12.047 108.871  1.00 48.29           C  
ANISOU 1770  CA  SER A 268     5695   6656   5996    646    227   -592       C  
ATOM   1771  C   SER A 268      24.157 -11.668 109.038  1.00 46.78           C  
ANISOU 1771  C   SER A 268     5554   6430   5790    620    198   -538       C  
ATOM   1772  O   SER A 268      23.270 -12.540 109.226  1.00 46.18           O  
ANISOU 1772  O   SER A 268     5513   6315   5718    631    139   -570       O  
ATOM   1773  CB  SER A 268      25.862 -12.478 107.420  1.00 49.63           C  
ANISOU 1773  CB  SER A 268     5849   6922   6084    683    257   -640       C  
ATOM   1774  OG  SER A 268      27.247 -12.528 107.134  1.00 52.03           O  
ANISOU 1774  OG  SER A 268     6097   7278   6394    703    304   -677       O  
ATOM   1775  N   TRP A 269      23.909 -10.369 108.948  1.00 45.08           N  
ANISOU 1775  N   TRP A 269     5339   6228   5561    586    239   -455       N  
ATOM   1776  CA  TRP A 269      22.576  -9.822 109.187  1.00 43.40           C  
ANISOU 1776  CA  TRP A 269     5167   5980   5344    561    216   -396       C  
ATOM   1777  C   TRP A 269      21.938 -10.269 110.487  1.00 42.18           C  
ANISOU 1777  C   TRP A 269     5038   5737   5251    548    157   -406       C  
ATOM   1778  O   TRP A 269      20.723 -10.348 110.578  1.00 42.03           O  
ANISOU 1778  O   TRP A 269     5052   5695   5221    540    122   -387       O  
ATOM   1779  CB  TRP A 269      21.659 -10.125 108.003  1.00 43.21           C  
ANISOU 1779  CB  TRP A 269     5167   6014   5238    581    206   -400       C  
ATOM   1780  CG  TRP A 269      22.202  -9.507 106.797  1.00 43.30           C  
ANISOU 1780  CG  TRP A 269     5153   6117   5179    588    268   -372       C  
ATOM   1781  CD1 TRP A 269      22.769 -10.157 105.732  1.00 39.34           C  
ANISOU 1781  CD1 TRP A 269     4633   5700   4614    622    287   -430       C  
ATOM   1782  CD2 TRP A 269      22.336  -8.087 106.533  1.00 40.34           C  
ANISOU 1782  CD2 TRP A 269     4767   5766   4796    558    325   -278       C  
ATOM   1783  NE1 TRP A 269      23.222  -9.234 104.822  1.00 41.74           N  
ANISOU 1783  NE1 TRP A 269     4914   6085   4861    614    354   -373       N  
ATOM   1784  CE2 TRP A 269      22.948  -7.962 105.265  1.00 41.01           C  
ANISOU 1784  CE2 TRP A 269     4827   5953   4803    574    376   -275       C  
ATOM   1785  CE3 TRP A 269      21.969  -6.933 107.221  1.00 36.48           C  
ANISOU 1785  CE3 TRP A 269     4286   5218   4356    521    336   -199       C  
ATOM   1786  CZ2 TRP A 269      23.218  -6.714 104.671  1.00 42.22           C  
ANISOU 1786  CZ2 TRP A 269     4964   6151   4928    549    439   -184       C  
ATOM   1787  CZ3 TRP A 269      22.229  -5.680 106.631  1.00 39.27           C  
ANISOU 1787  CZ3 TRP A 269     4624   5607   4691    499    395   -113       C  
ATOM   1788  CH2 TRP A 269      22.869  -5.586 105.372  1.00 40.72           C  
ANISOU 1788  CH2 TRP A 269     4782   5891   4797    512    446   -102       C  
ATOM   1789  N   SER A 270      22.742 -10.589 111.497  1.00 41.86           N  
ANISOU 1789  N   SER A 270     4979   5651   5274    545    143   -434       N  
ATOM   1790  CA  SER A 270      22.145 -10.958 112.797  1.00 41.00           C  
ANISOU 1790  CA  SER A 270     4894   5466   5219    529     89   -433       C  
ATOM   1791  C   SER A 270      21.535  -9.735 113.491  1.00 39.41           C  
ANISOU 1791  C   SER A 270     4703   5233   5038    489    103   -364       C  
ATOM   1792  O   SER A 270      20.805  -9.891 114.447  1.00 39.33           O  
ANISOU 1792  O   SER A 270     4715   5172   5057    472     65   -356       O  
ATOM   1793  CB  SER A 270      23.148 -11.619 113.715  1.00 40.05           C  
ANISOU 1793  CB  SER A 270     4751   5310   5155    538     65   -476       C  
ATOM   1794  OG  SER A 270      24.264 -10.762 113.794  1.00 41.64           O  
ANISOU 1794  OG  SER A 270     4912   5534   5375    526    115   -460       O  
ATOM   1795  N   GLY A 271      21.844  -8.545 112.973  1.00 38.76           N  
ANISOU 1795  N   GLY A 271     4603   5181   4942    474    160   -317       N  
ATOM   1796  CA  GLY A 271      21.316  -7.286 113.447  1.00 36.92           C  
ANISOU 1796  CA  GLY A 271     4377   4919   4733    440    180   -253       C  
ATOM   1797  C   GLY A 271      20.145  -6.842 112.585  1.00 37.34           C  
ANISOU 1797  C   GLY A 271     4455   4995   4737    443    185   -207       C  
ATOM   1798  O   GLY A 271      19.721  -5.688 112.661  1.00 36.20           O  
ANISOU 1798  O   GLY A 271     4313   4834   4606    422    209   -148       O  
ATOM   1799  N   SER A 272      19.586  -7.752 111.783  1.00 37.34           N  
ANISOU 1799  N   SER A 272     4473   5031   4684    470    158   -235       N  
ATOM   1800  CA  SER A 272      18.423  -7.378 110.955  1.00 38.51           C  
ANISOU 1800  CA  SER A 272     4644   5209   4782    474    156   -192       C  
ATOM   1801  C   SER A 272      17.136  -7.215 111.814  1.00 38.37           C  
ANISOU 1801  C   SER A 272     4650   5136   4794    458    117   -170       C  
ATOM   1802  O   SER A 272      17.150  -7.498 113.002  1.00 38.20           O  
ANISOU 1802  O   SER A 272     4631   5061   4824    443     93   -191       O  
ATOM   1803  CB  SER A 272      18.218  -8.407 109.863  1.00 38.16           C  
ANISOU 1803  CB  SER A 272     4607   5222   4669    506    135   -238       C  
ATOM   1804  OG  SER A 272      17.783  -9.606 110.421  1.00 38.61           O  
ANISOU 1804  OG  SER A 272     4680   5242   4746    513     77   -296       O  
ATOM   1805  N   HIS A 273      16.031  -6.777 111.235  1.00 38.71           N  
ANISOU 1805  N   HIS A 273     4708   5198   4803    461    112   -127       N  
ATOM   1806  CA  HIS A 273      14.860  -6.535 112.048  1.00 38.76           C  
ANISOU 1806  CA  HIS A 273     4729   5158   4841    446     82   -106       C  
ATOM   1807  C   HIS A 273      14.356  -7.894 112.522  1.00 40.11           C  
ANISOU 1807  C   HIS A 273     4914   5311   5015    448     25   -163       C  
ATOM   1808  O   HIS A 273      14.390  -8.856 111.758  1.00 41.25           O  
ANISOU 1808  O   HIS A 273     5064   5490   5119    468      4   -205       O  
ATOM   1809  CB  HIS A 273      13.763  -5.866 111.255  1.00 38.39           C  
ANISOU 1809  CB  HIS A 273     4690   5139   4757    454     83    -50       C  
ATOM   1810  CG  HIS A 273      14.098  -4.507 110.738  1.00 39.11           C  
ANISOU 1810  CG  HIS A 273     4770   5242   4849    452    135     20       C  
ATOM   1811  ND1 HIS A 273      14.255  -3.401 111.562  1.00 41.01           N  
ANISOU 1811  ND1 HIS A 273     5003   5425   5155    431    162     56       N  
ATOM   1812  CD2 HIS A 273      14.205  -4.046 109.468  1.00 37.55           C  
ANISOU 1812  CD2 HIS A 273     4570   5105   4595    466    162     65       C  
ATOM   1813  CE1 HIS A 273      14.486  -2.322 110.824  1.00 38.46           C  
ANISOU 1813  CE1 HIS A 273     4671   5117   4824    431    203    123       C  
ATOM   1814  NE2 HIS A 273      14.458  -2.688 109.551  1.00 41.23           N  
ANISOU 1814  NE2 HIS A 273     5025   5542   5098    452    205    134       N  
ATOM   1815  N   LEU A 274      13.879  -8.010 113.765  1.00 40.36           N  
ANISOU 1815  N   LEU A 274     4951   5289   5094    428      0   -167       N  
ATOM   1816  CA  LEU A 274      13.323  -9.283 114.178  1.00 41.01           C  
ANISOU 1816  CA  LEU A 274     5047   5353   5181    425    -54   -209       C  
ATOM   1817  C   LEU A 274      11.951  -9.470 113.595  1.00 40.12           C  
ANISOU 1817  C   LEU A 274     4945   5262   5035    428    -82   -197       C  
ATOM   1818  O   LEU A 274      11.213  -8.482 113.472  1.00 40.22           O  
ANISOU 1818  O   LEU A 274     4955   5283   5043    425    -66   -147       O  
ATOM   1819  CB  LEU A 274      13.187  -9.354 115.688  1.00 41.58           C  
ANISOU 1819  CB  LEU A 274     5121   5373   5306    400    -70   -209       C  
ATOM   1820  CG  LEU A 274      14.427  -9.585 116.515  1.00 47.70           C  
ANISOU 1820  CG  LEU A 274     5886   6121   6117    394    -64   -235       C  
ATOM   1821  CD1 LEU A 274      13.979 -10.380 117.715  1.00 51.52           C  
ANISOU 1821  CD1 LEU A 274     6379   6566   6630    375   -108   -247       C  
ATOM   1822  CD2 LEU A 274      15.520 -10.344 115.725  1.00 51.63           C  
ANISOU 1822  CD2 LEU A 274     6377   6641   6598    420    -63   -278       C  
ATOM   1823  N   ARG A 275      11.598 -10.730 113.333  1.00 38.64           N  
ANISOU 1823  N   ARG A 275     4769   5078   4835    433   -128   -243       N  
ATOM   1824  CA  ARG A 275      10.316 -11.126 112.773  1.00 38.44           C  
ANISOU 1824  CA  ARG A 275     4750   5074   4780    433   -165   -244       C  
ATOM   1825  C   ARG A 275       9.510 -12.019 113.684  1.00 37.68           C  
ANISOU 1825  C   ARG A 275     4662   4935   4721    407   -213   -261       C  
ATOM   1826  O   ARG A 275      10.071 -12.798 114.467  1.00 38.36           O  
ANISOU 1826  O   ARG A 275     4753   4978   4845    398   -230   -289       O  
ATOM   1827  CB  ARG A 275      10.531 -11.859 111.466  1.00 39.30           C  
ANISOU 1827  CB  ARG A 275     4864   5232   4836    459   -179   -289       C  
ATOM   1828  CG  ARG A 275      11.132 -10.972 110.401  1.00 44.01           C  
ANISOU 1828  CG  ARG A 275     5452   5890   5381    482   -132   -263       C  
ATOM   1829  CD  ARG A 275      11.095 -11.678 109.083  1.00 51.94           C  
ANISOU 1829  CD  ARG A 275     6459   6957   6319    507   -150   -309       C  
ATOM   1830  NE  ARG A 275       9.720 -11.576 108.570  1.00 59.04           N  
ANISOU 1830  NE  ARG A 275     7362   7887   7184    504   -181   -288       N  
ATOM   1831  CZ  ARG A 275       9.351 -11.838 107.313  1.00 60.96           C  
ANISOU 1831  CZ  ARG A 275     7606   8202   7355    524   -198   -309       C  
ATOM   1832  NH1 ARG A 275      10.268 -12.241 106.419  1.00 63.94           N  
ANISOU 1832  NH1 ARG A 275     7981   8631   7683    549   -181   -355       N  
ATOM   1833  NH2 ARG A 275       8.076 -11.704 106.959  1.00 57.17           N  
ANISOU 1833  NH2 ARG A 275     7124   7748   6850    520   -231   -286       N  
ATOM   1834  N   TRP A 276       8.190 -11.887 113.608  1.00 35.87           N  
ANISOU 1834  N   TRP A 276     4429   4716   4483    396   -234   -238       N  
ATOM   1835  CA  TRP A 276       7.305 -12.742 114.353  1.00 35.51           C  
ANISOU 1835  CA  TRP A 276     4385   4638   4468    367   -278   -250       C  
ATOM   1836  C   TRP A 276       7.588 -14.181 113.898  1.00 36.31           C  
ANISOU 1836  C   TRP A 276     4500   4728   4570    371   -321   -312       C  
ATOM   1837  O   TRP A 276       7.669 -14.447 112.700  1.00 35.51           O  
ANISOU 1837  O   TRP A 276     4401   4667   4426    395   -330   -344       O  
ATOM   1838  CB  TRP A 276       5.853 -12.388 114.017  1.00 34.97           C  
ANISOU 1838  CB  TRP A 276     4305   4599   4381    360   -294   -222       C  
ATOM   1839  CG  TRP A 276       5.420 -10.995 114.446  1.00 36.10           C  
ANISOU 1839  CG  TRP A 276     4434   4750   4533    361   -257   -164       C  
ATOM   1840  CD1 TRP A 276       5.070  -9.963 113.630  1.00 31.72           C  
ANISOU 1840  CD1 TRP A 276     3869   4235   3948    384   -235   -127       C  
ATOM   1841  CD2 TRP A 276       5.254 -10.514 115.813  1.00 34.15           C  
ANISOU 1841  CD2 TRP A 276     4178   4467   4330    338   -239   -140       C  
ATOM   1842  NE1 TRP A 276       4.723  -8.873 114.394  1.00 35.48           N  
ANISOU 1842  NE1 TRP A 276     4333   4693   4456    380   -206    -84       N  
ATOM   1843  CE2 TRP A 276       4.822  -9.178 115.727  1.00 34.77           C  
ANISOU 1843  CE2 TRP A 276     4243   4561   4408    352   -206    -96       C  
ATOM   1844  CE3 TRP A 276       5.422 -11.099 117.084  1.00 32.31           C  
ANISOU 1844  CE3 TRP A 276     3949   4194   4135    309   -249   -151       C  
ATOM   1845  CZ2 TRP A 276       4.565  -8.381 116.870  1.00 35.65           C  
ANISOU 1845  CZ2 TRP A 276     4341   4648   4557    339   -181    -74       C  
ATOM   1846  CZ3 TRP A 276       5.165 -10.331 118.215  1.00 38.17           C  
ANISOU 1846  CZ3 TRP A 276     4678   4922   4903    294   -224   -125       C  
ATOM   1847  CH2 TRP A 276       4.728  -8.964 118.099  1.00 35.20           C  
ANISOU 1847  CH2 TRP A 276     4286   4562   4528    310   -189    -92       C  
ATOM   1848  N   GLY A 277       7.722 -15.103 114.845  1.00 36.98           N  
ANISOU 1848  N   GLY A 277     4592   4757   4702    349   -350   -328       N  
ATOM   1849  CA  GLY A 277       8.029 -16.494 114.528  1.00 38.44           C  
ANISOU 1849  CA  GLY A 277     4789   4913   4903    353   -394   -388       C  
ATOM   1850  C   GLY A 277       9.476 -16.788 114.160  1.00 40.16           C  
ANISOU 1850  C   GLY A 277     5012   5127   5120    386   -379   -430       C  
ATOM   1851  O   GLY A 277       9.847 -17.955 114.066  1.00 41.27           O  
ANISOU 1851  O   GLY A 277     5162   5233   5288    393   -416   -482       O  
ATOM   1852  N   GLN A 278      10.316 -15.776 113.949  1.00 40.19           N  
ANISOU 1852  N   GLN A 278     5007   5164   5099    408   -327   -411       N  
ATOM   1853  CA  GLN A 278      11.732 -16.066 113.686  1.00 41.66           C  
ANISOU 1853  CA  GLN A 278     5190   5349   5289    438   -310   -452       C  
ATOM   1854  C   GLN A 278      12.463 -16.585 114.961  1.00 40.59           C  
ANISOU 1854  C   GLN A 278     5057   5150   5215    427   -324   -452       C  
ATOM   1855  O   GLN A 278      12.333 -15.996 116.009  1.00 41.06           O  
ANISOU 1855  O   GLN A 278     5113   5192   5296    403   -312   -404       O  
ATOM   1856  CB  GLN A 278      12.424 -14.837 113.151  1.00 42.11           C  
ANISOU 1856  CB  GLN A 278     5233   5459   5307    456   -250   -425       C  
ATOM   1857  CG  GLN A 278      13.907 -14.974 113.156  1.00 46.61           C  
ANISOU 1857  CG  GLN A 278     5792   6027   5890    480   -226   -456       C  
ATOM   1858  CD  GLN A 278      14.621 -13.667 112.885  1.00 51.80           C  
ANISOU 1858  CD  GLN A 278     6431   6726   6524    486   -162   -417       C  
ATOM   1859  OE1 GLN A 278      14.003 -12.605 112.770  1.00 51.27           O  
ANISOU 1859  OE1 GLN A 278     6364   6680   6437    473   -137   -363       O  
ATOM   1860  NE2 GLN A 278      15.955 -13.742 112.799  1.00 56.20           N  
ANISOU 1860  NE2 GLN A 278     6971   7291   7090    506   -137   -445       N  
ATOM   1861  N   PRO A 279      13.163 -17.729 114.885  1.00 39.87           N  
ANISOU 1861  N   PRO A 279     4970   5026   5154    446   -355   -506       N  
ATOM   1862  CA  PRO A 279      13.797 -18.255 116.097  1.00 38.28           C  
ANISOU 1862  CA  PRO A 279     4770   4764   5011    438   -375   -499       C  
ATOM   1863  C   PRO A 279      15.052 -17.484 116.438  1.00 37.75           C  
ANISOU 1863  C   PRO A 279     4684   4714   4945    454   -331   -488       C  
ATOM   1864  O   PRO A 279      15.700 -16.968 115.560  1.00 37.81           O  
ANISOU 1864  O   PRO A 279     4677   4770   4920    480   -292   -507       O  
ATOM   1865  CB  PRO A 279      14.173 -19.699 115.726  1.00 38.77           C  
ANISOU 1865  CB  PRO A 279     4841   4784   5108    462   -423   -565       C  
ATOM   1866  CG  PRO A 279      14.300 -19.708 114.278  1.00 40.35           C  
ANISOU 1866  CG  PRO A 279     5035   5037   5259    494   -408   -620       C  
ATOM   1867  CD  PRO A 279      13.239 -18.688 113.766  1.00 40.34           C  
ANISOU 1867  CD  PRO A 279     5034   5094   5199    475   -382   -579       C  
ATOM   1868  N   LEU A 280      15.361 -17.388 117.727  1.00 37.30           N  
ANISOU 1868  N   LEU A 280     4625   4623   4925    434   -338   -454       N  
ATOM   1869  CA  LEU A 280      16.496 -16.640 118.213  1.00 37.02           C  
ANISOU 1869  CA  LEU A 280     4568   4601   4897    442   -302   -443       C  
ATOM   1870  C   LEU A 280      16.764 -17.218 119.582  1.00 36.13           C  
ANISOU 1870  C   LEU A 280     4459   4439   4831    427   -339   -424       C  
ATOM   1871  O   LEU A 280      15.885 -17.892 120.177  1.00 35.73           O  
ANISOU 1871  O   LEU A 280     4427   4352   4797    401   -380   -403       O  
ATOM   1872  CB  LEU A 280      16.153 -15.165 118.330  1.00 37.43           C  
ANISOU 1872  CB  LEU A 280     4612   4690   4921    421   -252   -397       C  
ATOM   1873  CG  LEU A 280      14.851 -14.839 119.098  1.00 39.49           C  
ANISOU 1873  CG  LEU A 280     4885   4939   5180    383   -263   -351       C  
ATOM   1874  CD1 LEU A 280      15.175 -14.759 120.523  1.00 40.33           C  
ANISOU 1874  CD1 LEU A 280     4988   5020   5315    361   -272   -328       C  
ATOM   1875  CD2 LEU A 280      14.291 -13.508 118.678  1.00 42.32           C  
ANISOU 1875  CD2 LEU A 280     5238   5335   5507    375   -218   -319       C  
ATOM   1876  N   ARG A 281      17.982 -16.988 120.046  1.00 35.00           N  
ANISOU 1876  N   ARG A 281     4294   4298   4706    441   -325   -431       N  
ATOM   1877  CA  ARG A 281      18.404 -17.342 121.403  1.00 35.78           C  
ANISOU 1877  CA  ARG A 281     4391   4363   4841    428   -357   -408       C  
ATOM   1878  C   ARG A 281      18.311 -16.069 122.232  1.00 34.13           C  
ANISOU 1878  C   ARG A 281     4171   4182   4615    397   -322   -367       C  
ATOM   1879  O   ARG A 281      18.402 -14.932 121.699  1.00 34.28           O  
ANISOU 1879  O   ARG A 281     4177   4238   4608    396   -270   -366       O  
ATOM   1880  CB  ARG A 281      19.876 -17.904 121.419  1.00 36.20           C  
ANISOU 1880  CB  ARG A 281     4421   4404   4928    467   -370   -446       C  
ATOM   1881  CG  ARG A 281      19.961 -19.312 120.947  1.00 37.41           C  
ANISOU 1881  CG  ARG A 281     4585   4513   5114    498   -417   -485       C  
ATOM   1882  CD  ARG A 281      21.260 -20.126 121.359  1.00 41.53           C  
ANISOU 1882  CD  ARG A 281     5087   5004   5688    536   -450   -512       C  
ATOM   1883  NE  ARG A 281      22.061 -20.068 120.173  1.00 45.33           N  
ANISOU 1883  NE  ARG A 281     5544   5518   6160    579   -418   -574       N  
ATOM   1884  CZ  ARG A 281      22.550 -21.051 119.449  1.00 42.33           C  
ANISOU 1884  CZ  ARG A 281     5158   5117   5808    625   -439   -635       C  
ATOM   1885  NH1 ARG A 281      22.529 -22.340 119.785  1.00 37.43           N  
ANISOU 1885  NH1 ARG A 281     4553   4426   5244    643   -502   -649       N  
ATOM   1886  NH2 ARG A 281      23.154 -20.649 118.365  1.00 43.73           N  
ANISOU 1886  NH2 ARG A 281     5310   5349   5956    654   -392   -683       N  
ATOM   1887  N   ILE A 282      18.158 -16.245 123.533  1.00 33.41           N  
ANISOU 1887  N   ILE A 282     4084   4072   4536    372   -349   -335       N  
ATOM   1888  CA  ILE A 282      18.001 -15.098 124.440  1.00 32.60           C  
ANISOU 1888  CA  ILE A 282     3973   3997   4418    341   -320   -305       C  
ATOM   1889  C   ILE A 282      19.070 -15.242 125.491  1.00 32.95           C  
ANISOU 1889  C   ILE A 282     3999   4037   4482    344   -341   -304       C  
ATOM   1890  O   ILE A 282      19.015 -16.146 126.336  1.00 34.32           O  
ANISOU 1890  O   ILE A 282     4184   4187   4670    337   -389   -283       O  
ATOM   1891  CB  ILE A 282      16.579 -15.067 125.040  1.00 32.96           C  
ANISOU 1891  CB  ILE A 282     4038   4040   4445    304   -330   -266       C  
ATOM   1892  CG1 ILE A 282      15.530 -14.966 123.927  1.00 31.59           C  
ANISOU 1892  CG1 ILE A 282     3877   3873   4253    305   -316   -270       C  
ATOM   1893  CG2 ILE A 282      16.391 -13.932 126.065  1.00 31.43           C  
ANISOU 1893  CG2 ILE A 282     3832   3874   4234    276   -302   -245       C  
ATOM   1894  CD1 ILE A 282      14.049 -15.015 124.476  1.00 35.65           C  
ANISOU 1894  CD1 ILE A 282     4404   4387   4753    269   -327   -233       C  
ATOM   1895  N   ARG A 283      20.083 -14.397 125.391  1.00 32.94           N  
ANISOU 1895  N   ARG A 283     3969   4061   4484    354   -307   -325       N  
ATOM   1896  CA  ARG A 283      21.274 -14.506 126.220  1.00 33.27           C  
ANISOU 1896  CA  ARG A 283     3986   4107   4548    361   -326   -334       C  
ATOM   1897  C   ARG A 283      21.167 -13.554 127.411  1.00 34.04           C  
ANISOU 1897  C   ARG A 283     4075   4229   4630    326   -315   -315       C  
ATOM   1898  O   ARG A 283      20.857 -12.333 127.239  1.00 35.29           O  
ANISOU 1898  O   ARG A 283     4226   4408   4775    308   -267   -317       O  
ATOM   1899  CB  ARG A 283      22.475 -14.076 125.394  1.00 32.99           C  
ANISOU 1899  CB  ARG A 283     3917   4090   4527    389   -292   -372       C  
ATOM   1900  CG  ARG A 283      23.813 -14.213 126.067  1.00 31.15           C  
ANISOU 1900  CG  ARG A 283     3649   3866   4322    403   -312   -389       C  
ATOM   1901  CD  ARG A 283      24.804 -13.367 125.371  1.00 31.09           C  
ANISOU 1901  CD  ARG A 283     3602   3887   4323    413   -263   -419       C  
ATOM   1902  NE  ARG A 283      26.093 -13.330 126.056  1.00 37.79           N  
ANISOU 1902  NE  ARG A 283     4409   4750   5199    421   -278   -437       N  
ATOM   1903  CZ  ARG A 283      27.101 -14.216 125.920  1.00 37.07           C  
ANISOU 1903  CZ  ARG A 283     4292   4654   5138    461   -308   -463       C  
ATOM   1904  NH1 ARG A 283      26.984 -15.287 125.151  1.00 38.13           N  
ANISOU 1904  NH1 ARG A 283     4441   4764   5283    498   -327   -479       N  
ATOM   1905  NH2 ARG A 283      28.220 -14.043 126.603  1.00 34.60           N  
ANISOU 1905  NH2 ARG A 283     3936   4361   4850    464   -322   -476       N  
ATOM   1906  N   HIS A 284      21.467 -14.062 128.602  1.00 33.41           N  
ANISOU 1906  N   HIS A 284     3993   4150   4553    318   -358   -298       N  
ATOM   1907  CA  HIS A 284      21.530 -13.210 129.766  1.00 33.44           C  
ANISOU 1907  CA  HIS A 284     3983   4185   4537    287   -351   -291       C  
ATOM   1908  C   HIS A 284      22.847 -12.452 129.781  1.00 33.81           C  
ANISOU 1908  C   HIS A 284     3989   4254   4604    296   -331   -327       C  
ATOM   1909  O   HIS A 284      23.930 -13.067 129.800  1.00 35.00           O  
ANISOU 1909  O   HIS A 284     4118   4401   4779    322   -359   -341       O  
ATOM   1910  CB  HIS A 284      21.358 -14.009 131.042  1.00 34.22           C  
ANISOU 1910  CB  HIS A 284     4093   4288   4621    273   -405   -256       C  
ATOM   1911  CG  HIS A 284      21.367 -13.157 132.275  1.00 34.68           C  
ANISOU 1911  CG  HIS A 284     4138   4390   4649    242   -399   -254       C  
ATOM   1912  ND1 HIS A 284      20.221 -12.569 132.788  1.00 34.20           N  
ANISOU 1912  ND1 HIS A 284     4091   4351   4552    209   -377   -240       N  
ATOM   1913  CD2 HIS A 284      22.383 -12.747 133.062  1.00 32.46           C  
ANISOU 1913  CD2 HIS A 284     3826   4140   4367    240   -410   -274       C  
ATOM   1914  CE1 HIS A 284      20.537 -11.842 133.843  1.00 31.30           C  
ANISOU 1914  CE1 HIS A 284     3705   4026   4163    189   -374   -254       C  
ATOM   1915  NE2 HIS A 284      21.844 -11.915 134.018  1.00 33.24           N  
ANISOU 1915  NE2 HIS A 284     3924   4278   4429    205   -395   -275       N  
ATOM   1916  N   VAL A 285      22.796 -11.126 129.801  1.00 33.44           N  
ANISOU 1916  N   VAL A 285     3928   4226   4551    274   -284   -343       N  
ATOM   1917  CA  VAL A 285      24.043 -10.366 129.613  1.00 33.44           C  
ANISOU 1917  CA  VAL A 285     3886   4241   4579    278   -259   -377       C  
ATOM   1918  C   VAL A 285      25.051 -10.561 130.705  1.00 34.86           C  
ANISOU 1918  C   VAL A 285     4036   4443   4765    276   -298   -390       C  
ATOM   1919  O   VAL A 285      26.151 -10.995 130.423  1.00 36.25           O  
ANISOU 1919  O   VAL A 285     4183   4621   4969    302   -313   -408       O  
ATOM   1920  CB  VAL A 285      23.854  -8.870 129.290  1.00 33.76           C  
ANISOU 1920  CB  VAL A 285     3915   4286   4625    254   -199   -391       C  
ATOM   1921  CG1 VAL A 285      25.228  -8.150 129.082  1.00 29.69           C  
ANISOU 1921  CG1 VAL A 285     3351   3783   4146    253   -175   -424       C  
ATOM   1922  CG2 VAL A 285      22.992  -8.723 128.059  1.00 31.90           C  
ANISOU 1922  CG2 VAL A 285     3705   4033   4384    263   -163   -374       C  
ATOM   1923  N   THR A 286      24.711 -10.308 131.958  1.00 35.50           N  
ANISOU 1923  N   THR A 286     4122   4547   4819    249   -319   -383       N  
ATOM   1924  CA  THR A 286      25.797 -10.307 132.945  1.00 36.38           C  
ANISOU 1924  CA  THR A 286     4198   4691   4935    246   -354   -401       C  
ATOM   1925  C   THR A 286      26.343 -11.690 133.261  1.00 38.09           C  
ANISOU 1925  C   THR A 286     4414   4903   5157    277   -418   -378       C  
ATOM   1926  O   THR A 286      27.421 -11.793 133.824  1.00 39.48           O  
ANISOU 1926  O   THR A 286     4553   5102   5344    286   -449   -394       O  
ATOM   1927  CB  THR A 286      25.456  -9.560 134.292  1.00 35.59           C  
ANISOU 1927  CB  THR A 286     4096   4630   4798    208   -361   -410       C  
ATOM   1928  OG1 THR A 286      24.524 -10.350 135.046  1.00 33.76           O  
ANISOU 1928  OG1 THR A 286     3898   4408   4521    201   -396   -366       O  
ATOM   1929  CG2 THR A 286      24.927  -8.185 134.043  1.00 33.53           C  
ANISOU 1929  CG2 THR A 286     3834   4365   4543    182   -302   -437       C  
ATOM   1930  N   THR A 287      25.599 -12.742 132.983  1.00 39.06           N  
ANISOU 1930  N   THR A 287     4574   4994   5272    292   -441   -341       N  
ATOM   1931  CA  THR A 287      26.114 -14.068 133.299  1.00 41.07           C  
ANISOU 1931  CA  THR A 287     4829   5233   5543    322   -505   -316       C  
ATOM   1932  C   THR A 287      26.482 -14.846 132.038  1.00 42.52           C  
ANISOU 1932  C   THR A 287     5012   5373   5770    366   -503   -330       C  
ATOM   1933  O   THR A 287      27.094 -15.877 132.125  1.00 44.10           O  
ANISOU 1933  O   THR A 287     5205   5553   5998    400   -552   -322       O  
ATOM   1934  CB  THR A 287      25.107 -14.959 134.085  1.00 41.20           C  
ANISOU 1934  CB  THR A 287     4887   5239   5527    307   -548   -257       C  
ATOM   1935  OG1 THR A 287      23.914 -15.111 133.320  1.00 43.04           O  
ANISOU 1935  OG1 THR A 287     5157   5440   5756    299   -521   -243       O  
ATOM   1936  CG2 THR A 287      24.784 -14.406 135.461  1.00 40.04           C  
ANISOU 1936  CG2 THR A 287     4739   5147   5327    268   -558   -240       C  
ATOM   1937  N   GLY A 288      26.078 -14.379 130.864  1.00 43.13           N  
ANISOU 1937  N   GLY A 288     5098   5437   5853    367   -449   -352       N  
ATOM   1938  CA  GLY A 288      26.395 -15.089 129.644  1.00 43.43           C  
ANISOU 1938  CA  GLY A 288     5134   5444   5923    409   -445   -373       C  
ATOM   1939  C   GLY A 288      25.562 -16.339 129.473  1.00 43.63           C  
ANISOU 1939  C   GLY A 288     5202   5423   5953    422   -485   -344       C  
ATOM   1940  O   GLY A 288      25.840 -17.138 128.585  1.00 45.15           O  
ANISOU 1940  O   GLY A 288     5395   5585   6176    460   -494   -366       O  
ATOM   1941  N   ARG A 289      24.559 -16.570 130.303  1.00 42.46           N  
ANISOU 1941  N   ARG A 289     5087   5268   5777    390   -509   -298       N  
ATOM   1942  CA  ARG A 289      23.845 -17.842 130.116  1.00 42.44           C  
ANISOU 1942  CA  ARG A 289     5121   5214   5790    400   -551   -270       C  
ATOM   1943  C   ARG A 289      22.675 -17.685 129.173  1.00 41.84           C  
ANISOU 1943  C   ARG A 289     5074   5124   5699    386   -515   -274       C  
ATOM   1944  O   ARG A 289      22.276 -16.570 128.867  1.00 42.41           O  
ANISOU 1944  O   ARG A 289     5143   5228   5743    365   -463   -285       O  
ATOM   1945  CB  ARG A 289      23.436 -18.455 131.436  1.00 43.14           C  
ANISOU 1945  CB  ARG A 289     5229   5299   5865    376   -604   -209       C  
ATOM   1946  CG  ARG A 289      24.587 -18.534 132.434  1.00 44.68           C  
ANISOU 1946  CG  ARG A 289     5393   5519   6066    390   -642   -202       C  
ATOM   1947  CD  ARG A 289      24.300 -19.596 133.452  1.00 49.19           C  
ANISOU 1947  CD  ARG A 289     5986   6068   6636    382   -708   -136       C  
ATOM   1948  NE  ARG A 289      25.506 -19.794 134.231  1.00 55.41           N  
ANISOU 1948  NE  ARG A 289     6740   6876   7436    405   -752   -130       N  
ATOM   1949  CZ  ARG A 289      25.708 -19.398 135.486  1.00 52.62           C  
ANISOU 1949  CZ  ARG A 289     6375   6579   7039    381   -772   -102       C  
ATOM   1950  NH1 ARG A 289      24.760 -18.837 136.207  1.00 48.40           N  
ANISOU 1950  NH1 ARG A 289     5860   6086   6444    331   -752    -73       N  
ATOM   1951  NH2 ARG A 289      26.875 -19.641 136.025  1.00 53.37           N  
ANISOU 1951  NH2 ARG A 289     6437   6691   7152    409   -816   -102       N  
ATOM   1952  N   TYR A 290      22.147 -18.788 128.673  1.00 40.95           N  
ANISOU 1952  N   TYR A 290     4988   4962   5609    400   -546   -267       N  
ATOM   1953  CA  TYR A 290      21.143 -18.745 127.625  1.00 39.53           C  
ANISOU 1953  CA  TYR A 290     4831   4771   5418    393   -519   -280       C  
ATOM   1954  C   TYR A 290      19.821 -19.274 128.113  1.00 39.36           C  
ANISOU 1954  C   TYR A 290     4843   4726   5385    356   -545   -231       C  
ATOM   1955  O   TYR A 290      19.782 -20.339 128.720  1.00 39.78           O  
ANISOU 1955  O   TYR A 290     4910   4739   5465    354   -599   -198       O  
ATOM   1956  CB  TYR A 290      21.640 -19.540 126.424  1.00 39.29           C  
ANISOU 1956  CB  TYR A 290     4797   4706   5424    440   -528   -329       C  
ATOM   1957  CG  TYR A 290      22.644 -18.739 125.657  1.00 38.63           C  
ANISOU 1957  CG  TYR A 290     4679   4664   5337    468   -480   -378       C  
ATOM   1958  CD1 TYR A 290      24.002 -18.686 126.043  1.00 35.24           C  
ANISOU 1958  CD1 TYR A 290     4212   4248   4931    494   -487   -396       C  
ATOM   1959  CD2 TYR A 290      22.227 -17.979 124.566  1.00 37.47           C  
ANISOU 1959  CD2 TYR A 290     4532   4545   5159    465   -425   -401       C  
ATOM   1960  CE1 TYR A 290      24.901 -17.899 125.313  1.00 36.04           C  
ANISOU 1960  CE1 TYR A 290     4276   4390   5029    512   -437   -438       C  
ATOM   1961  CE2 TYR A 290      23.108 -17.210 123.851  1.00 36.60           C  
ANISOU 1961  CE2 TYR A 290     4389   4474   5041    484   -377   -436       C  
ATOM   1962  CZ  TYR A 290      24.426 -17.155 124.229  1.00 36.79           C  
ANISOU 1962  CZ  TYR A 290     4376   4512   5092    505   -380   -454       C  
ATOM   1963  OH  TYR A 290      25.221 -16.335 123.482  1.00 36.41           O  
ANISOU 1963  OH  TYR A 290     4292   4507   5037    517   -327   -485       O  
ATOM   1964  N   LEU A 291      18.750 -18.516 127.899  1.00 38.48           N  
ANISOU 1964  N   LEU A 291     4743   4641   5238    324   -506   -222       N  
ATOM   1965  CA  LEU A 291      17.396 -19.010 128.217  1.00 38.85           C  
ANISOU 1965  CA  LEU A 291     4816   4671   5275    287   -526   -180       C  
ATOM   1966  C   LEU A 291      17.178 -20.372 127.554  1.00 39.44           C  
ANISOU 1966  C   LEU A 291     4911   4682   5394    303   -570   -188       C  
ATOM   1967  O   LEU A 291      17.485 -20.546 126.378  1.00 39.56           O  
ANISOU 1967  O   LEU A 291     4923   4683   5425    337   -562   -239       O  
ATOM   1968  CB  LEU A 291      16.335 -18.005 127.721  1.00 38.06           C  
ANISOU 1968  CB  LEU A 291     4717   4606   5138    265   -475   -184       C  
ATOM   1969  CG  LEU A 291      14.944 -18.192 128.371  1.00 40.27           C  
ANISOU 1969  CG  LEU A 291     5013   4890   5398    218   -485   -135       C  
ATOM   1970  CD1 LEU A 291      14.968 -17.874 129.919  1.00 35.04           C  
ANISOU 1970  CD1 LEU A 291     4344   4262   4709    187   -489    -93       C  
ATOM   1971  CD2 LEU A 291      13.788 -17.460 127.612  1.00 35.49           C  
ANISOU 1971  CD2 LEU A 291     4408   4308   4769    205   -445   -144       C  
ATOM   1972  N   ALA A 292      16.686 -21.353 128.297  1.00 40.72           N  
ANISOU 1972  N   ALA A 292     5091   4806   5577    279   -619   -139       N  
ATOM   1973  CA  ALA A 292      16.555 -22.706 127.752  1.00 41.39           C  
ANISOU 1973  CA  ALA A 292     5193   4816   5715    294   -668   -148       C  
ATOM   1974  C   ALA A 292      15.418 -23.517 128.336  1.00 42.38           C  
ANISOU 1974  C   ALA A 292     5342   4906   5855    246   -704    -89       C  
ATOM   1975  O   ALA A 292      15.031 -23.300 129.475  1.00 42.06           O  
ANISOU 1975  O   ALA A 292     5302   4894   5786    207   -705    -27       O  
ATOM   1976  CB  ALA A 292      17.867 -23.459 127.969  1.00 43.15           C  
ANISOU 1976  CB  ALA A 292     5408   4999   5987    338   -709   -160       C  
ATOM   1977  N   LEU A 293      14.904 -24.475 127.556  1.00 44.34           N  
ANISOU 1977  N   LEU A 293     5606   5093   6146    248   -735   -109       N  
ATOM   1978  CA  LEU A 293      14.073 -25.562 128.075  1.00 46.51           C  
ANISOU 1978  CA  LEU A 293     5902   5310   6460    207   -784    -53       C  
ATOM   1979  C   LEU A 293      14.961 -26.783 128.301  1.00 49.23           C  
ANISOU 1979  C   LEU A 293     6256   5573   6878    238   -846    -46       C  
ATOM   1980  O   LEU A 293      15.711 -27.181 127.433  1.00 50.07           O  
ANISOU 1980  O   LEU A 293     6359   5642   7023    290   -858   -113       O  
ATOM   1981  CB  LEU A 293      12.989 -25.968 127.095  1.00 46.36           C  
ANISOU 1981  CB  LEU A 293     5893   5263   6458    188   -788    -83       C  
ATOM   1982  CG  LEU A 293      12.202 -27.235 127.475  1.00 46.13           C  
ANISOU 1982  CG  LEU A 293     5884   5158   6487    145   -844    -33       C  
ATOM   1983  CD1 LEU A 293      11.507 -27.080 128.827  1.00 44.98           C  
ANISOU 1983  CD1 LEU A 293     5737   5045   6310     85   -841     64       C  
ATOM   1984  CD2 LEU A 293      11.189 -27.579 126.398  1.00 44.57           C  
ANISOU 1984  CD2 LEU A 293     5691   4937   6306    129   -849    -78       C  
ATOM   1985  N   THR A 294      14.837 -27.391 129.458  1.00 51.95           N  
ANISOU 1985  N   THR A 294     6610   5890   7238    207   -884     37       N  
ATOM   1986  CA  THR A 294      15.722 -28.467 129.896  1.00 55.01           C  
ANISOU 1986  CA  THR A 294     7004   6202   7693    237   -947     62       C  
ATOM   1987  C   THR A 294      14.850 -29.616 130.389  1.00 57.34           C  
ANISOU 1987  C   THR A 294     7324   6423   8040    188   -998    136       C  
ATOM   1988  O   THR A 294      13.866 -29.375 131.092  1.00 57.90           O  
ANISOU 1988  O   THR A 294     7398   6532   8068    126   -983    203       O  
ATOM   1989  CB  THR A 294      16.583 -27.887 131.015  1.00 54.82           C  
ANISOU 1989  CB  THR A 294     6965   6238   7628    246   -942    106       C  
ATOM   1990  OG1 THR A 294      17.919 -27.724 130.553  1.00 55.07           O  
ANISOU 1990  OG1 THR A 294     6976   6269   7678    313   -941     41       O  
ATOM   1991  CG2 THR A 294      16.564 -28.682 132.197  1.00 54.67           C  
ANISOU 1991  CG2 THR A 294     6958   6185   7629    220   -994    202       C  
ATOM   1992  N   GLU A 295      15.179 -30.850 130.020  1.00 60.04           N  
ANISOU 1992  N   GLU A 295     7680   6658   8475    215  -1057    122       N  
ATOM   1993  CA  GLU A 295      14.339 -32.011 130.411  1.00 62.67           C  
ANISOU 1993  CA  GLU A 295     8035   6904   8871    165  -1109    193       C  
ATOM   1994  C   GLU A 295      14.212 -32.224 131.933  1.00 64.03           C  
ANISOU 1994  C   GLU A 295     8214   7089   9024    119  -1133    322       C  
ATOM   1995  O   GLU A 295      13.117 -32.511 132.455  1.00 64.59           O  
ANISOU 1995  O   GLU A 295     8295   7157   9090     49  -1137    397       O  
ATOM   1996  CB  GLU A 295      14.808 -33.310 129.714  1.00 63.70           C  
ANISOU 1996  CB  GLU A 295     8181   6906   9118    207  -1171    147       C  
ATOM   1997  N   ASP A 296      15.319 -32.054 132.646  1.00 65.24           N  
ANISOU 1997  N   ASP A 296     8358   7268   9163    157  -1146    348       N  
ATOM   1998  CA  ASP A 296      15.335 -32.362 134.068  1.00 66.99           C  
ANISOU 1998  CA  ASP A 296     8586   7502   9366    122  -1177    470       C  
ATOM   1999  C   ASP A 296      14.733 -31.259 134.935  1.00 66.85           C  
ANISOU 1999  C   ASP A 296     8555   7611   9232     70  -1122    517       C  
ATOM   2000  O   ASP A 296      13.984 -31.558 135.869  1.00 68.67           O  
ANISOU 2000  O   ASP A 296     8795   7857   9440      8  -1133    618       O  
ATOM   2001  CB  ASP A 296      16.747 -32.748 134.536  1.00 67.94           C  
