CNRS Nantes University US2B US2B
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***  LIVA_SerB  ***

elNémo ID: 231202102516493312

Job options:

ID        	=	 231202102516493312
JOBID     	=	 LIVA_SerB
USERID    	=	 lionel-marie.vangeesbergen
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 LIVA_SerB

CRYST1  143.210  143.210  143.210  90.00  90.00  90.00 I 21 3        2
ATOM      1  N   VAL A   9      23.533 -14.692  30.847  1.00110.68           N  
ANISOU    1  N   VAL A   9     9979  10929  21146   -542  -2808   2248       N  
ATOM      2  CA  VAL A   9      22.564 -14.799  31.931  1.00111.13           C  
ANISOU    2  CA  VAL A   9    10813  10882  20531   -582  -3254   1869       C  
ATOM      3  C   VAL A   9      21.755 -16.089  31.766  1.00110.62           C  
ANISOU    3  C   VAL A   9    11172  11051  19808   -308  -2836   1620       C  
ATOM      4  O   VAL A   9      21.800 -16.727  30.713  1.00 98.98           O  
ANISOU    4  O   VAL A   9     9475   9816  18316   -104  -2198   1704       O  
ATOM      5  CB  VAL A   9      21.650 -13.554  31.989  1.00104.32           C  
ANISOU    5  CB  VAL A   9    10363   9977  19299   -796  -3336   1736       C  
ATOM      6  CG1 VAL A   9      20.503 -13.675  31.001  1.00101.39           C  
ANISOU    6  CG1 VAL A   9    10280   9931  18312   -677  -2611   1597       C  
ATOM      7  CG2 VAL A   9      21.139 -13.321  33.409  1.00102.05           C  
ANISOU    7  CG2 VAL A   9    10732   9427  18616   -883  -4035   1458       C  
ATOM      8  N   SER A  10      21.014 -16.463  32.806  1.00 97.53           N  
ANISOU    8  N   SER A  10    10152   9299  17605   -296  -3199   1329       N  
ATOM      9  CA  SER A  10      20.406 -17.785  32.875  1.00 92.35           C  
ANISOU    9  CA  SER A  10     9864   8788  16439    -65  -2948   1131       C  
ATOM     10  C   SER A  10      19.111 -17.863  32.070  1.00 82.20           C  
ANISOU   10  C   SER A  10     8934   7769  14528     -7  -2352    968       C  
ATOM     11  O   SER A  10      18.333 -16.904  31.985  1.00 74.04           O  
ANISOU   11  O   SER A  10     8139   6762  13230   -154  -2308    891       O  
ATOM     12  CB  SER A  10      20.135 -18.173  34.328  1.00 88.62           C  
ANISOU   12  CB  SER A  10     9937   8094  15643    -72  -3549    925       C  
ATOM     13  OG  SER A  10      19.558 -17.096  35.044  1.00102.95           O  
ANISOU   13  OG  SER A  10    12169   9750  17195   -258  -3914    804       O  
ATOM     14  N   LEU A  11      18.892 -19.032  31.481  1.00 72.62           N  
ANISOU   14  N   LEU A  11     7764   6729  13098    217  -1929    917       N  
ATOM     15  CA  LEU A  11      17.706 -19.341  30.702  1.00 72.56           C  
ANISOU   15  CA  LEU A  11     8096   6942  12530    292  -1423    767       C  
ATOM     16  C   LEU A  11      16.767 -20.223  31.508  1.00 69.50           C  
ANISOU   16  C   LEU A  11     8279   6530  11598    342  -1567    529       C  
ATOM     17  O   LEU A  11      17.194 -20.995  32.372  1.00 65.42           O  
ANISOU   17  O   LEU A  11     7850   5871  11135    415  -1901    498       O  
ATOM     18  CB  LEU A  11      18.086 -20.057  29.406  1.00 67.91           C  
ANISOU   18  CB  LEU A  11     7221   6527  12056    521   -856    880       C  
ATOM     19  CG  LEU A  11      19.085 -19.337  28.507  1.00 72.01           C  
ANISOU   19  CG  LEU A  11     7141   7087  13133    526   -589   1173       C  
ATOM     20  CD1 LEU A  11      19.099 -19.977  27.136  1.00 73.54           C  
ANISOU   20  CD1 LEU A  11     7262   7470  13211    793     74   1235       C  
ATOM     21  CD2 LEU A  11      18.665 -17.881  28.394  1.00 72.70           C  
ANISOU   21  CD2 LEU A  11     7239   7169  13213    268   -643   1210       C  
ATOM     22  N   VAL A  12      15.480 -20.105  31.211  1.00 64.16           N  
ANISOU   22  N   VAL A  12     7975   5981  10421    303  -1311    384       N  
ATOM     23  CA  VAL A  12      14.464 -20.970  31.787  1.00 61.53           C  
ANISOU   23  CA  VAL A  12     8137   5651   9592    347  -1334    205       C  
ATOM     24  C   VAL A  12      13.572 -21.467  30.656  1.00 59.38           C  
ANISOU   24  C   VAL A  12     7974   5567   9019    422   -849    147       C  
ATOM     25  O   VAL A  12      13.248 -20.720  29.725  1.00 48.94           O  
ANISOU   25  O   VAL A  12     6544   4367   7682    374   -567    183       O  
ATOM     26  CB  VAL A  12      13.649 -20.243  32.883  1.00 60.08           C  
ANISOU   26  CB  VAL A  12     8363   5369   9097    203  -1621     95       C  
ATOM     27  CG1 VAL A  12      12.972 -18.975  32.332  1.00 52.17           C  
ANISOU   27  CG1 VAL A  12     7356   4462   8003     74  -1432     92       C  
ATOM     28  CG2 VAL A  12      12.637 -21.182  33.525  1.00 56.46           C  
ANISOU   28  CG2 VAL A  12     8377   4907   8169    257  -1599    -33       C  
ATOM     29  N   ALA A  13      13.223 -22.743  30.708  1.00 56.92           N  
ANISOU   29  N   ALA A  13     7890   5253   8486    543   -786     67       N  
ATOM     30  CA  ALA A  13      12.219 -23.302  29.819  1.00 49.11           C  
ANISOU   30  CA  ALA A  13     7108   4380   7170    589   -449    -11       C  
ATOM     31  C   ALA A  13      10.902 -23.404  30.574  1.00 50.06           C  
ANISOU   31  C   ALA A  13     7633   4482   6905    466   -543   -114       C  
ATOM     32  O   ALA A  13      10.882 -23.651  31.783  1.00 49.30           O  
ANISOU   32  O   ALA A  13     7733   4266   6731    437   -823   -138       O  
ATOM     33  CB  ALA A  13      12.642 -24.679  29.307  1.00 46.88           C  
ANISOU   33  CB  ALA A  13     6836   4071   6905    805   -322    -21       C  
ATOM     34  N   THR A  14       9.799 -23.184  29.864  1.00 45.74           N  
ANISOU   34  N   THR A  14     7210   4044   6127    404   -306   -155       N  
ATOM     35  CA  THR A  14       8.478 -23.353  30.453  1.00 39.73           C  
ANISOU   35  CA  THR A  14     6765   3276   5055    302   -327   -210       C  
ATOM     36  C   THR A  14       7.690 -24.278  29.544  1.00 41.02           C  
ANISOU   36  C   THR A  14     7054   3474   5059    334   -138   -244       C  
ATOM     37  O   THR A  14       7.640 -24.061  28.329  1.00 41.04           O  
ANISOU   37  O   THR A  14     6962   3556   5077    371     60   -248       O  
ATOM     38  CB  THR A  14       7.745 -22.013  30.633  1.00 41.76           C  
ANISOU   38  CB  THR A  14     7046   3596   5225    172   -294   -208       C  
ATOM     39  CG2 THR A  14       6.441 -22.231  31.411  1.00 42.47           C  
ANISOU   39  CG2 THR A  14     7433   3669   5034    104   -286   -226       C  
ATOM     40  OG1 THR A  14       8.568 -21.127  31.405  1.00 43.31           O  
ANISOU   40  OG1 THR A  14     7159   3714   5583    146   -527   -185       O  
ATOM     41  N   LEU A  15       7.143 -25.346  30.124  1.00 45.15           N  
ANISOU   41  N   LEU A  15     7814   3907   5434    325   -224   -259       N  
ATOM     42  CA  LEU A  15       6.240 -26.252  29.424  1.00 38.53           C  
ANISOU   42  CA  LEU A  15     7136   3047   4457    310   -133   -282       C  
ATOM     43  C   LEU A  15       4.818 -25.897  29.816  1.00 36.83           C  
ANISOU   43  C   LEU A  15     7032   2864   4097    141    -94   -241       C  
ATOM     44  O   LEU A  15       4.537 -25.682  31.000  1.00 40.62           O  
ANISOU   44  O   LEU A  15     7607   3317   4509     87   -158   -195       O  
ATOM     45  CB  LEU A  15       6.528 -27.714  29.785  1.00 40.67           C  
ANISOU   45  CB  LEU A  15     7581   3167   4707    396   -264   -293       C  
ATOM     46  CG  LEU A  15       7.998 -28.108  29.737  1.00 45.78           C  
ANISOU   46  CG  LEU A  15     8098   3760   5535    592   -328   -309       C  
ATOM     47  CD1 LEU A  15       8.146 -29.597  30.095  1.00 42.47           C  
ANISOU   47  CD1 LEU A  15     7897   3170   5071    684   -471   -324       C  
ATOM     48  CD2 LEU A  15       8.548 -27.831  28.351  1.00 50.47           C  
ANISOU   48  CD2 LEU A  15     8520   4434   6220    730   -112   -330       C  
ATOM     49  N   ILE A  16       3.918 -25.854  28.832  1.00 39.12           N  
ANISOU   49  N   ILE A  16     7327   3195   4340     78     10   -245       N  
ATOM     50  CA  ILE A  16       2.564 -25.364  29.076  1.00 38.47           C  
ANISOU   50  CA  ILE A  16     7262   3159   4197    -73     70   -178       C  
ATOM     51  C   ILE A  16       1.553 -26.228  28.336  1.00 36.57           C  
ANISOU   51  C   ILE A  16     7111   2841   3942   -154     38   -153       C  
ATOM     52  O   ILE A  16       1.645 -26.399  27.113  1.00 39.04           O  
ANISOU   52  O   ILE A  16     7450   3137   4248   -106     29   -220       O  
ATOM     53  CB  ILE A  16       2.393 -23.880  28.657  1.00 38.01           C  
ANISOU   53  CB  ILE A  16     7047   3235   4160   -100    183   -185       C  
ATOM     54  CG1 ILE A  16       3.382 -22.980  29.405  1.00 39.54           C  
ANISOU   54  CG1 ILE A  16     7165   3458   4401    -47    148   -202       C  
ATOM     55  CG2 ILE A  16       0.937 -23.437  28.845  1.00 37.18           C  
ANISOU   55  CG2 ILE A  16     6936   3169   4021   -223    259   -103       C  
ATOM     56  CD1 ILE A  16       3.706 -21.591  28.684  1.00 33.97           C  
ANISOU   56  CD1 ILE A  16     6280   2852   3774    -48    231   -217       C  
ATOM     57  N   ALA A  17       0.565 -26.736  29.067  1.00 40.21           N  
ANISOU   57  N   ALA A  17     7636   3238   4404   -275     17    -40       N  
ATOM     58  CA  ALA A  17      -0.567 -27.431  28.474  1.00 38.67           C  
ANISOU   58  CA  ALA A  17     7474   2948   4272   -406    -58     30       C  
ATOM     59  C   ALA A  17      -1.802 -26.537  28.528  1.00 42.65           C  
ANISOU   59  C   ALA A  17     7810   3545   4851   -530     54    147       C  
ATOM     60  O   ALA A  17      -1.850 -25.529  29.239  1.00 40.15           O  
ANISOU   60  O   ALA A  17     7408   3347   4498   -502    211    180       O  
ATOM     61  CB  ALA A  17      -0.836 -28.766  29.196  1.00 38.97           C  
ANISOU   61  CB  ALA A  17     7659   2814   4333   -472   -164    128       C  
ATOM     62  N   ASN A  18      -2.810 -26.930  27.777  1.00 42.28           N  
ANISOU   62  N   ASN A  18     7730   3415   4920   -657    -56    212       N  
ATOM     63  CA  ASN A  18      -4.121 -26.309  27.910  1.00 41.23           C  
ANISOU   63  CA  ASN A  18     7393   3337   4936   -784     31    374       C  
ATOM     64  C   ASN A  18      -4.791 -26.831  29.181  1.00 44.27           C  
ANISOU   64  C   ASN A  18     7739   3677   5406   -867    150    588       C  
ATOM     65  O   ASN A  18      -4.758 -28.038  29.433  1.00 44.84           O  
ANISOU   65  O   ASN A  18     7931   3591   5513   -930     30    647       O  
ATOM     66  CB  ASN A  18      -4.962 -26.650  26.678  1.00 42.63           C  
ANISOU   66  CB  ASN A  18     7542   3396   5258   -905   -200    392       C  
ATOM     67  CG  ASN A  18      -6.186 -25.783  26.549  1.00 49.41           C  
ANISOU   67  CG  ASN A  18     8140   4328   6304  -1004   -137    538       C  
ATOM     68  ND2 ASN A  18      -6.284 -25.060  25.439  1.00 44.23           N  
ANISOU   68  ND2 ASN A  18     7472   3705   5628   -978   -233    441       N  
ATOM     69  OD1 ASN A  18      -7.047 -25.775  27.423  1.00 49.77           O  
ANISOU   69  OD1 ASN A  18     8002   4391   6517  -1087     10    751       O  
ATOM     70  N   PRO A  19      -5.378 -25.970  30.020  1.00 42.75           N  
ANISOU   70  N   PRO A  19     7414   3603   5226   -846    406    718       N  
ATOM     71  CA  PRO A  19      -6.046 -26.490  31.231  1.00 48.43           C  
ANISOU   71  CA  PRO A  19     8128   4273   5999   -891    588    959       C  
ATOM     72  C   PRO A  19      -7.212 -27.416  30.928  1.00 51.74           C  
ANISOU   72  C   PRO A  19     8378   4550   6732  -1104    492   1191       C  
ATOM     73  O   PRO A  19      -7.599 -28.212  31.799  1.00 50.44           O  
ANISOU   73  O   PRO A  19     8239   4292   6636  -1169    594   1405       O  
ATOM     74  CB  PRO A  19      -6.511 -25.218  31.959  1.00 51.61           C  
ANISOU   74  CB  PRO A  19     8439   4829   6340   -778    904   1038       C  
ATOM     75  CG  PRO A  19      -6.445 -24.129  30.936  1.00 51.92           C  
ANISOU   75  CG  PRO A  19     8352   4974   6401   -748    833    884       C  
ATOM     76  CD  PRO A  19      -5.353 -24.495  29.988  1.00 44.63           C  
ANISOU   76  CD  PRO A  19     7558   4008   5392   -743    564    653       C  
ATOM     77  N   ALA A  20      -7.791 -27.339  29.728  1.00 50.09           N  
ANISOU   77  N   ALA A  20     8006   4297   6728  -1219    274   1174       N  
ATOM     78  CA  ALA A  20      -8.838 -28.272  29.318  1.00 49.40           C  
ANISOU   78  CA  ALA A  20     7765   4018   6988  -1450     63   1385       C  
ATOM     79  C   ALA A  20      -8.290 -29.614  28.860  1.00 50.67           C  
ANISOU   79  C   ALA A  20     8189   3949   7116  -1524   -282   1284       C  
ATOM     80  O   ALA A  20      -9.065 -30.559  28.679  1.00 57.74           O  
ANISOU   80  O   ALA A  20     9012   4629   8296  -1733   -502   1469       O  
ATOM     81  CB  ALA A  20      -9.679 -27.644  28.199  1.00 52.71           C  
ANISOU   81  CB  ALA A  20     7950   4439   7637  -1538   -114   1399       C  
ATOM     82  N   LYS A  21      -6.976 -29.736  28.669  1.00 47.59           N  
ANISOU   82  N   LYS A  21     8094   3577   6412  -1355   -344   1010       N  
ATOM     83  CA  LYS A  21      -6.338 -30.997  28.255  1.00 51.92           C  
ANISOU   83  CA  LYS A  21     8933   3903   6889  -1359   -640    891       C  
ATOM     84  C   LYS A  21      -4.985 -31.043  28.962  1.00 53.97           C  
ANISOU   84  C   LYS A  21     9402   4246   6859  -1149   -495    736       C  
ATOM     85  O   LYS A  21      -3.913 -30.919  28.358  1.00 49.91           O  
ANISOU   85  O   LYS A  21     9047   3763   6155   -976   -559    496       O  
ATOM     86  CB  LYS A  21      -6.199 -31.086  26.731  1.00 53.30           C  
ANISOU   86  CB  LYS A  21     9250   3975   7026  -1335   -959    687       C  
ATOM     87  CG  LYS A  21      -6.373 -32.474  26.179  1.00 55.75           C  
ANISOU   87  CG  LYS A  21     9680   4104   7400  -1378  -1297    653       C  
ATOM     88  CD  LYS A  21      -5.829 -32.573  24.761  1.00 62.94           C  
ANISOU   88  CD  LYS A  21    10850   4966   8100  -1223  -1536    394       C  
ATOM     89  CE  LYS A  21      -6.901 -32.245  23.742  1.00 76.82           C  
ANISOU   89  CE  LYS A  21    12505   6670  10014  -1344  -1787    435       C  
ATOM     90  NZ  LYS A  21      -6.344 -32.169  22.363  1.00 79.66           N1+
ANISOU   90  NZ  LYS A  21    13179   6997  10091  -1153  -1965    196       N1+
ATOM     91  N   ALA A  22      -5.042 -31.179  30.285  1.00 47.42           N  
ANISOU   91  N   ALA A  22     8564   3447   6006  -1152   -284    899       N  
ATOM     92  CA  ALA A  22      -3.903 -30.867  31.143  1.00 49.56           C  
ANISOU   92  CA  ALA A  22     8987   3822   6020   -954   -138    784       C  
ATOM     93  C   ALA A  22      -3.043 -32.113  31.220  1.00 46.52           C  
ANISOU   93  C   ALA A  22     8868   3250   5557   -899   -348    700       C  
ATOM     94  O   ALA A  22      -3.179 -32.936  32.125  1.00 48.79           O  
ANISOU   94  O   ALA A  22     9265   3423   5850   -947   -340    851       O  
ATOM     95  CB  ALA A  22      -4.371 -30.394  32.514  1.00 53.80           C  
ANISOU   95  CB  ALA A  22     9482   4451   6507   -943    167    986       C  
ATOM     96  N   ALA A  23      -2.157 -32.260  30.237  1.00 46.98           N  
ANISOU   96  N   ALA A  23     9030   3279   5540   -773   -518    466       N  
ATOM     97  CA  ALA A  23      -1.392 -33.482  30.041  1.00 44.61           C  
ANISOU   97  CA  ALA A  23     8940   2821   5188   -678   -727    361       C  
ATOM     98  C   ALA A  23       0.021 -33.407  30.601  1.00 47.97           C  
ANISOU   98  C   ALA A  23     9486   3281   5460   -457   -688    235       C  
ATOM     99  O   ALA A  23       0.792 -34.353  30.418  1.00 47.43           O  
ANISOU   99  O   ALA A  23     9542   3127   5352   -328   -835    137       O  
ATOM    100  CB  ALA A  23      -1.338 -33.828  28.546  1.00 48.71           C  
ANISOU  100  CB  ALA A  23     9512   3286   5710   -628   -922    199       C  
ATOM    101  N   LEU A  24       0.382 -32.312  31.275  1.00 44.04           N  
ANISOU  101  N   LEU A  24     8879   2962   4891   -393   -509    232       N  
ATOM    102  CA  LEU A  24       1.733 -32.141  31.814  1.00 44.52           C  
ANISOU  102  CA  LEU A  24     8990   3061   4866   -197   -531    125       C  
ATOM    103  C   LEU A  24       1.824 -32.844  33.168  1.00 48.18           C  
ANISOU  103  C   LEU A  24     9653   3400   5256   -201   -586    245       C  
ATOM    104  O   LEU A  24       1.878 -32.221  34.234  1.00 44.16           O  
ANISOU  104  O   LEU A  24     9179   2956   4642   -180   -499    310       O  
ATOM    105  CB  LEU A  24       2.086 -30.654  31.918  1.00 38.69           C  
ANISOU  105  CB  LEU A  24     8066   2535   4099   -141   -388     69       C  
ATOM    106  CG  LEU A  24       3.549 -30.334  32.269  1.00 41.78           C  
ANISOU  106  CG  LEU A  24     8434   2953   4487     42   -465    -37       C  
ATOM    107  CD1 LEU A  24       4.512 -31.036  31.306  1.00 43.83           C  
ANISOU  107  CD1 LEU A  24     8679   3145   4828    200   -552   -156       C  
ATOM    108  CD2 LEU A  24       3.805 -28.790  32.293  1.00 43.07           C  
ANISOU  108  CD2 LEU A  24     8409   3293   4661     57   -363    -76       C  
ATOM    109  N   ALA A  25       1.828 -34.187  33.109  1.00 43.02           N  
ANISOU  109  N   ALA A  25     9137   2579   4631   -213   -743    270       N  
ATOM    110  CA  ALA A  25       1.861 -34.997  34.316  1.00 43.12           C  
ANISOU  110  CA  ALA A  25     9314   2501   4570   -221   -797    391       C  
ATOM    111  C   ALA A  25       3.185 -34.787  35.048  1.00 42.50           C  
ANISOU  111  C   ALA A  25     9332   2420   4395    -21   -896    298       C  
ATOM    112  O   ALA A  25       4.201 -34.467  34.420  1.00 46.47           O  
ANISOU  112  O   ALA A  25     9741   2954   4962    135   -969    138       O  
ATOM    113  CB  ALA A  25       1.684 -36.491  33.976  1.00 44.98           C  
ANISOU  113  CB  ALA A  25     9628   2587   4875   -266   -972    410       C  
ATOM    114  N   PRO A  26       3.199 -34.959  36.378  1.00 49.82           N  
ANISOU  114  N   PRO A  26    10440   3306   5184    -12   -906    409       N  
ATOM    115  CA  PRO A  26       4.469 -34.858  37.120  1.00 49.23           C  
ANISOU  115  CA  PRO A  26    10473   3196   5036    171  -1092    324       C  
ATOM    116  C   PRO A  26       5.598 -35.674  36.513  1.00 54.30           C  
ANISOU  116  C   PRO A  26    11056   3763   5811    325  -1306    192       C  
ATOM    117  O   PRO A  26       6.718 -35.164  36.379  1.00 55.14           O  
ANISOU  117  O   PRO A  26    11052   3889   6012    483  -1416     83       O  
ATOM    118  CB  PRO A  26       4.088 -35.378  38.512  1.00 50.79           C  
ANISOU  118  CB  PRO A  26    10938   3320   5042    139  -1088    476       C  
ATOM    119  CG  PRO A  26       2.641 -35.091  38.638  1.00 58.98           C  
ANISOU  119  CG  PRO A  26    11947   4420   6044    -32   -792    650       C  
ATOM    120  CD  PRO A  26       2.079 -35.329  37.263  1.00 57.76           C  
ANISOU  120  CD  PRO A  26    11555   4282   6108   -155   -756    627       C  
ATOM    121  N   SER A  27       5.335 -36.937  36.146  1.00 51.29           N  
ANISOU  121  N   SER A  27    10736   3285   5465    292  -1366    213       N  
ATOM    122  CA  SER A  27       6.380 -37.766  35.548  1.00 50.01           C  
ANISOU  122  CA  SER A  27    10549   3045   5409    478  -1535     90       C  
ATOM    123  C   SER A  27       6.892 -37.183  34.247  1.00 55.17           C  
ANISOU  123  C   SER A  27    10992   3777   6195    601  -1453    -53       C  
ATOM    124  O   SER A  27       8.069 -37.360  33.912  1.00 55.70           O  
ANISOU  124  O   SER A  27    10977   3809   6377    826  -1531   -149       O  
ATOM    125  CB  SER A  27       5.879 -39.193  35.301  1.00 50.44           C  
ANISOU  125  CB  SER A  27    10742   2967   5455    413  -1617    130       C  
ATOM    126  OG  SER A  27       5.191 -39.709  36.423  1.00 57.54           O  
ANISOU  126  OG  SER A  27    11822   3793   6250    267  -1630    296       O  
ATOM    127  N   LEU A  28       6.019 -36.516  33.490  1.00 49.15           N  
ANISOU  127  N   LEU A  28    10138   3108   5430    470  -1282    -56       N  
ATOM    128  CA  LEU A  28       6.430 -35.940  32.218  1.00 53.19           C  
ANISOU  128  CA  LEU A  28    10491   3692   6025    590  -1174   -185       C  
ATOM    129  C   LEU A  28       7.322 -34.721  32.433  1.00 53.97           C  
ANISOU  129  C   LEU A  28    10419   3870   6216    702  -1127   -227       C  
ATOM    130  O   LEU A  28       8.328 -34.551  31.738  1.00 53.24           O  
ANISOU  130  O   LEU A  28    10161   3811   6256    906  -1085   -312       O  
ATOM    131  CB  LEU A  28       5.188 -35.581  31.406  1.00 56.59           C  
ANISOU  131  CB  LEU A  28    10896   4186   6420    404  -1052   -168       C  
ATOM    132  CG  LEU A  28       5.308 -35.428  29.899  1.00 55.68           C  
ANISOU  132  CG  LEU A  28    10732   4107   6317    511   -973   -293       C  
ATOM    133  CD1 LEU A  28       6.023 -36.617  29.289  1.00 53.62           C  
ANISOU  133  CD1 LEU A  28    10598   3734   6042    722  -1069   -381       C  
ATOM    134  CD2 LEU A  28       3.949 -35.185  29.275  1.00 53.08           C  
ANISOU  134  CD2 LEU A  28    10404   3807   5959    293   -943   -250       C  
ATOM    135  N   GLY A  29       6.975 -33.864  33.397  1.00 53.80           N  
ANISOU  135  N   GLY A  29    10381   3926   6134    571  -1114   -150       N  
ATOM    136  CA  GLY A  29       7.847 -32.743  33.723  1.00 54.27           C  
ANISOU  136  CA  GLY A  29    10219   4110   6290    641  -1132   -177       C  
ATOM    137  C   GLY A  29       9.221 -33.194  34.186  1.00 56.09           C  
ANISOU  137  C   GLY A  29    10413   4226   6672    840  -1360   -198       C  
ATOM    138  O   GLY A  29      10.237 -32.600  33.822  1.00 54.22           O  
ANISOU  138  O   GLY A  29     9885   4063   6653    960  -1368   -231       O  
ATOM    139  N   ILE A  30       9.272 -34.264  34.978  1.00 56.54           N  
ANISOU  139  N   ILE A  30    10744   4089   6649    875  -1553   -154       N  
ATOM    140  CA  ILE A  30      10.555 -34.805  35.426  1.00 54.21           C  
ANISOU  140  CA  ILE A  30    10413   3667   6516   1075  -1807   -165       C  
ATOM    141  C   ILE A  30      11.367 -35.323  34.243  1.00 55.15           C  
ANISOU  141  C   ILE A  30    10329   3771   6854   1302  -1724   -240       C  
ATOM    142  O   ILE A  30      12.570 -35.061  34.136  1.00 57.54           O  
ANISOU  142  O   ILE A  30    10343   4090   7428   1481  -1794   -243       O  
ATOM    143  CB  ILE A  30      10.330 -35.902  36.480  1.00 53.86           C  
ANISOU  143  CB  ILE A  30    10646   3527   6290   1030  -1978    -98       C  
ATOM    144  CG1 ILE A  30       9.734 -35.301  37.754  1.00 63.91           C  
ANISOU  144  CG1 ILE A  30    12134   4822   7329    879  -2030    -15       C  
ATOM    145  CG2 ILE A  30      11.622 -36.681  36.768  1.00 62.72           C  
ANISOU  145  CG2 ILE A  30    11717   4521   7592   1246  -2237   -119       C  
ATOM    146  CD1 ILE A  30       9.067 -36.350  38.643  1.00 66.62           C  
ANISOU  146  CD1 ILE A  30    12795   5085   7431    795  -2064     80       C  
ATOM    147  N   LYS A  31      10.725 -36.068  33.336  1.00 56.67           N  
ANISOU  147  N   LYS A  31    10642   3954   6938   1299  -1562   -285       N  
ATOM    148  CA  LYS A  31      11.447 -36.569  32.168  1.00 55.34           C  
ANISOU  148  CA  LYS A  31    10372   3752   6903   1564  -1444   -366       C  
ATOM    149  C   LYS A  31      12.003 -35.428  31.328  1.00 61.11           C  
ANISOU  149  C   LYS A  31    10734   4678   7807   1651  -1208   -382       C  
ATOM    150  O   LYS A  31      13.140 -35.499  30.850  1.00 55.64           O  
ANISOU  150  O   LYS A  31     9798   3993   7350   1915  -1130   -381       O  
ATOM    151  CB  LYS A  31      10.548 -37.461  31.318  1.00 58.03           C  
ANISOU  151  CB  LYS A  31    10923   4083   7043   1500  -1342   -416       C  
ATOM    152  CG  LYS A  31      11.310 -38.197  30.245  1.00 69.49           C  
ANISOU  152  CG  LYS A  31    12372   5477   8554   1805  -1238   -503       C  
ATOM    153  CD  LYS A  31      11.034 -39.676  30.341  1.00 76.83           C  
ANISOU  153  CD  LYS A  31    13565   6275   9353   1798  -1397   -517       C  
ATOM    154  CE  LYS A  31      12.192 -40.512  29.822  1.00 74.26           C  
ANISOU  154  CE  LYS A  31    13227   5854   9134   2160  -1366   -578       C  
ATOM    155  NZ  LYS A  31      12.387 -41.755  30.629  1.00 71.00           N1+
ANISOU  155  NZ  LYS A  31    12987   5288   8701   2170  -1620   -551       N1+
ATOM    156  N   ALA A  32      11.210 -34.376  31.128  1.00 54.00           N  
ANISOU  156  N   ALA A  32     9759   3948   6809   1433  -1065   -374       N  
ATOM    157  CA  ALA A  32      11.683 -33.217  30.377  1.00 62.24           C  
ANISOU  157  CA  ALA A  32    10451   5187   8009   1474   -840   -365       C  
ATOM    158  C   ALA A  32      12.886 -32.571  31.052  1.00 58.73           C  
ANISOU  158  C   ALA A  32     9661   4772   7880   1538   -976   -286       C  
ATOM    159  O   ALA A  32      13.882 -32.246  30.395  1.00 61.45           O  
ANISOU  159  O   ALA A  32     9666   5183   8499   1721   -824   -242       O  
ATOM    160  CB  ALA A  32      10.557 -32.194  30.221  1.00 54.41           C  
ANISOU  160  CB  ALA A  32     9472   4346   6855   1214   -721   -363       C  
ATOM    161  N   SER A  33      12.812 -32.364  32.366  1.00 52.69           N  
ANISOU  161  N   SER A  33     8987   3941   7092   1394  -1270   -248       N  
ATOM    162  CA  SER A  33      13.915 -31.680  33.031  1.00 56.20           C  
ANISOU  162  CA  SER A  33     9134   4371   7849   1426  -1493   -175       C  
ATOM    163  C   SER A  33      15.182 -32.522  32.997  1.00 60.64           C  
ANISOU  163  C   SER A  33     9509   4808   8722   1699  -1613   -135       C  
ATOM    164  O   SER A  33      16.285 -31.979  32.874  1.00 69.14           O  
ANISOU  164  O   SER A  33    10158   5913  10200   1796  -1650    -45       O  
ATOM    165  CB  SER A  33      13.534 -31.330  34.466  1.00 56.29           C  
ANISOU  165  CB  SER A  33     9398   4292   7696   1249  -1817   -160       C  
ATOM    166  OG  SER A  33      13.188 -32.497  35.176  1.00 64.34           O  
ANISOU  166  OG  SER A  33    10800   5142   8504   1277  -1981   -170       O  
ATOM    167  N   ALA A  34      15.047 -33.843  33.089  1.00 60.39           N  
ANISOU  167  N   ALA A  34     9770   4627   8550   1827  -1675   -180       N  
ATOM    168  CA  ALA A  34      16.217 -34.699  32.930  1.00 61.97           C  
ANISOU  168  CA  ALA A  34     9798   4704   9043   2134  -1745   -147       C  
ATOM    169  C   ALA A  34      16.776 -34.600  31.516  1.00 68.66           C  
ANISOU  169  C   ALA A  34    10331   5672  10086   2373  -1332   -132       C  
ATOM    170  O   ALA A  34      17.993 -34.685  31.323  1.00 71.64           O  
ANISOU  170  O   ALA A  34    10327   6028  10866   2620  -1307    -37       O  
ATOM    171  CB  ALA A  34      15.862 -36.142  33.277  1.00 65.22           C  
ANISOU  171  CB  ALA A  34    10648   4906   9227   2222  -1894   -206       C  
ATOM    172  N   ALA A  35      15.909 -34.374  30.525  1.00 65.55           N  
ANISOU  172  N   ALA A  35    10086   5399   9422   2313  -1000   -204       N  
ATOM    173  CA  ALA A  35      16.354 -34.320  29.137  1.00 74.07           C  
ANISOU  173  CA  ALA A  35    10983   6572  10588   2571   -576   -194       C  
ATOM    174  C   ALA A  35      17.219 -33.102  28.845  1.00 70.92           C  
ANISOU  174  C   ALA A  35    10029   6339  10579   2582   -402    -44       C  
ATOM    175  O   ALA A  35      17.926 -33.094  27.833  1.00 81.96           O  
ANISOU  175  O   ALA A  35    11187   7800  12156   2860    -33     29       O  
ATOM    176  CB  ALA A  35      15.150 -34.334  28.196  1.00 66.17           C  
ANISOU  176  CB  ALA A  35    10340   5625   9174   2482   -342   -311       C  
ATOM    177  N   VAL A  36      17.183 -32.078  29.698  1.00 65.28           N  
ANISOU  177  N   VAL A  36     9128   5677   9999   2299   -651     18       N  
ATOM    178  CA  VAL A  36      18.005 -30.888  29.525  1.00 69.04           C  
ANISOU  178  CA  VAL A  36     9071   6267  10895   2260   -569    181       C  
ATOM    179  C   VAL A  36      18.991 -30.721  30.681  1.00 76.83           C  
ANISOU  179  C   VAL A  36     9752   7125  12315   2223  -1023    296       C  
ATOM    180  O   VAL A  36      19.549 -29.643  30.862  1.00 73.89           O  
ANISOU  180  O   VAL A  36     8982   6792  12302   2093  -1123    430       O  
ATOM    181  CB  VAL A  36      17.140 -29.622  29.336  1.00 69.03           C  
ANISOU  181  CB  VAL A  36     9106   6415  10705   1962   -475    160       C  
ATOM    182  CG1 VAL A  36      16.447 -29.644  27.980  1.00 66.39           C  
ANISOU  182  CG1 VAL A  36     8956   6204  10064   2043    -16     95       C  
ATOM    183  CG2 VAL A  36      16.130 -29.449  30.464  1.00 60.17           C  
ANISOU  183  CG2 VAL A  36     8360   5237   9267   1673   -829     53       C  
ATOM    184  N   ASN A  37      19.226 -31.794  31.446  1.00 71.08           N  
ANISOU  184  N   ASN A  37     9223   6216  11570   2338  -1333    251       N  
ATOM    185  CA AASN A  37      20.114 -31.775  32.615  0.52 78.08           C  
ANISOU  185  CA AASN A  37     9910   6933  12825   2318  -1852    345       C  
ATOM    186  CA BASN A  37      20.124 -31.765  32.602  0.48 78.08           C  
ANISOU  186  CA BASN A  37     9902   6934  12830   2319  -1848    347       C  
ATOM    187  C   ASN A  37      19.842 -30.551  33.485  1.00 78.25           C  
ANISOU  187  C   ASN A  37     9944   6946  12841   1984  -2198    358       C  
ATOM    188  O   ASN A  37      20.744 -29.806  33.870  1.00 92.15           O  
ANISOU  188  O   ASN A  37    11294   8645  15074   1924  -2478    500       O  
ATOM    189  CB AASN A  37      21.586 -31.837  32.204  0.52 80.73           C  
ANISOU  189  CB AASN A  37     9612   7245  13815   2584  -1780    547       C  
ATOM    190  CB BASN A  37      21.585 -31.789  32.153  0.48 80.72           C  
ANISOU  190  CB BASN A  37     9595   7254  13819   2582  -1758    552       C  
ATOM    191  CG AASN A  37      21.835 -32.782  31.043  0.52 83.21           C  
ANISOU  191  CG AASN A  37     9895   7609  14111   2964  -1273    546       C  
ATOM    192  CG BASN A  37      22.537 -32.059  33.294  0.48 85.49           C  
ANISOU  192  CG BASN A  37    10012   7638  14834   2616  -2342    647       C  
ATOM    193  ND2AASN A  37      21.755 -34.081  31.309  0.52 84.77           N  
ANISOU  193  ND2AASN A  37    10444   7652  14112   3160  -1394    440       N  
ATOM    194  ND2BASN A  37      23.572 -31.235  33.407  0.48 94.55           N  
ANISOU  194  ND2BASN A  37    10553   8763  16610   2576  -2517    858       N  
ATOM    195  OD1AASN A  37      22.099 -32.350  29.921  0.52 90.47           O  
ANISOU  195  OD1AASN A  37    10518   8684  15170   3095   -777    642       O  
ATOM    196  OD1BASN A  37      22.339 -32.986  34.077  0.48 87.52           O  
ANISOU  196  OD1BASN A  37    10668   7724  14861   2664  -2664    546       O  
ATOM    197  N   ALA A  38      18.567 -30.358  33.808  1.00 72.30           N  
ANISOU  197  N   ALA A  38     9680   6232  11558   1773  -2191    216       N  
ATOM    198  CA  ALA A  38      18.128 -29.131  34.456  1.00 71.56           C  
ANISOU  198  CA  ALA A  38     9672   6151  11367   1493  -2406    206       C  
ATOM    199  C   ALA A  38      18.610 -29.021  35.897  1.00 84.90           C  
ANISOU  199  C   ALA A  38    11501   7607  13151   1424  -3031    226       C  
ATOM    200  O   ALA A  38      18.807 -30.018  36.595  1.00 77.84           O  
ANISOU  200  O   ALA A  38    10849   6545  12182   1538  -3300    204       O  
ATOM    201  CB  ALA A  38      16.609 -29.041  34.437  1.00 64.84           C  
ANISOU  201  CB  ALA A  38     9302   5397   9937   1332  -2196     70       C  
ATOM    202  N   THR A  39      18.761 -27.771  36.347  1.00104.16           N  
ANISOU  202  N   THR A  39    13843  10010  15724   1234  -3290    265       N  
ATOM    203  CA  THR A  39      19.090 -27.510  37.743  1.00109.43           C  
ANISOU  203  CA  THR A  39    14765  10421  16392   1155  -3932    259       C  
ATOM    204  C   THR A  39      17.913 -27.833  38.661  1.00112.36           C  
ANISOU  204  C   THR A  39    15870  10729  16092   1095  -4000    117       C  
ATOM    205  O   THR A  39      18.112 -28.303  39.787  1.00114.29           O  
ANISOU  205  O   THR A  39    16479  10744  16203   1140  -4448    101       O  
ATOM    206  CB  THR A  39      19.531 -26.054  37.909  1.00110.68           C  
ANISOU  206  CB  THR A  39    14667  10525  16861    971  -4205    331       C  
ATOM    207  CG2 THR A  39      20.606 -25.706  36.888  1.00100.03           C  
ANISOU  207  CG2 THR A  39    12541   9264  16201   1016  -4028    524       C  
ATOM    208  OG1 THR A  39      18.410 -25.176  37.724  1.00101.40           O  
ANISOU  208  OG1 THR A  39    13763   9488  15274    808  -3934    234       O  
ATOM    209  N   GLY A  40      16.688 -27.600  38.198  1.00 99.96           N  
ANISOU  209  N   GLY A  40    14520   9348  14111   1004  -3555     37       N  
ATOM    210  CA  GLY A  40      15.516 -27.873  39.002  1.00 91.08           C  
ANISOU  210  CA  GLY A  40    14023   8182  12400    951  -3530    -48       C  
ATOM    211  C   GLY A  40      14.258 -27.989  38.165  1.00 78.56           C  
ANISOU  211  C   GLY A  40    12517   6825  10507    890  -2970    -94       C  
ATOM    212  O   GLY A  40      14.309 -28.091  36.938  1.00 70.79           O  
ANISOU  212  O   GLY A  40    11178   6009   9708    920  -2621    -85       O  
ATOM    213  N   LEU A  41      13.118 -27.975  38.857  1.00 72.41           N  
ANISOU  213  N   LEU A  41    12224   6031   9257    817  -2893   -130       N  
ATOM    214  CA  LEU A  41      11.804 -28.112  38.225  1.00 61.92           C  
ANISOU  214  CA  LEU A  41    10990   4883   7653    739  -2422   -148       C  
ATOM    215  C   LEU A  41      10.778 -27.473  39.147  1.00 67.98           C  
ANISOU  215  C   LEU A  41    12187   5627   8014    657  -2389   -151       C  
ATOM    216  O   LEU A  41      10.621 -27.913  40.288  1.00 62.18           O  
ANISOU  216  O   LEU A  41    11893   4724   7009    706  -2578   -126       O  
ATOM    217  CB  LEU A  41      11.471 -29.594  37.965  1.00 59.51           C  
ANISOU  217  CB  LEU A  41    10809   4549   7253    806  -2280   -132       C  
ATOM    218  CG  LEU A  41      10.058 -29.925  37.478  1.00 56.70           C  
ANISOU  218  CG  LEU A  41    10597   4309   6636    703  -1893   -122       C  
ATOM    219  CD1 LEU A  41       9.884 -29.481  36.040  1.00 60.80           C  
ANISOU  219  CD1 LEU A  41    10756   5025   7321    668  -1592   -162       C  
ATOM    220  CD2 LEU A  41       9.794 -31.420  37.590  1.00 59.45           C  
ANISOU  220  CD2 LEU A  41    11172   4534   6883    750  -1895    -86       C  
ATOM    221  N   TYR A  42      10.090 -26.437  38.673  1.00 55.18           N  
ANISOU  221  N   TYR A  42    10467   4162   6337    559  -2137   -172       N  
ATOM    222  CA  TYR A  42       9.183 -25.657  39.511  1.00 60.75           C  
ANISOU  222  CA  TYR A  42    11552   4846   6684    526  -2079   -173       C  
ATOM    223  C   TYR A  42       7.801 -25.663  38.885  1.00 58.12           C  
ANISOU  223  C   TYR A  42    11190   4701   6192    445  -1604   -138       C  
ATOM    224  O   TYR A  42       7.628 -25.215  37.745  1.00 51.16           O  
ANISOU  224  O   TYR A  42     9956   3989   5495    376  -1395   -161       O  
ATOM    225  CB  TYR A  42       9.678 -24.220  39.703  1.00 62.16           C  
ANISOU  225  CB  TYR A  42    11675   4982   6963    498  -2304   -226       C  
ATOM    226  CG  TYR A  42      10.993 -24.135  40.432  1.00 70.12           C  
ANISOU  226  CG  TYR A  42    12725   5756   8160    555  -2858   -241       C  
ATOM    227  CD1 TYR A  42      12.196 -24.273  39.753  1.00 76.02           C  
ANISOU  227  CD1 TYR A  42    12977   6503   9405    550  -3040   -215       C  
ATOM    228  CD2 TYR A  42      11.033 -23.938  41.808  1.00 89.40           C  
ANISOU  228  CD2 TYR A  42    15662   8024  10280    620  -3182   -261       C  
ATOM    229  CE1 TYR A  42      13.408 -24.205  40.424  1.00 82.62           C  
ANISOU  229  CE1 TYR A  42    13791   7107  10495    591  -3589   -198       C  
ATOM    230  CE2 TYR A  42      12.239 -23.869  42.487  1.00 92.13           C  
ANISOU  230  CE2 TYR A  42    16014   8188  10803    650  -3743   -276       C  
ATOM    231  CZ  TYR A  42      13.423 -24.002  41.789  1.00 93.53           C  
ANISOU  231  CZ  TYR A  42    15684   8293  11560    628  -3978   -238       C  
ATOM    232  OH  TYR A  42      14.628 -23.935  42.454  1.00105.44           O  
ANISOU  232  OH  TYR A  42    17136   9606  13319    640  -4565   -232       O  
ATOM    233  N   TRP A  43       6.822 -26.172  39.626  1.00 51.03           N  
ANISOU  233  N   TRP A  43    10658   3761   4971    458  -1441    -60       N  
ATOM    234  CA  TRP A  43       5.467 -26.241  39.101  1.00 55.93           C  
ANISOU  234  CA  TRP A  43    11212   4535   5504    371  -1020     14       C  
ATOM    235  C   TRP A  43       4.784 -24.890  39.274  1.00 49.49           C  
ANISOU  235  C   TRP A  43    10452   3801   4549    366   -853      4       C  
ATOM    236  O   TRP A  43       4.694 -24.372  40.390  1.00 51.44           O  
ANISOU  236  O   TRP A  43    11088   3935   4523    465   -927     10       O  
ATOM    237  CB  TRP A  43       4.678 -27.349  39.782  1.00 53.12           C  
ANISOU  237  CB  TRP A  43    11156   4094   4932    374   -878    154       C  
ATOM    238  CG  TRP A  43       5.152 -28.698  39.301  1.00 51.41           C  
ANISOU  238  CG  TRP A  43    10832   3812   4889    357   -996    160       C  
ATOM    239  CD1 TRP A  43       6.042 -29.535  39.909  1.00 57.67           C  
ANISOU  239  CD1 TRP A  43    11815   4425   5672    449  -1295    154       C  
ATOM    240  CD2 TRP A  43       4.811 -29.306  38.058  1.00 45.50           C  
ANISOU  240  CD2 TRP A  43     9786   3152   4349    265   -851    158       C  
ATOM    241  CE2 TRP A  43       5.510 -30.526  37.979  1.00 51.30           C  
ANISOU  241  CE2 TRP A  43    10565   3750   5176    321  -1048    145       C  
ATOM    242  CE3 TRP A  43       3.980 -28.931  36.996  1.00 44.63           C  
ANISOU  242  CE3 TRP A  43     9413   3199   4344    155   -604    161       C  
ATOM    243  NE1 TRP A  43       6.248 -30.653  39.128  1.00 54.28           N  
ANISOU  243  NE1 TRP A  43    11218   3972   5432    430  -1310    150       N  
ATOM    244  CZ2 TRP A  43       5.389 -31.387  36.891  1.00 50.67           C  
ANISOU  244  CZ2 TRP A  43    10319   3674   5259    283   -995    124       C  
ATOM    245  CZ3 TRP A  43       3.857 -29.794  35.905  1.00 45.02           C  
ANISOU  245  CZ3 TRP A  43     9302   3247   4557    102   -584    143       C  
ATOM    246  CH2 TRP A  43       4.563 -31.009  35.866  1.00 50.11           C  
ANISOU  246  CH2 TRP A  43    10038   3742   5261    173   -774    119       C  
ATOM    247  N   LEU A  44       4.319 -24.330  38.169  1.00 45.55           N  
ANISOU  247  N   LEU A  44     9612   3478   4218    277   -641    -16       N  
ATOM    248  CA  LEU A  44       3.493 -23.128  38.198  1.00 44.76           C  
ANISOU  248  CA  LEU A  44     9534   3466   4007    276   -434    -11       C  
ATOM    249  C   LEU A  44       2.019 -23.468  38.338  1.00 58.26           C  
ANISOU  249  C   LEU A  44    11312   5246   5580    252    -57    139       C  
ATOM    250  O   LEU A  44       1.273 -22.719  38.975  1.00 47.50           O  
ANISOU  250  O   LEU A  44    10147   3888   4011    332    134    191       O  
ATOM    251  CB  LEU A  44       3.721 -22.308  36.926  1.00 45.77           C  
ANISOU  251  CB  LEU A  44     9263   3733   4394    194   -407    -88       C  
ATOM    252  CG  LEU A  44       5.171 -21.947  36.584  1.00 48.41           C  
ANISOU  252  CG  LEU A  44     9407   4018   4968    197   -716   -182       C  
ATOM    253  CD1 LEU A  44       5.212 -21.156  35.274  1.00 42.78           C  
ANISOU  253  CD1 LEU A  44     8323   3452   4480    120   -591   -211       C  
ATOM    254  CD2 LEU A  44       5.834 -21.164  37.729  1.00 51.44           C  
ANISOU  254  CD2 LEU A  44    10076   4225   5243    271  -1036   -231       C  
ATOM    255  N   ALA A  45       1.592 -24.595  37.765  1.00 47.60           N  
ANISOU  255  N   ALA A  45     9801   3927   4359    154     45    223       N  
ATOM    256  CA  ALA A  45       0.224 -25.071  37.917  1.00 42.79           C  
ANISOU  256  CA  ALA A  45     9202   3350   3707     98    362    414       C  
ATOM    257  C   ALA A  45       0.232 -26.576  37.692  1.00 43.76           C  
ANISOU  257  C   ALA A  45     9302   3389   3937      7    293    492       C  
ATOM    258  O   ALA A  45       0.754 -27.034  36.677  1.00 44.97           O  
ANISOU  258  O   ALA A  45     9247   3553   4287    -56    133    393       O  
ATOM    259  CB  ALA A  45      -0.716 -24.395  36.916  1.00 41.73           C  
ANISOU  259  CB  ALA A  45     8737   3373   3745      6    573    442       C  
ATOM    260  N   ASP A  46      -0.339 -27.320  38.628  1.00 43.20           N  
ANISOU  260  N   ASP A  46     9474   3217   3723     18    425    676       N  
ATOM    261  CA  ASP A  46      -0.288 -28.781  38.547  1.00 47.42           C  
ANISOU  261  CA  ASP A  46    10045   3626   4347    -68    322    761       C  
ATOM    262  C   ASP A  46      -0.927 -29.250  37.248  1.00 47.98           C  
ANISOU  262  C   ASP A  46     9772   3745   4713   -245    346    788       C  
ATOM    263  O   ASP A  46      -1.988 -28.760  36.853  1.00 45.95           O  
ANISOU  263  O   ASP A  46     9300   3588   4570   -332    562    893       O  
ATOM    264  CB  ASP A  46      -0.992 -29.414  39.737  1.00 49.21           C  
ANISOU  264  CB  ASP A  46    10478   3797   4420    -44    516    966       C  
ATOM    265  CG  ASP A  46      -0.213 -29.258  41.034  1.00 62.16           C  
ANISOU  265  CG  ASP A  46    12505   5360   5752    145    394    887       C  