ANISOU 2001  CB  ASP A 296     8699   7594   9521    185  -1226    486       C  
ATOM   2002  N   GLN A 297      15.008 -29.999 134.581  1.00 65.47           N  
ANISOU 2002  N   GLN A 297     8360   7526   8989     93  -1062    443       N  
ATOM   2003  CA  GLN A 297      14.745 -28.808 135.405  1.00 64.06           C  
ANISOU 2003  CA  GLN A 297     8165   7472   8705     61  -1010    466       C  
ATOM   2004  C   GLN A 297      13.708 -27.815 134.807  1.00 61.86           C  
ANISOU 2004  C   GLN A 297     7876   7254   8373     31   -941    415       C  
ATOM   2005  O   GLN A 297      13.445 -26.771 135.424  1.00 61.83           O  
ANISOU 2005  O   GLN A 297     7857   7348   8286      8   -894    423       O  
ATOM   2006  CB  GLN A 297      16.079 -28.045 135.626  1.00 64.26           C  
ANISOU 2006  CB  GLN A 297     8168   7552   8697    116  -1000    423       C  
ATOM   2007  CG  GLN A 297      16.905 -28.326 136.909  1.00 69.11           C  
ANISOU 2007  CG  GLN A 297     8778   8190   9292    123  -1045    499       C  
ATOM   2008  CD  GLN A 297      16.985 -27.080 137.874  1.00 76.09           C  
ANISOU 2008  CD  GLN A 297     9640   9204  10067    101  -1002    508       C  
ATOM   2009  OE1 GLN A 297      18.067 -26.456 138.050  1.00 75.00           O  
ANISOU 2009  OE1 GLN A 297     9479   9111   9907    141   -998    466       O  
ATOM   2010  NE2 GLN A 297      15.825 -26.708 138.475  1.00 76.49           N  
ANISOU 2010  NE2 GLN A 297     9695   9316  10053     37   -968    554       N  
ATOM   2011  N   GLY A 298      13.150 -28.081 133.619  1.00 59.50           N  
ANISOU 2011  N   GLY A 298     7585   6903   8120     35   -935    358       N  
ATOM   2012  CA  GLY A 298      12.216 -27.124 132.984  1.00 55.59           C  
ANISOU 2012  CA  GLY A 298     7078   6467   7578     14   -874    309       C  
ATOM   2013  C   GLY A 298      12.884 -25.875 132.386  1.00 53.38           C  
ANISOU 2013  C   GLY A 298     6780   6248   7255     60   -823    226       C  
ATOM   2014  O   GLY A 298      13.989 -25.980 131.812  1.00 53.63           O  
ANISOU 2014  O   GLY A 298     6809   6249   7320    117   -835    172       O  
ATOM   2015  N   LEU A 299      12.235 -24.701 132.503  1.00 50.31           N  
ANISOU 2015  N   LEU A 299     6376   5942   6798     37   -764    215       N  
ATOM   2016  CA  LEU A 299      12.835 -23.413 132.065  1.00 47.63           C  
ANISOU 2016  CA  LEU A 299     6018   5661   6419     74   -713    147       C  
ATOM   2017  C   LEU A 299      13.971 -22.917 132.970  1.00 46.81           C  
ANISOU 2017  C   LEU A 299     5901   5599   6285     94   -713    156       C  
ATOM   2018  O   LEU A 299      13.774 -22.578 134.136  1.00 46.45           O  
ANISOU 2018  O   LEU A 299     5849   5609   6190     62   -706    204       O  
ATOM   2019  CB  LEU A 299      11.794 -22.294 131.991  1.00 47.18           C  
ANISOU 2019  CB  LEU A 299     5948   5673   6307     45   -655    136       C  
ATOM   2020  CG  LEU A 299      12.308 -20.913 131.535  1.00 45.99           C  
ANISOU 2020  CG  LEU A 299     5779   5575   6122     77   -601     74       C  
ATOM   2021  CD1 LEU A 299      12.700 -20.949 130.092  1.00 43.60           C  
ANISOU 2021  CD1 LEU A 299     5479   5236   5853    120   -596      9       C  
ATOM   2022  CD2 LEU A 299      11.302 -19.788 131.776  1.00 44.90           C  
ANISOU 2022  CD2 LEU A 299     5625   5504   5931     48   -548     75       C  
ATOM   2023  N   VAL A 300      15.160 -22.839 132.420  1.00 45.29           N  
ANISOU 2023  N   VAL A 300     5701   5388   6120    147   -718    103       N  
ATOM   2024  CA  VAL A 300      16.263 -22.339 133.193  1.00 45.09           C  
ANISOU 2024  CA  VAL A 300     5657   5403   6070    166   -719    103       C  
ATOM   2025  C   VAL A 300      17.137 -21.496 132.293  1.00 43.91           C  
ANISOU 2025  C   VAL A 300     5487   5270   5925    211   -682     24       C  
ATOM   2026  O   VAL A 300      16.795 -21.212 131.140  1.00 43.90           O  
ANISOU 2026  O   VAL A 300     5488   5258   5934    223   -651    -24       O  
ATOM   2027  CB  VAL A 300      17.133 -23.487 133.802  1.00 45.81           C  
ANISOU 2027  CB  VAL A 300     5754   5446   6205    187   -788    146       C  
ATOM   2028  CG1 VAL A 300      16.325 -24.345 134.735  1.00 47.17           C  
ANISOU 2028  CG1 VAL A 300     5947   5601   6374    140   -826    238       C  
ATOM   2029  CG2 VAL A 300      17.714 -24.347 132.702  1.00 46.60           C  
ANISOU 2029  CG2 VAL A 300     5860   5464   6382    236   -817    100       C  
ATOM   2030  N   VAL A 301      18.286 -21.130 132.821  1.00 42.52           N  
ANISOU 2030  N   VAL A 301     5290   5122   5742    234   -688     13       N  
ATOM   2031  CA  VAL A 301      19.270 -20.465 132.037  1.00 41.93           C  
ANISOU 2031  CA  VAL A 301     5192   5059   5680    275   -658    -56       C  
ATOM   2032  C   VAL A 301      20.537 -21.343 132.047  1.00 42.31           C  
ANISOU 2032  C   VAL A 301     5229   5068   5780    321   -708    -64       C  
ATOM   2033  O   VAL A 301      20.899 -21.924 133.063  1.00 42.54           O  
ANISOU 2033  O   VAL A 301     5258   5092   5813    319   -757    -15       O  
ATOM   2034  CB  VAL A 301      19.404 -19.037 132.575  1.00 41.30           C  
ANISOU 2034  CB  VAL A 301     5091   5055   5548    255   -610    -72       C  
ATOM   2035  CG1 VAL A 301      20.785 -18.674 132.860  1.00 42.53           C  
ANISOU 2035  CG1 VAL A 301     5214   5232   5711    283   -616   -100       C  
ATOM   2036  CG2 VAL A 301      18.760 -18.073 131.613  1.00 39.72           C  
ANISOU 2036  CG2 VAL A 301     4889   4869   5332    249   -549   -111       C  
ATOM   2037  N   VAL A 302      21.199 -21.448 130.911  1.00 42.25           N  
ANISOU 2037  N   VAL A 302     5209   5034   5810    366   -697   -125       N  
ATOM   2038  CA  VAL A 302      22.130 -22.552 130.685  1.00 43.33           C  
ANISOU 2038  CA  VAL A 302     5339   5115   6010    415   -748   -138       C  
ATOM   2039  C   VAL A 302      23.499 -22.076 130.179  1.00 43.92           C  
ANISOU 2039  C   VAL A 302     5372   5214   6101    463   -727   -201       C  
ATOM   2040  O   VAL A 302      23.576 -21.104 129.457  1.00 43.40           O  
ANISOU 2040  O   VAL A 302     5291   5188   6010    462   -669   -246       O  
ATOM   2041  CB  VAL A 302      21.425 -23.539 129.730  1.00 43.76           C  
ANISOU 2041  CB  VAL A 302     5422   5099   6108    425   -766   -153       C  
ATOM   2042  CG1 VAL A 302      22.135 -23.732 128.424  1.00 44.02           C  
ANISOU 2042  CG1 VAL A 302     5439   5111   6177    479   -752   -233       C  
ATOM   2043  CG2 VAL A 302      21.063 -24.782 130.435  1.00 43.21           C  
ANISOU 2043  CG2 VAL A 302     5378   4964   6077    413   -833    -89       C  
ATOM   2044  N   ASP A 303      24.584 -22.728 130.564  1.00 45.54           N  
ANISOU 2044  N   ASP A 303     5555   5399   6347    502   -774   -200       N  
ATOM   2045  CA  ASP A 303      25.884 -22.347 129.992  1.00 47.11           C  
ANISOU 2045  CA  ASP A 303     5708   5623   6568    549   -753   -264       C  
ATOM   2046  C   ASP A 303      25.901 -22.468 128.460  1.00 46.92           C  
ANISOU 2046  C   ASP A 303     5682   5580   6566    582   -717   -334       C  
ATOM   2047  O   ASP A 303      25.276 -23.402 127.870  1.00 45.94           O  
ANISOU 2047  O   ASP A 303     5588   5395   6471    592   -740   -340       O  
ATOM   2048  CB  ASP A 303      27.028 -23.207 130.563  1.00 48.71           C  
ANISOU 2048  CB  ASP A 303     5885   5799   6823    595   -817   -255       C  
ATOM   2049  CG  ASP A 303      27.342 -22.898 132.018  1.00 53.20           C  
ANISOU 2049  CG  ASP A 303     6442   6411   7361    571   -848   -198       C  
ATOM   2050  OD1 ASP A 303      27.104 -21.747 132.485  1.00 55.77           O  
ANISOU 2050  OD1 ASP A 303     6760   6803   7626    528   -808   -193       O  
ATOM   2051  OD2 ASP A 303      27.846 -23.821 132.710  1.00 59.83           O  
ANISOU 2051  OD2 ASP A 303     7278   7218   8237    597   -917   -158       O  
ATOM   2052  N   ALA A 304      26.656 -21.560 127.834  1.00 46.63           N  
ANISOU 2052  N   ALA A 304     5608   5595   6515    597   -663   -386       N  
ATOM   2053  CA  ALA A 304      26.844 -21.555 126.380  1.00 47.39           C  
ANISOU 2053  CA  ALA A 304     5693   5694   6620    629   -622   -453       C  
ATOM   2054  C   ALA A 304      27.214 -22.930 125.840  1.00 49.36           C  
ANISOU 2054  C   ALA A 304     5943   5879   6931    686   -668   -489       C  
ATOM   2055  O   ALA A 304      26.740 -23.349 124.769  1.00 49.66           O  
ANISOU 2055  O   ALA A 304     6000   5894   6975    701   -656   -531       O  
ATOM   2056  CB  ALA A 304      27.877 -20.542 125.967  1.00 46.08           C  
ANISOU 2056  CB  ALA A 304     5475   5591   6440    642   -567   -494       C  
ATOM   2057  N   CYS A 305      28.038 -23.656 126.568  1.00 50.72           N  
ANISOU 2057  N   CYS A 305     6096   6021   7153    718   -725   -476       N  
ATOM   2058  CA  CYS A 305      28.420 -24.946 126.033  1.00 54.16           C  
ANISOU 2058  CA  CYS A 305     6531   6389   7658    777   -769   -516       C  
ATOM   2059  C   CYS A 305      27.230 -25.935 125.987  1.00 53.86           C  
ANISOU 2059  C   CYS A 305     6550   6271   7644    760   -811   -489       C  
ATOM   2060  O   CYS A 305      27.221 -26.829 125.153  1.00 55.27           O  
ANISOU 2060  O   CYS A 305     6736   6396   7869    800   -830   -542       O  
ATOM   2061  CB  CYS A 305      29.659 -25.507 126.746  1.00 54.91           C  
ANISOU 2061  CB  CYS A 305     6586   6468   7810    825   -821   -511       C  
ATOM   2062  SG  CYS A 305      29.243 -25.861 128.446  1.00 60.51           S  
ANISOU 2062  SG  CYS A 305     7325   7148   8519    786   -892   -401       S  
ATOM   2063  N   LYS A 306      26.214 -25.736 126.820  1.00 53.56           N  
ANISOU 2063  N   LYS A 306     6549   6230   7572    699   -823   -413       N  
ATOM   2064  CA  LYS A 306      24.977 -26.533 126.747  1.00 53.56           C  
ANISOU 2064  CA  LYS A 306     6599   6164   7588    670   -854   -384       C  
ATOM   2065  C   LYS A 306      23.851 -25.908 125.878  1.00 52.41           C  
ANISOU 2065  C   LYS A 306     6475   6048   7388    632   -800   -406       C  
ATOM   2066  O   LYS A 306      22.711 -26.411 125.872  1.00 52.59           O  
ANISOU 2066  O   LYS A 306     6536   6028   7416    597   -820   -378       O  
ATOM   2067  CB  LYS A 306      24.453 -26.827 128.158  1.00 54.16           C  
ANISOU 2067  CB  LYS A 306     6699   6217   7661    625   -901   -283       C  
ATOM   2068  CG  LYS A 306      25.451 -27.568 129.069  1.00 60.00           C  
ANISOU 2068  CG  LYS A 306     7421   6922   8455    662   -967   -246       C  
ATOM   2069  CD  LYS A 306      25.391 -29.114 128.737  1.00 72.64           C  
ANISOU 2069  CD  LYS A 306     9044   8407  10151    699  -1033   -253       C  
ATOM   2070  CE  LYS A 306      26.688 -29.932 129.115  1.00 77.33           C  
ANISOU 2070  CE  LYS A 306     9607   8953  10821    768  -1094   -256       C  
ATOM   2071  NZ  LYS A 306      26.580 -31.354 128.598  1.00 79.89           N  
ANISOU 2071  NZ  LYS A 306     9952   9157  11245    808  -1151   -279       N  
ATOM   2072  N   ALA A 307      24.140 -24.833 125.143  1.00 50.67           N  
ANISOU 2072  N   ALA A 307     6231   5901   7119    637   -733   -452       N  
ATOM   2073  CA  ALA A 307      23.058 -24.070 124.530  1.00 49.97           C  
ANISOU 2073  CA  ALA A 307     6163   5851   6973    597   -683   -454       C  
ATOM   2074  C   ALA A 307      22.751 -24.457 123.065  1.00 50.46           C  
ANISOU 2074  C   ALA A 307     6232   5902   7038    623   -668   -527       C  
ATOM   2075  O   ALA A 307      22.771 -23.628 122.161  1.00 49.84           O  
ANISOU 2075  O   ALA A 307     6140   5884   6912    627   -610   -564       O  
ATOM   2076  CB  ALA A 307      23.278 -22.547 124.704  1.00 48.53           C  
ANISOU 2076  CB  ALA A 307     5956   5753   6728    572   -619   -443       C  
ATOM   2077  N   HIS A 308      22.449 -25.724 122.828  1.00 51.39           N  
ANISOU 2077  N   HIS A 308     6371   5943   7211    640   -721   -546       N  
ATOM   2078  CA  HIS A 308      22.174 -26.135 121.465  1.00 52.65           C  
ANISOU 2078  CA  HIS A 308     6537   6096   7373    666   -712   -624       C  
ATOM   2079  C   HIS A 308      20.816 -25.600 121.044  1.00 52.58           C  
ANISOU 2079  C   HIS A 308     6554   6116   7307    616   -685   -607       C  
ATOM   2080  O   HIS A 308      19.944 -25.378 121.892  1.00 53.05           O  
ANISOU 2080  O   HIS A 308     6635   6170   7354    562   -695   -534       O  
ATOM   2081  CB  HIS A 308      22.264 -27.660 121.292  1.00 53.11           C  
ANISOU 2081  CB  HIS A 308     6609   6055   7515    701   -779   -662       C  
ATOM   2082  CG  HIS A 308      21.472 -28.427 122.297  1.00 53.46           C  
ANISOU 2082  CG  HIS A 308     6688   6021   7605    659   -840   -587       C  
ATOM   2083  ND1 HIS A 308      20.156 -28.792 122.087  1.00 55.33           N  
ANISOU 2083  ND1 HIS A 308     6958   6225   7842    614   -857   -573       N  
ATOM   2084  CD2 HIS A 308      21.802 -28.887 123.527  1.00 54.20           C  
ANISOU 2084  CD2 HIS A 308     6783   6066   7742    653   -887   -517       C  
ATOM   2085  CE1 HIS A 308      19.707 -29.446 123.147  1.00 55.28           C  
ANISOU 2085  CE1 HIS A 308     6973   6152   7880    579   -909   -495       C  
ATOM   2086  NE2 HIS A 308      20.687 -29.512 124.038  1.00 56.64           N  
ANISOU 2086  NE2 HIS A 308     7129   6316   8076    602   -928   -458       N  
ATOM   2087  N   THR A 309      20.653 -25.436 119.732  1.00 52.82           N  
ANISOU 2087  N   THR A 309     6581   6184   7305    636   -653   -674       N  
ATOM   2088  CA  THR A 309      19.465 -24.887 119.086  1.00 53.65           C  
ANISOU 2088  CA  THR A 309     6704   6329   7352    599   -626   -670       C  
ATOM   2089  C   THR A 309      18.110 -25.277 119.665  1.00 53.31           C  
ANISOU 2089  C   THR A 309     6693   6241   7322    543   -664   -615       C  
ATOM   2090  O   THR A 309      17.266 -24.422 119.905  1.00 52.21           O  
ANISOU 2090  O   THR A 309     6560   6144   7135    500   -635   -566       O  
ATOM   2091  CB  THR A 309      19.527 -25.171 117.595  1.00 54.43           C  
ANISOU 2091  CB  THR A 309     6797   6452   7430    637   -612   -761       C  
ATOM   2092  OG1 THR A 309      20.609 -24.400 117.082  1.00 58.84           O  
ANISOU 2092  OG1 THR A 309     7321   7083   7952    673   -556   -791       O  
ATOM   2093  CG2 THR A 309      18.264 -24.718 116.860  1.00 55.28           C  
ANISOU 2093  CG2 THR A 309     6922   6602   7479    603   -594   -758       C  
ATOM   2094  N   LYS A 310      17.911 -26.562 119.901  1.00 53.98           N  
ANISOU 2094  N   LYS A 310     6796   6238   7477    545   -727   -623       N  
ATOM   2095  CA  LYS A 310      16.603 -27.045 120.311  1.00 53.83           C  
ANISOU 2095  CA  LYS A 310     6804   6174   7475    490   -763   -576       C  
ATOM   2096  C   LYS A 310      16.256 -26.649 121.739  1.00 51.42           C  
ANISOU 2096  C   LYS A 310     6505   5871   7163    440   -765   -475       C  
ATOM   2097  O   LYS A 310      15.113 -26.318 122.039  1.00 50.74           O  
ANISOU 2097  O   LYS A 310     6429   5802   7049    388   -758   -427       O  
ATOM   2098  CB  LYS A 310      16.542 -28.560 120.091  1.00 56.16           C  
ANISOU 2098  CB  LYS A 310     7116   6367   7856    505   -831   -617       C  
ATOM   2099  CG  LYS A 310      16.629 -28.917 118.576  1.00 62.99           C  
ANISOU 2099  CG  LYS A 310     7976   7241   8715    547   -828   -730       C  
ATOM   2100  CD  LYS A 310      16.679 -30.447 118.299  1.00 74.23           C  
ANISOU 2100  CD  LYS A 310     9413   8555  10234    570   -897   -788       C  
ATOM   2101  CE  LYS A 310      15.938 -30.826 116.974  1.00 77.68           C  
ANISOU 2101  CE  LYS A 310     9858   8999  10657    572   -906   -879       C  
ATOM   2102  NZ  LYS A 310      14.538 -30.232 116.965  1.00 79.78           N  
ANISOU 2102  NZ  LYS A 310    10135   9311  10869    505   -891   -829       N  
ATOM   2103  N   ALA A 311      17.258 -26.656 122.606  1.00 49.56           N  
ANISOU 2103  N   ALA A 311     6257   5624   6949    460   -774   -445       N  
ATOM   2104  CA  ALA A 311      17.068 -26.310 124.003  1.00 47.98           C  
ANISOU 2104  CA  ALA A 311     6060   5434   6736    418   -778   -354       C  
ATOM   2105  C   ALA A 311      16.737 -24.833 124.142  1.00 46.29           C  
ANISOU 2105  C   ALA A 311     5833   5312   6442    392   -713   -331       C  
ATOM   2106  O   ALA A 311      15.966 -24.432 125.019  1.00 45.53           O  
ANISOU 2106  O   ALA A 311     5744   5236   6319    342   -707   -266       O  
ATOM   2107  CB  ALA A 311      18.327 -26.594 124.781  1.00 47.58           C  
ANISOU 2107  CB  ALA A 311     5995   5362   6720    452   -802   -337       C  
ATOM   2108  N   THR A 312      17.280 -24.068 123.203  1.00 44.43           N  
ANISOU 2108  N   THR A 312     5580   5129   6173    425   -666   -388       N  
ATOM   2109  CA  THR A 312      17.588 -22.703 123.401  1.00 42.64           C  
ANISOU 2109  CA  THR A 312     5333   4975   5892    420   -609   -375       C  
ATOM   2110  C   THR A 312      16.931 -21.709 122.413  1.00 42.67           C  
ANISOU 2110  C   THR A 312     5335   5039   5840    412   -555   -397       C  
ATOM   2111  O   THR A 312      17.105 -20.527 122.559  1.00 42.94           O  
ANISOU 2111  O   THR A 312     5353   5126   5835    404   -508   -382       O  
ATOM   2112  CB  THR A 312      19.136 -22.699 123.442  1.00 42.94           C  
ANISOU 2112  CB  THR A 312     5345   5019   5952    468   -606   -407       C  
ATOM   2113  OG1 THR A 312      19.577 -22.148 124.672  1.00 45.24           O  
ANISOU 2113  OG1 THR A 312     5623   5332   6234    450   -603   -357       O  
ATOM   2114  CG2 THR A 312      19.826 -22.138 122.266  1.00 36.96           C  
ANISOU 2114  CG2 THR A 312     4564   4306   5171    507   -559   -471       C  
ATOM   2115  N   SER A 313      16.201 -22.198 121.399  1.00 43.18           N  
ANISOU 2115  N   SER A 313     5412   5091   5903    415   -566   -432       N  
ATOM   2116  CA  SER A 313      15.443 -21.362 120.447  1.00 42.69           C  
ANISOU 2116  CA  SER A 313     5349   5085   5786    407   -525   -445       C  
ATOM   2117  C   SER A 313      14.048 -20.996 120.895  1.00 41.18           C  
ANISOU 2117  C   SER A 313     5169   4905   5574    356   -524   -393       C  
ATOM   2118  O   SER A 313      13.224 -21.863 121.153  1.00 40.42           O  
ANISOU 2118  O   SER A 313     5088   4765   5506    329   -567   -379       O  
ATOM   2119  CB  SER A 313      15.274 -22.029 119.086  1.00 42.74           C  
ANISOU 2119  CB  SER A 313     5360   5086   5791    435   -539   -514       C  
ATOM   2120  OG  SER A 313      16.526 -22.113 118.503  1.00 46.24           O  
ANISOU 2120  OG  SER A 313     5787   5542   6239    485   -524   -568       O  
ATOM   2121  N   PHE A 314      13.794 -19.691 120.930  1.00 39.88           N  
ANISOU 2121  N   PHE A 314     4992   4797   5364    344   -474   -368       N  
ATOM   2122  CA  PHE A 314      12.470 -19.172 121.234  1.00 38.64           C  
ANISOU 2122  CA  PHE A 314     4838   4660   5182    304   -464   -325       C  
ATOM   2123  C   PHE A 314      12.095 -18.318 120.060  1.00 39.28           C  
ANISOU 2123  C   PHE A 314     4912   4793   5219    319   -427   -345       C  
ATOM   2124  O   PHE A 314      12.959 -18.069 119.178  1.00 39.83           O  
ANISOU 2124  O   PHE A 314     4975   4886   5273    356   -403   -383       O  
ATOM   2125  CB  PHE A 314      12.500 -18.331 122.521  1.00 37.21           C  
ANISOU 2125  CB  PHE A 314     4649   4498   4993    278   -440   -274       C  
ATOM   2126  CG  PHE A 314      12.843 -19.119 123.735  1.00 35.34           C  
ANISOU 2126  CG  PHE A 314     4418   4222   4789    261   -478   -245       C  
ATOM   2127  CD1 PHE A 314      14.171 -19.512 123.973  1.00 34.78           C  
ANISOU 2127  CD1 PHE A 314     4342   4128   4743    291   -492   -263       C  
ATOM   2128  CD2 PHE A 314      11.848 -19.511 124.619  1.00 35.07           C  
ANISOU 2128  CD2 PHE A 314     4390   4175   4759    216   -501   -197       C  
ATOM   2129  CE1 PHE A 314      14.508 -20.269 125.071  1.00 34.19           C  
ANISOU 2129  CE1 PHE A 314     4274   4018   4700    279   -533   -231       C  
ATOM   2130  CE2 PHE A 314      12.157 -20.268 125.753  1.00 36.29           C  
ANISOU 2130  CE2 PHE A 314     4553   4297   4940    199   -537   -160       C  
ATOM   2131  CZ  PHE A 314      13.516 -20.667 125.968  1.00 38.49           C  
ANISOU 2131  CZ  PHE A 314     4829   4550   5245    233   -556   -176       C  
ATOM   2132  N   CYS A 315      10.836 -17.861 120.035  1.00 38.24           N  
ANISOU 2132  N   CYS A 315     4780   4685   5066    291   -420   -316       N  
ATOM   2133  CA  CYS A 315      10.474 -16.829 119.122  1.00 38.20           C  
ANISOU 2133  CA  CYS A 315     4766   4733   5018    305   -381   -317       C  
ATOM   2134  C   CYS A 315       9.339 -15.968 119.692  1.00 38.37           C  
ANISOU 2134  C   CYS A 315     4778   4777   5025    274   -363   -269       C  
ATOM   2135  O   CYS A 315       8.664 -16.375 120.650  1.00 39.83           O  
ANISOU 2135  O   CYS A 315     4963   4941   5229    239   -384   -242       O  
ATOM   2136  CB  CYS A 315      10.085 -17.466 117.795  1.00 38.75           C  
ANISOU 2136  CB  CYS A 315     4842   4813   5070    322   -405   -361       C  
ATOM   2137  SG  CYS A 315       8.454 -18.280 117.849  1.00 38.57           S  
ANISOU 2137  SG  CYS A 315     4823   4771   5060    282   -454   -352       S  
ATOM   2138  N   PHE A 316       9.103 -14.814 119.077  1.00 37.17           N  
ANISOU 2138  N   PHE A 316     4615   4668   4841    288   -323   -257       N  
ATOM   2139  CA  PHE A 316       7.995 -13.924 119.435  1.00 36.01           C  
ANISOU 2139  CA  PHE A 316     4456   4544   4684    269   -304   -218       C  
ATOM   2140  C   PHE A 316       6.760 -14.235 118.582  1.00 36.11           C  
ANISOU 2140  C   PHE A 316     4465   4577   4678    265   -329   -221       C  
ATOM   2141  O   PHE A 316       6.865 -14.373 117.341  1.00 37.43           O  
ANISOU 2141  O   PHE A 316     4636   4768   4819    290   -335   -248       O  
ATOM   2142  CB  PHE A 316       8.446 -12.461 119.272  1.00 35.42           C  
ANISOU 2142  CB  PHE A 316     4370   4494   4595    288   -251   -201       C  
ATOM   2143  CG  PHE A 316       9.507 -12.057 120.272  1.00 36.18           C  
ANISOU 2143  CG  PHE A 316     4463   4572   4712    284   -228   -198       C  
ATOM   2144  CD1 PHE A 316       9.211 -11.976 121.631  1.00 37.43           C  
ANISOU 2144  CD1 PHE A 316     4617   4719   4888    256   -230   -180       C  
ATOM   2145  CD2 PHE A 316      10.809 -11.795 119.868  1.00 36.72           C  
ANISOU 2145  CD2 PHE A 316     4531   4642   4781    308   -206   -216       C  
ATOM   2146  CE1 PHE A 316      10.210 -11.647 122.582  1.00 37.91           C  
ANISOU 2146  CE1 PHE A 316     4673   4768   4963    251   -215   -183       C  
ATOM   2147  CE2 PHE A 316      11.790 -11.442 120.796  1.00 36.61           C  
ANISOU 2147  CE2 PHE A 316     4509   4613   4789    302   -189   -218       C  
ATOM   2148  CZ  PHE A 316      11.489 -11.386 122.165  1.00 36.62           C  
ANISOU 2148  CZ  PHE A 316     4507   4602   4805    274   -197   -202       C  
ATOM   2149  N   ARG A 317       5.597 -14.352 119.219  1.00 34.08           N  
ANISOU 2149  N   ARG A 317     4197   4320   4432    233   -344   -197       N  
ATOM   2150  CA  ARG A 317       4.364 -14.669 118.497  1.00 33.64           C  
ANISOU 2150  CA  ARG A 317     4132   4287   4364    224   -372   -199       C  
ATOM   2151  C   ARG A 317       3.326 -13.573 118.710  1.00 33.55           C  
ANISOU 2151  C   ARG A 317     4095   4310   4341    220   -346   -162       C  
ATOM   2152  O   ARG A 317       3.226 -12.976 119.805  1.00 32.87           O  
ANISOU 2152  O   ARG A 317     3998   4220   4269    205   -320   -136       O  
ATOM   2153  CB  ARG A 317       3.778 -15.996 119.000  1.00 33.78           C  
ANISOU 2153  CB  ARG A 317     4152   4269   4412    184   -420   -206       C  
ATOM   2154  CG  ARG A 317       4.648 -17.237 118.719  1.00 34.97           C  
ANISOU 2154  CG  ARG A 317     4327   4376   4585    190   -457   -247       C  
ATOM   2155  CD  ARG A 317       4.699 -17.629 117.200  1.00 30.88           C  
ANISOU 2155  CD  ARG A 317     3815   3875   4042    219   -478   -300       C  
ATOM   2156  NE  ARG A 317       3.345 -17.538 116.655  1.00 34.23           N  
ANISOU 2156  NE  ARG A 317     4222   4335   4450    204   -496   -294       N  
ATOM   2157  CZ  ARG A 317       2.438 -18.501 116.811  1.00 33.53           C  
ANISOU 2157  CZ  ARG A 317     4127   4222   4390    166   -542   -301       C  
ATOM   2158  NH1 ARG A 317       2.783 -19.594 117.446  1.00 33.05           N  
ANISOU 2158  NH1 ARG A 317     4080   4099   4377    142   -572   -310       N  
ATOM   2159  NH2 ARG A 317       1.207 -18.373 116.355  1.00 30.81           N  
ANISOU 2159  NH2 ARG A 317     3760   3915   4032    150   -558   -296       N  
ATOM   2160  N   VAL A 318       2.524 -13.325 117.683  1.00 32.77           N  
ANISOU 2160  N   VAL A 318     3984   4248   4218    234   -356   -162       N  
ATOM   2161  CA  VAL A 318       1.469 -12.335 117.795  1.00 31.35           C  
ANISOU 2161  CA  VAL A 318     3778   4101   4034    235   -337   -128       C  
ATOM   2162  C   VAL A 318       0.351 -12.872 118.706  1.00 32.83           C  
ANISOU 2162  C   VAL A 318     3943   4285   4246    192   -358   -116       C  
ATOM   2163  O   VAL A 318      -0.281 -12.101 119.422  1.00 33.27           O  
ANISOU 2163  O   VAL A 318     3974   4356   4310    186   -332    -89       O  
ATOM   2164  CB  VAL A 318       0.912 -11.947 116.360  1.00 32.48           C  
ANISOU 2164  CB  VAL A 318     3911   4290   4140    266   -348   -128       C  
ATOM   2165  CG1 VAL A 318      -0.272 -10.943 116.441  1.00 27.62           C  
ANISOU 2165  CG1 VAL A 318     3262   3707   3526    273   -335    -90       C  
ATOM   2166  CG2 VAL A 318       2.053 -11.460 115.399  1.00 28.99           C  
ANISOU 2166  CG2 VAL A 318     3489   3859   3665    305   -324   -134       C  
ATOM   2167  N   SER A 319       0.079 -14.181 118.647  1.00 33.29           N  
ANISOU 2167  N   SER A 319     4007   4324   4316    162   -403   -137       N  
ATOM   2168  CA  SER A 319      -0.998 -14.777 119.425  1.00 35.05           C  
ANISOU 2168  CA  SER A 319     4207   4546   4564    114   -424   -120       C  
ATOM   2169  C   SER A 319      -0.674 -16.245 119.687  1.00 37.20           C  
ANISOU 2169  C   SER A 319     4500   4769   4864     80   -466   -138       C  
ATOM   2170  O   SER A 319       0.336 -16.742 119.202  1.00 36.21           O  
ANISOU 2170  O   SER A 319     4405   4614   4740    100   -480   -170       O  
ATOM   2171  CB  SER A 319      -2.316 -14.658 118.690  1.00 34.37           C  
ANISOU 2171  CB  SER A 319     4088   4503   4468    112   -445   -119       C  
ATOM   2172  OG  SER A 319      -2.343 -15.617 117.650  1.00 36.49           O  
ANISOU 2172  OG  SER A 319     4368   4765   4731    110   -493   -157       O  
ATOM   2173  N   LYS A 320      -1.495 -16.921 120.488  1.00 40.15           N  
ANISOU 2173  N   LYS A 320     4856   5133   5265     29   -485   -117       N  
ATOM   2174  CA  LYS A 320      -1.221 -18.311 120.807  1.00 43.91           C  
ANISOU 2174  CA  LYS A 320     5353   5554   5778     -7   -527   -124       C  
ATOM   2175  C   LYS A 320      -1.919 -19.236 119.850  1.00 47.51           C  
ANISOU 2175  C   LYS A 320     5803   6000   6250    -24   -579   -157       C  
ATOM   2176  O   LYS A 320      -2.179 -20.355 120.193  1.00 48.94           O  
ANISOU 2176  O   LYS A 320     5987   6137   6472    -68   -617   -155       O  
ATOM   2177  CB  LYS A 320      -1.603 -18.694 122.239  1.00 42.56           C  
ANISOU 2177  CB  LYS A 320     5170   5370   5630    -59   -522    -76       C  
ATOM   2178  CG  LYS A 320      -1.042 -17.805 123.317  1.00 42.31           C  
ANISOU 2178  CG  LYS A 320     5140   5357   5579    -48   -473    -47       C  
ATOM   2179  CD  LYS A 320      -0.783 -18.560 124.634  1.00 39.92           C  
ANISOU 2179  CD  LYS A 320     4846   5025   5296    -92   -481     -8       C  
ATOM   2180  CE  LYS A 320      -0.565 -17.588 125.765  1.00 36.96           C  
ANISOU 2180  CE  LYS A 320     4460   4690   4892    -89   -431     18       C  
ATOM   2181  NZ  LYS A 320      -0.588 -18.213 127.104  1.00 33.43           N  
ANISOU 2181  NZ  LYS A 320     4013   4238   4450   -136   -436     65       N  
ATOM   2182  N   GLU A 321      -2.228 -18.784 118.652  1.00 52.21           N  
ANISOU 2182  N   GLU A 321     6389   6635   6814      9   -585   -188       N  
ATOM   2183  CA  GLU A 321      -2.808 -19.670 117.662  1.00 57.98           C  
ANISOU 2183  CA  GLU A 321     7114   7361   7554     -5   -639   -231       C  
ATOM   2184  C   GLU A 321      -1.793 -20.592 117.022  1.00 60.87           C  
ANISOU 2184  C   GLU A 321     7517   7677   7933     14   -670   -287       C  
ATOM   2185  O   GLU A 321      -0.573 -20.353 117.116  1.00 59.96           O  
ANISOU 2185  O   GLU A 321     7430   7544   7808     49   -645   -294       O  
ATOM   2186  CB  GLU A 321      -3.572 -18.868 116.633  1.00 59.11           C  
ANISOU 2186  CB  GLU A 321     7230   7575   7654     23   -637   -241       C  
ATOM   2187  CG  GLU A 321      -4.708 -18.111 117.337  1.00 65.72           C  
ANISOU 2187  CG  GLU A 321     8023   8455   8493      2   -613   -190       C  
ATOM   2188  CD  GLU A 321      -5.957 -17.980 116.496  1.00 76.01           C  
ANISOU 2188  CD  GLU A 321     9286   9814   9783     -1   -642   -201       C  
ATOM   2189  OE1 GLU A 321      -5.817 -17.486 115.338  1.00 80.16           O  
ANISOU 2189  OE1 GLU A 321     9816  10379  10264     45   -648   -224       O  
ATOM   2190  OE2 GLU A 321      -7.066 -18.353 117.002  1.00 79.04           O  
ANISOU 2190  OE2 GLU A 321     9629  10205  10196    -51   -658   -182       O  
ATOM   2191  N   LYS A 322      -2.296 -21.658 116.388  1.00 65.65           N  
ANISOU 2191  N   LYS A 322     8121   8259   8564    -11   -726   -332       N  
ATOM   2192  CA  LYS A 322      -1.432 -22.772 115.971  1.00 70.14           C  
ANISOU 2192  CA  LYS A 322     8722   8763   9163     -2   -763   -390       C  
ATOM   2193  C   LYS A 322      -0.374 -22.459 114.896  1.00 71.40           C  
ANISOU 2193  C   LYS A 322     8905   8948   9276     64   -751   -446       C  
ATOM   2194  O   LYS A 322       0.688 -23.068 114.911  1.00 72.33           O  
ANISOU 2194  O   LYS A 322     9050   9014   9417     84   -758   -479       O  
ATOM   2195  CB  LYS A 322      -2.227 -24.038 115.644  1.00 71.94           C  
ANISOU 2195  CB  LYS A 322     8941   8949   9442    -48   -829   -429       C  
ATOM   2196  CG  LYS A 322      -3.020 -23.967 114.315  1.00 77.43           C  
ANISOU 2196  CG  LYS A 322     9615   9705  10101    -38   -859   -485       C  
ATOM   2197  CD  LYS A 322      -3.863 -25.258 114.070  1.00 84.72           C  
ANISOU 2197  CD  LYS A 322    10525  10580  11084    -93   -928   -527       C  
ATOM   2198  CE  LYS A 322      -4.490 -25.284 112.641  1.00 88.05           C  
ANISOU 2198  CE  LYS A 322    10928  11064  11462    -78   -967   -599       C  
ATOM   2199  NZ  LYS A 322      -3.496 -25.507 111.520  1.00 87.78           N  
ANISOU 2199  NZ  LYS A 322    10925  11038  11390    -20   -977   -684       N  
ATOM   2200  N   LEU A 323      -0.615 -21.506 114.004  1.00 73.26           N  
ANISOU 2200  N   LEU A 323     9127   9263   9446     99   -730   -452       N  
ATOM   2201  CA  LEU A 323       0.437 -21.066 113.042  1.00 75.57           C  
ANISOU 2201  CA  LEU A 323     9439   9591   9685    159   -706   -491       C  
ATOM   2202  C   LEU A 323       0.644 -21.997 111.827  1.00 77.32           C  
ANISOU 2202  C   LEU A 323     9671   9813   9894    177   -752   -583       C  
ATOM   2203  O   LEU A 323       1.138 -23.130 111.958  1.00 78.48           O  
ANISOU 2203  O   LEU A 323     9837   9890  10093    169   -785   -630       O  
ATOM   2204  CB  LEU A 323       1.799 -20.764 113.741  1.00 75.74           C  
ANISOU 2204  CB  LEU A 323     9483   9578   9716    184   -663   -471       C  
ATOM   2205  CG  LEU A 323       3.115 -21.588 113.844  1.00 77.50           C  
ANISOU 2205  CG  LEU A 323     9734   9741   9972    205   -671   -515       C  
ATOM   2206  CD1 LEU A 323       4.368 -20.644 114.130  1.00 78.39           C  
ANISOU 2206  CD1 LEU A 323     9854   9869  10059    244   -612   -489       C  
ATOM   2207  CD2 LEU A 323       3.082 -22.733 114.886  1.00 78.78           C  
ANISOU 2207  CD2 LEU A 323     9906   9811  10215    163   -709   -506       C  
ATOM   2208  N   LYS A 328      10.074 -17.826 107.846  1.00103.68           N  
ANISOU 2208  N   LYS A 328    13051  13446  12898    527   -388   -667       N  
ATOM   2209  CA  LYS A 328       9.962 -17.967 106.397  1.00104.91           C  
ANISOU 2209  CA  LYS A 328    13203  13688  12970    555   -392   -717       C  
ATOM   2210  C   LYS A 328      11.302 -18.409 105.756  1.00105.36           C  
ANISOU 2210  C   LYS A 328    13253  13774  13003    596   -366   -789       C  
ATOM   2211  O   LYS A 328      11.909 -19.422 106.170  1.00105.75           O  
ANISOU 2211  O   LYS A 328    13307  13761  13114    605   -390   -853       O  
ATOM   2212  CB  LYS A 328       9.438 -16.659 105.768  1.00104.90           C  
ANISOU 2212  CB  LYS A 328    13192  13769  12894    557   -358   -641       C  
ATOM   2213  N   ARG A 329      11.735 -17.663 104.733  1.00104.96           N  
ANISOU 2213  N   ARG A 329    13191  13823  12866    622   -319   -777       N  
ATOM   2214  CA  ARG A 329      13.063 -17.825 104.132  1.00104.07           C  
ANISOU 2214  CA  ARG A 329    13065  13755  12722    660   -279   -829       C  
ATOM   2215  C   ARG A 329      13.870 -16.565 104.450  1.00102.41           C  
ANISOU 2215  C   ARG A 329    12840  13563  12506    657   -208   -744       C  
ATOM   2216  O   ARG A 329      13.512 -15.461 104.009  1.00102.41           O  
ANISOU 2216  O   ARG A 329    12838  13624  12450    650   -175   -667       O  
ATOM   2217  CB  ARG A 329      12.961 -18.042 102.615  1.00105.42           C  
ANISOU 2217  CB  ARG A 329    13231  14038  12788    690   -279   -890       C  
ATOM   2218  N   ASP A 330      14.940 -16.742 105.228  1.00100.00           N  
ANISOU 2218  N   ASP A 330    12526  13203  12265    662   -188   -755       N  
ATOM   2219  CA  ASP A 330      15.735 -15.624 105.770  1.00 97.11           C  
ANISOU 2219  CA  ASP A 330    12144  12835  11917    652   -128   -680       C  
ATOM   2220  C   ASP A 330      16.581 -14.848 104.739  1.00 94.80           C  
ANISOU 2220  C   ASP A 330    11829  12644  11547    672    -60   -662       C  
ATOM   2221  O   ASP A 330      17.345 -15.425 103.970  1.00 95.01           O  
ANISOU 2221  O   ASP A 330    11840  12725  11535    706    -46   -734       O  
ATOM   2222  CB  ASP A 330      16.589 -16.074 106.983  1.00 97.51           C  
ANISOU 2222  CB  ASP A 330    12189  12799  12061    648   -134   -697       C  
ATOM   2223  CG  ASP A 330      17.461 -17.304 106.689  1.00 98.86           C  
ANISOU 2223  CG  ASP A 330    12350  12963  12250    686   -151   -802       C  
ATOM   2224  OD1 ASP A 330      18.681 -17.235 106.972  1.00 98.71           O  
ANISOU 2224  OD1 ASP A 330    12307  12941  12259    702   -118   -814       O  
ATOM   2225  OD2 ASP A 330      16.928 -18.334 106.191  1.00100.31           O  
ANISOU 2225  OD2 ASP A 330    12547  13141  12424    700   -200   -875       O  
ATOM   2226  N   VAL A 331      16.429 -13.526 104.778  1.00 91.13           N  
ANISOU 2226  N   VAL A 331    11361  12201  11064    651    -18   -563       N  
ATOM   2227  CA  VAL A 331      16.975 -12.607 103.780  1.00 88.14           C  
ANISOU 2227  CA  VAL A 331    10963  11919  10608    661     46   -518       C  
ATOM   2228  C   VAL A 331      18.420 -12.139 104.067  1.00 84.95           C  
ANISOU 2228  C   VAL A 331    10528  11516  10234    661    107   -505       C  
ATOM   2229  O   VAL A 331      19.006 -12.422 105.126  1.00 84.19           O  
ANISOU 2229  O   VAL A 331    10425  11344  10221    654    100   -526       O  
ATOM   2230  CB  VAL A 331      16.054 -11.347 103.582  1.00 88.50           C  
ANISOU 2230  CB  VAL A 331    11018  11984  10623    639     59   -408       C  
ATOM   2231  CG1 VAL A 331      16.017 -10.934 102.096  1.00 90.04           C  
ANISOU 2231  CG1 VAL A 331    11207  12303  10703    658     90   -385       C  
ATOM   2232  CG2 VAL A 331      14.632 -11.603 104.100  1.00 88.58           C  
ANISOU 2232  CG2 VAL A 331    11053  11939  10663    623     -4   -400       C  