ATOM    266  OD1 ASP A  46       1.021 -29.060  40.981  1.00 56.57           O  
ANISOU  266  OD1 ASP A  46    11918   4575   5002    221     59    708       O  
ATOM    267  OD2 ASP A  46      -0.833 -29.404  42.104  1.00 63.78           O1-
ANISOU  267  OD2 ASP A  46    12883   5562   5788    219    614   1015       O1-
ATOM    268  N   ASP A  47      -0.249 -30.167  36.562  1.00 51.12           N  
ANISOU  268  N   ASP A  47    10138   4054   5233   -277     96    686       N  
ATOM    269  CA  ASP A  47      -0.682 -30.783  35.307  1.00 48.25           C  
ANISOU  269  CA  ASP A  47     9567   3667   5099   -414     25    676       C  
ATOM    270  C   ASP A  47      -0.745 -29.802  34.145  1.00 53.09           C  
ANISOU  270  C   ASP A  47     9917   4438   5817   -426     50    540       C  
ATOM    271  O   ASP A  47      -1.154 -30.203  33.033  1.00 45.02           O  
ANISOU  271  O   ASP A  47     8771   3385   4951   -524    -31    520       O  
ATOM    272  CB  ASP A  47      -2.044 -31.490  35.442  1.00 48.63           C  
ANISOU  272  CB  ASP A  47     9569   3628   5280   -600    155    940       C  
ATOM    273  CG  ASP A  47      -2.047 -32.558  36.515  1.00 45.11           C  
ANISOU  273  CG  ASP A  47     9328   3057   4755   -596    146   1087       C  
ATOM    274  OD1 ASP A  47      -0.960 -33.004  36.945  1.00 49.08           O  
ANISOU  274  OD1 ASP A  47    10046   3486   5116   -467    -39    964       O  
ATOM    275  OD2 ASP A  47      -3.141 -32.985  36.942  1.00 50.49           O1-
ANISOU  275  OD2 ASP A  47     9909   3725   5549   -715    318   1336       O1-
ATOM    276  N   ILE A  48      -0.316 -28.548  34.331  1.00 39.82           N  
ANISOU  276  N   ILE A  48     8187   2896   4047   -325    123    443       N  
ATOM    277  CA  ILE A  48      -0.547 -27.512  33.334  1.00 41.69           C  
ANISOU  277  CA  ILE A  48     8189   3280   4373   -348    188    360       C  
ATOM    278  C   ILE A  48       0.735 -26.789  32.936  1.00 42.34           C  
ANISOU  278  C   ILE A  48     8218   3427   4441   -226     80    168       C  
ATOM    279  O   ILE A  48       0.962 -26.555  31.752  1.00 40.29           O  
ANISOU  279  O   ILE A  48     7807   3225   4278   -227     56     75       O  
ATOM    280  CB  ILE A  48      -1.600 -26.503  33.823  1.00 40.35           C  
ANISOU  280  CB  ILE A  48     7948   3213   4171   -372    434    483       C  
ATOM    281  CG1 ILE A  48      -2.981 -27.163  33.879  1.00 46.15           C  
ANISOU  281  CG1 ILE A  48     8596   3898   5041   -516    569    716       C  
ATOM    282  CG2 ILE A  48      -1.645 -25.303  32.879  1.00 39.58           C  
ANISOU  282  CG2 ILE A  48     7643   3256   4141   -367    467    377       C  
ATOM    283  CD1 ILE A  48      -4.006 -26.358  34.648  1.00 46.57           C  
ANISOU  283  CD1 ILE A  48     8601   4032   5060   -488    881    895       C  
ATOM    284  N   ALA A  49       1.577 -26.404  33.898  1.00 41.85           N  
ANISOU  284  N   ALA A  49     8285   3341   4273   -120      6    127       N  
ATOM    285  CA  ALA A  49       2.751 -25.631  33.514  1.00 41.81           C  
ANISOU  285  CA  ALA A  49     8159   3386   4340    -37   -107     -9       C  
ATOM    286  C   ALA A  49       3.876 -25.788  34.522  1.00 39.86           C  
ANISOU  286  C   ALA A  49     8068   3028   4050     69   -325    -43       C  
ATOM    287  O   ALA A  49       3.651 -25.762  35.736  1.00 42.30           O  
ANISOU  287  O   ALA A  49     8636   3257   4178     99   -355     14       O  
ATOM    288  CB  ALA A  49       2.408 -24.130  33.359  1.00 39.21           C  
ANISOU  288  CB  ALA A  49     7718   3177   4001    -54      7    -29       C  
ATOM    289  N   CYS A  50       5.097 -25.923  34.015  1.00 45.10           N  
ANISOU  289  N   CYS A  50     8579   3674   4885    142   -476   -124       N  
ATOM    290  CA  CYS A  50       6.256 -25.964  34.897  1.00 44.91           C  
ANISOU  290  CA  CYS A  50     8635   3530   4899    237   -746   -148       C  
ATOM    291  C   CYS A  50       7.408 -25.182  34.286  1.00 46.56           C  
ANISOU  291  C   CYS A  50     8538   3783   5369    279   -840   -201       C  
ATOM    292  O   CYS A  50       7.531 -25.075  33.061  1.00 47.95           O  
ANISOU  292  O   CYS A  50     8464   4065   5689    282   -676   -218       O  
ATOM    293  CB  CYS A  50       6.707 -27.398  35.195  1.00 46.34           C  
ANISOU  293  CB  CYS A  50     8946   3571   5088    310   -888   -132       C  
ATOM    294  SG  CYS A  50       7.299 -28.344  33.770  1.00 48.01           S  
ANISOU  294  SG  CYS A  50     8927   3798   5514    392   -830   -183       S  
ATOM    295  N   ASP A  51       8.258 -24.669  35.167  1.00 45.89           N  
ANISOU  295  N   ASP A  51     8498   3592   5348    316  -1120   -208       N  
ATOM    296  CA  ASP A  51       9.494 -23.986  34.820  1.00 49.05           C  
ANISOU  296  CA  ASP A  51     8581   3981   6075    340  -1283   -210       C  
ATOM    297  C   ASP A  51      10.669 -24.942  34.940  1.00 57.66           C  
ANISOU  297  C   ASP A  51     9553   4959   7396    458  -1496   -188       C  
ATOM    298  O   ASP A  51      10.783 -25.686  35.922  1.00 55.08           O  
ANISOU  298  O   ASP A  51     9498   4482   6947    511  -1722   -187       O  
ATOM    299  CB  ASP A  51       9.741 -22.808  35.759  1.00 45.93           C  
ANISOU  299  CB  ASP A  51     8311   3482   5659    295  -1554   -221       C  
ATOM    300  CG  ASP A  51       9.135 -21.514  35.262  1.00 48.46           C  
ANISOU  300  CG  ASP A  51     8549   3915   5948    202  -1374   -234       C  
ATOM    301  OD1 ASP A  51       8.650 -21.442  34.106  1.00 47.59           O  
ANISOU  301  OD1 ASP A  51     8232   3974   5878    167  -1055   -225       O  
ATOM    302  OD2 ASP A  51       9.123 -20.569  36.071  1.00 49.55           O1-
ANISOU  302  OD2 ASP A  51     8886   3945   5994    179  -1581   -260       O1-
ATOM    303  N   ILE A  52      11.565 -24.886  33.962  1.00 54.57           N  
ANISOU  303  N   ILE A  52     8761   4629   7344    520  -1413   -152       N  
ATOM    304  CA  ILE A  52      12.756 -25.732  33.967  1.00 60.33           C  
ANISOU  304  CA  ILE A  52     9300   5261   8363    670  -1574   -109       C  
ATOM    305  C   ILE A  52      13.975 -24.834  33.780  1.00 63.69           C  
ANISOU  305  C   ILE A  52     9288   5666   9246    668  -1721    -16       C  
ATOM    306  O   ILE A  52      14.348 -24.513  32.641  1.00 56.43           O  
ANISOU  306  O   ILE A  52     8011   4873   8558    708  -1433     50       O  
ATOM    307  CB  ILE A  52      12.665 -26.821  32.886  1.00 55.99           C  
ANISOU  307  CB  ILE A  52     8693   4782   7797    807  -1266   -124       C  
ATOM    308  CG1 ILE A  52      11.382 -27.641  33.065  1.00 54.70           C  
ANISOU  308  CG1 ILE A  52     8940   4608   7236    756  -1169   -190       C  
ATOM    309  CG2 ILE A  52      13.853 -27.763  32.972  1.00 56.66           C  
ANISOU  309  CG2 ILE A  52     8615   4750   8163   1006  -1418    -80       C  
ATOM    310  CD1 ILE A  52      11.273 -28.849  32.127  1.00 51.48           C  
ANISOU  310  CD1 ILE A  52     8580   4195   6786    891   -974   -223       C  
ATOM    311  N   PRO A  53      14.601 -24.370  34.859  1.00 61.31           N  
ANISOU  311  N   PRO A  53     9015   5189   9091    619  -2173     11       N  
ATOM    312  CA  PRO A  53      15.836 -23.594  34.707  1.00 71.40           C  
ANISOU  312  CA  PRO A  53     9821   6404  10901    595  -2379    138       C  
ATOM    313  C   PRO A  53      16.903 -24.427  34.020  1.00 69.60           C  
ANISOU  313  C   PRO A  53     9162   6194  11088    782  -2259    250       C  
ATOM    314  O   PRO A  53      17.161 -25.573  34.391  1.00 68.17           O  
ANISOU  314  O   PRO A  53     9101   5923  10877    929  -2376    227       O  
ATOM    315  CB  PRO A  53      16.223 -23.243  36.148  1.00 69.94           C  
ANISOU  315  CB  PRO A  53     9879   5962  10732    528  -2990    121       C  
ATOM    316  CG  PRO A  53      14.954 -23.345  36.919  1.00 78.07           C  
ANISOU  316  CG  PRO A  53    11532   6976  11154    492  -2971    -17       C  
ATOM    317  CD  PRO A  53      14.157 -24.434  36.261  1.00 74.42           C  
ANISOU  317  CD  PRO A  53    11170   6680  10426    576  -2523    -59       C  
ATOM    318  N   LEU A  54      17.501 -23.850  33.002  1.00 69.63           N  
ANISOU  318  N   LEU A  54     8680   6309  11469    796  -1992    385       N  
ATOM    319  CA  LEU A  54      18.480 -24.597  32.236  1.00 72.56           C  
ANISOU  319  CA  LEU A  54     8633   6715  12223   1024  -1765    515       C  
ATOM    320  C   LEU A  54      19.870 -24.403  32.836  1.00 76.17           C  
ANISOU  320  C   LEU A  54     8640   6990  13311   1036  -2196    694       C  
ATOM    321  O   LEU A  54      20.179 -23.319  33.344  1.00 73.85           O  
ANISOU  321  O   LEU A  54     8204   6589  13265    833  -2547    766       O  
ATOM    322  CB  LEU A  54      18.469 -24.131  30.784  1.00 68.46           C  
ANISOU  322  CB  LEU A  54     7821   6399  11792   1077  -1196    609       C  
ATOM    323  CG  LEU A  54      17.073 -24.235  30.166  1.00 70.00           C  
ANISOU  323  CG  LEU A  54     8456   6743  11396   1045   -847    439       C  
ATOM    324  CD1 LEU A  54      17.037 -23.630  28.781  1.00 59.98           C  
ANISOU  324  CD1 LEU A  54     6970   5647  10174   1086   -346    530       C  
ATOM    325  CD2 LEU A  54      16.621 -25.694  30.130  1.00 63.98           C  
ANISOU  325  CD2 LEU A  54     8049   5960  10302   1225   -762    304       C  
ATOM    326  N   PRO A  55      20.711 -25.436  32.813  1.00 81.18           N  
ANISOU  326  N   PRO A  55     9057   7559  14229   1271  -2221    770       N  
ATOM    327  CA  PRO A  55      22.101 -25.252  33.245  1.00 83.07           C  
ANISOU  327  CA  PRO A  55     8756   7628  15178   1296  -2611    986       C  
ATOM    328  C   PRO A  55      22.803 -24.213  32.386  1.00 92.66           C  
ANISOU  328  C   PRO A  55     9331   8931  16946   1231  -2355   1238       C  
ATOM    329  O   PRO A  55      22.485 -24.023  31.209  1.00 90.69           O  
ANISOU  329  O   PRO A  55     8986   8895  16577   1302  -1742   1274       O  
ATOM    330  CB  PRO A  55      22.725 -26.643  33.084  1.00 89.24           C  
ANISOU  330  CB  PRO A  55     9419   8374  16113   1624  -2508   1020       C  
ATOM    331  CG  PRO A  55      21.809 -27.424  32.240  1.00 82.74           C  
ANISOU  331  CG  PRO A  55     8974   7725  14738   1784  -1956    859       C  
ATOM    332  CD  PRO A  55      20.470 -26.750  32.198  1.00 72.94           C  
ANISOU  332  CD  PRO A  55     8189   6594  12930   1541  -1844    689       C  
ATOM    333  N   LEU A  56      23.759 -23.525  33.000  1.00 99.54           N  
ANISOU  333  N   LEU A  56     9782   9608  18429   1087  -2862   1425       N  
ATOM    334  CA  LEU A  56      24.373 -22.366  32.370  1.00104.38           C  
ANISOU  334  CA  LEU A  56     9803  10255  19602    943  -2723   1691       C  
ATOM    335  C   LEU A  56      25.266 -22.811  31.223  1.00102.01           C  
ANISOU  335  C   LEU A  56     8860  10099  19802   1221  -2127   1965       C  
ATOM    336  O   LEU A  56      26.161 -23.642  31.408  1.00105.99           O  
ANISOU  336  O   LEU A  56     9033  10513  20724   1443  -2234   2090       O  
ATOM    337  CB  LEU A  56      25.168 -21.571  33.399  1.00108.90           C  
ANISOU  337  CB  LEU A  56    10115  10526  20737    698  -3516   1828       C  
ATOM    338  CG  LEU A  56      24.308 -20.824  34.421  1.00115.38           C  
ANISOU  338  CG  LEU A  56    11587  11190  21063    430  -4050   1586       C  
ATOM    339  CD1 LEU A  56      25.104 -20.562  35.696  1.00117.92           C  
ANISOU  339  CD1 LEU A  56    11889  11143  21771    278  -4951   1632       C  
ATOM    340  CD2 LEU A  56      23.751 -19.529  33.833  1.00108.52           C  
ANISOU  340  CD2 LEU A  56    10721  10424  20089    207  -3798   1607       C  
ATOM    341  N   GLY A  57      25.020 -22.263  30.038  1.00 99.33           N  
ANISOU  341  N   GLY A  57     8368   9972  19402   1238  -1485   2066       N  
ATOM    342  CA  GLY A  57      25.806 -22.593  28.869  1.00104.82           C  
ANISOU  342  CA  GLY A  57     8519  10810  20498   1536   -820   2342       C  
ATOM    343  C   GLY A  57      25.062 -23.356  27.801  1.00104.09           C  
ANISOU  343  C   GLY A  57     8843  10940  19766   1830   -110   2177       C  
ATOM    344  O   GLY A  57      25.632 -23.594  26.730  1.00116.73           O  
ANISOU  344  O   GLY A  57    10097  12662  21593   2123    522   2393       O  
ATOM    345  N   MET A  58      23.818 -23.757  28.048  1.00 96.81           N  
ANISOU  345  N   MET A  58     8661  10054  18067   1777   -193   1820       N  
ATOM    346  CA  MET A  58      23.036 -24.415  27.014  1.00 94.98           C  
ANISOU  346  CA  MET A  58     8862   9993  17233   2015    397   1659       C  
ATOM    347  C   MET A  58      22.369 -23.379  26.124  1.00 92.53           C  
ANISOU  347  C   MET A  58     8650   9838  16668   1868    779   1679       C  
ATOM    348  O   MET A  58      21.707 -22.457  26.612  1.00 98.98           O  
ANISOU  348  O   MET A  58     9647  10635  17324   1533    469   1587       O  
ATOM    349  CB  MET A  58      21.977 -25.336  27.615  1.00 87.31           C  
ANISOU  349  CB  MET A  58     8596   8975  15603   2009    140   1307       C  
ATOM    350  CG  MET A  58      21.184 -26.073  26.543  1.00 92.27           C  
ANISOU  350  CG  MET A  58     9680   9728  15651   2244    663   1145       C  
ATOM    351  SD  MET A  58      19.886 -27.157  27.158  1.00 95.02           S  
ANISOU  351  SD  MET A  58    10810  10002  15292   2201    379    784       S  
ATOM    352  CE  MET A  58      20.279 -27.186  28.888  1.00 84.44           C  
ANISOU  352  CE  MET A  58     9398   8465  14221   2001   -364    776       C  
ATOM    353  N   GLU A  59      22.552 -23.534  24.816  1.00 99.56           N  
ANISOU  353  N   GLU A  59     9457  10866  17504   2146   1456   1803       N  
ATOM    354  CA  GLU A  59      21.864 -22.690  23.851  1.00 94.88           C  
ANISOU  354  CA  GLU A  59     9050  10414  16587   2058   1854   1810       C  
ATOM    355  C   GLU A  59      20.358 -22.885  23.979  1.00 87.85           C  
ANISOU  355  C   GLU A  59     8889   9552  14937   1922   1694   1447       C  
ATOM    356  O   GLU A  59      19.879 -24.003  24.183  1.00 85.90           O  
ANISOU  356  O   GLU A  59     9056   9265  14316   2064   1604   1222       O  
ATOM    357  CB  GLU A  59      22.337 -23.042  22.438  1.00104.21           C  
ANISOU  357  CB  GLU A  59    10130  11708  17755   2461   2620   1989       C  
ATOM    358  CG  GLU A  59      23.313 -22.048  21.827  1.00115.19           C  
ANISOU  358  CG  GLU A  59    10864  13152  19752   2457   2998   2410       C  
ATOM    359  CD  GLU A  59      23.177 -21.951  20.319  1.00130.09           C  
ANISOU  359  CD  GLU A  59    12994  15181  21252   2696   3729   2498       C  
ATOM    360  OE1 GLU A  59      22.363 -21.129  19.839  1.00129.12           O  
ANISOU  360  OE1 GLU A  59    13110  15122  20828   2552   3867   2455       O  
ATOM    361  OE2 GLU A  59      23.897 -22.690  19.614  1.00128.86           O1-
ANISOU  361  OE2 GLU A  59    12872  15064  21023   2992   4102   2594       O1-
ATOM    362  N   ALA A  60      19.608 -21.783  23.883  1.00 83.88           N  
ANISOU  362  N   ALA A  60     8522   9103  14245   1637   1642   1410       N  
ATOM    363  CA  ALA A  60      18.152 -21.881  23.963  1.00 82.00           C  
ANISOU  363  CA  ALA A  60     8906   8897  13354   1506   1516   1109       C  
ATOM    364  C   ALA A  60      17.603 -22.794  22.875  1.00 82.94           C  
ANISOU  364  C   ALA A  60     9447   9081  12984   1795   1934    982       C  
ATOM    365  O   ALA A  60      16.653 -23.552  23.106  1.00 73.86           O  
ANISOU  365  O   ALA A  60     8779   7897  11387   1787   1764    733       O  
ATOM    366  CB  ALA A  60      17.524 -20.492  23.863  1.00 74.36           C  
ANISOU  366  CB  ALA A  60     7967   7977  12310   1210   1467   1128       C  
ATOM    367  N   SER A  61      18.200 -22.742  21.684  1.00 79.58           N  
ANISOU  367  N   SER A  61     8867   8728  12643   2060   2479   1166       N  
ATOM    368  CA  SER A  61      17.768 -23.601  20.589  1.00 72.02           C  
ANISOU  368  CA  SER A  61     8379   7791  11196   2381   2866   1046       C  
ATOM    369  C   SER A  61      17.935 -25.078  20.933  1.00 84.92           C  
ANISOU  369  C   SER A  61    10218   9317  12729   2629   2746    897       C  
ATOM    370  O   SER A  61      17.120 -25.914  20.522  1.00 80.09           O  
ANISOU  370  O   SER A  61    10167   8653  11609   2751   2754    673       O  
ATOM    371  CB  SER A  61      18.554 -23.245  19.327  1.00 90.29           C  
ANISOU  371  CB  SER A  61    10480  10182  13645   2670   3510   1312       C  
ATOM    372  OG  SER A  61      18.695 -24.370  18.482  1.00111.14           O  
ANISOU  372  OG  SER A  61    13467  12786  15975   3114   3880   1246       O  
ATOM    373  N   GLU A  62      18.988 -25.421  21.684  1.00 92.75           N  
ANISOU  373  N   GLU A  62    10770  10249  14222   2701   2597   1026       N  
ATOM    374  CA  GLU A  62      19.190 -26.808  22.100  1.00 84.27           C  
ANISOU  374  CA  GLU A  62     9880   9053  13084   2933   2442    894       C  
ATOM    375  C   GLU A  62      18.053 -27.295  22.988  1.00 76.40           C  
ANISOU  375  C   GLU A  62     9354   7972  11702   2682   1934    610       C  
ATOM    376  O   GLU A  62      17.461 -28.352  22.735  1.00 75.84           O  
ANISOU  376  O   GLU A  62     9774   7818  11224   2834   1925    415       O  
ATOM    377  CB  GLU A  62      20.515 -26.958  22.844  1.00 84.78           C  
ANISOU  377  CB  GLU A  62     9342   9057  13814   3017   2297   1105       C  
ATOM    378  CG  GLU A  62      21.239 -28.251  22.552  1.00104.88           C  
ANISOU  378  CG  GLU A  62    11906  11518  16427   3476   2515   1118       C  
ATOM    379  CD  GLU A  62      22.556 -28.340  23.281  1.00120.99           C  
ANISOU  379  CD  GLU A  62    13288  13490  19192   3554   2344   1355       C  
ATOM    380  OE1 GLU A  62      23.451 -27.517  22.992  1.00127.76           O  
ANISOU  380  OE1 GLU A  62    13529  14418  20597   3564   2590   1672       O  
ATOM    381  OE2 GLU A  62      22.681 -29.219  24.162  1.00108.82           O1-
ANISOU  381  OE2 GLU A  62    11840  11810  17696   3590   1935   1240       O1-
ATOM    382  N   ALA A  63      17.766 -26.555  24.061  1.00 78.49           N  
ANISOU  382  N   ALA A  63     9483   8234  12105   2310   1504    600       N  
ATOM    383  CA  ALA A  63      16.719 -26.972  24.984  1.00 71.14           C  
ANISOU  383  CA  ALA A  63     8969   7226  10834   2087   1075    377       C  
ATOM    384  C   ALA A  63      15.394 -27.150  24.261  1.00 66.75           C  
ANISOU  384  C   ALA A  63     8931   6705   9727   2042   1207    199       C  
ATOM    385  O   ALA A  63      14.667 -28.120  24.509  1.00 66.55           O  
ANISOU  385  O   ALA A  63     9314   6581   9391   2046   1031     31       O  
ATOM    386  CB  ALA A  63      16.582 -25.951  26.111  1.00 68.25           C  
ANISOU  386  CB  ALA A  63     8430   6855  10647   1734    675    408       C  
ATOM    387  N   ASP A  64      15.078 -26.237  23.342  1.00 67.80           N  
ANISOU  387  N   ASP A  64     9050   6954   9756   1997   1494    251       N  
ATOM    388  CA  ASP A  64      13.794 -26.293  22.653  1.00 62.22           C  
ANISOU  388  CA  ASP A  64     8814   6263   8564   1931   1555     95       C  
ATOM    389  C   ASP A  64      13.634 -27.603  21.896  1.00 65.22           C  
ANISOU  389  C   ASP A  64     9612   6531   8636   2230   1686    -28       C  
ATOM    390  O   ASP A  64      12.657 -28.333  22.097  1.00 64.59           O  
ANISOU  390  O   ASP A  64     9935   6350   8256   2140   1443   -196       O  
ATOM    391  CB  ASP A  64      13.646 -25.100  21.707  1.00 61.93           C  
ANISOU  391  CB  ASP A  64     8690   6351   8489   1882   1853    195       C  
ATOM    392  CG  ASP A  64      12.231 -24.951  21.192  1.00 68.60           C  
ANISOU  392  CG  ASP A  64     9972   7202   8892   1744   1799     44       C  
ATOM    393  OD1 ASP A  64      11.858 -25.725  20.282  1.00 72.45           O  
ANISOU  393  OD1 ASP A  64    10859   7617   9051   1947   1929    -56       O  
ATOM    394  OD2 ASP A  64      11.489 -24.087  21.707  1.00 72.88           O1-
ANISOU  394  OD2 ASP A  64    10474   7796   9421   1446   1601     26       O1-
ATOM    395  N   ALA A  65      14.591 -27.926  21.027  1.00 69.62           N  
ANISOU  395  N   ALA A  65    10091   7085   9276   2598   2072     67       N  
ATOM    396  CA  ALA A  65      14.495 -29.175  20.285  1.00 67.55           C  
ANISOU  396  CA  ALA A  65    10297   6681   8690   2932   2193    -64       C  
ATOM    397  C   ALA A  65      14.570 -30.377  21.213  1.00 72.57           C  
ANISOU  397  C   ALA A  65    11042   7160   9373   2961   1851   -170       C  
ATOM    398  O   ALA A  65      13.914 -31.398  20.967  1.00 72.03           O  
ANISOU  398  O   ALA A  65    11478   6928   8965   3042   1710   -344       O  
ATOM    399  CB  ALA A  65      15.596 -29.247  19.233  1.00 73.86           C  
ANISOU  399  CB  ALA A  65    10984   7506   9575   3377   2736     85       C  
ATOM    400  N   SER A  66      15.356 -30.275  22.285  1.00 69.69           N  
ANISOU  400  N   SER A  66    10235   6815   9431   2887   1676    -61       N  
ATOM    401  CA  SER A  66      15.474 -31.388  23.220  1.00 72.18           C  
ANISOU  401  CA  SER A  66    10662   6969   9793   2918   1336   -143       C  
ATOM    402  C   SER A  66      14.165 -31.621  23.960  1.00 65.30           C  
ANISOU  402  C   SER A  66    10143   6028   8641   2572    932   -294       C  
ATOM    403  O   SER A  66      13.726 -32.769  24.115  1.00 61.40           O  
ANISOU  403  O   SER A  66    10034   5359   7937   2627    743   -418       O  
ATOM    404  CB  SER A  66      16.609 -31.121  24.206  1.00 77.76           C  
ANISOU  404  CB  SER A  66    10825   7695  11025   2905   1188     21       C  
ATOM    405  OG  SER A  66      16.783 -32.218  25.079  1.00 80.24           O  
ANISOU  405  OG  SER A  66    11273   7840  11376   2967    859    -49       O  
ATOM    406  N   LEU A  67      13.526 -30.541  24.411  1.00 60.42           N  
ANISOU  406  N   LEU A  67     9397   5532   8029   2226    815   -266       N  
ATOM    407  CA  LEU A  67      12.262 -30.667  25.123  1.00 57.72           C  
ANISOU  407  CA  LEU A  67     9337   5140   7452   1915    504   -364       C  
ATOM    408  C   LEU A  67      11.149 -31.119  24.187  1.00 59.76           C  
ANISOU  408  C   LEU A  67    10038   5333   7336   1906    553   -486       C  
ATOM    409  O   LEU A  67      10.312 -31.947  24.565  1.00 60.43           O  
ANISOU  409  O   LEU A  67    10437   5276   7248   1789    307   -566       O  
ATOM    410  CB  LEU A  67      11.902 -29.335  25.785  1.00 52.75           C  
ANISOU  410  CB  LEU A  67     8469   4651   6922   1604    412   -298       C  
ATOM    411  CG  LEU A  67      12.821 -28.907  26.935  1.00 55.98           C  
ANISOU  411  CG  LEU A  67     8535   5061   7674   1549    208   -197       C  
ATOM    412  CD1 LEU A  67      12.714 -27.416  27.164  1.00 52.61           C  
ANISOU  412  CD1 LEU A  67     7863   4761   7364   1328    203   -124       C  
ATOM    413  CD2 LEU A  67      12.494 -29.668  28.220  1.00 54.21           C  
ANISOU  413  CD2 LEU A  67     8528   4697   7370   1446   -152   -246       C  
ATOM    414  N   ARG A  68      11.108 -30.571  22.968  1.00 58.37           N  
ANISOU  414  N   ARG A  68     9902   5236   7041   2019    844   -483       N  
ATOM    415  CA  ARG A  68      10.074 -30.975  22.023  1.00 57.37           C  
ANISOU  415  CA  ARG A  68    10234   5008   6555   2021    824   -602       C  
ATOM    416  C   ARG A  68      10.204 -32.450  21.674  1.00 60.67           C  
ANISOU  416  C   ARG A  68    11044   5200   6807   2269    740   -710       C  
ATOM    417  O   ARG A  68       9.197 -33.152  21.516  1.00 60.48           O  
ANISOU  417  O   ARG A  68    11307   5097   6574   2091    470   -775       O  
ATOM    418  CB  ARG A  68      10.139 -30.107  20.766  1.00 59.01           C  
ANISOU  418  CB  ARG A  68    10458   5323   6640   2140   1154   -570       C  
ATOM    419  CG  ARG A  68       9.694 -28.659  21.021  1.00 55.00           C  
ANISOU  419  CG  ARG A  68     9652   5008   6238   1841   1169   -483       C  
ATOM    420  CD  ARG A  68       9.502 -27.892  19.731  1.00 60.80           C  
ANISOU  420  CD  ARG A  68    10508   5810   6784   1929   1438   -462       C  
ATOM    421  NE  ARG A  68       9.375 -26.459  19.969  1.00 56.70           N  
ANISOU  421  NE  ARG A  68     9649   5468   6425   1696   1496   -353       N  
ATOM    422  CZ  ARG A  68       8.238 -25.838  20.262  1.00 59.06           C  
ANISOU  422  CZ  ARG A  68     9980   5805   6654   1400   1290   -383       C  
ATOM    423  NH1 ARG A  68       7.088 -26.491  20.321  1.00 61.37           N1+
ANISOU  423  NH1 ARG A  68    10582   5981   6755   1273   1020   -493       N1+
ATOM    424  NH2 ARG A  68       8.255 -24.524  20.482  1.00 64.17           N  
ANISOU  424  NH2 ARG A  68    10332   6595   7454   1232   1357   -285       N  
ATOM    425  N   ALA A  69      11.436 -32.945  21.563  1.00 62.95           N  
ANISOU  425  N   ALA A  69    11212   5472   7235   2599    926   -672       N  
ATOM    426  CA  ALA A  69      11.625 -34.361  21.268  1.00 69.79           C  
ANISOU  426  CA  ALA A  69    12342   6217   7958   2762    812   -739       C  
ATOM    427  C   ALA A  69      11.063 -35.233  22.387  1.00 70.00           C  
ANISOU  427  C   ALA A  69    12484   6099   8013   2539    398   -784       C  
ATOM    428  O   ALA A  69      10.303 -36.176  22.133  1.00 69.04           O  
ANISOU  428  O   ALA A  69    12685   5872   7674   2436    162   -848       O  
ATOM    429  CB  ALA A  69      13.105 -34.651  21.034  1.00 67.81           C  
ANISOU  429  CB  ALA A  69    11872   5987   7907   3163   1116   -666       C  
ATOM    430  N   THR A  70      11.416 -34.920  23.639  1.00 66.88           N  
ANISOU  430  N   THR A  70    11836   5686   7889   2457    289   -724       N  
ATOM    431  CA  THR A  70      10.900 -35.682  24.776  1.00 64.09           C  
ANISOU  431  CA  THR A  70    11592   5212   7547   2232    -78   -730       C  
ATOM    432  C   THR A  70       9.379 -35.644  24.828  1.00 71.53           C  
ANISOU  432  C   THR A  70    12724   6159   8294   1860   -276   -742       C  
ATOM    433  O   THR A  70       8.735 -36.633  25.195  1.00 63.22           O  
ANISOU  433  O   THR A  70    11863   5001   7158   1710   -528   -742       O  
ATOM    434  CB  THR A  70      11.487 -35.142  26.084  1.00 61.83           C  
ANISOU  434  CB  THR A  70    10988   4960   7545   2158   -183   -634       C  
ATOM    435  CG2 THR A  70      11.140 -36.035  27.253  1.00 72.09           C  
ANISOU  435  CG2 THR A  70    12470   6093   8828   2010   -526   -626       C  
ATOM    436  OG1 THR A  70      12.910 -35.032  25.965  1.00 74.68           O  
ANISOU  436  OG1 THR A  70    12290   6640   9445   2462     -5   -569       O  
ATOM    437  N   LEU A  71       8.788 -34.522  24.446  1.00 55.03           N  
ANISOU  437  N   LEU A  71    10559   4186   6162   1716   -158   -732       N  
ATOM    438  CA  LEU A  71       7.351 -34.339  24.557  1.00 52.51           C  
ANISOU  438  CA  LEU A  71    10333   3881   5737   1372   -330   -710       C  
ATOM    439  C   LEU A  71       6.606 -34.759  23.304  1.00 56.70           C  
ANISOU  439  C   LEU A  71    11111   4379   6052   1366   -383   -761       C  
ATOM    440  O   LEU A  71       5.381 -34.606  23.257  1.00 66.78           O  
ANISOU  440  O   LEU A  71    12437   5650   7287   1099   -542   -726       O  
ATOM    441  CB  LEU A  71       7.029 -32.874  24.863  1.00 55.86           C  
ANISOU  441  CB  LEU A  71    10532   4453   6241   1201   -210   -660       C  
ATOM    442  CG  LEU A  71       7.512 -32.368  26.220  1.00 52.06           C  
ANISOU  442  CG  LEU A  71     9747   4084   5950   1099   -244   -566       C  
ATOM    443  CD1 LEU A  71       7.467 -30.831  26.326  1.00 53.84           C  
ANISOU  443  CD1 LEU A  71     9661   4538   6256    968    -98   -506       C  
ATOM    444  CD2 LEU A  71       6.736 -33.019  27.358  1.00 58.83           C  
ANISOU  444  CD2 LEU A  71    10746   4822   6783    886   -484   -512       C  
ATOM    445  N   ASP A  72       7.308 -35.288  22.302  1.00 63.36           N  
ANISOU  445  N   ASP A  72    12118   5188   6767   1664   -267   -825       N  
ATOM    446  CA  ASP A  72       6.728 -35.424  20.975  1.00 64.35           C  
ANISOU  446  CA  ASP A  72    12514   5286   6649   1704   -298   -866       C  
ATOM    447  C   ASP A  72       5.423 -36.197  21.046  1.00 68.94           C  
ANISOU  447  C   ASP A  72    13294   5728   7171   1434   -682   -852       C  
ATOM    448  O   ASP A  72       5.382 -37.324  21.545  1.00 64.95           O  
ANISOU  448  O   ASP A  72    12901   5087   6690   1409   -891   -849       O  
ATOM    449  CB  ASP A  72       7.715 -36.118  20.033  1.00 78.07           C  
ANISOU  449  CB  ASP A  72    14461   6973   8228   2089   -132   -920       C  
ATOM    450  CG  ASP A  72       7.164 -36.266  18.623  1.00 89.22           C  
ANISOU  450  CG  ASP A  72    16233   8330   9338   2163   -186   -951       C  
ATOM    451  OD1 ASP A  72       7.122 -35.247  17.895  1.00 89.53           O  
ANISOU  451  OD1 ASP A  72    16238   8483   9296   2200     21   -927       O  
ATOM    452  OD2 ASP A  72       6.763 -37.388  18.246  1.00 84.74           O1-
ANISOU  452  OD2 ASP A  72    16004   7586   8610   2186   -457   -990       O1-
ATOM    453  N   GLY A  73       4.351 -35.569  20.577  1.00 67.24           N  
ANISOU  453  N   GLY A  73    13098   5538   6912   1230   -780   -826       N  
ATOM    454  CA  GLY A  73       3.038 -36.177  20.657  1.00 71.98           C  
ANISOU  454  CA  GLY A  73    13810   6002   7536    955  -1147   -778       C  
ATOM    455  C   GLY A  73       2.147 -35.437  21.631  1.00 79.84           C  
ANISOU  455  C   GLY A  73    14513   7072   8752    624  -1180   -675       C  
ATOM    456  O   GLY A  73       1.027 -35.046  21.297  1.00 91.26           O  
ANISOU  456  O   GLY A  73    15937   8500  10236    416  -1330   -626       O  
ATOM    457  N   ALA A  74       2.655 -35.200  22.826  1.00 60.91           N  
ANISOU  457  N   ALA A  74    11896   4750   6499    591  -1039   -632       N  
ATOM    458  CA  ALA A  74       1.836 -34.608  23.869  1.00 50.20           C  
ANISOU  458  CA  ALA A  74    10310   3444   5320    302  -1049   -512       C  
ATOM    459  C   ALA A  74       1.483 -33.165  23.512  1.00 63.78           C  
ANISOU  459  C   ALA A  74    11877   5307   7050    236   -888   -509       C  
ATOM    460  O   ALA A  74       2.318 -32.439  22.959  1.00 51.49           O  
ANISOU  460  O   ALA A  74    10302   3854   5407    435   -672   -590       O  
ATOM    461  CB  ALA A  74       2.572 -34.653  25.202  1.00 50.01           C  
ANISOU  461  CB  ALA A  74    10158   3454   5389    327   -946   -467       C  
ATOM    462  N   PRO A  75       0.259 -32.713  23.829  1.00 51.83           N  
ANISOU  462  N   PRO A  75    10234   3795   5664    -37   -971   -398       N  
ATOM    463  CA  PRO A  75      -0.158 -31.343  23.497  1.00 53.22           C  
ANISOU  463  CA  PRO A  75    10274   4091   5858   -107   -838   -389       C  
ATOM    464  C   PRO A  75       0.382 -30.351  24.519  1.00 46.86           C  
ANISOU  464  C   PRO A  75     9230   3464   5111   -103   -579   -348       C  
ATOM    465  O   PRO A  75      -0.348 -29.772  25.353  1.00 42.05           O  
ANISOU  465  O   PRO A  75     8401   2959   4618   -284   -519   -216       O  
ATOM    466  CB  PRO A  75      -1.687 -31.451  23.519  1.00 55.06           C  
ANISOU  466  CB  PRO A  75    10425   4239   6256   -389  -1052   -252       C  
ATOM    467  CG  PRO A  75      -1.979 -32.553  24.485  1.00 54.28           C  
ANISOU  467  CG  PRO A  75    10307   4032   6284   -512  -1168   -136       C  
ATOM    468  CD  PRO A  75      -0.744 -33.397  24.657  1.00 53.56           C  
ANISOU  468  CD  PRO A  75    10389   3910   6053   -289  -1144   -244       C  
ATOM    469  N   ILE A  76       1.703 -30.180  24.497  1.00 45.55           N  
ANISOU  469  N   ILE A  76     9046   3382   4878    124   -417   -434       N  
ATOM    470  CA  ILE A  76       2.405 -29.349  25.468  1.00 42.78           C  
ANISOU  470  CA  ILE A  76     8436   3218   4602    145   -242   -390       C  
ATOM    471  C   ILE A  76       3.310 -28.388  24.702  1.00 43.46           C  
ANISOU  471  C   ILE A  76     8399   3449   4663    313    -40   -449       C  
ATOM    472  O   ILE A  76       4.099 -28.821  23.847  1.00 43.15           O  
ANISOU  472  O   ILE A  76     8487   3353   4554    533     25   -527       O  
ATOM    473  CB  ILE A  76       3.226 -30.198  26.449  1.00 47.61           C  
ANISOU  473  CB  ILE A  76     9091   3748   5250    231   -302   -384       C  
ATOM    474  CG1 ILE A  76       2.275 -31.073  27.279  1.00 49.08           C  
ANISOU  474  CG1 ILE A  76     9397   3790   5463     44   -467   -282       C  
ATOM    475  CG2 ILE A  76       4.020 -29.288  27.399  1.00 41.78           C  
ANISOU  475  CG2 ILE A  76     8122   3163   4590    261   -198   -349       C  
ATOM    476  CD1 ILE A  76       2.946 -32.202  27.926  1.00 56.79           C  
ANISOU  476  CD1 ILE A  76    10528   4613   6438    140   -585   -288       C  
ATOM    477  N   ASP A  77       3.180 -27.092  24.995  1.00 42.40           N  
ANISOU  477  N   ASP A  77     8035   3486   4588    224     77   -398       N  
ATOM    478  CA  ASP A  77       3.986 -26.056  24.371  1.00 43.23           C  
ANISOU  478  CA  ASP A  77     7985   3724   4717    337    268   -410       C  
ATOM    479  C   ASP A  77       5.332 -25.920  25.075  1.00 45.73           C  
ANISOU  479  C   ASP A  77     8113   4082   5182    449    323   -388       C  
ATOM    480  O   ASP A  77       5.495 -26.270  26.246  1.00 39.96           O  
ANISOU  480  O   ASP A  77     7361   3310   4514    402    195   -365       O  
ATOM    481  CB  ASP A  77       3.251 -24.699  24.394  1.00 36.52           C  
ANISOU  481  CB  ASP A  77     6985   3005   3888    184    327   -359       C  
ATOM    482  CG  ASP A  77       2.036 -24.690  23.485  1.00 41.44           C  
ANISOU  482  CG  ASP A  77     7748   3585   4412     98    260   -367       C  
ATOM    483  OD1 ASP A  77       2.240 -24.941  22.301  1.00 44.54           O  
ANISOU  483  OD1 ASP A  77     8314   3920   4687    225    286   -425       O  
ATOM    484  OD2 ASP A  77       0.902 -24.422  23.946  1.00 41.59           O1-
ANISOU  484  OD2 ASP A  77     7711   3615   4477    -76    182   -305       O1-
ATOM    485  N   VAL A  78       6.305 -25.387  24.341  1.00 45.35           N  
ANISOU  485  N   VAL A  78     7924   4102   5203    601    508   -374       N  
ATOM    486  CA  VAL A  78       7.645 -25.149  24.860  1.00 40.10           C  
ANISOU  486  CA  VAL A  78     7001   3468   4767    702    548   -316       C  
ATOM    487  C   VAL A  78       8.046 -23.720  24.524  1.00 45.38           C  
ANISOU  487  C   VAL A  78     7410   4261   5570    660    698   -235       C  
ATOM    488  O   VAL A  78       7.991 -23.315  23.357  1.00 46.11           O  
ANISOU  488  O   VAL A  78     7530   4404   5585    732    909   -218       O  
ATOM    489  CB  VAL A  78       8.677 -26.119  24.262  1.00 44.50           C  
ANISOU  489  CB  VAL A  78     7585   3954   5370    978    664   -327       C  
ATOM    490  CG1 VAL A  78      10.060 -25.806  24.813  1.00 51.65           C  
ANISOU  490  CG1 VAL A  78     8137   4885   6601   1067    684   -228       C  
ATOM    491  CG2 VAL A  78       8.282 -27.585  24.538  1.00 43.93           C  
ANISOU  491  CG2 VAL A  78     7814   3718   5157   1025    486   -413       C  
ATOM    492  N   VAL A  79       8.489 -22.978  25.528  1.00 39.11           N  
ANISOU  492  N   VAL A  79     6403   3487   4971    554    571   -180       N  
ATOM    493  CA  VAL A  79       9.093 -21.666  25.315  1.00 41.20           C  
ANISOU  493  CA  VAL A  79     6392   3824   5440    509    661    -80       C  
ATOM    494  C   VAL A  79      10.377 -21.619  26.132  1.00 50.45           C  
ANISOU  494  C   VAL A  79     7290   4936   6944    542    511      1       C  
ATOM    495  O   VAL A  79      10.481 -22.239  27.193  1.00 49.91           O  
ANISOU  495  O   VAL A  79     7301   4777   6886    529    263    -42       O  
ATOM    496  CB  VAL A  79       8.153 -20.483  25.695  1.00 43.40           C  
ANISOU  496  CB  VAL A  79     6712   4146   5632    305    578    -92       C  
ATOM    497  CG1 VAL A  79       6.804 -20.600  24.996  1.00 42.59           C  
ANISOU  497  CG1 VAL A  79     6848   4082   5252    262    664   -157       C  
ATOM    498  CG2 VAL A  79       7.947 -20.379  27.199  1.00 43.58           C  
ANISOU  498  CG2 VAL A  79     6804   4100   5657    196    300   -125       C  
ATOM    499  N   VAL A  80      11.372 -20.899  25.619  1.00 45.27           N  
ANISOU  499  N   VAL A  80     6305   4313   6583    584    652    140       N  
ATOM    500  CA  VAL A  80      12.642 -20.707  26.309  1.00 44.96           C  
ANISOU  500  CA  VAL A  80     5925   4198   6959    590    473    259       C  
ATOM    501  C   VAL A  80      12.975 -19.223  26.279  1.00 48.79           C  
ANISOU  501  C   VAL A  80     6150   4691   7696    428    439    386       C  
ATOM    502  O   VAL A  80      12.790 -18.560  25.252  1.00 50.06           O  
ANISOU  502  O   VAL A  80     6257   4941   7821    425    730    456       O  
ATOM    503  CB  VAL A  80      13.782 -21.527  25.669  1.00 49.71           C  
ANISOU  503  CB  VAL A  80     6285   4796   7805    844    696    368       C  
ATOM    504  CG1 VAL A  80      15.058 -21.391  26.483  1.00 55.60           C  
ANISOU  504  CG1 VAL A  80     6636   5441   9047    837    442    508       C  
ATOM    505  CG2 VAL A  80      13.383 -23.009  25.547  1.00 53.34           C  
ANISOU  505  CG2 VAL A  80     7070   5221   7974   1023    737    227       C  
ATOM    506  N   GLN A  81      13.466 -18.703  27.400  1.00 45.83           N  
ANISOU  506  N   GLN A  81     5654   4194   7566    295     56    418       N  
ATOM    507  CA  GLN A  81      13.753 -17.275  27.489  1.00 52.77           C  
ANISOU  507  CA  GLN A  81     6332   5026   8694    116    -66    528       C  
ATOM    508  C   GLN A  81      14.701 -17.031  28.658  1.00 50.93           C  
ANISOU  508  C   GLN A  81     5916   4599   8836     28   -546    592       C  
ATOM    509  O   GLN A  81      14.936 -17.912  29.485  1.00 55.83           O  
ANISOU  509  O   GLN A  81     6641   5132   9438     99   -794    522       O  
ATOM    510  CB  GLN A  81      12.464 -16.473  27.661  1.00 49.11           C  
ANISOU  510  CB  GLN A  81     6209   4589   7862    -22   -106    397       C  
ATOM    511  CG  GLN A  81      11.840 -16.698  29.021  1.00 51.84           C  
ANISOU  511  CG  GLN A  81     6907   4830   7958    -72   -457    235       C  
ATOM    512  CD  GLN A  81      10.427 -16.188  29.114  1.00 46.12           C  
ANISOU  512  CD  GLN A  81     6524   4161   6839   -137   -389    113       C  
ATOM    513  NE2 GLN A  81       9.524 -17.038  29.592  1.00 42.35           N  
ANISOU  513  NE2 GLN A  81     6354   3707   6030    -86   -377     -6       N  
ATOM    514  OE1 GLN A  81      10.145 -15.041  28.779  1.00 44.00           O  
ANISOU  514  OE1 GLN A  81     6228   3902   6588   -231   -348    144       O  
ATOM    515  N   GLU A  82      15.242 -15.812  28.713  1.00 56.96           N  
ANISOU  515  N   GLU A  82     6426   5269   9948   -134   -712    733       N  
ATOM    516  CA  GLU A  82      15.999 -15.388  29.885  1.00 55.62           C  
ANISOU  516  CA  GLU A  82     6165   4860  10110   -259  -1283    775       C  
ATOM    517  C   GLU A  82      15.056 -15.209  31.066  1.00 58.59           C  
ANISOU  517  C   GLU A  82     7098   5124  10038   -322  -1637    542       C  
ATOM    518  O   GLU A  82      13.949 -14.683  30.920  1.00 58.66           O  
ANISOU  518  O   GLU A  82     7418   5210   9659   -362  -1482    426       O  
ATOM    519  CB  GLU A  82      16.741 -14.081  29.602  1.00 61.09           C  
ANISOU  519  CB  GLU A  82     6469   5445  11298   -442  -1401    994       C  
ATOM    520  CG  GLU A  82      17.812 -14.193  28.541  1.00 67.99           C  
ANISOU  520  CG  GLU A  82     6738   6402  12695   -374  -1038   1290       C  
ATOM    521  CD  GLU A  82      18.312 -12.839  28.068  1.00 79.25           C  
ANISOU  521  CD  GLU A  82     7806   7749  14556   -574  -1039   1535       C  
ATOM    522  OE1 GLU A  82      17.762 -11.799  28.494  1.00 77.72           O  
ANISOU  522  OE1 GLU A  82     7874   7437  14220   -762  -1325   1446       O  
ATOM    523  OE2 GLU A  82      19.262 -12.819  27.264  1.00 81.18           O1-
ANISOU  523  OE2 GLU A  82     7510   8039  15294   -529   -735   1834       O1-
ATOM    524  N   GLN A  83      15.496 -15.644  32.248  1.00 60.65           N  
ANISOU  524  N   GLN A  83     7501   5194  10350   -307  -2107    488       N  
ATOM    525  CA  GLN A  83      14.602 -15.590  33.399  1.00 63.54           C  
ANISOU  525  CA  GLN A  83     8462   5450  10231   -311  -2381    282       C  
ATOM    526  C   GLN A  83      14.379 -14.158  33.869  1.00 63.55           C  
ANISOU  526  C   GLN A  83     8658   5282  10207   -461  -2679    251       C  
ATOM    527  O   GLN A  83      13.253 -13.788  34.228  1.00 59.91           O  
ANISOU  527  O   GLN A  83     8651   4840   9273   -442  -2604    100       O  
ATOM    528  CB  GLN A  83      15.144 -16.456  34.537  1.00 70.55           C  
ANISOU  528  CB  GLN A  83     9521   6152  11131   -232  -2811    238       C  
ATOM    529  CG  GLN A  83      14.636 -16.055  35.924  1.00 78.89           C  
ANISOU  529  CG  GLN A  83    11182   6985  11807   -248  -3249     82       C  
ATOM    530  CD  GLN A  83      13.175 -16.441  36.159  1.00 67.14           C  
ANISOU  530  CD  GLN A  83    10200   5634   9676   -153  -2915    -77       C  
ATOM    531  NE2 GLN A  83      12.473 -15.646  36.963  1.00 77.78           N  
ANISOU  531  NE2 GLN A  83    12030   6855  10668   -159  -3077   -186       N  
ATOM    532  OE1 GLN A  83      12.690 -17.438  35.630  1.00 65.04           O  
ANISOU  532  OE1 GLN A  83     9893   5566   9253    -68  -2523    -88       O  
ATOM    533  N   GLU A  84      15.418 -13.319  33.801  1.00 59.10           N  
ANISOU  533  N   GLU A  84     7734   4546  10174   -605  -2991    413       N  
ATOM    534  CA  GLU A  84      15.438 -12.089  34.585  1.00 71.61           C  
ANISOU  534  CA  GLU A  84     9584   5851  11775   -742  -3490    369       C  
ATOM    535  C   GLU A  84      14.287 -11.154  34.237  1.00 77.33           C  
ANISOU  535  C   GLU A  84    10599   6664  12119   -770  -3218    269       C  
ATOM    536  O   GLU A  84      13.682 -10.550  35.130  1.00 90.21           O  
ANISOU  536  O   GLU A  84    12758   8120  13397   -754  -3493    111       O  
ATOM    537  CB  GLU A  84      16.777 -11.370  34.410  1.00 72.37           C  
ANISOU  537  CB  GLU A  84     9154   5740  12605   -927  -3861    608       C  
ATOM    538  CG  GLU A  84      17.767 -11.644  35.535  1.00 95.40           C  
ANISOU  538  CG  GLU A  84    12089   8334  15824   -955  -4571    631       C  
ATOM    539  CD  GLU A  84      17.089 -12.027  36.842  1.00100.61           C  
ANISOU  539  CD  GLU A  84    13510   8849  15867   -822  -4894    367       C  
ATOM    540  OE1 GLU A  84      16.502 -11.136  37.501  1.00113.46           O  
ANISOU  540  OE1 GLU A  84    15603  10463  17043   -777  -5044    251       O  
ATOM    541  OE2 GLU A  84      17.111 -13.229  37.192  1.00107.66           O1-
ANISOU  541  OE2 GLU A  84    14501   9807  16597   -670  -4848    312       O1-
ATOM    542  N   ARG A  85      13.968 -11.003  32.961  1.00 61.40           N  
ANISOU  542  N   ARG A  85     8281   4896  10152   -786  -2689    360       N  
ATOM    543  CA  ARG A  85      13.010  -9.973  32.580  1.00 71.52           C  
ANISOU  543  CA  ARG A  85     9777   6225  11173   -830  -2498    298       C  
ATOM    544  C   ARG A  85      11.712 -10.544  32.018  1.00 55.54           C  
ANISOU  544  C   ARG A  85     7950   4488   8665   -694  -1965    183       C  
ATOM    545  O   ARG A  85      11.020  -9.879  31.242  1.00 53.93           O  
ANISOU  545  O   ARG A  85     7746   4398   8348   -719  -1676    192       O  
ATOM    546  CB  ARG A  85      13.637  -9.000  31.589  1.00 74.97           C  
ANISOU  546  CB  ARG A  85     9763   6649  12075   -995  -2410    517       C  
ATOM    547  CG  ARG A  85      14.818  -8.183  32.129  1.00 92.34           C  
ANISOU  547  CG  ARG A  85    11752   8515  14818  -1184  -2995    663       C  
ATOM    548  CD  ARG A  85      14.747  -6.743  31.612  1.00 92.65           C  
ANISOU  548  CD  ARG A  85    11723   8446  15033  -1356  -3023    767       C  
ATOM    549  NE  ARG A  85      13.367  -6.260  31.619  1.00118.65           N  
ANISOU  549  NE  ARG A  85    15515  11819  17746  -1268  -2822    559       N  
ATOM    550  CZ  ARG A  85      12.554  -6.262  30.569  1.00 97.16           C  
ANISOU  550  CZ  ARG A  85    12751   9371  14795  -1204  -2266    565       C  
ATOM    551  NH1 ARG A  85      12.973  -6.650  29.376  1.00 90.63           N1+
ANISOU  551  NH1 ARG A  85    11469   8754  14212  -1212  -1836    759       N1+
ATOM    552  NH2 ARG A  85      11.279  -5.917  30.732  1.00 68.97           N  
ANISOU  552  NH2 ARG A  85     9626   5854  10725  -1104  -2137    375       N  
ATOM    553  N   ARG A  86      11.339 -11.747  32.450  1.00 53.45           N  
ANISOU  553  N   ARG A  86     7874   4311   8124   -557  -1875     82       N  
ATOM    554  CA  ARG A  86      10.207 -12.438  31.847  1.00 45.85           C  
ANISOU  554  CA  ARG A  86     7021   3598   6801   -454  -1408     12       C  
ATOM    555  C   ARG A  86       8.861 -11.846  32.254  1.00 45.44           C  
ANISOU  555  C   ARG A  86     7384   3555   6328   -414  -1327   -116       C  
ATOM    556  O   ARG A  86       7.892 -11.980  31.506  1.00 42.41           O  
ANISOU  556  O   ARG A  86     7000   3360   5755   -380   -960   -131       O  
ATOM    557  CB  ARG A  86      10.264 -13.921  32.199  1.00 47.40           C  
ANISOU  557  CB  ARG A  86     7278   3850   6881   -339  -1366    -31       C  
ATOM    558  CG  ARG A  86       9.995 -14.190  33.642  1.00 48.64           C  
ANISOU  558  CG  ARG A  86     7875   3843   6762   -276  -1673   -145       C  
ATOM    559  CD  ARG A  86      10.394 -15.616  33.998  1.00 49.25           C  
ANISOU  559  CD  ARG A  86     7954   3925   6834   -185  -1716   -147       C  
ATOM    560  NE  ARG A  86       9.526 -16.603  33.371  1.00 46.71           N  
ANISOU  560  NE  ARG A  86     7651   3809   6287   -115  -1305   -170       N  
ATOM    561  CZ  ARG A  86       9.389 -17.842  33.817  1.00 48.28           C  
ANISOU  561  CZ  ARG A  86     8006   4005   6332    -29  -1298   -199       C  
ATOM    562  NH1 ARG A  86      10.098 -18.285  34.842  1.00 47.04           N1+
ANISOU  562  NH1 ARG A  86     7991   3669   6212     16  -1654   -208       N1+
ATOM    563  NH2 ARG A  86       8.497 -18.644  33.242  1.00 44.25           N  
ANISOU  563  NH2 ARG A  86     7536   3647   5630      6   -966   -213       N  
ATOM    564  N   ARG A  87       8.754 -11.192  33.403  1.00 45.57           N  
ANISOU  564  N   ARG A  87     7766   3356   6192   -398  -1663   -202       N  
ATOM    565  CA  ARG A  87       7.465 -10.636  33.802  1.00 43.82           C  
ANISOU  565  CA  ARG A  87     7937   3143   5569   -307  -1526   -307       C  
ATOM    566  C   ARG A  87       7.340  -9.230  33.234  1.00 46.37           C  
ANISOU  566  C   ARG A  87     8194   3416   6008   -391  -1534   -280       C  
ATOM    567  O   ARG A  87       8.132  -8.350  33.577  1.00 48.98           O  
ANISOU  567  O   ARG A  87     8544   3513   6553   -481  -1918   -260       O  
ATOM    568  CB  ARG A  87       7.301 -10.612  35.319  1.00 54.31           C  
ANISOU  568  CB  ARG A  87     9797   4252   6587   -184  -1822   -419       C  
ATOM    569  CG  ARG A  87       5.843 -10.479  35.737  1.00 50.44           C  
ANISOU  569  CG  ARG A  87     9685   3833   5648    -21  -1519   -493       C  
ATOM    570  CD  ARG A  87       5.695 -10.459  37.252  1.00 62.53           C  
ANISOU  570  CD  ARG A  87    11688   5254   6817    153  -1712   -541       C  
ATOM    571  NE  ARG A  87       5.713 -11.809  37.808  1.00 61.64           N  
ANISOU  571  NE  ARG A  87    11693   5167   6562    221  -1667   -530       N  
ATOM    572  CZ  ARG A  87       5.399 -12.099  39.063  1.00 66.80           C  
ANISOU  572  CZ  ARG A  87    12770   5764   6848    394  -1712   -527       C  
ATOM    573  NH1 ARG A  87       5.057 -11.154  39.925  1.00 63.61           N1+
ANISOU  573  NH1 ARG A  87    12734   5265   6171    540  -1803   -533       N1+
ATOM    574  NH2 ARG A  87       5.427 -13.368  39.463  1.00 69.82           N  
ANISOU  574  NH2 ARG A  87    13240   6161   7128    437  -1659   -500       N  
ATOM    575  N   LYS A  88       6.351  -9.021  32.370  1.00 41.03           N  
ANISOU  575  N   LYS A  88     7446   2933   5211   -369  -1153   -269       N  
ATOM    576  CA  LYS A  88       6.230  -7.784  31.611  1.00 39.37           C  
ANISOU  576  CA  LYS A  88     7129   2702   5129   -451  -1114   -220       C  
ATOM    577  C   LYS A  88       5.198  -6.859  32.242  1.00 40.96           C  
ANISOU  577  C   LYS A  88     7738   2802   5024   -334  -1133   -326       C  
ATOM    578  O   LYS A  88       4.337  -7.286  33.010  1.00 45.07           O  
ANISOU  578  O   LYS A  88     8564   3348   5213   -172  -1019   -411       O  
ATOM    579  CB  LYS A  88       5.855  -8.107  30.157  1.00 40.59           C  
ANISOU  579  CB  LYS A  88     6962   3108   5351   -484   -713   -131       C  
ATOM    580  CG  LYS A  88       6.858  -9.056  29.525  1.00 38.00           C  
ANISOU  580  CG  LYS A  88     6284   2872   5282   -538   -640    -28       C  
ATOM    581  CD  LYS A  88       8.246  -8.402  29.511  1.00 42.19           C  
ANISOU  581  CD  LYS A  88     6565   3233   6233   -673   -912     98       C  
ATOM    582  CE  LYS A  88       9.228  -9.177  28.636  1.00 41.39           C  
ANISOU  582  CE  LYS A  88     6046   3243   6437   -693   -730    250       C  
ATOM    583  NZ  LYS A  88      10.617  -8.676  28.838  1.00 41.17           N1+
ANISOU  583  NZ  LYS A  88     5721   3030   6892   -822  -1025    407       N1+
ATOM    584  N   LYS A  89       5.303  -5.567  31.928  1.00 40.88           N  
ANISOU  584  N   LYS A  89     7738   2659   5135   -404  -1262   -304       N  
ATOM    585  CA  LYS A  89       4.413  -4.571  32.512  1.00 39.52           C  
ANISOU  585  CA  LYS A  89     7974   2352   4689   -266  -1301   -407       C  
ATOM    586  C   LYS A  89       3.490  -3.927  31.487  1.00 39.63           C  
ANISOU  586  C   LYS A  89     7865   2507   4685   -253   -995   -364       C  
ATOM    587  O   LYS A  89       2.784  -2.964  31.815  1.00 43.07           O  
ANISOU  587  O   LYS A  89     8593   2824   4947   -133  -1016   -432       O  
ATOM    588  CB  LYS A  89       5.244  -3.511  33.226  1.00 50.13           C  
ANISOU  588  CB  LYS A  89     9438   3479   6131   -310  -1752   -415       C  
ATOM    589  CG  LYS A  89       5.960  -4.155  34.380  1.00 54.57           C  
ANISOU  589  CG  LYS A  89    10142   3965   6626   -265  -2051   -452       C  
ATOM    590  CD  LYS A  89       6.444  -3.168  35.397  1.00 83.48           C  
ANISOU  590  CD  LYS A  89    14077   7430  10213   -219  -2495   -480       C  
ATOM    591  CE  LYS A  89       7.949  -3.218  35.425  1.00 85.72           C  
ANISOU  591  CE  LYS A  89    14080   7568  10921   -420  -2926   -382       C  
ATOM    592  NZ  LYS A  89       8.364  -4.104  36.547  1.00 67.78           N1+
ANISOU  592  NZ  LYS A  89    12019   5245   8488   -319  -3162   -423       N1+
ATOM    593  N   ILE A  90       3.511  -4.417  30.247  1.00 38.99           N  
ANISOU  593  N   ILE A  90     7393   2653   4771   -356   -733   -254       N  
ATOM    594  CA  ILE A  90       2.582  -4.023  29.193  1.00 37.67           C  
ANISOU  594  CA  ILE A  90     7116   2633   4565   -336   -451   -208       C  
ATOM    595  C   ILE A  90       2.090  -5.299  28.526  1.00 35.89           C  
ANISOU  595  C   ILE A  90     6684   2668   4285   -316   -148   -174       C  
ATOM    596  O   ILE A  90       2.889  -6.196  28.236  1.00 38.00           O  
ANISOU  596  O   ILE A  90     6752   3005   4680   -393   -135   -127       O  
ATOM    597  CB  ILE A  90       3.232  -3.110  28.136  1.00 41.44           C  
ANISOU  597  CB  ILE A  90     7378   3055   5313   -499   -502    -83       C  
ATOM    598  CG1 ILE A  90       3.720  -1.804  28.754  1.00 43.29           C  
ANISOU  598  CG1 ILE A  90     7818   2987   5645   -549   -858   -102       C  
ATOM    599  CG2 ILE A  90       2.258  -2.853  26.961  1.00 37.99           C  
ANISOU  599  CG2 ILE A  90     6855   2777   4804   -466   -218    -32       C  
ATOM    600  CD1 ILE A  90       4.798  -1.102  27.956  1.00 42.65           C  
ANISOU  600  CD1 ILE A  90     7466   2800   5941   -768   -982     71       C  
ATOM    601  N   LEU A  91       0.786  -5.393  28.299  1.00 36.72           N  
ANISOU  601  N   LEU A  91     6837   2891   4222   -207     72   -191       N  
ATOM    602  CA  LEU A  91       0.225  -6.413  27.419  1.00 34.24           C  
ANISOU  602  CA  LEU A  91     6331   2782   3897   -219    299   -143       C  
ATOM    603  C   LEU A  91      -0.374  -5.698  26.222  1.00 36.95           C  
ANISOU  603  C   LEU A  91     6587   3174   4280   -239    395    -82       C  
ATOM    604  O   LEU A  91      -1.150  -4.757  26.387  1.00 37.85           O  
ANISOU  604  O   LEU A  91     6816   3227   4337   -157    394    -98       O  
ATOM    605  CB  LEU A  91      -0.858  -7.242  28.109  1.00 34.96           C  
ANISOU  605  CB  LEU A  91     6509   2952   3823    -99    440   -172       C  
ATOM    606  CG  LEU A  91      -1.661  -8.182  27.196  1.00 34.63           C  
ANISOU  606  CG  LEU A  91     6287   3072   3798   -124    609   -114       C  
ATOM    607  CD1 LEU A  91      -0.818  -9.381  26.681  1.00 36.56           C  
ANISOU  607  CD1 LEU A  91     6409   3378   4103   -214    598   -104       C  
ATOM    608  CD2 LEU A  91      -2.890  -8.666  27.964  1.00 36.23           C  
ANISOU  608  CD2 LEU A  91     6544   3317   3906    -10    751    -94       C  
ATOM    609  N   ILE A  92      -0.032  -6.140  25.019  1.00 37.93           N  
ANISOU  609  N   ILE A  92     6545   3391   4477   -320    480    -12       N  
ATOM    610  CA  ILE A  92      -0.755  -5.684  23.844  1.00 34.62           C  
ANISOU  610  CA  ILE A  92     6098   3019   4039   -317    563     44       C  
ATOM    611  C   ILE A  92      -1.232  -6.947  23.133  1.00 40.48           C  
ANISOU  611  C   ILE A  92     6776   3888   4716   -309    663     52       C  
ATOM    612  O   ILE A  92      -0.434  -7.854  22.856  1.00 33.79           O  
ANISOU  612  O   ILE A  92     5874   3081   3884   -341    703     60       O  
ATOM    613  CB  ILE A  92       0.079  -4.762  22.930  1.00 36.98           C  
ANISOU  613  CB  ILE A  92     6353   3251   4446   -404    552    140       C  
ATOM    614  CG1 ILE A  92      -0.763  -4.276  21.735  1.00 33.65           C  
ANISOU  614  CG1 ILE A  92     5971   2859   3956   -379    616    196       C  
ATOM    615  CG2 ILE A  92       1.393  -5.395  22.488  1.00 39.41           C  
ANISOU  615  CG2 ILE A  92     6519   3588   4867   -478    617    213       C  
ATOM    616  CD1 ILE A  92      -0.106  -3.166  20.936  1.00 38.62           C  
ANISOU  616  CD1 ILE A  92     6606   3396   4672   -452    619    312       C  
ATOM    617  N   ALA A  93      -2.541  -7.054  22.939  1.00 35.45           N  
ANISOU  617  N   ALA A  93     6149   3291   4031   -255    680     54       N  
ATOM    618  CA  ALA A  93      -3.148  -8.298  22.484  1.00 35.16           C  
ANISOU  618  CA  ALA A  93     6070   3327   3962   -261    697     59       C  
ATOM    619  C   ALA A  93      -4.090  -8.039  21.317  1.00 37.33           C  
ANISOU  619  C   ALA A  93     6356   3600   4229   -254    644    108       C  
ATOM    620  O   ALA A  93      -4.896  -7.107  21.353  1.00 36.36           O  
ANISOU  620  O   ALA A  93     6218   3446   4149   -208    617    137       O  
ATOM    621  CB  ALA A  93      -3.917  -8.965  23.629  1.00 36.31           C  
ANISOU  621  CB  ALA A  93     6179   3497   4120   -218    726     46       C  
ATOM    622  N   ASP A  94      -4.001  -8.887  20.298  1.00 34.29           N  
ANISOU  622  N   ASP A  94     6028   3223   3777   -280    607    114       N  
ATOM    623  CA  ASP A  94      -4.901  -8.830  19.158  1.00 39.36           C  
ANISOU  623  CA  ASP A  94     6741   3828   4388   -273    482    152       C  
ATOM    624  C   ASP A  94      -6.308  -9.279  19.544  1.00 36.99           C  
ANISOU  624  C   ASP A  94     6306   3523   4225   -281    368    185       C  
ATOM    625  O   ASP A  94      -6.476 -10.128  20.418  1.00 36.61           O  
ANISOU  625  O   ASP A  94     6158   3507   4246   -302    406    181       O  
ATOM    626  CB  ASP A  94      -4.399  -9.756  18.060  1.00 36.04           C  
ANISOU  626  CB  ASP A  94     6498   3380   3814   -269    451    133       C  
ATOM    627  CG  ASP A  94      -5.301  -9.733  16.876  1.00 36.92           C  
ANISOU  627  CG  ASP A  94     6761   3409   3856   -254    255    160       C  
ATOM    628  OD1 ASP A  94      -5.596  -8.607  16.444  1.00 39.02           O  
ANISOU  628  OD1 ASP A  94     7059   3646   4120   -232    228    209       O  
ATOM    629  OD2 ASP A  94      -5.731 -10.800  16.407  1.00 39.47           O1-
ANISOU  629  OD2 ASP A  94     7190   3672   4134   -264     91    134       O1-
ATOM    630  N   MET A  95      -7.336  -8.763  18.842  1.00 35.82           N  
ANISOU  630  N   MET A  95     5140   3688   4781   -138    706    158       N  
ATOM    631  CA  MET A  95      -8.701  -9.195  19.191  1.00 34.42           C  
ANISOU  631  CA  MET A  95     4898   3588   4592   -121    803    239       C  
ATOM    632  C   MET A  95      -9.149 -10.422  18.394  1.00 38.83           C  
ANISOU  632  C   MET A  95     5340   4190   5224   -240    784    272       C  
ATOM    633  O   MET A  95      -9.284 -11.508  18.963  1.00 37.89           O  
ANISOU  633  O   MET A  95     5248   4049   5100   -301    782    310       O  
ATOM    634  CB  MET A  95      -9.694  -8.036  19.075  1.00 37.73           C  
ANISOU  634  CB  MET A  95     5282   4080   4974    -12    872    272       C  
ATOM    635  CG  MET A  95     -11.105  -8.510  19.477  1.00 38.51           C  
ANISOU  635  CG  MET A  95     5261   4318   5055      7    985    372       C  
ATOM    636  SD  MET A  95     -12.488  -7.429  19.102  1.00 42.11           S  
ANISOU  636  SD  MET A  95     5597   4925   5480    156   1066    419       S  
ATOM    637  CE  MET A  95     -12.350  -7.157  17.329  1.00 41.80           C  
ANISOU  637  CE  MET A  95     5474   4868   5540     75    962    382       C  
ATOM    638  N   ASP A  96      -9.380 -10.277  17.083  1.00 33.17           N  
ANISOU  638  N   ASP A  96     4522   3517   4564   -280    752    260       N  
ATOM    639  CA  ASP A  96     -10.011 -11.370  16.327  1.00 37.90           C  
ANISOU  639  CA  ASP A  96     5031   4149   5218   -392    718    297       C  
ATOM    640  C   ASP A  96      -9.140 -12.616  16.280  1.00 37.05           C  
ANISOU  640  C   ASP A  96     5009   3943   5124   -455    626    247       C  
ATOM    641  O   ASP A  96      -7.976 -12.564  15.866  1.00 35.93           O  
ANISOU  641  O   ASP A  96     4914   3757   4982   -420    568    156       O  
ATOM    642  CB  ASP A  96     -10.317 -10.943  14.897  1.00 36.13           C  
ANISOU  642  CB  ASP A  96     4714   3978   5036   -410    683    281       C  
ATOM    643  CG  ASP A  96     -11.356  -9.867  14.823  1.00 39.50           C  
ANISOU  643  CG  ASP A  96     5054   4503   5451   -335    750    336       C  
ATOM    644  OD1 ASP A  96     -12.457 -10.079  15.344  1.00 40.21           O  
ANISOU  644  OD1 ASP A  96     5052   4688   5537   -337    814    423       O  
ATOM    645  OD2 ASP A  96     -11.059  -8.797  14.243  1.00 41.18           O1-
ANISOU  645  OD2 ASP A  96     5292   4706   5650   -270    735    296       O1-
ATOM    646  N   SER A  97      -9.744 -13.752  16.639  1.00 34.99           N  
ANISOU  646  N   SER A  97     4767   3659   4869   -551    606    314       N  
ATOM    647  CA  SER A  97      -9.119 -15.071  16.702  1.00 40.48           C  
ANISOU  647  CA  SER A  97     5588   4231   5560   -602    498    278       C  
ATOM    648  C   SER A  97      -7.982 -15.124  17.707  1.00 45.79           C  
ANISOU  648  C   SER A  97     6390   4821   6186   -514    484    220       C  
ATOM    649  O   SER A  97      -7.190 -16.069  17.691  1.00 39.86           O  
ANISOU  649  O   SER A  97     5754   3968   5425   -500    380    160       O  
ATOM    650  CB  SER A  97      -8.625 -15.536  15.325  1.00 39.10           C  
ANISOU  650  CB  SER A  97     5421   4021   5415   -606    391    189       C  
ATOM    651  OG  SER A  97      -9.720 -15.649  14.425  1.00 42.51           O  
ANISOU  651  OG  SER A  97     5759   4508   5885   -705    373    247       O  
ATOM    652  N   THR A  98      -7.869 -14.120  18.569  1.00 37.87           N  
ANISOU  652  N   THR A  98     5387   3855   5145   -438    569    232       N  
ATOM    653  CA  THR A  98      -6.883 -14.151  19.643  1.00 36.50           C  
ANISOU  653  CA  THR A  98     5344   3603   4920   -366    542    190       C  
ATOM    654  C   THR A  98      -7.625 -14.012  20.967  1.00 41.35           C  
ANISOU  654  C   THR A  98     6016   4230   5464   -363    635    284       C  
ATOM    655  O   THR A  98      -7.804 -15.020  21.654  1.00 36.86           O  
ANISOU  655  O   THR A  98     5544   3601   4862   -423    613    339       O  
ATOM    656  CB  THR A  98      -5.801 -13.074  19.450  1.00 34.06           C  
ANISOU  656  CB  THR A  98     5020   3310   4611   -280    522    103       C  
ATOM    657  CG2 THR A  98      -4.860 -13.035  20.660  1.00 36.40           C  
ANISOU  657  CG2 THR A  98     5445   3533   4851   -216    478     70       C  
ATOM    658  OG1 THR A  98      -5.023 -13.396  18.285  1.00 33.96           O  
ANISOU  658  OG1 THR A  98     4949   3314   4641   -280    446     24       O  
ATOM    659  N   MET A  99      -8.106 -12.811  21.330  1.00 40.17           N  
ANISOU  659  N   MET A  99     5826   4159   5277   -289    737    308       N  
ATOM    660  CA  MET A  99      -8.872 -12.726  22.574  1.00 40.52           C  
ANISOU  660  CA  MET A  99     5920   4246   5228   -258    844    398       C  
ATOM    661  C   MET A  99     -10.323 -13.158  22.427  1.00 39.31           C  
ANISOU  661  C   MET A  99     5627   4229   5080   -349    939    527       C  
ATOM    662  O   MET A  99     -10.969 -13.433  23.445  1.00 40.82           O  
ANISOU  662  O   MET A  99     5842   4481   5186   -362   1031    627       O  
ATOM    663  CB  MET A  99      -8.792 -11.321  23.199  1.00 38.70           C  
ANISOU  663  CB  MET A  99     5750   4035   4920   -103    905    365       C  
ATOM    664  CG  MET A  99      -7.356 -10.854  23.172  1.00 41.97           C  
ANISOU  664  CG  MET A  99     6272   4331   5345    -63    785    253       C  
ATOM    665  SD  MET A  99      -6.449 -11.626  24.558  1.00 37.92           S  
ANISOU  665  SD  MET A  99     5959   3694   4754    -49    714    238       S  
ATOM    666  CE  MET A  99      -7.636 -11.627  25.915  1.00 39.13           C  
ANISOU  666  CE  MET A  99     6194   3910   4764      9    868    349       C  
ATOM    667  N   ILE A 100     -10.844 -13.251  21.202  1.00 38.98           N  
ANISOU  667  N   ILE A 100     5433   4249   5128   -424    914    538       N  
ATOM    668  CA  ILE A 100     -12.159 -13.844  20.983  1.00 41.29           C  
ANISOU  668  CA  ILE A 100     5577   4673   5441   -555    965    670       C  
ATOM    669  C   ILE A 100     -11.995 -15.006  20.016  1.00 38.91           C  
ANISOU  669  C   ILE A 100     5287   4275   5222   -720    820    661       C  
ATOM    670  O   ILE A 100     -11.008 -15.097  19.285  1.00 41.62           O  
ANISOU  670  O   ILE A 100     5704   4502   5607   -686    712    541       O  
ATOM    671  CB  ILE A 100     -13.180 -12.822  20.446  1.00 42.14           C  
ANISOU  671  CB  ILE A 100     5486   4963   5563   -478   1058    706       C  
ATOM    672  CG1 ILE A 100     -12.680 -12.226  19.121  1.00 38.39           C  
ANISOU  672  CG1 ILE A 100     4985   4436   5167   -438    970    597       C  
ATOM    673  CG2 ILE A 100     -13.441 -11.739  21.487  1.00 40.19           C  
ANISOU  673  CG2 ILE A 100     5262   4804   5203   -282   1195    714       C  
ATOM    674  CD1 ILE A 100     -13.747 -11.408  18.383  1.00 40.52           C  
ANISOU  674  CD1 ILE A 100     5067   4867   5462   -383   1021    637       C  
ATOM    675  N   GLY A 101     -12.981 -15.901  20.019  1.00 43.12           N  
ANISOU  675  N   GLY A 101     5752   4868   5765   -902    813    794       N  
ATOM    676  CA  GLY A 101     -12.887 -17.063  19.154  1.00 45.52           C  
ANISOU  676  CA  GLY A 101     6119   5048   6128  -1065    647    788       C  
ATOM    677  C   GLY A 101     -13.160 -16.807  17.687  1.00 47.43           C  
ANISOU  677  C   GLY A 101     6241   5328   6452  -1080    580    739       C  
ATOM    678  O   GLY A 101     -12.850 -17.668  16.857  1.00 48.27           O  
ANISOU  678  O   GLY A 101     6444   5304   6592  -1163    426    690       O  
ATOM    679  N   GLN A 102     -13.706 -15.644  17.344  1.00 42.49           N  
ANISOU  679  N   GLN A 102     5434   4865   5844   -983    682    743       N  
ATOM    680  CA  GLN A 102     -14.245 -15.387  16.016  1.00 41.30           C  
ANISOU  680  CA  GLN A 102     5150   4782   5761  -1016    624    732       C  
ATOM    681  C   GLN A 102     -13.467 -14.287  15.305  1.00 44.11           C  
ANISOU  681  C   GLN A 102     5520   5115   6124   -839    632    597       C  
ATOM    682  O   GLN A 102     -12.600 -13.618  15.877  1.00 41.36           O  
ANISOU  682  O   GLN A 102     5261   4721   5735   -701    686    524       O  
ATOM    683  CB  GLN A 102     -15.726 -14.984  16.102  1.00 47.37           C  
ANISOU  683  CB  GLN A 102     5672   5786   6540  -1063    717    876       C  
ATOM    684  CG  GLN A 102     -16.647 -16.072  16.658  1.00 43.61           C  
ANISOU  684  CG  GLN A 102     5131   5381   6059  -1297    706   1049       C  
ATOM    685  CD  GLN A 102     -16.486 -16.255  18.158  1.00 55.10           C  
ANISOU  685  CD  GLN A 102     6667   6844   7424  -1280    821   1113       C  
ATOM    686  NE2 GLN A 102     -16.625 -17.490  18.617  1.00 50.88           N  
ANISOU  686  NE2 GLN A 102     6230   6232   6872  -1501    749   1216       N  
ATOM    687  OE1 GLN A 102     -16.219 -15.299  18.893  1.00 48.51           O  
ANISOU  687  OE1 GLN A 102     5838   6066   6526  -1074    959   1070       O  
ATOM    688  N   GLU A 103     -13.812 -14.101  14.028  1.00 37.93           N  
ANISOU  688  N   GLU A 103     4656   4367   5388   -863    565    576       N  
ATOM    689  CA  GLU A 103     -13.410 -12.941  13.232  1.00 41.64           C  
ANISOU  689  CA  GLU A 103     5106   4856   5858   -728    578    490       C  
ATOM    690  C   GLU A 103     -14.638 -12.048  13.108  1.00 44.50           C  
ANISOU  690  C   GLU A 103     5286   5392   6231   -676    648    571       C  
ATOM    691  O   GLU A 103     -15.633 -12.452  12.489  1.00 44.75           O  
ANISOU  691  O   GLU A 103     5184   5513   6306   -783    594    646       O  
ATOM    692  CB  GLU A 103     -12.910 -13.383  11.856  1.00 42.63           C  
ANISOU  692  CB  GLU A 103     5290   4902   6004   -773    451    407       C  
ATOM    693  CG  GLU A 103     -11.602 -14.190  11.901  1.00 37.23           C  
ANISOU  693  CG  GLU A 103     4781   4073   5293   -762    384    306       C  
ATOM    694  CD  GLU A 103     -10.421 -13.278  12.135  1.00 40.37           C  
ANISOU  694  CD  GLU A 103     5226   4460   5655   -627    445    222       C  
ATOM    695  OE1 GLU A 103     -10.474 -12.116  11.671  1.00 41.57           O  
ANISOU  695  OE1 GLU A 103     5317   4676   5800   -566    488    215       O  
ATOM    696  OE2 GLU A 103      -9.458 -13.709  12.797  1.00 41.45           O1-
ANISOU  696  OE2 GLU A 103     5463   4520   5766   -590    434    170       O1-
ATOM    697  N   CYS A 104     -14.590 -10.840  13.696  1.00 39.96           N  
ANISOU  697  N   CYS A 104     4711   4864   5609   -505    750    557       N  
ATOM    698  CA  CYS A 104     -15.808 -10.032  13.711  1.00 45.29           C  
ANISOU  698  CA  CYS A 104     5218   5716   6274   -408    818    632       C  
ATOM    699  C   CYS A 104     -16.274  -9.736  12.287  1.00 44.01           C  
ANISOU  699  C   CYS A 104     4970   5592   6159   -426    725    623       C  
ATOM    700  O   CYS A 104     -17.484  -9.642  12.039  1.00 45.73           O  
ANISOU  700  O   CYS A 104     4996   5980   6401   -425    730    710       O  
ATOM    701  CB  CYS A 104     -15.632  -8.703  14.468  1.00 42.98           C  
ANISOU  701  CB  CYS A 104     4999   5429   5902   -184    913    596       C  
ATOM    702  SG  CYS A 104     -14.301  -7.553  13.890  1.00 48.00           S  
ANISOU  702  SG  CYS A 104     5850   5881   6508    -89    844    464       S  
ATOM    703  N   ILE A 105     -15.340  -9.624  11.331  1.00 41.63           N  
ANISOU  703  N   ILE A 105     4796   5157   5864   -444    637    527       N  
ATOM    704  CA  ILE A 105     -15.752  -9.256   9.980  1.00 40.23           C  
ANISOU  704  CA  ILE A 105     4566   5010   5707   -447    549    518       C  
ATOM    705  C   ILE A 105     -16.458 -10.435   9.316  1.00 44.03           C  
ANISOU  705  C   ILE A 105     4949   5532   6247   -626    447    573       C  
ATOM    706  O   ILE A 105     -17.396 -10.240   8.532  1.00 44.42           O  
ANISOU  706  O   ILE A 105     4871   5683   6324   -639    384    620       O  
ATOM    707  CB  ILE A 105     -14.548  -8.773   9.146  1.00 43.62           C  
ANISOU  707  CB  ILE A 105     5159   5311   6103   -423    499    415       C  
ATOM    708  CG1 ILE A 105     -15.002  -8.350   7.757  1.00 44.05           C  
ANISOU  708  CG1 ILE A 105     5181   5396   6158   -422    411    413       C  
ATOM    709  CG2 ILE A 105     -13.584  -9.902   8.911  1.00 43.25           C  
ANISOU  709  CG2 ILE A 105     5208   5164   6061   -536    446    353       C  
ATOM    710  CD1 ILE A 105     -14.242  -7.163   7.251  1.00 57.58           C  
ANISOU  710  CD1 ILE A 105     7024   7044   7811   -336    408    361       C  
ATOM    711  N   ASP A 106     -16.052 -11.674   9.637  1.00 40.80           N  
ANISOU  711  N   ASP A 106     4613   5038   5853   -767    408    570       N  
ATOM    712  CA  ASP A 106     -16.752 -12.839   9.097  1.00 39.89           C  
ANISOU  712  CA  ASP A 106     4445   4929   5783   -961    281    631       C  
ATOM    713  C   ASP A 106     -18.143 -12.960   9.696  1.00 47.90           C  
ANISOU  713  C   ASP A 106     5229   6137   6833  -1040    322    787       C  
ATOM    714  O   ASP A 106     -19.087 -13.372   9.012  1.00 48.46           O  
ANISOU  714  O   ASP A 106     5170   6292   6949  -1173    214    863       O  
ATOM    715  CB  ASP A 106     -15.957 -14.129   9.348  1.00 46.10           C  
ANISOU  715  CB  ASP A 106     5413   5546   6559  -1076    209    589       C  
ATOM    716  CG  ASP A 106     -14.602 -14.146   8.625  1.00 43.84           C  
ANISOU  716  CG  ASP A 106     5318   5112   6226   -989    162    437       C  
ATOM    717  OD1 ASP A 106     -14.382 -13.304   7.726  1.00 44.06           O  
ANISOU  717  OD1 ASP A 106     5338   5168   6233   -897    162    381       O  
ATOM    718  OD2 ASP A 106     -13.756 -15.005   8.953  1.00 39.32           O1-
ANISOU  718  OD2 ASP A 106     4902   4411   5629  -1006    124    378       O1-
ATOM    719  N   GLU A 107     -18.291 -12.617  10.975  1.00 45.12           N  
ANISOU  719  N   GLU A 107     4816   5876   6453   -962    475    842       N  
ATOM    720  CA  GLU A 107     -19.612 -12.698  11.584  1.00 49.27           C  
ANISOU  720  CA  GLU A 107     5089   6640   6992  -1019    543   1000       C  
ATOM    721  C   GLU A 107     -20.532 -11.612  11.049  1.00 50.77           C  
ANISOU  721  C   GLU A 107     5074   7027   7190   -864    567   1028       C  
ATOM    722  O   GLU A 107     -21.729 -11.846  10.885  1.00 50.99           O  
ANISOU  722  O   GLU A 107     4853   7267   7256   -958    540   1155       O  
ATOM    723  CB  GLU A 107     -19.487 -12.617  13.101  1.00 45.67           C  
ANISOU  723  CB  GLU A 107     4642   6238   6473   -950    712   1046       C  
ATOM    724  CG  GLU A 107     -18.570 -13.687  13.674  1.00 50.04           C  
ANISOU  724  CG  GLU A 107     5413   6588   7011  -1087    674   1020       C  
ATOM    725  CD  GLU A 107     -19.145 -15.077  13.487  1.00 55.80           C  
ANISOU  725  CD  GLU A 107     6111   7308   7783  -1387    547   1136       C  
ATOM    726  OE1 GLU A 107     -20.390 -15.206  13.470  1.00 54.52           O  
ANISOU  726  OE1 GLU A 107     5699   7367   7648  -1508    556   1288       O  
ATOM    727  OE2 GLU A 107     -18.355 -16.034  13.342  1.00 50.53           O1-
ANISOU  727  OE2 GLU A 107     5670   6413   7117  -1500    426   1079       O1-
ATOM    728  N   LEU A 108     -19.997 -10.425  10.757  1.00 49.06           N  
ANISOU  728  N   LEU A 108     4962   6745   6935   -635    600    917       N  
ATOM    729  CA  LEU A 108     -20.810  -9.417  10.085  1.00 48.04           C  
ANISOU  729  CA  LEU A 108     4690   6759   6806   -476    581    930       C  
ATOM    730  C   LEU A 108     -21.224  -9.890   8.701  1.00 54.03           C  
ANISOU  730  C   LEU A 108     5392   7510   7628   -629    399    942       C  
ATOM    731  O   LEU A 108     -22.372  -9.694   8.287  1.00 52.19           O  
ANISOU  731  O   LEU A 108     4928   7476   7426   -618    354   1027       O  
ATOM    732  CB  LEU A 108     -20.041  -8.102   9.990  1.00 45.86           C  
ANISOU  732  CB  LEU A 108     4604   6358   6465   -236    616    811       C  
ATOM    733  CG  LEU A 108     -19.924  -7.359  11.316  1.00 47.26           C  
ANISOU  733  CG  LEU A 108     4825   6571   6560    -31    774    804       C  
ATOM    734  CD1 LEU A 108     -19.207  -6.046  11.110  1.00 52.59           C  
ANISOU  734  CD1 LEU A 108     5719   7094   7169    172    761    697       C  
ATOM    735  CD2 LEU A 108     -21.303  -7.125  11.901  1.00 55.29           C  
ANISOU  735  CD2 LEU A 108     5568   7882   7556     92    870    917       C  
ATOM    736  N   ALA A 109     -20.300 -10.529   7.977  1.00 48.68           N  
ANISOU  736  N   ALA A 109     4922   6614   6959   -758    288    856       N  
ATOM    737  CA  ALA A 109     -20.600 -10.991   6.624  1.00 48.86           C  
ANISOU  737  CA  ALA A 109     4946   6601   7016   -888    104    849       C  
ATOM    738  C   ALA A 109     -21.733 -12.014   6.604  1.00 53.39           C  
ANISOU  738  C   ALA A 109     5319   7311   7657  -1120      5    988       C  
ATOM    739  O   ALA A 109     -22.512 -12.056   5.646  1.00 53.52           O  
ANISOU  739  O   ALA A 109     5224   7405   7707  -1186   -138   1028       O  
ATOM    740  CB  ALA A 109     -19.337 -11.573   5.986  1.00 49.60           C  
ANISOU  740  CB  ALA A 109     5314   6451   7080   -955     24    725       C  
ATOM    741  N   GLU A 110     -21.855 -12.834   7.648  1.00 51.12           N  
ANISOU  741  N   GLU A 110     4985   7056   7382  -1262     66   1073       N  
ATOM    742  CA  GLU A 110     -22.960 -13.787   7.706  1.00 50.30           C  
ANISOU  742  CA  GLU A 110     4680   7097   7335  -1525    -31   1236       C  
ATOM    743  C   GLU A 110     -24.302 -13.075   7.600  1.00 60.30           C  
ANISOU  743  C   GLU A 110     5593   8687   8633  -1453     -4   1354       C  
ATOM    744  O   GLU A 110     -25.244 -13.582   6.977  1.00 60.34           O  
ANISOU  744  O   GLU A 110     5420   8812   8694  -1647   -160   1460       O  
ATOM    745  CB  GLU A 110     -22.882 -14.590   9.004  1.00 52.56           C  
ANISOU  745  CB  GLU A 110     4971   7391   7608  -1667     65   1328       C  
ATOM    746  CG  GLU A 110     -24.156 -15.364   9.374  1.00 54.85           C  
ANISOU  746  CG  GLU A 110     4988   7911   7942  -1941     22   1546       C  
ATOM    747  CD  GLU A 110     -24.359 -16.586   8.505  1.00 67.98           C  
ANISOU  747  CD  GLU A 110     6754   9423   9652  -2266   -249   1586       C  
ATOM    748  OE1 GLU A 110     -23.372 -17.048   7.895  1.00 67.46           O  
ANISOU  748  OE1 GLU A 110     7018   9049   9564  -2269   -374   1439       O  
ATOM    749  OE2 GLU A 110     -25.498 -17.089   8.435  1.00 73.15           O1-
ANISOU  749  OE2 GLU A 110     7165  10273  10355  -2514   -344   1766       O1-
ATOM    750  N   GLU A 111     -24.401 -11.886   8.191  1.00 55.56           N  
ANISOU  750  N   GLU A 111     4896   8228   7987  -1161    178   1333       N  
ATOM    751  CA  GLU A 111     -25.641 -11.123   8.151  1.00 68.41           C  
ANISOU  751  CA  GLU A 111     6189  10179   9623  -1019    217   1430       C  
ATOM    752  C   GLU A 111     -25.930 -10.575   6.764  1.00 65.26           C  
ANISOU  752  C   GLU A 111     5786   9759   9250   -942     47   1373       C  
ATOM    753  O   GLU A 111     -27.087 -10.274   6.454  1.00 66.48           O  
ANISOU  753  O   GLU A 111     5643  10182   9435   -903     -2   1471       O  
ATOM    754  CB  GLU A 111     -25.559  -9.991   9.164  1.00 56.06           C  
ANISOU  754  CB  GLU A 111     4599   8724   7976   -683    441   1396       C  
ATOM    755  CG  GLU A 111     -25.419 -10.493  10.580  1.00 64.20           C  
ANISOU  755  CG  GLU A 111     5611   9818   8965   -744    615   1468       C  
ATOM    756  CD  GLU A 111     -26.653 -11.203  11.058  1.00 64.62           C  
ANISOU  756  CD  GLU A 111     5301  10206   9046   -941    649   1679       C  
ATOM    757  OE1 GLU A 111     -27.755 -10.629  10.892  1.00 70.40           O  
ANISOU  757  OE1 GLU A 111     5711  11258   9781   -807    673   1762       O  
ATOM    758  OE2 GLU A 111     -26.521 -12.314  11.619  1.00 78.55           O1-
ANISOU  758  OE2 GLU A 111     7098  11927  10822  -1224    649   1770       O1-
ATOM    759  N   ALA A 112     -24.905 -10.431   5.933  1.00 57.28           N  
ANISOU  759  N   ALA A 112     5091   8458   8217   -913    -42   1224       N  
ATOM    760  CA  ALA A 112     -25.064 -10.089   4.530  1.00 58.06           C  
ANISOU  760  CA  ALA A 112     5242   8498   8323   -887   -223   1171       C  
ATOM    761  C   ALA A 112     -25.185 -11.325   3.653  1.00 61.58           C  
ANISOU  761  C   ALA A 112     5741   8842   8816  -1197   -444   1196       C  
ATOM    762  O   ALA A 112     -25.201 -11.199   2.425  1.00 60.95           O  
ANISOU  762  O   ALA A 112     5757   8677   8726  -1200   -612   1141       O  
ATOM    763  CB  ALA A 112     -23.886  -9.227   4.060  1.00 54.78           C  
ANISOU  763  CB  ALA A 112     5140   7842   7831   -695   -194   1009       C  
ATOM    764  N   GLY A 113     -25.257 -12.510   4.257  1.00 57.94           N  
ANISOU  764  N   GLY A 113     5255   8369   8391  -1456   -460   1278       N  
ATOM    765  CA  GLY A 113     -25.309 -13.754   3.510  1.00 57.95           C  
ANISOU  765  CA  GLY A 113     5372   8225   8421  -1758   -693   1296       C  
ATOM    766  C   GLY A 113     -24.030 -14.102   2.784  1.00 66.24           C  
ANISOU  766  C   GLY A 113     6818   8943   9408  -1741   -772   1122       C  
ATOM    767  O   GLY A 113     -24.070 -14.821   1.782  1.00 57.73           O  
ANISOU  767  O   GLY A 113     5881   7731   8322  -1896   -995   1093       O  
ATOM    768  N   LEU A 114     -22.887 -13.616   3.266  1.00 52.09           N  
ANISOU  768  N   LEU A 114     5207   7026   7559  -1552   -600   1006       N  
ATOM    769  CA  LEU A 114     -21.640 -13.720   2.517  1.00 53.61           C  
ANISOU  769  CA  LEU A 114     5725   6969   7677  -1483   -644    840       C  
ATOM    770  C   LEU A 114     -20.511 -14.264   3.384  1.00 50.68           C  
ANISOU  770  C   LEU A 114     5541   6441   7274  -1480   -537    774       C  
ATOM    771  O   LEU A 114     -19.333 -13.969   3.134  1.00 47.35           O  
ANISOU  771  O   LEU A 114     5322   5885   6785  -1342   -479    641       O  
ATOM    772  CB  LEU A 114     -21.252 -12.365   1.927  1.00 54.49           C  
ANISOU  772  CB  LEU A 114     5877   7094   7734  -1235   -571    755       C  
ATOM    773  CG  LEU A 114     -22.094 -11.911   0.732  1.00 60.90           C  
ANISOU  773  CG  LEU A 114     6608   7987   8546  -1218   -727    780       C  
ATOM    774  CD1 LEU A 114     -21.861 -10.435   0.423  1.00 58.28           C  
ANISOU  774  CD1 LEU A 114     6299   7686   8159   -967   -637    730       C  
ATOM    775  CD2 LEU A 114     -21.786 -12.765  -0.476  1.00 60.97           C  
ANISOU  775  CD2 LEU A 114     6836   7826   8505  -1347   -932    707       C  
ATOM    776  N   ARG A 115     -20.845 -15.073   4.393  1.00 52.57           N  
ANISOU  776  N   ARG A 115     5712   6707   7554  -1640   -516    873       N  
ATOM    777  CA  ARG A 115     -19.824 -15.530   5.335  1.00 52.34           C  
ANISOU  777  CA  ARG A 115     5855   6540   7494  -1618   -414    818       C  
ATOM    778  C   ARG A 115     -18.700 -16.273   4.624  1.00 54.07           C  
ANISOU  778  C   ARG A 115     6388   6508   7647  -1612   -531    670       C  
ATOM    779  O   ARG A 115     -17.518 -15.968   4.822  1.00 49.19           O  
ANISOU  779  O   ARG A 115     5912   5803   6976  -1448   -427    554       O  
ATOM    780  CB  ARG A 115     -20.441 -16.433   6.404  1.00 53.32           C  
ANISOU  780  CB  ARG A 115     5888   6715   7657  -1830   -413    965       C  
ATOM    781  CG  ARG A 115     -19.362 -17.109   7.264  1.00 52.61           C  
ANISOU  781  CG  ARG A 115     6030   6437   7524  -1825   -362    903       C  
ATOM    782  CD  ARG A 115     -19.931 -18.171   8.187  1.00 56.25           C  
ANISOU  782  CD  ARG A 115     6467   6902   8006  -2076   -402   1055       C  
ATOM    783  NE  ARG A 115     -20.805 -17.613   9.212  1.00 53.91           N  
ANISOU  783  NE  ARG A 115     5876   6875   7734  -2083   -223   1209       N  
ATOM    784  CZ  ARG A 115     -20.382 -17.107  10.364  1.00 67.40           C  
ANISOU  784  CZ  ARG A 115     7570   8635   9405  -1933    -17   1204       C  
ATOM    785  NH1 ARG A 115     -19.091 -17.036  10.658  1.00 53.78           N1+
ANISOU  785  NH1 ARG A 115     6085   6718   7632  -1778     32   1060       N1+
ATOM    786  NH2 ARG A 115     -21.275 -16.667  11.247  1.00 53.93           N  
ANISOU  786  NH2 ARG A 115     5598   7194   7699  -1931    140   1349       N  
ATOM    787  N   ASP A 116     -19.044 -17.272   3.803  1.00 52.46           N  
ANISOU  787  N   ASP A 116     6302   6194   7436  -1783   -757    673       N  
ATOM    788  CA  ASP A 116     -17.993 -18.094   3.202  1.00 53.80           C  
ANISOU  788  CA  ASP A 116     6796   6126   7520  -1746   -873    525       C  
ATOM    789  C   ASP A 116     -17.089 -17.261   2.298  1.00 49.92           C  
ANISOU  789  C   ASP A 116     6389   5628   6949  -1512   -805    378       C  
ATOM    790  O   ASP A 116     -15.855 -17.384   2.354  1.00 52.84           O  
ANISOU  790  O   ASP A 116     6929   5901   7246  -1369   -740    254       O  
ATOM    791  CB  ASP A 116     -18.604 -19.266   2.430  1.00 55.10           C  
ANISOU  791  CB  ASP A 116     7106   6156   7674  -1963  -1156    551       C  
ATOM    792  CG  ASP A 116     -19.426 -20.184   3.315  1.00 66.90           C  
ANISOU  792  CG  ASP A 116     8543   7642   9235  -2243  -1244    715       C  
ATOM    793  OD1 ASP A 116     -19.141 -20.263   4.529  1.00 59.68           O  
ANISOU  793  OD1 ASP A 116     7594   6743   8337  -2240  -1099    762       O  
ATOM    794  OD2 ASP A 116     -20.348 -20.841   2.792  1.00 71.72           O1-
ANISOU  794  OD2 ASP A 116     9152   8227   9871  -2483  -1468    806       O1-
ATOM    795  N   HIS A 117     -17.683 -16.386   1.481  1.00 47.01           N  
ANISOU  795  N   HIS A 117     5893   5379   6588  -1474   -817    401       N  
ATOM    796  CA  HIS A 117     -16.899 -15.545   0.582  1.00 47.00           C  
ANISOU  796  CA  HIS A 117     5976   5383   6499  -1285   -757    288       C  
ATOM    797  C   HIS A 117     -15.946 -14.656   1.366  1.00 49.05           C  
ANISOU  797  C   HIS A 117     6200   5690   6747  -1122   -531    251       C  
ATOM    798  O   HIS A 117     -14.757 -14.549   1.040  1.00 46.03           O  
ANISOU  798  O   HIS A 117     5958   5255   6277  -1001   -473    140       O  
ATOM    799  CB  HIS A 117     -17.825 -14.686  -0.281  1.00 52.69           C  
ANISOU  799  CB  HIS A 117     6562   6225   7234  -1278   -815    343       C  