ATOM   2233  N   GLU A 332      18.972 -11.421 103.093  1.00 81.20           N  
ANISOU 2233  N   GLU A 332    10032  11133   9685    668    167   -469       N  
ATOM   2234  CA  GLU A 332      20.335 -10.960 103.120  1.00 77.25           C  
ANISOU 2234  CA  GLU A 332     9496  10657   9199    667    231   -457       C  
ATOM   2235  C   GLU A 332      20.305  -9.432 103.113  1.00 73.49           C  
ANISOU 2235  C   GLU A 332     9015  10189   8721    634    281   -335       C  
ATOM   2236  O   GLU A 332      20.937  -8.774 102.275  1.00 74.29           O  
ANISOU 2236  O   GLU A 332     9092  10372   8764    634    342   -292       O  
ATOM   2237  CB  GLU A 332      21.112 -11.552 101.929  1.00 78.86           C  
ANISOU 2237  CB  GLU A 332     9674  10970   9321    704    262   -528       C  
ATOM   2238  CG  GLU A 332      21.833 -12.896 102.233  1.00 81.49           C  
ANISOU 2238  CG  GLU A 332     9993  11273   9697    738    234   -651       C  
ATOM   2239  CD  GLU A 332      23.095 -12.727 103.155  1.00 86.35           C  
ANISOU 2239  CD  GLU A 332    10573  11837  10398    730    266   -651       C  
ATOM   2240  OE1 GLU A 332      24.040 -11.927 102.822  1.00 86.71           O  
ANISOU 2240  OE1 GLU A 332    10582  11941  10424    722    336   -609       O  
ATOM   2241  OE2 GLU A 332      23.132 -13.397 104.227  1.00 85.81           O  
ANISOU 2241  OE2 GLU A 332    10514  11672  10419    731    218   -690       O  
ATOM   2242  N   GLY A 333      19.536  -8.883 104.050  1.00 67.60           N  
ANISOU 2242  N   GLY A 333     8290   9357   8039    606    255   -279       N  
ATOM   2243  CA  GLY A 333      19.459  -7.451 104.302  1.00 61.18           C  
ANISOU 2243  CA  GLY A 333     7474   8521   7252    574    294   -171       C  
ATOM   2244  C   GLY A 333      18.780  -7.204 105.641  1.00 56.10           C  
ANISOU 2244  C   GLY A 333     6850   7767   6698    550    256   -151       C  
ATOM   2245  O   GLY A 333      18.631  -8.123 106.454  1.00 55.09           O  
ANISOU 2245  O   GLY A 333     6732   7583   6615    554    209   -216       O  
ATOM   2246  N   MET A 334      18.359  -5.973 105.875  1.00 51.72           N  
ANISOU 2246  N   MET A 334     6300   7181   6169    526    276    -61       N  
ATOM   2247  CA  MET A 334      17.653  -5.635 107.121  1.00 47.77           C  
ANISOU 2247  CA  MET A 334     5816   6586   5749    505    245    -43       C  
ATOM   2248  C   MET A 334      16.268  -6.247 107.215  1.00 45.82           C  
ANISOU 2248  C   MET A 334     5597   6325   5488    515    183    -62       C  
ATOM   2249  O   MET A 334      15.780  -6.460 108.306  1.00 45.71           O  
ANISOU 2249  O   MET A 334     5594   6242   5534    502    149    -79       O  
ATOM   2250  CB  MET A 334      17.562  -4.128 107.347  1.00 46.21           C  
ANISOU 2250  CB  MET A 334     5613   6353   5592    479    283     52       C  
ATOM   2251  CG  MET A 334      18.901  -3.475 107.671  1.00 46.13           C  
ANISOU 2251  CG  MET A 334     5572   6326   5629    456    337     67       C  
ATOM   2252  SD  MET A 334      19.631  -4.140 109.189  1.00 44.04           S  
ANISOU 2252  SD  MET A 334     5296   5989   5448    443    314    -13       S  
ATOM   2253  CE  MET A 334      18.768  -3.159 110.439  1.00 38.44           C  
ANISOU 2253  CE  MET A 334     4603   5183   4821    415    297     30       C  
ATOM   2254  N   GLY A 335      15.638  -6.563 106.096  1.00 44.47           N  
ANISOU 2254  N   GLY A 335     5436   6226   5236    536    168    -62       N  
ATOM   2255  CA  GLY A 335      14.312  -7.186 106.135  1.00 43.13           C  
ANISOU 2255  CA  GLY A 335     5288   6048   5053    543    106    -85       C  
ATOM   2256  C   GLY A 335      13.191  -6.238 106.581  1.00 42.21           C  
ANISOU 2256  C   GLY A 335     5179   5888   4969    530     95    -11       C  
ATOM   2257  O   GLY A 335      13.424  -5.055 106.886  1.00 41.89           O  
ANISOU 2257  O   GLY A 335     5131   5817   4967    516    133     58       O  
ATOM   2258  N   PRO A 336      11.966  -6.756 106.620  1.00 41.30           N  
ANISOU 2258  N   PRO A 336     5078   5771   4845    534     41    -28       N  
ATOM   2259  CA  PRO A 336      10.787  -5.935 106.951  1.00 39.74           C  
ANISOU 2259  CA  PRO A 336     4883   5543   4672    527     26     35       C  
ATOM   2260  C   PRO A 336      10.739  -5.678 108.445  1.00 38.61           C  
ANISOU 2260  C   PRO A 336     4739   5308   4623    503     26     33       C  
ATOM   2261  O   PRO A 336      10.764  -6.622 109.219  1.00 38.77           O  
ANISOU 2261  O   PRO A 336     4764   5293   4673    493     -3    -28       O  
ATOM   2262  CB  PRO A 336       9.595  -6.846 106.530  1.00 40.07           C  
ANISOU 2262  CB  PRO A 336     4933   5618   4673    538    -36     -3       C  
ATOM   2263  CG  PRO A 336      10.189  -8.312 106.509  1.00 39.84           C  
ANISOU 2263  CG  PRO A 336     4909   5596   4632    540    -60   -103       C  
ATOM   2264  CD  PRO A 336      11.625  -8.113 106.112  1.00 40.69           C  
ANISOU 2264  CD  PRO A 336     5008   5731   4721    549     -7   -108       C  
ATOM   2265  N   PRO A 337      10.646  -4.408 108.871  1.00 38.30           N  
ANISOU 2265  N   PRO A 337     4693   5230   4629    495     57    100       N  
ATOM   2266  CA  PRO A 337      10.451  -4.120 110.305  1.00 36.81           C  
ANISOU 2266  CA  PRO A 337     4502   4962   4523    473     54     92       C  
ATOM   2267  C   PRO A 337       9.092  -4.709 110.822  1.00 36.38           C  
ANISOU 2267  C   PRO A 337     4452   4894   4477    471      2     70       C  
ATOM   2268  O   PRO A 337       8.109  -4.537 110.178  1.00 35.59           O  
ANISOU 2268  O   PRO A 337     4351   4827   4345    485    -19     99       O  
ATOM   2269  CB  PRO A 337      10.390  -2.584 110.327  1.00 37.14           C  
ANISOU 2269  CB  PRO A 337     4536   4975   4601    472     93    170       C  
ATOM   2270  CG  PRO A 337       9.922  -2.197 109.003  1.00 37.44           C  
ANISOU 2270  CG  PRO A 337     4575   5073   4576    495     94    227       C  
ATOM   2271  CD  PRO A 337      10.504  -3.193 108.035  1.00 37.74           C  
ANISOU 2271  CD  PRO A 337     4618   5187   4537    506     88    186       C  
ATOM   2272  N   GLU A 338       9.041  -5.375 111.970  1.00 36.09           N  
ANISOU 2272  N   GLU A 338     4417   4813   4482    451    -19     22       N  
ATOM   2273  CA  GLU A 338       7.824  -6.016 112.378  1.00 36.72           C  
ANISOU 2273  CA  GLU A 338     4498   4888   4566    444    -65      3       C  
ATOM   2274  C   GLU A 338       7.459  -5.786 113.862  1.00 37.03           C  
ANISOU 2274  C   GLU A 338     4530   4871   4668    421    -66     -1       C  
ATOM   2275  O   GLU A 338       6.278  -5.615 114.187  1.00 36.93           O  
ANISOU 2275  O   GLU A 338     4509   4856   4668    418    -84     13       O  
ATOM   2276  CB  GLU A 338       7.876  -7.503 112.056  1.00 37.18           C  
ANISOU 2276  CB  GLU A 338     4566   4969   4593    442   -106    -58       C  
ATOM   2277  CG  GLU A 338       7.614  -7.802 110.569  1.00 40.70           C  
ANISOU 2277  CG  GLU A 338     5015   5484   4966    466   -122    -60       C  
ATOM   2278  CD  GLU A 338       7.576  -9.288 110.175  1.00 42.82           C  
ANISOU 2278  CD  GLU A 338     5292   5771   5207    466   -168   -132       C  
ATOM   2279  OE1 GLU A 338       7.493 -10.167 111.028  1.00 43.07           O  
ANISOU 2279  OE1 GLU A 338     5328   5758   5278    446   -196   -172       O  
ATOM   2280  OE2 GLU A 338       7.639  -9.587 108.965  1.00 47.51           O  
ANISOU 2280  OE2 GLU A 338     5888   6425   5736    487   -176   -149       O  
ATOM   2281  N   ILE A 339       8.463  -5.750 114.739  1.00 35.70           N  
ANISOU 2281  N   ILE A 339     4363   4665   4536    405    -45    -22       N  
ATOM   2282  CA  ILE A 339       8.210  -5.737 116.168  1.00 34.38           C  
ANISOU 2282  CA  ILE A 339     4191   4457   4416    382    -49    -36       C  
ATOM   2283  C   ILE A 339       8.716  -4.403 116.725  1.00 35.21           C  
ANISOU 2283  C   ILE A 339     4286   4529   4564    379     -5    -12       C  
ATOM   2284  O   ILE A 339       9.874  -4.034 116.520  1.00 35.10           O  
ANISOU 2284  O   ILE A 339     4271   4508   4558    380     25    -11       O  
ATOM   2285  CB  ILE A 339       8.914  -6.929 116.881  1.00 33.76           C  
ANISOU 2285  CB  ILE A 339     4121   4362   4344    365    -72    -85       C  
ATOM   2286  CG1 ILE A 339       8.413  -8.295 116.355  1.00 31.84           C  
ANISOU 2286  CG1 ILE A 339     3888   4139   4070    365   -119   -114       C  
ATOM   2287  CG2 ILE A 339       8.684  -6.888 118.382  1.00 32.20           C  
ANISOU 2287  CG2 ILE A 339     3917   4132   4185    339    -76    -94       C  
ATOM   2288  CD1 ILE A 339       9.313  -9.419 116.764  1.00 25.86           C  
ANISOU 2288  CD1 ILE A 339     3141   3362   3323    358   -140   -157       C  
ATOM   2289  N   LYS A 340       7.831  -3.676 117.397  1.00 34.84           N  
ANISOU 2289  N   LYS A 340     4227   4461   4548    376      0      4       N  
ATOM   2290  CA  LYS A 340       8.144  -2.343 117.878  1.00 35.46           C  
ANISOU 2290  CA  LYS A 340     4295   4503   4674    375     39     22       C  
ATOM   2291  C   LYS A 340       8.418  -2.345 119.376  1.00 34.22           C  
ANISOU 2291  C   LYS A 340     4131   4316   4553    351     43    -17       C  
ATOM   2292  O   LYS A 340       7.684  -3.045 120.146  1.00 34.09           O  
ANISOU 2292  O   LYS A 340     4114   4310   4530    338     16    -39       O  
ATOM   2293  CB  LYS A 340       6.957  -1.441 117.626  1.00 37.02           C  
ANISOU 2293  CB  LYS A 340     4481   4697   4888    395     43     60       C  
ATOM   2294  CG  LYS A 340       6.769  -1.096 116.200  1.00 42.88           C  
ANISOU 2294  CG  LYS A 340     5226   5465   5599    421     45    111       C  
ATOM   2295  CD  LYS A 340       5.317  -0.747 115.948  1.00 54.73           C  
ANISOU 2295  CD  LYS A 340     6713   6979   7101    442     26    141       C  
ATOM   2296  CE  LYS A 340       5.063   0.777 115.900  1.00 62.97           C  
ANISOU 2296  CE  LYS A 340     7745   7983   8198    462     56    188       C  
ATOM   2297  NZ  LYS A 340       4.101   1.103 114.764  1.00 65.36           N  
ANISOU 2297  NZ  LYS A 340     8041   8319   8475    495     38    245       N  
ATOM   2298  N   TYR A 341       9.468  -1.612 119.784  1.00 31.45           N  
ANISOU 2298  N   TYR A 341     3777   3936   4238    342     74    -26       N  
ATOM   2299  CA  TYR A 341       9.688  -1.317 121.187  1.00 31.32           C  
ANISOU 2299  CA  TYR A 341     3751   3894   4257    321     80    -62       C  
ATOM   2300  C   TYR A 341       8.459  -0.625 121.766  1.00 32.17           C  
ANISOU 2300  C   TYR A 341     3844   3990   4387    327     84    -59       C  
ATOM   2301  O   TYR A 341       7.881   0.258 121.121  1.00 32.18           O  
ANISOU 2301  O   TYR A 341     3840   3978   4409    349     99    -24       O  
ATOM   2302  CB  TYR A 341      10.941  -0.440 121.382  1.00 30.91           C  
ANISOU 2302  CB  TYR A 341     3691   3809   4245    311    114    -70       C  
ATOM   2303  CG  TYR A 341      12.212  -1.262 121.208  1.00 31.16           C  
ANISOU 2303  CG  TYR A 341     3727   3857   4257    301    107    -88       C  
ATOM   2304  CD1 TYR A 341      12.516  -2.287 122.128  1.00 26.98           C  
ANISOU 2304  CD1 TYR A 341     3199   3339   3711    286     78   -128       C  
ATOM   2305  CD2 TYR A 341      13.093  -1.045 120.120  1.00 27.59           C  
ANISOU 2305  CD2 TYR A 341     3273   3410   3800    309    130    -64       C  
ATOM   2306  CE1 TYR A 341      13.616  -3.084 121.963  1.00 28.87           C  
ANISOU 2306  CE1 TYR A 341     3441   3592   3938    284     68   -146       C  
ATOM   2307  CE2 TYR A 341      14.248  -1.794 119.997  1.00 25.40           C  
ANISOU 2307  CE2 TYR A 341     2994   3150   3508    304    126    -88       C  
ATOM   2308  CZ  TYR A 341      14.476  -2.823 120.914  1.00 29.86           C  
ANISOU 2308  CZ  TYR A 341     3561   3722   4062    294     93   -130       C  
ATOM   2309  OH  TYR A 341      15.577  -3.630 120.856  1.00 33.91           O  
ANISOU 2309  OH  TYR A 341     4070   4249   4565    294     83   -155       O  
ATOM   2310  N   GLY A 342       8.052  -1.038 122.964  1.00 32.50           N  
ANISOU 2310  N   GLY A 342     3880   4042   4426    309     70    -94       N  
ATOM   2311  CA  GLY A 342       6.934  -0.403 123.660  1.00 34.22           C  
ANISOU 2311  CA  GLY A 342     4080   4257   4665    314     78   -102       C  
ATOM   2312  C   GLY A 342       5.538  -0.794 123.146  1.00 35.90           C  
ANISOU 2312  C   GLY A 342     4287   4500   4856    329     58    -76       C  
ATOM   2313  O   GLY A 342       4.705  -1.250 123.928  1.00 36.20           O  
ANISOU 2313  O   GLY A 342     4312   4563   4880    317     45    -93       O  
ATOM   2314  N   GLU A 343       5.290  -0.664 121.838  1.00 36.12           N  
ANISOU 2314  N   GLU A 343     4320   4531   4874    353     53    -34       N  
ATOM   2315  CA  GLU A 343       3.937  -0.815 121.288  1.00 35.89           C  
ANISOU 2315  CA  GLU A 343     4277   4528   4829    371     34     -9       C  
ATOM   2316  C   GLU A 343       3.529  -2.247 120.974  1.00 36.01           C  
ANISOU 2316  C   GLU A 343     4301   4585   4795    357     -6    -12       C  
ATOM   2317  O   GLU A 343       2.350  -2.554 120.993  1.00 39.62           O  
ANISOU 2317  O   GLU A 343     4741   5070   5243    358    -26     -6       O  
ATOM   2318  CB  GLU A 343       3.732   0.096 120.093  1.00 34.50           C  
ANISOU 2318  CB  GLU A 343     4100   4341   4667    406     44     40       C  
ATOM   2319  CG  GLU A 343       4.241   1.466 120.410  1.00 39.15           C  
ANISOU 2319  CG  GLU A 343     4683   4876   5316    415     82     44       C  
ATOM   2320  CD  GLU A 343       4.104   2.485 119.304  1.00 46.96           C  
ANISOU 2320  CD  GLU A 343     5671   5843   6329    448     95    103       C  
ATOM   2321  OE1 GLU A 343       3.546   2.141 118.228  1.00 51.94           O  
ANISOU 2321  OE1 GLU A 343     6304   6510   6920    467     72    144       O  
ATOM   2322  OE2 GLU A 343       4.582   3.638 119.499  1.00 48.83           O  
ANISOU 2322  OE2 GLU A 343     5904   6025   6624    453    126    111       O  
ATOM   2323  N   SER A 344       4.460  -3.136 120.704  1.00 34.49           N  
ANISOU 2323  N   SER A 344     4131   4397   4576    343    -20    -23       N  
ATOM   2324  CA  SER A 344       4.102  -4.477 120.341  1.00 33.24           C  
ANISOU 2324  CA  SER A 344     3982   4269   4381    331    -60    -29       C  
ATOM   2325  C   SER A 344       3.945  -5.388 121.542  1.00 33.93           C  
ANISOU 2325  C   SER A 344     4068   4359   4467    297    -78    -56       C  
ATOM   2326  O   SER A 344       4.868  -5.538 122.322  1.00 34.02           O  
ANISOU 2326  O   SER A 344     4088   4353   4485    281    -70    -76       O  
ATOM   2327  CB  SER A 344       5.166  -5.066 119.428  1.00 32.75           C  
ANISOU 2327  CB  SER A 344     3943   4208   4293    337    -68    -34       C  
ATOM   2328  OG  SER A 344       5.202  -4.402 118.182  1.00 31.11           O  
ANISOU 2328  OG  SER A 344     3736   4012   4072    365    -56     -2       O  
ATOM   2329  N   LEU A 345       2.795  -6.057 121.654  1.00 34.32           N  
ANISOU 2329  N   LEU A 345     4104   4433   4505    283   -105    -53       N  
ATOM   2330  CA  LEU A 345       2.643  -7.142 122.607  1.00 34.04           C  
ANISOU 2330  CA  LEU A 345     4070   4403   4463    246   -128    -67       C  
ATOM   2331  C   LEU A 345       3.160  -8.479 122.041  1.00 33.98           C  
ANISOU 2331  C   LEU A 345     4086   4387   4437    235   -166    -76       C  
ATOM   2332  O   LEU A 345       2.873  -8.819 120.920  1.00 35.87           O  
ANISOU 2332  O   LEU A 345     4330   4637   4661    249   -187    -74       O  
ATOM   2333  CB  LEU A 345       1.208  -7.191 123.079  1.00 33.67           C  
ANISOU 2333  CB  LEU A 345     3992   4383   4417    232   -134    -58       C  
ATOM   2334  CG  LEU A 345       0.957  -6.030 124.078  1.00 36.02           C  
ANISOU 2334  CG  LEU A 345     4267   4685   4735    238    -94    -64       C  
ATOM   2335  CD1 LEU A 345      -0.489  -5.889 124.404  1.00 34.46           C  
ANISOU 2335  CD1 LEU A 345     4032   4522   4541    233    -93    -57       C  
ATOM   2336  CD2 LEU A 345       1.780  -6.176 125.402  1.00 35.30           C  
ANISOU 2336  CD2 LEU A 345     4185   4587   4643    212    -81    -86       C  
ATOM   2337  N   CYS A 346       3.949  -9.223 122.784  1.00 32.57           N  
ANISOU 2337  N   CYS A 346     3924   4190   4261    214   -178    -90       N  
ATOM   2338  CA  CYS A 346       4.582 -10.417 122.242  1.00 34.10           C  
ANISOU 2338  CA  CYS A 346     4140   4367   4448    211   -212   -104       C  
ATOM   2339  C   CYS A 346       4.427 -11.613 123.175  1.00 33.36           C  
ANISOU 2339  C   CYS A 346     4052   4261   4363    174   -245   -103       C  
ATOM   2340  O   CYS A 346       4.653 -11.507 124.349  1.00 34.55           O  
ANISOU 2340  O   CYS A 346     4198   4410   4517    155   -235    -96       O  
ATOM   2341  CB  CYS A 346       6.104 -10.185 122.116  1.00 34.56           C  
ANISOU 2341  CB  CYS A 346     4215   4406   4511    230   -195   -121       C  
ATOM   2342  SG  CYS A 346       6.608  -8.704 121.249  1.00 40.15           S  
ANISOU 2342  SG  CYS A 346     4917   5121   5217    266   -149   -114       S  
ATOM   2343  N   PHE A 347       4.112 -12.759 122.645  1.00 33.23           N  
ANISOU 2343  N   PHE A 347     4045   4233   4348    163   -287   -109       N  
ATOM   2344  CA  PHE A 347       4.034 -13.958 123.419  1.00 33.18           C  
ANISOU 2344  CA  PHE A 347     4046   4204   4357    127   -321   -101       C  
ATOM   2345  C   PHE A 347       5.294 -14.661 123.034  1.00 34.82           C  
ANISOU 2345  C   PHE A 347     4279   4375   4575    145   -341   -126       C  
ATOM   2346  O   PHE A 347       5.609 -14.733 121.859  1.00 36.56           O  
ANISOU 2346  O   PHE A 347     4508   4596   4789    174   -347   -153       O  
ATOM   2347  CB  PHE A 347       2.857 -14.801 122.923  1.00 33.28           C  
ANISOU 2347  CB  PHE A 347     4051   4219   4375    104   -358    -98       C  
ATOM   2348  CG  PHE A 347       1.513 -14.266 123.297  1.00 30.28           C  
ANISOU 2348  CG  PHE A 347     3638   3877   3989     83   -343    -73       C  
ATOM   2349  CD1 PHE A 347       0.989 -14.497 124.567  1.00 30.57           C  
ANISOU 2349  CD1 PHE A 347     3660   3924   4030     42   -339    -45       C  
ATOM   2350  CD2 PHE A 347       0.762 -13.549 122.372  1.00 28.66           C  
ANISOU 2350  CD2 PHE A 347     3414   3704   3771    106   -333    -78       C  
ATOM   2351  CE1 PHE A 347      -0.304 -14.033 124.912  1.00 31.89           C  
ANISOU 2351  CE1 PHE A 347     3790   4134   4192     24   -323    -26       C  
ATOM   2352  CE2 PHE A 347      -0.512 -13.069 122.695  1.00 31.37           C  
ANISOU 2352  CE2 PHE A 347     3721   4084   4113     92   -321    -58       C  
ATOM   2353  CZ  PHE A 347      -1.059 -13.331 123.977  1.00 32.27           C  
ANISOU 2353  CZ  PHE A 347     3817   4210   4235     50   -315    -35       C  
ATOM   2354  N   VAL A 348       6.055 -15.130 124.010  1.00 35.81           N  
ANISOU 2354  N   VAL A 348     4415   4478   4714    133   -351   -119       N  
ATOM   2355  CA  VAL A 348       7.274 -15.822 123.754  1.00 34.91           C  
ANISOU 2355  CA  VAL A 348     4320   4328   4616    153   -372   -142       C  
ATOM   2356  C   VAL A 348       6.968 -17.321 123.752  1.00 35.88           C  
ANISOU 2356  C   VAL A 348     4456   4409   4768    131   -427   -141       C  
ATOM   2357  O   VAL A 348       6.391 -17.851 124.707  1.00 36.30           O  
ANISOU 2357  O   VAL A 348     4508   4453   4833     91   -445   -105       O  
ATOM   2358  CB  VAL A 348       8.308 -15.456 124.834  1.00 35.10           C  
ANISOU 2358  CB  VAL A 348     4343   4350   4642    154   -356   -134       C  
ATOM   2359  CG1 VAL A 348       9.640 -16.293 124.704  1.00 34.25           C  
ANISOU 2359  CG1 VAL A 348     4251   4205   4558    177   -383   -156       C  
ATOM   2360  CG2 VAL A 348       8.617 -13.984 124.742  1.00 33.96           C  
ANISOU 2360  CG2 VAL A 348     4185   4238   4480    174   -304   -141       C  
ATOM   2361  N   GLN A 349       7.409 -18.008 122.702  1.00 35.04           N  
ANISOU 2361  N   GLN A 349     4364   4277   4675    156   -452   -181       N  
ATOM   2362  CA  GLN A 349       7.206 -19.449 122.569  1.00 35.30           C  
ANISOU 2362  CA  GLN A 349     4410   4257   4745    140   -507   -192       C  
ATOM   2363  C   GLN A 349       8.558 -20.209 122.443  1.00 35.46           C  
ANISOU 2363  C   GLN A 349     4446   4230   4796    172   -530   -224       C  
ATOM   2364  O   GLN A 349       9.460 -19.776 121.738  1.00 35.07           O  
ANISOU 2364  O   GLN A 349     4396   4197   4731    214   -508   -261       O  
ATOM   2365  CB  GLN A 349       6.359 -19.717 121.317  1.00 34.22           C  
ANISOU 2365  CB  GLN A 349     4271   4130   4602    143   -524   -225       C  
ATOM   2366  CG  GLN A 349       6.031 -21.156 121.102  1.00 38.28           C  
ANISOU 2366  CG  GLN A 349     4796   4586   5161    123   -582   -244       C  
ATOM   2367  CD  GLN A 349       4.912 -21.374 120.053  1.00 39.34           C  
ANISOU 2367  CD  GLN A 349     4922   4739   5286    113   -602   -273       C  
ATOM   2368  OE1 GLN A 349       4.920 -20.769 118.976  1.00 38.82           O  
ANISOU 2368  OE1 GLN A 349     4851   4718   5181    146   -584   -308       O  
ATOM   2369  NE2 GLN A 349       3.953 -22.235 120.386  1.00 36.20           N  
ANISOU 2369  NE2 GLN A 349     4521   4310   4925     64   -641   -255       N  
ATOM   2370  N   HIS A 350       8.696 -21.338 123.113  1.00 35.91           N  
ANISOU 2370  N   HIS A 350     4516   4232   4898    153   -575   -206       N  
ATOM   2371  CA  HIS A 350       9.853 -22.176 122.875  1.00 37.59           C  
ANISOU 2371  CA  HIS A 350     4742   4393   5149    188   -604   -242       C  
ATOM   2372  C   HIS A 350       9.638 -22.926 121.535  1.00 38.73           C  
ANISOU 2372  C   HIS A 350     4893   4512   5311    208   -632   -306       C  
ATOM   2373  O   HIS A 350       8.601 -23.619 121.352  1.00 39.51           O  
ANISOU 2373  O   HIS A 350     4996   4584   5431    174   -666   -304       O  
ATOM   2374  CB  HIS A 350      10.029 -23.128 124.053  1.00 38.13           C  
ANISOU 2374  CB  HIS A 350     4821   4405   5263    162   -646   -194       C  
ATOM   2375  CG  HIS A 350      11.176 -24.072 123.904  1.00 39.48           C  
ANISOU 2375  CG  HIS A 350     5003   4514   5484    200   -684   -226       C  
ATOM   2376  ND1 HIS A 350      12.480 -23.700 124.150  1.00 42.23           N  
ANISOU 2376  ND1 HIS A 350     5344   4875   5828    239   -668   -238       N  
ATOM   2377  CD2 HIS A 350      11.215 -25.378 123.560  1.00 39.22           C  
ANISOU 2377  CD2 HIS A 350     4984   4404   5513    205   -738   -250       C  
ATOM   2378  CE1 HIS A 350      13.279 -24.732 123.946  1.00 39.30           C  
ANISOU 2378  CE1 HIS A 350     4980   4441   5512    272   -710   -268       C  
ATOM   2379  NE2 HIS A 350      12.536 -25.758 123.585  1.00 41.59           N  
ANISOU 2379  NE2 HIS A 350     5286   4673   5845    253   -753   -277       N  
ATOM   2380  N   VAL A 351      10.575 -22.782 120.590  1.00 38.17           N  
ANISOU 2380  N   VAL A 351     4821   4454   5228    259   -618   -367       N  
ATOM   2381  CA  VAL A 351      10.318 -23.271 119.248  1.00 38.23           C  
ANISOU 2381  CA  VAL A 351     4831   4460   5233    280   -635   -435       C  
ATOM   2382  C   VAL A 351      10.156 -24.815 119.161  1.00 41.25           C  
ANISOU 2382  C   VAL A 351     5230   4758   5685    272   -702   -466       C  
ATOM   2383  O   VAL A 351       9.159 -25.299 118.594  1.00 41.24           O  
ANISOU 2383  O   VAL A 351     5231   4746   5690    249   -730   -488       O  
ATOM   2384  CB  VAL A 351      11.310 -22.712 118.183  1.00 38.18           C  
ANISOU 2384  CB  VAL A 351     4816   4502   5188    337   -598   -492       C  
ATOM   2385  CG1 VAL A 351      11.153 -23.441 116.844  1.00 33.68           C  
ANISOU 2385  CG1 VAL A 351     4251   3930   4616    361   -624   -573       C  
ATOM   2386  CG2 VAL A 351      11.064 -21.224 117.961  1.00 36.42           C  
ANISOU 2386  CG2 VAL A 351     4579   4358   4899    335   -539   -463       C  
ATOM   2387  N   ALA A 352      11.101 -25.586 119.711  1.00 41.60           N  
ANISOU 2387  N   ALA A 352     5283   4740   5785    291   -730   -468       N  
ATOM   2388  CA  ALA A 352      10.989 -27.050 119.592  1.00 42.91           C  
ANISOU 2388  CA  ALA A 352     5463   4813   6026    287   -794   -499       C  
ATOM   2389  C   ALA A 352       9.790 -27.671 120.323  1.00 44.02           C  
ANISOU 2389  C   ALA A 352     5613   4906   6206    220   -833   -439       C  
ATOM   2390  O   ALA A 352       9.173 -28.609 119.802  1.00 45.20           O  
ANISOU 2390  O   ALA A 352     5770   5002   6401    203   -878   -476       O  
ATOM   2391  CB  ALA A 352      12.275 -27.736 120.040  1.00 42.97           C  
ANISOU 2391  CB  ALA A 352     5476   4760   6092    327   -819   -510       C  
ATOM   2392  N   SER A 353       9.464 -27.209 121.530  1.00 43.85           N  
ANISOU 2392  N   SER A 353     5588   4902   6170    179   -817   -350       N  
ATOM   2393  CA  SER A 353       8.322 -27.805 122.243  1.00 44.11           C  
ANISOU 2393  CA  SER A 353     5624   4897   6237    112   -848   -287       C  
ATOM   2394  C   SER A 353       6.984 -27.160 121.992  1.00 43.11           C  
ANISOU 2394  C   SER A 353     5483   4833   6065     70   -824   -272       C  
ATOM   2395  O   SER A 353       5.992 -27.737 122.349  1.00 43.86           O  
ANISOU 2395  O   SER A 353     5575   4898   6191     14   -852   -235       O  
ATOM   2396  CB  SER A 353       8.546 -27.769 123.744  1.00 44.85           C  
ANISOU 2396  CB  SER A 353     5721   4982   6338     84   -847   -194       C  
ATOM   2397  OG  SER A 353       8.533 -26.432 124.215  1.00 48.51           O  
ANISOU 2397  OG  SER A 353     6169   5537   6727     82   -788   -162       O  
ATOM   2398  N   GLY A 354       6.941 -25.934 121.467  1.00 41.91           N  
ANISOU 2398  N   GLY A 354     5315   4767   5840     93   -772   -292       N  
ATOM   2399  CA  GLY A 354       5.658 -25.204 121.347  1.00 40.08           C  
ANISOU 2399  CA  GLY A 354     5064   4599   5565     57   -747   -268       C  
ATOM   2400  C   GLY A 354       5.175 -24.572 122.638  1.00 40.25           C  
ANISOU 2400  C   GLY A 354     5073   4656   5565     17   -718   -185       C  
ATOM   2401  O   GLY A 354       4.110 -23.967 122.652  1.00 41.93           O  
ANISOU 2401  O   GLY A 354     5264   4920   5745    -12   -696   -163       O  
ATOM   2402  N   LEU A 355       5.922 -24.725 123.741  1.00 38.95           N  
ANISOU 2402  N   LEU A 355     4918   4468   5415     14   -718   -139       N  
ATOM   2403  CA  LEU A 355       5.491 -24.250 125.052  1.00 37.68           C  
ANISOU 2403  CA  LEU A 355     4746   4343   5229    -27   -694    -62       C  
ATOM   2404  C   LEU A 355       5.620 -22.726 125.158  1.00 36.70           C  
ANISOU 2404  C   LEU A 355     4605   4302   5039     -4   -631    -64       C  
ATOM   2405  O   LEU A 355       6.463 -22.126 124.477  1.00 35.58           O  
ANISOU 2405  O   LEU A 355     4466   4176   4877     47   -609   -110       O  
ATOM   2406  CB  LEU A 355       6.319 -24.910 126.136  1.00 38.30           C  
ANISOU 2406  CB  LEU A 355     4840   4375   5339    -32   -719    -16       C  
ATOM   2407  CG  LEU A 355       6.258 -26.452 126.212  1.00 42.08           C  
ANISOU 2407  CG  LEU A 355     5336   4756   5894    -56   -785      0       C  
ATOM   2408  CD1 LEU A 355       7.236 -27.038 127.251  1.00 39.95           C  
ANISOU 2408  CD1 LEU A 355     5083   4442   5654    -51   -812     50       C  
ATOM   2409  CD2 LEU A 355       4.811 -26.965 126.431  1.00 40.69           C  
ANISOU 2409  CD2 LEU A 355     5149   4572   5739   -127   -802     43       C  
ATOM   2410  N   TRP A 356       4.761 -22.120 125.985  1.00 36.10           N  
ANISOU 2410  N   TRP A 356     4508   4276   4931    -42   -603    -15       N  
ATOM   2411  CA  TRP A 356       4.638 -20.666 126.129  1.00 34.77           C  
ANISOU 2411  CA  TRP A 356     4321   4182   4709    -26   -545    -17       C  
ATOM   2412  C   TRP A 356       5.343 -20.221 127.369  1.00 35.20           C  
ANISOU 2412  C   TRP A 356     4375   4256   4742    -27   -524     17       C  
ATOM   2413  O   TRP A 356       5.230 -20.879 128.399  1.00 36.17           O  
ANISOU 2413  O   TRP A 356     4501   4366   4874    -64   -544     67       O  
ATOM   2414  CB  TRP A 356       3.193 -20.283 126.281  1.00 33.90           C  
ANISOU 2414  CB  TRP A 356     4184   4117   4581    -64   -528      8       C  
ATOM   2415  CG  TRP A 356       2.405 -20.624 125.047  1.00 36.37           C  
ANISOU 2415  CG  TRP A 356     4490   4421   4909    -64   -550    -27       C  
ATOM   2416  CD1 TRP A 356       1.469 -21.633 124.904  1.00 36.21           C  
ANISOU 2416  CD1 TRP A 356     4463   4372   4924   -108   -590    -15       C  
ATOM   2417  CD2 TRP A 356       2.490 -19.979 123.767  1.00 35.25           C  
ANISOU 2417  CD2 TRP A 356     4346   4301   4747    -19   -536    -79       C  
ATOM   2418  NE1 TRP A 356       0.965 -21.630 123.611  1.00 36.21           N  
ANISOU 2418  NE1 TRP A 356     4456   4379   4924    -92   -604    -64       N  
ATOM   2419  CE2 TRP A 356       1.582 -20.642 122.894  1.00 36.18           C  
ANISOU 2419  CE2 TRP A 356     4456   4408   4883    -36   -572   -101       C  
ATOM   2420  CE3 TRP A 356       3.251 -18.923 123.267  1.00 31.02           C  
ANISOU 2420  CE3 TRP A 356     3813   3794   4178     32   -499   -106       C  
ATOM   2421  CZ2 TRP A 356       1.391 -20.245 121.569  1.00 37.25           C  
ANISOU 2421  CZ2 TRP A 356     4587   4571   4996     -2   -571   -147       C  
ATOM   2422  CZ3 TRP A 356       3.077 -18.542 121.944  1.00 34.40           C  
ANISOU 2422  CZ3 TRP A 356     4238   4244   4588     64   -496   -145       C  
ATOM   2423  CH2 TRP A 356       2.153 -19.200 121.104  1.00 35.50           C  
ANISOU 2423  CH2 TRP A 356     4370   4381   4737     49   -532   -166       C  
ATOM   2424  N   LEU A 357       6.081 -19.121 127.283  1.00 34.46           N  
ANISOU 2424  N   LEU A 357     4278   4196   4620     10   -485    -10       N  
ATOM   2425  CA  LEU A 357       6.660 -18.541 128.451  1.00 36.01           C  
ANISOU 2425  CA  LEU A 357     4470   4422   4791      7   -462     13       C  
ATOM   2426  C   LEU A 357       5.561 -17.930 129.307  1.00 37.67           C  
ANISOU 2426  C   LEU A 357     4656   4689   4967    -30   -431     46       C  
ATOM   2427  O   LEU A 357       4.783 -17.090 128.845  1.00 38.12           O  
ANISOU 2427  O   LEU A 357     4695   4782   5009    -25   -399     30       O  
ATOM   2428  CB  LEU A 357       7.631 -17.465 128.044  1.00 35.89           C  
ANISOU 2428  CB  LEU A 357     4452   4426   4760     53   -427    -29       C  
ATOM   2429  CG  LEU A 357       8.271 -16.668 129.166  1.00 37.88           C  
ANISOU 2429  CG  LEU A 357     4694   4713   4985     52   -400    -20       C  
ATOM   2430  CD1 LEU A 357       9.212 -17.567 129.902  1.00 35.19           C  
ANISOU 2430  CD1 LEU A 357     4368   4344   4660     50   -440      1       C  
ATOM   2431  CD2 LEU A 357       9.022 -15.413 128.602  1.00 36.19           C  
ANISOU 2431  CD2 LEU A 357     4472   4516   4763     92   -359    -64       C  
ATOM   2432  N   THR A 358       5.476 -18.378 130.546  1.00 39.00           N  
ANISOU 2432  N   THR A 358     4824   4871   5124    -66   -443     95       N  
ATOM   2433  CA  THR A 358       4.480 -17.879 131.448  1.00 40.34           C  
ANISOU 2433  CA  THR A 358     4968   5102   5257   -103   -412    125       C  
ATOM   2434  C   THR A 358       4.988 -17.881 132.915  1.00 42.18           C  
ANISOU 2434  C   THR A 358     5200   5370   5455   -123   -409    162       C  
ATOM   2435  O   THR A 358       6.172 -18.012 133.180  1.00 41.41           O  
ANISOU 2435  O   THR A 358     5120   5254   5362   -101   -427    157       O  
ATOM   2436  CB  THR A 358       3.115 -18.634 131.241  1.00 41.10           C  
ANISOU 2436  CB  THR A 358     5051   5193   5371   -148   -429    157       C  
ATOM   2437  OG1 THR A 358       2.081 -17.946 131.954  1.00 38.96           O  
ANISOU 2437  OG1 THR A 358     4746   4994   5062   -175   -388    175       O  
ATOM   2438  CG2 THR A 358       3.171 -20.102 131.713  1.00 39.52           C  
ANISOU 2438  CG2 THR A 358     4869   4945   5202   -187   -480    212       C  
ATOM   2439  N   TYR A 359       4.086 -17.723 133.858  1.00 45.24           N  
ANISOU 2439  N   TYR A 359     5565   5816   5806   -163   -388    198       N  
ATOM   2440  CA  TYR A 359       4.464 -17.592 135.244  1.00 48.63           C  
ANISOU 2440  CA  TYR A 359     5992   6298   6189   -182   -380    228       C  
ATOM   2441  C   TYR A 359       3.767 -18.629 136.074  1.00 51.99           C  
ANISOU 2441  C   TYR A 359     6413   6736   6604   -240   -402    306       C  
ATOM   2442  O   TYR A 359       2.805 -19.248 135.613  1.00 51.84           O  
ANISOU 2442  O   TYR A 359     6387   6694   6614   -270   -413    329       O  
ATOM   2443  CB  TYR A 359       4.097 -16.216 135.770  1.00 47.85           C  
ANISOU 2443  CB  TYR A 359     5863   6276   6042   -174   -323    192       C  
ATOM   2444  CG  TYR A 359       2.672 -15.850 135.546  1.00 49.05           C  
ANISOU 2444  CG  TYR A 359     5984   6464   6189   -193   -291    190       C  
ATOM   2445  CD1 TYR A 359       1.678 -16.248 136.433  1.00 49.46           C  
ANISOU 2445  CD1 TYR A 359     6013   6571   6210   -245   -281    241       C  
ATOM   2446  CD2 TYR A 359       2.305 -15.106 134.437  1.00 49.33           C  
ANISOU 2446  CD2 TYR A 359     6010   6483   6251   -160   -270    142       C  
ATOM   2447  CE1 TYR A 359       0.339 -15.892 136.223  1.00 51.04           C  
ANISOU 2447  CE1 TYR A 359     6177   6810   6408   -261   -250    236       C  
ATOM   2448  CE2 TYR A 359       0.976 -14.756 134.204  1.00 50.81           C  
ANISOU 2448  CE2 TYR A 359     6163   6704   6437   -172   -243    140       C  
ATOM   2449  CZ  TYR A 359       0.002 -15.150 135.094  1.00 52.49           C  
ANISOU 2449  CZ  TYR A 359     6350   6972   6622   -222   -233    184       C  
ATOM   2450  OH  TYR A 359      -1.311 -14.777 134.851  1.00 56.24           O  
ANISOU 2450  OH  TYR A 359     6785   7486   7099   -232   -207    178       O  
ATOM   2451  N   ALA A 360       4.268 -18.794 137.306  1.00 56.20           N  
ANISOU 2451  N   ALA A 360     6951   7310   7095   -257   -409    346       N  
ATOM   2452  CA  ALA A 360       3.725 -19.752 138.282  1.00 60.02           C  
ANISOU 2452  CA  ALA A 360     7431   7816   7557   -316   -429    434       C  
ATOM   2453  C   ALA A 360       3.240 -19.008 139.534  1.00 62.08           C  
ANISOU 2453  C   ALA A 360     7662   8192   7734   -342   -382    447       C  
ATOM   2454  O   ALA A 360       2.078 -18.657 139.628  1.00 63.34           O  
ANISOU 2454  O   ALA A 360     7790   8403   7873   -368   -344    446       O  
ATOM   2455  CB  ALA A 360       4.770 -20.798 138.635  1.00 60.11           C  
ANISOU 2455  CB  ALA A 360     7475   7773   7591   -315   -488    485       C  
ATOM   2456  N   ALA A 361       4.129 -18.797 140.499  1.00 64.74           N  
ANISOU 2456  N   ALA A 361     8006   8572   8021   -334   -388    455       N  
ATOM   2457  CA  ALA A 361       3.847 -17.999 141.732  1.00 66.45           C  
ANISOU 2457  CA  ALA A 361     8193   8906   8147   -351   -344    450       C  
ATOM   2458  C   ALA A 361       5.144 -17.722 142.529  1.00 66.81           C  
ANISOU 2458  C   ALA A 361     8253   8982   8151   -328   -363    438       C  
ATOM   2459  O   ALA A 361       6.257 -18.161 142.122  1.00 66.89           O  
ANISOU 2459  O   ALA A 361     8290   8920   8203   -297   -408    438       O  
ATOM   2460  CB  ALA A 361       2.759 -18.680 142.622  1.00 67.57           C  
ANISOU 2460  CB  ALA A 361     8316   9112   8245   -419   -335    537       C  
ATOM   2461  N   VAL A 371       6.948  -6.937 147.706  1.00 79.26           N  
ANISOU 2461  N   VAL A 371     9627  11121   9368   -176    -48   -316       N  
ATOM   2462  CA  VAL A 371       8.167  -7.263 146.969  1.00 78.56           C  
ANISOU 2462  CA  VAL A 371     9568  10938   9342   -159    -95   -298       C  
ATOM   2463  C   VAL A 371       7.908  -8.363 145.886  1.00 76.74           C  
ANISOU 2463  C   VAL A 371     9366  10621   9171   -162   -120   -205       C  
ATOM   2464  O   VAL A 371       8.583  -9.409 145.890  1.00 76.73           O  
ANISOU 2464  O   VAL A 371     9389  10598   9167   -172   -171   -135       O  
ATOM   2465  CB  VAL A 371       9.328  -7.639 147.980  1.00 80.08           C  
ANISOU 2465  CB  VAL A 371     9767  11190   9468   -172   -143   -288       C  
ATOM   2466  CG1 VAL A 371       9.062  -9.038 148.694  1.00 81.33           C  
ANISOU 2466  CG1 VAL A 371     9938  11411   9552   -210   -178   -171       C  
ATOM   2467  CG2 VAL A 371      10.792  -7.505 147.329  1.00 80.10           C  
ANISOU 2467  CG2 VAL A 371     9786  11106   9541   -145   -183   -313       C  
ATOM   2468  N   LEU A 372       6.950  -8.101 144.968  1.00 74.25           N  
ANISOU 2468  N   LEU A 372     9044  10256   8910   -150    -86   -209       N  
ATOM   2469  CA  LEU A 372       6.459  -9.078 143.931  1.00 71.69           C  
ANISOU 2469  CA  LEU A 372     8740   9860   8638   -155   -105   -133       C  
ATOM   2470  C   LEU A 372       7.501  -9.807 143.020  1.00 67.97           C  
ANISOU 2470  C   LEU A 372     8304   9293   8228   -139   -155    -97       C  
ATOM   2471  O   LEU A 372       8.233  -9.189 142.251  1.00 65.39           O  
ANISOU 2471  O   LEU A 372     7984   8903   7959   -106   -154   -146       O  
ATOM   2472  CB  LEU A 372       5.287  -8.500 143.086  1.00 72.72           C  
ANISOU 2472  CB  LEU A 372     8853   9962   8816   -140    -61   -157       C  
ATOM   2473  CG  LEU A 372       5.076  -6.968 142.831  1.00 75.30           C  
ANISOU 2473  CG  LEU A 372     9156  10279   9177   -105    -13   -254       C  
ATOM   2474  CD1 LEU A 372       6.156  -6.289 141.959  1.00 75.22           C  
ANISOU 2474  CD1 LEU A 372     9162  10180   9237    -68    -22   -300       C  
ATOM   2475  CD2 LEU A 372       3.664  -6.622 142.264  1.00 76.62           C  
ANISOU 2475  CD2 LEU A 372     9297  10443   9371    -96     27   -258       C  
ATOM   2476  N   LYS A 373       7.509 -11.136 143.147  1.00 65.20           N  
ANISOU 2476  N   LYS A 373     7972   8935   7865   -164   -196    -10       N  
ATOM   2477  CA  LYS A 373       8.412 -12.037 142.448  1.00 62.64           C  
ANISOU 2477  CA  LYS A 373     7680   8529   7592   -151   -248     31       C  
ATOM   2478  C   LYS A 373       7.671 -13.346 142.092  1.00 60.83           C  
ANISOU 2478  C   LYS A 373     7465   8266   7381   -178   -274    118       C  
ATOM   2479  O   LYS A 373       7.180 -14.009 142.961  1.00 61.38           O  
ANISOU 2479  O   LYS A 373     7532   8390   7399   -216   -283    180       O  
ATOM   2480  CB  LYS A 373       9.613 -12.302 143.340  1.00 62.73           C  
ANISOU 2480  CB  LYS A 373     7697   8572   7564   -152   -288     40       C  
ATOM   2481  CG  LYS A 373      10.593 -13.292 142.811  1.00 64.41           C  
ANISOU 2481  CG  LYS A 373     7936   8711   7825   -137   -345     83       C  
ATOM   2482  CD  LYS A 373      11.936 -13.222 143.548  1.00 66.53           C  
ANISOU 2482  CD  LYS A 373     8203   9009   8068   -125   -381     68       C  
ATOM   2483  CE  LYS A 373      12.934 -14.141 142.863  1.00 68.63           C  
ANISOU 2483  CE  LYS A 373     8490   9191   8396   -100   -434    100       C  
ATOM   2484  NZ  LYS A 373      14.273 -14.226 143.512  1.00 72.12           N  
ANISOU 2484  NZ  LYS A 373     8926   9656   8820    -85   -477     95       N  
ATOM   2485  N   LYS A 374       7.551 -13.688 140.814  1.00 58.48           N  
ANISOU 2485  N   LYS A 374     7183   7882   7155   -161   -283    121       N  
ATOM   2486  CA  LYS A 374       6.884 -14.932 140.370  1.00 56.74           C  
ANISOU 2486  CA  LYS A 374     6977   7617   6964   -186   -312    193       C  
ATOM   2487  C   LYS A 374       7.888 -15.762 139.597  1.00 54.88           C  
ANISOU 2487  C   LYS A 374     6772   7291   6788   -161   -363    207       C  
ATOM   2488  O   LYS A 374       8.708 -15.199 138.878  1.00 55.02           O  
ANISOU 2488  O   LYS A 374     6794   7270   6840   -120   -359    151       O  
ATOM   2489  CB  LYS A 374       5.742 -14.616 139.411  1.00 56.74           C  
ANISOU 2489  CB  LYS A 374     6964   7594   6999   -184   -279    173       C  
ATOM   2490  CG  LYS A 374       4.601 -13.859 140.019  1.00 60.25           C  
ANISOU 2490  CG  LYS A 374     7373   8121   7397   -204   -227    157       C  
ATOM   2491  CD  LYS A 374       3.481 -13.638 139.026  1.00 64.88           C  
ANISOU 2491  CD  LYS A 374     7945   8683   8024   -200   -204    143       C  
ATOM   2492  CE  LYS A 374       3.808 -12.504 138.056  1.00 69.58           C  
ANISOU 2492  CE  LYS A 374     8539   9240   8660   -149   -179     69       C  
ATOM   2493  NZ  LYS A 374       2.663 -12.177 137.105  1.00 72.67           N  
ANISOU 2493  NZ  LYS A 374     8911   9616   9084   -140   -157     56       N  
ATOM   2494  N   LYS A 375       7.832 -17.082 139.711  1.00 52.44           N  
ANISOU 2494  N   LYS A 375     6481   6947   6495   -185   -409    281       N  
ATOM   2495  CA  LYS A 375       8.717 -17.917 138.926  1.00 50.55           C  
ANISOU 2495  CA  LYS A 375     6269   6617   6321   -158   -458    288       C  
ATOM   2496  C   LYS A 375       8.240 -18.030 137.458  1.00 48.89           C  
ANISOU 2496  C   LYS A 375     6065   6336   6174   -140   -452    256       C  
ATOM   2497  O   LYS A 375       7.045 -18.195 137.199  1.00 49.11           O  
ANISOU 2497  O   LYS A 375     6085   6369   6206   -169   -437    274       O  
ATOM   2498  CB  LYS A 375       8.891 -19.309 139.587  1.00 51.37           C  
ANISOU 2498  CB  LYS A 375     6391   6698   6430   -186   -515    378       C  
ATOM   2499  CG  LYS A 375       9.730 -20.258 138.739  1.00 52.82           C  
ANISOU 2499  CG  LYS A 375     6600   6778   6690   -154   -568    381       C  
ATOM   2500  CD  LYS A 375      10.523 -21.261 139.536  1.00 60.67           C  
ANISOU 2500  CD  LYS A 375     7609   7753   7688   -157   -627    450       C  
ATOM   2501  CE  LYS A 375      11.195 -22.313 138.614  1.00 63.65           C  
ANISOU 2501  CE  LYS A 375     8010   8018   8155   -124   -681    450       C  
ATOM   2502  NZ  LYS A 375      10.217 -23.128 137.796  1.00 64.87           N  
ANISOU 2502  NZ  LYS A 375     8177   8103   8367   -147   -691    468       N  
ATOM   2503  N   ALA A 376       9.163 -17.933 136.513  1.00 46.65           N  
ANISOU 2503  N   ALA A 376     5793   5997   5936    -95   -464    209       N  
ATOM   2504  CA  ALA A 376       8.833 -18.038 135.107  1.00 45.50           C  
ANISOU 2504  CA  ALA A 376     5654   5794   5841    -75   -461    175       C  
ATOM   2505  C   ALA A 376       8.939 -19.509 134.677  1.00 45.95           C  
ANISOU 2505  C   ALA A 376     5735   5773   5952    -79   -517    212       C  
ATOM   2506  O   ALA A 376       9.876 -20.187 135.053  1.00 46.19           O  
ANISOU 2506  O   ALA A 376     5779   5774   5999    -68   -558    235       O  
ATOM   2507  CB  ALA A 376       9.762 -17.154 134.261  1.00 43.63           C  
ANISOU 2507  CB  ALA A 376     5415   5542   5621    -24   -439    105       C  
ATOM   2508  N   ILE A 377       7.961 -19.989 133.898  1.00 45.60           N  
ANISOU 2508  N   ILE A 377     5693   5695   5937    -96   -522    217       N  
ATOM   2509  CA  ILE A 377       7.902 -21.379 133.471  1.00 45.60           C  
ANISOU 2509  CA  ILE A 377     5713   5616   5995   -106   -576    245       C  
ATOM   2510  C   ILE A 377       7.489 -21.463 131.996  1.00 45.53           C  
ANISOU 2510  C   ILE A 377     5708   5565   6027    -87   -575    192       C  
ATOM   2511  O   ILE A 377       7.069 -20.452 131.380  1.00 44.27           O  
ANISOU 2511  O   ILE A 377     5533   5444   5844    -72   -532    148       O  
ATOM   2512  CB  ILE A 377       6.891 -22.218 134.306  1.00 45.65           C  
ANISOU 2512  CB  ILE A 377     5718   5627   5998   -170   -595    327       C  
ATOM   2513  CG1 ILE A 377       5.460 -21.867 133.882  1.00 46.20           C  
ANISOU 2513  CG1 ILE A 377     5767   5728   6059   -201   -563    319       C  
ATOM   2514  CG2 ILE A 377       7.083 -21.994 135.779  1.00 44.39           C  
ANISOU 2514  CG2 ILE A 377     5550   5534   5780   -194   -587    381       C  
ATOM   2515  CD1 ILE A 377       4.365 -22.680 134.541  1.00 43.45           C  
ANISOU 2515  CD1 ILE A 377     5410   5386   5714   -269   -576    395       C  
ATOM   2516  N   LEU A 378       7.629 -22.672 131.446  1.00 44.89           N  
ANISOU 2516  N   LEU A 378     5646   5404   6005    -85   -626    196       N  
ATOM   2517  CA  LEU A 378       7.131 -22.984 130.131  1.00 44.68           C  
ANISOU 2517  CA  LEU A 378     5624   5338   6016    -75   -635    149       C  
ATOM   2518  C   LEU A 378       5.935 -23.895 130.334  1.00 46.22           C  
ANISOU 2518  C   LEU A 378     5817   5507   6238   -134   -662    199       C  
ATOM   2519  O   LEU A 378       6.029 -24.848 131.094  1.00 49.10           O  
ANISOU 2519  O   LEU A 378     6193   5831   6630   -163   -701    259       O  
ATOM   2520  CB  LEU A 378       8.198 -23.660 129.294  1.00 42.78           C  
ANISOU 2520  CB  LEU A 378     5402   5026   5825    -26   -672    102       C  
ATOM   2521  CG  LEU A 378       9.228 -22.698 128.731  1.00 40.93           C  
ANISOU 2521  CG  LEU A 378     5162   4822   5566     31   -638     41       C  
ATOM   2522  CD1 LEU A 378      10.451 -23.427 128.166  1.00 36.77           C  
ANISOU 2522  CD1 LEU A 378     4649   4233   5087     80   -673      1       C  
ATOM   2523  CD2 LEU A 378       8.631 -21.694 127.661  1.00 37.02           C  
ANISOU 2523  CD2 LEU A 378     4654   4372   5041     45   -593     -9       C  
ATOM   2524  N   HIS A 379       4.825 -23.615 129.673  1.00 45.74           N  
ANISOU 2524  N   HIS A 379     5740   5469   6172   -152   -645    178       N  
ATOM   2525  CA  HIS A 379       3.596 -24.345 129.882  1.00 46.68           C  
ANISOU 2525  CA  HIS A 379     5848   5575   6314   -214   -664    224       C  
ATOM   2526  C   HIS A 379       2.848 -24.477 128.545  1.00 47.60           C  
ANISOU 2526  C   HIS A 379     5957   5673   6457   -211   -674    168       C  
ATOM   2527  O   HIS A 379       2.963 -23.612 127.649  1.00 46.73           O  
ANISOU 2527  O   HIS A 379     5840   5595   6319   -167   -647    107       O  
ATOM   2528  CB  HIS A 379       2.742 -23.603 130.906  1.00 46.53           C  
ANISOU 2528  CB  HIS A 379     5800   5643   6238   -255   -619    273       C  
ATOM   2529  CG  HIS A 379       1.467 -24.291 131.239  1.00 50.14           C  
ANISOU 2529  CG  HIS A 379     6238   6100   6714   -325   -631    327       C  
ATOM   2530  ND1 HIS A 379       1.363 -25.217 132.255  1.00 53.03           N  
ANISOU 2530  ND1 HIS A 379     6611   6443   7098   -377   -658    410       N  
ATOM   2531  CD2 HIS A 379       0.245 -24.230 130.658  1.00 52.14           C  
ANISOU 2531  CD2 HIS A 379     6463   6371   6975   -353   -624    314       C  
ATOM   2532  CE1 HIS A 379       0.126 -25.677 132.306  1.00 53.55           C  
ANISOU 2532  CE1 HIS A 379     6653   6514   7182   -438   -662    446       C  
ATOM   2533  NE2 HIS A 379      -0.573 -25.093 131.347  1.00 53.16           N  
ANISOU 2533  NE2 HIS A 379     6580   6490   7128   -424   -642    385       N  
ATOM   2534  N   GLN A 380       2.097 -25.564 128.410  1.00 48.39           N  
ANISOU 2534  N   GLN A 380     6056   5720   6610   -258   -716    190       N  
ATOM   2535  CA  GLN A 380       1.374 -25.881 127.192  1.00 49.38           C  
ANISOU 2535  CA  GLN A 380     6174   5822   6765   -261   -737    136       C  
ATOM   2536  C   GLN A 380       0.344 -24.822 126.834  1.00 47.79           C  
ANISOU 2536  C   GLN A 380     5937   5707   6514   -266   -694    119       C  
ATOM   2537  O   GLN A 380       0.169 -24.537 125.676  1.00 46.38           O  
ANISOU 2537  O   GLN A 380     5754   5537   6331   -236   -695     57       O  
ATOM   2538  CB  GLN A 380       0.668 -27.209 127.392  1.00 51.81           C  
ANISOU 2538  CB  GLN A 380     6482   6061   7142   -325   -788    176       C  
ATOM   2539  CG  GLN A 380       0.416 -28.044 126.135  1.00 59.17           C  
ANISOU 2539  CG  GLN A 380     7422   6926   8135   -322   -837    109       C  
ATOM   2540  CD  GLN A 380      -0.466 -29.258 126.470  1.00 69.16           C  
ANISOU 2540  CD  GLN A 380     8680   8126   9470   -399   -883    157       C  
ATOM   2541  OE1 GLN A 380      -1.648 -29.314 126.071  1.00 73.20           O  
ANISOU 2541  OE1 GLN A 380     9162   8660   9991   -442   -887    149       O  
ATOM   2542  NE2 GLN A 380       0.088 -30.217 127.247  1.00 70.58           N  
ANISOU 2542  NE2 GLN A 380     8886   8227   9705   -419   -918    214       N  
ATOM   2543  N   GLU A 381      -0.311 -24.242 127.839  1.00 47.16           N  
ANISOU 2543  N   GLU A 381     5830   5693   6395   -301   -655    175       N  
ATOM   2544  CA  GLU A 381      -1.368 -23.243 127.646  1.00 47.11           C  
ANISOU 2544  CA  GLU A 381     5784   5769   6348   -306   -613    165       C  
ATOM   2545  C   GLU A 381      -1.002 -21.818 128.106  1.00 44.95           C  
ANISOU 2545  C   GLU A 381     5501   5568   6011   -267   -553    160       C  
ATOM   2546  O   GLU A 381      -1.391 -20.857 127.467  1.00 44.98           O  
ANISOU 2546  O   GLU A 381     5485   5618   5989   -237   -525    123       O  
ATOM   2547  CB  GLU A 381      -2.656 -23.648 128.354  1.00 48.02           C  
ANISOU 2547  CB  GLU A 381     5863   5910   6472   -380   -612    224       C  
ATOM   2548  CG  GLU A 381      -3.404 -24.777 127.677  1.00 55.65           C  
ANISOU 2548  CG  GLU A 381     6823   6820   7501   -424   -664    218       C  
ATOM   2549  CD  GLU A 381      -2.917 -26.173 128.114  1.00 65.84           C  
ANISOU 2549  CD  GLU A 381     8146   8016   8855   -460   -716    259       C  
ATOM   2550  OE1 GLU A 381      -2.894 -26.472 129.351  1.00 67.83           O  
ANISOU 2550  OE1 GLU A 381     8397   8273   9101   -502   -708    338       O  
ATOM   2551  OE2 GLU A 381      -2.558 -26.972 127.201  1.00 69.96           O  
ANISOU 2551  OE2 GLU A 381     8692   8458   9431   -445   -766    211       O  
ATOM   2552  N   GLY A 382      -0.271 -21.687 129.203  1.00 43.49           N  
ANISOU 2552  N   GLY A 382     5328   5392   5804   -268   -538    195       N  
ATOM   2553  CA  GLY A 382       0.042 -20.394 129.769  1.00 41.33           C  
ANISOU 2553  CA  GLY A 382     5044   5185   5476   -239   -484    188       C  
ATOM   2554  C   GLY A 382      -1.221 -19.676 130.206  1.00 41.38           C  
ANISOU 2554  C   GLY A 382     5004   5268   5450   -266   -443    204       C  
ATOM   2555  O   GLY A 382      -2.253 -20.301 130.369  1.00 40.13           O  
ANISOU 2555  O   GLY A 382     4823   5117   5309   -317   -456    238       O  
ATOM   2556  N   HIS A 383      -1.148 -18.347 130.342  1.00 40.17           N  
ANISOU 2556  N   HIS A 383     4835   5170   5258   -230   -394    176       N  
ATOM   2557  CA  HIS A 383      -2.259 -17.574 130.833  1.00 39.68           C  
ANISOU 2557  CA  HIS A 383     4727   5183   5167   -246   -351    184       C  
ATOM   2558  C   HIS A 383      -2.601 -16.536 129.789  1.00 39.03           C  
ANISOU 2558  C   HIS A 383     4628   5116   5085   -198   -330    135       C  
ATOM   2559  O   HIS A 383      -1.753 -16.184 128.944  1.00 38.57           O  
ANISOU 2559  O   HIS A 383     4598   5024   5035   -150   -336     97       O  
ATOM   2560  CB  HIS A 383      -1.851 -16.893 132.128  1.00 40.53           C  
ANISOU 2560  CB  HIS A 383     4830   5343   5228   -246   -311    196       C  
ATOM   2561  CG  HIS A 383      -1.530 -17.850 133.213  1.00 43.78           C  
ANISOU 2561  CG  HIS A 383     5255   5750   5629   -292   -331    254       C  
ATOM   2562  ND1 HIS A 383      -2.464 -18.252 134.144  1.00 45.99           N  
ANISOU 2562  ND1 HIS A 383     5505   6081   5888   -351   -320    308       N  
ATOM   2563  CD2 HIS A 383      -0.393 -18.528 133.495  1.00 45.69           C  
ANISOU 2563  CD2 HIS A 383     5537   5944   5880   -289   -365    273       C  
ATOM   2564  CE1 HIS A 383      -1.903 -19.113 134.975  1.00 49.37           C  
ANISOU 2564  CE1 HIS A 383     5956   6493   6310   -383   -345    363       C  
ATOM   2565  NE2 HIS A 383      -0.647 -19.299 134.602  1.00 47.24           N  
ANISOU 2565  NE2 HIS A 383     5728   6160   6059   -344   -375    342       N  
ATOM   2566  N   MET A 384      -3.811 -16.004 129.880  1.00 37.69           N  
ANISOU 2566  N   MET A 384     4412   5002   4906   -209   -303    137       N  
ATOM   2567  CA  MET A 384      -4.322 -15.091 128.890  1.00 37.61           C  
ANISOU 2567  CA  MET A 384     4381   5009   4901   -166   -289    100       C  
ATOM   2568  C   MET A 384      -3.537 -13.749 128.845  1.00 36.65           C  
ANISOU 2568  C   MET A 384     4270   4894   4763   -108   -250     65       C  
ATOM   2569  O   MET A 384      -3.568 -13.015 127.839  1.00 34.36           O  
ANISOU 2569  O   MET A 384     3978   4597   4481    -62   -245     38       O  
ATOM   2570  CB  MET A 384      -5.821 -14.873 129.134  1.00 37.70           C  
ANISOU 2570  CB  MET A 384     4333   5082   4911   -193   -270    114       C  
ATOM   2571  CG  MET A 384      -6.128 -14.445 130.543  1.00 42.14           C  
ANISOU 2571  CG  MET A 384     4865   5704   5440   -215   -225    133       C  
ATOM   2572  SD  MET A 384      -6.149 -12.613 130.726  1.00 48.41           S  
ANISOU 2572  SD  MET A 384     5635   6544   6215   -151   -164     86       S  
ATOM   2573  CE  MET A 384      -7.833 -12.542 129.862  1.00 50.19           C  
ANISOU 2573  CE  MET A 384     5799   6805   6467   -154   -172     86       C  
ATOM   2574  N   ASP A 385      -2.827 -13.450 129.928  1.00 36.53           N  
ANISOU 2574  N   ASP A 385     4266   4891   4724   -110   -226     69       N  
ATOM   2575  CA  ASP A 385      -2.077 -12.205 129.993  1.00 37.26           C  
ANISOU 2575  CA  ASP A 385     4366   4985   4806    -63   -190     34       C  
ATOM   2576  C   ASP A 385      -0.558 -12.421 129.865  1.00 36.98           C  
ANISOU 2576  C   ASP A 385     4377   4899   4773    -44   -207     23       C  
ATOM   2577  O   ASP A 385       0.204 -11.578 130.314  1.00 36.61           O  
ANISOU 2577  O   ASP A 385     4336   4857   4716    -21   -180      0       O  
ATOM   2578  CB  ASP A 385      -2.405 -11.428 131.249  1.00 36.74           C  
ANISOU 2578  CB  ASP A 385     4269   4977   4712    -70   -145     28       C  
ATOM   2579  CG  ASP A 385      -2.017 -12.195 132.529  1.00 43.30           C  
ANISOU 2579  CG  ASP A 385     5111   5829   5512   -116   -151     59       C  
ATOM   2580  OD1 ASP A 385      -1.843 -13.445 132.495  1.00 46.29           O  
ANISOU 2580  OD1 ASP A 385     5511   6177   5898   -150   -192     96       O  
ATOM   2581  OD2 ASP A 385      -1.874 -11.545 133.586  1.00 48.99           O  
ANISOU 2581  OD2 ASP A 385     5818   6596   6200   -116   -117     45       O  
ATOM   2582  N   ASP A 386      -0.143 -13.521 129.220  1.00 36.61           N  
ANISOU 2582  N   ASP A 386     4359   4805   4745    -53   -252     33       N  
ATOM   2583  CA  ASP A 386       1.268 -13.790 128.926  1.00 36.69           C  
ANISOU 2583  CA  ASP A 386     4408   4768   4764    -30   -270     19       C  
ATOM   2584  C   ASP A 386       2.018 -12.792 128.020  1.00 36.50           C  
ANISOU 2584  C   ASP A 386     4394   4729   4746     23   -250    -19       C  
ATOM   2585  O   ASP A 386       3.227 -12.841 127.977  1.00 37.34           O  
ANISOU 2585  O   ASP A 386     4525   4807   4856     41   -255    -33       O  
ATOM   2586  CB  ASP A 386       1.428 -15.186 128.298  1.00 36.07           C  
ANISOU 2586  CB  ASP A 386     4353   4639   4712    -46   -323     29       C  
ATOM   2587  CG  ASP A 386       1.305 -16.314 129.300  1.00 38.67           C  
ANISOU 2587  CG  ASP A 386     4688   4960   5045    -96   -351     73       C  
ATOM   2588  OD1 ASP A 386       1.419 -16.078 130.513  1.00 40.69           O  
ANISOU 2588  OD1 ASP A 386     4936   5250   5274   -115   -331     96       O  
ATOM   2589  OD2 ASP A 386       1.073 -17.467 128.890  1.00 41.44           O  
ANISOU 2589  OD2 ASP A 386     5050   5269   5425   -119   -394     87       O  
ATOM   2590  N   ALA A 387       1.346 -11.950 127.235  1.00 36.80           N  
ANISOU 2590  N   ALA A 387     4414   4782   4786     48   -229    -31       N  
ATOM   2591  CA  ALA A 387       2.068 -11.091 126.238  1.00 35.42           C  
ANISOU 2591  CA  ALA A 387     4250   4589   4617     96   -213    -56       C  
ATOM   2592  C   ALA A 387       2.948 -10.093 126.944  1.00 34.45           C  
ANISOU 2592  C   ALA A 387     4129   4467   4493    111   -177    -71       C  
ATOM   2593  O   ALA A 387       2.488  -9.478 127.922  1.00 34.51           O  
ANISOU 2593  O   ALA A 387     4115   4505   4493    100   -150    -72       O  
ATOM   2594  CB  ALA A 387       1.095 -10.335 125.385  1.00 36.18           C  
ANISOU 2594  CB  ALA A 387     4324   4706   4716    119   -200    -55       C  
ATOM   2595  N   LEU A 388       4.177  -9.931 126.451  1.00 32.02           N  
ANISOU 2595  N   LEU A 388     3844   4131   4193    135   -175    -87       N  
ATOM   2596  CA  LEU A 388       5.185  -9.063 127.047  1.00 31.47           C  
ANISOU 2596  CA  LEU A 388     3775   4055   4127    146   -146   -106       C  
ATOM   2597  C   LEU A 388       5.380  -7.850 126.136  1.00 31.37           C  
ANISOU 2597  C   LEU A 388     3757   4031   4129    182   -115   -116       C  
ATOM   2598  O   LEU A 388       5.055  -7.904 124.951  1.00 30.80           O  
ANISOU 2598  O   LEU A 388     3690   3956   4058    201   -122   -106       O  
ATOM   2599  CB  LEU A 388       6.556  -9.812 127.116  1.00 31.16           C  
ANISOU 2599  CB  LEU A 388     3760   3990   4090    146   -169   -114       C  
ATOM   2600  CG  LEU A 388       6.582 -11.078 127.979  1.00 31.10           C  
ANISOU 2600  CG  LEU A 388     3761   3982   4074    113   -206    -97       C  
ATOM   2601  CD1 LEU A 388       7.928 -11.883 127.958  1.00 26.79           C  
ANISOU 2601  CD1 LEU A 388     3237   3405   3538    121   -235   -104       C  
ATOM   2602  CD2 LEU A 388       6.189 -10.679 129.384  1.00 30.34           C  
ANISOU 2602  CD2 LEU A 388     3647   3922   3957     88   -189    -90       C  
ATOM   2603  N   PHE A 389       5.938  -6.757 126.651  1.00 31.45           N  
ANISOU 2603  N   PHE A 389     3759   4036   4153    191    -81   -133       N  
ATOM   2604  CA  PHE A 389       6.402  -5.700 125.738  1.00 31.08           C  
ANISOU 2604  CA  PHE A 389     3713   3967   4129    222    -54   -136       C  
ATOM   2605  C   PHE A 389       7.905  -5.503 125.916  1.00 31.92           C  
ANISOU 2605  C   PHE A 389     3830   4053   4247    223    -45   -155       C  
ATOM   2606  O   PHE A 389       8.463  -5.895 126.951  1.00 32.83           O  
ANISOU 2606  O   PHE A 389     3946   4174   4355    202    -55   -171       O  
ATOM   2607  CB  PHE A 389       5.549  -4.422 125.815  1.00 29.63           C  
ANISOU 2607  CB  PHE A 389     3507   3785   3967    237    -21   -135       C  
ATOM   2608  CG  PHE A 389       5.739  -3.616 127.064  1.00 30.95           C  
ANISOU 2608  CG  PHE A 389     3659   3953   4148    228      4   -166       C  
ATOM   2609  CD1 PHE A 389       6.832  -2.712 127.185  1.00 32.27           C  
ANISOU 2609  CD1 PHE A 389     3828   4089   4344    235     29   -188       C  
ATOM   2610  CD2 PHE A 389       4.842  -3.699 128.117  1.00 28.85           C  
ANISOU 2610  CD2 PHE A 389     3373   3720   3868    211      7   -178       C  
ATOM   2611  CE1 PHE A 389       6.990  -1.906 128.333  1.00 29.63           C  
ANISOU 2611  CE1 PHE A 389     3477   3756   4026    226     51   -227       C  
ATOM   2612  CE2 PHE A 389       5.020  -2.894 129.293  1.00 28.86           C  
ANISOU 2612  CE2 PHE A 389     3358   3729   3877    204     33   -217       C  
ATOM   2613  CZ  PHE A 389       6.110  -2.004 129.403  1.00 23.47           C  
ANISOU 2613  CZ  PHE A 389     2679   3013   3225    212     52   -245       C  
ATOM   2614  N   LEU A 390       8.570  -4.956 124.902  1.00 31.97           N  
ANISOU 2614  N   LEU A 390     3840   4039   4268    244    -28   -150       N  
ATOM   2615  CA  LEU A 390      10.023  -4.864 124.915  1.00 32.16           C  
ANISOU 2615  CA  LEU A 390     3868   4047   4304    244    -19   -166       C  
ATOM   2616  C   LEU A 390      10.493  -3.424 125.079  1.00 32.38           C  
ANISOU 2616  C   LEU A 390     3882   4053   4369    248     21   -176       C  
ATOM   2617  O   LEU A 390       9.934  -2.518 124.438  1.00 33.39           O  
ANISOU 2617  O   LEU A 390     4005   4168   4515    265     44   -156       O  
ATOM   2618  CB  LEU A 390      10.541  -5.390 123.575  1.00 32.70           C  
ANISOU 2618  CB  LEU A 390     3949   4115   4360    263    -27   -154       C  
ATOM   2619  CG  LEU A 390      10.099  -6.823 123.259  1.00 35.05           C  
ANISOU 2619  CG  LEU A 390     4261   4426   4629    261    -69   -151       C  
ATOM   2620  CD1 LEU A 390      10.844  -7.296 122.044  1.00 37.46           C  
ANISOU 2620  CD1 LEU A 390     4577   4734   4924    282    -74   -155       C  
ATOM   2621  CD2 LEU A 390      10.414  -7.747 124.417  1.00 33.43           C  
ANISOU 2621  CD2 LEU A 390     4061   4219   4422    238    -99   -166       C  
ATOM   2622  N   THR A 391      11.531  -3.202 125.878  1.00 30.80           N  
ANISOU 2622  N   THR A 391     3674   3844   4183    234     26   -205       N  
ATOM   2623  CA  THR A 391      12.101  -1.870 125.979  1.00 30.75           C  
ANISOU 2623  CA  THR A 391     3654   3810   4220    234     62   -219       C  
ATOM   2624  C   THR A 391      13.615  -1.962 125.820  1.00 31.67           C  
ANISOU 2624  C   THR A 391     3765   3918   4349    227     65   -232       C  
ATOM   2625  O   THR A 391      14.278  -2.782 126.449  1.00 32.60           O  
ANISOU 2625  O   THR A 391     3883   4053   4450    216     40   -252       O  
ATOM   2626  CB  THR A 391      11.727  -1.191 127.332  1.00 30.55           C  
ANISOU 2626  CB  THR A 391     3613   3785   4209    219     71   -255       C  
ATOM   2627  OG1 THR A 391      10.306  -1.221 127.480  1.00 30.05           O  
ANISOU 2627  OG1 THR A 391     3549   3737   4131    226     68   -244       O  
ATOM   2628  CG2 THR A 391      12.202   0.255 127.399  1.00 27.98           C  
ANISOU 2628  CG2 THR A 391     3272   3419   3940    218    106   -275       C  
ATOM   2629  N   ARG A 392      14.165  -1.097 124.987  1.00 32.57           N  
ANISOU 2629  N   ARG A 392     3873   4008   4495    234     97   -217       N  
ATOM   2630  CA  ARG A 392      15.526  -1.159 124.618  1.00 33.49           C  
ANISOU 2630  CA  ARG A 392     3979   4122   4623    229    106   -223       C  
ATOM   2631  C   ARG A 392      16.358  -0.519 125.708  1.00 35.25           C  
ANISOU 2631  C   ARG A 392     4181   4330   4882    206    113   -265       C  
ATOM   2632  O   ARG A 392      16.028   0.582 126.219  1.00 35.18           O  
ANISOU 2632  O   ARG A 392     4162   4293   4910    196    133   -280       O  
ATOM   2633  CB  ARG A 392      15.663  -0.399 123.323  1.00 34.40           C  
ANISOU 2633  CB  ARG A 392     4093   4221   4758    242    141   -183       C  
ATOM   2634  CG  ARG A 392      17.138  -0.170 122.871  1.00 38.84           C  
ANISOU 2634  CG  ARG A 392     4636   4780   5341    232    163   -185       C  
ATOM   2635  CD  ARG A 392      17.391  -0.700 121.501  1.00 42.41           C  
ANISOU 2635  CD  ARG A 392     5094   5259   5759    252    171   -152       C  
ATOM   2636  NE  ARG A 392      18.821  -0.698 121.190  1.00 45.36           N  
ANISOU 2636  NE  ARG A 392     5445   5643   6147    243    190   -162       N  
ATOM   2637  CZ  ARG A 392      19.402   0.008 120.217  1.00 43.73           C  
ANISOU 2637  CZ  ARG A 392     5225   5436   5954    240    231   -127       C  
ATOM   2638  NH1 ARG A 392      18.715   0.806 119.432  1.00 40.61           N  
ANISOU 2638  NH1 ARG A 392     4840   5028   5562    247    256    -75       N  
ATOM   2639  NH2 ARG A 392      20.702  -0.088 120.039  1.00 43.70           N  
ANISOU 2639  NH2 ARG A 392     5194   5448   5962    231    248   -142       N  
ATOM   2640  N   CYS A 393      17.462  -1.180 126.044  1.00 35.33           N  
ANISOU 2640  N   CYS A 393     4181   4358   4885    197     95   -288       N  
ATOM   2641  CA  CYS A 393      18.362  -0.691 127.058  1.00 36.92           C  
ANISOU 2641  CA  CYS A 393     4359   4555   5115    174     94   -332       C  
ATOM   2642  C   CYS A 393      19.177   0.475 126.486  1.00 37.22           C  
ANISOU 2642  C   CYS A 393     4374   4559   5209    162    135   -329       C  
ATOM   2643  O   CYS A 393      19.360   0.515 125.279  1.00 38.05           O  
ANISOU 2643  O   CYS A 393     4482   4660   5317    174    157   -290       O  
ATOM   2644  CB  CYS A 393      19.272  -1.855 127.397  1.00 37.26           C  
ANISOU 2644  CB  CYS A 393     4396   4629   5133    175     59   -347       C  
ATOM   2645  SG  CYS A 393      20.448  -1.523 128.650  1.00 46.28           S  
ANISOU 2645  SG  CYS A 393     5506   5781   6298    149     45   -400       S  
ATOM   2646  N   GLN A 394      19.700   1.423 127.269  1.00 36.35           N  
ANISOU 2646  N   GLN A 394     4241   4427   5145    137    147   -368       N  
ATOM   2647  CA  GLN A 394      20.576   2.422 126.577  1.00 36.51           C  
ANISOU 2647  CA  GLN A 394     4238   4411   5224    122    186   -356       C  
ATOM   2648  C   GLN A 394      22.051   2.025 126.663  1.00 37.47           C  
ANISOU 2648  C   GLN A 394     4328   4555   5352    108    178   -379       C  
ATOM   2649  O   GLN A 394      22.379   1.109 127.473  1.00 37.53           O  
ANISOU 2649  O   GLN A 394     4333   4600   5326    110    138   -411       O  
ATOM   2650  CB  GLN A 394      20.291   3.867 127.030  1.00 36.37           C  
ANISOU 2650  CB  GLN A 394     4209   4338   5270    103    210   -377       C  
ATOM   2651  CG  GLN A 394      18.830   4.247 126.822  1.00 35.08           C  
ANISOU 2651  CG  GLN A 394     4072   4154   5104    125    219   -351       C  
ATOM   2652  CD  GLN A 394      18.430   5.638 127.351  1.00 36.32           C  
ANISOU 2652  CD  GLN A 394     4219   4252   5329    114    239   -380       C  
ATOM   2653  OE1 GLN A 394      19.183   6.326 128.058  1.00 39.08           O  
ANISOU 2653  OE1 GLN A 394     4545   4577   5728     86    244   -431       O  
ATOM   2654  NE2 GLN A 394      17.246   6.040 127.006  1.00 30.51           N  
ANISOU 2654  NE2 GLN A 394     3499   3492   4600    137    250   -351       N  
ATOM   2655  N   GLN A 395      22.941   2.663 125.878  1.00 41.09           N  
ANISOU 2655  N   GLN A 395     4911   5021   5679   -140   -459    120       N  
ATOM   2656  CA  GLN A 395      24.287   2.125 125.799  1.00 43.10           C  
ANISOU 2656  CA  GLN A 395     5201   5344   5833   -163   -415     29       C  
ATOM   2657  C   GLN A 395      25.093   2.100 127.077  1.00 42.71           C  
ANISOU 2657  C   GLN A 395     5092   5350   5788   -148   -327    -63       C  
ATOM   2658  O   GLN A 395      25.776   1.102 127.345  1.00 42.76           O  
ANISOU 2658  O   GLN A 395     5092   5422   5734   -136   -326   -126       O  
ATOM   2659  CB  GLN A 395      25.110   2.524 124.555  1.00 44.60           C  
ANISOU 2659  CB  GLN A 395     5474   5550   5921   -210   -402     28       C  
ATOM   2660  CG  GLN A 395      25.914   3.793 124.628  1.00 52.16           C  
ANISOU 2660  CG  GLN A 395     6438   6501   6878   -258   -311     15       C  
ATOM   2661  CD  GLN A 395      27.281   3.658 125.290  1.00 58.04           C  
ANISOU 2661  CD  GLN A 395     7146   7335   7570   -277   -223    -88       C  
ATOM   2662  OE1 GLN A 395      28.055   2.732 125.003  1.00 60.86           O  
ANISOU 2662  OE1 GLN A 395     7509   7789   7827   -265   -219   -144       O  
ATOM   2663  NE2 GLN A 395      27.600   4.620 126.170  1.00 60.43           N  
ANISOU 2663  NE2 GLN A 395     7415   7608   7938   -299   -160   -120       N  
ATOM   2664  N   GLU A 396      24.993   3.141 127.888  1.00 42.73           N  
ANISOU 2664  N   GLU A 396     5054   5323   5858   -137   -264    -76       N  
ATOM   2665  CA  GLU A 396      25.752   3.175 129.124  1.00 42.97           C  
ANISOU 2665  CA  GLU A 396     5033   5409   5886   -121   -189   -169       C  
ATOM   2666  C   GLU A 396      25.468   1.935 129.992  1.00 41.83           C  
ANISOU 2666  C   GLU A 396     4827   5327   5740    -76   -210   -180       C  
ATOM   2667  O   GLU A 396      26.355   1.371 130.633  1.00 41.46           O  
ANISOU 2667  O   GLU A 396     4759   5351   5643    -68   -176   -256       O  
ATOM   2668  CB  GLU A 396      25.495   4.474 129.908  1.00 44.05           C  
ANISOU 2668  CB  GLU A 396     5147   5491   6099    -99   -140   -189       C  
ATOM   2669  CG  GLU A 396      26.054   4.398 131.361  1.00 50.31           C  
ANISOU 2669  CG  GLU A 396     5878   6350   6887    -64    -77   -288       C  
ATOM   2670  CD  GLU A 396      26.013   5.721 132.164  1.00 57.65           C  
ANISOU 2670  CD  GLU A 396     6805   7223   7875    -36    -35   -342       C  
ATOM   2671  OE1 GLU A 396      26.755   6.667 131.787  1.00 58.55           O  
ANISOU 2671  OE1 GLU A 396     6976   7276   7992   -101    -21   -372       O  
ATOM   2672  OE2 GLU A 396      25.259   5.774 133.195  1.00 59.57           O  
ANISOU 2672  OE2 GLU A 396     6989   7489   8155     51    -20   -356       O  
ATOM   2673  N   GLU A 397      24.231   1.499 130.011  1.00 41.26           N  
ANISOU 2673  N   GLU A 397     4722   5232   5722    -50   -273    -94       N  
ATOM   2674  CA  GLU A 397      23.843   0.485 130.984  1.00 41.13           C  
ANISOU 2674  CA  GLU A 397     4635   5272   5718    -20   -290    -78       C  
ATOM   2675  C   GLU A 397      24.193  -0.883 130.389  1.00 38.61           C  
ANISOU 2675  C   GLU A 397     4368   4959   5344    -45   -372    -77       C  
ATOM   2676  O   GLU A 397      24.649  -1.768 131.069  1.00 38.26           O  
ANISOU 2676  O   GLU A 397     4306   4960   5271    -31   -376   -111       O  
ATOM   2677  CB  GLU A 397      22.342   0.648 131.356  1.00 41.61           C  
ANISOU 2677  CB  GLU A 397     4616   5328   5866     11   -318     27       C  
ATOM   2678  CG  GLU A 397      21.669  -0.521 132.048  1.00 48.33           C  
ANISOU 2678  CG  GLU A 397     5391   6236   6737     13   -365    100       C  
ATOM   2679  CD  GLU A 397      20.150  -0.296 132.427  1.00 57.49           C  
ANISOU 2679  CD  GLU A 397     6438   7426   7978     42   -381    219       C  
ATOM   2680  OE1 GLU A 397      19.366   0.349 131.659  1.00 58.64           O  
ANISOU 2680  OE1 GLU A 397     6585   7521   8173     48   -417    277       O  
ATOM   2681  OE2 GLU A 397      19.753  -0.810 133.511  1.00 59.22           O  
ANISOU 2681  OE2 GLU A 397     6559   7735   8206     61   -358    263       O  
ATOM   2682  N   SER A 398      23.936  -1.014 129.111  1.00 37.06           N  
ANISOU 2682  N   SER A 398     4242   4708   5130    -72   -447    -39       N  
ATOM   2683  CA  SER A 398      24.312  -2.149 128.285  1.00 36.72           C  
ANISOU 2683  CA  SER A 398     4278   4653   5020    -82   -537    -59       C  
ATOM   2684  C   SER A 398      25.844  -2.420 128.338  1.00 34.76           C  
ANISOU 2684  C   SER A 398     4065   4470   4672    -61   -478   -180       C  
ATOM   2685  O   SER A 398      26.305  -3.522 128.637  1.00 35.01           O  
ANISOU 2685  O   SER A 398     4113   4522   4667    -32   -519   -224       O  
ATOM   2686  CB  SER A 398      23.959  -1.701 126.886  1.00 37.46           C  
ANISOU 2686  CB  SER A 398     4443   4697   5092   -106   -589    -17       C  
ATOM   2687  OG  SER A 398      23.800  -2.816 126.118  1.00 42.94           O  
ANISOU 2687  OG  SER A 398     5209   5362   5745   -108   -710    -12       O  
ATOM   2688  N   GLN A 399      26.632  -1.391 128.091  1.00 32.14           N  
ANISOU 2688  N   GLN A 399     3739   4172   4303    -76   -386   -227       N  
ATOM   2689  CA  GLN A 399      28.045  -1.527 128.263  1.00 31.90           C  
ANISOU 2689  CA  GLN A 399     3707   4226   4188    -62   -320   -330       C  
ATOM   2690  C   GLN A 399      28.408  -1.950 129.664  1.00 31.26           C  
ANISOU 2690  C   GLN A 399     3559   4193   4127    -29   -285   -379       C  
ATOM   2691  O   GLN A 399      29.125  -2.929 129.848  1.00 33.21           O  
ANISOU 2691  O   GLN A 399     3816   4486   4315     12   -308   -440       O  
ATOM   2692  CB  GLN A 399      28.783  -0.259 127.837  1.00 31.75           C  
ANISOU 2692  CB  GLN A 399     3688   4237   4138   -110   -230   -350       C  
ATOM   2693  CG  GLN A 399      30.202  -0.340 128.064  1.00 31.36           C  
ANISOU 2693  CG  GLN A 399     3612   4295   4010   -106   -162   -443       C  
ATOM   2694  CD  GLN A 399      30.901   0.983 127.748  1.00 37.27           C  
ANISOU 2694  CD  GLN A 399     4348   5069   4745   -182    -79   -443       C  
ATOM   2695  OE1 GLN A 399      30.827   1.916 128.522  1.00 36.52           O  