ATOM    800  CG  HIS A 117     -17.096 -13.778  -1.221  1.00 53.44           C  
ANISOU  800  CG  HIS A 117     6754   6324   7227  -1112   -760    253       C  
ATOM    801  CD2 HIS A 117     -16.735 -12.477  -1.108  1.00 59.28           C  
ANISOU  801  CD2 HIS A 117     7431   7144   7947   -973   -606    254       C  
ATOM    802  ND1 HIS A 117     -16.609 -14.205  -2.438  1.00 63.17           N  
ANISOU  802  ND1 HIS A 117     8197   7464   8340  -1085   -874    153       N  
ATOM    803  CE1 HIS A 117     -16.001 -13.200  -3.045  1.00 59.66           C  
ANISOU  803  CE1 HIS A 117     7790   7069   7810   -951   -778    110       C  
ATOM    804  NE2 HIS A 117     -16.063 -12.140  -2.259  1.00 52.94           N  
ANISOU  804  NE2 HIS A 117     6783   6310   7022   -894   -627    173       N  
ATOM    805  N   VAL A 118     -16.458 -13.997   2.403  1.00 46.07           N  
ANISOU  805  N   VAL A 118     5632   5425   6447  -1115   -406    346       N  
ATOM    806  CA  VAL A 118     -15.619 -13.088   3.173  1.00 44.26           C  
ANISOU  806  CA  VAL A 118     5392   5224   6202   -971   -219    316       C  
ATOM    807  C   VAL A 118     -14.614 -13.872   4.006  1.00 42.70           C  
ANISOU  807  C   VAL A 118     5315   4923   5988   -969   -172    258       C  
ATOM    808  O   VAL A 118     -13.445 -13.484   4.117  1.00 43.90           O  
ANISOU  808  O   VAL A 118     5546   5048   6085   -856    -83    177       O  
ATOM    809  CB  VAL A 118     -16.501 -12.176   4.042  1.00 47.36           C  
ANISOU  809  CB  VAL A 118     5579   5758   6656   -930   -114    422       C  
ATOM    810  CG1 VAL A 118     -15.668 -11.476   5.135  1.00 45.07           C  
ANISOU  810  CG1 VAL A 118     5316   5460   6349   -809     55    396       C  
ATOM    811  CG2 VAL A 118     -17.234 -11.176   3.160  1.00 43.07           C  
ANISOU  811  CG2 VAL A 118     4948   5309   6108   -862   -155    452       C  
ATOM    812  N   ALA A 119     -15.051 -14.988   4.608  1.00 43.44           N  
ANISOU  812  N   ALA A 119     5423   4959   6122  -1103   -244    310       N  
ATOM    813  CA  ALA A 119     -14.145 -15.779   5.439  1.00 40.76           C  
ANISOU  813  CA  ALA A 119     5220   4505   5760  -1091   -221    259       C  
ATOM    814  C   ALA A 119     -12.951 -16.299   4.643  1.00 49.21           C  
ANISOU  814  C   ALA A 119     6498   5463   6739   -992   -285    111       C  
ATOM    815  O   ALA A 119     -11.857 -16.451   5.198  1.00 42.86           O  
ANISOU  815  O   ALA A 119     5774   4614   5898   -891   -219     39       O  
ATOM    816  CB  ALA A 119     -14.894 -16.944   6.095  1.00 44.10           C  
ANISOU  816  CB  ALA A 119     5662   4866   6228  -1281   -320    355       C  
ATOM    817  N   ALA A 120     -13.128 -16.575   3.349  1.00 43.24           N  
ANISOU  817  N   ALA A 120     5825   4675   5931  -1003   -413     62       N  
ATOM    818  CA  ALA A 120     -11.995 -17.042   2.552  1.00 45.64           C  
ANISOU  818  CA  ALA A 120     6318   4905   6117   -870   -456    -85       C  
ATOM    819  C   ALA A 120     -10.969 -15.930   2.360  1.00 42.87           C  
ANISOU  819  C   ALA A 120     5902   4674   5714   -715   -289   -140       C  
ATOM    820  O   ALA A 120      -9.753 -16.182   2.354  1.00 43.37           O  
ANISOU  820  O   ALA A 120     6047   4734   5699   -586   -244   -239       O  
ATOM    821  CB  ALA A 120     -12.482 -17.580   1.205  1.00 45.25           C  
ANISOU  821  CB  ALA A 120     6396   4793   6003   -911   -638   -124       C  
ATOM    822  N   ILE A 121     -11.438 -14.690   2.214  1.00 39.29           N  
ANISOU  822  N   ILE A 121     5299   4333   5294   -728   -206    -69       N  
ATOM    823  CA  ILE A 121     -10.522 -13.559   2.121  1.00 39.32           C  
ANISOU  823  CA  ILE A 121     5255   4434   5250   -628    -66    -93       C  
ATOM    824  C   ILE A 121      -9.829 -13.337   3.459  1.00 42.97           C  
ANISOU  824  C   ILE A 121     5671   4900   5754   -594     49    -85       C  
ATOM    825  O   ILE A 121      -8.605 -13.155   3.526  1.00 39.31           O  
ANISOU  825  O   ILE A 121     5228   4476   5233   -511    120   -146       O  
ATOM    826  CB  ILE A 121     -11.281 -12.301   1.666  1.00 40.24           C  
ANISOU  826  CB  ILE A 121     5273   4629   5386   -650    -40    -14       C  
ATOM    827  CG1 ILE A 121     -11.889 -12.523   0.275  1.00 47.06           C  
ANISOU  827  CG1 ILE A 121     6197   5489   6194   -677   -169    -28       C  
ATOM    828  CG2 ILE A 121     -10.350 -11.080   1.703  1.00 41.12           C  
ANISOU  828  CG2 ILE A 121     5364   4812   5447   -585     86    -17       C  
ATOM    829  CD1 ILE A 121     -12.949 -11.487  -0.103  1.00 47.86           C  
ANISOU  829  CD1 ILE A 121     6200   5651   6332   -702   -190     62       C  
ATOM    830  N   THR A 122     -10.609 -13.353   4.546  1.00 38.76           N  
ANISOU  830  N   THR A 122     5068   4345   5315   -658     66     -3       N  
ATOM    831  CA  THR A 122     -10.043 -13.204   5.884  1.00 40.11           C  
ANISOU  831  CA  THR A 122     5221   4505   5515   -625    159      6       C  
ATOM    832  C   THR A 122      -8.924 -14.203   6.128  1.00 40.37           C  
ANISOU  832  C   THR A 122     5366   4470   5502   -567    131    -87       C  
ATOM    833  O   THR A 122      -7.868 -13.844   6.659  1.00 37.50           O  
ANISOU  833  O   THR A 122     4996   4137   5117   -493    204   -124       O  
ATOM    834  CB  THR A 122     -11.144 -13.379   6.929  1.00 37.64           C  
ANISOU  834  CB  THR A 122     4836   4183   5281   -704    170    108       C  
ATOM    835  CG2 THR A 122     -10.577 -13.239   8.338  1.00 39.29           C  
ANISOU  835  CG2 THR A 122     5055   4373   5501   -661    262    116       C  
ATOM    836  OG1 THR A 122     -12.138 -12.369   6.716  1.00 39.64           O  
ANISOU  836  OG1 THR A 122     4967   4529   5565   -708    203    185       O  
ATOM    837  N   ALA A 123      -9.135 -15.462   5.732  1.00 37.77           N  
ANISOU  837  N   ALA A 123     5153   4046   5153   -594      5   -126       N  
ATOM    838  CA  ALA A 123      -8.126 -16.497   5.948  1.00 36.99           C  
ANISOU  838  CA  ALA A 123     5193   3864   4996   -501    -48   -224       C  
ATOM    839  C   ALA A 123      -6.829 -16.182   5.207  1.00 38.95           C  
ANISOU  839  C   ALA A 123     5439   4214   5147   -347      6   -330       C  
ATOM    840  O   ALA A 123      -5.736 -16.377   5.748  1.00 36.83           O  
ANISOU  840  O   ALA A 123     5180   3968   4848   -240     42   -389       O  
ATOM    841  CB  ALA A 123      -8.669 -17.853   5.508  1.00 39.94           C  
ANISOU  841  CB  ALA A 123     5739   4089   5347   -556   -226   -249       C  
ATOM    842  N   ARG A 124      -6.930 -15.656   3.984  1.00 36.06           N  
ANISOU  842  N   ARG A 124     5044   3932   4725   -338     15   -343       N  
ATOM    843  CA  ARG A 124      -5.725 -15.295   3.240  1.00 41.73           C  
ANISOU  843  CA  ARG A 124     5734   4789   5331   -212     87   -419       C  
ATOM    844  C   ARG A 124      -5.024 -14.100   3.871  1.00 38.88           C  
ANISOU  844  C   ARG A 124     5225   4549   4999   -228    222   -367       C  
ATOM    845  O   ARG A 124      -3.789 -14.051   3.905  1.00 37.56           O  
ANISOU  845  O   ARG A 124     5008   4495   4769   -135    280   -419       O  
ATOM    846  CB  ARG A 124      -6.077 -15.010   1.783  1.00 39.67           C  
ANISOU  846  CB  ARG A 124     5500   4586   4988   -216     61   -430       C  
ATOM    847  CG  ARG A 124      -6.355 -16.288   1.008  1.00 45.15           C  
ANISOU  847  CG  ARG A 124     6383   5169   5603   -155    -90   -519       C  
ATOM    848  CD  ARG A 124      -7.280 -15.997  -0.142  1.00 55.13           C  
ANISOU  848  CD  ARG A 124     7682   6428   6836   -229   -159   -489       C  
ATOM    849  NE  ARG A 124      -6.574 -15.228  -1.156  1.00 58.86           N  
ANISOU  849  NE  ARG A 124     8112   7070   7182   -151    -61   -513       N  
ATOM    850  CZ  ARG A 124      -7.077 -14.165  -1.768  1.00 71.75           C  
ANISOU  850  CZ  ARG A 124     9677   8772   8814   -236    -26   -434       C  
ATOM    851  NH1 ARG A 124      -8.290 -13.710  -1.485  1.00 60.55           N1+
ANISOU  851  NH1 ARG A 124     8207   7283   7516   -370    -78   -337       N1+
ATOM    852  NH2 ARG A 124      -6.340 -13.534  -2.677  1.00 73.78           N  
ANISOU  852  NH2 ARG A 124     9914   9184   8935   -178     64   -447       N  
ATOM    853  N   ALA A 125      -5.793 -13.140   4.387  1.00 38.93           N  
ANISOU  853  N   ALA A 125     5162   4537   5092   -339    262   -265       N  
ATOM    854  CA  ALA A 125      -5.207 -11.987   5.074  1.00 39.67           C  
ANISOU  854  CA  ALA A 125     5167   4699   5207   -365    356   -215       C  
ATOM    855  C   ALA A 125      -4.537 -12.410   6.377  1.00 38.62           C  
ANISOU  855  C   ALA A 125     5035   4528   5112   -325    367   -238       C  
ATOM    856  O   ALA A 125      -3.445 -11.926   6.721  1.00 37.50           O  
ANISOU  856  O   ALA A 125     4832   4472   4944   -303    416   -247       O  
ATOM    857  CB  ALA A 125      -6.292 -10.930   5.337  1.00 36.07           C  
ANISOU  857  CB  ALA A 125     4683   4207   4817   -450    374   -115       C  
ATOM    858  N   MET A 126      -5.176 -13.309   7.118  1.00 37.21           N  
ANISOU  858  N   MET A 126     4926   4225   4988   -330    311   -236       N  
ATOM    859  CA AMET A 126      -4.567 -13.844   8.330  0.51 37.83           C  
ANISOU  859  CA AMET A 126     5039   4249   5087   -283    304   -260       C  
ATOM    860  CA BMET A 126      -4.565 -13.834   8.331  0.49 37.83           C  
ANISOU  860  CA BMET A 126     5037   4249   5086   -283    304   -260       C  
ATOM    861  C   MET A 126      -3.236 -14.522   8.030  1.00 37.07           C  
ANISOU  861  C   MET A 126     4954   4216   4913   -149    280   -366       C  
ATOM    862  O   MET A 126      -2.285 -14.426   8.816  1.00 36.71           O  
ANISOU  862  O   MET A 126     4870   4210   4866    -96    298   -385       O  
ATOM    863  CB AMET A 126      -5.525 -14.834   8.999  0.51 39.62           C  
ANISOU  863  CB AMET A 126     5363   4330   5363   -331    235   -229       C  
ATOM    864  CB BMET A 126      -5.548 -14.790   9.015  0.49 39.62           C  
ANISOU  864  CB BMET A 126     5359   4332   5364   -334    238   -226       C  
ATOM    865  CG AMET A 126      -6.794 -14.215   9.560  0.51 39.25           C  
ANISOU  865  CG AMET A 126     5264   4266   5384   -439    279   -115       C  
ATOM    866  CG BMET A 126      -5.067 -15.398  10.322  0.49 43.07           C  
ANISOU  866  CG BMET A 126     5866   4686   5812   -296    219   -236       C  
ATOM    867  SD AMET A 126      -8.106 -15.428   9.840  0.51 45.21           S  
ANISOU  867  SD AMET A 126     6089   4909   6181   -553    189    -49       S  
ATOM    868  SD BMET A 126      -6.149 -16.726  10.913  0.49 51.10           S  
ANISOU  868  SD BMET A 126     7025   5532   6859   -388    119   -183       S  
ATOM    869  CE AMET A 126      -7.160 -16.783  10.524  0.51 46.90           C  
ANISOU  869  CE AMET A 126     6475   4990   6354   -487    100   -124       C  
ATOM    870  CE BMET A 126      -7.748 -15.910  10.919  0.49 44.54           C  
ANISOU  870  CE BMET A 126     6071   4756   6095   -539    188    -46       C  
ATOM    871  N   ASN A 127      -3.144 -15.218   6.897  1.00 36.34           N  
ANISOU  871  N   ASN A 127     4915   4146   4748    -74    231   -438       N  
ATOM    872  CA  ASN A 127      -1.951 -15.988   6.588  1.00 33.87           C  
ANISOU  872  CA  ASN A 127     4623   3907   4340    106    206   -552       C  
ATOM    873  C   ASN A 127      -0.861 -15.143   5.936  1.00 40.19           C  
ANISOU  873  C   ASN A 127     5254   4949   5066    150    308   -562       C  
ATOM    874  O   ASN A 127       0.276 -15.612   5.811  1.00 42.51           O  
ANISOU  874  O   ASN A 127     5502   5371   5280    313    315   -644       O  
ATOM    875  CB  ASN A 127      -2.308 -17.156   5.669  1.00 36.88           C  
ANISOU  875  CB  ASN A 127     5172   4195   4645    196     96   -637       C  
ATOM    876  CG  ASN A 127      -1.260 -18.253   5.687  1.00 45.07           C  
ANISOU  876  CG  ASN A 127     6301   5238   5586    428     30   -768       C  
ATOM    877  ND2 ASN A 127      -0.833 -18.697   4.500  1.00 46.91           N  
ANISOU  877  ND2 ASN A 127     6585   5556   5683    590     12   -869       N  
ATOM    878  OD1 ASN A 127      -0.830 -18.695   6.754  1.00 49.49           O  
ANISOU  878  OD1 ASN A 127     6897   5729   6179    481     -8   -783       O  
ATOM    879  N   GLY A 128      -1.180 -13.921   5.514  1.00 39.41           N  
ANISOU  879  N   GLY A 128     5064   4926   4983     12    383   -474       N  
ATOM    880  CA  GLY A 128      -0.204 -13.063   4.869  1.00 39.06           C  
ANISOU  880  CA  GLY A 128     4869   5111   4860      1    474   -452       C  
ATOM    881  C   GLY A 128      -0.164 -13.165   3.370  1.00 41.66           C  
ANISOU  881  C   GLY A 128     5204   5561   5065     56    501   -487       C  
ATOM    882  O   GLY A 128       0.758 -12.613   2.747  1.00 42.77           O  
ANISOU  882  O   GLY A 128     5211   5931   5110     59    588   -469       O  
ATOM    883  N   GLU A 129      -1.130 -13.849   2.760  1.00 39.20           N  
ANISOU  883  N   GLU A 129     5044   5111   4739     86    425   -528       N  
ATOM    884  CA  GLU A 129      -1.144 -14.019   1.315  1.00 40.67           C  
ANISOU  884  CA  GLU A 129     5274   5390   4787    154    432   -572       C  
ATOM    885  C   GLU A 129      -1.716 -12.819   0.583  1.00 45.73           C  
ANISOU  885  C   GLU A 129     5880   6074   5420     -6    478   -468       C  
ATOM    886  O   GLU A 129      -1.550 -12.726  -0.639  1.00 49.17           O  
ANISOU  886  O   GLU A 129     6333   6630   5720     34    509   -486       O  
ATOM    887  CB  GLU A 129      -1.954 -15.251   0.939  1.00 42.73           C  
ANISOU  887  CB  GLU A 129     5744   5463   5029    238    295   -659       C  
ATOM    888  CG  GLU A 129      -1.304 -16.539   1.398  1.00 45.43           C  
ANISOU  888  CG  GLU A 129     6181   5751   5330    436    224   -780       C  
ATOM    889  CD  GLU A 129      -2.204 -17.718   1.163  1.00 59.13           C  
ANISOU  889  CD  GLU A 129     8166   7244   7057    467     51   -844       C  
ATOM    890  OE1 GLU A 129      -2.866 -17.730   0.106  1.00 55.66           O  
ANISOU  890  OE1 GLU A 129     7819   6774   6556    435      0   -850       O  
ATOM    891  OE2 GLU A 129      -2.262 -18.611   2.031  1.00 51.12           O1-
ANISOU  891  OE2 GLU A 129     7268   6062   6093    506    -49   -879       O1-
ATOM    892  N   ILE A 130      -2.420 -11.934   1.290  1.00 41.13           N  
ANISOU  892  N   ILE A 130     5275   5389   4965   -165    476   -366       N  
ATOM    893  CA  ILE A 130      -2.846 -10.651   0.742  1.00 46.38           C  
ANISOU  893  CA  ILE A 130     5918   6085   5620   -303    509   -262       C  
ATOM    894  C   ILE A 130      -2.600  -9.589   1.800  1.00 41.47           C  
ANISOU  894  C   ILE A 130     5224   5448   5084   -417    548   -172       C  
ATOM    895  O   ILE A 130      -2.662  -9.860   3.003  1.00 42.83           O  
ANISOU  895  O   ILE A 130     5392   5525   5356   -405    528   -182       O  
ATOM    896  CB  ILE A 130      -4.330 -10.667   0.304  1.00 40.86           C  
ANISOU  896  CB  ILE A 130     5323   5234   4967   -349    419   -237       C  
ATOM    897  CG1 ILE A 130      -5.217 -11.124   1.454  1.00 43.90           C  
ANISOU  897  CG1 ILE A 130     5730   5450   5500   -369    356   -228       C  
ATOM    898  CG2 ILE A 130      -4.525 -11.604  -0.857  1.00 56.13           C  
ANISOU  898  CG2 ILE A 130     7358   7174   6794   -256    357   -321       C  
ATOM    899  CD1 ILE A 130      -6.618 -11.513   1.013  1.00 51.62           C  
ANISOU  899  CD1 ILE A 130     6778   6315   6520   -404    250   -213       C  
ATOM    900  N   ALA A 131      -2.288  -8.370   1.349  1.00 41.05           N  
ANISOU  900  N   ALA A 131     5138   5480   4977   -533    592    -82       N  
ATOM    901  CA  ALA A 131      -2.061  -7.282   2.291  1.00 44.43           C  
ANISOU  901  CA  ALA A 131     5547   5865   5469   -650    598      4       C  
ATOM    902  C   ALA A 131      -3.340  -6.981   3.058  1.00 43.63           C  
ANISOU  902  C   ALA A 131     5538   5558   5483   -656    539     30       C  
ATOM    903  O   ALA A 131      -4.448  -7.097   2.527  1.00 43.26           O  
ANISOU  903  O   ALA A 131     5550   5436   5449   -630    497     31       O  
ATOM    904  CB  ALA A 131      -1.573  -6.021   1.564  1.00 50.13           C  
ANISOU  904  CB  ALA A 131     6265   6687   6097   -799    627    110       C  
ATOM    905  N   PHE A 132      -3.171  -6.590   4.321  1.00 40.05           N  
ANISOU  905  N   PHE A 132     5087   5028   5100   -680    533     52       N  
ATOM    906  CA  PHE A 132      -4.319  -6.402   5.197  1.00 42.34           C  
ANISOU  906  CA  PHE A 132     5448   5158   5482   -648    498     70       C  
ATOM    907  C   PHE A 132      -5.261  -5.316   4.688  1.00 48.93           C  
ANISOU  907  C   PHE A 132     6364   5926   6302   -679    465    139       C  
ATOM    908  O   PHE A 132      -6.481  -5.500   4.687  1.00 42.20           O  
ANISOU  908  O   PHE A 132     5526   5010   5497   -618    439    142       O  
ATOM    909  CB  PHE A 132      -3.868  -6.065   6.610  1.00 46.94           C  
ANISOU  909  CB  PHE A 132     6048   5678   6110   -657    498     80       C  
ATOM    910  CG  PHE A 132      -5.006  -5.867   7.531  1.00 57.01           C  
ANISOU  910  CG  PHE A 132     7390   6822   7451   -599    485     98       C  
ATOM    911  CD1 PHE A 132      -5.727  -6.955   7.998  1.00 51.55           C  
ANISOU  911  CD1 PHE A 132     6670   6099   6818   -529    493     64       C  
ATOM    912  CD2 PHE A 132      -5.426  -4.583   7.849  1.00 56.41           C  
ANISOU  912  CD2 PHE A 132     7414   6660   7360   -611    460    156       C  
ATOM    913  CE1 PHE A 132      -6.809  -6.778   8.821  1.00 58.49           C  
ANISOU  913  CE1 PHE A 132     7577   6906   7741   -478    501     97       C  
ATOM    914  CE2 PHE A 132      -6.511  -4.397   8.659  1.00 51.38           C  
ANISOU  914  CE2 PHE A 132     6824   5938   6760   -517    463    168       C  
ATOM    915  CZ  PHE A 132      -7.206  -5.497   9.147  1.00 48.17           C  
ANISOU  915  CZ  PHE A 132     6345   5544   6412   -454    496    144       C  
ATOM    916  N   GLU A 133      -4.725  -4.153   4.287  1.00 43.80           N  
ANISOU  916  N   GLU A 133     5769   5290   5582   -777    454    206       N  
ATOM    917  CA AGLU A 133      -5.614  -3.025   4.002  0.48 43.41           C  
ANISOU  917  CA AGLU A 133     5842   5137   5514   -782    398    270       C  
ATOM    918  CA BGLU A 133      -5.608  -3.023   4.008  0.52 43.41           C  
ANISOU  918  CA BGLU A 133     5842   5137   5514   -782    398    270       C  
ATOM    919  C   GLU A 133      -6.523  -3.281   2.811  1.00 40.16           C  
ANISOU  919  C   GLU A 133     5430   4750   5078   -741    374    268       C  
ATOM    920  O   GLU A 133      -7.748  -3.104   2.948  1.00 41.73           O  
ANISOU  920  O   GLU A 133     5658   4874   5325   -655    332    277       O  
ATOM    921  CB AGLU A 133      -4.824  -1.727   3.797  0.48 44.40           C  
ANISOU  921  CB AGLU A 133     6072   5243   5557   -923    362    354       C  
ATOM    922  CB BGLU A 133      -4.759  -1.755   3.868  0.52 44.43           C  
ANISOU  922  CB BGLU A 133     6070   5248   5563   -925    364    352       C  
ATOM    923  CG AGLU A 133      -5.771  -0.618   3.323  0.48 40.94           C  
ANISOU  923  CG AGLU A 133     5798   4680   5078   -904    282    414       C  
ATOM    924  CG BGLU A 133      -3.993  -1.421   5.168  0.52 47.35           C  
ANISOU  924  CG BGLU A 133     6464   5564   5963   -970    351    357       C  
ATOM    925  CD AGLU A 133      -5.107   0.723   3.091  0.48 46.20           C  
ANISOU  925  CD AGLU A 133     6626   5278   5649  -1061    212    511       C  
ATOM    926  CD BGLU A 133      -2.678  -2.209   5.339  0.52 48.22           C  
ANISOU  926  CD BGLU A 133     6414   5834   6072  -1033    407    326       C  
ATOM    927  OE1AGLU A 133      -4.111   1.033   3.772  0.48 46.92           O  
ANISOU  927  OE1AGLU A 133     6727   5367   5733  -1177    203    538       O  
ATOM    928  OE1BGLU A 133      -2.295  -2.992   4.435  0.52 44.92           O  
ANISOU  928  OE1BGLU A 133     5873   5578   5616  -1025    466    297       O  
ATOM    929  OE2AGLU A 133      -5.620   1.492   2.260  0.48 43.73           O1-
ANISOU  929  OE2AGLU A 133     6448   4900   5267  -1076    146    568       O1-
ATOM    930  OE2BGLU A 133      -2.026  -2.032   6.387  0.52 43.92           O1-
ANISOU  930  OE2BGLU A 133     5876   5258   5555  -1071    382    328       O1-
ATOM    931  N   PRO A 134      -6.033  -3.694   1.635  1.00 38.64           N  
ANISOU  931  N   PRO A 134     5203   4673   4805   -785    394    257       N  
ATOM    932  CA  PRO A 134      -6.990  -3.961   0.547  1.00 43.12           C  
ANISOU  932  CA  PRO A 134     5795   5243   5346   -740    347    250       C  
ATOM    933  C   PRO A 134      -7.964  -5.084   0.872  1.00 40.38           C  
ANISOU  933  C   PRO A 134     5382   4865   5097   -646    320    189       C  
ATOM    934  O   PRO A 134      -9.117  -5.034   0.431  1.00 41.90           O  
ANISOU  934  O   PRO A 134     5588   5021   5312   -607    251    206       O  
ATOM    935  CB  PRO A 134      -6.104  -4.299  -0.665  1.00 49.90           C  
ANISOU  935  CB  PRO A 134     6640   6246   6075   -790    387    237       C  
ATOM    936  CG  PRO A 134      -4.722  -4.380  -0.180  1.00 54.24           C  
ANISOU  936  CG  PRO A 134     7110   6900   6597   -846    466    233       C  
ATOM    937  CD  PRO A 134      -4.626  -3.876   1.211  1.00 47.42           C  
ANISOU  937  CD  PRO A 134     6250   5936   5830   -868    457    256       C  
ATOM    938  N   ALA A 135      -7.535  -6.088   1.643  1.00 39.89           N  
ANISOU  938  N   ALA A 135     5250   4816   5088   -620    359    128       N  
ATOM    939  CA  ALA A 135      -8.443  -7.156   2.057  1.00 39.84           C  
ANISOU  939  CA  ALA A 135     5200   4765   5171   -570    321     93       C  
ATOM    940  C   ALA A 135      -9.549  -6.631   2.961  1.00 42.61           C  
ANISOU  940  C   ALA A 135     5526   5052   5611   -538    309    149       C  
ATOM    941  O   ALA A 135     -10.704  -7.054   2.847  1.00 39.85           O  
ANISOU  941  O   ALA A 135     5127   4699   5314   -522    257    166       O  
ATOM    942  CB  ALA A 135      -7.663  -8.254   2.774  1.00 39.32           C  
ANISOU  942  CB  ALA A 135     5104   4707   5129   -548    355     25       C  
ATOM    943  N   LEU A 136      -9.217  -5.731   3.885  1.00 41.11           N  
ANISOU  943  N   LEU A 136     5366   4825   5429   -525    352    179       N  
ATOM    944  CA  LEU A 136     -10.257  -5.153   4.731  1.00 36.82           C  
ANISOU  944  CA  LEU A 136     4814   4238   4939   -449    351    223       C  
ATOM    945  C   LEU A 136     -11.240  -4.322   3.904  1.00 39.67           C  
ANISOU  945  C   LEU A 136     5199   4597   5274   -402    286    270       C  
ATOM    946  O   LEU A 136     -12.458  -4.419   4.094  1.00 39.49           O  
ANISOU  946  O   LEU A 136     5095   4605   5303   -330    264    298       O  
ATOM    947  CB  LEU A 136      -9.620  -4.303   5.839  1.00 38.58           C  
ANISOU  947  CB  LEU A 136     5115   4395   5147   -428    389    234       C  
ATOM    948  CG  LEU A 136     -10.606  -3.769   6.865  1.00 41.02           C  
ANISOU  948  CG  LEU A 136     5433   4668   5484   -306    403    263       C  
ATOM    949  CD1 LEU A 136     -11.111  -4.927   7.726  1.00 43.81           C  
ANISOU  949  CD1 LEU A 136     5667   5069   5909   -287    456    255       C  
ATOM    950  CD2 LEU A 136      -9.948  -2.673   7.704  1.00 39.36           C  
ANISOU  950  CD2 LEU A 136     5374   4358   5224   -279    402    268       C  
ATOM    951  N   ARG A 137     -10.730  -3.476   2.999  1.00 38.38           N  
ANISOU  951  N   ARG A 137     5144   4412   5025   -443    251    289       N  
ATOM    952  CA  ARG A 137     -11.623  -2.664   2.163  1.00 39.37           C  
ANISOU  952  CA  ARG A 137     5325   4520   5112   -389    169    334       C  
ATOM    953  C   ARG A 137     -12.571  -3.540   1.351  1.00 43.70           C  
ANISOU  953  C   ARG A 137     5767   5140   5696   -382    112    325       C  
ATOM    954  O   ARG A 137     -13.776  -3.263   1.265  1.00 42.67           O  
ANISOU  954  O   ARG A 137     5584   5031   5600   -293     52    359       O  
ATOM    955  CB  ARG A 137     -10.817  -1.774   1.211  1.00 36.87           C  
ANISOU  955  CB  ARG A 137     5160   4170   4680   -474    135    366       C  
ATOM    956  CG  ARG A 137     -10.157  -0.577   1.870  1.00 36.84           C  
ANISOU  956  CG  ARG A 137     5305   4064   4629   -498    132    404       C  
ATOM    957  CD  ARG A 137      -9.618   0.356   0.809  1.00 44.36           C  
ANISOU  957  CD  ARG A 137     6415   4981   5458   -606     74    468       C  
ATOM    958  NE  ARG A 137      -8.568   1.215   1.339  1.00 44.39           N  
ANISOU  958  NE  ARG A 137     6546   4910   5409   -720     70    512       N  
ATOM    959  CZ  ARG A 137      -8.753   2.458   1.758  1.00 54.21           C  
ANISOU  959  CZ  ARG A 137     7995   5992   6609   -690    -20    558       C  
ATOM    960  NH1 ARG A 137      -9.956   3.014   1.770  1.00 49.31           N1+
ANISOU  960  NH1 ARG A 137     7464   5282   5991   -508    -98    557       N1+
ATOM    961  NH2 ARG A 137      -7.707   3.155   2.196  1.00 50.75           N  
ANISOU  961  NH2 ARG A 137     7680   5482   6121   -838    -45    605       N  
ATOM    962  N   GLU A 138     -12.034  -4.600   0.741  1.00 41.49           N  
ANISOU  962  N   GLU A 138     5461   4902   5400   -467    116    278       N  
ATOM    963  CA  GLU A 138     -12.839  -5.507  -0.071  1.00 43.11           C  
ANISOU  963  CA  GLU A 138     5607   5147   5625   -483     32    264       C  
ATOM    964  C   GLU A 138     -13.946  -6.150   0.749  1.00 44.86           C  
ANISOU  964  C   GLU A 138     5682   5398   5965   -460     14    287       C  
ATOM    965  O   GLU A 138     -15.095  -6.243   0.301  1.00 44.71           O  
ANISOU  965  O   GLU A 138     5585   5423   5980   -447    -77    325       O  
ATOM    966  CB  GLU A 138     -11.941  -6.587  -0.676  1.00 44.32           C  
ANISOU  966  CB  GLU A 138     5798   5319   5723   -547     40    192       C  
ATOM    967  CG  GLU A 138     -12.683  -7.537  -1.622  1.00 46.91           C  
ANISOU  967  CG  GLU A 138     6125   5655   6045   -571    -79    168       C  
ATOM    968  CD  GLU A 138     -11.799  -8.644  -2.172  1.00 57.87           C  
ANISOU  968  CD  GLU A 138     7590   7043   7355   -589    -82     78       C  
ATOM    969  OE1 GLU A 138     -10.568  -8.613  -1.941  1.00 57.25           O  
ANISOU  969  OE1 GLU A 138     7538   6996   7220   -573     22     40       O  
ATOM    970  OE2 GLU A 138     -12.341  -9.544  -2.847  1.00 54.24           O1-
ANISOU  970  OE2 GLU A 138     7168   6558   6881   -610   -199     45       O1-
ATOM    971  N   ARG A 139     -13.610  -6.628   1.951  1.00 41.15           N  
ANISOU  971  N   ARG A 139     5164   4919   5552   -467     97    274       N  
ATOM    972  CA  ARG A 139     -14.597  -7.324   2.774  1.00 41.21           C  
ANISOU  972  CA  ARG A 139     5029   4973   5656   -476     96    314       C  
ATOM    973  C   ARG A 139     -15.636  -6.360   3.333  1.00 41.83           C  
ANISOU  973  C   ARG A 139     5013   5116   5763   -359    116    383       C  
ATOM    974  O   ARG A 139     -16.838  -6.653   3.317  1.00 41.00           O  
ANISOU  974  O   ARG A 139     4754   5109   5714   -357     68    442       O  
ATOM    975  CB  ARG A 139     -13.888  -8.076   3.905  1.00 40.54           C  
ANISOU  975  CB  ARG A 139     4950   4853   5602   -510    177    285       C  
ATOM    976  CG  ARG A 139     -13.040  -9.251   3.434  1.00 41.73           C  
ANISOU  976  CG  ARG A 139     5179   4951   5724   -589    139    212       C  
ATOM    977  CD  ARG A 139     -12.239  -9.838   4.597  1.00 40.17           C  
ANISOU  977  CD  ARG A 139     5006   4710   5546   -593    211    181       C  
ATOM    978  NE  ARG A 139     -11.072  -9.006   4.895  1.00 39.76           N  
ANISOU  978  NE  ARG A 139     5016   4646   5444   -539    292    148       N  
ATOM    979  CZ  ARG A 139     -10.367  -9.088   6.015  1.00 44.03           C  
ANISOU  979  CZ  ARG A 139     5576   5157   5997   -521    356    131       C  
ATOM    980  NH1 ARG A 139     -10.658  -9.980   6.944  1.00 38.31           N1+
ANISOU  980  NH1 ARG A 139     4828   4405   5322   -540    363    142       N1+
ATOM    981  NH2 ARG A 139      -9.360  -8.236   6.217  1.00 39.94           N  
ANISOU  981  NH2 ARG A 139     5107   4636   5434   -498    404    115       N  
ATOM    982  N   VAL A 140     -15.199  -5.201   3.827  1.00 39.78           N  
ANISOU  982  N   VAL A 140     4848   4809   5457   -254    176    379       N  
ATOM    983  CA  VAL A 140     -16.154  -4.261   4.406  1.00 38.57           C  
ANISOU  983  CA  VAL A 140     4640   4709   5307    -91    193    428       C  
ATOM    984  C   VAL A 140     -17.112  -3.729   3.340  1.00 41.17           C  
ANISOU  984  C   VAL A 140     4932   5090   5621    -23     82    462       C  
ATOM    985  O   VAL A 140     -18.286  -3.464   3.627  1.00 43.97           O  
ANISOU  985  O   VAL A 140     5139   5562   6004    101     71    512       O  
ATOM    986  CB  VAL A 140     -15.384  -3.135   5.122  1.00 42.13           C  
ANISOU  986  CB  VAL A 140     5266   5052   5692      4    246    405       C  
ATOM    987  CG1 VAL A 140     -16.299  -1.956   5.474  1.00 41.06           C  
ANISOU  987  CG1 VAL A 140     5149   4934   5517    223    231    435       C  
ATOM    988  CG2 VAL A 140     -14.701  -3.685   6.377  1.00 40.49           C  
ANISOU  988  CG2 VAL A 140     5058   4820   5507    -34    347    381       C  
ATOM    989  N   ALA A 141     -16.653  -3.583   2.093  1.00 42.93           N  
ANISOU  989  N   ALA A 141     5275   5247   5788    -94     -3    440       N  
ATOM    990  CA  ALA A 141     -17.555  -3.079   1.056  1.00 46.74           C  
ANISOU  990  CA  ALA A 141     5744   5768   6248    -28   -126    473       C  
ATOM    991  C   ALA A 141     -18.765  -3.983   0.891  1.00 46.45           C  
ANISOU  991  C   ALA A 141     5474   5878   6298    -62   -191    515       C  
ATOM    992  O   ALA A 141     -19.854  -3.508   0.536  1.00 45.40           O  
ANISOU  992  O   ALA A 141     5239   5836   6173     49   -276    562       O  
ATOM    993  CB  ALA A 141     -16.827  -2.936  -0.282  1.00 42.09           C  
ANISOU  993  CB  ALA A 141     5330   5095   5568   -122   -200    448       C  
ATOM    994  N   LEU A 142     -18.598  -5.282   1.144  1.00 44.86           N  
ANISOU  994  N   LEU A 142     5189   5699   6157   -219   -170    506       N  
ATOM    995  CA  LEU A 142     -19.707  -6.222   1.049  1.00 48.01           C  
ANISOU  995  CA  LEU A 142     5377   6226   6639   -308   -250    565       C  
ATOM    996  C   LEU A 142     -20.692  -6.088   2.201  1.00 50.24           C  
ANISOU  996  C   LEU A 142     5426   6676   6986   -219   -171    644       C  
ATOM    997  O   LEU A 142     -21.773  -6.684   2.142  1.00 49.37           O  
ANISOU  997  O   LEU A 142     5094   6721   6944   -291   -239    722       O  
ATOM    998  CB  LEU A 142     -19.168  -7.652   0.977  1.00 43.61           C  
ANISOU  998  CB  LEU A 142     4859   5602   6107   -509   -275    532       C  
ATOM    999  CG  LEU A 142     -18.217  -7.888  -0.203  1.00 46.91           C  
ANISOU  999  CG  LEU A 142     5494   5891   6437   -567   -344    447       C  
ATOM   1000  CD1 LEU A 142     -17.534  -9.219  -0.047  1.00 46.10           C  
ANISOU 1000  CD1 LEU A 142     5466   5710   6341   -699   -348    394       C  
ATOM   1001  CD2 LEU A 142     -18.975  -7.846  -1.527  1.00 53.99           C  
ANISOU 1001  CD2 LEU A 142     6393   6814   7308   -588   -519    464       C  
ATOM   1002  N   LEU A 143     -20.362  -5.309   3.227  1.00 45.89           N  
ANISOU 1002  N   LEU A 143     4920   6112   6404    -66    -35    631       N  
ATOM   1003  CA  LEU A 143     -21.271  -5.036   4.332  1.00 46.47           C  
ANISOU 1003  CA  LEU A 143     4792   6362   6502     73     60    698       C  
ATOM   1004  C   LEU A 143     -22.116  -3.787   4.110  1.00 48.24           C  
ANISOU 1004  C   LEU A 143     4969   6680   6682    334     23    717       C  
ATOM   1005  O   LEU A 143     -22.920  -3.437   4.981  1.00 52.78           O  
ANISOU 1005  O   LEU A 143     5371   7431   7253    509    108    766       O  
ATOM   1006  CB  LEU A 143     -20.471  -4.897   5.636  1.00 46.31           C  
ANISOU 1006  CB  LEU A 143     4877   6269   6451    125    218    664       C  
ATOM   1007  CG  LEU A 143     -19.461  -6.010   5.949  1.00 45.40           C  
ANISOU 1007  CG  LEU A 143     4851   6036   6362    -87    253    630       C  
ATOM   1008  CD1 LEU A 143     -18.807  -5.796   7.307  1.00 49.02           C  
ANISOU 1008  CD1 LEU A 143     5395   6444   6786    -14    395    606       C  
ATOM   1009  CD2 LEU A 143     -20.157  -7.369   5.907  1.00 45.99           C  
ANISOU 1009  CD2 LEU A 143     4737   6221   6517   -289    206    704       C  
ATOM   1010  N   LYS A 144     -21.951  -3.108   2.980  1.00 48.19           N  
ANISOU 1010  N   LYS A 144     5120   6564   6627    380   -101    681       N  
ATOM   1011  CA  LYS A 144     -22.719  -1.904   2.703  1.00 52.92           C  
ANISOU 1011  CA  LYS A 144     5718   7218   7171    645   -166    694       C  
ATOM   1012  C   LYS A 144     -24.208  -2.188   2.847  1.00 57.44           C  
ANISOU 1012  C   LYS A 144     5932   8087   7807    728   -190    783       C  
ATOM   1013  O   LYS A 144     -24.715  -3.181   2.322  1.00 56.33           O  
ANISOU 1013  O   LYS A 144     5599   8056   7746    526   -272    838       O  
ATOM   1014  CB  LYS A 144     -22.400  -1.406   1.289  1.00 48.80           C  
ANISOU 1014  CB  LYS A 144     5404   6546   6592    617   -325    663       C  
ATOM   1015  CG  LYS A 144     -23.249  -0.240   0.798  1.00 53.55           C  
ANISOU 1015  CG  LYS A 144     6029   7185   7133    881   -440    679       C  
ATOM   1016  CD  LYS A 144     -23.017   0.011  -0.701  1.00 55.77           C  
ANISOU 1016  CD  LYS A 144     6497   7336   7359    801   -610    667       C  
ATOM   1017  CE  LYS A 144     -21.575   0.418  -1.015  1.00 60.56           C  
ANISOU 1017  CE  LYS A 144     7449   7687   7872    686   -585    615       C  
ATOM   1018  NZ  LYS A 144     -21.480   1.183  -2.304  1.00 62.77           N1+
ANISOU 1018  NZ  LYS A 144     7959   7843   8049    707   -742    620       N1+
ATOM   1019  N   GLY A 145     -24.897  -1.339   3.600  1.00 54.47           N  
ANISOU 1019  N   GLY A 145     5462   7848   7385   1027   -123    799       N  
ATOM   1020  CA  GLY A 145     -26.331  -1.439   3.769  1.00 62.60           C  
ANISOU 1020  CA  GLY A 145     6119   9211   8457   1157   -131    890       C  
ATOM   1021  C   GLY A 145     -26.788  -2.144   5.032  1.00 62.05           C  
ANISOU 1021  C   GLY A 145     5765   9384   8426   1120     46    966       C  
ATOM   1022  O   GLY A 145     -27.957  -2.007   5.406  1.00 70.50           O  
ANISOU 1022  O   GLY A 145     6513  10775   9500   1292     84   1047       O  
ATOM   1023  N   LEU A 146     -25.913  -2.893   5.689  1.00 56.37           N  
ANISOU 1023  N   LEU A 146     5150   8542   7727    907    154    950       N  
ATOM   1024  CA  LEU A 146     -26.304  -3.604   6.902  1.00 57.01           C  
ANISOU 1024  CA  LEU A 146     4993   8838   7831    847    320   1034       C  
ATOM   1025  C   LEU A 146     -26.749  -2.612   7.972  1.00 63.49           C  
ANISOU 1025  C   LEU A 146     5767   9812   8544   1227    471   1026       C  
ATOM   1026  O   LEU A 146     -26.049  -1.618   8.216  1.00 64.50           O  
ANISOU 1026  O   LEU A 146     6210   9721   8576   1443    490    919       O  
ATOM   1027  CB  LEU A 146     -25.141  -4.438   7.433  1.00 60.56           C  
ANISOU 1027  CB  LEU A 146     5637   9074   8298    597    393    998       C  
ATOM   1028  CG  LEU A 146     -24.826  -5.760   6.741  1.00 63.95           C  
ANISOU 1028  CG  LEU A 146     6065   9411   8823    219    281   1025       C  
ATOM   1029  CD1 LEU A 146     -23.717  -6.486   7.493  1.00 57.91           C  
ANISOU 1029  CD1 LEU A 146     5488   8462   8055     54    372    984       C  
ATOM   1030  CD2 LEU A 146     -26.069  -6.623   6.632  1.00 61.98           C  
ANISOU 1030  CD2 LEU A 146     5447   9450   8655     48    228   1173       C  
ATOM   1031  N   PRO A 147     -27.884  -2.846   8.634  1.00 69.33           N  
ANISOU 1031  N   PRO A 147     6131  10927   9284   1316    576   1140       N  
ATOM   1032  CA  PRO A 147     -28.349  -1.914   9.668  1.00 71.65           C  
ANISOU 1032  CA  PRO A 147     6379  11397   9447   1724    733   1124       C  
ATOM   1033  C   PRO A 147     -27.418  -1.935  10.865  1.00 73.37           C  
ANISOU 1033  C   PRO A 147     6843  11446   9587   1734    894   1067       C  
ATOM   1034  O   PRO A 147     -26.900  -2.981  11.247  1.00 66.68           O  
ANISOU 1034  O   PRO A 147     5996  10540   8799   1417    949   1109       O  
ATOM   1035  CB  PRO A 147     -29.724  -2.469  10.057  1.00 77.26           C  
ANISOU 1035  CB  PRO A 147     6571  12597  10186   1723    823   1290       C  
ATOM   1036  CG  PRO A 147     -29.666  -3.913   9.665  1.00 69.07           C  
ANISOU 1036  CG  PRO A 147     5386  11566   9293   1223    755   1396       C  
ATOM   1037  CD  PRO A 147     -28.808  -3.973   8.442  1.00 72.12           C  
ANISOU 1037  CD  PRO A 147     6084  11575   9744   1042    548   1296       C  
ATOM   1038  N   LEU A 148     -27.237  -0.772  11.490  1.00 68.37           N  
ANISOU 1038  N   LEU A 148     6435  10733   8810   2114    955    971       N  
ATOM   1039  CA  LEU A 148     -26.343  -0.712  12.644  1.00 62.61           C  
ANISOU 1039  CA  LEU A 148     5967   9830   7993   2139   1086    910       C  
ATOM   1040  C   LEU A 148     -26.741  -1.682  13.754  1.00 70.83           C  
ANISOU 1040  C   LEU A 148     6738  11146   9028   2017   1284   1025       C  
ATOM   1041  O   LEU A 148     -25.881  -2.079  14.548  1.00 69.37           O  
ANISOU 1041  O   LEU A 148     6746  10795   8817   1886   1364    998       O  
ATOM   1042  CB  LEU A 148     -26.286   0.712  13.190  1.00 70.33           C  
ANISOU 1042  CB  LEU A 148     7219  10708   8794   2597   1103    797       C  
ATOM   1043  CG  LEU A 148     -25.412   1.666  12.377  1.00 73.66           C  
ANISOU 1043  CG  LEU A 148     8066  10728   9195   2642    909    675       C  
ATOM   1044  CD1 LEU A 148     -25.808   3.109  12.639  1.00 68.94           C  
ANISOU 1044  CD1 LEU A 148     7678  10092   8425   3134    870    590       C  
ATOM   1045  CD2 LEU A 148     -23.936   1.428  12.680  1.00 66.44           C  
ANISOU 1045  CD2 LEU A 148     7486   9466   8294   2384    899    610       C  
ATOM   1046  N   SER A 149     -27.989  -2.123  13.793  1.00 77.95           N  
ANISOU 1046  N   SER A 149     7196  12466   9956   2023   1354   1165       N  
ATOM   1047  CA  SER A 149     -28.450  -3.080  14.802  1.00 65.13           C  
ANISOU 1047  CA  SER A 149     5290  11137   8318   1865   1541   1309       C  
ATOM   1048  C   SER A 149     -27.727  -4.397  14.741  1.00 70.22           C  
ANISOU 1048  C   SER A 149     5997  11600   9083   1376   1500   1362       C  
ATOM   1049  O   SER A 149     -27.683  -5.125  15.715  1.00 77.25           O  
ANISOU 1049  O   SER A 149     6824  12589   9938   1232   1643   1446       O  
ATOM   1050  CB  SER A 149     -29.929  -3.352  14.598  1.00 71.50           C  
ANISOU 1050  CB  SER A 149     5572  12439   9156   1890   1581   1473       C  
ATOM   1051  OG  SER A 149     -30.198  -3.673  13.253  1.00 85.18           O  
ANISOU 1051  OG  SER A 149     7184  14139  11040   1670   1367   1504       O  
ATOM   1052  N   VAL A 150     -27.166  -4.712  13.592  1.00 70.21           N  
ANISOU 1052  N   VAL A 150     6135  11334   9207   1135   1302   1311       N  
ATOM   1053  CA  VAL A 150     -26.481  -5.976  13.404  1.00 78.65           C  
ANISOU 1053  CA  VAL A 150     7286  12215  10381    704   1234   1345       C  
ATOM   1054  C   VAL A 150     -25.306  -6.145  14.356  1.00 80.57           C  
ANISOU 1054  C   VAL A 150     7848  12203  10562    671   1322   1268       C  
ATOM   1055  O   VAL A 150     -25.064  -7.225  14.856  1.00 80.00           O  
ANISOU 1055  O   VAL A 150     7763  12115  10520    398   1359   1342       O  
ATOM   1056  CB  VAL A 150     -26.050  -6.103  11.930  1.00 78.30           C  
ANISOU 1056  CB  VAL A 150     7373  11930  10447    534   1005   1276       C  
ATOM   1057  CG1 VAL A 150     -25.013  -7.173  11.707  1.00 85.29           C  
ANISOU 1057  CG1 VAL A 150     8471  12531  11404    188    923   1246       C  
ATOM   1058  CG2 VAL A 150     -27.249  -6.377  11.045  1.00 89.21           C  
ANISOU 1058  CG2 VAL A 150     8407  13576  11911    444    892   1389       C  
ATOM   1059  N   ILE A 151     -24.600  -5.070  14.639  1.00 66.19           N  
ANISOU 1059  N   ILE A 151     6321  10182   8647    948   1343   1127       N  
ATOM   1060  CA  ILE A 151     -23.442  -5.173  15.487  1.00 67.74           C  
ANISOU 1060  CA  ILE A 151     6821  10130   8788    914   1397   1050       C  
ATOM   1061  C   ILE A 151     -23.795  -5.752  16.834  1.00 70.44           C  
ANISOU 1061  C   ILE A 151     7042  10672   9050    896   1584   1152       C  
ATOM   1062  O   ILE A 151     -23.273  -6.789  17.213  1.00 66.38           O  
ANISOU 1062  O   ILE A 151     6584  10063   8574    622   1590   1194       O  
ATOM   1063  CB  ILE A 151     -22.746  -3.825  15.629  1.00 62.26           C  
ANISOU 1063  CB  ILE A 151     6455   9211   7991   1216   1372    900       C  
ATOM   1064  CG1 ILE A 151     -22.141  -3.425  14.286  1.00 70.25           C  
ANISOU 1064  CG1 ILE A 151     7632   9979   9080   1143   1182    813       C  
ATOM   1065  CG2 ILE A 151     -21.655  -3.891  16.679  1.00 70.43           C  
ANISOU 1065  CG2 ILE A 151     7773  10035   8953   1199   1433    834       C  
ATOM   1066  CD1 ILE A 151     -22.157  -1.941  14.022  1.00 70.62           C  
ANISOU 1066  CD1 ILE A 151     7873   9926   9034   1468   1120    721       C  
ATOM   1067  N   ASP A 152     -24.689  -5.085  17.554  1.00 67.16           N  