ANISOU 2695  OE1 GLN A 399     4216   4935   4723   -216    -35   -444       O  
ATOM   2696  NE2 GLN A 399      31.576   1.058 126.594  1.00 39.72           N  
ANISOU 2696  NE2 GLN A 399     4690   5446   4957   -208    -63   -437       N  
ATOM   2697  N   ALA A 400      27.901  -1.262 130.664  1.00 29.71           N  
ANISOU 2697  N   ALA A 400     3297   3986   4005    -34   -237   -355       N  
ATOM   2698  CA  ALA A 400      28.139  -1.674 132.020  1.00 29.67           C  
ANISOU 2698  CA  ALA A 400     3230   4037   4008      1   -208   -391       C  
ATOM   2699  C   ALA A 400      27.850  -3.145 132.232  1.00 30.58           C  
ANISOU 2699  C   ALA A 400     3356   4148   4116     30   -297   -359       C  
ATOM   2700  O   ALA A 400      28.644  -3.830 132.900  1.00 31.40           O  
ANISOU 2700  O   ALA A 400     3447   4308   4175     65   -292   -418       O  
ATOM   2701  CB  ALA A 400      27.258  -0.870 132.980  1.00 29.64           C  
ANISOU 2701  CB  ALA A 400     3159   4023   4081     10   -165   -351       C  
ATOM   2702  N   ALA A 401      26.707  -3.635 131.738  1.00 30.28           N  
ANISOU 2702  N   ALA A 401     3340   4038   4128     12   -389   -260       N  
ATOM   2703  CA  ALA A 401      26.386  -5.016 132.005  1.00 31.80           C  
ANISOU 2703  CA  ALA A 401     3547   4206   4328     21   -491   -216       C  
ATOM   2704  C   ALA A 401      27.419  -5.974 131.366  1.00 32.62           C  
ANISOU 2704  C   ALA A 401     3742   4304   4349     60   -551   -304       C  
ATOM   2705  O   ALA A 401      27.852  -6.903 132.003  1.00 32.40           O  
ANISOU 2705  O   ALA A 401     3719   4289   4302     95   -588   -327       O  
ATOM   2706  CB  ALA A 401      24.957  -5.354 131.578  1.00 31.44           C  
ANISOU 2706  CB  ALA A 401     3502   4085   4360    -22   -593    -87       C  
ATOM   2707  N   ARG A 402      27.823  -5.745 130.118  1.00 33.64           N  
ANISOU 2707  N   ARG A 402     3942   4422   4419     64   -562   -352       N  
ATOM   2708  CA  ARG A 402      28.907  -6.557 129.569  1.00 35.64           C  
ANISOU 2708  CA  ARG A 402     4266   4702   4572    128   -598   -455       C  
ATOM   2709  C   ARG A 402      30.200  -6.436 130.407  1.00 35.85           C  
ANISOU 2709  C   ARG A 402     4235   4841   4546    173   -500   -551       C  
ATOM   2710  O   ARG A 402      30.820  -7.479 130.721  1.00 36.52           O  
ANISOU 2710  O   ARG A 402     4347   4939   4591    242   -552   -607       O  
ATOM   2711  CB  ARG A 402      29.152  -6.249 128.078  1.00 37.09           C  
ANISOU 2711  CB  ARG A 402     4524   4890   4678    132   -608   -489       C  
ATOM   2712  CG  ARG A 402      30.361  -6.915 127.476  1.00 38.07           C  
ANISOU 2712  CG  ARG A 402     4705   5083   4676    219   -618   -607       C  
ATOM   2713  CD  ARG A 402      30.123  -8.393 127.355  1.00 40.56           C  
ANISOU 2713  CD  ARG A 402     5114   5310   4988    282   -775   -628       C  
ATOM   2714  NE  ARG A 402      31.346  -9.095 126.975  1.00 41.41           N  
ANISOU 2714  NE  ARG A 402     5269   5490   4974    398   -784   -760       N  
ATOM   2715  CZ  ARG A 402      31.406 -10.278 126.369  1.00 41.63           C  
ANISOU 2715  CZ  ARG A 402     5416   5452   4951    487   -924   -821       C  
ATOM   2716  NH1 ARG A 402      30.305 -10.925 126.043  1.00 39.51           N  
ANISOU 2716  NH1 ARG A 402     5236   5029   4747    452  -1080   -757       N  
ATOM   2717  NH2 ARG A 402      32.589 -10.808 126.071  1.00 42.45           N  
ANISOU 2717  NH2 ARG A 402     5548   5646   4935    616   -914   -952       N  
ATOM   2718  N   MET A 403      30.569  -5.218 130.835  1.00 34.30           N  
ANISOU 2718  N   MET A 403     3962   4712   4356    136   -375   -568       N  
ATOM   2719  CA  MET A 403      31.775  -5.084 131.643  1.00 35.20           C  
ANISOU 2719  CA  MET A 403     4014   4935   4424    167   -296   -657       C  
ATOM   2720  C   MET A 403      31.666  -5.893 132.922  1.00 36.64           C  
ANISOU 2720  C   MET A 403     4166   5120   4636    205   -330   -646       C  
ATOM   2721  O   MET A 403      32.678  -6.406 133.431  1.00 38.35           O  
ANISOU 2721  O   MET A 403     4362   5412   4798    264   -321   -721       O  
ATOM   2722  CB  MET A 403      32.113  -3.640 131.994  1.00 35.17           C  
ANISOU 2722  CB  MET A 403     3942   4982   4437    108   -179   -674       C  
ATOM   2723  CG  MET A 403      32.107  -2.635 130.801  1.00 35.72           C  
ANISOU 2723  CG  MET A 403     4041   5038   4494     46   -143   -652       C  
ATOM   2724  SD  MET A 403      32.761  -1.084 131.400  1.00 47.84           S  
ANISOU 2724  SD  MET A 403     5504   6619   6053    -27    -29   -686       S  
ATOM   2725  CE  MET A 403      31.860  -0.001 130.381  1.00 48.92           C  
ANISOU 2725  CE  MET A 403     5693   6653   6240    -97    -32   -594       C  
ATOM   2726  N   ILE A 404      30.464  -6.034 133.472  1.00 36.67           N  
ANISOU 2726  N   ILE A 404     4156   5056   4720    175   -369   -543       N  
ATOM   2727  CA  ILE A 404      30.333  -6.756 134.737  1.00 36.14           C  
ANISOU 2727  CA  ILE A 404     4052   5009   4673    200   -394   -510       C  
ATOM   2728  C   ILE A 404      30.556  -8.220 134.423  1.00 38.29           C  
ANISOU 2728  C   ILE A 404     4405   5224   4920    250   -521   -514       C  
ATOM   2729  O   ILE A 404      31.225  -8.931 135.175  1.00 39.77           O  
ANISOU 2729  O   ILE A 404     4586   5450   5074    305   -541   -548       O  
ATOM   2730  CB  ILE A 404      28.941  -6.559 135.391  1.00 35.94           C  
ANISOU 2730  CB  ILE A 404     3973   4951   4730    154   -400   -382       C  
ATOM   2731  CG1 ILE A 404      28.799  -5.136 135.940  1.00 33.73           C  
ANISOU 2731  CG1 ILE A 404     3618   4730   4468    137   -279   -401       C  
ATOM   2732  CG2 ILE A 404      28.661  -7.591 136.458  1.00 30.92           C  
ANISOU 2732  CG2 ILE A 404     3314   4326   4106    168   -456   -310       C  
ATOM   2733  CD1 ILE A 404      27.335  -4.760 136.117  1.00 27.26           C  
ANISOU 2733  CD1 ILE A 404     2752   3879   3726    106   -282   -283       C  
ATOM   2734  N   HIS A 405      30.010  -8.673 133.306  1.00 38.90           N  
ANISOU 2734  N   HIS A 405     4567   5203   5011    237   -617   -483       N  
ATOM   2735  CA  HIS A 405      30.241 -10.036 132.863  1.00 40.63           C  
ANISOU 2735  CA  HIS A 405     4889   5344   5204    294   -757   -508       C  
ATOM   2736  C   HIS A 405      31.738 -10.414 132.731  1.00 41.34           C  
ANISOU 2736  C   HIS A 405     5003   5513   5191    404   -737   -652       C  
ATOM   2737  O   HIS A 405      32.154 -11.462 133.194  1.00 41.36           O  
ANISOU 2737  O   HIS A 405     5045   5490   5179    473   -818   -675       O  
ATOM   2738  CB  HIS A 405      29.569 -10.252 131.522  1.00 41.13           C  
ANISOU 2738  CB  HIS A 405     5046   5305   5275    271   -855   -486       C  
ATOM   2739  CG  HIS A 405      29.863 -11.580 130.925  1.00 41.74           C  
ANISOU 2739  CG  HIS A 405     5252   5291   5316    345  -1010   -540       C  
ATOM   2740  ND1 HIS A 405      29.441 -12.755 131.502  1.00 44.59           N  
ANISOU 2740  ND1 HIS A 405     5663   5544   5735    341  -1150   -474       N  
ATOM   2741  CD2 HIS A 405      30.555 -11.927 129.817  1.00 42.08           C  
ANISOU 2741  CD2 HIS A 405     5390   5334   5264    432  -1054   -656       C  
ATOM   2742  CE1 HIS A 405      29.828 -13.774 130.750  1.00 44.80           C  
ANISOU 2742  CE1 HIS A 405     5825   5481   5716    424  -1288   -555       C  
ATOM   2743  NE2 HIS A 405      30.514 -13.297 129.729  1.00 42.51           N  
ANISOU 2743  NE2 HIS A 405     5561   5265   5325    492  -1227   -674       N  
ATOM   2744  N   SER A 406      32.535  -9.548 132.115  1.00 41.38           N  
ANISOU 2744  N   SER A 406     4976   5619   5125    419   -631   -739       N  
ATOM   2745  CA  SER A 406      33.940  -9.849 131.915  1.00 42.46           C  
ANISOU 2745  CA  SER A 406     5111   5863   5159    522   -603   -869       C  
ATOM   2746  C   SER A 406      34.728  -9.756 133.172  1.00 42.00           C  
ANISOU 2746  C   SER A 406     4960   5906   5092    549   -537   -903       C  
ATOM   2747  O   SER A 406      35.566 -10.622 133.453  1.00 43.20           O  
ANISOU 2747  O   SER A 406     5127   6095   5194    654   -584   -973       O  
ATOM   2748  CB  SER A 406      34.543  -8.935 130.889  1.00 42.14           C  
ANISOU 2748  CB  SER A 406     5047   5922   5043    512   -507   -928       C  
ATOM   2749  OG  SER A 406      33.934  -9.353 129.686  1.00 46.99           O  
ANISOU 2749  OG  SER A 406     5769   6445   5638    524   -599   -914       O  
ATOM   2750  N   THR A 407      34.472  -8.694 133.914  1.00 40.20           N  
ANISOU 2750  N   THR A 407     4641   5722   4909    463   -437   -861       N  
ATOM   2751  CA  THR A 407      35.071  -8.524 135.203  1.00 39.10           C  
ANISOU 2751  CA  THR A 407     4416   5675   4764    477   -381   -887       C  
ATOM   2752  C   THR A 407      34.755  -9.720 136.115  1.00 39.56           C  
ANISOU 2752  C   THR A 407     4508   5676   4848    525   -483   -833       C  
ATOM   2753  O   THR A 407      35.653 -10.307 136.699  1.00 39.89           O  
ANISOU 2753  O   THR A 407     4533   5782   4842    607   -502   -891       O  
ATOM   2754  CB  THR A 407      34.601  -7.209 135.796  1.00 38.13           C  
ANISOU 2754  CB  THR A 407     4217   5578   4691    382   -280   -849       C  
ATOM   2755  OG1 THR A 407      34.886  -6.171 134.840  1.00 36.86           O  
ANISOU 2755  OG1 THR A 407     4046   5446   4514    329   -208   -883       O  
ATOM   2756  CG2 THR A 407      35.333  -6.918 137.083  1.00 38.67           C  
ANISOU 2756  CG2 THR A 407     4200   5757   4736    398   -223   -899       C  
ATOM   2757  N   ALA A 408      33.498 -10.099 136.254  1.00 38.88           N  
ANISOU 2757  N   ALA A 408     4463   5474   4837    472   -553   -712       N  
ATOM   2758  CA  ALA A 408      33.257 -11.188 137.153  1.00 40.08           C  
ANISOU 2758  CA  ALA A 408     4639   5580   5011    500   -647   -642       C  
ATOM   2759  C   ALA A 408      34.062 -12.403 136.683  1.00 41.59           C  
ANISOU 2759  C   ALA A 408     4925   5724   5155    613   -763   -717       C  
ATOM   2760  O   ALA A 408      34.630 -13.116 137.488  1.00 42.87           O  
ANISOU 2760  O   ALA A 408     5087   5909   5293    682   -807   -727       O  
ATOM   2761  CB  ALA A 408      31.758 -11.508 137.286  1.00 38.88           C  
ANISOU 2761  CB  ALA A 408     4508   5316   4949    412   -719   -481       C  
ATOM   2762  N   GLY A 409      34.123 -12.646 135.379  1.00 42.88           N  
ANISOU 2762  N   GLY A 409     5173   5825   5296    646   -817   -773       N  
ATOM   2763  CA  GLY A 409      34.799 -13.838 134.871  1.00 43.84           C  
ANISOU 2763  CA  GLY A 409     5401   5889   5368    777   -941   -857       C  
ATOM   2764  C   GLY A 409      36.274 -13.783 135.237  1.00 45.28           C  
ANISOU 2764  C   GLY A 409     5515   6229   5459    892   -871   -983       C  
ATOM   2765  O   GLY A 409      36.837 -14.750 135.740  1.00 46.75           O  
ANISOU 2765  O   GLY A 409     5740   6399   5625    998   -957  -1013       O  
ATOM   2766  N   LEU A 410      36.889 -12.635 134.996  1.00 44.81           N  
ANISOU 2766  N   LEU A 410     5353   6323   5350    866   -721  -1049       N  
ATOM   2767  CA  LEU A 410      38.295 -12.463 135.209  1.00 46.25           C  
ANISOU 2767  CA  LEU A 410     5449   6678   5446    956   -649  -1165       C  
ATOM   2768  C   LEU A 410      38.651 -12.638 136.674  1.00 47.51           C  
ANISOU 2768  C   LEU A 410     5541   6893   5618    971   -644  -1144       C  
ATOM   2769  O   LEU A 410      39.536 -13.428 136.983  1.00 48.97           O  
ANISOU 2769  O   LEU A 410     5730   7125   5753   1100   -699  -1210       O  
ATOM   2770  CB  LEU A 410      38.754 -11.096 134.708  1.00 45.38           C  
ANISOU 2770  CB  LEU A 410     5234   6709   5297    882   -496  -1208       C  
ATOM   2771  CG  LEU A 410      40.243 -10.806 134.854  1.00 45.62           C  
ANISOU 2771  CG  LEU A 410     5149   6944   5240    951   -414  -1318       C  
ATOM   2772  CD1 LEU A 410      41.032 -11.904 134.181  1.00 43.94           C  
ANISOU 2772  CD1 LEU A 410     4988   6766   4939   1130   -490  -1416       C  
ATOM   2773  CD2 LEU A 410      40.564  -9.422 134.245  1.00 43.66           C  
ANISOU 2773  CD2 LEU A 410     4808   6811   4968    842   -277  -1330       C  
ATOM   2774  N   TYR A 411      37.958 -11.941 137.574  1.00 47.03           N  
ANISOU 2774  N   TYR A 411     5423   6831   5616    855   -586  -1054       N  
ATOM   2775  CA  TYR A 411      38.345 -12.011 138.962  1.00 47.86           C  
ANISOU 2775  CA  TYR A 411     5459   7015   5711    872   -573  -1041       C  
ATOM   2776  C   TYR A 411      37.990 -13.357 139.573  1.00 49.15           C  
ANISOU 2776  C   TYR A 411     5709   7068   5899    932   -714   -962       C  
ATOM   2777  O   TYR A 411      38.632 -13.781 140.540  1.00 48.82           O  
ANISOU 2777  O   TYR A 411     5634   7094   5822    999   -738   -974       O  
ATOM   2778  CB  TYR A 411      37.772 -10.861 139.792  1.00 46.57           C  
ANISOU 2778  CB  TYR A 411     5212   6900   5583    752   -469   -986       C  
ATOM   2779  CG  TYR A 411      38.143  -9.467 139.332  1.00 46.08           C  
ANISOU 2779  CG  TYR A 411     5073   6928   5509    680   -343  -1055       C  
ATOM   2780  CD1 TYR A 411      39.127  -9.250 138.372  1.00 44.01           C  
ANISOU 2780  CD1 TYR A 411     4786   6743   5192    715   -309  -1155       C  
ATOM   2781  CD2 TYR A 411      37.526  -8.347 139.903  1.00 46.07           C  
ANISOU 2781  CD2 TYR A 411     5019   6937   5547    581   -262  -1018       C  
ATOM   2782  CE1 TYR A 411      39.437  -7.974 137.945  1.00 44.15           C  
ANISOU 2782  CE1 TYR A 411     4736   6833   5206    627   -203  -1193       C  
ATOM   2783  CE2 TYR A 411      37.858  -7.054 139.507  1.00 44.65           C  
ANISOU 2783  CE2 TYR A 411     4785   6812   5369    508   -166  -1075       C  
ATOM   2784  CZ  TYR A 411      38.795  -6.882 138.532  1.00 44.82           C  
ANISOU 2784  CZ  TYR A 411     4787   6896   5345    519   -140  -1152       C  
ATOM   2785  OH  TYR A 411      39.068  -5.601 138.128  1.00 46.96           O  
ANISOU 2785  OH  TYR A 411     5009   7209   5626    425    -54  -1182       O  
ATOM   2786  N   ASN A 412      36.992 -14.036 139.013  1.00 50.44           N  
ANISOU 2786  N   ASN A 412     5983   7058   6123    903   -819   -877       N  
ATOM   2787  CA  ASN A 412      36.688 -15.376 139.505  1.00 53.21           C  
ANISOU 2787  CA  ASN A 412     6431   7281   6506    948   -977   -792       C  
ATOM   2788  C   ASN A 412      37.771 -16.370 139.159  1.00 54.68           C  
ANISOU 2788  C   ASN A 412     6689   7451   6635   1120  -1078   -905       C  
ATOM   2789  O   ASN A 412      38.156 -17.183 139.984  1.00 55.52           O  
ANISOU 2789  O   ASN A 412     6820   7544   6733   1194  -1161   -880       O  
ATOM   2790  CB  ASN A 412      35.301 -15.870 139.107  1.00 52.94           C  
ANISOU 2790  CB  ASN A 412     6491   7061   6563    851  -1082   -654       C  
ATOM   2791  CG  ASN A 412      34.231 -15.313 140.032  1.00 54.99           C  
ANISOU 2791  CG  ASN A 412     6668   7349   6876    713  -1017   -499       C  
ATOM   2792  OD1 ASN A 412      33.328 -14.608 139.589  1.00 59.00           O  
ANISOU 2792  OD1 ASN A 412     7149   7839   7430    613   -963   -448       O  
ATOM   2793  ND2 ASN A 412      34.351 -15.591 141.333  1.00 55.08           N  
ANISOU 2793  ND2 ASN A 412     6632   7424   6870    720  -1016   -427       N  
ATOM   2794  N   GLN A 413      38.282 -16.270 137.946  1.00 55.71           N  
ANISOU 2794  N   GLN A 413     6849   7599   6719   1192  -1066  -1030       N  
ATOM   2795  CA  GLN A 413      39.406 -17.062 137.556  1.00 57.82           C  
ANISOU 2795  CA  GLN A 413     7162   7895   6913   1381  -1136  -1163       C  
ATOM   2796  C   GLN A 413      40.637 -16.711 138.415  1.00 57.82           C  
ANISOU 2796  C   GLN A 413     7022   8102   6843   1454  -1046  -1237       C  
ATOM   2797  O   GLN A 413      41.432 -17.594 138.753  1.00 58.69           O  
ANISOU 2797  O   GLN A 413     7162   8224   6916   1608  -1134  -1292       O  
ATOM   2798  CB  GLN A 413      39.672 -16.889 136.063  1.00 58.29           C  
ANISOU 2798  CB  GLN A 413     7261   7972   6916   1441  -1117  -1280       C  
ATOM   2799  CG  GLN A 413      41.121 -16.823 135.717  1.00 61.75           C  
ANISOU 2799  CG  GLN A 413     7621   8602   7239   1601  -1053  -1440       C  
ATOM   2800  CD  GLN A 413      41.362 -16.970 134.262  1.00 66.25           C  
ANISOU 2800  CD  GLN A 413     8256   9182   7734   1696  -1066  -1549       C  
ATOM   2801  OE1 GLN A 413      41.481 -18.076 133.778  1.00 73.07           O  
ANISOU 2801  OE1 GLN A 413     9256   9935   8574   1850  -1212  -1616       O  
ATOM   2802  NE2 GLN A 413      41.432 -15.859 133.542  1.00 66.53           N  
ANISOU 2802  NE2 GLN A 413     8203   9348   7728   1611   -921  -1569       N  
ATOM   2803  N   PHE A 414      40.785 -15.439 138.781  1.00 56.56           N  
ANISOU 2803  N   PHE A 414     6720   8099   6672   1346   -884  -1238       N  
ATOM   2804  CA  PHE A 414      41.972 -15.013 139.511  1.00 56.73           C  
ANISOU 2804  CA  PHE A 414     6602   8325   6628   1398   -804  -1316       C  
ATOM   2805  C   PHE A 414      41.856 -15.476 140.942  1.00 57.46           C  
ANISOU 2805  C   PHE A 414     6690   8402   6740   1401   -862  -1232       C  
ATOM   2806  O   PHE A 414      42.849 -15.665 141.621  1.00 58.87           O  
ANISOU 2806  O   PHE A 414     6799   8707   6864   1495   -866  -1289       O  
ATOM   2807  CB  PHE A 414      42.185 -13.502 139.415  1.00 55.44           C  
ANISOU 2807  CB  PHE A 414     6301   8312   6450   1273   -635  -1347       C  
ATOM   2808  CG  PHE A 414      43.215 -12.965 140.370  1.00 55.92           C  
ANISOU 2808  CG  PHE A 414     6218   8567   6464   1282   -566  -1404       C  
ATOM   2809  CD1 PHE A 414      44.584 -13.147 140.133  1.00 57.99           C  
ANISOU 2809  CD1 PHE A 414     6393   8996   6645   1407   -555  -1522       C  
ATOM   2810  CD2 PHE A 414      42.828 -12.284 141.513  1.00 54.74           C  
ANISOU 2810  CD2 PHE A 414     6012   8445   6342   1174   -517  -1344       C  
ATOM   2811  CE1 PHE A 414      45.542 -12.648 141.024  1.00 57.48           C  
ANISOU 2811  CE1 PHE A 414     6184   9115   6540   1405   -503  -1572       C  
ATOM   2812  CE2 PHE A 414      43.779 -11.776 142.408  1.00 55.94           C  
ANISOU 2812  CE2 PHE A 414     6036   8771   6446   1179   -469  -1405       C  
ATOM   2813  CZ  PHE A 414      45.137 -11.955 142.159  1.00 55.60           C  
ANISOU 2813  CZ  PHE A 414     5905   8887   6334   1286   -466  -1515       C  
ATOM   2814  N   ILE A 415      40.629 -15.680 141.393  1.00 57.60           N  
ANISOU 2814  N   ILE A 415     6777   8278   6830   1297   -908  -1086       N  
ATOM   2815  CA  ILE A 415      40.377 -16.157 142.750  1.00 57.77           C  
ANISOU 2815  CA  ILE A 415     6799   8288   6862   1288   -963   -976       C  
ATOM   2816  C   ILE A 415      40.604 -17.663 142.762  1.00 59.88           C  
ANISOU 2816  C   ILE A 415     7195   8421   7136   1422  -1145   -955       C  
ATOM   2817  O   ILE A 415      40.992 -18.227 143.776  1.00 60.68           O  
ANISOU 2817  O   ILE A 415     7292   8551   7212   1483  -1206   -913       O  
ATOM   2818  CB  ILE A 415      38.929 -15.779 143.243  1.00 56.12           C  
ANISOU 2818  CB  ILE A 415     6596   8005   6721   1122   -934   -812       C  
ATOM   2819  CG1 ILE A 415      38.906 -14.343 143.791  1.00 54.61           C  
ANISOU 2819  CG1 ILE A 415     6270   7974   6506   1028   -768   -838       C  
ATOM   2820  CG2 ILE A 415      38.393 -16.770 144.275  1.00 55.27           C  
ANISOU 2820  CG2 ILE A 415     6548   7818   6636   1117  -1048   -654       C  
ATOM   2821  CD1 ILE A 415      37.459 -13.726 143.938  1.00 49.78           C  
ANISOU 2821  CD1 ILE A 415     5650   7306   5957    882   -713   -711       C  
ATOM   2822  N   LYS A 416      40.368 -18.299 141.622  1.00 61.62           N  
ANISOU 2822  N   LYS A 416     7538   8489   7386   1471  -1240   -987       N  
ATOM   2823  CA  LYS A 416      40.409 -19.756 141.518  1.00 64.72           C  
ANISOU 2823  CA  LYS A 416     8087   8700   7802   1592  -1441   -965       C  
ATOM   2824  C   LYS A 416      41.871 -20.223 141.523  1.00 65.43           C  
ANISOU 2824  C   LYS A 416     8156   8897   7808   1809  -1474  -1117       C  
ATOM   2825  O   LYS A 416      42.196 -21.264 142.072  1.00 66.25           O  
ANISOU 2825  O   LYS A 416     8340   8920   7914   1923  -1617  -1090       O  
ATOM   2826  CB  LYS A 416      39.700 -20.196 140.243  1.00 65.67           C  
ANISOU 2826  CB  LYS A 416     8350   8628   7974   1579  -1536   -974       C  
ATOM   2827  CG  LYS A 416      38.698 -21.311 140.439  1.00 72.09           C  
ANISOU 2827  CG  LYS A 416     9322   9186   8882   1524  -1731   -818       C  
ATOM   2828  CD  LYS A 416      39.288 -22.691 140.068  1.00 83.43           C  
ANISOU 2828  CD  LYS A 416    10929  10458  10314   1719  -1940   -895       C  
ATOM   2829  CE  LYS A 416      38.325 -23.879 140.466  1.00 89.57           C  
ANISOU 2829  CE  LYS A 416    11873  10959  11200   1644  -2163   -711       C  
ATOM   2830  NZ  LYS A 416      37.040 -23.961 139.633  1.00 90.67           N  
ANISOU 2830  NZ  LYS A 416    12107  10913  11431   1490  -2239   -627       N  
ATOM   2831  N   GLY A 417      42.731 -19.412 140.916  1.00 65.30           N  
ANISOU 2831  N   GLY A 417     8022   9071   7719   1859  -1340  -1267       N  
ATOM   2832  CA  GLY A 417      44.168 -19.595 140.926  1.00 66.82           C  
ANISOU 2832  CA  GLY A 417     8135   9432   7820   2049  -1330  -1413       C  
ATOM   2833  C   GLY A 417      44.745 -19.395 142.313  1.00 67.49           C  
ANISOU 2833  C   GLY A 417     8105   9662   7877   2049  -1297  -1378       C  
ATOM   2834  O   GLY A 417      45.656 -20.112 142.718  1.00 69.57           O  
ANISOU 2834  O   GLY A 417     8364   9975   8096   2222  -1380  -1433       O  
ATOM   2835  N   LEU A 418      44.217 -18.437 143.060  1.00 66.32           N  
ANISOU 2835  N   LEU A 418     7866   9584   7750   1868  -1186  -1292       N  
ATOM   2836  CA  LEU A 418      44.650 -18.268 144.423  1.00 66.52           C  
ANISOU 2836  CA  LEU A 418     7798   9737   7739   1863  -1168  -1254       C  
ATOM   2837  C   LEU A 418      44.255 -19.477 145.272  1.00 68.27           C  
ANISOU 2837  C   LEU A 418     8143   9807   7990   1914  -1333  -1122       C  
ATOM   2838  O   LEU A 418      45.045 -19.969 146.056  1.00 69.51           O  
ANISOU 2838  O   LEU A 418     8274  10039   8098   2032  -1396  -1135       O  
ATOM   2839  CB  LEU A 418      44.091 -16.979 144.992  1.00 64.73           C  
ANISOU 2839  CB  LEU A 418     7467   9604   7522   1671  -1022  -1202       C  
ATOM   2840  CG  LEU A 418      44.890 -15.687 144.901  1.00 63.13           C  
ANISOU 2840  CG  LEU A 418     7096   9618   7271   1622   -870  -1321       C  
ATOM   2841  CD1 LEU A 418      45.822 -15.673 143.764  1.00 65.02           C  
ANISOU 2841  CD1 LEU A 418     7292   9939   7474   1722   -846  -1459       C  
ATOM   2842  CD2 LEU A 418      43.935 -14.540 144.795  1.00 61.79           C  
ANISOU 2842  CD2 LEU A 418     6903   9427   7147   1434   -755  -1271       C  
ATOM   2843  N   ASP A 419      43.047 -19.982 145.102  1.00 69.24           N  
ANISOU 2843  N   ASP A 419     8399   9716   8191   1824  -1412   -986       N  
ATOM   2844  CA  ASP A 419      42.652 -21.149 145.869  1.00 71.87           C  
ANISOU 2844  CA  ASP A 419     8854   9895   8558   1851  -1579   -837       C  
ATOM   2845  C   ASP A 419      43.534 -22.357 145.566  1.00 74.08           C  
ANISOU 2845  C   ASP A 419     9240  10085   8823   2076  -1748   -920       C  
ATOM   2846  O   ASP A 419      43.889 -23.083 146.479  1.00 75.93           O  
ANISOU 2846  O   ASP A 419     9507  10305   9040   2157  -1854   -853       O  
ATOM   2847  CB  ASP A 419      41.168 -21.455 145.690  1.00 71.38           C  
ANISOU 2847  CB  ASP A 419     8903   9626   8593   1691  -1639   -663       C  
ATOM   2848  CG  ASP A 419      40.282 -20.402 146.337  1.00 72.71           C  
ANISOU 2848  CG  ASP A 419     8961   9900   8767   1497  -1489   -554       C  
ATOM   2849  OD1 ASP A 419      40.827 -19.429 146.933  1.00 72.13           O  
ANISOU 2849  OD1 ASP A 419     8742  10043   8622   1488  -1347   -623       O  
ATOM   2850  OD2 ASP A 419      39.030 -20.542 146.255  1.00 76.51           O  
ANISOU 2850  OD2 ASP A 419     9497  10250   9322   1357  -1519   -401       O  
ATOM   2851  N   SER A 420      43.913 -22.528 144.301  1.00 74.80           N  
ANISOU 2851  N   SER A 420     9380  10131   8911   2187  -1769  -1068       N  
ATOM   2852  CA  SER A 420      44.770 -23.624 143.830  1.00 77.24           C  
ANISOU 2852  CA  SER A 420     9793  10361   9196   2434  -1924  -1183       C  
ATOM   2853  C   SER A 420      46.055 -23.886 144.630  1.00 79.07           C  
ANISOU 2853  C   SER A 420     9934  10760   9348   2614  -1946  -1252       C  
ATOM   2854  O   SER A 420      46.432 -25.043 144.850  1.00 81.01           O  
ANISOU 2854  O   SER A 420    10301  10879   9601   2787  -2128  -1249       O  
ATOM   2855  CB  SER A 420      45.174 -23.370 142.386  1.00 76.57           C  
ANISOU 2855  CB  SER A 420     9704  10316   9073   2529  -1871  -1366       C  
ATOM   2856  OG  SER A 420      44.171 -23.857 141.539  1.00 77.89           O  
ANISOU 2856  OG  SER A 420    10045  10235   9313   2473  -1974  -1323       O  
ATOM   2857  N   PHE A 421      46.747 -22.821 145.022  1.00 78.54           N  
ANISOU 2857  N   PHE A 421     9660  10972   9211   2580  -1773  -1320       N  
ATOM   2858  CA  PHE A 421      47.983 -22.986 145.755  1.00 80.01           C  
ANISOU 2858  CA  PHE A 421     9739  11342   9321   2741  -1790  -1390       C  
ATOM   2859  C   PHE A 421      47.894 -22.513 147.185  1.00 80.40           C  
ANISOU 2859  C   PHE A 421     9693  11508   9348   2620  -1742  -1273       C  
ATOM   2860  O   PHE A 421      48.904 -22.145 147.764  1.00 81.39           O  
ANISOU 2860  O   PHE A 421     9668  11858   9399   2691  -1693  -1348       O  
ATOM   2861  CB  PHE A 421      49.173 -22.343 145.029  1.00 79.63           C  
ANISOU 2861  CB  PHE A 421     9520  11546   9191   2853  -1669  -1589       C  
ATOM   2862  CG  PHE A 421      49.037 -20.863 144.744  1.00 76.00           C  
ANISOU 2862  CG  PHE A 421     8900  11259   8718   2656  -1458  -1619       C  
ATOM   2863  CD1 PHE A 421      49.043 -19.921 145.770  1.00 74.04           C  
ANISOU 2863  CD1 PHE A 421     8517  11162   8454   2501  -1354  -1565       C  
ATOM   2864  CD2 PHE A 421      49.002 -20.407 143.432  1.00 72.48           C  
ANISOU 2864  CD2 PHE A 421     8439  10835   8265   2641  -1370  -1713       C  
ATOM   2865  CE1 PHE A 421      48.965 -18.557 145.481  1.00 71.37           C  
ANISOU 2865  CE1 PHE A 421     8046  10961   8110   2329  -1179  -1601       C  
ATOM   2866  CE2 PHE A 421      48.928 -19.057 143.147  1.00 69.69           C  
ANISOU 2866  CE2 PHE A 421     7947  10630   7903   2463  -1189  -1732       C  
ATOM   2867  CZ  PHE A 421      48.902 -18.134 144.167  1.00 69.19           C  
ANISOU 2867  CZ  PHE A 421     7762  10687   7840   2306  -1099  -1677       C  
ATOM   2868  N   SER A 422      46.692 -22.553 147.753  1.00 80.61           N  
ANISOU 2868  N   SER A 422     9802  11394   9431   2445  -1761  -1091       N  
ATOM   2869  CA  SER A 422      46.441 -21.994 149.074  1.00 80.67           C  
ANISOU 2869  CA  SER A 422     9721  11527   9403   2318  -1694   -977       C  
ATOM   2870  C   SER A 422      47.078 -22.879 150.116  1.00 83.08           C  
ANISOU 2870  C   SER A 422    10053  11851   9661   2458  -1832   -920       C  
ATOM   2871  O   SER A 422      47.895 -22.412 150.952  1.00 83.31           O  
ANISOU 2871  O   SER A 422     9944  12105   9607   2495  -1781   -968       O  
ATOM   2872  CB  SER A 422      44.935 -21.850 149.337  1.00 79.89           C  
ANISOU 2872  CB  SER A 422     9695  11290   9368   2107  -1674   -789       C  
ATOM   2873  OG  SER A 422      44.691 -21.312 150.625  1.00 78.38           O  
ANISOU 2873  OG  SER A 422     9417  11240   9122   2004  -1603   -687       O  
ATOM   2874  N   GLY A 423      46.729 -24.163 150.063  1.00 84.91           N  
ANISOU 2874  N   GLY A 423    10470  11842   9949   2536  -2022   -817       N  
ATOM   2875  CA  GLY A 423      47.341 -25.124 151.002  1.00 88.26           C  
ANISOU 2875  CA  GLY A 423    10946  12253  10336   2686  -2181   -751       C  
ATOM   2876  C   GLY A 423      48.795 -25.531 150.748  1.00 89.59           C  
ANISOU 2876  C   GLY A 423    11066  12525  10449   2954  -2247   -933       C  
ATOM   2877  O   GLY A 423      49.389 -26.169 151.598  1.00 90.99           O  
ANISOU 2877  O   GLY A 423    11256  12731  10584   3082  -2364   -888       O  
ATOM   2878  N   LYS A 424      49.366 -25.116 149.609  1.00 90.02           N  
ANISOU 2878  N   LYS A 424    11048  12660  10495   3037  -2165  -1130       N  
ATOM   2879  CA  LYS A 424      50.492 -25.817 148.944  1.00 92.49           C  
ANISOU 2879  CA  LYS A 424    11373  12990  10778   3320  -2261  -1300       C  
ATOM   2880  C   LYS A 424      51.750 -24.993 148.591  1.00 92.92           C  
ANISOU 2880  C   LYS A 424    11193  13367  10745   3420  -2119  -1501       C  
ATOM   2881  O   LYS A 424      51.819 -24.428 147.488  1.00 91.93           O  
ANISOU 2881  O   LYS A 424    11010  13304  10617   3401  -2004  -1622       O  
ATOM   2882  CB  LYS A 424      50.010 -26.476 147.635  1.00 92.66           C  
ANISOU 2882  CB  LYS A 424    11574  12763  10868   3389  -2349  -1355       C  
ATOM   2883  CG  LYS A 424      48.666 -27.172 147.689  1.00 93.23           C  
ANISOU 2883  CG  LYS A 424    11869  12507  11045   3251  -2481  -1167       C  
ATOM   2884  CD  LYS A 424      48.337 -27.833 146.353  1.00 96.06           C  
ANISOU 2884  CD  LYS A 424    12405  12630  11462   3342  -2588  -1254       C  
ATOM   2885  CE  LYS A 424      46.839 -28.161 146.234  1.00 97.72           C  
ANISOU 2885  CE  LYS A 424    12791  12551  11785   3126  -2670  -1069       C  
ATOM   2886  NZ  LYS A 424      46.235 -28.621 147.533  1.00 98.29           N  
ANISOU 2886  NZ  LYS A 424    12924  12523  11899   2999  -2767   -821       N  
ATOM   2887  N   PRO A 425      52.776 -24.989 149.482  1.00 94.70           N  
ANISOU 2887  N   PRO A 425    11285  13799  10896   3533  -2138  -1532       N  
ATOM   2888  CA  PRO A 425      54.082 -24.387 149.144  1.00 95.67           C  
ANISOU 2888  CA  PRO A 425    11179  14232  10940   3651  -2036  -1716       C  
ATOM   2889  C   PRO A 425      54.747 -25.147 147.991  1.00 97.97           C  
ANISOU 2889  C   PRO A 425    11512  14494  11218   3921  -2107  -1872       C  
ATOM   2890  O   PRO A 425      54.529 -26.362 147.832  1.00 99.16           O  
ANISOU 2890  O   PRO A 425    11871  14397  11407   4088  -2294  -1846       O  
ATOM   2891  CB  PRO A 425      54.916 -24.578 150.416  1.00 96.90           C  
ANISOU 2891  CB  PRO A 425    11235  14551  11031   3746  -2109  -1688       C  
ATOM   2892  CG  PRO A 425      54.006 -25.215 151.438  1.00 97.07           C  
ANISOU 2892  CG  PRO A 425    11436  14355  11089   3665  -2234  -1480       C  
ATOM   2893  CD  PRO A 425      52.856 -25.818 150.700  1.00 96.01           C  
ANISOU 2893  CD  PRO A 425    11531  13898  11052   3608  -2300  -1400       C  
ATOM   2894  N   ARG A 426      55.535 -24.436 147.186  1.00 98.58           N  
ANISOU 2894  N   ARG A 426    11399  14820  11238   3963  -1965  -2029       N  
ATOM   2895  CA  ARG A 426      56.136 -25.023 145.973  1.00100.67           C  
ANISOU 2895  CA  ARG A 426    11683  15100  11467   4217  -1999  -2190       C  
ATOM   2896  C   ARG A 426      57.481 -25.745 146.238  1.00103.18           C  
ANISOU 2896  C   ARG A 426    11904  15586  11712   4541  -2102  -2298       C  
ATOM   2897  O   ARG A 426      58.194 -25.444 147.209  1.00103.48           O  
ANISOU 2897  O   ARG A 426    11775  15833  11710   4541  -2092  -2279       O  
ATOM   2898  CB  ARG A 426      56.295 -23.957 144.879  1.00 99.68           C  
ANISOU 2898  CB  ARG A 426    11401  15170  11304   4112  -1792  -2292       C  
ATOM   2899  CG  ARG A 426      56.945 -22.677 145.385  1.00 99.56           C  
ANISOU 2899  CG  ARG A 426    11104  15480  11245   3945  -1623  -2301       C  
ATOM   2900  CD  ARG A 426      57.421 -21.780 144.262  1.00100.48           C  
ANISOU 2900  CD  ARG A 426    11041  15829  11309   3898  -1443  -2410       C  
ATOM   2901  NE  ARG A 426      58.273 -20.722 144.801  1.00100.49           N  
ANISOU 2901  NE  ARG A 426    10765  16149  11269   3776  -1323  -2427       N  
ATOM   2902  CZ  ARG A 426      59.552 -20.531 144.488  1.00101.56           C  
ANISOU 2902  CZ  ARG A 426    10661  16607  11321   3911  -1266  -2538       C  
ATOM   2903  NH1 ARG A 426      60.160 -21.314 143.604  1.00102.76           N  
ANISOU 2903  NH1 ARG A 426    10810  16827  11409   4196  -1302  -2654       N  
ATOM   2904  NH2 ARG A 426      60.216 -19.529 145.051  1.00100.84           N  
ANISOU 2904  NH2 ARG A 426    10329  16777  11209   3756  -1173  -2534       N  
ATOM   2905  N   LEU A 436      48.015 -17.554 136.764  1.00 65.66           N  
ANISOU 2905  N   LEU A 436     7546  10116   7286   2398   -891  -2004       N  
ATOM   2906  CA  LEU A 436      47.423 -16.329 137.327  1.00 63.87           C  
ANISOU 2906  CA  LEU A 436     7235   9905   7126   2136   -775  -1896       C  
ATOM   2907  C   LEU A 436      47.375 -15.207 136.288  1.00 63.26           C  
ANISOU 2907  C   LEU A 436     7081   9938   7017   2010   -627  -1909       C  
ATOM   2908  O   LEU A 436      48.383 -14.886 135.651  1.00 65.00           O  
ANISOU 2908  O   LEU A 436     7173  10384   7142   2081   -540  -1998       O  
ATOM   2909  CB  LEU A 436      48.139 -15.821 138.569  1.00 62.37           C  
ANISOU 2909  CB  LEU A 436     6882   9880   6934   2091   -720  -1885       C  
ATOM   2910  CG  LEU A 436      48.037 -16.460 139.950  1.00 62.71           C  
ANISOU 2910  CG  LEU A 436     6965   9844   7019   2124   -826  -1823       C  
ATOM   2911  CD1 LEU A 436      48.341 -15.383 140.981  1.00 60.77           C  
ANISOU 2911  CD1 LEU A 436     6558   9752   6779   1975   -724  -1793       C  
ATOM   2912  CD2 LEU A 436      46.709 -17.113 140.268  1.00 62.48           C  
ANISOU 2912  CD2 LEU A 436     7126   9534   7080   2066   -941  -1699       C  
ATOM   2913  N   PRO A 437      46.189 -14.625 136.094  1.00 60.91           N  
ANISOU 2913  N   PRO A 437     6858   9488   6796   1826   -601  -1811       N  
ATOM   2914  CA  PRO A 437      46.094 -13.654 135.017  1.00 59.98           C  
ANISOU 2914  CA  PRO A 437     6693   9450   6647   1720   -482  -1815       C  
ATOM   2915  C   PRO A 437      46.519 -12.285 135.516  1.00 59.18           C  
ANISOU 2915  C   PRO A 437     6415   9513   6558   1548   -339  -1787       C  
ATOM   2916  O   PRO A 437      45.727 -11.334 135.513  1.00 57.96           O  
ANISOU 2916  O   PRO A 437     6268   9284   6470   1361   -278  -1706       O  
ATOM   2917  CB  PRO A 437      44.619 -13.702 134.640  1.00 59.28           C  
ANISOU 2917  CB  PRO A 437     6768   9115   6641   1613   -539  -1721       C  
ATOM   2918  CG  PRO A 437      44.076 -14.933 135.345  1.00 59.97           C  
ANISOU 2918  CG  PRO A 437     6995   9002   6789   1697   -705  -1684       C  
ATOM   2919  CD  PRO A 437      44.884 -15.112 136.547  1.00 59.11           C  
ANISOU 2919  CD  PRO A 437     6789   8999   6671   1755   -708  -1701       C  
ATOM   2920  N   ILE A 438      47.775 -12.196 135.943  1.00 59.42           N  
ANISOU 2920  N   ILE A 438     6287   9763   6527   1616   -298  -1856       N  
ATOM   2921  CA  ILE A 438      48.322 -10.961 136.480  1.00 58.79           C  
ANISOU 2921  CA  ILE A 438     6034   9843   6459   1456   -186  -1841       C  
ATOM   2922  C   ILE A 438      48.157  -9.782 135.519  1.00 57.97           C  
ANISOU 2922  C   ILE A 438     5885   9790   6352   1289    -68  -1804       C  
ATOM   2923  O   ILE A 438      47.617  -8.754 135.884  1.00 56.74           O  
ANISOU 2923  O   ILE A 438     5719   9569   6271   1100    -20  -1737       O  
ATOM   2924  CB  ILE A 438      49.802 -11.143 136.909  1.00 60.02           C  
ANISOU 2924  CB  ILE A 438     6014  10254   6538   1568   -171  -1927       C  
ATOM   2925  CG1 ILE A 438      49.859 -11.610 138.353  1.00 61.85           C  
ANISOU 2925  CG1 ILE A 438     6250  10440   6809   1611   -257  -1920       C  
ATOM   2926  CG2 ILE A 438      50.571  -9.846 136.824  1.00 60.18           C  
ANISOU 2926  CG2 ILE A 438     5839  10485   6540   1406    -45  -1925       C  
ATOM   2927  CD1 ILE A 438      49.331 -12.994 138.526  1.00 65.35           C  
ANISOU 2927  CD1 ILE A 438     6866  10698   7265   1781   -398  -1915       C  
ATOM   2928  N   GLU A 439      48.625  -9.933 134.289  1.00 58.87           N  
ANISOU 2928  N   GLU A 439     5975  10022   6371   1369    -27  -1847       N  
ATOM   2929  CA  GLU A 439      48.568  -8.828 133.332  1.00 59.17           C  
ANISOU 2929  CA  GLU A 439     5961  10132   6391   1213     85  -1798       C  
ATOM   2930  C   GLU A 439      47.161  -8.216 133.183  1.00 55.86           C  
ANISOU 2930  C   GLU A 439     5680   9473   6071   1049     80  -1700       C  
ATOM   2931  O   GLU A 439      47.017  -6.991 133.169  1.00 54.97           O  
ANISOU 2931  O   GLU A 439     5511   9368   6006    857    158  -1636       O  
ATOM   2932  CB  GLU A 439      49.004  -9.333 131.984  1.00 61.20           C  
ANISOU 2932  CB  GLU A 439     6220  10515   6516   1356    109  -1853       C  
ATOM   2933  CG  GLU A 439      49.865  -8.394 131.216  1.00 68.09           C  
ANISOU 2933  CG  GLU A 439     6921  11644   7306   1263    245  -1835       C  
ATOM   2934  CD  GLU A 439      50.604  -9.152 130.108  1.00 76.95           C  
ANISOU 2934  CD  GLU A 439     8009  12967   8262   1477    266  -1921       C  
ATOM   2935  OE1 GLU A 439      51.840  -9.379 130.254  1.00 78.65           O  
ANISOU 2935  OE1 GLU A 439     8049  13443   8393   1589    305  -1988       O  
ATOM   2936  OE2 GLU A 439      49.921  -9.551 129.124  1.00 78.60           O  
ANISOU 2936  OE2 GLU A 439     8369  13072   8424   1546    236  -1927       O  
ATOM   2937  N   ALA A 440      46.162  -9.094 133.077  1.00 53.25           N  
ANISOU 2937  N   ALA A 440     5525   8932   5775   1131    -22  -1687       N  
ATOM   2938  CA  ALA A 440      44.804  -8.737 132.776  1.00 51.24           C  
ANISOU 2938  CA  ALA A 440     5402   8465   5602   1015    -42  -1598       C  
ATOM   2939  C   ALA A 440      44.152  -8.135 134.009  1.00 49.87           C  
ANISOU 2939  C   ALA A 440     5223   8177   5546    880    -44  -1531       C  
ATOM   2940  O   ALA A 440      43.595  -7.051 133.939  1.00 48.78           O  
ANISOU 2940  O   ALA A 440     5080   7985   5467    721     14  -1466       O  
ATOM   2941  CB  ALA A 440      44.023  -9.965 132.293  1.00 51.03           C  
ANISOU 2941  CB  ALA A 440     5552   8264   5573   1146   -168  -1607       C  
ATOM   2942  N   VAL A 441      44.264  -8.831 135.138  1.00 49.13           N  
ANISOU 2942  N   VAL A 441     5132   8058   5477    957   -112  -1551       N  
ATOM   2943  CA  VAL A 441      43.809  -8.309 136.403  1.00 47.91           C  
ANISOU 2943  CA  VAL A 441     4956   7843   5403    856   -108  -1502       C  
ATOM   2944  C   VAL A 441      44.308  -6.864 136.590  1.00 48.44           C  
ANISOU 2944  C   VAL A 441     4899   8022   5484    701     -1  -1507       C  
ATOM   2945  O   VAL A 441      43.539  -5.969 136.960  1.00 49.09           O  
ANISOU 2945  O   VAL A 441     5003   8007   5642    571     27  -1451       O  
ATOM   2946  CB  VAL A 441      44.213  -9.235 137.576  1.00 47.88           C  
ANISOU 2946  CB  VAL A 441     4941   7861   5389    972   -185  -1532       C  
ATOM   2947  CG1 VAL A 441      44.220  -8.481 138.910  1.00 48.09           C  
ANISOU 2947  CG1 VAL A 441     4893   7921   5456    875   -153  -1515       C  
ATOM   2948  CG2 VAL A 441      43.285 -10.428 137.653  1.00 44.73           C  
ANISOU 2948  CG2 VAL A 441     4695   7276   5025   1056   -305  -1479       C  
ATOM   2949  N   ILE A 442      45.574  -6.607 136.312  1.00 49.30           N  
ANISOU 2949  N   ILE A 442     4877   8334   5523    713     53  -1569       N  
ATOM   2950  CA  ILE A 442      46.103  -5.260 136.531  1.00 48.63           C  
ANISOU 2950  CA  ILE A 442     4673   8346   5459    549    133  -1566       C  
ATOM   2951  C   ILE A 442      45.404  -4.268 135.601  1.00 48.05           C  
ANISOU 2951  C   ILE A 442     4650   8179   5427    404    189  -1494       C  
ATOM   2952  O   ILE A 442      44.892  -3.233 136.051  1.00 47.67           O  
ANISOU 2952  O   ILE A 442     4615   8038   5459    264    209  -1455       O  
ATOM   2953  CB  ILE A 442      47.674  -5.175 136.404  1.00 49.74           C  
ANISOU 2953  CB  ILE A 442     4633   8750   5516    573    178  -1633       C  
ATOM   2954  CG1 ILE A 442      48.333  -5.945 137.551  1.00 49.89           C  
ANISOU 2954  CG1 ILE A 442     4592   8853   5510    696    116  -1700       C  
ATOM   2955  CG2 ILE A 442      48.162  -3.688 136.331  1.00 47.08           C  
ANISOU 2955  CG2 ILE A 442     4182   8496   5210    363    255  -1606       C  
ATOM   2956  CD1 ILE A 442      49.855  -6.071 137.391  1.00 53.51           C  
ANISOU 2956  CD1 ILE A 442     4866   9585   5880    758    147  -1767       C  
ATOM   2957  N   LEU A 443      45.381  -4.586 134.318  1.00 47.50           N  
ANISOU 2957  N   LEU A 443     4616   8134   5297    450    207  -1479       N  
ATOM   2958  CA  LEU A 443      44.767  -3.694 133.353  1.00 47.76           C  
ANISOU 2958  CA  LEU A 443     4699   8092   5355    322    254  -1402       C  
ATOM   2959  C   LEU A 443      43.257  -3.512 133.666  1.00 46.63           C  
ANISOU 2959  C   LEU A 443     4695   7703   5317    276    207  -1337       C  
ATOM   2960  O   LEU A 443      42.710  -2.406 133.560  1.00 46.64           O  
ANISOU 2960  O   LEU A 443     4718   7617   5388    136    240  -1276       O  
ATOM   2961  CB  LEU A 443      44.965  -4.202 131.916  1.00 47.72           C  
ANISOU 2961  CB  LEU A 443     4719   8167   5245    405    273  -1402       C  
ATOM   2962  CG  LEU A 443      44.483  -3.225 130.824  1.00 48.14           C  
ANISOU 2962  CG  LEU A 443     4810   8179   5303    267    327  -1312       C  
ATOM   2963  CD1 LEU A 443      45.191  -1.860 130.914  1.00 46.87           C  
ANISOU 2963  CD1 LEU A 443     4522   8120   5166     79    409  -1269       C  
ATOM   2964  CD2 LEU A 443      44.645  -3.804 129.434  1.00 45.75           C  
ANISOU 2964  CD2 LEU A 443     4540   7968   4874    367    340  -1319       C  
ATOM   2965  N   SER A 444      42.613  -4.587 134.089  1.00 45.38           N  
ANISOU 2965  N   SER A 444     4624   7442   5174    393    127  -1344       N  
ATOM   2966  CA  SER A 444      41.216  -4.527 134.416  1.00 44.94           C  
ANISOU 2966  CA  SER A 444     4675   7189   5211    357     83  -1274       C  
ATOM   2967  C   SER A 444      40.995  -3.535 135.559  1.00 44.45           C  
ANISOU 2967  C   SER A 444     4570   7094   5225    255    113  -1263       C  
ATOM   2968  O   SER A 444      40.251  -2.567 135.412  1.00 43.16           O  
ANISOU 2968  O   SER A 444     4440   6831   5128    152    139  -1210       O  
ATOM   2969  CB  SER A 444      40.691  -5.919 134.723  1.00 43.99           C  
ANISOU 2969  CB  SER A 444     4641   6983   5091    487    -16  -1273       C  
ATOM   2970  OG  SER A 444      39.552  -5.829 135.507  1.00 44.40           O  
ANISOU 2970  OG  SER A 444     4742   6896   5230    445    -48  -1204       O  
ATOM   2971  N   LEU A 445      41.706  -3.756 136.665  1.00 45.26           N  
ANISOU 2971  N   LEU A 445     4600   7289   5310    294    105  -1323       N  
ATOM   2972  CA  LEU A 445      41.728  -2.815 137.786  1.00 44.67           C  
ANISOU 2972  CA  LEU A 445     4477   7214   5283    211    129  -1342       C  
ATOM   2973  C   LEU A 445      41.985  -1.401 137.340  1.00 44.82           C  
ANISOU 2973  C   LEU A 445     4459   7236   5335     62    188  -1336       C  
ATOM   2974  O   LEU A 445      41.262  -0.499 137.735  1.00 46.07           O  
ANISOU 2974  O   LEU A 445     4657   7283   5565    -14    195  -1313       O  
ATOM   2975  CB  LEU A 445      42.773  -3.221 138.794  1.00 45.02           C  
ANISOU 2975  CB  LEU A 445     4429   7400   5277    270    111  -1419       C  
ATOM   2976  CG  LEU A 445      42.378  -4.119 139.963  1.00 45.79           C  
ANISOU 2976  CG  LEU A 445     4558   7470   5370    372     50  -1417       C  
ATOM   2977  CD1 LEU A 445      40.982  -4.582 139.930  1.00 43.60           C  
ANISOU 2977  CD1 LEU A 445     4391   7034   5140    396     15  -1330       C  
ATOM   2978  CD2 LEU A 445      43.316  -5.281 140.191  1.00 44.46           C  
ANISOU 2978  CD2 LEU A 445     4346   7419   5128    504      2  -1465       C  
ATOM   2979  N   GLN A 446      42.973  -1.191 136.489  1.00 45.41           N  
ANISOU 2979  N   GLN A 446     4461   7435   5358     21    228  -1349       N  
ATOM   2980  CA  GLN A 446      43.327   0.181 136.117  1.00 46.71           C  
ANISOU 2980  CA  GLN A 446     4583   7607   5558   -144    275  -1328       C  
ATOM   2981  C   GLN A 446      42.197   0.809 135.347  1.00 46.05           C  
ANISOU 2981  C   GLN A 446     4609   7354   5536   -209    282  -1243       C  
ATOM   2982  O   GLN A 446      41.950   2.000 135.491  1.00 45.81           O  
ANISOU 2982  O   GLN A 446     4596   7233   5577   -330    291  -1220       O  
ATOM   2983  CB  GLN A 446      44.606   0.261 135.255  1.00 47.41           C  
ANISOU 2983  CB  GLN A 446     4555   7890   5568   -186    324  -1332       C  
ATOM   2984  CG  GLN A 446      45.864   0.018 135.986  1.00 48.56           C  
ANISOU 2984  CG  GLN A 446     4561   8223   5666   -163    323  -1410       C  
ATOM   2985  CD  GLN A 446      47.118  -0.074 135.059  1.00 54.24           C  
ANISOU 2985  CD  GLN A 446     5142   9177   6292   -176    379  -1407       C  
ATOM   2986  OE1 GLN A 446      47.042  -0.282 133.800  1.00 52.03           O  
ANISOU 2986  OE1 GLN A 446     4883   8935   5951   -154    420  -1358       O  
ATOM   2987  NE2 GLN A 446      48.279   0.088 135.691  1.00 51.15           N  
ANISOU 2987  NE2 GLN A 446     4599   8958   5877   -210    381  -1460       N  
ATOM   2988  N   ASP A 447      41.581  -0.001 134.477  1.00 45.97           N  
ANISOU 2988  N   ASP A 447     4671   7302   5493   -126    269  -1199       N  
ATOM   2989  CA  ASP A 447      40.466   0.409 133.618  1.00 45.29           C  
ANISOU 2989  CA  ASP A 447     4688   7067   5452   -168    264  -1113       C  
ATOM   2990  C   ASP A 447      39.258   0.780 134.468  1.00 44.00           C  
ANISOU 2990  C   ASP A 447     4594   6737   5388   -170    232  -1091       C  
ATOM   2991  O   ASP A 447      38.696   1.861 134.303  1.00 44.37           O  
ANISOU 2991  O   ASP A 447     4681   6673   5504   -259    241  -1047       O  
ATOM   2992  CB  ASP A 447      40.116  -0.706 132.636  1.00 45.35           C  
ANISOU 2992  CB  ASP A 447     4759   7077   5395    -61    235  -1090       C  
ATOM   2993  CG  ASP A 447      41.017  -0.695 131.350  1.00 49.43           C  
ANISOU 2993  CG  ASP A 447     5231   7742   5807    -76    283  -1082       C  
ATOM   2994  OD1 ASP A 447      41.568   0.378 131.021  1.00 49.96           O  
ANISOU 2994  OD1 ASP A 447     5240   7866   5876   -207    340  -1048       O  
ATOM   2995  OD2 ASP A 447      41.147  -1.755 130.647  1.00 51.59           O  
ANISOU 2995  OD2 ASP A 447     5535   8076   5992     44    260  -1107       O  
ATOM   2996  N   LEU A 448      38.887  -0.080 135.416  1.00 42.11           N  
ANISOU 2996  N   LEU A 448     4362   6487   5151    -69    193  -1120       N  
ATOM   2997  CA  LEU A 448      37.738   0.220 136.270  1.00 40.54           C  
ANISOU 2997  CA  LEU A 448     4208   6167   5028    -59    173  -1094       C  
ATOM   2998  C   LEU A 448      38.011   1.457 137.115  1.00 41.18           C  
ANISOU 2998  C   LEU A 448     4257   6237   5153   -134    198  -1145       C  
ATOM   2999  O   LEU A 448      37.124   2.322 137.264  1.00 41.02           O  
ANISOU 2999  O   LEU A 448     4285   6096   5203   -166    199  -1117       O  
ATOM   3000  CB  LEU A 448      37.314  -0.975 137.115  1.00 38.98           C  
ANISOU 3000  CB  LEU A 448     4017   5979   4814     53    129  -1094       C  
ATOM   3001  CG  LEU A 448      36.784  -2.176 136.311  1.00 37.69           C  
ANISOU 3001  CG  LEU A 448     3915   5773   4631    121     75  -1037       C  
ATOM   3002  CD1 LEU A 448      36.338  -3.327 137.219  1.00 37.76           C  
ANISOU 3002  CD1 LEU A 448     3936   5774   4637    209     17  -1016       C  
ATOM   3003  CD2 LEU A 448      35.638  -1.786 135.412  1.00 37.11           C  
ANISOU 3003  CD2 LEU A 448     3912   5574   4613     79     63   -951       C  
ATOM   3004  N   ILE A 449      39.241   1.592 137.633  1.00 41.00           N  
ANISOU 3004  N   ILE A 449     4152   6336   5090   -162    211  -1223       N  
ATOM   3005  CA  ILE A 449      39.528   2.800 138.415  1.00 40.36           C  
ANISOU 3005  CA  ILE A 449     4053   6230   5054   -244    214  -1281       C  
ATOM   3006  C   ILE A 449      39.263   4.065 137.570  1.00 41.27           C  
ANISOU 3006  C   ILE A 449     4218   6226   5238   -367    226  -1231       C  
ATOM   3007  O   ILE A 449      38.638   5.009 138.056  1.00 41.91           O  
ANISOU 3007  O   ILE A 449     4353   6184   5388   -392    210  -1246       O  
ATOM   3008  CB  ILE A 449      40.928   2.759 139.056  1.00 40.89           C  
ANISOU 3008  CB  ILE A 449     4016   6452   5068   -270    212  -1368       C  
ATOM   3009  CG1 ILE A 449      40.985   1.610 140.063  1.00 39.47           C  
ANISOU 3009  CG1 ILE A 449     3808   6359   4831   -137    188  -1410       C  
ATOM   3010  CG2 ILE A 449      41.278   4.074 139.699  1.00 38.89           C  
ANISOU 3010  CG2 ILE A 449     3754   6156   4867   -378    197  -1429       C  
ATOM   3011  CD1 ILE A 449      42.396   1.047 140.321  1.00 35.88           C  
ANISOU 3011  CD1 ILE A 449     3243   6089   4302   -117    181  -1474       C  
ATOM   3012  N   GLY A 450      39.671   4.073 136.299  1.00 40.88           N  
ANISOU 3012  N   GLY A 450     4159   6209   5164   -431    249  -1169       N  
ATOM   3013  CA  GLY A 450      39.405   5.215 135.434  1.00 41.76           C  
ANISOU 3013  CA  GLY A 450     4325   6209   5335   -551    255  -1098       C  
ATOM   3014  C   GLY A 450      37.906   5.371 135.163  1.00 42.68           C  
ANISOU 3014  C   GLY A 450     4548   6157   5513   -498    235  -1034       C  
ATOM   3015  O   GLY A 450      37.406   6.487 135.087  1.00 44.73           O  
ANISOU 3015  O   GLY A 450     4869   6276   5851   -561    218  -1008       O  
ATOM   3016  N   TYR A 451      37.180   4.261 135.000  1.00 41.19           N  
ANISOU 3016  N   TYR A 451     4380   5978   5293   -383    227  -1005       N  
ATOM   3017  CA  TYR A 451      35.768   4.300 134.685  1.00 40.94           C  
ANISOU 3017  CA  TYR A 451     4428   5813   5317   -336    204   -933       C  
ATOM   3018  C   TYR A 451      34.952   4.900 135.863  1.00 42.69           C  
ANISOU 3018  C   TYR A 451     4669   5944   5608   -291    190   -971       C  
ATOM   3019  O   TYR A 451      33.906   5.536 135.647  1.00 42.01           O  
ANISOU 3019  O   TYR A 451     4642   5731   5590   -281    175   -921       O  
ATOM   3020  CB  TYR A 451      35.357   2.866 134.441  1.00 39.14           C  
ANISOU 3020  CB  TYR A 451     4202   5632   5037   -236    183   -905       C  
ATOM   3021  CG  TYR A 451      33.923   2.573 134.081  1.00 37.37           C  
ANISOU 3021  CG  TYR A 451     4039   5302   4859   -185    146   -822       C  
ATOM   3022  CD1 TYR A 451      33.409   2.898 132.839  1.00 34.02           C  
ANISOU 3022  CD1 TYR A 451     3674   4804   4450   -225    132   -740       C  
ATOM   3023  CD2 TYR A 451      33.085   1.901 134.988  1.00 36.22           C  
ANISOU 3023  CD2 TYR A 451     3882   5145   4734    -99    122   -814       C  
ATOM   3024  CE1 TYR A 451      32.096   2.576 132.508  1.00 36.58           C  
ANISOU 3024  CE1 TYR A 451     4042   5041   4815   -180     86   -662       C  
ATOM   3025  CE2 TYR A 451      31.782   1.541 134.656  1.00 34.82           C  
ANISOU 3025  CE2 TYR A 451     3740   4891   4599    -62     83   -726       C  
ATOM   3026  CZ  TYR A 451      31.282   1.892 133.429  1.00 37.59           C  
ANISOU 3026  CZ  TYR A 451     4147   5165   4972   -102     61   -654       C  
ATOM   3027  OH  TYR A 451      29.976   1.527 133.105  1.00 37.28           O  
ANISOU 3027  OH  TYR A 451     4131   5055   4977    -69     11   -564       O  
ATOM   3028  N   PHE A 452      35.436   4.662 137.093  1.00 43.59           N  
ANISOU 3028  N   PHE A 452     4731   6137   5694   -249    194  -1061       N  
ATOM   3029  CA  PHE A 452      34.780   5.126 138.305  1.00 45.40           C  
ANISOU 3029  CA  PHE A 452     4971   6323   5958   -186    187  -1114       C  
ATOM   3030  C   PHE A 452      35.328   6.450 138.825  1.00 48.04           C  
ANISOU 3030  C   PHE A 452     5321   6600   6332   -256    176  -1200       C  
ATOM   3031  O   PHE A 452      34.897   6.929 139.853  1.00 49.22           O  
ANISOU 3031  O   PHE A 452     5487   6717   6497   -194    165  -1268       O  
ATOM   3032  CB  PHE A 452      34.751   4.031 139.388  1.00 43.48           C  
ANISOU 3032  CB  PHE A 452     4674   6195   5653    -83    189  -1147       C  
ATOM   3033  CG  PHE A 452      33.837   2.863 139.039  1.00 42.73           C  
ANISOU 3033  CG  PHE A 452     4583   6104   5546    -12    178  -1049       C  
ATOM   3034  CD1 PHE A 452      32.492   3.069 138.775  1.00 42.44           C  
ANISOU 3034  CD1 PHE A 452     4582   5976   5567     21    171   -969       C  
ATOM   3035  CD2 PHE A 452      34.323   1.565 138.939  1.00 40.72           C  
ANISOU 3035  CD2 PHE A 452     4301   5941   5231     21    162  -1034       C  
ATOM   3036  CE1 PHE A 452      31.637   1.986 138.427  1.00 39.67           C  
ANISOU 3036  CE1 PHE A 452     4231   5626   5216     66    145   -869       C  
ATOM   3037  CE2 PHE A 452      33.483   0.513 138.623  1.00 39.58           C  
ANISOU 3037  CE2 PHE A 452     4175   5776   5088     72    130   -944       C  
ATOM   3038  CZ  PHE A 452      32.128   0.733 138.367  1.00 39.01           C  
ANISOU 3038  CZ  PHE A 452     4131   5613   5077     84    120   -858       C  
ATOM   3039  N   GLU A 453      36.210   7.086 138.075  1.00 50.56           N  
ANISOU 3039  N   GLU A 453     5643   6901   6667   -387    172  -1191       N  
ATOM   3040  CA  GLU A 453      36.803   8.348 138.517  1.00 53.82           C  
ANISOU 3040  CA  GLU A 453     6078   7243   7129   -481    140  -1265       C  
ATOM   3041  C   GLU A 453      35.758   9.449 138.669  1.00 54.02           C  
ANISOU 3041  C   GLU A 453     6204   7078   7243   -452    106  -1269       C  
ATOM   3042  O   GLU A 453      34.906   9.605 137.803  1.00 53.96           O  
ANISOU 3042  O   GLU A 453     6250   6975   7278   -441    107  -1174       O  
ATOM   3043  CB  GLU A 453      37.894   8.754 137.525  1.00 55.34           C  
ANISOU 3043  CB  GLU A 453     6241   7462   7323   -647    143  -1216       C  
ATOM   3044  CG  GLU A 453      38.378  10.185 137.631  1.00 63.66           C  
ANISOU 3044  CG  GLU A 453     7339   8395   8454   -787     92  -1246       C  
ATOM   3045  CD  GLU A 453      39.876  10.345 137.306  1.00 71.18           C  
ANISOU 3045  CD  GLU A 453     8199   9467   9379   -951     94  -1239       C  
ATOM   3046  OE1 GLU A 453      40.406   9.549 136.487  1.00 71.89           O  
ANISOU 3046  OE1 GLU A 453     8211   9709   9396   -969    148  -1171       O  
ATOM   3047  OE2 GLU A 453      40.508  11.270 137.887  1.00 74.67           O  
ANISOU 3047  OE2 GLU A 453     8645   9855   9870  -1058     37  -1305       O  
ATOM   3048  N   PRO A 454      35.792  10.198 139.786  1.00 55.11           N  
ANISOU 3048  N   PRO A 454     6372   7164   7404   -423     68  -1388       N  
ATOM   3049  CA  PRO A 454      34.884  11.375 139.916  1.00 56.79           C  
ANISOU 3049  CA  PRO A 454     6692   7181   7703   -383     24  -1411       C  
ATOM   3050  C   PRO A 454      35.243  12.475 138.912  1.00 59.19           C  
ANISOU 3050  C   PRO A 454     7070   7324   8095   -542    -24  -1349       C  
ATOM   3051  O   PRO A 454      36.384  12.544 138.482  1.00 59.78           O  
ANISOU 3051  O   PRO A 454     7103   7451   8160   -697    -29  -1326       O  
ATOM   3052  CB  PRO A 454      35.138  11.878 141.335  1.00 57.02           C  
ANISOU 3052  CB  PRO A 454     6737   7211   7716   -326    -15  -1574       C  
ATOM   3053  CG  PRO A 454      35.975  10.860 142.016  1.00 55.00           C  
ANISOU 3053  CG  PRO A 454     6376   7162   7361   -317     15  -1622       C  
ATOM   3054  CD  PRO A 454      36.577   9.946 141.008  1.00 54.70           C  
ANISOU 3054  CD  PRO A 454     6261   7231   7289   -400     59  -1512       C  
ATOM   3055  N   PRO A 455      34.281  13.326 138.533  1.00 61.36           N  
ANISOU 3055  N   PRO A 455     7447   7413   8453   -504    -61  -1312       N  
ATOM   3056  CA  PRO A 455      34.463  14.400 137.499  1.00 63.27           C  
ANISOU 3056  CA  PRO A 455     7777   7476   8785   -652   -116  -1225       C  
ATOM   3057  C   PRO A 455      35.583  15.421 137.762  1.00 65.34           C  
ANISOU 3057  C   PRO A 455     8077   7649   9099   -821   -191  -1286       C  
ATOM   3058  O   PRO A 455      35.682  15.939 138.870  1.00 66.30           O  
ANISOU 3058  O   PRO A 455     8237   7714   9238   -773   -246  -1432       O  
ATOM   3059  CB  PRO A 455      33.113  15.138 137.498  1.00 64.07           C  
ANISOU 3059  CB  PRO A 455     7987   7391   8965   -521   -157  -1221       C  
ATOM   3060  CG  PRO A 455      32.323  14.577 138.700  1.00 63.66           C  
ANISOU 3060  CG  PRO A 455     7894   7434   8860   -309   -122  -1329       C  
ATOM   3061  CD  PRO A 455      32.874  13.198 138.955  1.00 61.51           C  
ANISOU 3061  CD  PRO A 455     7492   7399   8479   -310    -47  -1324       C  
ATOM   3062  N   GLN A 465      27.885  19.098 134.501  1.00 87.55           N  
ANISOU 3062  N   GLN A 465    11471   9416  12377   -163   -440   -872       N  
ATOM   3063  CA  GLN A 465      28.538  18.288 135.535  1.00 86.95           C  
ANISOU 3063  CA  GLN A 465    11290   9537  12212   -155   -369   -995       C  
ATOM   3064  C   GLN A 465      27.566  17.422 136.378  1.00 85.50           C  
ANISOU 3064  C   GLN A 465    11000   9524  11961     64   -295  -1059       C  
ATOM   3065  O   GLN A 465      27.617  17.398 137.625  1.00 85.07           O  
ANISOU 3065  O   GLN A 465    10921   9533  11870    172   -280  -1212       O  
ATOM   3066  CB  GLN A 465      29.417  19.183 136.419  1.00 89.03           C  
ANISOU 3066  CB  GLN A 465    11633   9683  12513   -216   -440  -1146       C  
ATOM   3067  CG  GLN A 465      30.491  18.446 137.242  1.00 89.41           C  
ANISOU 3067  CG  GLN A 465    11578   9924  12469   -286   -385  -1244       C  
ATOM   3068  CD  GLN A 465      30.306  18.643 138.743  1.00 91.96           C  
ANISOU 3068  CD  GLN A 465    11911  10265  12765   -120   -400  -1448       C  
ATOM   3069  OE1 GLN A 465      29.187  18.832 139.218  1.00 93.22           O  
ANISOU 3069  OE1 GLN A 465    12093  10395  12931     94   -400  -1504       O  
ATOM   3070  NE2 GLN A 465      31.408  18.620 139.492  1.00 91.47           N  
ANISOU 3070  NE2 GLN A 465    11827  10263  12664   -212   -415  -1559       N  
ATOM   3071  N   SER A 466      26.685  16.722 135.646  1.00 83.94           N  
ANISOU 3071  N   SER A 466    10740   9406  11748    118   -256   -929       N  
ATOM   3072  CA  SER A 466      25.815  15.632 136.125  1.00 81.18           C  
ANISOU 3072  CA  SER A 466    10261   9252  11331    266   -181   -923       C  
ATOM   3073  C   SER A 466      26.503  14.300 135.728  1.00 79.16           C  
ANISOU 3073  C   SER A 466     9908   9182  10987    142   -116   -853       C  
ATOM   3074  O   SER A 466      25.853  13.262 135.477  1.00 77.96           O  
ANISOU 3074  O   SER A 466     9667   9160  10794    189    -75   -771       O  
ATOM   3075  CB  SER A 466      24.481  15.717 135.409  1.00 81.43           C  
ANISOU 3075  CB  SER A 466    10290   9238  11413    373   -202   -808       C  
ATOM   3076  OG  SER A 466      24.630  15.365 134.032  1.00 79.31           O  
ANISOU 3076  OG  SER A 466    10033   8957  11146    233   -215   -651       O  
ATOM   3077  N   LYS A 467      27.825  14.364 135.625  1.00 77.59           N  
ANISOU 3077  N   LYS A 467     9730   8987  10765    -19   -116   -883       N  
ATOM   3078  CA  LYS A 467      28.635  13.185 135.541  1.00 75.49           C  
ANISOU 3078  CA  LYS A 467     9373   8902  10407   -104    -57   -864       C  
ATOM   3079  C   LYS A 467      28.480  12.381 136.843  1.00 73.67           C  
ANISOU 3079  C   LYS A 467     9050   8832  10109     17     -7   -962       C  
ATOM   3080  O   LYS A 467      28.718  11.168 136.859  1.00 72.12           O  
ANISOU 3080  O   LYS A 467     8769   8795   9839      4     40   -931       O  
ATOM   3081  CB  LYS A 467      30.099  13.568 135.296  1.00 76.35           C  
ANISOU 3081  CB  LYS A 467     9508   8994  10507   -288    -70   -887       C  
ATOM   3082  CG  LYS A 467      30.310  14.692 134.266  1.00 80.04           C  
ANISOU 3082  CG  LYS A 467    10081   9277  11052   -417   -133   -801       C  
ATOM   3083  CD  LYS A 467      29.917  14.284 132.831  1.00 84.12           C  
ANISOU 3083  CD  LYS A 467    10601   9810  11551   -463   -123   -633       C  
ATOM   3084  CE  LYS A 467      31.143  14.195 131.884  1.00 85.91           C  
ANISOU 3084  CE  LYS A 467    10815  10100  11726   -660   -105   -552       C  
ATOM   3085  NZ  LYS A 467      30.770  13.541 130.578  1.00 85.14           N  
ANISOU 3085  NZ  LYS A 467    10708  10068  11573   -675    -86   -411       N  
ATOM   3086  N   LEU A 468      28.076  13.057 137.925  1.00 73.25           N  
ANISOU 3086  N   LEU A 468     9021   8735  10076    140    -21  -1079       N  
ATOM   3087  CA  LEU A 468      27.872  12.405 139.220  1.00 71.72           C  
ANISOU 3087  CA  LEU A 468     8744   8702   9806    265     29  -1166       C  
ATOM   3088  C   LEU A 468      26.709  11.434 139.175  1.00 69.77           C  
ANISOU 3088  C   LEU A 468     8402   8576   9530    373     74  -1066       C  
ATOM   3089  O   LEU A 468      26.678  10.469 139.948  1.00 68.81           O  
ANISOU 3089  O   LEU A 468     8189   8624   9330    423    123  -1076       O  
ATOM   3090  CB  LEU A 468      27.596  13.407 140.341  1.00 73.58           C  
ANISOU 3090  CB  LEU A 468     9032   8871  10055    397      2  -1318       C  
ATOM   3091  CG  LEU A 468      28.617  14.386 140.882  1.00 76.44           C  
ANISOU 3091  CG  LEU A 468     9485   9124  10436    331    -58  -1464       C  
ATOM   3092  CD1 LEU A 468      29.926  13.668 141.243  1.00 76.09           C  
ANISOU 3092  CD1 LEU A 468     9378   9218  10316    206    -34  -1503       C  
ATOM   3093  CD2 LEU A 468      28.806  15.546 139.874  1.00 79.47           C  
ANISOU 3093  CD2 LEU A 468     9996   9264  10936    218   -143  -1421       C  
ATOM   3094  N   ARG A 469      25.746  11.718 138.298  1.00 68.87           N  
ANISOU 3094  N   ARG A 469     8311   8374   9484    403     49   -961       N  
ATOM   3095  CA  ARG A 469      24.607  10.840 138.083  1.00 67.40           C  
ANISOU 3095  CA  ARG A 469     8033   8290   9287    479     73   -845       C  
ATOM   3096  C   ARG A 469      25.056   9.536 137.441  1.00 64.06           C  
ANISOU 3096  C   ARG A 469     7561   7964   8816    363     86   -751       C  
ATOM   3097  O   ARG A 469      24.856   8.482 138.059  1.00 63.22           O  
ANISOU 3097  O   ARG A 469     7363   8008   8650    401    122   -731       O  
ATOM   3098  CB  ARG A 469      23.510  11.513 137.256  1.00 69.18           C  
ANISOU 3098  CB  ARG A 469     8293   8393   9597    537     29   -758       C  
ATOM   3099  CG  ARG A 469      22.447  12.236 138.081  1.00 73.78           C  
ANISOU 3099  CG  ARG A 469     8854   8973  10206    736     34   -817       C  
ATOM   3100  CD  ARG A 469      21.328  12.840 137.167  1.00 79.47           C  
ANISOU 3100  CD  ARG A 469     9600   9581  11016    801    -19   -717       C  
ATOM   3101  NE  ARG A 469      20.753  14.084 137.706  1.00 83.60           N  
ANISOU 3101  NE  ARG A 469    10177   9999  11588    972    -46   -814       N  
ATOM   3102  CZ  ARG A 469      20.758  15.262 137.070  1.00 85.68           C  
ANISOU 3102  CZ  ARG A 469    10574  10039  11940    971   -126   -824       C  
ATOM   3103  NH1 ARG A 469      21.288  15.366 135.853  1.00 84.18           N  
ANISOU 3103  NH1 ARG A 469    10466   9726  11791    798   -176   -726       N  
ATOM   3104  NH2 ARG A 469      20.199  16.332 137.637  1.00 86.74           N  
ANISOU 3104  NH2 ARG A 469    10763  10077  12117   1152   -160   -927       N  
ATOM   3105  N   SER A 470      25.675   9.583 136.248  1.00 61.45           N  
ANISOU 3105  N   SER A 470     7292   7554   8501    230     55   -694       N  
ATOM   3106  CA  SER A 470      26.238   8.331 135.652  1.00 58.97           C  
ANISOU 3106  CA  SER A 470     6943   7336   8126    138     64   -633       C  
ATOM   3107  C   SER A 470      27.031   7.528 136.646  1.00 56.61           C  
ANISOU 3107  C   SER A 470     6584   7174   7750    140    104   -712       C  
ATOM   3108  O   SER A 470      26.784   6.335 136.803  1.00 55.44           O  
ANISOU 3108  O   SER A 470     6373   7132   7559    161    111   -662       O  
ATOM   3109  CB  SER A 470      27.143   8.582 134.479  1.00 58.45           C  
ANISOU 3109  CB  SER A 470     6946   7206   8055      1     43   -601       C  
ATOM   3110  OG  SER A 470      26.490   9.476 133.641  1.00 62.31           O  
ANISOU 3110  OG  SER A 470     7503   7558   8613     -3      1   -531       O  
ATOM   3111  N   LEU A 471      27.940   8.205 137.337  1.00 55.09           N  
ANISOU 3111  N   LEU A 471     6416   6970   7545    118    117   -830       N  
ATOM   3112  CA  LEU A 471      28.852   7.547 138.235  1.00 54.12           C  
ANISOU 3112  CA  LEU A 471     6242   6975   7346    111    146   -910       C  
ATOM   3113  C   LEU A 471      28.107   6.747 139.279  1.00 53.46           C  
ANISOU 3113  C   LEU A 471     6079   7013   7219    228    174   -903       C  
ATOM   3114  O   LEU A 471      28.367   5.546 139.474  1.00 52.54           O  
ANISOU 3114  O   LEU A 471     5909   7010   7044    221    183   -871       O  
ATOM   3115  CB  LEU A 471      29.741   8.563 138.919  1.00 54.63           C  
ANISOU 3115  CB  LEU A 471     6345   6997   7415     81    140  -1043       C  
ATOM   3116  CG  LEU A 471      31.179   8.161 139.142  1.00 54.24           C  
ANISOU 3116  CG  LEU A 471     6266   7039   7305     -9    148  -1107       C  
ATOM   3117  CD1 LEU A 471      31.857   9.234 139.929  1.00 54.72           C  
ANISOU 3117  CD1 LEU A 471     6362   7048   7380    -34    125  -1238       C  
ATOM   3118  CD2 LEU A 471      31.316   6.865 139.837  1.00 54.54           C  
ANISOU 3118  CD2 LEU A 471     6223   7239   7260     48    176  -1110       C  
ATOM   3119  N   ARG A 472      27.190   7.425 139.955  1.00 53.97           N  
ANISOU 3119  N   ARG A 472     6137   7059   7308    340    184   -931       N  
ATOM   3120  CA  ARG A 472      26.350   6.812 140.967  1.00 54.19           C  
ANISOU 3120  CA  ARG A 472     6077   7223   7289    458    221   -909       C  
ATOM   3121  C   ARG A 472      25.581   5.644 140.345  1.00 51.60           C  
ANISOU 3121  C   ARG A 472     5689   6946   6969    439    210   -750       C  
ATOM   3122  O   ARG A 472      25.466   4.597 140.950  1.00 51.16           O  
ANISOU 3122  O   ARG A 472     5562   7016   6858    457    226   -705       O  
ATOM   3123  CB  ARG A 472      25.399   7.863 141.582  1.00 56.13           C  
ANISOU 3123  CB  ARG A 472     6325   7440   7562    598    234   -961       C  
ATOM   3124  CG  ARG A 472      25.826   8.356 142.979  1.00 61.60           C  
ANISOU 3124  CG  ARG A 472     7019   8201   8184    686    260  -1117       C  
ATOM   3125  CD  ARG A 472      25.379   9.841 143.341  1.00 69.93           C  
ANISOU 3125  CD  ARG A 472     8146   9145   9281    804    242  -1235       C  
ATOM   3126  NE  ARG A 472      24.022  10.189 142.882  1.00 74.98           N  
ANISOU 3126  NE  ARG A 472     8762   9744   9982    905    242  -1150       N  
ATOM   3127  CZ  ARG A 472      23.666  11.370 142.356  1.00 79.91           C  
ANISOU 3127  CZ  ARG A 472     9477  10189  10694    946    194  -1184       C  
ATOM   3128  NH1 ARG A 472      24.546  12.370 142.221  1.00 81.13           N  
ANISOU 3128  NH1 ARG A 472     9760  10172  10892    882    136  -1297       N  
ATOM   3129  NH2 ARG A 472      22.412  11.558 141.954  1.00 81.74           N  
ANISOU 3129  NH2 ARG A 472     9670  10412  10977   1048    194  -1097       N  
ATOM   3130  N   ASN A 473      25.087   5.816 139.129  1.00 49.73           N  
ANISOU 3130  N   ASN A 473     5489   6605   6801    395    172   -664       N  
ATOM   3131  CA  ASN A 473      24.331   4.763 138.513  1.00 49.37           C  
ANISOU 3131  CA  ASN A 473     5397   6594   6769    371    142   -522       C  
ATOM   3132  C   ASN A 473      25.220   3.576 138.051  1.00 47.37           C  
ANISOU 3132  C   ASN A 473     5160   6369   6469    276    115   -500       C  
ATOM   3133  O   ASN A 473      24.896   2.413 138.312  1.00 45.93           O  
ANISOU 3133  O   ASN A 473     4924   6266   6261    277     98   -426       O  
ATOM   3134  CB  ASN A 473      23.465   5.341 137.405  1.00 51.01           C  
ANISOU 3134  CB  ASN A 473     5637   6688   7056    367    100   -441       C  
ATOM   3135  CG  ASN A 473      22.762   4.263 136.568  1.00 55.61           C  
ANISOU 3135  CG  ASN A 473     6188   7286   7657    320     45   -298       C  
ATOM   3136  OD1 ASN A 473      21.987   3.412 137.082  1.00 57.73           O  
ANISOU 3136  OD1 ASN A 473     6363   7655   7918    350     42   -215       O  
ATOM   3137  ND2 ASN A 473      23.009   4.317 135.244  1.00 60.58           N  
ANISOU 3137  ND2 ASN A 473     6896   7816   8307    240     -6   -263       N  
ATOM   3138  N   ARG A 474      26.360   3.877 137.432  1.00 45.36           N  
ANISOU 3138  N   ARG A 474     4977   6058   6200    200    109   -566       N  
ATOM   3139  CA  ARG A 474      27.345   2.846 137.108  1.00 43.72           C  
ANISOU 3139  CA  ARG A 474     4780   5897   5934    139     92   -576       C  
ATOM   3140  C   ARG A 474      27.868   2.135 138.339  1.00 43.62           C  
ANISOU 3140  C   ARG A 474     4713   6003   5856    178    116   -627       C  
ATOM   3141  O   ARG A 474      27.981   0.897 138.334  1.00 43.29           O  
ANISOU 3141  O   ARG A 474     4655   6013   5781    173     84   -580       O  
ATOM   3142  CB  ARG A 474      28.470   3.405 136.250  1.00 43.95           C  
ANISOU 3142  CB  ARG A 474     4873   5876   5951     57     94   -632       C  
ATOM   3143  CG  ARG A 474      27.918   3.827 134.920  1.00 43.07           C  
ANISOU 3143  CG  ARG A 474     4818   5662   5885     15     59   -551       C  
ATOM   3144  CD  ARG A 474      28.909   4.508 134.062  1.00 45.61           C  
ANISOU 3144  CD  ARG A 474     5195   5943   6192    -73     67   -580       C  
ATOM   3145  NE  ARG A 474      29.367   5.796 134.554  1.00 47.05           N  
ANISOU 3145  NE  ARG A 474     5396   6072   6407    -99     94   -653       N  
ATOM   3146  CZ  ARG A 474      30.593   6.001 135.023  1.00 50.08           C  
ANISOU 3146  CZ  ARG A 474     5764   6510   6754   -148    121   -744       C  
ATOM   3147  NH1 ARG A 474      31.442   4.953 135.099  1.00 49.72           N  
ANISOU 3147  NH1 ARG A 474     5675   6586   6632   -156    134   -772       N  
ATOM   3148  NH2 ARG A 474      30.969   7.233 135.423  1.00 46.70           N  
ANISOU 3148  NH2 ARG A 474     5365   6010   6368   -187    124   -807       N  
ATOM   3149  N   GLN A 475      28.124   2.874 139.417  1.00 43.26           N  
ANISOU 3149  N   GLN A 475     4647   5998   5793    223    161   -720       N  
ATOM   3150  CA  GLN A 475      28.525   2.220 140.653  1.00 43.31           C  
ANISOU 3150  CA  GLN A 475     4598   6129   5727    269    181   -761       C  
ATOM   3151  C   GLN A 475      27.418   1.327 141.140  1.00 42.83           C  
ANISOU 3151  C   GLN A 475     4474   6139   5661    322    175   -644       C  
ATOM   3152  O   GLN A 475      27.646   0.263 141.702  1.00 42.86           O  
ANISOU 3152  O   GLN A 475     4444   6228   5612    329    162   -610       O  
ATOM   3153  CB  GLN A 475      28.799   3.230 141.755  1.00 44.87           C  
ANISOU 3153  CB  GLN A 475     4789   6360   5899    323    222   -882       C  
ATOM   3154  CG  GLN A 475      30.121   3.966 141.648  1.00 46.59           C  
ANISOU 3154  CG  GLN A 475     5052   6541   6109    256    218  -1006       C  
ATOM   3155  CD  GLN A 475      30.155   5.150 142.579  1.00 47.85           C  
ANISOU 3155  CD  GLN A 475     5229   6686   6267    308    234  -1126       C  
ATOM   3156  OE1 GLN A 475      29.182   5.889 142.692  1.00 52.60           O  
ANISOU 3156  OE1 GLN A 475     5846   7230   6909    376    242  -1122       O  
ATOM   3157  NE2 GLN A 475      31.263   5.325 143.271  1.00 50.21           N  
ANISOU 3157  NE2 GLN A 475     5524   7039   6514    285    230  -1240       N  