ANISOU 1067  N   ASP A 152     6469  10540   8508   1204   1734   1193       N  
ATOM   1068  CA  ASP A 152     -25.098  -5.580  18.864  1.00 69.15           C  
ANISOU 1068  CA  ASP A 152     6591  11028   8653   1208   1937   1304       C  
ATOM   1069  C   ASP A 152     -25.566  -7.025  18.777  1.00 69.94           C  
ANISOU 1069  C   ASP A 152     6419  11297   8859    792   1940   1485       C  
ATOM   1070  O   ASP A 152     -25.271  -7.839  19.661  1.00 75.16           O  
ANISOU 1070  O   ASP A 152     7132  11944   9479    608   2025   1558       O  
ATOM   1071  CB  ASP A 152     -26.210  -4.698  19.426  1.00 83.04           C  
ANISOU 1071  CB  ASP A 152     8137  13153  10260   1615   2099   1339       C  
ATOM   1072  CG  ASP A 152     -25.682  -3.434  20.061  1.00104.30           C  
ANISOU 1072  CG  ASP A 152    11180  15665  12783   2030   2134   1173       C  
ATOM   1073  OD1 ASP A 152     -24.598  -3.488  20.682  1.00 95.27           O  
ANISOU 1073  OD1 ASP A 152    10377  14227  11596   1973   2126   1090       O  
ATOM   1074  OD2 ASP A 152     -26.355  -2.387  19.929  1.00116.46           O1-
ANISOU 1074  OD2 ASP A 152    12668  17351  14230   2418   2151   1125       O1-
ATOM   1075  N   LYS A 153     -26.294  -7.358  17.708  1.00 73.16           N  
ANISOU 1075  N   LYS A 153     6558  11846   9393    631   1825   1565       N  
ATOM   1076  CA  LYS A 153     -26.788  -8.717  17.513  1.00 72.56           C  
ANISOU 1076  CA  LYS A 153     6243  11906   9419    206   1780   1744       C  
ATOM   1077  C   LYS A 153     -25.638  -9.716  17.461  1.00 70.56           C  
ANISOU 1077  C   LYS A 153     6296  11276   9236   -120   1665   1701       C  
ATOM   1078  O   LYS A 153     -25.661 -10.746  18.144  1.00 69.86           O  
ANISOU 1078  O   LYS A 153     6183  11227   9135   -382   1712   1825       O  
ATOM   1079  CB  LYS A 153     -27.616  -8.775  16.226  1.00 75.25           C  
ANISOU 1079  CB  LYS A 153     6313  12392   9887    105   1622   1801       C  
ATOM   1080  CG  LYS A 153     -28.234 -10.128  15.909  1.00 87.34           C  
ANISOU 1080  CG  LYS A 153     7596  14064  11526   -351   1531   1995       C  
ATOM   1081  CD  LYS A 153     -28.642 -10.203  14.441  1.00 87.57           C  
ANISOU 1081  CD  LYS A 153     7508  14073  11691   -476   1300   1991       C  
ATOM   1082  CE  LYS A 153     -28.647 -11.635  13.933  1.00 83.98           C  
ANISOU 1082  CE  LYS A 153     7059  13500  11348   -969   1114   2096       C  
ATOM   1083  NZ  LYS A 153     -29.505 -11.790  12.726  1.00 87.35           N1+
ANISOU 1083  NZ  LYS A 153     7285  14030  11874  -1099    904   2140       N1+
ATOM   1084  N   VAL A 154     -24.614  -9.415  16.660  1.00 74.60           N  
ANISOU 1084  N   VAL A 154     7103  11431   9810    -96   1512   1528       N  
ATOM   1085  CA  VAL A 154     -23.486 -10.330  16.501  1.00 71.97           C  
ANISOU 1085  CA  VAL A 154     7049  10758   9538   -358   1392   1469       C  
ATOM   1086  C   VAL A 154     -22.739 -10.494  17.817  1.00 67.41           C  
ANISOU 1086  C   VAL A 154     6686  10071   8857   -318   1516   1447       C  
ATOM   1087  O   VAL A 154     -22.427 -11.615  18.240  1.00 63.78           O  
ANISOU 1087  O   VAL A 154     6303   9521   8410   -579   1492   1515       O  
ATOM   1088  CB  VAL A 154     -22.552  -9.830  15.388  1.00 63.63           C  
ANISOU 1088  CB  VAL A 154     6231   9401   8543   -296   1232   1292       C  
ATOM   1089  CG1 VAL A 154     -21.252 -10.599  15.425  1.00 57.42           C  
ANISOU 1089  CG1 VAL A 154     5742   8292   7783   -471   1148   1208       C  
ATOM   1090  CG2 VAL A 154     -23.231  -9.959  14.036  1.00 72.50           C  
ANISOU 1090  CG2 VAL A 154     7178  10598   9769   -406   1078   1325       C  
ATOM   1091  N   ILE A 155     -22.425  -9.376  18.473  1.00 63.33           N  
ANISOU 1091  N   ILE A 155     6300   9537   8227     14   1628   1348       N  
ATOM   1092  CA  ILE A 155     -21.706  -9.429  19.744  1.00 68.35           C  
ANISOU 1092  CA  ILE A 155     7159  10063   8749     79   1733   1317       C  
ATOM   1093  C   ILE A 155     -22.456 -10.297  20.742  1.00 74.29           C  
ANISOU 1093  C   ILE A 155     7729  11065   9432    -72   1875   1505       C  
ATOM   1094  O   ILE A 155     -21.892 -11.219  21.345  1.00 65.31           O  
ANISOU 1094  O   ILE A 155     6746   9789   8281   -276   1864   1543       O  
ATOM   1095  CB  ILE A 155     -21.484  -8.006  20.289  1.00 71.92           C  
ANISOU 1095  CB  ILE A 155     7764  10492   9069    476   1819   1195       C  
ATOM   1096  CG1 ILE A 155     -20.682  -7.171  19.284  1.00 64.29           C  
ANISOU 1096  CG1 ILE A 155     7001   9260   8167    570   1660   1031       C  
ATOM   1097  CG2 ILE A 155     -20.815  -8.052  21.657  1.00 75.92           C  
ANISOU 1097  CG2 ILE A 155     8505  10900   9442    549   1919   1168       C  
ATOM   1098  CD1 ILE A 155     -20.287  -5.805  19.801  1.00 68.67           C  
ANISOU 1098  CD1 ILE A 155     7790   9709   8591    914   1692    906       C  
ATOM   1099  N   SER A 156     -23.754 -10.036  20.898  1.00 72.96           N  
ANISOU 1099  N   SER A 156     7223  11285   9214     21   2006   1636       N  
ATOM   1100  CA  SER A 156     -24.520 -10.669  21.957  1.00 79.72           C  
ANISOU 1100  CA  SER A 156     7881  12442   9966    -84   2182   1831       C  
ATOM   1101  C   SER A 156     -24.694 -12.163  21.721  1.00 78.38           C  
ANISOU 1101  C   SER A 156     7626  12255   9898   -559   2079   1995       C  
ATOM   1102  O   SER A 156     -24.789 -12.931  22.683  1.00 82.83           O  
ANISOU 1102  O   SER A 156     8209  12883  10377   -731   2165   2123       O  
ATOM   1103  CB  SER A 156     -25.879  -9.981  22.071  1.00 81.69           C  
ANISOU 1103  CB  SER A 156     7754  13148  10139    149   2337   1927       C  
ATOM   1104  OG  SER A 156     -25.725  -8.691  22.641  1.00 95.95           O  
ANISOU 1104  OG  SER A 156     9692  14974  11792    613   2463   1794       O  
ATOM   1105  N   THR A 157     -24.722 -12.598  20.461  1.00 68.24           N  
ANISOU 1105  N   THR A 157     6294  10855   8780   -773   1872   1984       N  
ATOM   1106  CA  THR A 157     -25.102 -13.967  20.139  1.00 69.41           C  
ANISOU 1106  CA  THR A 157     6348  11008   9015  -1219   1743   2150       C  
ATOM   1107  C   THR A 157     -24.006 -14.835  19.532  1.00 71.71           C  
ANISOU 1107  C   THR A 157     6977  10864   9405  -1448   1514   2050       C  
ATOM   1108  O   THR A 157     -24.129 -16.063  19.583  1.00 70.46           O  
ANISOU 1108  O   THR A 157     6856  10640   9277  -1804   1408   2179       O  
ATOM   1109  CB  THR A 157     -26.318 -13.972  19.197  1.00 80.53           C  
ANISOU 1109  CB  THR A 157     7443  12643  10514  -1300   1636   2208       C  
ATOM   1110  CG2 THR A 157     -27.281 -12.834  19.518  1.00 83.13           C  
ANISOU 1110  CG2 THR A 157     7497  13335  10753   -948   1807   2210       C  
ATOM   1111  OG1 THR A 157     -25.877 -13.925  17.829  1.00 77.41           O  
ANISOU 1111  OG1 THR A 157     7097  12055  10260  -1368   1445   2132       O  
ATOM   1112  N   ARG A 158     -22.947 -14.265  18.966  1.00 66.60           N  
ANISOU 1112  N   ARG A 158     6587   9920   8796  -1256   1425   1827       N  
ATOM   1113  CA  ARG A 158     -21.949 -15.110  18.322  1.00 64.68           C  
ANISOU 1113  CA  ARG A 158     6632   9310   8634  -1443   1213   1730       C  
ATOM   1114  C   ARG A 158     -20.503 -14.867  18.734  1.00 59.19           C  
ANISOU 1114  C   ARG A 158     6284   8311   7894  -1274   1210   1547       C  
ATOM   1115  O   ARG A 158     -19.639 -15.644  18.316  1.00 60.45           O  
ANISOU 1115  O   ARG A 158     6676   8192   8101  -1405   1048   1470       O  
ATOM   1116  CB  ARG A 158     -22.044 -14.992  16.793  1.00 65.78           C  
ANISOU 1116  CB  ARG A 158     6723   9379   8892  -1479   1033   1653       C  
ATOM   1117  CG  ARG A 158     -23.377 -15.459  16.211  1.00 68.97           C  
ANISOU 1117  CG  ARG A 158     6810  10033   9362  -1714    961   1832       C  
ATOM   1118  CD  ARG A 158     -23.176 -16.005  14.813  1.00 62.11           C  
ANISOU 1118  CD  ARG A 158     6043   8958   8598  -1883    706   1765       C  
ATOM   1119  NE  ARG A 158     -23.023 -14.921  13.848  1.00 70.41           N  
ANISOU 1119  NE  ARG A 158     7072   9998   9682  -1631    682   1619       N  
ATOM   1120  CZ  ARG A 158     -24.019 -14.338  13.193  1.00 81.97           C  
ANISOU 1120  CZ  ARG A 158     8257  11702  11187  -1575    667   1674       C  
ATOM   1121  NH1 ARG A 158     -25.276 -14.735  13.342  1.00 69.50           N1+
ANISOU 1121  NH1 ARG A 158     6353  10424   9630  -1761    673   1876       N1+
ATOM   1122  NH2 ARG A 158     -23.746 -13.332  12.367  1.00 69.45           N  
ANISOU 1122  NH2 ARG A 158     6715  10060   9612  -1335    639   1532       N  
ATOM   1123  N   ILE A 159     -20.199 -13.846  19.525  1.00 53.39           N  
ANISOU 1123  N   ILE A 159     5601   7621   7065   -985   1366   1474       N  
ATOM   1124  CA  ILE A 159     -18.823 -13.618  19.962  1.00 50.64           C  
ANISOU 1124  CA  ILE A 159     5567   6998   6675   -852   1345   1315       C  
ATOM   1125  C   ILE A 159     -18.605 -14.305  21.304  1.00 57.06           C  
ANISOU 1125  C   ILE A 159     6510   7784   7385   -929   1421   1396       C  
ATOM   1126  O   ILE A 159     -19.419 -14.171  22.224  1.00 53.50           O  
ANISOU 1126  O   ILE A 159     5920   7575   6832   -895   1590   1527       O  
ATOM   1127  CB  ILE A 159     -18.502 -12.116  20.042  1.00 54.76           C  
ANISOU 1127  CB  ILE A 159     6135   7527   7144   -517   1425   1183       C  
ATOM   1128  CG1 ILE A 159     -18.692 -11.456  18.674  1.00 55.76           C  
ANISOU 1128  CG1 ILE A 159     6164   7660   7362   -454   1333   1111       C  
ATOM   1129  CG2 ILE A 159     -17.063 -11.903  20.504  1.00 53.71           C  
ANISOU 1129  CG2 ILE A 159     6311   7124   6974   -420   1380   1036       C  
ATOM   1130  CD1 ILE A 159     -17.849 -12.093  17.580  1.00 52.50           C  
ANISOU 1130  CD1 ILE A 159     5883   7011   7054   -617   1144   1023       C  
ATOM   1131  N   THR A 160     -17.517 -15.067  21.409  1.00 47.81           N  
ANISOU 1131  N   THR A 160     5604   6331   6229  -1025   1295   1323       N  
ATOM   1132  CA  THR A 160     -17.148 -15.726  22.656  1.00 52.05           C  
ANISOU 1132  CA  THR A 160     6320   6792   6663  -1086   1335   1383       C  
ATOM   1133  C   THR A 160     -15.711 -15.370  23.024  1.00 54.84           C  
ANISOU 1133  C   THR A 160     6952   6898   6987   -908   1282   1204       C  
ATOM   1134  O   THR A 160     -14.851 -15.198  22.156  1.00 47.71           O  
ANISOU 1134  O   THR A 160     6134   5827   6168   -858   1155   1057       O  
ATOM   1135  CB  THR A 160     -17.288 -17.251  22.567  1.00 56.64           C  
ANISOU 1135  CB  THR A 160     6976   7268   7278  -1415   1199   1501       C  
ATOM   1136  CG2 THR A 160     -18.732 -17.647  22.267  1.00 57.07           C  
ANISOU 1136  CG2 THR A 160     6741   7583   7360  -1643   1234   1706       C  
ATOM   1137  OG1 THR A 160     -16.407 -17.755  21.552  1.00 55.18           O  
ANISOU 1137  OG1 THR A 160     6956   6816   7193  -1461    987   1364       O  
ATOM   1138  N   LEU A 161     -15.461 -15.250  24.325  1.00 45.83           N  
ANISOU 1138  N   LEU A 161     5944   5755   5716   -817   1381   1226       N  
ATOM   1139  CA  LEU A 161     -14.127 -14.911  24.806  1.00 50.14           C  
ANISOU 1139  CA  LEU A 161     6745   6083   6223   -660   1320   1073       C  
ATOM   1140  C   LEU A 161     -13.226 -16.140  24.781  1.00 43.70           C  
ANISOU 1140  C   LEU A 161     6136   5025   5443   -811   1145   1044       C  
ATOM   1141  O   LEU A 161     -13.632 -17.233  25.180  1.00 46.87           O  
ANISOU 1141  O   LEU A 161     6585   5411   5811  -1008   1121   1176       O  
ATOM   1142  CB  LEU A 161     -14.198 -14.349  26.228  1.00 49.01           C  
ANISOU 1142  CB  LEU A 161     6696   6015   5909   -497   1469   1102       C  
ATOM   1143  CG  LEU A 161     -15.108 -13.140  26.485  1.00 50.01           C  
ANISOU 1143  CG  LEU A 161     6664   6387   5951   -286   1653   1126       C  
ATOM   1144  CD1 LEU A 161     -15.041 -12.716  27.950  1.00 52.80           C  
ANISOU 1144  CD1 LEU A 161     7177   6778   6107   -111   1781   1139       C  
ATOM   1145  CD2 LEU A 161     -14.736 -11.974  25.577  1.00 47.78           C  
ANISOU 1145  CD2 LEU A 161     6360   6050   5746   -112   1595    974       C  
ATOM   1146  N   THR A 162     -11.999 -15.959  24.322  1.00 45.88           N  
ANISOU 1146  N   THR A 162     6539   5116   5775   -715   1017    878       N  
ATOM   1147  CA  THR A 162     -11.054 -17.064  24.332  1.00 45.88           C  
ANISOU 1147  CA  THR A 162     6743   4896   5793   -791    847    829       C  
ATOM   1148  C   THR A 162     -10.742 -17.474  25.768  1.00 44.38           C  
ANISOU 1148  C   THR A 162     6755   4631   5475   -778    866    880       C  
ATOM   1149  O   THR A 162     -10.498 -16.597  26.613  1.00 43.09           O  
ANISOU 1149  O   THR A 162     6639   4508   5225   -618    957    847       O  
ATOM   1150  CB  THR A 162      -9.779 -16.658  23.617  1.00 42.33           C  
ANISOU 1150  CB  THR A 162     6345   4328   5413   -658    733    646       C  
ATOM   1151  CG2 THR A 162      -8.722 -17.777  23.714  1.00 35.88           C  
ANISOU 1151  CG2 THR A 162     5735   3303   4594   -675    558    580       C  
ATOM   1152  OG1 THR A 162     -10.086 -16.387  22.247  1.00 42.51           O  
ANISOU 1152  OG1 THR A 162     6202   4412   5536   -686    711    610       O  
ATOM   1153  N   PRO A 163     -10.766 -18.774  26.090  1.00 44.66           N  
ANISOU 1153  N   PRO A 163     6942   4546   5481   -944    768    964       N  
ATOM   1154  CA  PRO A 163     -10.450 -19.212  27.458  1.00 41.81           C  
ANISOU 1154  CA  PRO A 163     6804   4099   4985   -937    772   1020       C  
ATOM   1155  C   PRO A 163      -9.132 -18.631  27.956  1.00 44.72           C  
ANISOU 1155  C   PRO A 163     7321   4349   5322   -715    712    859       C  
ATOM   1156  O   PRO A 163      -8.145 -18.554  27.221  1.00 39.77           O  
ANISOU 1156  O   PRO A 163     6706   3621   4786   -626    582    709       O  
ATOM   1157  CB  PRO A 163     -10.375 -20.738  27.328  1.00 45.17           C  
ANISOU 1157  CB  PRO A 163     7411   4336   5416  -1135    595   1086       C  
ATOM   1158  CG  PRO A 163     -11.300 -21.044  26.216  1.00 47.90           C  
ANISOU 1158  CG  PRO A 163     7573   4766   5862  -1315    582   1157       C  
ATOM   1159  CD  PRO A 163     -11.179 -19.906  25.237  1.00 42.64           C  
ANISOU 1159  CD  PRO A 163     6687   4216   5298  -1157    639   1026       C  
ATOM   1160  N   GLY A 164      -9.130 -18.210  29.222  1.00 45.28           N  
ANISOU 1160  N   GLY A 164     7500   4452   5253   -628    807    898       N  
ATOM   1161  CA  GLY A 164      -7.950 -17.650  29.848  1.00 40.96           C  
ANISOU 1161  CA  GLY A 164     7109   3795   4659   -440    735    765       C  
ATOM   1162  C   GLY A 164      -7.793 -16.153  29.720  1.00 39.41           C  
ANISOU 1162  C   GLY A 164     6809   3693   4471   -269    814    668       C  
ATOM   1163  O   GLY A 164      -6.961 -15.571  30.434  1.00 39.90           O  
ANISOU 1163  O   GLY A 164     7014   3678   4466   -132    763    584       O  
ATOM   1164  N   GLY A 165      -8.545 -15.508  28.831  1.00 40.27           N  
ANISOU 1164  N   GLY A 165     6694   3950   4656   -277    912    678       N  
ATOM   1165  CA  GLY A 165      -8.338 -14.112  28.513  1.00 38.67           C  
ANISOU 1165  CA  GLY A 165     6420   3799   4473   -124    947    579       C  
ATOM   1166  C   GLY A 165      -8.558 -13.180  29.694  1.00 41.35           C  
ANISOU 1166  C   GLY A 165     6880   4184   4647     36   1053    586       C  
ATOM   1167  O   GLY A 165      -7.687 -12.374  30.048  1.00 40.69           O  
ANISOU 1167  O   GLY A 165     6930   4001   4528    160    973    479       O  
ATOM   1168  N   PRO A 166      -9.737 -13.250  30.317  1.00 42.90           N  
ANISOU 1168  N   PRO A 166     7031   4542   4728     39   1231    717       N  
ATOM   1169  CA  PRO A 166      -9.956 -12.408  31.512  1.00 41.06           C  
ANISOU 1169  CA  PRO A 166     6943   4358   4300    231   1340    717       C  
ATOM   1170  C   PRO A 166      -8.938 -12.667  32.607  1.00 40.26           C  
ANISOU 1170  C   PRO A 166     7130   4074   4092    272   1228    670       C  
ATOM   1171  O   PRO A 166      -8.426 -11.717  33.208  1.00 46.38           O  
ANISOU 1171  O   PRO A 166     8075   4775   4771    443   1190    577       O  
ATOM   1172  CB  PRO A 166     -11.379 -12.783  31.953  1.00 46.98           C  
ANISOU 1172  CB  PRO A 166     7557   5351   4941    189   1557    894       C  
ATOM   1173  CG  PRO A 166     -12.038 -13.272  30.700  1.00 50.34           C  
ANISOU 1173  CG  PRO A 166     7708   5881   5538     14   1562    958       C  
ATOM   1174  CD  PRO A 166     -10.958 -13.965  29.912  1.00 45.85           C  
ANISOU 1174  CD  PRO A 166     7200   5088   5132   -119   1344    869       C  
ATOM   1175  N   GLN A 167      -8.608 -13.935  32.871  1.00 42.00           N  
ANISOU 1175  N   GLN A 167     7433   4202   4324    121   1148    730       N  
ATOM   1176  CA  GLN A 167      -7.629 -14.216  33.915  1.00 39.91           C  
ANISOU 1176  CA  GLN A 167     7448   3761   3955    172   1023    686       C  
ATOM   1177  C   GLN A 167      -6.271 -13.625  33.555  1.00 41.48           C  
ANISOU 1177  C   GLN A 167     7708   3802   4251    250    821    514       C  
ATOM   1178  O   GLN A 167      -5.571 -13.090  34.422  1.00 44.04           O  
ANISOU 1178  O   GLN A 167     8238   4026   4468    368    740    446       O  
ATOM   1179  CB  GLN A 167      -7.521 -15.726  34.150  1.00 46.16           C  
ANISOU 1179  CB  GLN A 167     8330   4461   4746     -2    947    780       C  
ATOM   1180  CG  GLN A 167      -6.897 -16.093  35.466  1.00 52.48           C  
ANISOU 1180  CG  GLN A 167     9433   5125   5382     52    868    787       C  
ATOM   1181  CD  GLN A 167      -7.366 -17.442  35.960  1.00 70.78           C  
ANISOU 1181  CD  GLN A 167    11858   7416   7620   -123    882    950       C  
ATOM   1182  NE2 GLN A 167      -7.946 -17.474  37.154  1.00 65.21           N  
ANISOU 1182  NE2 GLN A 167    11296   6785   6695   -106   1019   1070       N  
ATOM   1183  OE1 GLN A 167      -7.175 -18.456  35.285  1.00 58.89           O  
ANISOU 1183  OE1 GLN A 167    10331   5811   6234   -270    757    968       O  
ATOM   1184  N   LEU A 168      -5.887 -13.698  32.276  1.00 39.78           N  
ANISOU 1184  N   LEU A 168     7312   3577   4227    179    736    451       N  
ATOM   1185  CA  LEU A 168      -4.627 -13.097  31.834  1.00 39.18           C  
ANISOU 1185  CA  LEU A 168     7241   3404   4242    229    563    310       C  
ATOM   1186  C   LEU A 168      -4.617 -11.600  32.101  1.00 42.14           C  
ANISOU 1186  C   LEU A 168     7673   3791   4548    357    588    250       C  
ATOM   1187  O   LEU A 168      -3.727 -11.074  32.787  1.00 39.62           O  
ANISOU 1187  O   LEU A 168     7530   3360   4162    428    458    178       O  
ATOM   1188  CB  LEU A 168      -4.412 -13.373  30.341  1.00 35.52           C  
ANISOU 1188  CB  LEU A 168     6552   2975   3969    138    513    270       C  
ATOM   1189  CG  LEU A 168      -3.319 -12.556  29.651  1.00 37.30           C  
ANISOU 1189  CG  LEU A 168     6706   3175   4289    167    384    151       C  
ATOM   1190  CD1 LEU A 168      -1.946 -12.830  30.280  1.00 38.73           C  
ANISOU 1190  CD1 LEU A 168     7020   3244   4452    204    193     79       C  
ATOM   1191  CD2 LEU A 168      -3.304 -12.841  28.108  1.00 35.42           C  
ANISOU 1191  CD2 LEU A 168     6238   3008   4212     85    376    127       C  
ATOM   1192  N   VAL A 169      -5.611 -10.895  31.562  1.00 39.59           N  
ANISOU 1192  N   VAL A 169     7216   3592   4232    390    734    280       N  
ATOM   1193  CA  VAL A 169      -5.652  -9.440  31.679  1.00 40.44           C  
ANISOU 1193  CA  VAL A 169     7405   3689   4273    527    738    217       C  
ATOM   1194  C   VAL A 169      -5.750  -9.032  33.144  1.00 44.63           C  
ANISOU 1194  C   VAL A 169     8208   4167   4583    679    765    217       C  
ATOM   1195  O   VAL A 169      -5.008  -8.162  33.617  1.00 42.83           O  
ANISOU 1195  O   VAL A 169     8179   3807   4286    760    630    131       O  
ATOM   1196  CB  VAL A 169      -6.820  -8.875  30.852  1.00 40.33           C  
ANISOU 1196  CB  VAL A 169     7201   3827   4294    564    893    255       C  
ATOM   1197  CG1 VAL A 169      -7.038  -7.383  31.161  1.00 43.53           C  
ANISOU 1197  CG1 VAL A 169     7753   4205   4581    753    902    196       C  
ATOM   1198  CG2 VAL A 169      -6.562  -9.086  29.364  1.00 37.15           C  
ANISOU 1198  CG2 VAL A 169     6573   3448   4095    426    832    233       C  
ATOM   1199  N   ARG A 170      -6.635  -9.688  33.901  1.00 44.20           N  
ANISOU 1199  N   ARG A 170     8180   4214   4401    706    928    322       N  
ATOM   1200  CA  ARG A 170      -6.869  -9.245  35.269  1.00 47.31           C  
ANISOU 1200  CA  ARG A 170     8831   4592   4551    880    988    328       C  
ATOM   1201  C   ARG A 170      -5.687  -9.579  36.175  1.00 46.32           C  
ANISOU 1201  C   ARG A 170     8964   4274   4362    866    797    276       C  
ATOM   1202  O   ARG A 170      -5.336  -8.782  37.052  1.00 46.26           O  
ANISOU 1202  O   ARG A 170     9218   4164   4194   1013    727    210       O  
ATOM   1203  CB  ARG A 170      -8.160  -9.856  35.812  1.00 47.69           C  
ANISOU 1203  CB  ARG A 170     8809   4847   4466    899   1235    475       C  
ATOM   1204  CG  ARG A 170      -9.387  -9.176  35.228  1.00 57.13           C  
ANISOU 1204  CG  ARG A 170     9792   6258   5656   1000   1426    513       C  
ATOM   1205  CD  ARG A 170     -10.634 -10.013  35.381  1.00 67.22           C  
ANISOU 1205  CD  ARG A 170    10871   7790   6879    925   1654    688       C  
ATOM   1206  NE  ARG A 170     -11.676  -9.608  34.445  1.00 63.33           N  
ANISOU 1206  NE  ARG A 170    10084   7511   6469    953   1786    728       N  
ATOM   1207  CZ  ARG A 170     -12.809 -10.270  34.248  1.00 74.79           C  
ANISOU 1207  CZ  ARG A 170    11276   9216   7927    846   1962    888       C  
ATOM   1208  NH1 ARG A 170     -13.171 -11.273  35.034  1.00 60.90           N1+
ANISOU 1208  NH1 ARG A 170     9532   7548   6060    717   2059   1037       N1+
ATOM   1209  NH2 ARG A 170     -13.615  -9.897  33.258  1.00 68.99           N  
ANISOU 1209  NH2 ARG A 170    10264   8652   7299    859   2034    909       N  
ATOM   1210  N   THR A 171      -5.063 -10.751  35.995  1.00 41.85           N  
ANISOU 1210  N   THR A 171     8347   3648   3906    707    694    301       N  
ATOM   1211  CA  THR A 171      -3.869 -11.052  36.786  1.00 47.84           C  
ANISOU 1211  CA  THR A 171     9330   4229   4616    711    486    244       C  
ATOM   1212  C   THR A 171      -2.744 -10.065  36.470  1.00 44.49           C  
ANISOU 1212  C   THR A 171     8945   3689   4271    732    273    112       C  
ATOM   1213  O   THR A 171      -2.034  -9.604  37.367  1.00 45.19           O  
ANISOU 1213  O   THR A 171     9279   3649   4244    805    125     54       O  
ATOM   1214  CB  THR A 171      -3.408 -12.499  36.543  1.00 43.73           C  
ANISOU 1214  CB  THR A 171     8747   3665   4203    567    399    286       C  
ATOM   1215  CG2 THR A 171      -2.177 -12.812  37.377  1.00 43.55           C  
ANISOU 1215  CG2 THR A 171     8949   3473   4126    598    171    225       C  
ATOM   1216  OG1 THR A 171      -4.456 -13.402  36.920  1.00 44.59           O  
ANISOU 1216  OG1 THR A 171     8859   3863   4221    508    574    429       O  
ATOM   1217  N   MET A 172      -2.562  -9.746  35.194  1.00 41.21           N  
ANISOU 1217  N   MET A 172     8292   3321   4045    649    246     75       N  
ATOM   1218  CA  MET A 172      -1.549  -8.788  34.787  1.00 38.70           C  
ANISOU 1218  CA  MET A 172     7979   2921   3804    625     56    -21       C  
ATOM   1219  C   MET A 172      -1.825  -7.412  35.387  1.00 42.84           C  
ANISOU 1219  C   MET A 172     8734   3374   4170    758     47    -63       C  
ATOM   1220  O   MET A 172      -0.923  -6.777  35.957  1.00 45.38           O  
ANISOU 1220  O   MET A 172     9258   3555   4432    769   -156   -128       O  
ATOM   1221  CB  MET A 172      -1.539  -8.852  33.260  1.00 42.51           C  
ANISOU 1221  CB  MET A 172     8154   3503   4496    508     82    -24       C  
ATOM   1222  CG  MET A 172      -0.398  -9.806  32.764  1.00 39.60           C  
ANISOU 1222  CG  MET A 172     7643   3132   4273    401    -70    -53       C  
ATOM   1223  SD  MET A 172      -0.011  -9.543  31.023  1.00 38.81           S  
ANISOU 1223  SD  MET A 172     7225   3138   4381    283    -90    -84       S  
ATOM   1224  CE  MET A 172       1.361  -8.356  31.125  1.00 38.20           C  
ANISOU 1224  CE  MET A 172     7201   2998   4314    228   -325   -152       C  
ATOM   1225  N   ARG A 173      -3.083  -6.974  35.357  1.00 42.25           N  
ANISOU 1225  N   ARG A 173     8655   3391   4005    875    255    -25       N  
ATOM   1226  CA  ARG A 173      -3.435  -5.684  35.957  1.00 43.19           C  
ANISOU 1226  CA  ARG A 173     9030   3436   3942   1056    251    -75       C  
ATOM   1227  C   ARG A 173      -3.217  -5.683  37.473  1.00 51.88           C  
ANISOU 1227  C   ARG A 173    10473   4428   4810   1186    195    -94       C  
ATOM   1228  O   ARG A 173      -2.772  -4.675  38.042  1.00 48.73           O  
ANISOU 1228  O   ARG A 173    10361   3869   4286   1279     36   -174       O  
ATOM   1229  CB  ARG A 173      -4.887  -5.349  35.618  1.00 47.05           C  
ANISOU 1229  CB  ARG A 173     9411   4092   4376   1194    502    -27       C  
ATOM   1230  CG  ARG A 173      -5.061  -4.925  34.176  1.00 44.24           C  
ANISOU 1230  CG  ARG A 173     8808   3794   4209   1106    507    -34       C  
ATOM   1231  CD  ARG A 173      -6.459  -4.398  33.906  1.00 53.28           C  
ANISOU 1231  CD  ARG A 173     9873   5092   5279   1281    719     -1       C  
ATOM   1232  NE  ARG A 173      -6.747  -3.220  34.723  1.00 54.32           N  
ANISOU 1232  NE  ARG A 173    10322   5134   5182   1538    702    -67       N  
ATOM   1233  CZ  ARG A 173      -7.752  -2.382  34.506  1.00 65.74           C  
ANISOU 1233  CZ  ARG A 173    11776   6664   6538   1752    820    -78       C  
ATOM   1234  NH1 ARG A 173      -8.559  -2.526  33.470  1.00 61.64           N1+
ANISOU 1234  NH1 ARG A 173    10950   6324   6148   1723    955    -23       N1+
ATOM   1235  NH2 ARG A 173      -7.946  -1.367  35.344  1.00 69.23           N  
ANISOU 1235  NH2 ARG A 173    12558   7004   6744   2019    786   -152       N  
ATOM   1236  N   LYS A 174      -3.541  -6.802  38.143  1.00 47.11           N  
ANISOU 1236  N   LYS A 174     9868   3898   4132   1187    312    -16       N  
ATOM   1237  CA  LYS A 174      -3.284  -6.953  39.583  1.00 48.06           C  
ANISOU 1237  CA  LYS A 174    10317   3920   4025   1295    257    -22       C  
ATOM   1238  C   LYS A 174      -1.823  -6.696  39.921  1.00 50.37           C  
ANISOU 1238  C   LYS A 174    10787   4002   4349   1224    -66   -112       C  
ATOM   1239  O   LYS A 174      -1.510  -6.193  41.008  1.00 52.50           O  
ANISOU 1239  O   LYS A 174    11398   4135   4416   1344   -182   -163       O  
ATOM   1240  CB  LYS A 174      -3.649  -8.375  40.024  1.00 47.46           C  
ANISOU 1240  CB  LYS A 174    10178   3940   3916   1229    389     93       C  
ATOM   1241  CG  LYS A 174      -3.172  -8.790  41.419  1.00 53.17           C  
ANISOU 1241  CG  LYS A 174    11225   4545   4433   1291    295     98       C  
ATOM   1242  CD  LYS A 174      -3.593 -10.258  41.680  1.00 64.28           C  
ANISOU 1242  CD  LYS A 174    12556   6041   5825   1186    422    234       C  
ATOM   1243  CE  LYS A 174      -2.999 -10.856  42.963  1.00 65.17           C  
ANISOU 1243  CE  LYS A 174    12986   6019   5756   1216    298    250       C  
ATOM   1244  NZ  LYS A 174      -3.642 -12.175  43.361  1.00 59.50           N1+
ANISOU 1244  NZ  LYS A 174    12258   5390   4962   1123    453    409       N1+
ATOM   1245  N   HIS A 175      -0.912  -7.051  39.011  1.00 45.97           N  
ANISOU 1245  N   HIS A 175    10000   3433   4033   1034   -217   -131       N  
ATOM   1246  CA  HIS A 175       0.511  -6.829  39.215  1.00 45.52           C  
ANISOU 1246  CA  HIS A 175    10034   3231   4030    944   -526   -201       C  
ATOM   1247  C   HIS A 175       1.004  -5.581  38.489  1.00 44.82           C  
ANISOU 1247  C   HIS A 175     9916   3081   4033    869   -677   -264       C  
ATOM   1248  O   HIS A 175       2.205  -5.461  38.222  1.00 49.10           O  
ANISOU 1248  O   HIS A 175    10389   3573   4694    723   -916   -297       O  
ATOM   1249  CB  HIS A 175       1.305  -8.071  38.797  1.00 45.53           C  
ANISOU 1249  CB  HIS A 175     9809   3281   4209    806   -610   -179       C  
ATOM   1250  CG  HIS A 175       1.023  -9.274  39.651  1.00 47.05           C  
ANISOU 1250  CG  HIS A 175    10113   3472   4290    860   -536   -117       C  
ATOM   1251  CD2 HIS A 175       1.674  -9.773  40.728  1.00 45.26           C  
ANISOU 1251  CD2 HIS A 175    10117   3134   3946    900   -693   -125       C  
ATOM   1252  ND1 HIS A 175      -0.078 -10.083  39.460  1.00 46.38           N  
ANISOU 1252  ND1 HIS A 175     9923   3506   4194    863   -285    -22       N  
ATOM   1253  CE1 HIS A 175      -0.079 -11.044  40.371  1.00 46.61           C  
ANISOU 1253  CE1 HIS A 175    10119   3490   4101    887   -288     32       C  
ATOM   1254  NE2 HIS A 175       0.971 -10.877  41.156  1.00 47.57           N  
ANISOU 1254  NE2 HIS A 175    10453   3468   4152    924   -532    -33       N  
ATOM   1255  N   GLY A 176       0.103  -4.639  38.209  1.00 45.72           N  
ANISOU 1255  N   GLY A 176    10091   3203   4078    970   -551   -273       N  
ATOM   1256  CA  GLY A 176       0.468  -3.297  37.774  1.00 49.95           C  
ANISOU 1256  CA  GLY A 176    10698   3650   4631    920   -715   -323       C  
ATOM   1257  C   GLY A 176       0.714  -3.137  36.293  1.00 55.50           C  
ANISOU 1257  C   GLY A 176    11100   4416   5571    743   -724   -310       C  
ATOM   1258  O   GLY A 176       1.159  -2.066  35.873  1.00 46.95           O  
ANISOU 1258  O   GLY A 176    10062   3263   4514    649   -886   -332       O  
ATOM   1259  N   ALA A 177       0.443  -4.160  35.479  1.00 47.24           N  
ANISOU 1259  N   ALA A 177     9713   3550   4687    673   -558   -257       N  
ATOM   1260  CA  ALA A 177       0.662  -4.043  34.040  1.00 42.12           C  
ANISOU 1260  CA  ALA A 177     8759   3000   4245    512   -553   -240       C  
ATOM   1261  C   ALA A 177      -0.433  -3.212  33.395  1.00 43.43           C  
ANISOU 1261  C   ALA A 177     8923   3192   4386    597   -404   -231       C  
ATOM   1262  O   ALA A 177      -1.572  -3.163  33.871  1.00 48.25           O  
ANISOU 1262  O   ALA A 177     9638   3833   4862    790   -223   -220       O  
ATOM   1263  CB  ALA A 177       0.705  -5.424  33.375  1.00 41.47           C  
ANISOU 1263  CB  ALA A 177     8353   3082   4321    436   -440   -198       C  
ATOM   1264  N   TYR A 178      -0.068  -2.533  32.308  1.00 42.40           N  
ANISOU 1264  N   TYR A 178     8668   3063   4377    456   -487   -231       N  
ATOM   1265  CA  TYR A 178      -1.004  -1.795  31.473  1.00 41.61           C  
ANISOU 1265  CA  TYR A 178     8531   2993   4285    515   -371   -220       C  
ATOM   1266  C   TYR A 178      -1.372  -2.684  30.294  1.00 42.89           C  
ANISOU 1266  C   TYR A 178     8317   3354   4624    431   -204   -170       C  
ATOM   1267  O   TYR A 178      -0.482  -3.288  29.688  1.00 43.28           O  
ANISOU 1267  O   TYR A 178     8152   3474   4818    258   -274   -160       O  
ATOM   1268  CB  TYR A 178      -0.370  -0.502  30.960  1.00 43.12           C  
ANISOU 1268  CB  TYR A 178     8850   3045   4488    388   -583   -237       C  
ATOM   1269  CG  TYR A 178      -1.338   0.430  30.263  1.00 44.54           C  
ANISOU 1269  CG  TYR A 178     9088   3201   4633    489   -505   -235       C  
ATOM   1270  CD1 TYR A 178      -1.590   0.302  28.900  1.00 46.21           C  
ANISOU 1270  CD1 TYR A 178     9013   3548   4998    383   -412   -191       C  
ATOM   1271  CD2 TYR A 178      -2.035   1.406  30.973  1.00 48.39           C  
ANISOU 1271  CD2 TYR A 178     9928   3538   4920    720   -525   -282       C  
ATOM   1272  CE1 TYR A 178      -2.493   1.143  28.262  1.00 45.25           C  
ANISOU 1272  CE1 TYR A 178     8951   3402   4840    489   -354   -189       C  
ATOM   1273  CE2 TYR A 178      -2.924   2.254  30.342  1.00 49.95           C  
ANISOU 1273  CE2 TYR A 178    10166   3737   5077    842   -466   -283       C  
ATOM   1274  CZ  TYR A 178      -3.147   2.119  28.996  1.00 48.54           C  
ANISOU 1274  CZ  TYR A 178     9717   3664   5062    726   -387   -237       C  
ATOM   1275  OH  TYR A 178      -4.040   2.961  28.372  1.00 49.92           O  
ANISOU 1275  OH  TYR A 178     9962   3813   5191    866   -345   -242       O  
ATOM   1276  N   THR A 179      -2.669  -2.782  29.975  1.00 39.52           N  
ANISOU 1276  N   THR A 179     7808   3030   4177    562      8   -141       N  
ATOM   1277  CA  THR A 179      -3.139  -3.774  28.999  1.00 37.48           C  
ANISOU 1277  CA  THR A 179     7223   2951   4067    489    161    -91       C  
ATOM   1278  C   THR A 179      -3.969  -3.100  27.912  1.00 45.48           C  
ANISOU 1278  C   THR A 179     8129   4025   5124    516    244    -74       C  
ATOM   1279  O   THR A 179      -4.850  -2.292  28.213  1.00 46.73           O  
ANISOU 1279  O   THR A 179     8435   4158   5162    696    306    -82       O  
ATOM   1280  CB  THR A 179      -3.947  -4.904  29.671  1.00 44.07           C  
ANISOU 1280  CB  THR A 179     8006   3888   4850    578    338    -44       C  
ATOM   1281  CG2 THR A 179      -3.140  -5.585  30.806  1.00 43.16           C  
ANISOU 1281  CG2 THR A 179     8035   3693   4671    566    244    -58       C  
ATOM   1282  OG1 THR A 179      -5.187  -4.392  30.194  1.00 41.00           O  
ANISOU 1282  OG1 THR A 179     7722   3544   4313    781    491    -24       O  
ATOM   1283  N   ALA A 180      -3.687  -3.441  26.640  1.00 39.33           N  
ANISOU 1283  N   ALA A 180     7103   3333   4507    358    240    -54       N  
ATOM   1284  CA  ALA A 180      -4.370  -2.843  25.501  1.00 37.05           C  
ANISOU 1284  CA  ALA A 180     6711   3098   4268    361    295    -36       C  
ATOM   1285  C   ALA A 180      -4.789  -3.914  24.505  1.00 38.85           C  
ANISOU 1285  C   ALA A 180     6640   3492   4630    281    412      5       C  
ATOM   1286  O   ALA A 180      -4.022  -4.828  24.199  1.00 38.69           O  
ANISOU 1286  O   ALA A 180     6486   3513   4703    153    376      1       O  
ATOM   1287  CB  ALA A 180      -3.482  -1.811  24.777  1.00 36.19           C  
ANISOU 1287  CB  ALA A 180     6665   2892   4193    222    121    -50       C  
ATOM   1288  N   LEU A 181      -6.003  -3.754  23.984  1.00 37.18           N  
ANISOU 1288  N   LEU A 181     6337   3371   4419    369    537     38       N  
ATOM   1289  CA  LEU A 181      -6.579  -4.611  22.962  1.00 33.20           C  
ANISOU 1289  CA  LEU A 181     5574   3010   4029    295    630     80       C  
ATOM   1290  C   LEU A 181      -6.467  -3.889  21.621  1.00 38.51           C  
ANISOU 1290  C   LEU A 181     6178   3685   4769    224    572     74       C  
ATOM   1291  O   LEU A 181      -7.019  -2.800  21.462  1.00 38.20           O  
ANISOU 1291  O   LEU A 181     6239   3607   4670    328    564     74       O  
ATOM   1292  CB  LEU A 181      -8.043  -4.892  23.311  1.00 35.41           C  
ANISOU 1292  CB  LEU A 181     5780   3415   4259    428    795    137       C  
ATOM   1293  CG  LEU A 181      -8.779  -5.779  22.314  1.00 38.58           C  
ANISOU 1293  CG  LEU A 181     5926   3962   4772    336    872    193       C  
ATOM   1294  CD1 LEU A 181      -8.258  -7.215  22.407  1.00 39.73           C  
ANISOU 1294  CD1 LEU A 181     6000   4110   4984    192    855    207       C  
ATOM   1295  CD2 LEU A 181     -10.265  -5.711  22.613  1.00 37.05           C  
ANISOU 1295  CD2 LEU A 181     5641   3920   4517    470   1021    262       C  
ATOM   1296  N   VAL A 182      -5.746  -4.468  20.660  1.00 36.06           N  
ANISOU 1296  N   VAL A 182     5718   3418   4565     65    527     69       N  
ATOM   1297  CA  VAL A 182      -5.628  -3.814  19.358  1.00 40.31           C  
ANISOU 1297  CA  VAL A 182     6195   3972   5148    -13    481     75       C  
ATOM   1298  C   VAL A 182      -6.219  -4.727  18.291  1.00 40.28           C  
ANISOU 1298  C   VAL A 182     5974   4098   5233    -59    556     98       C  
ATOM   1299  O   VAL A 182      -6.304  -5.948  18.462  1.00 39.37           O  
ANISOU 1299  O   VAL A 182     5763   4037   5160    -83    601    101       O  
ATOM   1300  CB  VAL A 182      -4.175  -3.422  19.013  1.00 40.10           C  
ANISOU 1300  CB  VAL A 182     6195   3902   5140   -167    350     56       C  
ATOM   1301  CG1 VAL A 182      -3.641  -2.417  20.025  1.00 37.95           C  
ANISOU 1301  CG1 VAL A 182     6164   3480   4775   -148    238     42       C  
ATOM   1302  CG2 VAL A 182      -3.281  -4.685  18.909  1.00 40.28           C  
ANISOU 1302  CG2 VAL A 182     6062   4010   5232   -252    345     34       C  
ATOM   1303  N   SER A 183      -6.674  -4.127  17.195  1.00 39.84           N  
ANISOU 1303  N   SER A 183     5872   4072   5195    -71    552    116       N  
ATOM   1304  CA  SER A 183      -7.362  -4.923  16.188  1.00 36.75           C  
ANISOU 1304  CA  SER A 183     5298   3792   4873   -106    606    138       C  
ATOM   1305  C   SER A 183      -7.396  -4.178  14.863  1.00 35.65           C  
ANISOU 1305  C   SER A 183     5136   3666   4743   -153    562    148       C  
ATOM   1306  O   SER A 183      -7.575  -2.955  14.842  1.00 36.44           O  
ANISOU 1306  O   SER A 183     5365   3695   4786    -99    520    159       O  
ATOM   1307  CB  SER A 183      -8.798  -5.244  16.629  1.00 38.46           C  
ANISOU 1307  CB  SER A 183     5450   4081   5083      4    705    182       C  
ATOM   1308  OG  SER A 183      -9.405  -6.136  15.720  1.00 37.97           O  
ANISOU 1308  OG  SER A 183     5218   4116   5094    -66    727    210       O  
ATOM   1309  N   GLY A 184      -7.210  -4.921  13.769  1.00 36.85           N  
ANISOU 1309  N   GLY A 184     5155   3896   4951   -246    560    143       N  
ATOM   1310  CA  GLY A 184      -7.649  -4.460  12.462  1.00 36.43           C  
ANISOU 1310  CA  GLY A 184     5060   3882   4901   -271    540    164       C  
ATOM   1311  C   GLY A 184      -9.148  -4.548  12.258  1.00 38.35           C  
ANISOU 1311  C   GLY A 184     5229   4179   5164   -180    582    200       C  
ATOM   1312  O   GLY A 184      -9.659  -4.077  11.235  1.00 40.66           O  
ANISOU 1312  O   GLY A 184     5499   4498   5453   -175    552    221       O  
ATOM   1313  N   GLY A 185      -9.853  -5.148  13.218  1.00 37.92           N  
ANISOU 1313  N   GLY A 185     5127   4159   5122   -113    647    218       N  
ATOM   1314  CA  GLY A 185     -11.306  -5.153  13.290  1.00 39.34           C  
ANISOU 1314  CA  GLY A 185     5205   4432   5309    -18    700    271       C  
ATOM   1315  C   GLY A 185     -11.855  -3.811  13.726  1.00 40.28           C  
ANISOU 1315  C   GLY A 185     5427   4526   5352    160    710    280       C  
ATOM   1316  O   GLY A 185     -11.215  -2.787  13.484  1.00 39.86           O  
ANISOU 1316  O   GLY A 185     5535   4359   5250    172    638    252       O  
ATOM   1317  N   PHE A 186     -13.010  -3.777  14.384  1.00 39.48           N  
ANISOU 1317  N   PHE A 186     5246   4529   5224    302    790    322       N  
ATOM   1318  CA  PHE A 186     -13.757  -2.531  14.484  1.00 45.91           C  
ANISOU 1318  CA  PHE A 186     6134   5350   5959    520    788    325       C  
ATOM   1319  C   PHE A 186     -14.066  -2.150  15.920  1.00 45.04           C  
ANISOU 1319  C   PHE A 186     6115   5251   5747    713    871    320       C  
ATOM   1320  O   PHE A 186     -14.313  -3.006  16.775  1.00 44.31           O  
ANISOU 1320  O   PHE A 186     5924   5256   5656    694    971    354       O  
ATOM   1321  CB  PHE A 186     -15.038  -2.615  13.656  1.00 45.57           C  
ANISOU 1321  CB  PHE A 186     5885   5472   5956    575    798    379       C  
ATOM   1322  CG  PHE A 186     -14.794  -3.189  12.302  1.00 48.35           C  
ANISOU 1322  CG  PHE A 186     6152   5822   6397    381    719    384       C  
ATOM   1323  CD1 PHE A 186     -14.043  -2.473  11.376  1.00 49.25           C  
ANISOU 1323  CD1 PHE A 186     6415   5804   6493    330    618    346       C  
ATOM   1324  CD2 PHE A 186     -15.246  -4.458  11.972  1.00 50.18           C  
ANISOU 1324  CD2 PHE A 186     6181   6172   6713    237    738    428       C  
ATOM   1325  CE1 PHE A 186     -13.762  -2.999  10.124  1.00 45.94           C  
ANISOU 1325  CE1 PHE A 186     5933   5393   6128    169    556    345       C  
ATOM   1326  CE2 PHE A 186     -14.976  -4.991  10.723  1.00 54.13           C  
ANISOU 1326  CE2 PHE A 186     6645   6651   7272     80    652    418       C  
ATOM   1327  CZ  PHE A 186     -14.227  -4.264   9.804  1.00 45.96           C  
ANISOU 1327  CZ  PHE A 186     5750   5505   6208     60    572    372       C  
ATOM   1328  N   THR A 187     -14.064  -0.833  16.147  1.00 41.14           N  
ANISOU 1328  N   THR A 187     5838   4646   5149    903    818    279       N  
ATOM   1329  CA ATHR A 187     -14.295  -0.289  17.483  0.72 45.99           C  
ANISOU 1329  CA ATHR A 187     6604   5241   5630   1131    876    254       C  
ATOM   1330  CA BTHR A 187     -14.285  -0.307  17.491  0.28 46.19           C  
ANISOU 1330  CA BTHR A 187     6628   5267   5657   1128    877    254       C  
ATOM   1331  C   THR A 187     -15.650  -0.703  18.038  1.00 51.28           C  
ANISOU 1331  C   THR A 187     7048   6172   6266   1305   1035    313       C  
ATOM   1332  O   THR A 187     -15.806  -0.844  19.258  1.00 51.62           O  
ANISOU 1332  O   THR A 187     7131   6268   6214   1423   1138    317       O  
ATOM   1333  CB ATHR A 187     -14.194   1.234  17.443  0.72 50.51           C  
ANISOU 1333  CB ATHR A 187     7474   5633   6085   1324    759    197       C  
ATOM   1334  CB BTHR A 187     -14.115   1.219  17.499  0.28 50.46           C  