ATOM   3158  N   SER A 476      26.196   1.789 140.958  1.00 42.72           N  
ANISOU 3158  N   SER A 476     4437   6094   5701    358    182   -574       N  
ATOM   3159  CA  SER A 476      25.063   1.040 141.454  1.00 42.99           C  
ANISOU 3159  CA  SER A 476     4386   6215   5733    398    181   -447       C  
ATOM   3160  C   SER A 476      24.904  -0.309 140.710  1.00 40.81           C  
ANISOU 3160  C   SER A 476     4117   5912   5476    323    105   -324       C  
ATOM   3161  O   SER A 476      24.779  -1.374 141.349  1.00 40.54           O  
ANISOU 3161  O   SER A 476     4036   5960   5406    320     87   -248       O  
ATOM   3162  CB  SER A 476      23.816   1.912 141.354  1.00 44.54           C  
ANISOU 3162  CB  SER A 476     4543   6394   5986    462    203   -404       C  
ATOM   3163  OG  SER A 476      22.726   1.251 141.916  1.00 48.88           O  
ANISOU 3163  OG  SER A 476     4984   7059   6527    500    212   -275       O  
ATOM   3164  N   LEU A 477      24.978  -0.269 139.377  1.00 38.23           N  
ANISOU 3164  N   LEU A 477     3859   5467   5199    261     53   -308       N  
ATOM   3165  CA  LEU A 477      24.931  -1.475 138.582  1.00 37.04           C  
ANISOU 3165  CA  LEU A 477     3741   5271   5061    199    -33   -223       C  
ATOM   3166  C   LEU A 477      25.932  -2.535 139.032  1.00 36.85           C  
ANISOU 3166  C   LEU A 477     3737   5292   4973    191    -58   -258       C  
ATOM   3167  O   LEU A 477      25.547  -3.710 139.194  1.00 36.28           O  
ANISOU 3167  O   LEU A 477     3651   5231   4904    172   -123   -158       O  
ATOM   3168  CB  LEU A 477      25.148  -1.146 137.120  1.00 37.17           C  
ANISOU 3168  CB  LEU A 477     3843   5172   5108    149    -75   -240       C  
ATOM   3169  CG  LEU A 477      24.004  -0.378 136.493  1.00 37.86           C  
ANISOU 3169  CG  LEU A 477     3918   5200   5267    152    -85   -170       C  
ATOM   3170  CD1 LEU A 477      24.349   0.036 135.081  1.00 35.25           C  
ANISOU 3170  CD1 LEU A 477     3680   4765   4949    102   -120   -190       C  
ATOM   3171  CD2 LEU A 477      22.706  -1.195 136.550  1.00 39.43           C  
ANISOU 3171  CD2 LEU A 477     4047   5424   5512    142   -145    -18       C  
ATOM   3172  N   PHE A 478      27.193  -2.124 139.233  1.00 36.10           N  
ANISOU 3172  N   PHE A 478     3673   5219   4825    203    -16   -391       N  
ATOM   3173  CA  PHE A 478      28.246  -3.035 139.673  1.00 37.07           C  
ANISOU 3173  CA  PHE A 478     3809   5394   4883    213    -38   -438       C  
ATOM   3174  C   PHE A 478      27.969  -3.542 141.102  1.00 38.96           C  
ANISOU 3174  C   PHE A 478     3978   5742   5082    256    -20   -393       C  
ATOM   3175  O   PHE A 478      28.090  -4.757 141.389  1.00 39.26           O  
ANISOU 3175  O   PHE A 478     4021   5797   5097    255    -81   -330       O  
ATOM   3176  CB  PHE A 478      29.630  -2.379 139.616  1.00 36.54           C  
ANISOU 3176  CB  PHE A 478     3765   5350   4770    211      7   -585       C  
ATOM   3177  CG  PHE A 478      30.274  -2.387 138.261  1.00 36.54           C  
ANISOU 3177  CG  PHE A 478     3829   5286   4770    169    -21   -619       C  
ATOM   3178  CD1 PHE A 478      31.486  -3.076 138.052  1.00 38.52           C  
ANISOU 3178  CD1 PHE A 478     4098   5579   4959    181    -42   -687       C  
ATOM   3179  CD2 PHE A 478      29.730  -1.657 137.200  1.00 34.58           C  
ANISOU 3179  CD2 PHE A 478     3617   4951   4572    127    -21   -588       C  
ATOM   3180  CE1 PHE A 478      32.104  -3.096 136.784  1.00 34.00           C  
ANISOU 3180  CE1 PHE A 478     3574   4979   4365    157    -58   -720       C  
ATOM   3181  CE2 PHE A 478      30.343  -1.647 135.934  1.00 33.14           C  
ANISOU 3181  CE2 PHE A 478     3491   4732   4369     90    -40   -613       C  
ATOM   3182  CZ  PHE A 478      31.529  -2.353 135.734  1.00 34.78           C  
ANISOU 3182  CZ  PHE A 478     3710   4999   4506    106    -52   -681       C  
ATOM   3183  N   GLN A 479      27.591  -2.633 142.002  1.00 39.95           N  
ANISOU 3183  N   GLN A 479     4045   5941   5194    301     56   -421       N  
ATOM   3184  CA  GLN A 479      27.270  -3.059 143.368  1.00 42.09           C  
ANISOU 3184  CA  GLN A 479     4244   6342   5407    349     83   -371       C  
ATOM   3185  C   GLN A 479      26.149  -4.068 143.417  1.00 42.03           C  
ANISOU 3185  C   GLN A 479     4190   6348   5430    322     33   -186       C  
ATOM   3186  O   GLN A 479      26.306  -5.080 144.077  1.00 41.70           O  
ANISOU 3186  O   GLN A 479     4134   6365   5346    319     -2   -117       O  
ATOM   3187  CB  GLN A 479      26.926  -1.885 144.236  1.00 42.84           C  
ANISOU 3187  CB  GLN A 479     4289   6517   5473    419    170   -438       C  
ATOM   3188  CG  GLN A 479      28.078  -0.924 144.303  1.00 48.66           C  
ANISOU 3188  CG  GLN A 479     5073   7232   6184    429    200   -617       C  
ATOM   3189  CD  GLN A 479      27.924   0.044 145.441  1.00 52.70           C  
ANISOU 3189  CD  GLN A 479     5550   7833   6643    514    266   -706       C  
ATOM   3190  OE1 GLN A 479      27.550  -0.341 146.551  1.00 58.15           O  
ANISOU 3190  OE1 GLN A 479     6176   8660   7259    576    295   -665       O  
ATOM   3191  NE2 GLN A 479      28.193   1.294 145.176  1.00 52.22           N  
ANISOU 3191  NE2 GLN A 479     5534   7694   6613    518    284   -826       N  
ATOM   3192  N   GLU A 480      25.050  -3.819 142.689  1.00 42.12           N  
ANISOU 3192  N   GLU A 480     4183   6303   5519    294     18    -98       N  
ATOM   3193  CA  GLU A 480      23.955  -4.773 142.686  1.00 43.67           C  
ANISOU 3193  CA  GLU A 480     4324   6513   5755    246    -42     90       C  
ATOM   3194  C   GLU A 480      24.350  -6.122 142.066  1.00 43.06           C  
ANISOU 3194  C   GLU A 480     4327   6334   5701    176   -166    148       C  
ATOM   3195  O   GLU A 480      23.724  -7.120 142.342  1.00 43.81           O  
ANISOU 3195  O   GLU A 480     4389   6442   5815    127   -234    300       O  
ATOM   3196  CB  GLU A 480      22.736  -4.197 142.002  1.00 44.58           C  
ANISOU 3196  CB  GLU A 480     4394   6595   5950    233    -42    167       C  
ATOM   3197  CG  GLU A 480      22.193  -2.936 142.634  1.00 50.04           C  
ANISOU 3197  CG  GLU A 480     5007   7383   6624    325     67    119       C  
ATOM   3198  CD  GLU A 480      21.546  -3.160 144.037  1.00 59.15           C  
ANISOU 3198  CD  GLU A 480     6030   8734   7709    380    133    209       C  
ATOM   3199  OE1 GLU A 480      21.390  -4.330 144.505  1.00 59.57           O  
ANISOU 3199  OE1 GLU A 480     6044   8848   7741    325     89    344       O  
ATOM   3200  OE2 GLU A 480      21.176  -2.132 144.663  1.00 63.18           O  
ANISOU 3200  OE2 GLU A 480     6481   9340   8184    484    226    146       O  
ATOM   3201  N   GLU A 481      25.395  -6.154 141.241  1.00 42.16           N  
ANISOU 3201  N   GLU A 481     4316   6121   5580    173   -201     26       N  
ATOM   3202  CA  GLU A 481      25.900  -7.438 140.737  1.00 42.41           C  
ANISOU 3202  CA  GLU A 481     4435   6064   5616    141   -321     49       C  
ATOM   3203  C   GLU A 481      27.034  -8.050 141.613  1.00 42.96           C  
ANISOU 3203  C   GLU A 481     4523   6193   5607    189   -322    -12       C  
ATOM   3204  O   GLU A 481      27.700  -8.981 141.202  1.00 42.80           O  
ANISOU 3204  O   GLU A 481     4585   6099   5578    193   -414    -35       O  
ATOM   3205  CB  GLU A 481      26.280  -7.345 139.256  1.00 41.30           C  
ANISOU 3205  CB  GLU A 481     4393   5796   5502    123   -374    -27       C  
ATOM   3206  CG  GLU A 481      25.064  -7.342 138.343  1.00 41.72           C  
ANISOU 3206  CG  GLU A 481     4448   5766   5637     61   -437     81       C  
ATOM   3207  CD  GLU A 481      24.412  -8.709 138.257  1.00 46.41           C  
ANISOU 3207  CD  GLU A 481     5066   6291   6277      1   -579    223       C  
ATOM   3208  OE1 GLU A 481      25.036  -9.616 137.657  1.00 48.41           O  
ANISOU 3208  OE1 GLU A 481     5430   6447   6519      3   -684    181       O  
ATOM   3209  OE2 GLU A 481      23.271  -8.909 138.755  1.00 50.62           O  
ANISOU 3209  OE2 GLU A 481     5510   6865   6859    -50   -594    380       O  
ATOM   3210  N   GLY A 482      27.202  -7.550 142.836  1.00 42.96           N  
ANISOU 3210  N   GLY A 482     4448   6330   5545    234   -229    -38       N  
ATOM   3211  CA  GLY A 482      28.114  -8.153 143.740  1.00 43.78           C  
ANISOU 3211  CA  GLY A 482     4558   6503   5574    278   -240    -71       C  
ATOM   3212  C   GLY A 482      29.577  -7.862 143.495  1.00 43.92           C  
ANISOU 3212  C   GLY A 482     4625   6520   5543    325   -223   -251       C  
ATOM   3213  O   GLY A 482      30.425  -8.579 143.968  1.00 44.81           O  
ANISOU 3213  O   GLY A 482     4758   6663   5603    364   -263   -279       O  
ATOM   3214  N   MET A 483      29.889  -6.808 142.781  1.00 44.24           N  
ANISOU 3214  N   MET A 483     4676   6534   5599    320   -166   -363       N  
ATOM   3215  CA  MET A 483      31.264  -6.502 142.520  1.00 45.93           C  
ANISOU 3215  CA  MET A 483     4916   6768   5769    348   -147   -516       C  
ATOM   3216  C   MET A 483      32.043  -6.113 143.787  1.00 45.74           C  
ANISOU 3216  C   MET A 483     4837   6877   5666    395    -90   -600       C  
ATOM   3217  O   MET A 483      33.234  -6.389 143.865  1.00 46.09           O  
ANISOU 3217  O   MET A 483     4888   6962   5661    427   -107   -691       O  
ATOM   3218  CB  MET A 483      31.392  -5.438 141.437  1.00 46.85           C  
ANISOU 3218  CB  MET A 483     5054   6827   5921    311   -103   -593       C  
ATOM   3219  CG  MET A 483      30.814  -5.871 140.080  1.00 51.00           C  
ANISOU 3219  CG  MET A 483     5645   7229   6503    273   -170   -528       C  
ATOM   3220  SD  MET A 483      31.796  -7.167 139.213  1.00 59.63           S  
ANISOU 3220  SD  MET A 483     6823   8275   7560    310   -272   -572       S  
ATOM   3221  CE  MET A 483      30.726  -8.602 139.535  1.00 56.53           C  
ANISOU 3221  CE  MET A 483     6466   7802   7212    300   -397   -408       C  
ATOM   3222  N   LEU A 484      31.383  -5.536 144.782  1.00 45.06           N  
ANISOU 3222  N   LEU A 484     4692   6870   5560    409    -29   -572       N  
ATOM   3223  CA  LEU A 484      32.060  -5.253 146.038  1.00 45.60           C  
ANISOU 3223  CA  LEU A 484     4716   7070   5540    460     11   -651       C  
ATOM   3224  C   LEU A 484      32.586  -6.482 146.736  1.00 45.79           C  
ANISOU 3224  C   LEU A 484     4742   7153   5503    498    -52   -603       C  
ATOM   3225  O   LEU A 484      33.769  -6.474 147.090  1.00 45.92           O  
ANISOU 3225  O   LEU A 484     4753   7233   5462    533    -59   -711       O  
ATOM   3226  CB  LEU A 484      31.200  -4.455 147.023  1.00 47.03           C  
ANISOU 3226  CB  LEU A 484     4840   7340   5691    492     86   -636       C  
ATOM   3227  CG  LEU A 484      31.174  -2.931 146.891  1.00 48.53           C  
ANISOU 3227  CG  LEU A 484     5028   7509   5902    494    153   -759       C  
ATOM   3228  CD1 LEU A 484      30.217  -2.311 147.930  1.00 47.76           C  
ANISOU 3228  CD1 LEU A 484     4876   7510   5760    560    218   -741       C  
ATOM   3229  CD2 LEU A 484      32.557  -2.389 147.040  1.00 45.27           C  
ANISOU 3229  CD2 LEU A 484     4630   7121   5451    491    154   -922       C  
ATOM   3230  N   SER A 485      31.754  -7.519 146.945  1.00 45.49           N  
ANISOU 3230  N   SER A 485     4708   7097   5480    488   -106   -437       N  
ATOM   3231  CA  SER A 485      32.259  -8.776 147.524  1.00 47.55           C  
ANISOU 3231  CA  SER A 485     4990   7383   5692    520   -189   -374       C  
ATOM   3232  C   SER A 485      33.390  -9.342 146.705  1.00 47.98           C  
ANISOU 3232  C   SER A 485     5111   7361   5760    545   -262   -465       C  
ATOM   3233  O   SER A 485      34.343  -9.906 147.266  1.00 49.39           O  
ANISOU 3233  O   SER A 485     5293   7596   5875    605   -304   -506       O  
ATOM   3234  CB  SER A 485      31.228  -9.880 147.577  1.00 47.13           C  
ANISOU 3234  CB  SER A 485     4953   7274   5681    478   -265   -169       C  
ATOM   3235  OG  SER A 485      30.013  -9.284 147.784  1.00 51.30           O  
ANISOU 3235  OG  SER A 485     5416   7846   6230    441   -196    -82       O  
ATOM   3236  N   LEU A 486      33.268  -9.185 145.393  1.00 47.00           N  
ANISOU 3236  N   LEU A 486     5033   7119   5706    510   -277   -494       N  
ATOM   3237  CA  LEU A 486      34.151  -9.808 144.491  1.00 48.38           C  
ANISOU 3237  CA  LEU A 486     5271   7224   5886    544   -347   -564       C  
ATOM   3238  C   LEU A 486      35.525  -9.224 144.697  1.00 48.86           C  
ANISOU 3238  C   LEU A 486     5288   7393   5882    591   -297   -726       C  
ATOM   3239  O   LEU A 486      36.473  -9.953 144.905  1.00 49.97           O  
ANISOU 3239  O   LEU A 486     5439   7571   5977    662   -353   -771       O  
ATOM   3240  CB  LEU A 486      33.650  -9.575 143.074  1.00 48.51           C  
ANISOU 3240  CB  LEU A 486     5338   7119   5974    495   -358   -564       C  
ATOM   3241  CG  LEU A 486      33.904 -10.685 142.051  1.00 49.70           C  
ANISOU 3241  CG  LEU A 486     5587   7151   6146    527   -475   -562       C  
ATOM   3242  CD1 LEU A 486      34.915 -10.152 141.136  1.00 51.84           C  
ANISOU 3242  CD1 LEU A 486     5860   7453   6386    557   -433   -709       C  
ATOM   3243  CD2 LEU A 486      34.348 -12.008 142.688  1.00 47.24           C  
ANISOU 3243  CD2 LEU A 486     5319   6826   5805    597   -584   -522       C  
ATOM   3244  N   VAL A 487      35.609  -7.898 144.688  1.00 48.33           N  
ANISOU 3244  N   VAL A 487     5170   7378   5815    550   -199   -809       N  
ATOM   3245  CA  VAL A 487      36.822  -7.195 144.969  1.00 47.61           C  
ANISOU 3245  CA  VAL A 487     5025   7394   5672    566   -153   -951       C  
ATOM   3246  C   VAL A 487      37.317  -7.507 146.385  1.00 49.25           C  
ANISOU 3246  C   VAL A 487     5187   7724   5799    623   -167   -964       C  
ATOM   3247  O   VAL A 487      38.496  -7.783 146.583  1.00 50.12           O  
ANISOU 3247  O   VAL A 487     5270   7915   5859    673   -194  -1047       O  
ATOM   3248  CB  VAL A 487      36.574  -5.730 144.809  1.00 47.57           C  
ANISOU 3248  CB  VAL A 487     4990   7387   5696    497    -66  -1010       C  
ATOM   3249  CG1 VAL A 487      37.815  -4.909 145.225  1.00 46.71           C  
ANISOU 3249  CG1 VAL A 487     4820   7386   5540    489    -31  -1152       C  
ATOM   3250  CG2 VAL A 487      36.172  -5.457 143.380  1.00 44.14           C  
ANISOU 3250  CG2 VAL A 487     4602   6839   5331    443    -60   -990       C  
ATOM   3251  N   LEU A 488      36.422  -7.512 147.365  1.00 50.12           N  
ANISOU 3251  N   LEU A 488     5286   7866   5891    624   -151   -876       N  
ATOM   3252  CA  LEU A 488      36.802  -7.917 148.719  1.00 51.38           C  
ANISOU 3252  CA  LEU A 488     5412   8151   5959    683   -171   -866       C  
ATOM   3253  C   LEU A 488      37.375  -9.302 148.801  1.00 52.02           C  
ANISOU 3253  C   LEU A 488     5527   8221   6016    747   -273   -815       C  
ATOM   3254  O   LEU A 488      38.281  -9.536 149.588  1.00 52.91           O  
ANISOU 3254  O   LEU A 488     5610   8442   6053    807   -300   -868       O  
ATOM   3255  CB  LEU A 488      35.632  -7.834 149.686  1.00 52.18           C  
ANISOU 3255  CB  LEU A 488     5493   8301   6031    679   -135   -752       C  
ATOM   3256  CG  LEU A 488      35.762  -6.749 150.746  1.00 54.22           C  
ANISOU 3256  CG  LEU A 488     5696   8694   6210    700    -62   -849       C  
ATOM   3257  CD1 LEU A 488      37.003  -7.006 151.589  1.00 55.70           C  
ANISOU 3257  CD1 LEU A 488     5859   9003   6303    758   -102   -935       C  
ATOM   3258  CD2 LEU A 488      35.895  -5.423 150.038  1.00 55.81           C  
ANISOU 3258  CD2 LEU A 488     5896   8841   6468    652     -4   -980       C  
ATOM   3259  N   ASN A 489      36.856 -10.231 148.005  1.00 51.75           N  
ANISOU 3259  N   ASN A 489     5564   8053   6047    739   -344   -715       N  
ATOM   3260  CA  ASN A 489      37.385 -11.572 148.053  1.00 52.78           C  
ANISOU 3260  CA  ASN A 489     5748   8145   6161    811   -460   -671       C  
ATOM   3261  C   ASN A 489      38.809 -11.656 147.535  1.00 52.38           C  
ANISOU 3261  C   ASN A 489     5686   8132   6083    887   -483   -823       C  
ATOM   3262  O   ASN A 489      39.593 -12.436 148.034  1.00 53.24           O  
ANISOU 3262  O   ASN A 489     5800   8287   6143    975   -556   -835       O  
ATOM   3263  CB  ASN A 489      36.495 -12.529 147.298  1.00 53.78           C  
ANISOU 3263  CB  ASN A 489     5966   8099   6368    782   -549   -540       C  
ATOM   3264  CG  ASN A 489      35.309 -12.953 148.111  1.00 56.99           C  
ANISOU 3264  CG  ASN A 489     6373   8497   6784    727   -569   -348       C  
ATOM   3265  OD1 ASN A 489      34.241 -13.112 147.578  1.00 62.95           O  
ANISOU 3265  OD1 ASN A 489     7157   9149   7613    654   -588   -240       O  
ATOM   3266  ND2 ASN A 489      35.485 -13.113 149.411  1.00 61.19           N  
ANISOU 3266  ND2 ASN A 489     6862   9154   7233    759   -562   -300       N  
ATOM   3267  N   CYS A 490      39.138 -10.844 146.541  1.00 51.15           N  
ANISOU 3267  N   CYS A 490     5508   7969   5956    853   -421   -931       N  
ATOM   3268  CA  CYS A 490      40.481 -10.790 146.069  1.00 51.49           C  
ANISOU 3268  CA  CYS A 490     5511   8089   5964    914   -423  -1067       C  
ATOM   3269  C   CYS A 490      41.378 -10.219 147.166  1.00 51.72           C  
ANISOU 3269  C   CYS A 490     5442   8290   5919    931   -388  -1151       C  
ATOM   3270  O   CYS A 490      42.431 -10.786 147.452  1.00 52.64           O  
ANISOU 3270  O   CYS A 490     5526   8492   5982   1024   -441  -1206       O  
ATOM   3271  CB  CYS A 490      40.574  -9.970 144.794  1.00 50.81           C  
ANISOU 3271  CB  CYS A 490     5414   7974   5916    854   -356  -1140       C  
ATOM   3272  SG  CYS A 490      39.623 -10.624 143.425  1.00 52.97           S  
ANISOU 3272  SG  CYS A 490     5806   8059   6262    842   -409  -1062       S  
ATOM   3273  N   ILE A 491      40.967  -9.111 147.786  1.00 51.11           N  
ANISOU 3273  N   ILE A 491     5320   8263   5836    852   -308  -1166       N  
ATOM   3274  CA  ILE A 491      41.762  -8.521 148.843  1.00 51.14           C  
ANISOU 3274  CA  ILE A 491     5243   8421   5767    862   -289  -1254       C  
ATOM   3275  C   ILE A 491      41.965  -9.520 149.983  1.00 52.92           C  
ANISOU 3275  C   ILE A 491     5474   8715   5918    954   -366  -1194       C  
ATOM   3276  O   ILE A 491      43.087  -9.691 150.443  1.00 53.20           O  
ANISOU 3276  O   ILE A 491     5452   8869   5893   1017   -403  -1271       O  
ATOM   3277  CB  ILE A 491      41.145  -7.250 149.371  1.00 50.52           C  
ANISOU 3277  CB  ILE A 491     5142   8362   5690    780   -209  -1281       C  
ATOM   3278  CG1 ILE A 491      41.108  -6.191 148.277  1.00 49.21           C  
ANISOU 3278  CG1 ILE A 491     4970   8128   5598    686   -145  -1344       C  
ATOM   3279  CG2 ILE A 491      41.921  -6.730 150.541  1.00 49.85           C  
ANISOU 3279  CG2 ILE A 491     4990   8429   5522    797   -211  -1376       C  
ATOM   3280  CD1 ILE A 491      40.189  -5.006 148.571  1.00 42.45           C  
ANISOU 3280  CD1 ILE A 491     4127   7232   4770    617    -78  -1350       C  
ATOM   3281  N   ASP A 492      40.910 -10.199 150.430  1.00 53.57           N  
ANISOU 3281  N   ASP A 492     5620   8730   6004    960   -395  -1046       N  
ATOM   3282  CA  ASP A 492      41.087 -11.097 151.567  1.00 55.88           C  
ANISOU 3282  CA  ASP A 492     5921   9093   6219   1037   -469   -969       C  
ATOM   3283  C   ASP A 492      42.075 -12.208 151.216  1.00 57.20           C  
ANISOU 3283  C   ASP A 492     6112   9241   6382   1143   -575   -989       C  
ATOM   3284  O   ASP A 492      42.973 -12.504 151.992  1.00 59.21           O  
ANISOU 3284  O   ASP A 492     6325   9612   6559   1221   -624  -1029       O  
ATOM   3285  CB  ASP A 492      39.757 -11.651 152.101  1.00 55.94           C  
ANISOU 3285  CB  ASP A 492     5981   9043   6229   1008   -482   -779       C  
ATOM   3286  CG  ASP A 492      38.921 -10.584 152.862  1.00 59.07           C  
ANISOU 3286  CG  ASP A 492     6331   9528   6585    950   -377   -770       C  
ATOM   3287  OD1 ASP A 492      39.291  -9.386 152.841  1.00 61.63           O  
ANISOU 3287  OD1 ASP A 492     6605   9913   6898    924   -304   -916       O  
ATOM   3288  OD2 ASP A 492      37.888 -10.921 153.490  1.00 60.25           O  
ANISOU 3288  OD2 ASP A 492     6492   9690   6710    932   -369   -616       O  
ATOM   3289  N   ARG A 493      41.951 -12.786 150.029  1.00 56.99           N  
ANISOU 3289  N   ARG A 493     6150   9072   6430   1156   -616   -974       N  
ATOM   3290  CA  ARG A 493      42.817 -13.876 149.635  1.00 57.69           C  
ANISOU 3290  CA  ARG A 493     6276   9130   6514   1281   -724  -1002       C  
ATOM   3291  C   ARG A 493      44.289 -13.494 149.465  1.00 58.54           C  
ANISOU 3291  C   ARG A 493     6281   9391   6573   1352   -706  -1171       C  
ATOM   3292  O   ARG A 493      45.176 -14.298 149.803  1.00 59.78           O  
ANISOU 3292  O   ARG A 493     6428   9603   6683   1480   -794  -1196       O  
ATOM   3293  CB  ARG A 493      42.272 -14.556 148.396  1.00 57.22           C  
ANISOU 3293  CB  ARG A 493     6323   8882   6538   1287   -778   -960       C  
ATOM   3294  CG  ARG A 493      41.273 -15.620 148.750  1.00 58.14           C  
ANISOU 3294  CG  ARG A 493     6552   8849   6691   1277   -881   -778       C  
ATOM   3295  CD  ARG A 493      40.267 -15.768 147.684  1.00 59.74           C  
ANISOU 3295  CD  ARG A 493     6838   8875   6984   1204   -895   -717       C  
ATOM   3296  NE  ARG A 493      39.592 -17.047 147.797  1.00 63.64           N  
ANISOU 3296  NE  ARG A 493     7453   9201   7525   1213  -1040   -560       N  
ATOM   3297  CZ  ARG A 493      38.306 -17.201 148.079  1.00 64.48           C  
ANISOU 3297  CZ  ARG A 493     7593   9225   7681   1098  -1052   -385       C  
ATOM   3298  NH1 ARG A 493      37.523 -16.147 148.284  1.00 65.87           N  
ANISOU 3298  NH1 ARG A 493     7688   9478   7860    985   -921   -354       N  
ATOM   3299  NH2 ARG A 493      37.802 -18.421 148.147  1.00 65.87           N  
ANISOU 3299  NH2 ARG A 493     7881   9241   7906   1096  -1203   -237       N  
ATOM   3300  N   LEU A 494      44.549 -12.297 148.944  1.00 57.73           N  
ANISOU 3300  N   LEU A 494     6097   9355   6483   1268   -599  -1275       N  
ATOM   3301  CA  LEU A 494      45.915 -11.803 148.853  1.00 59.12           C  
ANISOU 3301  CA  LEU A 494     6149   9699   6613   1301   -575  -1418       C  
ATOM   3302  C   LEU A 494      46.510 -11.413 150.216  1.00 60.54           C  
ANISOU 3302  C   LEU A 494     6243  10043   6716   1306   -582  -1457       C  
ATOM   3303  O   LEU A 494      47.729 -11.459 150.392  1.00 62.24           O  
ANISOU 3303  O   LEU A 494     6360  10406   6883   1374   -611  -1549       O  
ATOM   3304  CB  LEU A 494      46.043 -10.657 147.841  1.00 57.89           C  
ANISOU 3304  CB  LEU A 494     5935   9560   6499   1192   -470  -1500       C  
ATOM   3305  CG  LEU A 494      45.806 -11.100 146.382  1.00 58.93           C  
ANISOU 3305  CG  LEU A 494     6134   9578   6680   1218   -471  -1491       C  
ATOM   3306  CD1 LEU A 494      45.484  -9.901 145.514  1.00 58.06           C  
ANISOU 3306  CD1 LEU A 494     5998   9447   6617   1079   -365  -1519       C  
ATOM   3307  CD2 LEU A 494      46.993 -11.885 145.746  1.00 58.33           C  
ANISOU 3307  CD2 LEU A 494     6015   9588   6561   1369   -522  -1573       C  
ATOM   3308  N   ASN A 495      45.664 -11.034 151.172  1.00 60.50           N  
ANISOU 3308  N   ASN A 495     6268  10027   6691   1241   -559  -1390       N  
ATOM   3309  CA  ASN A 495      46.132 -10.600 152.480  1.00 61.70           C  
ANISOU 3309  CA  ASN A 495     6351  10335   6756   1245   -568  -1433       C  
ATOM   3310  C   ASN A 495      46.316 -11.749 153.456  1.00 63.77           C  
ANISOU 3310  C   ASN A 495     6646  10639   6945   1365   -672  -1349       C  
ATOM   3311  O   ASN A 495      46.695 -11.533 154.596  1.00 64.71           O  
ANISOU 3311  O   ASN A 495     6718  10896   6975   1384   -693  -1373       O  
ATOM   3312  CB  ASN A 495      45.240  -9.496 153.078  1.00 60.31           C  
ANISOU 3312  CB  ASN A 495     6183  10160   6571   1135   -487  -1430       C  
ATOM   3313  CG  ASN A 495      45.608  -8.108 152.562  1.00 59.48           C  
ANISOU 3313  CG  ASN A 495     6011  10082   6506   1026   -411  -1562       C  
ATOM   3314  OD1 ASN A 495      46.744  -7.864 152.153  1.00 60.33           O  
ANISOU 3314  OD1 ASN A 495     6030  10274   6616   1022   -422  -1663       O  
ATOM   3315  ND2 ASN A 495      44.653  -7.199 152.569  1.00 55.83           N  
ANISOU 3315  ND2 ASN A 495     5585   9550   6076    936   -339  -1555       N  
ATOM   3316  N   VAL A 496      46.044 -12.969 152.999  1.00 65.03           N  
ANISOU 3316  N   VAL A 496     6896  10671   7141   1444   -748  -1250       N  
ATOM   3317  CA  VAL A 496      46.457 -14.179 153.709  1.00 66.99           C  
ANISOU 3317  CA  VAL A 496     7181  10939   7334   1575   -872  -1177       C  
ATOM   3318  C   VAL A 496      47.983 -14.166 153.822  1.00 68.41           C  
ANISOU 3318  C   VAL A 496     7247  11284   7460   1676   -914  -1315       C  
ATOM   3319  O   VAL A 496      48.539 -14.695 154.785  1.00 69.58           O  
ANISOU 3319  O   VAL A 496     7377  11530   7531   1769   -998  -1294       O  
ATOM   3320  CB  VAL A 496      45.951 -15.473 152.980  1.00 67.51           C  
ANISOU 3320  CB  VAL A 496     7380  10800   7471   1641   -965  -1064       C  
ATOM   3321  CG1 VAL A 496      46.884 -16.649 153.196  1.00 68.09           C  
ANISOU 3321  CG1 VAL A 496     7476  10885   7510   1815  -1105  -1064       C  
ATOM   3322  CG2 VAL A 496      44.495 -15.838 153.404  1.00 66.86           C  
ANISOU 3322  CG2 VAL A 496     7401  10591   7413   1557   -973   -870       C  
ATOM   3323  N   TYR A 497      48.632 -13.511 152.860  1.00 68.54           N  
ANISOU 3323  N   TYR A 497     7179  11348   7515   1649   -852  -1447       N  
ATOM   3324  CA  TYR A 497      50.104 -13.371 152.791  1.00 70.72           C  
ANISOU 3324  CA  TYR A 497     7314  11807   7750   1725   -874  -1581       C  
ATOM   3325  C   TYR A 497      50.572 -12.045 153.382  1.00 71.66           C  
ANISOU 3325  C   TYR A 497     7305  12091   7831   1607   -809  -1681       C  
ATOM   3326  O   TYR A 497      49.943 -11.008 153.161  1.00 71.90           O  
ANISOU 3326  O   TYR A 497     7343  12075   7901   1460   -716  -1698       O  
ATOM   3327  CB  TYR A 497      50.613 -13.537 151.340  1.00 69.64           C  
ANISOU 3327  CB  TYR A 497     7146  11647   7667   1773   -850  -1654       C  
ATOM   3328  CG  TYR A 497      50.166 -14.850 150.797  1.00 69.99           C  
ANISOU 3328  CG  TYR A 497     7333  11514   7745   1899   -936  -1574       C  
ATOM   3329  CD1 TYR A 497      50.898 -16.000 151.058  1.00 70.62           C  
ANISOU 3329  CD1 TYR A 497     7428  11620   7786   2093  -1061  -1575       C  
ATOM   3330  CD2 TYR A 497      48.955 -14.973 150.081  1.00 68.35           C  
ANISOU 3330  CD2 TYR A 497     7260  11100   7612   1826   -910  -1492       C  
ATOM   3331  CE1 TYR A 497      50.469 -17.250 150.600  1.00 73.15           C  
ANISOU 3331  CE1 TYR A 497     7904  11745   8144   2213  -1167  -1503       C  
ATOM   3332  CE2 TYR A 497      48.505 -16.225 149.619  1.00 67.89           C  
ANISOU 3332  CE2 TYR A 497     7349  10855   7591   1932  -1014  -1415       C  
ATOM   3333  CZ  TYR A 497      49.269 -17.358 149.885  1.00 71.54           C  
ANISOU 3333  CZ  TYR A 497     7835  11328   8017   2124  -1146  -1424       C  
ATOM   3334  OH  TYR A 497      48.878 -18.608 149.465  1.00 71.63           O  
ANISOU 3334  OH  TYR A 497     8009  11138   8071   2235  -1273  -1357       O  
ATOM   3335  N   THR A 498      51.665 -12.090 154.138  1.00 73.69           N  
ANISOU 3335  N   THR A 498     7452  12531   8013   1676   -872  -1747       N  
ATOM   3336  CA  THR A 498      52.169 -10.913 154.837  1.00 75.03           C  
ANISOU 3336  CA  THR A 498     7510  12858   8141   1568   -844  -1846       C  
ATOM   3337  C   THR A 498      53.027 -10.031 153.932  1.00 75.51           C  
ANISOU 3337  C   THR A 498     7428  13012   8249   1479   -784  -1963       C  
ATOM   3338  O   THR A 498      53.143  -8.823 154.179  1.00 75.79           O  
ANISOU 3338  O   THR A 498     7402  13104   8292   1332   -741  -2036       O  
ATOM   3339  CB  THR A 498      53.026 -11.290 156.098  1.00 76.78           C  
ANISOU 3339  CB  THR A 498     7663  13256   8255   1668   -951  -1868       C  
ATOM   3340  OG1 THR A 498      53.986 -12.287 155.739  1.00 77.33           O  
ANISOU 3340  OG1 THR A 498     7673  13394   8315   1833  -1030  -1880       O  
ATOM   3341  CG2 THR A 498      52.158 -11.828 157.240  1.00 76.82           C  
ANISOU 3341  CG2 THR A 498     7793  13209   8188   1710   -998  -1749       C  
ATOM   3342  N   THR A 499      53.621 -10.608 152.883  1.00 75.85           N  
ANISOU 3342  N   THR A 499     7421  13074   8323   1566   -783  -1980       N  
ATOM   3343  CA  THR A 499      54.688  -9.877 152.196  1.00 76.48           C  
ANISOU 3343  CA  THR A 499     7325  13315   8421   1500   -738  -2081       C  
ATOM   3344  C   THR A 499      54.800  -9.836 150.656  1.00 75.22           C  
ANISOU 3344  C   THR A 499     7135  13127   8317   1488   -658  -2093       C  
ATOM   3345  O   THR A 499      54.706 -10.842 149.975  1.00 74.41           O  
ANISOU 3345  O   THR A 499     7095  12961   8217   1635   -677  -2062       O  
ATOM   3346  CB  THR A 499      56.027 -10.184 152.882  1.00 78.62           C  
ANISOU 3346  CB  THR A 499     7436  13819   8619   1602   -827  -2146       C  
ATOM   3347  OG1 THR A 499      56.606  -8.944 153.286  1.00 80.09           O  
ANISOU 3347  OG1 THR A 499     7488  14142   8802   1434   -811  -2227       O  
ATOM   3348  CG2 THR A 499      56.972 -11.002 151.992  1.00 79.85           C  
ANISOU 3348  CG2 THR A 499     7488  14085   8765   1767   -844  -2177       C  
ATOM   3349  N   TYR A 506      54.973 -20.157 147.500  1.00 78.02           N  
ANISOU 3349  N   TYR A 506     8324  12696   8626   3169  -1405  -1994       N  
ATOM   3350  CA  TYR A 506      53.487 -20.231 147.135  1.00 77.95           C  
ANISOU 3350  CA  TYR A 506     8522  12396   8698   3020  -1405  -1885       C  
ATOM   3351  C   TYR A 506      53.044 -20.019 145.662  1.00 77.37           C  
ANISOU 3351  C   TYR A 506     8503  12243   8653   2987  -1329  -1941       C  
ATOM   3352  O   TYR A 506      52.749 -20.988 144.933  1.00 77.49           O  
ANISOU 3352  O   TYR A 506     8683  12073   8688   3130  -1432  -1957       O  
ATOM   3353  CB  TYR A 506      52.589 -19.390 148.075  1.00 75.59           C  
ANISOU 3353  CB  TYR A 506     8227  12063   8432   2763  -1338  -1763       C  
ATOM   3354  CG  TYR A 506      52.455 -20.030 149.439  1.00 76.39           C  
ANISOU 3354  CG  TYR A 506     8393  12113   8518   2800  -1460  -1650       C  
ATOM   3355  CD1 TYR A 506      53.150 -19.512 150.541  1.00 76.21           C  
ANISOU 3355  CD1 TYR A 506     8221  12305   8430   2777  -1441  -1664       C  
ATOM   3356  CD2 TYR A 506      51.694 -21.196 149.616  1.00 76.14           C  
ANISOU 3356  CD2 TYR A 506     8574  11824   8533   2864  -1608  -1528       C  
ATOM   3357  CE1 TYR A 506      53.066 -20.113 151.798  1.00 78.76           C  
ANISOU 3357  CE1 TYR A 506     8603  12601   8722   2821  -1555  -1556       C  
ATOM   3358  CE2 TYR A 506      51.599 -21.811 150.871  1.00 78.31           C  
ANISOU 3358  CE2 TYR A 506     8907  12061   8785   2896  -1723  -1404       C  
ATOM   3359  CZ  TYR A 506      52.292 -21.264 151.961  1.00 80.17           C  
ANISOU 3359  CZ  TYR A 506     8989  12528   8942   2880  -1691  -1420       C  
ATOM   3360  OH  TYR A 506      52.211 -21.848 153.220  1.00 81.84           O  
ANISOU 3360  OH  TYR A 506     9258  12725   9115   2914  -1803  -1292       O  
ATOM   3361  N   ALA A 507      52.979 -18.754 145.251  1.00 77.03           N  
ANISOU 3361  N   ALA A 507     8333  12327   8608   2798  -1162  -1966       N  
ATOM   3362  CA  ALA A 507      52.709 -18.397 143.857  1.00 77.87           C  
ANISOU 3362  CA  ALA A 507     8457  12410   8721   2761  -1073  -2020       C  
ATOM   3363  C   ALA A 507      54.014 -18.477 143.108  1.00 80.09           C  
ANISOU 3363  C   ALA A 507     8582  12934   8914   2944  -1035  -2164       C  
ATOM   3364  O   ALA A 507      54.968 -19.075 143.614  1.00 82.46           O  
ANISOU 3364  O   ALA A 507     8808  13359   9165   3133  -1112  -2218       O  
ATOM   3365  CB  ALA A 507      52.162 -16.974 143.793  1.00 76.21           C  
ANISOU 3365  CB  ALA A 507     8169  12244   8545   2484   -918  -1977       C  
ATOM   3366  N   GLY A 508      54.105 -17.866 141.926  1.00 80.63           N  
ANISOU 3366  N   GLY A 508     8587  13095   8955   2895   -915  -2222       N  
ATOM   3367  CA  GLY A 508      55.452 -17.602 141.351  1.00 83.13           C  
ANISOU 3367  CA  GLY A 508     8681  13731   9174   3014   -833  -2340       C  
ATOM   3368  C   GLY A 508      56.382 -16.788 142.286  1.00 83.15           C  
ANISOU 3368  C   GLY A 508     8442  13996   9156   2919   -773  -2343       C  
ATOM   3369  O   GLY A 508      55.995 -16.396 143.375  1.00 82.38           O  
ANISOU 3369  O   GLY A 508     8358  13833   9111   2769   -793  -2268       O  
ATOM   3370  N   GLU A 509      57.618 -16.552 141.872  1.00 84.84           N  
ANISOU 3370  N   GLU A 509     8430  14518   9288   3010   -706  -2432       N  
ATOM   3371  CA  GLU A 509      58.355 -15.364 142.328  1.00 85.12           C  
ANISOU 3371  CA  GLU A 509     8217  14810   9315   2822   -604  -2426       C  
ATOM   3372  C   GLU A 509      58.056 -14.263 141.290  1.00 84.17           C  
ANISOU 3372  C   GLU A 509     8045  14735   9203   2609   -449  -2402       C  
ATOM   3373  O   GLU A 509      58.012 -13.074 141.623  1.00 83.80           O  
ANISOU 3373  O   GLU A 509     7899  14743   9197   2353   -370  -2354       O  
ATOM   3374  CB  GLU A 509      59.873 -15.620 142.476  1.00 87.15           C  
ANISOU 3374  CB  GLU A 509     8227  15402   9485   3005   -614  -2514       C  
ATOM   3375  N   GLU A 510      57.846 -14.682 140.037  1.00 84.05           N  
ANISOU 3375  N   GLU A 510     8107  14686   9142   2723   -417  -2438       N  
ATOM   3376  CA  GLU A 510      57.368 -13.800 138.975  1.00 82.89           C  
ANISOU 3376  CA  GLU A 510     7963  14533   8998   2541   -288  -2401       C  
ATOM   3377  C   GLU A 510      55.999 -13.212 139.391  1.00 79.65           C  
ANISOU 3377  C   GLU A 510     7731  13828   8703   2300   -293  -2297       C  
ATOM   3378  O   GLU A 510      55.850 -11.989 139.488  1.00 78.48           O  
ANISOU 3378  O   GLU A 510     7504  13716   8600   2048   -202  -2241       O  
ATOM   3379  CB  GLU A 510      57.297 -14.541 137.627  1.00 83.95           C  
ANISOU 3379  CB  GLU A 510     8187  14660   9049   2744   -281  -2466       C  
ATOM   3380  CG  GLU A 510      57.084 -13.629 136.403  1.00 85.29           C  
ANISOU 3380  CG  GLU A 510     8312  14909   9185   2585   -135  -2433       C  
ATOM   3381  CD  GLU A 510      56.908 -14.401 135.088  1.00 89.33           C  
ANISOU 3381  CD  GLU A 510     8941  15398   9602   2794   -141  -2504       C  
ATOM   3382  OE1 GLU A 510      57.616 -15.408 134.865  1.00 93.41           O  
ANISOU 3382  OE1 GLU A 510     9437  16028  10027   3092   -200  -2613       O  
ATOM   3383  OE2 GLU A 510      56.078 -13.992 134.250  1.00 89.21           O  
ANISOU 3383  OE2 GLU A 510     9039  15260   9596   2673    -90  -2457       O  
ATOM   3384  N   ALA A 511      55.028 -14.081 139.669  1.00 77.50           N  
ANISOU 3384  N   ALA A 511     7693  13273   8481   2381   -406  -2269       N  
ATOM   3385  CA  ALA A 511      53.750 -13.645 140.263  1.00 74.94           C  
ANISOU 3385  CA  ALA A 511     7519  12692   8261   2180   -421  -2166       C  
ATOM   3386  C   ALA A 511      53.911 -12.653 141.437  1.00 73.50           C  
ANISOU 3386  C   ALA A 511     7221  12584   8122   1986   -387  -2126       C  
ATOM   3387  O   ALA A 511      53.181 -11.664 141.518  1.00 71.04           O  
ANISOU 3387  O   ALA A 511     6938  12181   7872   1766   -323  -2064       O  
ATOM   3388  CB  ALA A 511      52.914 -14.855 140.709  1.00 74.71           C  
ANISOU 3388  CB  ALA A 511     7715  12396   8274   2306   -570  -2129       C  
ATOM   3389  N   ALA A 512      54.887 -12.902 142.316  1.00 73.74           N  