ANISOU 1334  CB BTHR A 187     7478   5616   6077   1315    757    194       C  
ATOM   1335  CG2ATHR A 187     -12.847   1.655  16.916  0.72 39.96           C  
ANISOU 1335  CG2ATHR A 187     6343   4064   4776   1107    600    166       C  
ATOM   1336  CG2BTHR A 187     -15.164   1.893  16.639  0.28 56.26           C  
ANISOU 1336  CG2BTHR A 187     8149   6429   6796   1494    730    210       C  
ATOM   1337  OG1ATHR A 187     -15.204   1.740  16.565  0.72 56.72           O  
ANISOU 1337  OG1ATHR A 187     8165   6512   6872   1470    740    218       O  
ATOM   1338  OG1BTHR A 187     -14.213   1.716  18.840  0.28 48.65           O  
ANISOU 1338  OG1BTHR A 187     7447   5339   5698   1543    797    153       O  
ATOM   1339  N   SER A 188     -16.642  -0.899  17.161  1.00 45.72           N  
ANISOU 1339  N   SER A 188     6097   5648   5628   1318   1055    369       N  
ATOM   1340  CA  SER A 188     -17.949  -1.386  17.595  1.00 59.68           C  
ANISOU 1340  CA  SER A 188     7583   7716   7378   1436   1204    453       C  
ATOM   1341  C   SER A 188     -17.820  -2.685  18.376  1.00 59.11           C  
ANISOU 1341  C   SER A 188     7382   7737   7340   1245   1313    517       C  
ATOM   1342  O   SER A 188     -18.652  -2.983  19.241  1.00 59.72           O  
ANISOU 1342  O   SER A 188     7310   8035   7345   1353   1461    588       O  
ATOM   1343  CB  SER A 188     -18.855  -1.605  16.379  1.00 61.34           C  
ANISOU 1343  CB  SER A 188     7525   8093   7689   1386   1168    514       C  
ATOM   1344  OG  SER A 188     -18.690  -0.592  15.400  1.00 83.61           O  
ANISOU 1344  OG  SER A 188    10498  10765  10503   1471   1026    455       O  
ATOM   1345  N   PHE A 189     -16.793  -3.478  18.074  1.00 48.97           N  
ANISOU 1345  N   PHE A 189     6155   6298   6153    967   1240    500       N  
ATOM   1346  CA  PHE A 189     -16.511  -4.707  18.803  1.00 46.76           C  
ANISOU 1346  CA  PHE A 189     5821   6048   5897    785   1307    550       C  
ATOM   1347  C   PHE A 189     -15.470  -4.513  19.901  1.00 49.15           C  
ANISOU 1347  C   PHE A 189     6392   6172   6112    825   1305    484       C  
ATOM   1348  O   PHE A 189     -15.678  -4.984  21.020  1.00 48.24           O  
ANISOU 1348  O   PHE A 189     6274   6135   5920    854   1413    529       O  
ATOM   1349  CB  PHE A 189     -16.050  -5.816  17.841  1.00 43.18           C  
ANISOU 1349  CB  PHE A 189     5277   5538   5590    488   1216    566       C  
ATOM   1350  CG  PHE A 189     -17.134  -6.332  16.942  1.00 49.69           C  
ANISOU 1350  CG  PHE A 189     5831   6549   6500    397   1211    653       C  
ATOM   1351  CD1 PHE A 189     -17.541  -5.608  15.832  1.00 52.61           C  
ANISOU 1351  CD1 PHE A 189     6146   6942   6902    470   1137    632       C  
ATOM   1352  CD2 PHE A 189     -17.741  -7.549  17.196  1.00 53.84           C  
ANISOU 1352  CD2 PHE A 189     6173   7217   7068    219   1260    763       C  
ATOM   1353  CE1 PHE A 189     -18.551  -6.086  15.001  1.00 54.01           C  
ANISOU 1353  CE1 PHE A 189     6072   7293   7156    382   1112    713       C  
ATOM   1354  CE2 PHE A 189     -18.747  -8.036  16.367  1.00 55.46           C  
ANISOU 1354  CE2 PHE A 189     6128   7592   7352    105   1228    853       C  
ATOM   1355  CZ  PHE A 189     -19.152  -7.302  15.268  1.00 48.14           C  
ANISOU 1355  CZ  PHE A 189     5132   6697   6460    192   1152    824       C  
ATOM   1356  N   THR A 190     -14.346  -3.840  19.616  1.00 44.69           N  
ANISOU 1356  N   THR A 190     6056   5376   5549    810   1177    388       N  
ATOM   1357  CA  THR A 190     -13.276  -3.792  20.617  1.00 43.77           C  
ANISOU 1357  CA  THR A 190     6172   5092   5365    801   1145    333       C  
ATOM   1358  C   THR A 190     -13.713  -3.069  21.882  1.00 46.33           C  
ANISOU 1358  C   THR A 190     6649   5438   5516   1064   1228    320       C  
ATOM   1359  O   THR A 190     -13.233  -3.391  22.969  1.00 44.30           O  
ANISOU 1359  O   THR A 190     6522   5125   5185   1064   1254    310       O  
ATOM   1360  CB  THR A 190     -12.008  -3.118  20.072  1.00 40.58           C  
ANISOU 1360  CB  THR A 190     5963   4467   4990    718    983    251       C  
ATOM   1361  CG2 THR A 190     -11.386  -3.924  18.931  1.00 39.02           C  
ANISOU 1361  CG2 THR A 190     5631   4259   4935    474    916    254       C  
ATOM   1362  OG1 THR A 190     -12.314  -1.794  19.611  1.00 44.69           O  
ANISOU 1362  OG1 THR A 190     6600   4927   5452    873    922    220       O  
ATOM   1363  N   ARG A 191     -14.592  -2.069  21.768  1.00 46.27           N  
ANISOU 1363  N   ARG A 191     6653   5504   5424   1312   1258    311       N  
ATOM   1364  CA  ARG A 191     -15.034  -1.359  22.963  1.00 47.42           C  
ANISOU 1364  CA  ARG A 191     6964   5678   5375   1612   1339    285       C  
ATOM   1365  C   ARG A 191     -15.772  -2.290  23.916  1.00 50.33           C  
ANISOU 1365  C   ARG A 191     7152   6289   5683   1635   1533    377       C  
ATOM   1366  O   ARG A 191     -15.526  -2.270  25.129  1.00 52.12           O  
ANISOU 1366  O   ARG A 191     7556   6480   5769   1737   1588    359       O  
ATOM   1367  CB  ARG A 191     -15.914  -0.171  22.568  1.00 54.20           C  
ANISOU 1367  CB  ARG A 191     7855   6589   6150   1909   1331    255       C  
ATOM   1368  CG  ARG A 191     -15.119   1.096  22.275  1.00 62.89           C  
ANISOU 1368  CG  ARG A 191     9311   7386   7199   1980   1132    151       C  
ATOM   1369  CD  ARG A 191     -16.033   2.267  21.880  1.00 77.95           C  
ANISOU 1369  CD  ARG A 191    11289   9322   9008   2303   1104    119       C  
ATOM   1370  NE  ARG A 191     -17.333   1.811  21.395  1.00 95.04           N  
ANISOU 1370  NE  ARG A 191    13074  11813  11224   2388   1244    201       N  
ATOM   1371  CZ  ARG A 191     -17.903   2.215  20.265  1.00 97.41           C  
ANISOU 1371  CZ  ARG A 191    13259  12163  11588   2433   1179    213       C  
ATOM   1372  NH1 ARG A 191     -17.307   3.081  19.458  1.00 82.24           N1+
ANISOU 1372  NH1 ARG A 191    11581   9982   9683   2398    986    156       N1+
ATOM   1373  NH2 ARG A 191     -19.092   1.722  19.925  1.00 85.58           N  
ANISOU 1373  NH2 ARG A 191    11391  10989  10138   2495   1302    298       N  
ATOM   1374  N   ARG A 192     -16.669  -3.127  23.387  1.00 50.41           N  
ANISOU 1374  N   ARG A 192     6819   6545   5789   1519   1629    486       N  
ATOM   1375  CA  ARG A 192     -17.407  -4.044  24.251  1.00 52.84           C  
ANISOU 1375  CA  ARG A 192     6939   7102   6038   1490   1810    605       C  
ATOM   1376  C   ARG A 192     -16.509  -5.166  24.745  1.00 54.24           C  
ANISOU 1376  C   ARG A 192     7198   7149   6263   1220   1780    629       C  
ATOM   1377  O   ARG A 192     -16.539  -5.519  25.930  1.00 53.32           O  
ANISOU 1377  O   ARG A 192     7156   7084   6018   1262   1885    669       O  
ATOM   1378  CB  ARG A 192     -18.611  -4.622  23.511  1.00 60.16           C  
ANISOU 1378  CB  ARG A 192     7474   8325   7059   1400   1890    732       C  
ATOM   1379  CG  ARG A 192     -19.719  -3.624  23.233  1.00 71.94           C  
ANISOU 1379  CG  ARG A 192     8830  10029   8476   1714   1954    732       C  
ATOM   1380  CD  ARG A 192     -20.795  -3.688  24.303  1.00 82.63           C  
ANISOU 1380  CD  ARG A 192    10010  11726   9658   1922   2180    830       C  
ATOM   1381  NE  ARG A 192     -21.573  -4.923  24.242  1.00 95.12           N  
ANISOU 1381  NE  ARG A 192    11227  13596  11320   1656   2285   1011       N  
ATOM   1382  CZ  ARG A 192     -22.554  -5.160  23.379  1.00 98.69           C  
ANISOU 1382  CZ  ARG A 192    11326  14297  11875   1583   2292   1110       C  
ATOM   1383  NH1 ARG A 192     -22.884  -4.280  22.446  1.00 92.83           N1+
ANISOU 1383  NH1 ARG A 192    10540  13555  11176   1765   2202   1040       N1+
ATOM   1384  NH2 ARG A 192     -23.221  -6.310  23.453  1.00 94.67           N  
ANISOU 1384  NH2 ARG A 192    10512  14036  11421   1307   2373   1290       N  
ATOM   1385  N   ILE A 193     -15.695  -5.724  23.850  1.00 48.92           N  
ANISOU 1385  N   ILE A 193     6523   6307   5756    964   1635    600       N  
ATOM   1386  CA  ILE A 193     -14.829  -6.846  24.206  1.00 49.93           C  
ANISOU 1386  CA  ILE A 193     6727   6310   5936    729   1584    614       C  
ATOM   1387  C   ILE A 193     -13.792  -6.416  25.234  1.00 49.05           C  
ANISOU 1387  C   ILE A 193     6926   5998   5712    826   1534    525       C  
ATOM   1388  O   ILE A 193     -13.505  -7.147  26.191  1.00 48.20           O  
ANISOU 1388  O   ILE A 193     6903   5868   5541    764   1569    562       O  
ATOM   1389  CB  ILE A 193     -14.170  -7.421  22.937  1.00 49.79           C  
ANISOU 1389  CB  ILE A 193     6649   6169   6100    495   1436    583       C  
ATOM   1390  CG1 ILE A 193     -15.225  -8.118  22.082  1.00 53.26           C  
ANISOU 1390  CG1 ILE A 193     6800   6799   6638    359   1471    688       C  
ATOM   1391  CG2 ILE A 193     -13.018  -8.384  23.285  1.00 45.53           C  
ANISOU 1391  CG2 ILE A 193     6246   5455   5598    320   1346    555       C  
ATOM   1392  CD1 ILE A 193     -16.117  -9.058  22.868  1.00 53.06           C  
ANISOU 1392  CD1 ILE A 193     6630   6970   6561    270   1601    836       C  
ATOM   1393  N   ALA A 194     -13.197  -5.236  25.047  1.00 47.59           N  
ANISOU 1393  N   ALA A 194     6934   5651   5497    961   1430    413       N  
ATOM   1394  CA  ALA A 194     -12.220  -4.764  26.022  1.00 45.90           C  
ANISOU 1394  CA  ALA A 194     7027   5240   5173   1038   1352    332       C  
ATOM   1395  C   ALA A 194     -12.843  -4.653  27.399  1.00 52.27           C  
ANISOU 1395  C   ALA A 194     7933   6150   5776   1245   1497    365       C  
ATOM   1396  O   ALA A 194     -12.230  -5.044  28.400  1.00 50.67           O  
ANISOU 1396  O   ALA A 194     7904   5856   5493   1220   1481    356       O  
ATOM   1397  CB  ALA A 194     -11.643  -3.413  25.604  1.00 47.77           C  
ANISOU 1397  CB  ALA A 194     7466   5294   5391   1140   1206    227       C  
ATOM   1398  N   GLU A 195     -14.069  -4.125  27.462  1.00 49.76           N  
ANISOU 1398  N   GLU A 195     7503   6040   5363   1466   1641    404       N  
ATOM   1399  CA  GLU A 195     -14.762  -3.987  28.735  1.00 52.60           C  
ANISOU 1399  CA  GLU A 195     7930   6552   5502   1698   1809    441       C  
ATOM   1400  C   GLU A 195     -15.090  -5.339  29.343  1.00 53.47           C  
ANISOU 1400  C   GLU A 195     7882   6831   5605   1518   1944    578       C  
ATOM   1401  O   GLU A 195     -14.976  -5.519  30.562  1.00 57.39           O  
ANISOU 1401  O   GLU A 195     8545   7330   5931   1597   2017    594       O  
ATOM   1402  CB  GLU A 195     -16.036  -3.172  28.543  1.00 51.93           C  
ANISOU 1402  CB  GLU A 195     7708   6703   5322   1991   1939    458       C  
ATOM   1403  CG  GLU A 195     -16.854  -3.003  29.798  1.00 61.88           C  
ANISOU 1403  CG  GLU A 195     8998   8183   6331   2273   2144    500       C  
ATOM   1404  CD  GLU A 195     -17.908  -1.937  29.629  1.00 97.28           C  
ANISOU 1404  CD  GLU A 195    13416  12854  10693   2647   2232    471       C  
ATOM   1405  OE1 GLU A 195     -18.638  -1.998  28.614  1.00 91.34           O  
ANISOU 1405  OE1 GLU A 195    12355  12276  10072   2604   2254    528       O  
ATOM   1406  OE2 GLU A 195     -17.985  -1.027  30.483  1.00115.85           O1-
ANISOU 1406  OE2 GLU A 195    16041  15164  12811   2997   2258    384       O1-
ATOM   1407  N   MET A 196     -15.519  -6.301  28.518  1.00 52.63           N  
ANISOU 1407  N   MET A 196     7477   6853   5665   1268   1967    682       N  
ATOM   1408  CA  MET A 196     -15.854  -7.613  29.063  1.00 53.80           C  
ANISOU 1408  CA  MET A 196     7502   7137   5803   1061   2069    829       C  
ATOM   1409  C   MET A 196     -14.623  -8.299  29.634  1.00 54.98           C  
ANISOU 1409  C   MET A 196     7901   7030   5960    904   1944    789       C  
ATOM   1410  O   MET A 196     -14.686  -8.900  30.711  1.00 56.48           O  
ANISOU 1410  O   MET A 196     8178   7263   6018    879   2029    866       O  
ATOM   1411  CB  MET A 196     -16.504  -8.501  28.002  1.00 57.31           C  
ANISOU 1411  CB  MET A 196     7620   7727   6427    803   2070    943       C  
ATOM   1412  CG  MET A 196     -17.795  -7.965  27.434  1.00 66.60           C  
ANISOU 1412  CG  MET A 196     8503   9197   7605    934   2185   1005       C  
ATOM   1413  SD  MET A 196     -18.289  -8.904  25.979  1.00 69.03           S  
ANISOU 1413  SD  MET A 196     8491   9586   8152    606   2100   1101       S  
ATOM   1414  CE  MET A 196     -18.349 -10.546  26.692  1.00 70.25           C  
ANISOU 1414  CE  MET A 196     8619   9779   8294    271   2138   1272       C  
ATOM   1415  N   ILE A 197     -13.490  -8.202  28.941  1.00 51.00           N  
ANISOU 1415  N   ILE A 197     7510   6271   5596    808   1744    673       N  
ATOM   1416  CA  ILE A 197     -12.287  -8.883  29.407  1.00 48.72           C  
ANISOU 1416  CA  ILE A 197     7425   5761   5326    674   1610    632       C  
ATOM   1417  C   ILE A 197     -11.609  -8.100  30.527  1.00 50.30           C  
ANISOU 1417  C   ILE A 197     7938   5818   5358    868   1569    541       C  
ATOM   1418  O   ILE A 197     -11.112  -8.687  31.496  1.00 52.08           O  
ANISOU 1418  O   ILE A 197     8334   5961   5494    830   1547    558       O  
ATOM   1419  CB  ILE A 197     -11.342  -9.126  28.224  1.00 43.96           C  
ANISOU 1419  CB  ILE A 197     6784   4992   4926    507   1424    553       C  
ATOM   1420  CG1 ILE A 197     -12.002 -10.097  27.243  1.00 44.04           C  
ANISOU 1420  CG1 ILE A 197     6536   5120   5077    305   1446    647       C  
ATOM   1421  CG2 ILE A 197     -10.018  -9.704  28.715  1.00 46.85           C  
ANISOU 1421  CG2 ILE A 197     7351   5148   5302    420   1273    494       C  
ATOM   1422  CD1 ILE A 197     -11.250 -10.250  25.935  1.00 41.33           C  
ANISOU 1422  CD1 ILE A 197     6136   4656   4910    183   1289    566       C  
ATOM   1423  N   GLY A 198     -11.583  -6.770  30.425  1.00 46.26           N  
ANISOU 1423  N   GLY A 198     7533   5256   4787   1077   1538    444       N  
ATOM   1424  CA  GLY A 198     -10.979  -5.955  31.464  1.00 49.83           C  
ANISOU 1424  CA  GLY A 198     8317   5551   5066   1262   1471    352       C  
ATOM   1425  C   GLY A 198      -9.748  -5.167  31.041  1.00 49.59           C  
ANISOU 1425  C   GLY A 198     8469   5262   5110   1230   1236    222       C  
ATOM   1426  O   GLY A 198      -8.932  -4.789  31.892  1.00 46.63           O  
ANISOU 1426  O   GLY A 198     8378   4712   4629   1288   1116    153       O  
ATOM   1427  N   PHE A 199      -9.596  -4.916  29.739  1.00 44.62           N  
ANISOU 1427  N   PHE A 199     7682   4615   4655   1123   1160    199       N  
ATOM   1428  CA  PHE A 199      -8.457  -4.152  29.233  1.00 43.05           C  
ANISOU 1428  CA  PHE A 199     7622   4208   4528   1055    945    102       C  
ATOM   1429  C   PHE A 199      -8.513  -2.691  29.681  1.00 46.87           C  
ANISOU 1429  C   PHE A 199     8390   4567   4852   1277    876     25       C  
ATOM   1430  O   PHE A 199      -9.587  -2.124  29.897  1.00 46.37           O  
ANISOU 1430  O   PHE A 199     8349   4608   4663   1512   1004     33       O  
ATOM   1431  CB  PHE A 199      -8.419  -4.193  27.705  1.00 42.82           C  
ANISOU 1431  CB  PHE A 199     7357   4219   4693    901    906    110       C  
ATOM   1432  CG  PHE A 199      -7.886  -5.475  27.134  1.00 39.43           C  
ANISOU 1432  CG  PHE A 199     6735   3824   4425    670    880    143       C  
ATOM   1433  CD1 PHE A 199      -6.530  -5.629  26.903  1.00 38.80           C  
ANISOU 1433  CD1 PHE A 199     6699   3617   4427    527    712     90       C  
ATOM   1434  CD2 PHE A 199      -8.744  -6.519  26.818  1.00 40.70           C  
ANISOU 1434  CD2 PHE A 199     6672   4147   4645    602   1013    230       C  
ATOM   1435  CE1 PHE A 199      -6.020  -6.810  26.361  1.00 35.80           C  
ANISOU 1435  CE1 PHE A 199     6157   3270   4175    364    682    104       C  
ATOM   1436  CE2 PHE A 199      -8.253  -7.711  26.282  1.00 36.28           C  
ANISOU 1436  CE2 PHE A 199     5986   3584   4215    410    963    249       C  
ATOM   1437  CZ  PHE A 199      -6.883  -7.861  26.049  1.00 36.34           C  
ANISOU 1437  CZ  PHE A 199     6052   3462   4293    313    801    177       C  
ATOM   1438  N   ASN A 200      -7.326  -2.065  29.769  1.00 42.75           N  
ANISOU 1438  N   ASN A 200     8088   3822   4334   1200    656    -49       N  
ATOM   1439  CA  ASN A 200      -7.240  -0.630  30.038  1.00 47.84           C  
ANISOU 1439  CA  ASN A 200     9048   4290   4839   1364    528   -125       C  
ATOM   1440  C   ASN A 200      -7.663   0.215  28.847  1.00 49.92           C  
ANISOU 1440  C   ASN A 200     9245   4552   5172   1382    501   -130       C  
ATOM   1441  O   ASN A 200      -8.177   1.326  29.035  1.00 47.70           O  
ANISOU 1441  O   ASN A 200     9194   4186   4745   1611    470   -178       O  
ATOM   1442  CB  ASN A 200      -5.818  -0.233  30.436  1.00 50.83           C  
ANISOU 1442  CB  ASN A 200     9670   4432   5212   1220    270   -181       C  
ATOM   1443  CG  ASN A 200      -5.359  -0.909  31.704  1.00 50.40           C  
ANISOU 1443  CG  ASN A 200     9744   4344   5060   1234    259   -188       C  
ATOM   1444  ND2 ASN A 200      -5.664  -0.300  32.851  1.00 55.64           N  
ANISOU 1444  ND2 ASN A 200    10735   4914   5492   1471    251   -236       N  
ATOM   1445  OD1 ASN A 200      -4.739  -1.968  31.660  1.00 49.84           O  
ANISOU 1445  OD1 ASN A 200     9502   4327   5109   1054    250   -155       O  
ATOM   1446  N   GLU A 201      -7.407  -0.236  27.625  1.00 45.68           N  
ANISOU 1446  N   GLU A 201     8436   4084   4835   1159    491    -90       N  
ATOM   1447  CA  GLU A 201      -7.802   0.559  26.467  1.00 46.19           C  
ANISOU 1447  CA  GLU A 201     8452   4142   4954   1169    458    -89       C  
ATOM   1448  C   GLU A 201      -7.861  -0.352  25.250  1.00 42.62           C  
ANISOU 1448  C   GLU A 201     7638   3853   4704    965    531    -29       C  
ATOM   1449  O   GLU A 201      -7.450  -1.506  25.300  1.00 43.37           O  
ANISOU 1449  O   GLU A 201     7560   4027   4892    813    573     -1       O  
ATOM   1450  CB  GLU A 201      -6.849   1.729  26.221  1.00 54.31           C  
ANISOU 1450  CB  GLU A 201     9754   4922   5958   1075    210   -134       C  
ATOM   1451  CG  GLU A 201      -5.503   1.363  25.650  1.00 57.30           C  
ANISOU 1451  CG  GLU A 201    10024   5259   6487    746     72   -114       C  
ATOM   1452  CD  GLU A 201      -4.731   2.589  25.173  1.00 49.53           C  
ANISOU 1452  CD  GLU A 201     9262   4071   5485    613   -161   -124       C  
ATOM   1453  OE1 GLU A 201      -5.217   3.317  24.282  1.00 65.58           O  
ANISOU 1453  OE1 GLU A 201    11318   6077   7522    641   -180   -109       O  
ATOM   1454  OE2 GLU A 201      -3.622   2.829  25.681  1.00 58.13           O1-
ANISOU 1454  OE2 GLU A 201    10508   5026   6555    464   -342   -136       O1-
ATOM   1455  N   GLU A 202      -8.405   0.180  24.157  1.00 44.15           N  
ANISOU 1455  N   GLU A 202     7744   4083   4948    983    534    -15       N  
ATOM   1456  CA  GLU A 202      -8.468  -0.559  22.901  1.00 40.21           C  
ANISOU 1456  CA  GLU A 202     6938   3717   4621    800    579     33       C  
ATOM   1457  C   GLU A 202      -8.248   0.413  21.753  1.00 40.94           C  
ANISOU 1457  C   GLU A 202     7087   3720   4749    733    456     28       C  
ATOM   1458  O   GLU A 202      -8.445   1.622  21.894  1.00 43.24           O  
ANISOU 1458  O   GLU A 202     7628   3873   4928    874    367     -2       O  
ATOM   1459  CB  GLU A 202      -9.807  -1.296  22.735  1.00 42.48           C  
ANISOU 1459  CB  GLU A 202     6973   4233   4934    901    772     90       C  
ATOM   1460  CG  GLU A 202     -11.056  -0.434  23.050  1.00 50.15           C  
ANISOU 1460  CG  GLU A 202     8013   5270   5772   1204    853     88       C  
ATOM   1461  CD  GLU A 202     -11.356   0.617  21.982  1.00 54.31           C  
ANISOU 1461  CD  GLU A 202     8587   5737   6309   1266    763     72       C  
ATOM   1462  OE1 GLU A 202     -11.216   0.306  20.782  1.00 48.41           O  
ANISOU 1462  OE1 GLU A 202     7664   5029   5699   1083    731    102       O  
ATOM   1463  OE2 GLU A 202     -11.744   1.757  22.339  1.00 58.50           O1-
ANISOU 1463  OE2 GLU A 202     9356   6175   6697   1511    716     27       O1-
ATOM   1464  N   ARG A 203      -7.817  -0.126  20.610  1.00 40.72           N  
ANISOU 1464  N   ARG A 203     6850   3762   4861    521    443     58       N  
ATOM   1465  CA  ARG A 203      -7.628   0.679  19.403  1.00 41.47           C  
ANISOU 1465  CA  ARG A 203     6971   3800   4986    429    343     72       C  
ATOM   1466  C   ARG A 203      -7.930  -0.185  18.191  1.00 44.11           C  
ANISOU 1466  C   ARG A 203     7010   4302   5448    317    423    109       C  
ATOM   1467  O   ARG A 203      -7.353  -1.266  18.051  1.00 39.63           O  
ANISOU 1467  O   ARG A 203     6275   3816   4967    174    455    112       O  
ATOM   1468  CB  ARG A 203      -6.201   1.217  19.282  1.00 43.19           C  
ANISOU 1468  CB  ARG A 203     7330   3875   5206    216    170     68       C  
ATOM   1469  CG  ARG A 203      -6.000   2.067  18.031  1.00 50.50           C  
ANISOU 1469  CG  ARG A 203     8295   4748   6143     93     70    104       C  
ATOM   1470  CD  ARG A 203      -4.748   2.881  18.128  1.00 51.32           C  
ANISOU 1470  CD  ARG A 203     8596   4696   6209   -105   -118    121       C  
ATOM   1471  NE  ARG A 203      -4.737   3.977  17.165  1.00 57.84           N  
ANISOU 1471  NE  ARG A 203     9564   5417   6994   -192   -236    167       N  
ATOM   1472  CZ  ARG A 203      -3.797   4.142  16.246  1.00 64.49           C  
ANISOU 1472  CZ  ARG A 203    10334   6291   7878   -466   -311    231       C  
ATOM   1473  NH1 ARG A 203      -2.790   3.287  16.124  1.00 57.61           N1+
ANISOU 1473  NH1 ARG A 203     9226   5572   7089   -654   -277    246       N1+
ATOM   1474  NH2 ARG A 203      -3.866   5.190  15.430  1.00 56.14           N  
ANISOU 1474  NH2 ARG A 203     9447   5120   6764   -544   -425    285       N  
ATOM   1475  N   ALA A 204      -8.799   0.296  17.310  1.00 40.45           N  
ANISOU 1475  N   ALA A 204     6506   3878   4987    393    435    131       N  
ATOM   1476  CA  ALA A 204      -9.220  -0.502  16.166  1.00 34.17           C  
ANISOU 1476  CA  ALA A 204     5453   3234   4297    305    497    164       C  
ATOM   1477  C   ALA A 204      -9.659   0.438  15.045  1.00 34.48           C  
ANISOU 1477  C   ALA A 204     5543   3240   4317    332    428    184       C  
ATOM   1478  O   ALA A 204      -9.693   1.660  15.211  1.00 38.91           O  
ANISOU 1478  O   ALA A 204     6345   3656   4783    431    334    173       O  
ATOM   1479  CB  ALA A 204     -10.342  -1.475  16.567  1.00 37.71           C  
ANISOU 1479  CB  ALA A 204     5702   3849   4776    409    640    188       C  
ATOM   1480  N   ASN A 205     -10.003  -0.152  13.900  1.00 38.33           N  
ANISOU 1480  N   ASN A 205     5832   3847   4886    249    457    211       N  
ATOM   1481  CA  ASN A 205     -10.575   0.605  12.792  1.00 40.79           C  
ANISOU 1481  CA  ASN A 205     6172   4147   5178    289    397    236       C  
ATOM   1482  C   ASN A 205     -12.028   0.973  13.089  1.00 43.92           C  
ANISOU 1482  C   ASN A 205     6542   4611   5534    552    443    242       C  
ATOM   1483  O   ASN A 205     -12.671   0.406  13.976  1.00 43.59           O  
ANISOU 1483  O   ASN A 205     6387   4681   5496    668    552    244       O  
ATOM   1484  CB  ASN A 205     -10.477  -0.221  11.509  1.00 40.99           C  
ANISOU 1484  CB  ASN A 205     6001   4285   5289    125    409    257       C  
ATOM   1485  CG  ASN A 205      -9.063  -0.238  10.955  1.00 39.56           C  
ANISOU 1485  CG  ASN A 205     5861   4058   5110    -96    353    256       C  
ATOM   1486  ND2 ASN A 205      -8.472  -1.423  10.839  1.00 37.38           N  
ANISOU 1486  ND2 ASN A 205     5426   3877   4898   -211    405    238       N  
ATOM   1487  OD1 ASN A 205      -8.492   0.819  10.683  1.00 41.88           O  
ANISOU 1487  OD1 ASN A 205     6336   4237   5338   -158    257    277       O  
ATOM   1488  N   ARG A 206     -12.554   1.929  12.332  1.00 43.79           N  
ANISOU 1488  N   ARG A 206     6624   4544   5470    652    360    254       N  
ATOM   1489  CA  ARG A 206     -13.908   2.421  12.556  1.00 45.57           C  
ANISOU 1489  CA  ARG A 206     6826   4846   5641    944    387    256       C  
ATOM   1490  C   ARG A 206     -14.746   2.205  11.307  1.00 44.79           C  
ANISOU 1490  C   ARG A 206     6538   4877   5603    941    370    296       C  
ATOM   1491  O   ARG A 206     -14.358   2.640  10.216  1.00 45.87           O  
ANISOU 1491  O   ARG A 206     6770   4921   5737    826    262    309       O  
ATOM   1492  CB  ARG A 206     -13.899   3.892  12.954  1.00 49.12           C  
ANISOU 1492  CB  ARG A 206     7622   5093   5948   1147    273    221       C  
ATOM   1493  CG  ARG A 206     -15.241   4.360  13.499  1.00 55.42           C  
ANISOU 1493  CG  ARG A 206     8402   5994   6661   1521    324    204       C  
ATOM   1494  CD  ARG A 206     -15.162   5.798  13.946  1.00 60.04           C  
ANISOU 1494  CD  ARG A 206     9389   6340   7082   1749    188    152       C  
ATOM   1495  NE  ARG A 206     -15.729   6.706  12.956  1.00 76.29           N  
ANISOU 1495  NE  ARG A 206    11566   8328   9093   1882     56    160       N  
ATOM   1496  CZ  ARG A 206     -15.038   7.666  12.361  1.00 68.66           C  
ANISOU 1496  CZ  ARG A 206    10929   7092   8065   1776   -135    164       C  
ATOM   1497  NH1 ARG A 206     -13.752   7.851  12.620  1.00 70.39           N1+
ANISOU 1497  NH1 ARG A 206    11360   7114   8272   1519   -215    167       N1+
ATOM   1498  NH2 ARG A 206     -15.651   8.463  11.486  1.00 72.62           N  
ANISOU 1498  NH2 ARG A 206    11550   7531   8513   1921   -258    176       N  
ATOM   1499  N   LEU A 207     -15.871   1.499  11.461  1.00 44.86           N  
ANISOU 1499  N   LEU A 207     6273   5111   5661   1043    471    326       N  
ATOM   1500  CA  LEU A 207     -16.824   1.376  10.363  1.00 45.80           C  
ANISOU 1500  CA  LEU A 207     6209   5365   5830   1071    433    367       C  
ATOM   1501  C   LEU A 207     -17.552   2.696  10.171  1.00 43.36           C  
ANISOU 1501  C   LEU A 207     6052   5006   5417   1361    345    354       C  
ATOM   1502  O   LEU A 207     -18.031   3.295  11.138  1.00 47.37           O  
ANISOU 1502  O   LEU A 207     6639   5530   5832   1633    386    328       O  
ATOM   1503  CB  LEU A 207     -17.846   0.275  10.633  1.00 46.71           C  
ANISOU 1503  CB  LEU A 207     5976   5748   6023   1075    546    420       C  
ATOM   1504  CG  LEU A 207     -17.357  -1.165  10.591  1.00 47.27           C  
ANISOU 1504  CG  LEU A 207     5892   5869   6200    790    599    442       C  
ATOM   1505  CD1 LEU A 207     -18.381  -2.070  11.242  1.00 50.00           C  
ANISOU 1505  CD1 LEU A 207     5952   6455   6589    807    711    511       C  
ATOM   1506  CD2 LEU A 207     -17.078  -1.587   9.150  1.00 46.34           C  
ANISOU 1506  CD2 LEU A 207     5740   5718   6148    589    497    447       C  
ATOM   1507  N   ILE A 208     -17.655   3.142   8.924  1.00 45.92           N  
ANISOU 1507  N   ILE A 208     6435   5272   5742   1325    219    369       N  
ATOM   1508  CA  ILE A 208     -18.426   4.342   8.618  1.00 48.48           C  
ANISOU 1508  CA  ILE A 208     6906   5545   5967   1613    110    360       C  
ATOM   1509  C   ILE A 208     -19.897   3.970   8.468  1.00 48.79           C  
ANISOU 1509  C   ILE A 208     6614   5874   6049   1807    158    397       C  
ATOM   1510  O   ILE A 208     -20.232   2.884   7.979  1.00 50.17           O  
ANISOU 1510  O   ILE A 208     6490   6232   6341   1625    202    446       O  
ATOM   1511  CB  ILE A 208     -17.873   5.018   7.351  1.00 46.73           C  
ANISOU 1511  CB  ILE A 208     6917   5127   5712   1480    -59    372       C  
ATOM   1512  CG1 ILE A 208     -16.380   5.337   7.515  1.00 47.95           C  
ANISOU 1512  CG1 ILE A 208     7351   5042   5827   1245   -100    360       C  
ATOM   1513  CG2 ILE A 208     -18.632   6.282   7.050  1.00 48.73           C  
ANISOU 1513  CG2 ILE A 208     7374   5290   5851   1787   -198    362       C  
ATOM   1514  CD1 ILE A 208     -16.072   6.263   8.698  1.00 48.57           C  
ANISOU 1514  CD1 ILE A 208     7726   4939   5792   1417   -130    313       C  
ATOM   1515  N   ASP A 209     -20.788   4.861   8.905  1.00 54.54           N  
ANISOU 1515  N   ASP A 209     7393   6654   6675   2184    140    376       N  
ATOM   1516  CA  ASP A 209     -22.222   4.653   8.750  1.00 59.10           C  
ANISOU 1516  CA  ASP A 209     7634   7543   7279   2402    176    419       C  
ATOM   1517  C   ASP A 209     -22.875   5.982   8.401  1.00 65.06           C  
ANISOU 1517  C   ASP A 209     8587   8226   7908   2776     32    384       C  
ATOM   1518  O   ASP A 209     -22.301   7.049   8.622  1.00 63.60           O  
ANISOU 1518  O   ASP A 209     8814   7754   7597   2905    -67    322       O  
ATOM   1519  CB  ASP A 209     -22.858   4.058  10.018  1.00 60.61           C  
ANISOU 1519  CB  ASP A 209     7551   8011   7469   2534    376    442       C  
ATOM   1520  CG  ASP A 209     -22.756   4.984  11.227  1.00 67.09           C  
ANISOU 1520  CG  ASP A 209     8634   8733   8122   2864    424    369       C  
ATOM   1521  OD1 ASP A 209     -23.438   6.025  11.247  1.00 66.47           O  
ANISOU 1521  OD1 ASP A 209     8674   8660   7921   3251    355    330       O  
ATOM   1522  OD2 ASP A 209     -22.003   4.668  12.169  1.00 62.32           O1-
ANISOU 1522  OD2 ASP A 209     8134   8043   7500   2755    520    346       O1-
ATOM   1523  N   ASP A 210     -24.087   5.914   7.845  1.00 70.72           N  
ANISOU 1523  N   ASP A 210     9018   9198   8655   2948      2    427       N  
ATOM   1524  CA  ASP A 210     -24.872   7.114   7.582  1.00 73.03           C  
ANISOU 1524  CA  ASP A 210     9454   9470   8822   3368   -132    392       C  
ATOM   1525  C   ASP A 210     -25.794   7.472   8.741  1.00 78.56           C  
ANISOU 1525  C   ASP A 210    10023  10412   9417   3815     -8    364       C  
ATOM   1526  O   ASP A 210     -26.736   8.249   8.554  1.00 75.55           O  
ANISOU 1526  O   ASP A 210     9627  10135   8943   4218    -90    344       O  
ATOM   1527  CB  ASP A 210     -25.695   6.957   6.300  1.00 75.03           C  
ANISOU 1527  CB  ASP A 210     9483   9876   9149   3355   -260    448       C  
ATOM   1528  CG  ASP A 210     -26.607   5.744   6.326  1.00 77.06           C  
ANISOU 1528  CG  ASP A 210     9184  10550   9545   3245   -138    537       C  
ATOM   1529  OD1 ASP A 210     -27.001   5.300   7.425  1.00 71.86           O  
ANISOU 1529  OD1 ASP A 210     8281  10136   8887   3336     50    558       O  
ATOM   1530  OD2 ASP A 210     -26.943   5.237   5.236  1.00 86.85           O1-
ANISOU 1530  OD2 ASP A 210    10241  11873  10884   3055   -241    593       O1-
ATOM   1531  N   GLY A 211     -25.553   6.916   9.925  1.00 71.27           N  
ANISOU 1531  N   GLY A 211     9000   9590   8489   3770    190    363       N  
ATOM   1532  CA  GLY A 211     -26.447   7.076  11.043  1.00 80.57           C  
ANISOU 1532  CA  GLY A 211     9994  11060   9559   4165    348    354       C  
ATOM   1533  C   GLY A 211     -27.475   5.975  11.194  1.00 80.90           C  
ANISOU 1533  C   GLY A 211     9439  11592   9710   4098    518    469       C  
ATOM   1534  O   GLY A 211     -28.020   5.803  12.290  1.00 86.66           O  
ANISOU 1534  O   GLY A 211     9966  12599  10360   4310    711    488       O  
ATOM   1535  N   THR A 212     -27.768   5.235  10.129  1.00 79.94           N  
ANISOU 1535  N   THR A 212     9036  11586   9751   3803    446    554       N  
ATOM   1536  CA  THR A 212     -28.679   4.101  10.249  1.00 74.62           C  
ANISOU 1536  CA  THR A 212     7807  11354   9191   3655    579    684       C  
ATOM   1537  C   THR A 212     -28.090   2.796   9.724  1.00 74.53           C  
ANISOU 1537  C   THR A 212     7676  11280   9361   3096    569    755       C  
ATOM   1538  O   THR A 212     -28.340   1.742  10.314  1.00 72.79           O  
ANISOU 1538  O   THR A 212     7149  11300   9209   2888    719    848       O  
ATOM   1539  CB  THR A 212     -30.025   4.410   9.539  1.00 80.43           C  
ANISOU 1539  CB  THR A 212     8211  12414   9935   3917    488    738       C  
ATOM   1540  CG2 THR A 212     -30.364   5.894   9.623  1.00 78.43           C  
ANISOU 1540  CG2 THR A 212     8232  12071   9496   4477    397    630       C  
ATOM   1541  OG1 THR A 212     -29.955   4.029   8.162  1.00 96.52           O  
ANISOU 1541  OG1 THR A 212    10211  14351  12109   3614    297    775       O  
ATOM   1542  N   ARG A 213     -27.295   2.836   8.650  1.00 80.72           N  
ANISOU 1542  N   ARG A 213     8717  11746  10208   2854    396    715       N  
ATOM   1543  CA  ARG A 213     -26.710   1.634   8.063  1.00 76.26           C  
ANISOU 1543  CA  ARG A 213     8078  11106   9792   2370    369    763       C  
ATOM   1544  C   ARG A 213     -25.223   1.844   7.796  1.00 64.51           C  
ANISOU 1544  C   ARG A 213     7024   9200   8288   2175    307    675       C  
ATOM   1545  O   ARG A 213     -24.735   2.973   7.732  1.00 67.68           O  
ANISOU 1545  O   ARG A 213     7779   9354   8581   2366    228    595       O  
ATOM   1546  CB  ARG A 213     -27.418   1.243   6.752  1.00 70.28           C  
ANISOU 1546  CB  ARG A 213     7093  10476   9136   2235    207    828       C  
ATOM   1547  CG  ARG A 213     -28.936   1.233   6.851  1.00 85.91           C  
ANISOU 1547  CG  ARG A 213     8629  12886  11125   2455    227    921       C  
ATOM   1548  CD  ARG A 213     -29.604   1.304   5.488  1.00 90.22           C  
ANISOU 1548  CD  ARG A 213     9051  13496  11731   2433     11    955       C  
ATOM   1549  NE  ARG A 213     -30.058  -0.010   5.047  1.00108.56           N  
ANISOU 1549  NE  ARG A 213    11029  16019  14200   2057    -26   1070       N  
ATOM   1550  CZ  ARG A 213     -30.945  -0.760   5.687  1.00102.66           C  
ANISOU 1550  CZ  ARG A 213     9843  15655  13509   1987     85   1195       C  
ATOM   1551  NH1 ARG A 213     -31.607  -0.308   6.741  1.00107.58           N1+
ANISOU 1551  NH1 ARG A 213    10260  16567  14047   2309    256   1225       N1+
ATOM   1552  NH2 ARG A 213     -31.188  -1.993   5.248  1.00113.37           N  
ANISOU 1552  NH2 ARG A 213    10969  17112  14994   1582     17   1299       N  
ATOM   1553  N   LEU A 214     -24.502   0.735   7.632  1.00 57.80           N  
ANISOU 1553  N   LEU A 214     6145   8276   7539   1789    332    697       N  
ATOM   1554  CA  LEU A 214     -23.092   0.802   7.272  1.00 49.09           C  
ANISOU 1554  CA  LEU A 214     5386   6836   6429   1581    277    628       C  
ATOM   1555  C   LEU A 214     -22.928   1.313   5.845  1.00 53.25           C  
ANISOU 1555  C   LEU A 214     6074   7209   6948   1539     90    609       C  
ATOM   1556  O   LEU A 214     -23.705   0.968   4.951  1.00 55.24           O  
ANISOU 1556  O   LEU A 214     6126   7604   7258   1495     -3    658       O  
ATOM   1557  CB  LEU A 214     -22.448  -0.573   7.398  1.00 51.81           C  
ANISOU 1557  CB  LEU A 214     5638   7173   6874   1223    342    652       C  
ATOM   1558  CG  LEU A 214     -22.445  -1.226   8.779  1.00 53.86           C  
ANISOU 1558  CG  LEU A 214     5776   7549   7140   1200    517    681       C  
ATOM   1559  CD1 LEU A 214     -21.745  -2.576   8.674  1.00 49.03           C  
ANISOU 1559  CD1 LEU A 214     5130   6876   6621    842    529    698       C  
ATOM   1560  CD2 LEU A 214     -21.775  -0.334   9.819  1.00 51.59           C  
ANISOU 1560  CD2 LEU A 214     5763   7104   6736   1398    591    608       C  
ATOM   1561  N   THR A 215     -21.899   2.134   5.621  1.00 52.62           N  
ANISOU 1561  N   THR A 215     6366   6840   6788   1532     26    547       N  
ATOM   1562  CA  THR A 215     -21.625   2.588   4.262  1.00 48.05           C  
ANISOU 1562  CA  THR A 215     5966   6108   6183   1453   -140    542       C  
ATOM   1563  C   THR A 215     -20.832   1.576   3.449  1.00 48.43           C  
ANISOU 1563  C   THR A 215     5995   6105   6302   1095   -153    550       C  
ATOM   1564  O   THR A 215     -20.726   1.729   2.226  1.00 47.98           O  
ANISOU 1564  O   THR A 215     6032   5975   6222   1009   -278    557       O  
ATOM   1565  CB  THR A 215     -20.847   3.910   4.269  1.00 53.85           C  
ANISOU 1565  CB  THR A 215     7117   6557   6787   1556   -221    497       C  
ATOM   1566  CG2 THR A 215     -21.630   5.019   4.967  1.00 52.61           C  
ANISOU 1566  CG2 THR A 215     7054   6406   6527   1960   -246    471       C  
ATOM   1567  OG1 THR A 215     -19.582   3.704   4.917  1.00 49.90           O  
ANISOU 1567  OG1 THR A 215     6771   5907   6282   1364   -137    467       O  
ATOM   1568  N   GLY A 216     -20.266   0.555   4.084  1.00 46.95           N  
ANISOU 1568  N   GLY A 216     5708   5949   6181    904    -33    544       N  
ATOM   1569  CA  GLY A 216     -19.342  -0.307   3.382  1.00 43.24           C  
ANISOU 1569  CA  GLY A 216     5279   5401   5747    613    -46    530       C  
ATOM   1570  C   GLY A 216     -17.926   0.215   3.315  1.00 46.09           C  
ANISOU 1570  C   GLY A 216     5928   5548   6035    513    -40    488       C  
ATOM   1571  O   GLY A 216     -17.119  -0.307   2.533  1.00 44.70           O  
ANISOU 1571  O   GLY A 216     5805   5321   5857    310    -60    475       O  
ATOM   1572  N   THR A 217     -17.586   1.232   4.102  1.00 39.46           N  
ANISOU 1572  N   THR A 217     5279   4590   5124    650    -22    469       N  
ATOM   1573  CA  THR A 217     -16.213   1.720   4.136  1.00 44.08           C  
ANISOU 1573  CA  THR A 217     6118   4985   5643    517    -28    448       C  
ATOM   1574  C   THR A 217     -15.725   1.851   5.571  1.00 45.52           C  
ANISOU 1574  C   THR A 217     6364   5114   5819    568     63    418       C  
ATOM   1575  O   THR A 217     -16.496   1.818   6.539  1.00 42.64           O  
ANISOU 1575  O   THR A 217     5898   4837   5466    754    129    412       O  
ATOM   1576  CB  THR A 217     -16.056   3.067   3.413  1.00 45.01           C  
ANISOU 1576  CB  THR A 217     6521   4934   5647    573   -165    467       C  
ATOM   1577  CG2 THR A 217     -16.458   2.935   1.951  1.00 42.00           C  
ANISOU 1577  CG2 THR A 217     6104   4598   5256    513   -260    498       C  
ATOM   1578  OG1 THR A 217     -16.869   4.067   4.040  1.00 41.53           O  
ANISOU 1578  OG1 THR A 217     6185   4446   5148    865   -213    459       O  
ATOM   1579  N   VAL A 218     -14.412   2.027   5.673  1.00 42.43           N  
ANISOU 1579  N   VAL A 218     6139   4590   5392    398     62    406       N  
ATOM   1580  CA  VAL A 218     -13.693   2.138   6.931  1.00 41.41           C  
ANISOU 1580  CA  VAL A 218     6103   4383   5249    396    120    377       C  
ATOM   1581  C   VAL A 218     -13.105   3.532   6.997  1.00 46.66           C  
ANISOU 1581  C   VAL A 218     7097   4831   5800    413      5    385       C  
ATOM   1582  O   VAL A 218     -12.698   4.084   5.967  1.00 45.90           O  
ANISOU 1582  O   VAL A 218     7135   4652   5651    293    -91    422       O  
ATOM   1583  CB  VAL A 218     -12.582   1.068   7.004  1.00 45.19           C  
ANISOU 1583  CB  VAL A 218     6477   4904   5787    160    193    362       C  
ATOM   1584  CG1 VAL A 218     -11.805   1.174   8.288  1.00 52.36           C  
ANISOU 1584  CG1 VAL A 218     7481   5733   6680    152    232    334       C  
ATOM   1585  CG2 VAL A 218     -13.190  -0.314   6.831  1.00 47.22           C  
ANISOU 1585  CG2 VAL A 218     6463   5334   6143    130    267    358       C  
ATOM   1586  N   ALA A 219     -13.068   4.107   8.198  1.00 47.54           N  
ANISOU 1586  N   ALA A 219     7363   4842   5859    555      4    354       N  
ATOM   1587  CA  ALA A 219     -12.430   5.405   8.364  1.00 46.11           C  
ANISOU 1587  CA  ALA A 219     7540   4417   5562    544   -134    362       C  
ATOM   1588  C   ALA A 219     -10.968   5.346   7.930  1.00 46.43           C  
ANISOU 1588  C   ALA A 219     7641   4395   5605    207   -170    401       C  
ATOM   1589  O   ALA A 219     -10.227   4.418   8.271  1.00 45.62           O  
ANISOU 1589  O   ALA A 219     7367   4392   5574     54    -75    388       O  
ATOM   1590  CB  ALA A 219     -12.532   5.867   9.822  1.00 45.45           C  
ANISOU 1590  CB  ALA A 219     7619   4236   5415    744   -129    310       C  
ATOM   1591  N   GLU A 220     -10.550   6.359   7.186  1.00 52.61           N  
ANISOU 1591  N   GLU A 220     8671   5020   6298     96   -313    457       N  
ATOM   1592  CA  GLU A 220      -9.154   6.515   6.801  1.00 46.08           C  
ANISOU 1592  CA  GLU A 220     7915   4147   5446   -233   -359    518       C  
ATOM   1593  C   GLU A 220      -8.369   7.233   7.894  1.00 54.02           C  
ANISOU 1593  C   GLU A 220     9167   4965   6393   -293   -452    517       C  
ATOM   1594  O   GLU A 220      -8.884   8.180   8.503  1.00 51.92           O  
ANISOU 1594  O   GLU A 220     9186   4500   6042    -97   -566    491       O  
ATOM   1595  CB  GLU A 220      -9.036   7.336   5.516  1.00 63.15           C  
ANISOU 1595  CB  GLU A 220    10252   6223   7518   -365   -481    605       C  
ATOM   1596  CG  GLU A 220     -10.111   7.048   4.510  1.00 71.68           C  
ANISOU 1596  CG  GLU A 220    11212   7408   8615   -223   -459    600       C  
ATOM   1597  CD  GLU A 220      -9.609   6.055   3.508  1.00 72.58           C  
ANISOU 1597  CD  GLU A 220    11073   7727   8777   -427   -355    626       C  
ATOM   1598  OE1 GLU A 220      -8.459   5.603   3.705  1.00 59.20           O  
ANISOU 1598  OE1 GLU A 220     9284   6106   7103   -640   -289    640       O  
ATOM   1599  OE2 GLU A 220     -10.360   5.695   2.575  1.00 61.38           O1-
ANISOU 1599  OE2 GLU A 220     9548   6404   7371   -356   -345    626       O1-
ATOM   1600  N   PRO A 221      -7.097   6.856   8.111  1.00 53.44           N  
ANISOU 1600  N   PRO A 221     9010   4946   6350   -558   -428    545       N  
ATOM   1601  CA  PRO A 221      -6.418   5.774   7.397  1.00 51.42           C  
ANISOU 1601  CA  PRO A 221     8439   4929   6171   -753   -301    566       C  
ATOM   1602  C   PRO A 221      -6.630   4.428   8.060  1.00 52.04           C  
ANISOU 1602  C   PRO A 221     8235   5176   6361   -637   -142    482       C  
ATOM   1603  O   PRO A 221      -6.930   4.356   9.248  1.00 46.44           O  
ANISOU 1603  O   PRO A 221     7570   4408   5668   -484   -127    426       O  
ATOM   1604  CB  PRO A 221      -4.952   6.161   7.476  1.00 49.01           C  
ANISOU 1604  CB  PRO A 221     8197   4599   5826  -1062   -374    641       C  
ATOM   1605  CG  PRO A 221      -4.849   6.912   8.755  1.00 60.72           C  
ANISOU 1605  CG  PRO A 221     9942   5862   7268  -1000   -495    616       C  
ATOM   1606  CD  PRO A 221      -6.161   7.626   8.949  1.00 60.93           C  
ANISOU 1606  CD  PRO A 221    10205   5711   7236   -699   -561    571       C  
ATOM   1607  N   ILE A 222      -6.451   3.363   7.297  1.00 43.61           N  
ANISOU 1607  N   ILE A 222     6906   4310   5355   -711    -33    476       N  
ATOM   1608  CA  ILE A 222      -6.728   2.021   7.798  1.00 42.65           C  
ANISOU 1608  CA  ILE A 222     6544   4327   5332   -611     96    404       C  
ATOM   1609  C   ILE A 222      -5.577   1.569   8.683  1.00 43.83           C  
ANISOU 1609  C   ILE A 222     6636   4507   5509   -718    119    384       C  
ATOM   1610  O   ILE A 222      -4.402   1.718   8.323  1.00 39.86           O  
ANISOU 1610  O   ILE A 222     6112   4056   4978   -921     91    427       O  
ATOM   1611  CB  ILE A 222      -6.948   1.050   6.632  1.00 38.25           C  
ANISOU 1611  CB  ILE A 222     5781   3940   4813   -641    170    397       C  
ATOM   1612  CG1 ILE A 222      -8.128   1.534   5.783  1.00 49.71           C  
ANISOU 1612  CG1 ILE A 222     7292   5359   6235   -532    123    420       C  
ATOM   1613  CG2 ILE A 222      -7.157  -0.368   7.163  1.00 37.87           C  
ANISOU 1613  CG2 ILE A 222     5528   4004   4858   -568    272    330       C  
ATOM   1614  CD1 ILE A 222      -8.810   0.458   4.991  1.00 55.73           C  
ANISOU 1614  CD1 ILE A 222     7860   6263   7053   -489    181    392       C  
ATOM   1615  N   LEU A 223      -5.908   0.992   9.835  1.00 40.35           N  
ANISOU 1615  N   LEU A 223     6156   4058   5118   -583    171    325       N  
ATOM   1616  CA  LEU A 223      -4.908   0.513  10.774  1.00 42.53           C  
ANISOU 1616  CA  LEU A 223     6388   4351   5418   -652    181    299       C  
ATOM   1617  C   LEU A 223      -4.614  -0.960  10.503  1.00 36.77           C  
ANISOU 1617  C   LEU A 223     5412   3796   4762   -668    281    258       C  
ATOM   1618  O   LEU A 223      -5.511  -1.801  10.594  1.00 39.01           O  
ANISOU 1618  O   LEU A 223     5603   4124   5096   -546    353    223       O  
ATOM   1619  CB  LEU A 223      -5.394   0.695  12.207  1.00 39.53           C  
ANISOU 1619  CB  LEU A 223     6138   3855   5027   -491    175    260       C  
ATOM   1620  CG  LEU A 223      -5.885   2.078  12.621  1.00 43.20           C  
ANISOU 1620  CG  LEU A 223     6889   4126   5399   -391     71    274       C  
ATOM   1621  CD1 LEU A 223      -6.279   2.019  14.116  1.00 51.12           C  
ANISOU 1621  CD1 LEU A 223     7993   5056   6374   -206     95    221       C  
ATOM   1622  CD2 LEU A 223      -4.845   3.157  12.379  1.00 44.32           C  
ANISOU 1622  CD2 LEU A 223     7223   4144   5474   -596    -81    330       C  
ATOM   1623  N   GLY A 224      -3.358  -1.266  10.188  1.00 40.21           N  
ANISOU 1623  N   GLY A 224     5748   4335   5195   -817    276    266       N  
ATOM   1624  CA  GLY A 224      -2.971  -2.647   9.968  1.00 38.90           C  
ANISOU 1624  CA  GLY A 224     5384   4319   5077   -797    352    213       C  
ATOM   1625  C   GLY A 224      -1.759  -3.036  10.786  1.00 43.04           C  
ANISOU 1625  C   GLY A 224     5848   4891   5612   -847    333    190       C  
ATOM   1626  O   GLY A 224      -1.681  -2.720  11.976  1.00 37.93           O  
ANISOU 1626  O   GLY A 224     5310   4132   4969   -822    286    183       O  
ATOM   1627  N   ARG A 225      -0.794  -3.702  10.149  1.00 37.51           N  
ANISOU 1627  N   ARG A 225     4980   4368   4905   -901    363    175       N  
ATOM   1628  CA  ARG A 225       0.377  -4.210  10.865  1.00 36.92           C  
ANISOU 1628  CA  ARG A 225     4810   4376   4844   -919    341    146       C  
ATOM   1629  C   ARG A 225       1.155  -3.086  11.541  1.00 42.54           C  
ANISOU 1629  C   ARG A 225     5602   5032   5527  -1069    240    211       C  
ATOM   1630  O   ARG A 225       1.497  -3.177  12.731  1.00 38.42           O  
ANISOU 1630  O   ARG A 225     5133   4438   5027  -1043    182    186       O  
ATOM   1631  CB  ARG A 225       1.293  -4.978   9.895  1.00 42.52           C  
ANISOU 1631  CB  ARG A 225     5311   5322   5523   -926    394    124       C  
ATOM   1632  CG  ARG A 225       2.270  -5.975  10.546  1.00 51.05           C  
ANISOU 1632  CG  ARG A 225     6265   6508   6623   -844    385     58       C  
ATOM   1633  CD  ARG A 225       3.273  -6.612   9.522  1.00 53.26           C  
ANISOU 1633  CD  ARG A 225     6328   7064   6844   -817    441     33       C  
ATOM   1634  NE  ARG A 225       4.659  -6.614  10.001  1.00 61.34           N  
ANISOU 1634  NE  ARG A 225     7190   8262   7856   -861    402     46       N  
ATOM   1635  CZ  ARG A 225       5.429  -5.536  10.108  1.00 60.03           C  
ANISOU 1635  CZ  ARG A 225     6966   8176   7667  -1072    351    150       C  
ATOM   1636  NH1 ARG A 225       4.990  -4.331   9.765  1.00 55.91           N1+
ANISOU 1636  NH1 ARG A 225     6567   7553   7122  -1254    327    248       N1+
ATOM   1637  NH2 ARG A 225       6.661  -5.662  10.590  1.00 66.81           N  
ANISOU 1637  NH2 ARG A 225     7650   9213   8523  -1105    304    160       N  
ATOM   1638  N   GLU A 226       1.469  -2.023  10.794  1.00 40.43           N  
ANISOU 1638  N   GLU A 226     5366   4792   5205  -1244    200    301       N  
ATOM   1639  CA  GLU A 226       2.284  -0.954  11.366  1.00 41.11           C  
ANISOU 1639  CA  GLU A 226     5543   4819   5257  -1432     72    378       C  
ATOM   1640  C   GLU A 226       1.548  -0.215  12.482  1.00 40.45           C  
ANISOU 1640  C   GLU A 226     5744   4456   5170  -1368    -21    364       C  
ATOM   1641  O   GLU A 226       2.182   0.284  13.426  1.00 40.20           O  
ANISOU 1641  O   GLU A 226     5813   4338   5124  -1454   -141    383       O  
ATOM   1642  CB  GLU A 226       2.705   0.030  10.275  1.00 46.37           C  
ANISOU 1642  CB  GLU A 226     6212   5558   5850  -1659     39    496       C  
ATOM   1643  CG  GLU A 226       3.977  -0.367   9.535  1.00 63.79           C  
ANISOU 1643  CG  GLU A 226     8129   8081   8026  -1797     91    545       C  
ATOM   1644  CD  GLU A 226       5.119  -0.777  10.459  1.00 61.39           C  
ANISOU 1644  CD  GLU A 226     7672   7895   7757  -1832     39    530       C  
ATOM   1645  OE1 GLU A 226       5.433  -0.028  11.410  1.00 68.68           O  
ANISOU 1645  OE1 GLU A 226     8739   8672   8686  -1954   -107    570       O  
ATOM   1646  OE2 GLU A 226       5.701  -1.857  10.223  1.00 85.41           O1-
ANISOU 1646  OE2 GLU A 226    10464  11174  10813  -1723    129    471       O1-
ATOM   1647  N   ALA A 227       0.223  -0.112  12.386  1.00 37.30           N  
ANISOU 1647  N   ALA A 227     5476   3926   4771  -1210     25    334       N  
ATOM   1648  CA  ALA A 227      -0.536   0.550  13.446  1.00 40.82           C  
ANISOU 1648  CA  ALA A 227     6182   4139   5191  -1094    -42    311       C  
ATOM   1649  C   ALA A 227      -0.424  -0.190  14.776  1.00 41.39           C  
ANISOU 1649  C   ALA A 227     6250   4182   5293   -973    -29    241       C  
ATOM   1650  O   ALA A 227      -0.452   0.444  15.843  1.00 35.64           O  
ANISOU 1650  O   ALA A 227     5739   3285   4518   -938   -123    232       O  
ATOM   1651  CB  ALA A 227      -2.004   0.660  13.051  1.00 42.88           C  
ANISOU 1651  CB  ALA A 227     6517   4330   5446   -916     27    292       C  
ATOM   1652  N   LYS A 228      -0.321  -1.522  14.741  1.00 36.30           N  
ANISOU 1652  N   LYS A 228     5397   3683   4712   -899     72    190       N  
ATOM   1653  CA  LYS A 228      -0.147  -2.254  15.989  1.00 34.32           C  
ANISOU 1653  CA  LYS A 228     5160   3400   4480   -799     71    134       C  
ATOM   1654  C   LYS A 228       1.244  -2.007  16.559  1.00 37.18           C  
ANISOU 1654  C   LYS A 228     5511   3785   4830   -938    -53    150       C  
ATOM   1655  O   LYS A 228       1.401  -1.870  17.776  1.00 37.32           O  
ANISOU 1655  O   LYS A 228     5675   3683   4822   -896   -129    126       O  
ATOM   1656  CB  LYS A 228      -0.420  -3.758  15.791  1.00 33.98           C  
ANISOU 1656  CB  LYS A 228     4940   3475   4497   -689    184     80       C  
ATOM   1657  CG  LYS A 228      -1.861  -4.039  15.358  1.00 32.62           C  
ANISOU 1657  CG  LYS A 228     4774   3280   4340   -574    284     77       C  
ATOM   1658  CD  LYS A 228      -2.115  -5.552  15.153  1.00 33.98           C  
ANISOU 1658  CD  LYS A 228     4807   3540   4565   -501    360     34       C  
ATOM   1659  CE  LYS A 228      -3.599  -5.789  14.929  1.00 35.16           C  
ANISOU 1659  CE  LYS A 228     4963   3665   4730   -416    438     49       C  
ATOM   1660  NZ  LYS A 228      -3.908  -7.177  14.380  1.00 41.31           N1+
ANISOU 1660  NZ  LYS A 228     5624   4515   5556   -395    480     22       N1+
ATOM   1661  N   VAL A 229       2.262  -1.905  15.693  1.00 34.14           N  
ANISOU 1661  N   VAL A 229     4951   3568   4454  -1110    -80    197       N  
ATOM   1662  CA  VAL A 229       3.603  -1.552  16.143  1.00 35.82           C  
ANISOU 1662  CA  VAL A 229     5116   3840   4655  -1278   -211    236       C  
ATOM   1663  C   VAL A 229       3.593  -0.173  16.773  1.00 39.51           C  
ANISOU 1663  C   VAL A 229     5866   4087   5060  -1398   -372    289       C  
ATOM   1664  O   VAL A 229       4.168   0.057  17.845  1.00 37.35           O  
ANISOU 1664  O   VAL A 229     5699   3724   4767  -1438   -504    282       O  
ATOM   1665  CB  VAL A 229       4.606  -1.594  14.974  1.00 38.52           C  
ANISOU 1665  CB  VAL A 229     5190   4447   4998  -1450   -189    300       C  
ATOM   1666  CG1 VAL A 229       5.976  -1.119  15.427  1.00 42.69           C  
ANISOU 1666  CG1 VAL A 229     5638   5067   5513  -1659   -337    366       C  
ATOM   1667  CG2 VAL A 229       4.716  -2.984  14.418  1.00 40.64           C  
ANISOU 1667  CG2 VAL A 229     5215   4921   5304  -1295    -54    229       C  
ATOM   1668  N   GLU A 230       2.998   0.782  16.068  1.00 38.90           N  
ANISOU 1668  N   GLU A 230     5931   3910   4938  -1462   -384    343       N  
ATOM   1669  CA  GLU A 230       2.996   2.163  16.536  1.00 40.46           C  
ANISOU 1669  CA  GLU A 230     6446   3870   5058  -1577   -564    395       C  
ATOM   1670  C   GLU A 230       2.280   2.292  17.874  1.00 42.83           C  
ANISOU 1670  C   GLU A 230     7020   3939   5315  -1364   -606    314       C  
ATOM   1671  O   GLU A 230       2.695   3.079  18.736  1.00 43.62           O  
ANISOU 1671  O   GLU A 230     7364   3859   5350  -1439   -788    326       O  
ATOM   1672  CB  GLU A 230       2.351   3.029  15.471  1.00 44.83           C  
ANISOU 1672  CB  GLU A 230     7115   4352   5564  -1633   -561    457       C  
ATOM   1673  CG  GLU A 230       3.286   3.221  14.280  1.00 51.14           C  
ANISOU 1673  CG  GLU A 230     7708   5359   6364  -1912   -567    569       C  
ATOM   1674  CD  GLU A 230       2.580   3.694  13.038  1.00 67.00           C  
ANISOU 1674  CD  GLU A 230     9765   7356   8335  -1928   -511    619       C  
ATOM   1675  OE1 GLU A 230       1.328   3.774  13.050  1.00 61.29           O  
ANISOU 1675  OE1 GLU A 230     9198   6487   7603  -1703   -460    558       O  
ATOM   1676  OE2 GLU A 230       3.291   4.014  12.062  1.00 58.84           O1-
ANISOU 1676  OE2 GLU A 230     8610   6474   7272  -2171   -523    728       O1-
ATOM   1677  N   LYS A 231       1.212   1.523  18.067  1.00 38.33           N  
ANISOU 1677  N   LYS A 231     6418   3379   4768  -1105   -444    238       N  
ATOM   1678  CA  LYS A 231       0.496   1.588  19.338  1.00 44.39           C  
ANISOU 1678  CA  LYS A 231     7419   3972   5475   -888   -451    171       C  
ATOM   1679  C   LYS A 231       1.335   1.027  20.479  1.00 42.02           C  
ANISOU 1679  C   LYS A 231     7109   3678   5180   -899   -519    136       C  
ATOM   1680  O   LYS A 231       1.340   1.592  21.580  1.00 40.18           O  
ANISOU 1680  O   LYS A 231     7150   3258   4859   -842   -637    109       O  
ATOM   1681  CB  LYS A 231      -0.825   0.841  19.247  1.00 40.98           C  
ANISOU 1681  CB  LYS A 231     6908   3597   5065   -645   -254    124       C  
ATOM   1682  CG  LYS A 231      -1.696   0.976  20.493  1.00 40.69           C  
ANISOU 1682  CG  LYS A 231     7097   3423   4942   -406   -229     70       C  
ATOM   1683  CD  LYS A 231      -1.942   2.475  20.824  1.00 42.21           C  
ANISOU 1683  CD  LYS A 231     7651   3380   5007   -362   -379     72       C  
ATOM   1684  CE  LYS A 231      -2.976   2.614  21.908  1.00 47.86           C  
ANISOU 1684  CE  LYS A 231     8572   4001   5612    -65   -317     13       C  
ATOM   1685  NZ  LYS A 231      -3.103   4.039  22.316  1.00 46.43           N1+
ANISOU 1685  NZ  LYS A 231     8789   3568   5285     10   -489     -5       N1+
ATOM   1686  N   LEU A 232       2.047  -0.082  20.239  1.00 36.54           N  
ANISOU 1686  N   LEU A 232     6122   3189   4573   -951   -458    129       N  
ATOM   1687  CA  LEU A 232       2.989  -0.583  21.240  1.00 36.71           C  
ANISOU 1687  CA  LEU A 232     6122   3228   4600   -973   -552    102       C  
ATOM   1688  C   LEU A 232       4.042   0.463  21.589  1.00 42.09           C  
ANISOU 1688  C   LEU A 232     6933   3824   5237  -1197   -785    156       C  
ATOM   1689  O   LEU A 232       4.350   0.676  22.769  1.00 40.95           O  
ANISOU 1689  O   LEU A 232     6987   3539   5034  -1173   -921    127       O  
ATOM   1690  CB  LEU A 232       3.649  -1.875  20.744  1.00 35.34           C  
ANISOU 1690  CB  LEU A 232     5610   3301   4518   -979   -468     86       C  
ATOM   1691  CG  LEU A 232       4.805  -2.410  21.593  1.00 40.87           C  
ANISOU 1691  CG  LEU A 232     6236   4062   5231  -1010   -585     65       C  
ATOM   1692  CD1 LEU A 232       4.379  -2.635  23.055  1.00 38.72           C  
ANISOU 1692  CD1 LEU A 232     6211   3604   4897   -845   -621      8       C  
ATOM   1693  CD2 LEU A 232       5.356  -3.720  21.005  1.00 39.08           C  
ANISOU 1693  CD2 LEU A 232     5691   4077   5080   -955   -495     35       C  
ATOM   1694  N   VAL A 233       4.599   1.143  20.581  1.00 37.93           N  
ANISOU 1694  N   VAL A 233     6310   3376   4725  -1432   -846    243       N  
ATOM   1695  CA  VAL A 233       5.576   2.188  20.849  1.00 40.94           C  
ANISOU 1695  CA  VAL A 233     6819   3675   5062  -1699  -1088    320       C  
ATOM   1696  C   VAL A 233       4.941   3.304  21.678  1.00 42.39           C  
ANISOU 1696  C   VAL A 233     7464   3514   5128  -1637  -1235    298       C  
ATOM   1697  O   VAL A 233       5.549   3.822  22.628  1.00 42.60           O  
ANISOU 1697  O   VAL A 233     7699   3390   5095  -1730  -1450    302       O  
ATOM   1698  CB  VAL A 233       6.153   2.739  19.527  1.00 45.58           C  
ANISOU 1698  CB  VAL A 233     7231   4418   5671  -1979  -1106    440       C  
ATOM   1699  CG1 VAL A 233       6.901   4.033  19.784  1.00 45.45           C  
ANISOU 1699  CG1 VAL A 233     7431   4251   5587  -2284  -1378    542       C  
ATOM   1700  CG2 VAL A 233       7.072   1.719  18.852  1.00 43.35           C  
ANISOU 1700  CG2 VAL A 233     6495   4502   5473  -2045   -999    462       C  
ATOM   1701  N   GLU A 234       3.702   3.681  21.333  1.00 45.26           N  
ANISOU 1701  N   GLU A 234     8000   3751   5445  -1461  -1132    271       N  
ATOM   1702  CA  GLU A 234       3.036   4.801  22.006  1.00 44.68           C  
ANISOU 1702  CA  GLU A 234     8380   3358   5237  -1353  -1267    242       C  
ATOM   1703  C   GLU A 234       2.745   4.466  23.463  1.00 40.10           C  
ANISOU 1703  C   GLU A 234     7993   2657   4586  -1117  -1277    144       C  
ATOM   1704  O   GLU A 234       2.974   5.299  24.361  1.00 43.56           O  
ANISOU 1704  O   GLU A 234     8769   2874   4906  -1121  -1482    126       O  
ATOM   1705  CB  GLU A 234       1.733   5.150  21.274  1.00 43.64           C  
ANISOU 1705  CB  GLU A 234     8334   3173   5075  -1167  -1132    228       C  
ATOM   1706  CG  GLU A 234       1.020   6.414  21.789  1.00 48.48           C  
ANISOU 1706  CG  GLU A 234     9396   3497   5528  -1011  -1269    195       C  
ATOM   1707  CD  GLU A 234       0.105   6.166  22.990  1.00 47.22           C  
ANISOU 1707  CD  GLU A 234     9408   3258   5274   -647  -1181     83       C  
ATOM   1708  OE1 GLU A 234      -0.393   5.028  23.151  1.00 49.69           O  
ANISOU 1708  OE1 GLU A 234     9510   3715   5656   -490   -967     42       O  
ATOM   1709  OE2 GLU A 234      -0.099   7.124  23.780  1.00 49.77           O1-
ANISOU 1709  OE2 GLU A 234    10025   3450   5434   -514  -1314     43       O1-
ATOM   1710  N   ILE A 235       2.261   3.245  23.717  1.00 41.86           N  
ANISOU 1710  N   ILE A 235     8003   3038   4863   -912  -1061     85       N  
ATOM   1711  CA  ILE A 235       1.952   2.840  25.087  1.00 43.38           C  
ANISOU 1711  CA  ILE A 235     8366   3140   4976   -692  -1047      6       C  
ATOM   1712  C   ILE A 235       3.217   2.829  25.927  1.00 44.69           C  
ANISOU 1712  C   ILE A 235     8587   3263   5131   -855  -1261     10       C  
ATOM   1713  O   ILE A 235       3.259   3.387  27.031  1.00 46.58           O  
ANISOU 1713  O   ILE A 235     9170   3288   5241   -783  -1416    -32       O  
ATOM   1714  CB  ILE A 235       1.271   1.461  25.113  1.00 39.05           C  
ANISOU 1714  CB  ILE A 235     7563   2781   4493   -501   -789    -31       C  
ATOM   1715  CG1 ILE A 235      -0.156   1.536  24.580  1.00 42.75           C  
ANISOU 1715  CG1 ILE A 235     8029   3271   4944   -303   -597    -40       C  
ATOM   1716  CG2 ILE A 235       1.303   0.884  26.554  1.00 40.48           C  
ANISOU 1716  CG2 ILE A 235     7880   2903   4596   -346   -796    -88       C  
ATOM   1717  CD1 ILE A 235      -0.644   0.187  24.088  1.00 40.89           C  
ANISOU 1717  CD1 ILE A 235     7462   3257   4817   -240   -374    -37       C  
ATOM   1718  N   ALA A 236       4.270   2.185  25.421  1.00 41.71           N  
ANISOU 1718  N   ALA A 236     7871   3099   4878  -1060  -1280     57       N  
ATOM   1719  CA  ALA A 236       5.506   2.086  26.194  1.00 47.73           C  
ANISOU 1719  CA  ALA A 236     8627   3865   5642  -1209  -1487     66       C  
ATOM   1720  C   ALA A 236       6.058   3.464  26.541  1.00 53.22           C  
ANISOU 1720  C   ALA A 236     9644   4333   6246  -1418  -1784    111       C  
ATOM   1721  O   ALA A 236       6.467   3.710  27.682  1.00 50.28           O  
ANISOU 1721  O   ALA A 236     9519   3798   5787  -1412  -1977     78       O  
ATOM   1722  CB  ALA A 236       6.544   1.264  25.430  1.00 46.96           C  
ANISOU 1722  CB  ALA A 236     8080   4077   5687  -1381  -1454    116       C  
ATOM   1723  N   GLU A 237       6.082   4.380  25.577  1.00 47.93           N  
ANISOU 1723  N   GLU A 237     9003   3629   5581  -1615  -1845    192       N  
ATOM   1724  CA  GLU A 237       6.573   5.714  25.881  1.00 51.22           C  
ANISOU 1724  CA  GLU A 237     9680   3896   5884  -1774  -2105    254       C  
ATOM   1725  C   GLU A 237       5.696   6.396  26.927  1.00 49.15           C  
ANISOU 1725  C   GLU A 237     9828   3414   5432  -1469  -2142    172       C  
ATOM   1726  O   GLU A 237       6.201   7.089  27.822  1.00 55.77           O  
ANISOU 1726  O   GLU A 237    10903   4134   6151  -1503  -2367    184       O  
ATOM   1727  CB  GLU A 237       6.646   6.539  24.602  1.00 46.10           C  
ANISOU 1727  CB  GLU A 237     8956   3310   5250  -1985  -2118    366       C  
ATOM   1728  CG  GLU A 237       7.515   7.775  24.805  1.00 60.27           C  
ANISOU 1728  CG  GLU A 237    10916   5037   6947  -2223  -2400    472       C  
ATOM   1729  CD  GLU A 237       6.753   9.063  24.608  1.00 99.70           C  
ANISOU 1729  CD  GLU A 237    16257   9840  11785  -2125  -2472    481       C  
ATOM   1730  OE1 GLU A 237       5.652   9.008  24.020  1.00 96.43           O  
ANISOU 1730  OE1 GLU A 237    15868   9403  11369  -1925  -2288    427       O  
ATOM   1731  OE2 GLU A 237       7.244  10.122  25.059  1.00103.89           O1-
ANISOU 1731  OE2 GLU A 237    17043  10240  12189  -2240  -2726    543       O1-
ATOM   1732  N   ARG A 238       4.379   6.198  26.837  1.00 51.47           N  
ANISOU 1732  N   ARG A 238    10197   3672   5688  -1165  -1924     94       N  
ATOM   1733  CA  ARG A 238       3.453   6.887  27.730  1.00 51.38           C  
ANISOU 1733  CA  ARG A 238    10534   3509   5478   -859  -1934     18       C  
ATOM   1734  C   ARG A 238       3.563   6.364  29.159  1.00 51.02           C  
ANISOU 1734  C   ARG A 238    10614   3425   5348   -691  -1956    -53       C  
ATOM   1735  O   ARG A 238       3.402   7.136  30.114  1.00 51.50           O  
ANISOU 1735  O   ARG A 238    10996   3354   5217   -553  -2090    -86       O  
ATOM   1736  CB  ARG A 238       2.020   6.732  27.200  1.00 52.80           C  
ANISOU 1736  CB  ARG A 238    10694   3715   5650   -586  -1680    -32       C  
ATOM   1737  CG  ARG A 238       0.926   7.164  28.171  1.00 54.52           C  
ANISOU 1737  CG  ARG A 238    11202   3846   5668   -219  -1625   -120       C  
ATOM   1738  CD  ARG A 238      -0.376   7.489  27.446  1.00 49.14           C  
ANISOU 1738  CD  ARG A 238    10532   3180   4960     -3  -1458   -142       C  
ATOM   1739  NE  ARG A 238      -0.719   6.462  26.460  1.00 47.91           N  
ANISOU 1739  NE  ARG A 238    10046   3164   4994    -39  -1233   -117       N  
ATOM   1740  CZ  ARG A 238      -1.566   5.468  26.682  1.00 52.93           C  
ANISOU 1740  CZ  ARG A 238    10552   3896   5662    181   -989   -157       C  
ATOM   1741  NH1 ARG A 238      -2.078   5.257  27.882  1.00 47.48           N1+
ANISOU 1741  NH1 ARG A 238     9998   3206   4837    434   -919   -217       N1+
ATOM   1742  NH2 ARG A 238      -1.869   4.632  25.688  1.00 45.34           N  
ANISOU 1742  NH2 ARG A 238     9323   3042   4862    131   -815   -124       N  
ATOM   1743  N   VAL A 239       3.870   5.077  29.341  1.00 47.48           N  
ANISOU 1743  N   VAL A 239     9780   2930   5332   -614   -385   -641       N  
ATOM   1744  CA  VAL A 239       3.995   4.533  30.697  1.00 50.12           C  
ANISOU 1744  CA  VAL A 239    10280   3285   5480   -616   -473   -720       C  
ATOM   1745  C   VAL A 239       5.441   4.517  31.179  1.00 57.56           C  
ANISOU 1745  C   VAL A 239    11222   4243   6405   -891   -772   -776       C  
ATOM   1746  O   VAL A 239       5.740   3.903  32.214  1.00 57.08           O  
ANISOU 1746  O   VAL A 239    11264   4223   6200   -918   -906   -823       O  
ATOM   1747  CB  VAL A 239       3.359   3.145  30.825  1.00 55.11           C  
ANISOU 1747  CB  VAL A 239    10780   4060   6098   -466   -398   -689       C  
ATOM   1748  CG1 VAL A 239       1.876   3.211  30.477  1.00 48.96           C  
ANISOU 1748  CG1 VAL A 239     9998   3268   5336   -198   -104   -633       C  
ATOM   1749  CG2 VAL A 239       4.108   2.121  29.984  1.00 44.98           C  
ANISOU 1749  CG2 VAL A 239     9172   2930   4988   -585   -542   -644       C  
ATOM   1750  N   GLY A 240       6.338   5.203  30.476  1.00 53.09           N  
ANISOU 1750  N   GLY A 240    10548   3644   5978  -1097   -881   -762       N  
ATOM   1751  CA  GLY A 240       7.715   5.326  30.918  1.00 57.66           C  
ANISOU 1751  CA  GLY A 240    11100   4241   6566  -1374  -1164   -809       C  
ATOM   1752  C   GLY A 240       8.534   4.060  30.774  1.00 54.74           C  
ANISOU 1752  C   GLY A 240    10428   4067   6304  -1469  -1359   -783       C  
ATOM   1753  O   GLY A 240       9.506   3.872  31.509  1.00 54.28           O  
ANISOU 1753  O   GLY A 240    10367   4053   6205  -1636  -1618   -823       O  
ATOM   1754  N   LEU A 241       8.184   3.198  29.828  1.00 47.37           N  
ANISOU 1754  N   LEU A 241     9239   3248   5510  -1366  -1252   -712       N  
ATOM   1755  CA  LEU A 241       8.896   1.939  29.629  1.00 47.92           C  
ANISOU 1755  CA  LEU A 241     9026   3488   5691  -1428  -1416   -685       C  
ATOM   1756  C   LEU A 241       9.380   1.893  28.181  1.00 52.09           C  
ANISOU 1756  C   LEU A 241     9231   4093   6467  -1536  -1374   -608       C  
ATOM   1757  O   LEU A 241       9.437   2.946  27.532  1.00 49.84           O  
ANISOU 1757  O   LEU A 241     8967   3722   6246  -1622  -1280   -582       O  
ATOM   1758  CB  LEU A 241       7.987   0.746  29.974  1.00 51.03           C  
ANISOU 1758  CB  LEU A 241     9455   3941   5992  -1196  -1320   -677       C  
ATOM   1759  CG  LEU A 241       7.552   0.682  31.454  1.00 51.65           C  
ANISOU 1759  CG  LEU A 241     9862   3956   5808  -1099  -1347   -738       C  
ATOM   1760  CD1 LEU A 241       6.497  -0.417  31.685  1.00 44.12           C  
ANISOU 1760  CD1 LEU A 241     8945   3048   4772   -869  -1181   -714       C  
ATOM   1761  CD2 LEU A 241       8.761   0.484  32.348  1.00 51.92           C  
ANISOU 1761  CD2 LEU A 241     9919   4029   5779  -1277  -1681   -776       C  
ATOM   1762  N   THR A 242       9.762   0.716  27.686  1.00 47.89           N  
ANISOU 1762  N   THR A 242     8408   3722   6066  -1530  -1432   -563       N  
ATOM   1763  CA  THR A 242      10.125   0.471  26.295  1.00 50.65           C  
ANISOU 1763  CA  THR A 242     8391   4230   6624  -1556  -1316   -466       C  
ATOM   1764  C   THR A 242       9.369  -0.755  25.818  1.00 47.87           C  
ANISOU 1764  C   THR A 242     7869   4040   6281  -1309  -1150   -414       C  
ATOM   1765  O   THR A 242       8.785  -1.486  26.625  1.00 45.57           O  
ANISOU 1765  O   THR A 242     7692   3756   5865  -1156  -1159   -444       O  
ATOM   1766  CB  THR A 242      11.643   0.251  26.125  1.00 50.92           C  
ANISOU 1766  CB  THR A 242     8096   4413   6839  -1770  -1515   -442       C  
ATOM   1767  CG2 THR A 242      12.451   1.225  26.988  1.00 52.79           C  
ANISOU 1767  CG2 THR A 242     8510   4507   7041  -2043  -1771   -513       C  
ATOM   1768  OG1 THR A 242      11.982  -1.098  26.478  1.00 51.76           O  
ANISOU 1768  OG1 THR A 242     7984   4708   6974  -1645  -1612   -426       O  
ATOM   1769  N   PRO A 243       9.342  -1.021  24.499  1.00 42.35           N  
ANISOU 1769  N   PRO A 243     6917   3464   5711  -1279   -991   -337       N  
ATOM   1770  CA  PRO A 243       8.670  -2.241  24.036  1.00 41.67           C  
ANISOU 1770  CA  PRO A 243     6685   3523   5626  -1077   -858   -302       C  
ATOM   1771  C   PRO A 243       9.261  -3.512  24.611  1.00 38.65           C  
ANISOU 1771  C   PRO A 243     6148   3267   5271  -1023   -985   -316       C  
ATOM   1772  O   PRO A 243       8.576  -4.539  24.633  1.00 38.03           O  
ANISOU 1772  O   PRO A 243     6054   3248   5146   -857   -900   -308       O  
ATOM   1773  CB  PRO A 243       8.830  -2.181  22.507  1.00 43.98           C  
ANISOU 1773  CB  PRO A 243     6756   3915   6038  -1109   -705   -229       C  
ATOM   1774  CG  PRO A 243       8.866  -0.694  22.227  1.00 43.02           C  
ANISOU 1774  CG  PRO A 243     6798   3633   5914  -1249   -680   -210       C  
ATOM   1775  CD  PRO A 243       9.691  -0.135  23.366  1.00 46.75           C  
ANISOU 1775  CD  PRO A 243     7390   3997   6376  -1418   -896   -278       C  
ATOM   1776  N   GLU A 244      10.496  -3.477  25.109  1.00 44.60           N  
ANISOU 1776  N   GLU A 244     6790   4057   6099  -1160  -1197   -330       N  
ATOM   1777  CA  GLU A 244      11.064  -4.693  25.678  1.00 44.60           C  
ANISOU 1777  CA  GLU A 244     6646   4171   6128  -1074  -1333   -323       C  
ATOM   1778  C   GLU A 244      10.355  -5.106  26.967  1.00 44.37           C  
ANISOU 1778  C   GLU A 244     6911   4052   5897   -957  -1408   -363       C  
ATOM   1779  O   GLU A 244      10.433  -6.280  27.363  1.00 43.75           O  
ANISOU 1779  O   GLU A 244     6777   4042   5805   -828  -1457   -341       O  
ATOM   1780  CB  GLU A 244      12.568  -4.482  25.906  1.00 51.07           C  
ANISOU 1780  CB  GLU A 244     7241   5070   7093  -1247  -1567   -312       C  
ATOM   1781  CG  GLU A 244      13.266  -5.694  26.465  1.00 64.78           C  
ANISOU 1781  CG  GLU A 244     8800   6931   8884  -1136  -1732   -284       C  
ATOM   1782  CD  GLU A 244      13.552  -6.724  25.386  1.00 70.58           C  
ANISOU 1782  CD  GLU A 244     9214   7817   9786   -999  -1560   -228       C  
ATOM   1783  OE1 GLU A 244      13.453  -6.373  24.181  1.00 63.75           O  
ANISOU 1783  OE1 GLU A 244     8231   6986   9006  -1043  -1346   -212       O  
ATOM   1784  OE2 GLU A 244      13.847  -7.887  25.745  1.00 86.29           O1-
ANISOU 1784  OE2 GLU A 244    11108   9875  11804   -838  -1630   -200       O1-
ATOM   1785  N   ASP A 245       9.665  -4.166  27.621  1.00 43.88           N  
ANISOU 1785  N   ASP A 245     7180   3821   5670   -992  -1398   -417       N  
ATOM   1786  CA  ASP A 245       8.846  -4.411  28.805  1.00 42.69           C  
ANISOU 1786  CA  ASP A 245     7354   3569   5298   -879  -1403   -457       C  
ATOM   1787  C   ASP A 245       7.451  -4.921  28.483  1.00 40.39           C  
ANISOU 1787  C   ASP A 245     7120   3276   4950   -693  -1133   -432       C  
ATOM   1788  O   ASP A 245       6.623  -5.025  29.392  1.00 43.27           O  
ANISOU 1788  O   ASP A 245     7752   3554   5137   -598  -1073   -456       O  
ATOM   1789  CB  ASP A 245       8.743  -3.127  29.636  1.00 44.89           C  
ANISOU 1789  CB  ASP A 245     7983   3653   5418   -992  -1484   -538       C  
ATOM   1790  CG  ASP A 245      10.092  -2.587  29.998  1.00 54.74           C  
ANISOU 1790  CG  ASP A 245     9184   4899   6718  -1222  -1781   -569       C  
ATOM   1791  OD1 ASP A 245      10.787  -3.314  30.733  1.00 54.41           O  
ANISOU 1791  OD1 ASP A 245     9089   4938   6645  -1226  -2009   -560       O  
ATOM   1792  OD2 ASP A 245      10.460  -1.462  29.587  1.00 50.38           O1-
ANISOU 1792  OD2 ASP A 245     8648   4261   6234  -1402  -1800   -593       O1-
ATOM   1793  N   ALA A 246       7.166  -5.235  27.227  1.00 38.38           N  
ANISOU 1793  N   ALA A 246     6626   3122   4836   -650   -970   -382       N  
ATOM   1794  CA  ALA A 246       5.838  -5.649  26.809  1.00 35.99           C  
ANISOU 1794  CA  ALA A 246     6341   2836   4499   -509   -741   -353       C  
ATOM   1795  C   ALA A 246       5.822  -7.107  26.377  1.00 37.92           C  
ANISOU 1795  C   ALA A 246     6390   3207   4811   -429   -698   -316       C  
ATOM   1796  O   ALA A 246       6.823  -7.636  25.877  1.00 37.11           O  
ANISOU 1796  O   ALA A 246     6073   3196   4832   -465   -782   -301       O  
ATOM   1797  CB  ALA A 246       5.338  -4.780  25.645  1.00 38.55           C  
ANISOU 1797  CB  ALA A 246     6595   3156   4896   -525   -594   -325       C  
ATOM   1798  N   ILE A 247       4.671  -7.758  26.587  1.00 35.10           N  
ANISOU 1798  N   ILE A 247     6113   2847   4378   -321   -554   -300       N  
ATOM   1799  CA  ILE A 247       4.355  -9.041  25.968  1.00 32.58           C  
ANISOU 1799  CA  ILE A 247     5641   2619   4121   -264   -467   -268       C  
ATOM   1800  C   ILE A 247       3.237  -8.762  24.965  1.00 34.37           C  
ANISOU 1800  C   ILE A 247     5790   2891   4378   -247   -289   -245       C  
ATOM   1801  O   ILE A 247       2.287  -8.025  25.269  1.00 36.03           O  
ANISOU 1801  O   ILE A 247     6118   3050   4521   -208   -195   -237       O  
ATOM   1802  CB  ILE A 247       3.983 -10.119  27.016  1.00 33.81           C  
ANISOU 1802  CB  ILE A 247     5942   2732   4172   -190   -465   -256       C  
ATOM   1803  CG1 ILE A 247       3.626 -11.450  26.343  1.00 34.28           C  
ANISOU 1803  CG1 ILE A 247     5877   2851   4299   -154   -369   -230       C  
ATOM   1804  CG2 ILE A 247       2.842  -9.684  27.974  1.00 31.97           C  
ANISOU 1804  CG2 ILE A 247     5951   2414   3783   -144   -351   -256       C  
ATOM   1805  CD1 ILE A 247       3.759 -12.651  27.333  1.00 37.04           C  
ANISOU 1805  CD1 ILE A 247     6362   3138   4572    -94   -417   -204       C  
ATOM   1806  N   ALA A 248       3.414  -9.243  23.733  1.00 32.51           N  
ANISOU 1806  N   ALA A 248     5359   2753   4240   -271   -250   -233       N  
ATOM   1807  CA  ALA A 248       2.472  -9.021  22.647  1.00 33.84           C  
ANISOU 1807  CA  ALA A 248     5441   2987   4428   -270   -128   -203       C  
ATOM   1808  C   ALA A 248       1.972 -10.378  22.188  1.00 33.33           C  
ANISOU 1808  C   ALA A 248     5300   2987   4376   -260    -66   -204       C  
ATOM   1809  O   ALA A 248       2.749 -11.335  22.120  1.00 35.78           O  
ANISOU 1809  O   ALA A 248     5570   3303   4724   -262   -107   -230       O  
ATOM   1810  CB  ALA A 248       3.125  -8.301  21.461  1.00 34.29           C  
ANISOU 1810  CB  ALA A 248     5381   3093   4555   -336   -138   -191       C  
ATOM   1811  N   VAL A 249       0.688 -10.478  21.850  1.00 34.86           N  
ANISOU 1811  N   VAL A 249     5469   3226   4549   -251     30   -174       N  
ATOM   1812  CA  VAL A 249       0.145 -11.775  21.446  1.00 32.72           C  
ANISOU 1812  CA  VAL A 249     5147   3001   4285   -282     77   -182       C  
ATOM   1813  C   VAL A 249      -0.824 -11.569  20.297  1.00 33.02           C  
ANISOU 1813  C   VAL A 249     5068   3145   4331   -322    122   -152       C  
ATOM   1814  O   VAL A 249      -1.644 -10.643  20.308  1.00 32.38           O  
ANISOU 1814  O   VAL A 249     4963   3094   4245   -284    154    -99       O  
ATOM   1815  CB  VAL A 249      -0.537 -12.509  22.624  1.00 32.53           C  
ANISOU 1815  CB  VAL A 249     5230   2916   4215   -260    130   -169       C  
ATOM   1816  CG1 VAL A 249      -1.714 -11.660  23.183  1.00 33.25           C  
ANISOU 1816  CG1 VAL A 249     5345   3016   4273   -214    223   -120       C  
ATOM   1817  CG2 VAL A 249      -0.987 -13.969  22.192  1.00 33.58           C  
ANISOU 1817  CG2 VAL A 249     5333   3063   4364   -328    173   -182       C  
ATOM   1818  N   GLY A 250      -0.717 -12.431  19.289  1.00 32.47           N  
ANISOU 1818  N   GLY A 250     4941   3130   4268   -390    117   -185       N  
ATOM   1819  CA  GLY A 250      -1.702 -12.412  18.229  1.00 31.38           C  
ANISOU 1819  CA  GLY A 250     4710   3101   4113   -450    123   -159       C  
ATOM   1820  C   GLY A 250      -1.617 -13.701  17.444  1.00 33.88           C  
ANISOU 1820  C   GLY A 250     5034   3431   4407   -544    121   -224       C  
ATOM   1821  O   GLY A 250      -0.834 -14.602  17.759  1.00 35.71           O  
ANISOU 1821  O   GLY A 250     5343   3574   4650   -535    135   -282       O  
ATOM   1822  N   ASP A 251      -2.457 -13.781  16.419  1.00 32.41           N  
ANISOU 1822  N   ASP A 251     4782   3350   4182   -627     93   -212       N  
ATOM   1823  CA  ASP A 251      -2.629 -15.011  15.649  1.00 31.58           C  
ANISOU 1823  CA  ASP A 251     4718   3248   4031   -747     82   -285       C  
ATOM   1824  C   ASP A 251      -2.305 -14.854  14.174  1.00 34.50           C  
ANISOU 1824  C   ASP A 251     5105   3693   4312   -797     47   -318       C  
ATOM   1825  O   ASP A 251      -2.241 -15.877  13.462  1.00 37.27           O  
ANISOU 1825  O   ASP A 251     5543   4020   4596   -891     49   -405       O  
ATOM   1826  CB  ASP A 251      -4.078 -15.501  15.757  1.00 35.51           C  
ANISOU 1826  CB  ASP A 251     5141   3811   4542   -860     59   -252       C  
ATOM   1827  CG  ASP A 251      -5.048 -14.607  14.970  1.00 39.61           C  
ANISOU 1827  CG  ASP A 251     5510   4498   5042   -882    -22   -170       C  
ATOM   1828  OD1 ASP A 251      -5.213 -13.419  15.327  1.00 35.41           O  
ANISOU 1828  OD1 ASP A 251     4905   4002   4548   -758    -12    -83       O  
ATOM   1829  OD2 ASP A 251      -5.615 -15.076  13.964  1.00 40.16           O1-
ANISOU 1829  OD2 ASP A 251     5554   4655   5049  -1017   -107   -192       O1-
ATOM   1830  N   GLY A 252      -2.168 -13.618  13.672  1.00 34.32           N  
ANISOU 1830  N   GLY A 252     5031   3745   4265   -744     22   -250       N  
ATOM   1831  CA  GLY A 252      -2.215 -13.362  12.248  1.00 35.20           C  
ANISOU 1831  CA  GLY A 252     5165   3951   4259   -804    -21   -248       C  
ATOM   1832  C   GLY A 252      -0.967 -12.650  11.753  1.00 33.58           C  
ANISOU 1832  C   GLY A 252     5008   3725   4028   -745     44   -245       C  
ATOM   1833  O   GLY A 252      -0.162 -12.129  12.540  1.00 36.46           O  
ANISOU 1833  O   GLY A 252     5350   4018   4485   -663     92   -228       O  
ATOM   1834  N   ALA A 253      -0.818 -12.635  10.424  1.00 35.37           N  
ANISOU 1834  N   ALA A 253     5306   4017   4115   -805     42   -259       N  
ATOM   1835  CA  ALA A 253       0.334 -11.968   9.814  1.00 36.89           C  
ANISOU 1835  CA  ALA A 253     5542   4203   4273   -772    134   -244       C  
ATOM   1836  C   ALA A 253       0.409 -10.509  10.243  1.00 38.23           C  
ANISOU 1836  C   ALA A 253     5648   4365   4513   -706    118   -122       C  
ATOM   1837  O   ALA A 253       1.506  -9.976  10.481  1.00 36.69           O  
ANISOU 1837  O   ALA A 253     5440   4114   4385   -676    198   -113       O  
ATOM   1838  CB  ALA A 253       0.260 -12.080   8.289  1.00 39.08           C  
ANISOU 1838  CB  ALA A 253     5940   4561   4348   -852    137   -260       C  
ATOM   1839  N   ASN A 254      -0.749  -9.849  10.369  1.00 37.02           N  
ANISOU 1839  N   ASN A 254     5451   4261   4356   -682     15    -26       N  
ATOM   1840  CA  ASN A 254      -0.747  -8.433  10.734  1.00 38.91           C  
ANISOU 1840  CA  ASN A 254     5674   4458   4650   -603      9     88       C  
ATOM   1841  C   ASN A 254      -0.350  -8.203  12.188  1.00 38.77           C  
ANISOU 1841  C   ASN A 254     5624   4327   4780   -539     45     66       C  
ATOM   1842  O   ASN A 254      -0.214  -7.041  12.591  1.00 38.03           O  
ANISOU 1842  O   ASN A 254     5557   4161   4730   -485     50    136       O  
ATOM   1843  CB  ASN A 254      -2.107  -7.784  10.413  1.00 40.60           C  
ANISOU 1843  CB  ASN A 254     5848   4753   4825   -556   -101    208       C  
ATOM   1844  CG  ASN A 254      -3.231  -8.158  11.391  1.00 43.54           C  
ANISOU 1844  CG  ASN A 254     6099   5147   5296   -509   -146    211       C  
ATOM   1845  ND2 ASN A 254      -4.415  -7.570  11.166  1.00 47.21           N  
ANISOU 1845  ND2 ASN A 254     6478   5698   5761   -442   -234    328       N  
ATOM   1846  OD1 ASN A 254      -3.058  -8.949  12.326  1.00 49.58           O  
ANISOU 1846  OD1 ASN A 254     6842   5858   6138   -523    -98    124       O  
ATOM   1847  N   ASP A 255      -0.149  -9.259  12.978  1.00 32.91           N  
ANISOU 1847  N   ASP A 255     4857   3549   4096   -546     64    -29       N  
ATOM   1848  CA  ASP A 255       0.355  -9.098  14.341  1.00 34.05           C  
ANISOU 1848  CA  ASP A 255     5004   3588   4345   -493     80    -52       C  
ATOM   1849  C   ASP A 255       1.862  -9.216  14.435  1.00 38.43           C  
ANISOU 1849  C   ASP A 255     5560   4093   4951   -515    121   -104       C  
ATOM   1850  O   ASP A 255       2.415  -8.939  15.498  1.00 31.89           O  
ANISOU 1850  O   ASP A 255     4735   3183   4197   -486    100   -115       O  
ATOM   1851  CB  ASP A 255      -0.246 -10.143  15.276  1.00 31.89           C  
ANISOU 1851  CB  ASP A 255     4718   3294   4105   -479     72   -101       C  
ATOM   1852  CG  ASP A 255      -1.730 -10.038  15.349  1.00 34.88           C  
ANISOU 1852  CG  ASP A 255     5045   3736   4472   -463     46    -41       C  
ATOM   1853  OD1 ASP A 255      -2.195  -8.898  15.559  1.00 37.03           O  
ANISOU 1853  OD1 ASP A 255     5309   4001   4760   -386     42     40       O  
ATOM   1854  OD2 ASP A 255      -2.438 -11.065  15.171  1.00 34.70           O1-
ANISOU 1854  OD2 ASP A 255     4984   3767   4432   -527     33    -71       O1-
ATOM   1855  N   LEU A 256       2.531  -9.637  13.360  1.00 34.27           N  
ANISOU 1855  N   LEU A 256     5023   3617   4380   -563    180   -136       N  
ATOM   1856  CA  LEU A 256       3.952  -9.977  13.460  1.00 33.15           C  
ANISOU 1856  CA  LEU A 256     4830   3450   4315   -564    241   -186       C  
ATOM   1857  C   LEU A 256       4.821  -8.764  13.768  1.00 34.66           C  
ANISOU 1857  C   LEU A 256     4982   3604   4584   -592    237   -130       C  
ATOM   1858  O   LEU A 256       5.902  -8.910  14.363  1.00 35.11           O  
ANISOU 1858  O   LEU A 256     4956   3634   4748   -590    232   -158       O  
ATOM   1859  CB  LEU A 256       4.401 -10.671  12.178  1.00 33.68           C  
ANISOU 1859  CB  LEU A 256     4910   3580   4307   -593    347   -234       C  
ATOM   1860  CG  LEU A 256       3.897 -12.120  12.102  1.00 33.59           C  
ANISOU 1860  CG  LEU A 256     4957   3559   4248   -576    351   -326       C  
ATOM   1861  CD1 LEU A 256       4.206 -12.728  10.725  1.00 35.26           C  
ANISOU 1861  CD1 LEU A 256     5243   3816   4338   -610    464   -387       C  
ATOM   1862  CD2 LEU A 256       4.481 -12.989  13.224  1.00 37.97           C  
ANISOU 1862  CD2 LEU A 256     5474   4029   4923   -499    343   -379       C  
ATOM   1863  N   GLY A 257       4.399  -7.562  13.377  1.00 35.30           N  
ANISOU 1863  N   GLY A 257     5120   3674   4618   -625    228    -46       N  
ATOM   1864  CA  GLY A 257       5.182  -6.387  13.731  1.00 36.97           C  
ANISOU 1864  CA  GLY A 257     5330   3814   4904   -681    219      3       C  
ATOM   1865  C   GLY A 257       5.273  -6.174  15.234  1.00 36.77           C  
ANISOU 1865  C   GLY A 257     5321   3692   4958   -655    119    -27       C  
ATOM   1866  O   GLY A 257       6.362  -5.979  15.788  1.00 38.45           O  
ANISOU 1866  O   GLY A 257     5471   3872   5266   -712     83    -47       O  
ATOM   1867  N   MET A 258       4.127  -6.167  15.917  1.00 35.26           N  
ANISOU 1867  N   MET A 258     5215   3459   4723   -574     71    -25       N  
ATOM   1868  CA  MET A 258       4.175  -5.992  17.367  1.00 34.81           C  
ANISOU 1868  CA  MET A 258     5222   3302   4701   -544     -7    -60       C  