ANISOU 3389  N   ALA A 512     7121  12783   8113   2077   -436  -2170       N  
ATOM   3390  CA  ALA A 512      54.997 -12.116 143.531  1.00 72.90           C  
ANISOU 3390  CA  ALA A 512     6934  12727   8039   1920   -435  -2143       C  
ATOM   3391  C   ALA A 512      55.524 -10.732 143.233  1.00 72.75           C  
ANISOU 3391  C   ALA A 512     6734  12881   8025   1710   -319  -2156       C  
ATOM   3392  O   ALA A 512      55.435  -9.849 144.062  1.00 72.08           O  
ANISOU 3392  O   ALA A 512     6609  12800   7979   1537   -309  -2137       O  
ATOM   3393  CB  ALA A 512      55.844 -12.821 144.587  1.00 74.14           C  
ANISOU 3393  CB  ALA A 512     7015  13005   8150   2079   -539  -2181       C  
ATOM   3394  N   GLU A 513      56.043 -10.536 142.034  1.00 73.49           N  
ANISOU 3394  N   GLU A 513     6730  13116   8077   1723   -235  -2184       N  
ATOM   3395  CA  GLU A 513      56.474  -9.211 141.626  1.00 74.29           C  
ANISOU 3395  CA  GLU A 513     6671  13365   8190   1500   -126  -2169       C  
ATOM   3396  C   GLU A 513      55.302  -8.249 141.500  1.00 72.21           C  
ANISOU 3396  C   GLU A 513     6543  12880   8015   1272    -78  -2096       C  
ATOM   3397  O   GLU A 513      55.509  -7.037 141.484  1.00 72.88           O  
ANISOU 3397  O   GLU A 513     6530  13027   8135   1055    -17  -2074       O  
ATOM   3398  CB  GLU A 513      57.215  -9.265 140.289  1.00 75.95           C  
ANISOU 3398  CB  GLU A 513     6751  13784   8322   1568    -39  -2195       C  
ATOM   3399  CG  GLU A 513      58.643  -9.792 140.370  1.00 80.83           C  
ANISOU 3399  CG  GLU A 513     7148  14714   8848   1746    -54  -2269       C  
ATOM   3400  CD  GLU A 513      59.163 -10.275 139.009  1.00 87.23           C  
ANISOU 3400  CD  GLU A 513     7886  15702   9554   1912     17  -2308       C  
ATOM   3401  OE1 GLU A 513      58.426 -10.164 137.988  1.00 87.61           O  
ANISOU 3401  OE1 GLU A 513     8061  15629   9599   1876     75  -2276       O  
ATOM   3402  OE2 GLU A 513      60.314 -10.776 138.960  1.00 91.14           O  
ANISOU 3402  OE2 GLU A 513     8196  16471   9963   2092     12  -2374       O  
ATOM   3403  N   SER A 514      54.078  -8.779 141.404  1.00 69.84           N  
ANISOU 3403  N   SER A 514     6463  12321   7753   1318   -114  -2055       N  
ATOM   3404  CA  SER A 514      52.918  -7.959 141.106  1.00 67.43           C  
ANISOU 3404  CA  SER A 514     6283  11812   7524   1135    -66  -1985       C  
ATOM   3405  C   SER A 514      51.933  -7.856 142.284  1.00 66.31           C  
ANISOU 3405  C   SER A 514     6271  11474   7448   1075   -123  -1945       C  
ATOM   3406  O   SER A 514      51.007  -7.025 142.271  1.00 65.92           O  
ANISOU 3406  O   SER A 514     6304  11275   7466    917    -86  -1894       O  
ATOM   3407  CB  SER A 514      52.220  -8.501 139.854  1.00 67.04           C  
ANISOU 3407  CB  SER A 514     6367  11641   7462   1211    -47  -1959       C  
ATOM   3408  OG  SER A 514      52.949  -8.221 138.667  1.00 66.52           O  
ANISOU 3408  OG  SER A 514     6185  11759   7332   1210     38  -1979       O  
ATOM   3409  N   TRP A 515      52.130  -8.708 143.283  1.00 65.74           N  
ANISOU 3409  N   TRP A 515     6216  11413   7351   1210   -214  -1964       N  
ATOM   3410  CA  TRP A 515      51.359  -8.711 144.519  1.00 64.70           C  
ANISOU 3410  CA  TRP A 515     6180  11151   7252   1177   -269  -1924       C  
ATOM   3411  C   TRP A 515      51.018  -7.330 145.134  1.00 64.21           C  
ANISOU 3411  C   TRP A 515     6095  11064   7237    968   -223  -1919       C  
ATOM   3412  O   TRP A 515      49.873  -7.007 145.252  1.00 63.51           O  
ANISOU 3412  O   TRP A 515     6128  10802   7199    893   -207  -1864       O  
ATOM   3413  CB  TRP A 515      52.054  -9.614 145.544  1.00 65.69           C  
ANISOU 3413  CB  TRP A 515     6263  11375   7320   1336   -367  -1955       C  
ATOM   3414  CG  TRP A 515      51.272  -9.910 146.803  1.00 63.89           C  
ANISOU 3414  CG  TRP A 515     6145  11029   7100   1342   -433  -1898       C  
ATOM   3415  CD1 TRP A 515      50.313 -10.865 146.968  1.00 61.37           C  
ANISOU 3415  CD1 TRP A 515     5989  10529   6798   1425   -495  -1815       C  
ATOM   3416  CD2 TRP A 515      51.429  -9.274 148.081  1.00 63.34           C  
ANISOU 3416  CD2 TRP A 515     6021  11033   7011   1265   -450  -1915       C  
ATOM   3417  NE1 TRP A 515      49.864 -10.867 148.270  1.00 61.12           N  
ANISOU 3417  NE1 TRP A 515     5999  10472   6752   1403   -537  -1767       N  
ATOM   3418  CE2 TRP A 515      50.527  -9.897 148.971  1.00 61.99           C  
ANISOU 3418  CE2 TRP A 515     5983  10738   6834   1315   -509  -1836       C  
ATOM   3419  CE3 TRP A 515      52.240  -8.226 148.554  1.00 64.19           C  
ANISOU 3419  CE3 TRP A 515     5984  11302   7105   1151   -428  -1990       C  
ATOM   3420  CZ2 TRP A 515      50.398  -9.508 150.306  1.00 64.66           C  
ANISOU 3420  CZ2 TRP A 515     6313  11120   7134   1273   -535  -1833       C  
ATOM   3421  CZ3 TRP A 515      52.124  -7.839 149.884  1.00 65.63           C  
ANISOU 3421  CZ3 TRP A 515     6170  11509   7258   1109   -469  -2002       C  
ATOM   3422  CH2 TRP A 515      51.205  -8.480 150.749  1.00 66.63           C  
ANISOU 3422  CH2 TRP A 515     6431  11523   7361   1178   -516  -1927       C  
ATOM   3423  N   LYS A 516      51.989  -6.524 145.530  1.00 65.83           N  
ANISOU 3423  N   LYS A 516     6146  11439   7428    877   -210  -1980       N  
ATOM   3424  CA  LYS A 516      51.683  -5.241 146.182  1.00 65.53           C  
ANISOU 3424  CA  LYS A 516     6107  11358   7435    692   -191  -1992       C  
ATOM   3425  C   LYS A 516      50.933  -4.326 145.220  1.00 63.73           C  
ANISOU 3425  C   LYS A 516     5944  10991   7279    542   -112  -1948       C  
ATOM   3426  O   LYS A 516      50.026  -3.607 145.628  1.00 62.85           O  
ANISOU 3426  O   LYS A 516     5927  10735   7217    447   -103  -1929       O  
ATOM   3427  CB  LYS A 516      52.946  -4.532 146.746  1.00 67.20           C  
ANISOU 3427  CB  LYS A 516     6137  11773   7624    607   -214  -2068       C  
ATOM   3428  CG  LYS A 516      52.625  -3.203 147.507  1.00 71.84           C  
ANISOU 3428  CG  LYS A 516     6748  12291   8258    423   -221  -2100       C  
ATOM   3429  CD  LYS A 516      53.815  -2.155 147.586  1.00 81.42           C  
ANISOU 3429  CD  LYS A 516     7784  13666   9483    258   -234  -2162       C  
ATOM   3430  CE  LYS A 516      53.331  -0.631 147.791  1.00 83.32           C  
ANISOU 3430  CE  LYS A 516     8087  13767   9805     40   -231  -2182       C  
ATOM   3431  NZ  LYS A 516      52.720  -0.181 149.139  1.00 82.04           N  
ANISOU 3431  NZ  LYS A 516     8031  13506   9635     33   -294  -2241       N  
ATOM   3432  N   GLU A 517      51.300  -4.350 143.943  1.00 63.26           N  
ANISOU 3432  N   GLU A 517     5834  10986   7216    532    -56  -1931       N  
ATOM   3433  CA  GLU A 517      50.582  -3.531 142.960  1.00 62.10           C  
ANISOU 3433  CA  GLU A 517     5755  10709   7130    396     14  -1876       C  
ATOM   3434  C   GLU A 517      49.091  -3.910 142.910  1.00 59.40           C  
ANISOU 3434  C   GLU A 517     5604  10136   6828    442      7  -1813       C  
ATOM   3435  O   GLU A 517      48.241  -3.036 142.922  1.00 57.81           O  
ANISOU 3435  O   GLU A 517     5480   9792   6691    324     32  -1782       O  
ATOM   3436  CB  GLU A 517      51.197  -3.645 141.570  1.00 62.83           C  
ANISOU 3436  CB  GLU A 517     5767  10918   7188    402     76  -1859       C  
ATOM   3437  CG  GLU A 517      50.517  -2.762 140.545  1.00 64.80           C  
ANISOU 3437  CG  GLU A 517     6083  11047   7492    256    143  -1792       C  
ATOM   3438  CD  GLU A 517      51.223  -2.691 139.200  1.00 71.07           C  
ANISOU 3438  CD  GLU A 517     6778  11993   8234    235    215  -1767       C  
ATOM   3439  OE1 GLU A 517      50.774  -1.851 138.385  1.00 72.60           O  
ANISOU 3439  OE1 GLU A 517     7012  12104   8467     95    268  -1702       O  
ATOM   3440  OE2 GLU A 517      52.206  -3.449 138.946  1.00 73.96           O  
ANISOU 3440  OE2 GLU A 517     7022  12565   8514    365    219  -1809       O  
ATOM   3441  N   ILE A 518      48.799  -5.209 142.853  1.00 57.66           N  
ANISOU 3441  N   ILE A 518     5454   9880   6573    613    -36  -1794       N  
ATOM   3442  CA  ILE A 518      47.432  -5.660 142.763  1.00 55.81           C  
ANISOU 3442  CA  ILE A 518     5384   9441   6379    647    -54  -1721       C  
ATOM   3443  C   ILE A 518      46.631  -5.348 144.040  1.00 56.10           C  
ANISOU 3443  C   ILE A 518     5481   9390   6445    611    -80  -1700       C  
ATOM   3444  O   ILE A 518      45.449  -4.909 143.938  1.00 55.96           O  
ANISOU 3444  O   ILE A 518     5561   9218   6485    545    -55  -1641       O  
ATOM   3445  CB  ILE A 518      47.333  -7.141 142.383  1.00 55.68           C  
ANISOU 3445  CB  ILE A 518     5439   9392   6327    826   -115  -1702       C  
ATOM   3446  CG1 ILE A 518      47.826  -7.355 140.940  1.00 56.73           C  
ANISOU 3446  CG1 ILE A 518     5544   9586   6424    867    -79  -1723       C  
ATOM   3447  CG2 ILE A 518      45.916  -7.624 142.426  1.00 52.23           C  
ANISOU 3447  CG2 ILE A 518     5159   8746   5938    839   -150  -1614       C  
ATOM   3448  CD1 ILE A 518      48.010  -8.796 140.559  1.00 55.28           C  
ANISOU 3448  CD1 ILE A 518     5418   9394   6191   1068   -152  -1741       C  
ATOM   3449  N   VAL A 519      47.216  -5.537 145.232  1.00 55.46           N  
ANISOU 3449  N   VAL A 519     5341   9414   6318    658   -126  -1745       N  
ATOM   3450  CA  VAL A 519      46.407  -5.261 146.401  1.00 54.01           C  
ANISOU 3450  CA  VAL A 519     5218   9164   6140    637   -143  -1724       C  
ATOM   3451  C   VAL A 519      46.129  -3.782 146.484  1.00 53.11           C  
ANISOU 3451  C   VAL A 519     5098   9007   6075    484    -92  -1758       C  
ATOM   3452  O   VAL A 519      45.007  -3.375 146.783  1.00 52.47           O  
ANISOU 3452  O   VAL A 519     5104   8805   6028    453    -73  -1718       O  
ATOM   3453  CB  VAL A 519      46.798  -6.034 147.740  1.00 55.18           C  
ANISOU 3453  CB  VAL A 519     5344   9409   6213    750   -218  -1736       C  
ATOM   3454  CG1 VAL A 519      48.056  -6.780 147.627  1.00 55.31           C  
ANISOU 3454  CG1 VAL A 519     5266   9572   6176    851   -264  -1785       C  
ATOM   3455  CG2 VAL A 519      46.742  -5.179 148.988  1.00 54.62           C  
ANISOU 3455  CG2 VAL A 519     5251   9386   6115    690   -221  -1785       C  
ATOM   3456  N   ASN A 520      47.094  -2.977 146.090  1.00 52.80           N  
ANISOU 3456  N   ASN A 520     4959   9058   6045    386    -71  -1822       N  
ATOM   3457  CA  ASN A 520      46.855  -1.550 146.079  1.00 52.98           C  
ANISOU 3457  CA  ASN A 520     4993   9011   6128    231    -41  -1851       C  
ATOM   3458  C   ASN A 520      45.810  -1.094 145.094  1.00 51.89           C  
ANISOU 3458  C   ASN A 520     4951   8703   6062    169     12  -1780       C  
ATOM   3459  O   ASN A 520      45.034  -0.151 145.389  1.00 52.29           O  
ANISOU 3459  O   ASN A 520     5070   8635   6163     99     24  -1784       O  
ATOM   3460  CB  ASN A 520      48.128  -0.741 145.967  1.00 53.99           C  
ANISOU 3460  CB  ASN A 520     4990   9267   6258    113    -46  -1921       C  
ATOM   3461  CG  ASN A 520      48.976  -0.861 147.216  1.00 57.45           C  
ANISOU 3461  CG  ASN A 520     5343   9851   6633    150   -113  -2004       C  
ATOM   3462  OD1 ASN A 520      50.185  -1.071 147.138  1.00 61.03           O  
ANISOU 3462  OD1 ASN A 520     5660  10477   7052    149   -134  -2040       O  
ATOM   3463  ND2 ASN A 520      48.334  -0.769 148.386  1.00 59.07           N  
ANISOU 3463  ND2 ASN A 520     5624  10005   6815    193   -148  -2031       N  
ATOM   3464  N   LEU A 521      45.772  -1.773 143.952  1.00 50.44           N  
ANISOU 3464  N   LEU A 521     4778   8509   5878    210     36  -1722       N  
ATOM   3465  CA  LEU A 521      44.795  -1.480 142.926  1.00 48.47           C  
ANISOU 3465  CA  LEU A 521     4619   8109   5687    163     77  -1648       C  
ATOM   3466  C   LEU A 521      43.371  -1.901 143.366  1.00 47.15           C  
ANISOU 3466  C   LEU A 521     4570   7801   5545    231     63  -1585       C  
ATOM   3467  O   LEU A 521      42.428  -1.117 143.228  1.00 46.25           O  
ANISOU 3467  O   LEU A 521     4523   7560   5491    167     87  -1552       O  
ATOM   3468  CB  LEU A 521      45.189  -2.095 141.576  1.00 48.61           C  
ANISOU 3468  CB  LEU A 521     4618   8171   5680    196    100  -1614       C  
ATOM   3469  CG  LEU A 521      46.304  -1.409 140.780  1.00 47.78           C  
ANISOU 3469  CG  LEU A 521     4400   8192   5561     92    143  -1637       C  
ATOM   3470  CD1 LEU A 521      46.847  -2.340 139.673  1.00 44.15           C  
ANISOU 3470  CD1 LEU A 521     3903   7837   5034    188    161  -1624       C  
ATOM   3471  CD2 LEU A 521      45.868  -0.046 140.214  1.00 42.10           C  
ANISOU 3471  CD2 LEU A 521     3716   7362   4916    -79    183  -1597       C  
ATOM   3472  N   LEU A 522      43.236  -3.115 143.897  1.00 45.67           N  
ANISOU 3472  N   LEU A 522     4400   7641   5311    356     18  -1560       N  
ATOM   3473  CA  LEU A 522      42.002  -3.541 144.520  1.00 44.58           C  
ANISOU 3473  CA  LEU A 522     4344   7407   5186    408      1  -1488       C  
ATOM   3474  C   LEU A 522      41.432  -2.539 145.568  1.00 45.25           C  
ANISOU 3474  C   LEU A 522     4439   7472   5282    364     22  -1516       C  
ATOM   3475  O   LEU A 522      40.252  -2.195 145.525  1.00 44.11           O  
ANISOU 3475  O   LEU A 522     4356   7220   5182    349     45  -1458       O  
ATOM   3476  CB  LEU A 522      42.218  -4.891 145.144  1.00 44.58           C  
ANISOU 3476  CB  LEU A 522     4346   7464   5128    531    -62  -1462       C  
ATOM   3477  CG  LEU A 522      42.339  -6.046 144.149  1.00 47.13           C  
ANISOU 3477  CG  LEU A 522     4708   7751   5448    607   -102  -1421       C  
ATOM   3478  CD1 LEU A 522      43.144  -7.172 144.748  1.00 44.17           C  
ANISOU 3478  CD1 LEU A 522     4306   7469   5008    731   -173  -1442       C  
ATOM   3479  CD2 LEU A 522      40.920  -6.560 143.715  1.00 47.64           C  
ANISOU 3479  CD2 LEU A 522     4882   7652   5568    610   -123  -1304       C  
ATOM   3480  N   TYR A 523      42.280  -2.046 146.482  1.00 45.77           N  
ANISOU 3480  N   TYR A 523     4441   7646   5304    350      8  -1611       N  
ATOM   3481  CA  TYR A 523      41.835  -1.137 147.508  1.00 44.93           C  
ANISOU 3481  CA  TYR A 523     4352   7529   5191    330     15  -1662       C  
ATOM   3482  C   TYR A 523      41.395   0.140 146.842  1.00 44.94           C  
ANISOU 3482  C   TYR A 523     4393   7408   5276    225     52  -1679       C  
ATOM   3483  O   TYR A 523      40.357   0.699 147.180  1.00 43.81           O  
ANISOU 3483  O   TYR A 523     4308   7180   5156    236     72  -1667       O  
ATOM   3484  CB  TYR A 523      42.959  -0.847 148.501  1.00 46.77           C  
ANISOU 3484  CB  TYR A 523     4511   7900   5359    327    -25  -1774       C  
ATOM   3485  CG  TYR A 523      43.074  -1.819 149.672  1.00 47.11           C  
ANISOU 3485  CG  TYR A 523     4537   8057   5304    445    -67  -1763       C  
ATOM   3486  CD1 TYR A 523      42.001  -2.025 150.540  1.00 45.38           C  
ANISOU 3486  CD1 TYR A 523     4372   7823   5045    514    -57  -1710       C  
ATOM   3487  CD2 TYR A 523      44.267  -2.512 149.917  1.00 47.68           C  
ANISOU 3487  CD2 TYR A 523     4531   8266   5319    489   -117  -1798       C  
ATOM   3488  CE1 TYR A 523      42.095  -2.897 151.604  1.00 48.34           C  
ANISOU 3488  CE1 TYR A 523     4734   8309   5324    611    -95  -1680       C  
ATOM   3489  CE2 TYR A 523      44.382  -3.400 151.007  1.00 49.94           C  
ANISOU 3489  CE2 TYR A 523     4809   8653   5514    599   -165  -1778       C  
ATOM   3490  CZ  TYR A 523      43.287  -3.582 151.847  1.00 52.43           C  
ANISOU 3490  CZ  TYR A 523     5189   8944   5789    653   -154  -1713       C  
ATOM   3491  OH  TYR A 523      43.353  -4.465 152.917  1.00 54.87           O  
ANISOU 3491  OH  TYR A 523     5494   9356   6001    753   -201  -1670       O  
ATOM   3492  N   GLU A 524      42.171   0.594 145.865  1.00 45.31           N  
ANISOU 3492  N   GLU A 524     4405   7450   5363    128     60  -1699       N  
ATOM   3493  CA  GLU A 524      41.777   1.772 145.084  1.00 45.96           C  
ANISOU 3493  CA  GLU A 524     4533   7400   5529     18     87  -1692       C  
ATOM   3494  C   GLU A 524      40.418   1.590 144.384  1.00 44.29           C  
ANISOU 3494  C   GLU A 524     4407   7054   5369     49    118  -1588       C  
ATOM   3495  O   GLU A 524      39.632   2.565 144.311  1.00 43.94           O  
ANISOU 3495  O   GLU A 524     4423   6888   5384     12    131  -1587       O  
ATOM   3496  CB  GLU A 524      42.844   2.140 144.069  1.00 46.58           C  
ANISOU 3496  CB  GLU A 524     4548   7519   5630    -96     96  -1699       C  
ATOM   3497  CG  GLU A 524      42.914   3.625 143.714  1.00 52.16           C  
ANISOU 3497  CG  GLU A 524     5281   8123   6415   -245     95  -1724       C  
ATOM   3498  CD  GLU A 524      44.146   3.953 142.803  1.00 62.38           C  
ANISOU 3498  CD  GLU A 524     6483   9503   7717   -377    104  -1714       C  
ATOM   3499  OE1 GLU A 524      44.060   4.943 142.010  1.00 63.23           O  
ANISOU 3499  OE1 GLU A 524     6622   9508   7894   -508    114  -1674       O  
ATOM   3500  OE2 GLU A 524      45.182   3.206 142.866  1.00 62.69           O  
ANISOU 3500  OE2 GLU A 524     6412   9719   7690   -346    101  -1736       O  
ATOM   3501  N   LEU A 525      40.147   0.365 143.886  1.00 42.67           N  
ANISOU 3501  N   LEU A 525     4207   6865   5141    121    118  -1506       N  
ATOM   3502  CA  LEU A 525      38.879   0.068 143.194  1.00 41.68           C  
ANISOU 3502  CA  LEU A 525     4155   6621   5063    144    130  -1401       C  
ATOM   3503  C   LEU A 525      37.776   0.119 144.229  1.00 41.81           C  
ANISOU 3503  C   LEU A 525     4199   6610   5077    209    133  -1378       C  
ATOM   3504  O   LEU A 525      36.812   0.814 144.030  1.00 42.66           O  
ANISOU 3504  O   LEU A 525     4350   6618   5239    193    155  -1347       O  
ATOM   3505  CB  LEU A 525      38.825  -1.312 142.533  1.00 39.98           C  
ANISOU 3505  CB  LEU A 525     3951   6418   4823    208    106  -1328       C  
ATOM   3506  CG  LEU A 525      38.020  -1.522 141.233  1.00 38.25           C  
ANISOU 3506  CG  LEU A 525     3796   6085   4652    190    106  -1238       C  
ATOM   3507  CD1 LEU A 525      37.479  -2.930 141.137  1.00 36.25           C  
ANISOU 3507  CD1 LEU A 525     3580   5810   4383    273     55  -1160       C  
ATOM   3508  CD2 LEU A 525      36.923  -0.524 140.956  1.00 35.31           C  
ANISOU 3508  CD2 LEU A 525     3471   5591   4353    137    133  -1194       C  
ATOM   3509  N   LEU A 526      37.943  -0.630 145.314  1.00 41.36           N  
ANISOU 3509  N   LEU A 526     4111   6654   4949    287    113  -1387       N  
ATOM   3510  CA  LEU A 526      37.052  -0.629 146.428  1.00 41.46           C  
ANISOU 3510  CA  LEU A 526     4131   6692   4931    354    123  -1364       C  
ATOM   3511  C   LEU A 526      36.603   0.788 146.777  1.00 42.53           C  
ANISOU 3511  C   LEU A 526     4290   6773   5096    332    152  -1437       C  
ATOM   3512  O   LEU A 526      35.393   1.095 146.778  1.00 43.90           O  
ANISOU 3512  O   LEU A 526     4493   6884   5303    364    180  -1381       O  
ATOM   3513  CB  LEU A 526      37.738  -1.269 147.617  1.00 41.39           C  
ANISOU 3513  CB  LEU A 526     4078   6825   4825    419     94  -1403       C  
ATOM   3514  CG  LEU A 526      36.825  -1.571 148.800  1.00 44.20           C  
ANISOU 3514  CG  LEU A 526     4432   7244   5120    502    106  -1349       C  
ATOM   3515  CD1 LEU A 526      35.677  -2.500 148.369  1.00 42.85           C  
ANISOU 3515  CD1 LEU A 526     4282   7015   4983    521    105  -1184       C  
ATOM   3516  CD2 LEU A 526      37.586  -2.164 149.971  1.00 41.69           C  
ANISOU 3516  CD2 LEU A 526     4074   7073   4694    563     71  -1385       C  
ATOM   3517  N   ALA A 527      37.548   1.667 147.031  1.00 42.32           N  
ANISOU 3517  N   ALA A 527     4251   6764   5063    280    139  -1561       N  
ATOM   3518  CA  ALA A 527      37.185   3.003 147.367  1.00 43.49           C  
ANISOU 3518  CA  ALA A 527     4442   6839   5244    264    145  -1643       C  
ATOM   3519  C   ALA A 527      36.365   3.645 146.260  1.00 43.96           C  
ANISOU 3519  C   ALA A 527     4557   6739   5405    217    166  -1582       C  
ATOM   3520  O   ALA A 527      35.480   4.455 146.548  1.00 45.59           O  
ANISOU 3520  O   ALA A 527     4808   6873   5640    259    178  -1604       O  
ATOM   3521  CB  ALA A 527      38.399   3.841 147.718  1.00 43.35           C  
ANISOU 3521  CB  ALA A 527     4409   6844   5218    188    104  -1781       C  
ATOM   3522  N   SER A 528      36.625   3.296 145.010  1.00 43.25           N  
ANISOU 3522  N   SER A 528     4467   6604   5362    145    168  -1509       N  
ATOM   3523  CA  SER A 528      36.003   4.032 143.906  1.00 43.89           C  
ANISOU 3523  CA  SER A 528     4605   6536   5535     86    178  -1457       C  
ATOM   3524  C   SER A 528      34.618   3.546 143.673  1.00 44.10           C  
ANISOU 3524  C   SER A 528     4653   6520   5584    159    197  -1346       C  
ATOM   3525  O   SER A 528      33.796   4.275 143.098  1.00 43.92           O  
ANISOU 3525  O   SER A 528     4678   6378   5631    148    204  -1310       O  
ATOM   3526  CB  SER A 528      36.807   3.938 142.598  1.00 43.50           C  
ANISOU 3526  CB  SER A 528     4547   6468   5512    -20    175  -1418       C  
ATOM   3527  OG  SER A 528      38.023   4.671 142.724  1.00 45.53           O  
ANISOU 3527  OG  SER A 528     4776   6756   5768   -116    157  -1509       O  
ATOM   3528  N   LEU A 529      34.353   2.314 144.115  1.00 45.09           N  
ANISOU 3528  N   LEU A 529     4740   6739   5653    229    198  -1284       N  
ATOM   3529  CA  LEU A 529      33.011   1.756 144.030  1.00 46.20           C  
ANISOU 3529  CA  LEU A 529     4882   6857   5813    288    208  -1164       C  
ATOM   3530  C   LEU A 529      32.054   2.353 145.077  1.00 47.93           C  
ANISOU 3530  C   LEU A 529     5091   7105   6017    375    239  -1183       C  
ATOM   3531  O   LEU A 529      30.851   2.282 144.859  1.00 48.07           O  
ANISOU 3531  O   LEU A 529     5102   7091   6071    412    253  -1087       O  
ATOM   3532  CB  LEU A 529      33.044   0.244 144.158  1.00 46.23           C  
ANISOU 3532  CB  LEU A 529     4858   6938   5771    319    183  -1079       C  
ATOM   3533  CG  LEU A 529      33.467  -0.539 142.902  1.00 45.77           C  
ANISOU 3533  CG  LEU A 529     4824   6831   5736    269    146  -1027       C  
ATOM   3534  CD1 LEU A 529      33.706  -2.011 143.199  1.00 44.20           C  
ANISOU 3534  CD1 LEU A 529     4611   6697   5486    313    101   -973       C  
ATOM   3535  CD2 LEU A 529      32.404  -0.399 141.846  1.00 46.09           C  
ANISOU 3535  CD2 LEU A 529     4904   6758   5851    241    140   -932       C  
ATOM   3536  N   ILE A 530      32.584   2.946 146.171  1.00 48.86           N  
ANISOU 3536  N   ILE A 530     5201   7289   6076    413    245  -1308       N  
ATOM   3537  CA  ILE A 530      31.784   3.552 147.237  1.00 50.56           C  
ANISOU 3537  CA  ILE A 530     5409   7552   6250    519    275  -1353       C  
ATOM   3538  C   ILE A 530      31.778   5.072 147.207  1.00 51.42           C  
ANISOU 3538  C   ILE A 530     5582   7546   6409    520    266  -1477       C  
ATOM   3539  O   ILE A 530      30.813   5.692 147.591  1.00 50.95           O  
ANISOU 3539  O   ILE A 530     5534   7472   6353    615    289  -1494       O  
ATOM   3540  CB  ILE A 530      32.294   3.239 148.649  1.00 51.63           C  
ANISOU 3540  CB  ILE A 530     5507   7848   6263    587    278  -1427       C  
ATOM   3541  CG1 ILE A 530      32.701   1.795 148.823  1.00 52.97           C  
ANISOU 3541  CG1 ILE A 530     5627   8123   6376    577    264  -1334       C  
ATOM   3542  CG2 ILE A 530      31.182   3.540 149.657  1.00 55.97           C  
ANISOU 3542  CG2 ILE A 530     6031   8485   6749    720    325  -1427       C  
ATOM   3543  CD1 ILE A 530      31.652   0.842 148.300  1.00 55.88           C  
ANISOU 3543  CD1 ILE A 530     5972   8481   6780    581    275  -1153       C  
ATOM   3544  N   ARG A 531      32.885   5.683 146.812  1.00 52.74           N  
ANISOU 3544  N   ARG A 531     5789   7637   6611    418    226  -1567       N  
ATOM   3545  CA  ARG A 531      32.968   7.146 146.805  1.00 54.81           C  
ANISOU 3545  CA  ARG A 531     6128   7765   6931    401    194  -1684       C  
ATOM   3546  C   ARG A 531      31.672   7.717 146.314  1.00 55.46           C  
ANISOU 3546  C   ARG A 531     6251   7737   7085    463    212  -1627       C  
ATOM   3547  O   ARG A 531      31.259   7.413 145.217  1.00 54.97           O  
ANISOU 3547  O   ARG A 531     6189   7610   7089    412    220  -1505       O  
ATOM   3548  CB  ARG A 531      34.117   7.641 145.913  1.00 55.17           C  
ANISOU 3548  CB  ARG A 531     6205   7713   7044    237    150  -1710       C  
ATOM   3549  CG  ARG A 531      34.409   9.163 145.982  1.00 56.10           C  
ANISOU 3549  CG  ARG A 531     6412   7677   7228    187     92  -1831       C  
ATOM   3550  CD  ARG A 531      35.904   9.489 145.826  1.00 56.81           C  
ANISOU 3550  CD  ARG A 531     6492   7763   7330     29     39  -1896       C  
ATOM   3551  NE  ARG A 531      36.649   8.437 145.123  1.00 60.42           N  
ANISOU 3551  NE  ARG A 531     6865   8329   7762    -52     68  -1801       N  
ATOM   3552  CZ  ARG A 531      37.766   7.862 145.573  1.00 61.33           C  
ANISOU 3552  CZ  ARG A 531     6905   8588   7810    -89     57  -1846       C  
ATOM   3553  NH1 ARG A 531      38.309   8.244 146.707  1.00 63.72           N  
ANISOU 3553  NH1 ARG A 531     7203   8943   8064    -71     12  -1979       N  
ATOM   3554  NH2 ARG A 531      38.362   6.920 144.874  1.00 62.25           N  
ANISOU 3554  NH2 ARG A 531     6951   8798   7904   -135     82  -1765       N  
ATOM   3555  N   GLY A 532      31.027   8.532 147.138  1.00 57.81           N  
ANISOU 3555  N   GLY A 532     6581   8021   7362    587    213  -1720       N  
ATOM   3556  CA  GLY A 532      29.879   9.306 146.697  1.00 59.03           C  
ANISOU 3556  CA  GLY A 532     6780   8056   7592    661    217  -1693       C  
ATOM   3557  C   GLY A 532      28.615   8.510 146.838  1.00 59.69           C  
ANISOU 3557  C   GLY A 532     6778   8261   7642    772    281  -1565       C  
ATOM   3558  O   GLY A 532      27.584   8.907 146.276  1.00 61.49           O  
ANISOU 3558  O   GLY A 532     7015   8411   7939    826    289  -1501       O  
TER    3559      GLY A 532                                                      
HETATM 3560  O   HOH A2001      25.357   3.028 107.080  1.00 45.05           O  
HETATM 3561  O   HOH A2002      23.971  -6.611 116.421  1.00 43.37           O  
HETATM 3562  O   HOH A2003      37.021 -16.889 103.887  1.00 43.62           O  
HETATM 3563  O   HOH A2004      42.310 -22.054 105.224  1.00 60.19           O  
HETATM 3564  O   HOH A2005      34.766  -9.350 113.939  1.00 26.10           O  
HETATM 3565  O   HOH A2006      34.141  -5.678 129.014  1.00 27.40           O  
HETATM 3566  O   HOH A2007      36.716 -11.850 126.338  1.00 37.07           O  
HETATM 3567  O   HOH A2008      36.980  -6.731 131.407  1.00 48.68           O  
HETATM 3568  O   HOH A2009      40.667  -8.862 124.409  1.00 32.07           O  
HETATM 3569  O   HOH A2010      46.174  -5.434 126.690  1.00 27.80           O  
HETATM 3570  O   HOH A2011      44.947 -13.418 118.611  1.00 39.33           O  
HETATM 3571  O   HOH A2012      32.443 -19.704 119.495  1.00 28.12           O  
HETATM 3572  O   HOH A2013      32.251 -24.653 119.563  1.00 35.60           O  
HETATM 3573  O   HOH A2014      27.882 -11.733 123.277  1.00 33.94           O  
HETATM 3574  O   HOH A2015      31.093   4.771 117.312  1.00 49.61           O  
HETATM 3575  O   HOH A2016       6.630   4.471 113.757  1.00 52.71           O  
HETATM 3576  O   HOH A2017      31.835  -4.816 120.167  1.00 25.31           O  
HETATM 3577  O   HOH A2018      40.315   0.659 112.887  1.00 37.94           O  
HETATM 3578  O   HOH A2019      52.820 -10.934 116.766  1.00 53.24           O  
HETATM 3579  O   HOH A2020      46.148  -0.262 123.167  1.00 37.85           O  
HETATM 3580  O   HOH A2021      43.621   8.885 113.116  1.00 43.74           O  
HETATM 3581  O   HOH A2022      14.397 -25.304 117.725  1.00 38.05           O  
HETATM 3582  O   HOH A2023      46.941   0.769 111.070  1.00 47.75           O  
HETATM 3583  O   HOH A2024      -4.539 -12.854 121.520  1.00 20.27           O  
HETATM 3584  O   HOH A2025      33.092  -4.654  90.585  1.00 39.00           O  
HETATM 3585  O   HOH A2026      30.861  -9.399 103.179  1.00 46.48           O  
HETATM 3586  O   HOH A2027      -3.172  -9.977 124.613  1.00 19.69           O  
HETATM 3587  O   HOH A2028      51.194   2.836 104.740  1.00 36.22           O  
HETATM 3588  O   HOH A2029      44.955  -9.060 105.030  1.00 35.72           O  
HETATM 3589  O   HOH A2030      42.797 -16.238 119.063  1.00 27.24           O  
HETATM 3590  O   HOH A2031      47.053  -9.631 118.141  1.00 28.48           O  
HETATM 3591  O   HOH A2032      40.660 -16.442 105.495  1.00 31.79           O  
HETATM 3592  O   HOH A2033      43.167 -16.689 103.416  1.00 32.42           O  
HETATM 3593  O   HOH A2034      20.566  -1.022 112.778  1.00 47.73           O  
HETATM 3594  O   HOH A2035       9.366   4.081 112.574  1.00 37.41           O  
HETATM 3595  O   HOH A2036      11.617   9.930 115.331  1.00 26.67           O  
HETATM 3596  O   HOH A2037      19.867  -0.324 115.917  1.00 54.55           O  
HETATM 3597  O   HOH A2038       2.759  -6.861 129.060  1.00 30.62           O  
HETATM 3598  O   HOH A2039      23.618  -9.174 145.338  1.00 54.30           O  
HETATM 3599  O   HOH A2040      26.137 -15.077 142.561  1.00 44.93           O  
HETATM 3600  O   HOH A2041      18.098 -17.060 138.937  1.00 26.63           O  
HETATM 3601  O   HOH A2042       4.481 -14.470 129.893  1.00 39.50           O  
HETATM 3602  O   HOH A2043      19.856   1.352 135.419  1.00 33.87           O  
HETATM 3603  O   HOH A2044      19.881  -6.797 141.190  1.00 27.20           O  
HETATM 3604  O   HOH A2045      13.774  -7.872 131.388  1.00 24.30           O  
HETATM 3605  O   HOH A2046      22.102  -9.210 132.299  1.00 29.59           O  
HETATM 3606  O   HOH A2047      26.063  -7.735 125.160  1.00 32.16           O  
HETATM 3607  O   HOH A2048      25.320 -16.064 119.627  1.00 39.23           O  
HETATM 3608  O   HOH A2049      23.226 -14.285 116.232  1.00 32.55           O  
HETATM 3609  O   HOH A2050      24.411  -9.528 116.585  1.00 39.59           O  
HETATM 3610  O   HOH A2051      20.598  -3.574 114.130  1.00 32.03           O  
HETATM 3611  O   HOH A2052      11.223  -5.901 113.858  1.00 24.16           O  
HETATM 3612  O   HOH A2053      10.637 -13.997 116.864  1.00 24.09           O  
HETATM 3613  O   HOH A2054       3.645  -6.639 112.536  1.00 52.36           O  
HETATM 3614  O   HOH A2055      17.104 -16.420 113.380  1.00 36.37           O  
HETATM 3615  O   HOH A2056      22.164 -17.721 118.550  1.00 34.81           O  
HETATM 3616  O   HOH A2057      18.076 -18.618 124.408  1.00 34.29           O  
HETATM 3617  O   HOH A2058      27.219 -11.452 127.990  1.00 31.00           O  
HETATM 3618  O   HOH A2059      28.425 -12.898 136.587  1.00 38.54           O  
HETATM 3619  O   HOH A2060      23.058 -17.490 135.057  1.00 42.42           O  
HETATM 3620  O   HOH A2061      12.400 -24.242 135.928  1.00 55.51           O  
HETATM 3621  O   HOH A2062      12.724 -20.588 135.570  1.00 32.83           O  
HETATM 3622  O   HOH A2063       9.419 -24.944 133.080  1.00 35.66           O  
HETATM 3623  O   HOH A2064      21.460 -24.175 134.377  1.00 42.76           O  
HETATM 3624  O   HOH A2065      28.144 -19.907 129.469  1.00 60.43           O  
HETATM 3625  O   HOH A2066      30.162 -22.605 128.692  1.00 46.80           O  
HETATM 3626  O   HOH A2067      20.475 -28.738 118.802  1.00 45.95           O  
HETATM 3627  O   HOH A2068      13.775 -24.606 120.358  1.00 29.44           O  
HETATM 3628  O   HOH A2069      15.140 -23.591 115.877  1.00 42.15           O  
HETATM 3629  O   HOH A2070      -2.821 -11.653 120.125  1.00 19.22           O  
HETATM 3630  O   HOH A2071      -4.788 -17.053 120.210  1.00 47.70           O  
HETATM 3631  O   HOH A2072      -3.503 -15.404 122.008  1.00 33.47           O  
HETATM 3632  O   HOH A2073      -5.438 -14.999 116.421  1.00 37.00           O  
HETATM 3633  O   HOH A2074      18.525  -3.828 104.028  1.00 38.72           O  
HETATM 3634  O   HOH A2075      16.221  -6.629 103.338  1.00 45.98           O  
HETATM 3635  O   HOH A2076       5.918  -7.745 107.443  1.00 46.85           O  
HETATM 3636  O   HOH A2077       2.821  -1.601 116.591  1.00 58.14           O  
HETATM 3637  O   HOH A2078       7.336  -4.252 122.535  1.00 30.84           O  
HETATM 3638  O   HOH A2079       2.778  -4.578 116.861  1.00 32.68           O  
HETATM 3639  O   HOH A2080       0.716 -21.501 137.064  1.00 63.95           O  
HETATM 3640  O   HOH A2081       2.240 -27.854 130.245  1.00 39.40           O  
HETATM 3641  O   HOH A2082      -1.919 -11.057 126.834  1.00 35.72           O  
HETATM 3642  O   HOH A2083      -5.616 -17.573 131.640  1.00 24.44           O  
HETATM 3643  O   HOH A2084      -4.839 -13.820 125.694  1.00 21.48           O  
HETATM 3644  O   HOH A2085       4.549 -15.103 126.749  1.00 32.89           O  
HETATM 3645  O   HOH A2086      -0.239  -8.894 128.925  1.00 48.16           O  
HETATM 3646  O   HOH A2087       8.889   0.426 126.063  1.00 21.68           O  
HETATM 3647  O   HOH A2088      20.897  -2.348 122.486  1.00 34.56           O  
HETATM 3648  O   HOH A2089      12.802   1.434 123.906  1.00 18.63           O  
HETATM 3649  O   HOH A2090      19.419   2.622 122.754  1.00 59.19           O  
HETATM 3650  O   HOH A2091      15.909   4.823 124.866  1.00 24.32           O  
HETATM 3651  O   HOH A2092      22.047   5.968 129.399  1.00 31.13           O  
HETATM 3652  O   HOH A2093      28.948   0.340 124.311  1.00 30.65           O  
HETATM 3653  O   HOH A2094      21.607   4.488 123.868  1.00 36.18           O  
HETATM 3654  O   HOH A2095      26.550   6.525 123.337  1.00 60.56           O  
HETATM 3655  O   HOH A2096      23.551   5.825 127.518  1.00 27.08           O  
HETATM 3656  O   HOH A2097      21.966   3.436 130.845  1.00 27.97           O  
HETATM 3657  O   HOH A2098      19.346   2.233 130.073  1.00 29.55           O  
HETATM 3658  O   HOH A2099      35.105 -12.340 128.914  1.00 38.15           O  
HETATM 3659  O   HOH A2100      36.872 -12.074 131.193  1.00 35.95           O  
HETATM 3660  O   HOH A2101      37.193  -5.457 133.639  1.00 36.09           O  
HETATM 3661  O   HOH A2102      49.993 -12.171 132.630  1.00 45.85           O  
HETATM 3662  O   HOH A2103      48.760  -2.704 132.642  1.00 23.85           O  
HETATM 3663  O   HOH A2104      38.833   3.260 132.125  1.00 38.81           O  
HETATM 3664  O   HOH A2105      38.387   6.261 140.470  1.00 34.92           O  
HETATM 3665  O   HOH A2106      29.116   2.021 130.885  1.00 34.44           O  
HETATM 3666  O   HOH A2107      30.376  10.160 135.020  1.00 39.45           O  
HETATM 3667  O   HOH A2108      21.089   1.607 138.965  1.00 62.28           O  
HETATM 3668  O   HOH A2109      33.422   8.274 135.807  1.00 38.75           O  
HETATM 3669  O   HOH A2110      22.840  -4.322 138.633  1.00 27.35           O  
HETATM 3670  O   HOH A2111      28.612  -5.427 145.583  1.00 25.76           O  
HETATM 3671  O   HOH A2112      22.474  -9.212 141.371  1.00 38.75           O  
HETATM 3672  O   HOH A2113      21.764  -6.824 139.075  1.00 26.75           O  
HETATM 3673  O   HOH A2114      34.351 -17.067 148.077  1.00 59.18           O  
HETATM 3674  O   HOH A2115      54.439 -10.429 138.008  1.00 53.05           O  
HETATM 3675  O   HOH A2116      53.289  -6.214 137.080  1.00 44.06           O  
HETATM 3676  O   HOH A2117      49.376  -0.202 142.336  1.00 45.12           O  
HETATM 3677  O   HOH A2118      45.868   2.392 147.425  1.00 47.13           O  
HETATM 3678  O   HOH A2119      41.601   6.392 142.447  1.00 36.35           O  
HETATM 3679  O   HOH A2120      46.105   4.387 139.699  1.00 48.86           O  
HETATM 3680  O   HOH A2121      40.175   5.249 144.487  1.00 30.04           O  
MASTER      560    0    0   12   23    0    0    6 3679    1    0   43          
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.