ATOM   1869  C   MET A 258       4.760  -7.211  18.056  1.00 35.73           C  
ANISOU 1869  C   MET A 258     5272   3443   4861   -522    -49   -130       C  
ATOM   1870  O   MET A 258       5.472  -7.072  19.059  1.00 36.94           O  
ANISOU 1870  O   MET A 258     5443   3535   5057   -540   -138   -156       O  
ATOM   1871  CB  MET A 258       2.788  -5.662  17.913  1.00 33.52           C  
ANISOU 1871  CB  MET A 258     5167   3092   4479   -447     -2    -33       C  
ATOM   1872  CG  MET A 258       1.788  -6.797  17.905  1.00 36.75           C  
ANISOU 1872  CG  MET A 258     5526   3583   4854   -384     25    -49       C  
ATOM   1873  SD  MET A 258       0.251  -6.258  18.714  1.00 34.64           S  
ANISOU 1873  SD  MET A 258     5340   3268   4552   -265     60     -3       S  
ATOM   1874  CE  MET A 258      -0.679  -7.808  18.694  1.00 35.57           C  
ANISOU 1874  CE  MET A 258     5358   3498   4661   -261     88    -25       C  
ATOM   1875  N   ILE A 259       4.502  -8.405  17.518  1.00 32.96           N  
ANISOU 1875  N   ILE A 259     4862   3169   4494   -488      2   -158       N  
ATOM   1876  CA  ILE A 259       5.090  -9.614  18.085  1.00 31.70           C  
ANISOU 1876  CA  ILE A 259     4659   3007   4379   -446    -26   -213       C  
ATOM   1877  C   ILE A 259       6.608  -9.531  18.043  1.00 40.04           C  
ANISOU 1877  C   ILE A 259     5589   4083   5541   -478    -54   -221       C  
ATOM   1878  O   ILE A 259       7.293  -9.847  19.025  1.00 35.55           O  
ANISOU 1878  O   ILE A 259     4995   3482   5030   -449   -154   -236       O  
ATOM   1879  CB  ILE A 259       4.552 -10.851  17.339  1.00 30.95           C  
ANISOU 1879  CB  ILE A 259     4556   2962   4242   -420     50   -248       C  
ATOM   1880  CG1 ILE A 259       3.137 -11.180  17.865  1.00 33.23           C  
ANISOU 1880  CG1 ILE A 259     4934   3228   4464   -397     43   -240       C  
ATOM   1881  CG2 ILE A 259       5.475 -12.078  17.507  1.00 35.66           C  
ANISOU 1881  CG2 ILE A 259     5103   3544   4902   -364     58   -300       C  
ATOM   1882  CD1 ILE A 259       2.421 -12.244  17.044  1.00 36.51           C  
ANISOU 1882  CD1 ILE A 259     5353   3688   4829   -424     96   -272       C  
ATOM   1883  N   GLN A 260       7.158  -9.070  16.921  1.00 35.12           N  
ANISOU 1883  N   GLN A 260     4878   3522   4944   -543     31   -198       N  
ATOM   1884  CA  GLN A 260       8.612  -9.045  16.809  1.00 35.05           C  
ANISOU 1884  CA  GLN A 260     4698   3558   5063   -579     36   -196       C  
ATOM   1885  C   GLN A 260       9.240  -7.911  17.613  1.00 38.40           C  
ANISOU 1885  C   GLN A 260     5103   3932   5556   -680    -89   -165       C  
ATOM   1886  O   GLN A 260      10.363  -8.067  18.101  1.00 41.85           O  
ANISOU 1886  O   GLN A 260     5388   4400   6115   -699   -170   -168       O  
ATOM   1887  CB  GLN A 260       9.016  -8.984  15.330  1.00 38.80           C  
ANISOU 1887  CB  GLN A 260     5092   4117   5532   -622    206   -179       C  
ATOM   1888  CG  GLN A 260       8.783 -10.348  14.649  1.00 37.29           C  
ANISOU 1888  CG  GLN A 260     4916   3965   5288   -522    316   -240       C  
ATOM   1889  CD  GLN A 260       8.811 -10.287  13.127  1.00 44.21           C  
ANISOU 1889  CD  GLN A 260     5810   4912   6077   -564    491   -235       C  
ATOM   1890  NE2 GLN A 260       8.494 -11.407  12.487  1.00 43.33           N  
ANISOU 1890  NE2 GLN A 260     5769   4811   5882   -497    580   -304       N  
ATOM   1891  OE1 GLN A 260       9.151  -9.263  12.541  1.00 45.82           O  
ANISOU 1891  OE1 GLN A 260     5988   5145   6276   -661    548   -172       O  
ATOM   1892  N   LEU A 261       8.539  -6.777  17.778  1.00 34.35           N  
ANISOU 1892  N   LEU A 261     4746   3337   4970   -742   -116   -136       N  
ATOM   1893  CA  LEU A 261       9.102  -5.637  18.502  1.00 36.07           C  
ANISOU 1893  CA  LEU A 261     5002   3471   5234   -862   -232   -122       C  
ATOM   1894  C   LEU A 261       9.083  -5.865  20.012  1.00 36.81           C  
ANISOU 1894  C   LEU A 261     5188   3493   5305   -822   -404   -168       C  
ATOM   1895  O   LEU A 261      10.017  -5.465  20.715  1.00 39.64           O  
ANISOU 1895  O   LEU A 261     5501   3829   5731   -920   -550   -178       O  
ATOM   1896  CB  LEU A 261       8.330  -4.365  18.158  1.00 35.52           C  
ANISOU 1896  CB  LEU A 261     5112   3300   5083   -914   -185    -77       C  
ATOM   1897  CG  LEU A 261       8.891  -3.103  18.816  1.00 42.27           C  
ANISOU 1897  CG  LEU A 261     6060   4027   5974  -1063   -289    -72       C  
ATOM   1898  CD1 LEU A 261      10.352  -2.865  18.397  1.00 47.27           C  
ANISOU 1898  CD1 LEU A 261     6477   4728   6754  -1237   -299    -46       C  
ATOM   1899  CD2 LEU A 261       8.023  -1.902  18.484  1.00 42.83           C  
ANISOU 1899  CD2 LEU A 261     6351   3963   5961  -1070   -224    -22       C  
ATOM   1900  N   ALA A 262       8.039  -6.516  20.514  1.00 38.57           N  
ANISOU 1900  N   ALA A 262     5542   3686   5426   -693   -393   -192       N  
ATOM   1901  CA  ALA A 262       7.865  -6.693  21.948  1.00 38.75           C  
ANISOU 1901  CA  ALA A 262     5712   3629   5382   -648   -526   -227       C  
ATOM   1902  C   ALA A 262       8.984  -7.550  22.525  1.00 42.34           C  
ANISOU 1902  C   ALA A 262     6030   4140   5917   -633   -664   -239       C  
ATOM   1903  O   ALA A 262       9.549  -8.410  21.843  1.00 38.78           O  
ANISOU 1903  O   ALA A 262     5381   3788   5564   -585   -608   -228       O  
ATOM   1904  CB  ALA A 262       6.508  -7.345  22.218  1.00 34.38           C  
ANISOU 1904  CB  ALA A 262     5292   3052   4718   -520   -438   -234       C  
ATOM   1905  N   GLY A 263       9.307  -7.308  23.801  1.00 40.28           N  
ANISOU 1905  N   GLY A 263     5890   3810   5606   -661   -848   -260       N  
ATOM   1906  CA  GLY A 263      10.288  -8.152  24.475  1.00 39.74           C  
ANISOU 1906  CA  GLY A 263     5706   3795   5597   -620  -1018   -253       C  
ATOM   1907  C   GLY A 263       9.907  -9.621  24.453  1.00 41.38           C  
ANISOU 1907  C   GLY A 263     5902   4031   5790   -446   -943   -242       C  
ATOM   1908  O   GLY A 263      10.765 -10.498  24.285  1.00 42.40           O  
ANISOU 1908  O   GLY A 263     5840   4234   6035   -371   -985   -219       O  
ATOM   1909  N   THR A 264       8.618  -9.914  24.625  1.00 34.93           N  
ANISOU 1909  N   THR A 264     5285   3145   4840   -377   -825   -253       N  
ATOM   1910  CA  THR A 264       8.098 -11.269  24.467  1.00 34.33           C  
ANISOU 1910  CA  THR A 264     5222   3074   4749   -252   -724   -245       C  
ATOM   1911  C   THR A 264       6.966 -11.222  23.452  1.00 38.38           C  
ANISOU 1911  C   THR A 264     5746   3603   5235   -262   -520   -254       C  
ATOM   1912  O   THR A 264       5.975 -10.508  23.649  1.00 38.33           O  
ANISOU 1912  O   THR A 264     5873   3554   5137   -289   -463   -255       O  
ATOM   1913  CB  THR A 264       7.612 -11.816  25.809  1.00 38.30           C  
ANISOU 1913  CB  THR A 264     5957   3483   5110   -182   -798   -234       C  
ATOM   1914  CG2 THR A 264       6.994 -13.241  25.654  1.00 35.53           C  
ANISOU 1914  CG2 THR A 264     5650   3106   4743    -79   -679   -218       C  
ATOM   1915  OG1 THR A 264       8.725 -11.867  26.711  1.00 41.16           O  
ANISOU 1915  OG1 THR A 264     6309   3844   5485   -172  -1029   -215       O  
ATOM   1916  N   GLY A 265       7.132 -11.933  22.347  1.00 36.72           N  
ANISOU 1916  N   GLY A 265     5395   3456   5100   -236   -414   -262       N  
ATOM   1917  CA  GLY A 265       6.112 -11.966  21.319  1.00 35.86           C  
ANISOU 1917  CA  GLY A 265     5296   3378   4952   -261   -258   -270       C  
ATOM   1918  C   GLY A 265       5.628 -13.377  21.094  1.00 35.69           C  
ANISOU 1918  C   GLY A 265     5313   3336   4910   -201   -181   -291       C  
ATOM   1919  O   GLY A 265       6.431 -14.291  20.862  1.00 35.27           O  
ANISOU 1919  O   GLY A 265     5196   3281   4926   -135   -176   -308       O  
ATOM   1920  N   VAL A 266       4.314 -13.570  21.172  1.00 32.28           N  
ANISOU 1920  N   VAL A 266     4985   2883   4396   -223   -115   -287       N  
ATOM   1921  CA  VAL A 266       3.707 -14.903  21.190  1.00 31.26           C  
ANISOU 1921  CA  VAL A 266     4934   2705   4238   -204    -54   -302       C  
ATOM   1922  C   VAL A 266       2.738 -15.019  20.025  1.00 32.82           C  
ANISOU 1922  C   VAL A 266     5098   2966   4407   -285     41   -322       C  
ATOM   1923  O   VAL A 266       1.786 -14.230  19.911  1.00 33.33           O  
ANISOU 1923  O   VAL A 266     5147   3083   4433   -332     60   -290       O  
ATOM   1924  CB  VAL A 266       2.977 -15.167  22.515  1.00 34.55           C  
ANISOU 1924  CB  VAL A 266     5505   3039   4582   -186    -67   -267       C  
ATOM   1925  CG1 VAL A 266       2.342 -16.579  22.503  1.00 34.15           C  
ANISOU 1925  CG1 VAL A 266     5545   2919   4511   -200      8   -274       C  
ATOM   1926  CG2 VAL A 266       3.940 -14.975  23.683  1.00 35.70           C  
ANISOU 1926  CG2 VAL A 266     5716   3129   4720   -115   -198   -246       C  
ATOM   1927  N   ALA A 267       2.967 -16.009  19.167  1.00 31.62           N  
ANISOU 1927  N   ALA A 267     4944   2804   4265   -293     95   -374       N  
ATOM   1928  CA  ALA A 267       1.980 -16.408  18.175  1.00 34.54           C  
ANISOU 1928  CA  ALA A 267     5328   3216   4579   -392    154   -404       C  
ATOM   1929  C   ALA A 267       1.072 -17.449  18.816  1.00 37.20           C  
ANISOU 1929  C   ALA A 267     5776   3467   4891   -437    174   -403       C  
ATOM   1930  O   ALA A 267       1.524 -18.551  19.154  1.00 35.38           O  
ANISOU 1930  O   ALA A 267     5651   3115   4677   -393    192   -432       O  
ATOM   1931  CB  ALA A 267       2.663 -16.975  16.927  1.00 34.77           C  
ANISOU 1931  CB  ALA A 267     5354   3255   4601   -393    213   -477       C  
ATOM   1932  N   LEU A 268      -0.205 -17.117  18.973  1.00 34.69           N  
ANISOU 1932  N   LEU A 268     5431   3206   4544   -521    182   -361       N  
ATOM   1933  CA  LEU A 268      -1.151 -17.990  19.666  1.00 33.93           C  
ANISOU 1933  CA  LEU A 268     5414   3041   4436   -592    223   -340       C  
ATOM   1934  C   LEU A 268      -2.023 -18.730  18.660  1.00 35.27           C  
ANISOU 1934  C   LEU A 268     5573   3244   4583   -752    237   -383       C  
ATOM   1935  O   LEU A 268      -2.833 -18.102  17.970  1.00 38.15           O  
ANISOU 1935  O   LEU A 268     5812   3749   4935   -828    208   -361       O  
ATOM   1936  CB  LEU A 268      -2.022 -17.161  20.619  1.00 35.42           C  
ANISOU 1936  CB  LEU A 268     5558   3278   4621   -578    248   -258       C  
ATOM   1937  CG  LEU A 268      -3.086 -17.941  21.395  1.00 39.98           C  
ANISOU 1937  CG  LEU A 268     6191   3806   5192   -662    328   -216       C  
ATOM   1938  CD1 LEU A 268      -2.424 -18.844  22.454  1.00 37.15           C  
ANISOU 1938  CD1 LEU A 268     6033   3275   4806   -603    345   -211       C  
ATOM   1939  CD2 LEU A 268      -4.115 -17.012  22.037  1.00 39.05           C  
ANISOU 1939  CD2 LEU A 268     5983   3777   5078   -643    393   -137       C  
ATOM   1940  N   HIS A 269      -1.920 -20.051  18.624  1.00 33.38           N  
ANISOU 1940  N   HIS A 269     5478   2870   4335   -809    268   -438       N  
ATOM   1941  CA  HIS A 269      -2.753 -20.879  17.753  1.00 38.49           C  
ANISOU 1941  CA  HIS A 269     6160   3515   4948  -1000    267   -494       C  
ATOM   1942  C   HIS A 269      -2.744 -20.369  16.335  1.00 45.33           C  
ANISOU 1942  C   HIS A 269     6950   4515   5757  -1049    211   -546       C  
ATOM   1943  O   HIS A 269      -3.765 -20.279  15.685  1.00 41.07           O  
ANISOU 1943  O   HIS A 269     6330   4088   5186  -1205    154   -541       O  
ATOM   1944  CB  HIS A 269      -4.159 -21.031  18.309  1.00 41.33           C  
ANISOU 1944  CB  HIS A 269     6451   3919   5334  -1153    286   -424       C  
ATOM   1945  CG  HIS A 269      -4.235 -21.844  19.562  1.00 43.46           C  
ANISOU 1945  CG  HIS A 269     6863   4023   5625  -1150    368   -381       C  
ATOM   1946  CD2 HIS A 269      -3.853 -21.573  20.829  1.00 48.39           C  
ANISOU 1946  CD2 HIS A 269     7545   4585   6255  -1007    412   -310       C  
ATOM   1947  ND1 HIS A 269      -4.774 -23.109  19.592  1.00 59.16           N  
ANISOU 1947  ND1 HIS A 269     8988   5877   7613  -1325    409   -405       N  
ATOM   1948  CE1 HIS A 269      -4.716 -23.585  20.821  1.00 55.45           C  
ANISOU 1948  CE1 HIS A 269     8652   5267   7150  -1279    489   -338       C  
ATOM   1949  NE2 HIS A 269      -4.158 -22.672  21.591  1.00 49.11           N  
ANISOU 1949  NE2 HIS A 269     7807   4512   6340  -1082    485   -280       N  
ATOM   1950  N   ALA A 270      -1.563 -20.035  15.871  1.00 39.53           N  
ANISOU 1950  N   ALA A 270     6237   3775   5009   -917    225   -587       N  
ATOM   1951  CA  ALA A 270      -1.428 -19.505  14.548  1.00 36.99           C  
ANISOU 1951  CA  ALA A 270     5876   3570   4609   -950    196   -625       C  
ATOM   1952  C   ALA A 270      -1.132 -20.558  13.519  1.00 40.48           C  
ANISOU 1952  C   ALA A 270     6495   3925   4961  -1021    233   -753       C  
ATOM   1953  O   ALA A 270      -0.637 -21.615  13.830  1.00 39.70           O  
ANISOU 1953  O   ALA A 270     6550   3651   4884   -981    301   -816       O  
ATOM   1954  CB  ALA A 270      -0.316 -18.492  14.540  1.00 36.61           C  
ANISOU 1954  CB  ALA A 270     5748   3569   4592   -790    219   -593       C  
ATOM   1955  N   LYS A 271      -1.446 -20.248  12.272  1.00 42.37           N  
ANISOU 1955  N   LYS A 271     6740   4278   5082  -1119    186   -789       N  
ATOM   1956  CA  LYS A 271      -1.048 -21.268  11.345  1.00 44.56           C  
ANISOU 1956  CA  LYS A 271     7236   4444   5248  -1170    244   -929       C  
ATOM   1957  C   LYS A 271       0.389 -21.131  10.947  1.00 42.27           C  
ANISOU 1957  C   LYS A 271     6990   4115   4954   -985    377   -974       C  
ATOM   1958  O   LYS A 271       1.088 -20.224  11.422  1.00 39.40           O  
ANISOU 1958  O   LYS A 271     6468   3818   4685   -842    402   -889       O  
ATOM   1959  CB  LYS A 271      -2.047 -21.411  10.224  1.00 64.00           C  
ANISOU 1959  CB  LYS A 271     9763   6998   7554  -1391    133   -979       C  
ATOM   1960  CG  LYS A 271      -2.494 -20.472   9.420  1.00 86.25           C  
ANISOU 1960  CG  LYS A 271    12486  10007  10278  -1446     33   -926       C  
ATOM   1961  CD  LYS A 271      -3.803 -21.205   9.704  1.00 75.06           C  
ANISOU 1961  CD  LYS A 271    11057   8582   8881  -1666    -85   -931       C  
ATOM   1962  CE  LYS A 271      -4.961 -21.035   8.805  1.00 86.47           C  
ANISOU 1962  CE  LYS A 271    12451  10192  10209  -1880   -275   -918       C  
ATOM   1963  NZ  LYS A 271      -5.793 -19.835   9.211  1.00 96.97           N1+
ANISOU 1963  NZ  LYS A 271    13472  11732  11641  -1841   -380   -742       N1+
ATOM   1964  N   PRO A 272       0.913 -22.234  10.400  1.00 45.35           N  
ANISOU 1964  N   PRO A 272     7604   4350   5278   -968    483  -1106       N  
ATOM   1965  CA  PRO A 272       2.366 -22.370  10.298  1.00 50.39           C  
ANISOU 1965  CA  PRO A 272     8260   4917   5969   -747    649  -1144       C  
ATOM   1966  C   PRO A 272       3.170 -21.205   9.769  1.00 44.06           C  
ANISOU 1966  C   PRO A 272     7300   4277   5164   -653    709  -1088       C  
ATOM   1967  O   PRO A 272       4.202 -20.935  10.321  1.00 45.44           O  
ANISOU 1967  O   PRO A 272     7339   4447   5480   -481    780  -1040       O  
ATOM   1968  CB  PRO A 272       2.530 -23.594   9.397  1.00 53.08           C  
ANISOU 1968  CB  PRO A 272     8901   5090   6176   -777    761  -1311       C  
ATOM   1969  CG  PRO A 272       1.332 -24.415   9.672  1.00 54.65           C  
ANISOU 1969  CG  PRO A 272     9243   5184   6338   -986    645  -1349       C  
ATOM   1970  CD  PRO A 272       0.219 -23.449   9.935  1.00 49.16           C  
ANISOU 1970  CD  PRO A 272     8334   4694   5652  -1143    464  -1229       C  
ATOM   1971  N   ALA A 273       2.711 -20.550   8.728  1.00 45.79           N  
ANISOU 1971  N   ALA A 273     7540   4635   5224   -774    671  -1087       N  
ATOM   1972  CA  ALA A 273       3.478 -19.481   8.132  1.00 47.35           C  
ANISOU 1972  CA  ALA A 273     7628   4964   5399   -706    752  -1030       C  
ATOM   1973  C   ALA A 273       3.640 -18.329   9.091  1.00 44.66           C  
ANISOU 1973  C   ALA A 273     7035   4711   5224   -647    676   -883       C  
ATOM   1974  O   ALA A 273       4.660 -17.670   9.095  1.00 46.89           O  
ANISOU 1974  O   ALA A 273     7192   5040   5586   -549    768   -834       O  
ATOM   1975  CB  ALA A 273       2.811 -19.003   6.873  1.00 51.86           C  
ANISOU 1975  CB  ALA A 273     8308   5656   5741   -856    698  -1036       C  
ATOM   1976  N   VAL A 274       2.622 -18.101   9.899  1.00 39.18           N  
ANISOU 1976  N   VAL A 274     6273   4033   4579   -717    519   -816       N  
ATOM   1977  CA  VAL A 274       2.697 -17.028  10.875  1.00 37.25           C  
ANISOU 1977  CA  VAL A 274     5840   3843   4470   -661    451   -694       C  
ATOM   1978  C   VAL A 274       3.506 -17.451  12.089  1.00 40.39           C  
ANISOU 1978  C   VAL A 274     6177   4134   5034   -528    479   -690       C  
ATOM   1979  O   VAL A 274       4.384 -16.715  12.549  1.00 38.43           O  
ANISOU 1979  O   VAL A 274     5795   3914   4891   -443    491   -632       O  
ATOM   1980  CB  VAL A 274       1.282 -16.570  11.271  1.00 38.58           C  
ANISOU 1980  CB  VAL A 274     5960   4076   4624   -760    302   -619       C  
ATOM   1981  CG1 VAL A 274       1.376 -15.526  12.341  1.00 36.13           C  
ANISOU 1981  CG1 VAL A 274     5507   3784   4436   -684    259   -513       C  
ATOM   1982  CG2 VAL A 274       0.553 -16.012  10.027  1.00 41.87           C  
ANISOU 1982  CG2 VAL A 274     6408   4623   4879   -870    239   -594       C  
ATOM   1983  N   ALA A 275       3.232 -18.639  12.632  1.00 39.15           N  
ANISOU 1983  N   ALA A 275     6128   3848   4900   -519    475   -746       N  
ATOM   1984  CA  ALA A 275       3.968 -19.070  13.820  1.00 38.43           C  
ANISOU 1984  CA  ALA A 275     6003   3652   4948   -379    477   -723       C  
ATOM   1985  C   ALA A 275       5.458 -19.169  13.537  1.00 43.28           C  
ANISOU 1985  C   ALA A 275     6545   4255   5643   -224    586   -746       C  
ATOM   1986  O   ALA A 275       6.275 -18.921  14.432  1.00 46.55           O  
ANISOU 1986  O   ALA A 275     6833   4665   6190   -110    547   -687       O  
ATOM   1987  CB  ALA A 275       3.431 -20.422  14.311  1.00 43.14           C  
ANISOU 1987  CB  ALA A 275     6771   4082   5536   -398    476   -773       C  
ATOM   1988  N   ALA A 276       5.824 -19.502  12.294  1.00 42.33           N  
ANISOU 1988  N   ALA A 276     6498   4144   5440   -222    724   -829       N  
ATOM   1989  CA  ALA A 276       7.226 -19.571  11.878  1.00 48.89           C  
ANISOU 1989  CA  ALA A 276     7234   4990   6354    -69    876   -848       C  
ATOM   1990  C   ALA A 276       7.956 -18.243  12.027  1.00 49.35           C  
ANISOU 1990  C   ALA A 276     7048   5194   6510    -64    856   -748       C  
ATOM   1991  O   ALA A 276       9.190 -18.224  12.051  1.00 50.81           O  
ANISOU 1991  O   ALA A 276     7073   5407   6827     62    949   -731       O  
ATOM   1992  CB  ALA A 276       7.333 -20.017  10.417  1.00 47.48           C  
ANISOU 1992  CB  ALA A 276     7213   4806   6021    -91   1054   -958       C  
ATOM   1993  N   GLN A 277       7.239 -17.130  12.094  1.00 41.72           N  
ANISOU 1993  N   GLN A 277     6046   4318   5490   -200    746   -678       N  
ATOM   1994  CA  GLN A 277       7.882 -15.826  12.142  1.00 40.39           C  
ANISOU 1994  CA  GLN A 277     5694   4257   5397   -227    734   -589       C  
ATOM   1995  C   GLN A 277       7.895 -15.219  13.539  1.00 45.04           C  
ANISOU 1995  C   GLN A 277     6179   4830   6102   -220    563   -512       C  
ATOM   1996  O   GLN A 277       8.281 -14.049  13.694  1.00 45.47           O  
ANISOU 1996  O   GLN A 277     6117   4948   6210   -276    522   -442       O  
ATOM   1997  CB  GLN A 277       7.201 -14.883  11.156  1.00 39.75           C  
ANISOU 1997  CB  GLN A 277     5676   4264   5164   -364    746   -556       C  
ATOM   1998  CG  GLN A 277       7.228 -15.410   9.728  1.00 38.99           C  
ANISOU 1998  CG  GLN A 277     5719   4190   4907   -385    907   -633       C  
ATOM   1999  CD  GLN A 277       6.546 -14.456   8.762  1.00 43.79           C  
ANISOU 1999  CD  GLN A 277     6407   4890   5341   -515    887   -579       C  
ATOM   2000  NE2 GLN A 277       5.448 -14.901   8.158  1.00 44.68           N  
ANISOU 2000  NE2 GLN A 277     6697   5004   5275   -595    824   -626       N  
ATOM   2001  OE1 GLN A 277       6.988 -13.323   8.586  1.00 40.36           O  
ANISOU 2001  OE1 GLN A 277     5879   4520   4937   -552    914   -487       O  
ATOM   2002  N   ALA A 278       7.492 -15.981  14.556  1.00 41.01           N  
ANISOU 2002  N   ALA A 278     5740   4223   5618   -164    469   -525       N  
ATOM   2003  CA  ALA A 278       7.436 -15.504  15.928  1.00 42.04           C  
ANISOU 2003  CA  ALA A 278     5832   4327   5816   -154    311   -462       C  
ATOM   2004  C   ALA A 278       8.439 -16.273  16.772  1.00 48.49           C  
ANISOU 2004  C   ALA A 278     6583   5084   6758    -10    267   -457       C  
ATOM   2005  O   ALA A 278       8.681 -17.455  16.532  1.00 47.12           O  
ANISOU 2005  O   ALA A 278     6467   4837   6599     96    348   -506       O  
ATOM   2006  CB  ALA A 278       6.032 -15.669  16.525  1.00 46.01           C  
ANISOU 2006  CB  ALA A 278     6485   4772   6223   -211    238   -456       C  
ATOM   2007  N   LYS A 279       9.012 -15.598  17.773  1.00 46.95           N  
ANISOU 2007  N   LYS A 279     6286   4909   6646     -2    126   -396       N  
ATOM   2008  CA  LYS A 279      10.023 -16.257  18.595  1.00 54.86           C  
ANISOU 2008  CA  LYS A 279     7200   5877   7768    142     40   -370       C  
ATOM   2009  C   LYS A 279       9.409 -17.246  19.580  1.00 41.33           C  
ANISOU 2009  C   LYS A 279     5683   4028   5992    219    -35   -366       C  
ATOM   2010  O   LYS A 279      10.069 -18.220  19.955  1.00 47.28           O  
ANISOU 2010  O   LYS A 279     6428   4716   6820    377    -56   -353       O  
ATOM   2011  CB  LYS A 279      10.864 -15.214  19.332  1.00 74.65           C  
ANISOU 2011  CB  LYS A 279     9540   8456  10368     95   -121   -308       C  
ATOM   2012  CG  LYS A 279      11.943 -14.554  18.460  1.00 75.64           C  
ANISOU 2012  CG  LYS A 279     9408   8709  10622     51    -37   -294       C  
ATOM   2013  CD  LYS A 279      13.262 -14.417  19.218  1.00 89.50           C  
ANISOU 2013  CD  LYS A 279    10924  10529  12554    100   -195   -236       C  
ATOM   2014  CE  LYS A 279      13.285 -13.179  20.111  1.00 85.82           C  
ANISOU 2014  CE  LYS A 279    10463  10073  12070    -64   -405   -199       C  
ATOM   2015  NZ  LYS A 279      13.503 -11.918  19.344  1.00107.32           N1+
ANISOU 2015  NZ  LYS A 279    13084  12869  14823   -250   -328   -188       N1+
ATOM   2016  N   MET A 280       8.170 -17.018  20.016  1.00 41.57           N  
ANISOU 2016  N   MET A 280     5886   4012   5895    121    -64   -364       N  
ATOM   2017  CA  MET A 280       7.428 -17.965  20.845  1.00 39.50           C  
ANISOU 2017  CA  MET A 280     5830   3620   5560    159    -89   -354       C  
ATOM   2018  C   MET A 280       6.105 -18.323  20.205  1.00 37.05           C  
ANISOU 2018  C   MET A 280     5650   3279   5148     51     28   -398       C  
ATOM   2019  O   MET A 280       5.428 -17.471  19.617  1.00 39.13           O  
ANISOU 2019  O   MET A 280     5873   3631   5362    -66     61   -408       O  
ATOM   2020  CB  MET A 280       7.131 -17.440  22.276  1.00 36.82           C  
ANISOU 2020  CB  MET A 280     5585   3250   5156    140   -237   -292       C  
ATOM   2021  CG  MET A 280       8.309 -17.123  23.096  1.00 49.87           C  
ANISOU 2021  CG  MET A 280     7146   4927   6877    218   -410   -244       C  
ATOM   2022  SD  MET A 280       7.670 -16.697  24.733  1.00 42.90           S  
ANISOU 2022  SD  MET A 280     6488   3972   5840    183   -551   -194       S  
ATOM   2023  CE  MET A 280       9.243 -16.310  25.513  1.00 44.45           C  
ANISOU 2023  CE  MET A 280     6547   4221   6120    249   -806   -147       C  
ATOM   2024  N   ARG A 281       5.733 -19.582  20.340  1.00 36.83           N  
ANISOU 2024  N   ARG A 281     5780   3121   5094     84     78   -418       N  
ATOM   2025  CA AARG A 281       4.454 -20.044  19.842  0.54 42.56           C  
ANISOU 2025  CA AARG A 281     6627   3811   5733    -50    162   -457       C  
ATOM   2026  CA BARG A 281       4.464 -20.069  19.829  0.46 42.55           C  
ANISOU 2026  CA BARG A 281     6627   3807   5732    -49    164   -459       C  
ATOM   2027  C   ARG A 281       3.740 -20.831  20.927  1.00 41.24           C  
ANISOU 2027  C   ARG A 281     6644   3508   5518    -65    148   -412       C  
ATOM   2028  O   ARG A 281       4.353 -21.611  21.663  1.00 39.54           O  
ANISOU 2028  O   ARG A 281     6529   3165   5328     60    114   -379       O  
ATOM   2029  CB AARG A 281       4.618 -20.887  18.575  0.54 43.34           C  
ANISOU 2029  CB AARG A 281     6772   3868   5828    -54    277   -551       C  
ATOM   2030  CB BARG A 281       4.650 -20.966  18.588  0.46 43.36           C  
ANISOU 2030  CB BARG A 281     6783   3860   5833    -47    280   -553       C  
ATOM   2031  CG AARG A 281       5.634 -22.012  18.660  0.54 43.92           C  
ANISOU 2031  CG AARG A 281     6918   3798   5972    125    320   -574       C  
ATOM   2032  CG BARG A 281       5.555 -22.193  18.760  0.46 43.78           C  
ANISOU 2032  CG BARG A 281     6934   3751   5950    126    321   -573       C  
ATOM   2033  CD AARG A 281       5.856 -22.593  17.270  0.54 48.62           C  
ANISOU 2033  CD AARG A 281     7564   4366   6545    126    463   -685       C  
ATOM   2034  CD BARG A 281       5.550 -23.034  17.472  0.46 52.06           C  
ANISOU 2034  CD BARG A 281     8092   4728   6961    109    463   -689       C  
ATOM   2035  NE AARG A 281       4.623 -23.178  16.752  0.54 45.83           N  
ANISOU 2035  NE AARG A 281     7396   3943   6075    -59    503   -752       N  
ATOM   2036  NE BARG A 281       6.725 -23.888  17.312  0.46 51.19           N  
ANISOU 2036  NE BARG A 281     8010   4502   6938    330    544   -719       N  
ATOM   2037  CZ AARG A 281       4.412 -23.493  15.483  0.54 50.75           C  
ANISOU 2037  CZ AARG A 281     8105   4565   6614   -142    595   -860       C  
ATOM   2038  CZ BARG A 281       6.691 -25.213  17.247  0.46 60.29           C  
ANISOU 2038  CZ BARG A 281     9396   5433   8078    397    624   -772       C  
ATOM   2039  NH1AARG A 281       5.352 -23.324  14.560  0.54 41.66           N1+
ANISOU 2039  NH1AARG A 281     6891   3467   5471    -39    698   -916       N1+
ATOM   2040  NH1BARG A 281       5.555 -25.884  17.354  0.46 64.78           N1+
ANISOU 2040  NH1BARG A 281    10193   5869   8552    227    626   -801       N1+
ATOM   2041  NH2AARG A 281       3.224 -23.978  15.129  0.54 39.45           N  
ANISOU 2041  NH2AARG A 281     6826   3084   5080   -346    584   -911       N  
ATOM   2042  NH2BARG A 281       7.826 -25.884  17.065  0.46 61.35           N  
ANISOU 2042  NH2BARG A 281     9531   5471   8308    640    713   -791       N  
ATOM   2043  N   ILE A 282       2.445 -20.594  21.033  1.00 36.82           N  
ANISOU 2043  N   ILE A 282     6116   2980   4892   -214    178   -397       N  
ATOM   2044  CA  ILE A 282       1.572 -21.358  21.920  1.00 35.71           C  
ANISOU 2044  CA  ILE A 282     6143   2722   4702   -274    212   -351       C  
ATOM   2045  C   ILE A 282       0.536 -21.961  20.991  1.00 37.76           C  
ANISOU 2045  C   ILE A 282     6429   2977   4941   -453    291   -408       C  
ATOM   2046  O   ILE A 282      -0.341 -21.247  20.488  1.00 39.41           O  
ANISOU 2046  O   ILE A 282     6512   3330   5134   -573    296   -409       O  
ATOM   2047  CB  ILE A 282       0.927 -20.477  22.995  1.00 36.25           C  
ANISOU 2047  CB  ILE A 282     6203   2852   4721   -297    193   -273       C  
ATOM   2048  CG1 ILE A 282       1.999 -19.929  23.948  1.00 35.97           C  
ANISOU 2048  CG1 ILE A 282     6182   2804   4679   -146     80   -230       C  
ATOM   2049  CG2 ILE A 282      -0.160 -21.258  23.756  1.00 38.76           C  
ANISOU 2049  CG2 ILE A 282     6673   3069   4984   -395    279   -220       C  
ATOM   2050  CD1 ILE A 282       2.788 -21.019  24.723  1.00 37.62           C  
ANISOU 2050  CD1 ILE A 282     6558   2851   4884    -20     27   -190       C  
ATOM   2051  N   ASP A 283       0.681 -23.258  20.704  1.00 36.59           N  
ANISOU 2051  N   ASP A 283     6448   2660   4794   -465    339   -457       N  
ATOM   2052  CA  ASP A 283      -0.242 -23.995  19.846  1.00 40.77           C  
ANISOU 2052  CA  ASP A 283     7050   3150   5291   -665    394   -527       C  
ATOM   2053  C   ASP A 283      -1.271 -24.798  20.620  1.00 43.89           C  
ANISOU 2053  C   ASP A 283     7584   3423   5668   -816    443   -472       C  
ATOM   2054  O   ASP A 283      -2.285 -25.212  20.038  1.00 45.43           O  
ANISOU 2054  O   ASP A 283     7787   3627   5847  -1040    467   -511       O  
ATOM   2055  CB  ASP A 283       0.547 -24.935  18.928  1.00 41.07           C  
ANISOU 2055  CB  ASP A 283     7227   3048   5329   -605    437   -637       C  
ATOM   2056  CG  ASP A 283       1.603 -24.200  18.145  1.00 51.72           C  
ANISOU 2056  CG  ASP A 283     8432   4520   6700   -460    428   -682       C  
ATOM   2057  OD1 ASP A 283       1.243 -23.255  17.402  1.00 45.45           O  
ANISOU 2057  OD1 ASP A 283     7482   3914   5872   -548    402   -697       O  
ATOM   2058  OD2 ASP A 283       2.792 -24.522  18.322  1.00 49.16           O1-
ANISOU 2058  OD2 ASP A 283     8133   4111   6435   -253    448   -685       O1-
ATOM   2059  N   HIS A 284      -1.032 -25.037  21.906  1.00 41.17           N  
ANISOU 2059  N   HIS A 284     7355   2968   5320   -714    455   -379       N  
ATOM   2060  CA  HIS A 284      -1.875 -25.911  22.712  1.00 42.82           C  
ANISOU 2060  CA  HIS A 284     7740   3027   5503   -848    533   -312       C  
ATOM   2061  C   HIS A 284      -2.543 -25.186  23.866  1.00 44.18           C  
ANISOU 2061  C   HIS A 284     7849   3296   5642   -863    566   -196       C  
ATOM   2062  O   HIS A 284      -3.740 -25.366  24.079  1.00 44.36           O  
ANISOU 2062  O   HIS A 284     7849   3343   5663  -1059    655   -153       O  
ATOM   2063  CB  HIS A 284      -1.051 -27.092  23.245  1.00 44.27           C  
ANISOU 2063  CB  HIS A 284     8207   2936   5679   -712    548   -291       C  
ATOM   2064  CG  HIS A 284      -0.477 -27.953  22.158  1.00 44.11           C  
ANISOU 2064  CG  HIS A 284     8265   2810   5686   -676    554   -406       C  
ATOM   2065  CD2 HIS A 284       0.788 -28.066  21.688  1.00 49.80           C  
ANISOU 2065  CD2 HIS A 284     8993   3483   6445   -450    527   -463       C  
ATOM   2066  ND1 HIS A 284      -1.250 -28.794  21.389  1.00 47.89           N  
ANISOU 2066  ND1 HIS A 284     8802   3248   6148   -886    600   -478       N  
ATOM   2067  CE1 HIS A 284      -0.481 -29.406  20.504  1.00 52.73           C  
ANISOU 2067  CE1 HIS A 284     9487   3780   6766   -781    606   -579       C  
ATOM   2068  NE2 HIS A 284       0.759 -28.980  20.666  1.00 48.39           N  
ANISOU 2068  NE2 HIS A 284     8900   3228   6260   -510    579   -570       N  
ATOM   2069  N   GLY A 285      -1.808 -24.336  24.579  1.00 39.98           N  
ANISOU 2069  N   GLY A 285     7281   2827   5084   -669    501   -150       N  
ATOM   2070  CA  GLY A 285      -2.355 -23.628  25.725  1.00 42.40           C  
ANISOU 2070  CA  GLY A 285     7584   3199   5326   -660    546    -55       C  
ATOM   2071  C   GLY A 285      -3.423 -22.618  25.347  1.00 44.89           C  
ANISOU 2071  C   GLY A 285     7661   3727   5670   -771    599    -57       C  
ATOM   2072  O   GLY A 285      -3.638 -22.286  24.175  1.00 41.32           O  
ANISOU 2072  O   GLY A 285     7024   3397   5280   -841    561   -125       O  
ATOM   2073  N   ASP A 286      -4.119 -22.129  26.375  1.00 38.22           N  
ANISOU 2073  N   ASP A 286     6833   2921   4769   -773    696     27       N  
ATOM   2074  CA  ASP A 286      -5.042 -21.022  26.192  1.00 38.08           C  
ANISOU 2074  CA  ASP A 286     6587   3099   4784   -808    757     42       C  
ATOM   2075  C   ASP A 286      -4.342 -19.750  26.660  1.00 39.50           C  
ANISOU 2075  C   ASP A 286     6767   3333   4908   -620    686     36       C  
ATOM   2076  O   ASP A 286      -3.109 -19.713  26.757  1.00 36.55           O  
ANISOU 2076  O   ASP A 286     6491   2892   4507   -501    554      3       O  
ATOM   2077  CB  ASP A 286      -6.393 -21.323  26.883  1.00 38.55           C  
ANISOU 2077  CB  ASP A 286     6634   3173   4838   -943    952    132       C  
ATOM   2078  CG  ASP A 286      -6.330 -21.313  28.405  1.00 42.31           C  
ANISOU 2078  CG  ASP A 286     7349   3545   5181   -851   1061    215       C  
ATOM   2079  OD1 ASP A 286      -5.309 -20.914  28.998  1.00 39.94           O  
ANISOU 2079  OD1 ASP A 286     7214   3179   4783   -680    960    203       O  
ATOM   2080  OD2 ASP A 286      -7.359 -21.696  29.018  1.00 43.61           O1-
ANISOU 2080  OD2 ASP A 286     7532   3703   5333   -966   1255    298       O1-
ATOM   2081  N   LEU A 287      -5.101 -18.681  26.917  1.00 35.43           N  
ANISOU 2081  N   LEU A 287     6135   2938   4389   -592    771     68       N  
ATOM   2082  CA  LEU A 287      -4.423 -17.430  27.222  1.00 36.00           C  
ANISOU 2082  CA  LEU A 287     6230   3038   4412   -438    693     44       C  
ATOM   2083  C   LEU A 287      -3.732 -17.455  28.582  1.00 38.39           C  
ANISOU 2083  C   LEU A 287     6812   3209   4567   -336    670     67       C  
ATOM   2084  O   LEU A 287      -2.855 -16.621  28.821  1.00 37.03           O  
ANISOU 2084  O   LEU A 287     6694   3027   4347   -235    545     31       O  
ATOM   2085  CB  LEU A 287      -5.412 -16.266  27.112  1.00 36.80           C  
ANISOU 2085  CB  LEU A 287     6164   3272   4546   -408    798     69       C  
ATOM   2086  CG  LEU A 287      -5.653 -15.916  25.628  1.00 35.77           C  
ANISOU 2086  CG  LEU A 287     5772   3280   4538   -461    722     40       C  
ATOM   2087  CD1 LEU A 287      -7.006 -15.200  25.452  1.00 36.59           C  
ANISOU 2087  CD1 LEU A 287     5665   3528   4710   -457    846    102       C  
ATOM   2088  CD2 LEU A 287      -4.492 -15.039  25.071  1.00 35.21           C  
ANISOU 2088  CD2 LEU A 287     5701   3211   4465   -371    563    -20       C  
ATOM   2089  N   THR A 288      -4.057 -18.414  29.458  1.00 39.94           N  
ANISOU 2089  N   THR A 288     7198   3297   4682   -376    769    130       N  
ATOM   2090  CA  THR A 288      -3.270 -18.545  30.685  1.00 42.87           C  
ANISOU 2090  CA  THR A 288     7865   3538   4888   -276    700    160       C  
ATOM   2091  C   THR A 288      -1.814 -18.891  30.386  1.00 40.48           C  
ANISOU 2091  C   THR A 288     7594   3174   4612   -201    461    122       C  
ATOM   2092  O   THR A 288      -0.943 -18.634  31.230  1.00 37.46           O  
ANISOU 2092  O   THR A 288     7386   2732   4114   -101    323    132       O  
ATOM   2093  CB  THR A 288      -3.878 -19.575  31.654  1.00 40.74           C  
ANISOU 2093  CB  THR A 288     7823   3147   4508   -334    859    255       C  
ATOM   2094  CG2 THR A 288      -5.278 -19.127  32.118  1.00 43.47           C  
ANISOU 2094  CG2 THR A 288     8125   3568   4824   -389   1130    305       C  
ATOM   2095  OG1 THR A 288      -3.928 -20.902  31.083  1.00 39.55           O  
ANISOU 2095  OG1 THR A 288     7662   2916   4450   -441    864    273       O  
ATOM   2096  N   ALA A 289      -1.530 -19.435  29.196  1.00 39.74           N  
ANISOU 2096  N   ALA A 289     7329   3103   4666   -245    408     76       N  
ATOM   2097  CA  ALA A 289      -0.145 -19.681  28.801  1.00 37.07           C  
ANISOU 2097  CA  ALA A 289     6970   2732   4384   -151    216     38       C  
ATOM   2098  C   ALA A 289       0.700 -18.428  28.973  1.00 34.26           C  
ANISOU 2098  C   ALA A 289     6552   2454   4011    -68     66      4       C  
ATOM   2099  O   ALA A 289       1.857 -18.509  29.396  1.00 37.46           O  
ANISOU 2099  O   ALA A 289     7017   2818   4398     27   -109     12       O  
ATOM   2100  CB  ALA A 289      -0.072 -20.153  27.346  1.00 38.37           C  
ANISOU 2100  CB  ALA A 289     6946   2936   4696   -210    225    -27       C  
ATOM   2101  N   LEU A 290       0.142 -17.258  28.639  1.00 34.80           N  
ANISOU 2101  N   LEU A 290     6497   2631   4095   -106    124    -30       N  
ATOM   2102  CA  LEU A 290       0.920 -16.032  28.738  1.00 34.89           C  
ANISOU 2102  CA  LEU A 290     6470   2689   4095    -59    -11    -69       C  
ATOM   2103  C   LEU A 290       1.244 -15.674  30.184  1.00 36.79           C  
ANISOU 2103  C   LEU A 290     6967   2851   4162     -2    -92    -44       C  
ATOM   2104  O   LEU A 290       2.241 -14.984  30.428  1.00 39.09           O  
ANISOU 2104  O   LEU A 290     7268   3148   4437     25   -276    -73       O  
ATOM   2105  CB  LEU A 290       0.182 -14.874  28.060  1.00 40.25           C  
ANISOU 2105  CB  LEU A 290     7002   3469   4823    -99     82    -99       C  
ATOM   2106  CG  LEU A 290       0.463 -14.766  26.551  1.00 38.97           C  
ANISOU 2106  CG  LEU A 290     6594   3403   4810   -141     55   -138       C  
ATOM   2107  CD1 LEU A 290      -0.169 -15.978  25.819  1.00 38.02           C  
ANISOU 2107  CD1 LEU A 290     6405   3293   4748   -207    149   -133       C  
ATOM   2108  CD2 LEU A 290      -0.087 -13.429  26.061  1.00 42.74           C  
ANISOU 2108  CD2 LEU A 290     6973   3957   5308   -152    105   -148       C  
ATOM   2109  N   LEU A 291       0.441 -16.132  31.151  1.00 36.53           N  
ANISOU 2109  N   LEU A 291     7151   2743   3988      0     38     11       N  
ATOM   2110  CA  LEU A 291       0.818 -15.932  32.547  1.00 38.27           C  
ANISOU 2110  CA  LEU A 291     7668   2875   3998     55    -51     37       C  
ATOM   2111  C   LEU A 291       1.973 -16.845  32.925  1.00 40.44           C  
ANISOU 2111  C   LEU A 291     8031   3083   4253    116   -270     81       C  
ATOM   2112  O   LEU A 291       2.904 -16.423  33.621  1.00 41.25           O  
ANISOU 2112  O   LEU A 291     8247   3167   4258    160   -491     77       O  
ATOM   2113  CB  LEU A 291      -0.375 -16.176  33.480  1.00 37.93           C  
ANISOU 2113  CB  LEU A 291     7851   2771   3791     44    186     94       C  
ATOM   2114  CG  LEU A 291      -1.526 -15.165  33.322  1.00 39.56           C  
ANISOU 2114  CG  LEU A 291     7980   3045   4007     28    411     63       C  
ATOM   2115  CD1 LEU A 291      -2.762 -15.639  34.106  1.00 41.22           C  
ANISOU 2115  CD1 LEU A 291     8343   3217   4102     12    695    138       C  
ATOM   2116  CD2 LEU A 291      -1.086 -13.750  33.767  1.00 38.53           C  
ANISOU 2116  CD2 LEU A 291     7969   2899   3772     79    315    -10       C  
ATOM   2117  N   TYR A 292       1.932 -18.104  32.473  1.00 38.64           N  
ANISOU 2117  N   TYR A 292     7754   2809   4118    122   -221    127       N  
ATOM   2118  CA  TYR A 292       3.012 -19.033  32.791  1.00 39.03           C  
ANISOU 2118  CA  TYR A 292     7881   2779   4168    222   -415    183       C  
ATOM   2119  C   TYR A 292       4.314 -18.607  32.125  1.00 38.51           C  
ANISOU 2119  C   TYR A 292     7569   2805   4260    275   -636    134       C  
ATOM   2120  O   TYR A 292       5.388 -18.724  32.728  1.00 41.60           O  
ANISOU 2120  O   TYR A 292     8010   3179   4616    366   -875    175       O  
ATOM   2121  CB  TYR A 292       2.619 -20.454  32.384  1.00 38.85           C  
ANISOU 2121  CB  TYR A 292     7889   2654   4218    218   -283    233       C  
ATOM   2122  CG  TYR A 292       1.359 -20.924  33.079  1.00 41.41           C  
ANISOU 2122  CG  TYR A 292     8442   2889   4401    135    -55    299       C  
ATOM   2123  CD1 TYR A 292       1.256 -20.884  34.477  1.00 41.01           C  
ANISOU 2123  CD1 TYR A 292     8714   2759   4110    171    -68    378       C  
ATOM   2124  CD2 TYR A 292       0.272 -21.411  32.346  1.00 40.85           C  
ANISOU 2124  CD2 TYR A 292     8270   2820   4430      6    172    287       C  
ATOM   2125  CE1 TYR A 292       0.100 -21.313  35.127  1.00 42.64           C  
ANISOU 2125  CE1 TYR A 292     9128   2888   4185     89    181    449       C  
ATOM   2126  CE2 TYR A 292      -0.887 -21.834  32.984  1.00 40.51           C  
ANISOU 2126  CE2 TYR A 292     8398   2713   4283    -92    396    358       C  
ATOM   2127  CZ  TYR A 292      -0.973 -21.775  34.366  1.00 42.59           C  
ANISOU 2127  CZ  TYR A 292     8970   2898   4316    -47    420    442       C  
ATOM   2128  OH  TYR A 292      -2.122 -22.196  35.002  1.00 45.86           O  
ANISOU 2128  OH  TYR A 292     9548   3251   4625   -149    680    522       O  
ATOM   2129  N   ILE A 293       4.234 -18.105  30.888  1.00 38.57           N  
ANISOU 2129  N   ILE A 293     7301   2918   4438    216   -562     56       N  
ATOM   2130  CA  ILE A 293       5.412 -17.570  30.206  1.00 36.77           C  
ANISOU 2130  CA  ILE A 293     6822   2788   4360    242   -726     12       C  
ATOM   2131  C   ILE A 293       6.087 -16.515  31.078  1.00 36.32           C  
ANISOU 2131  C   ILE A 293     6830   2764   4207    229   -939      6       C  
ATOM   2132  O   ILE A 293       7.318 -16.492  31.229  1.00 41.96           O  
ANISOU 2132  O   ILE A 293     7438   3517   4987    280  -1169     24       O  
ATOM   2133  CB  ILE A 293       5.005 -16.999  28.828  1.00 37.75           C  
ANISOU 2133  CB  ILE A 293     6706   3015   4623    156   -582    -62       C  
ATOM   2134  CG1 ILE A 293       4.727 -18.119  27.811  1.00 37.22           C  
ANISOU 2134  CG1 ILE A 293     6553   2923   4664    166   -442    -73       C  
ATOM   2135  CG2 ILE A 293       6.036 -15.996  28.281  1.00 37.49           C  
ANISOU 2135  CG2 ILE A 293     6450   3091   4704    134   -715   -105       C  
ATOM   2136  CD1 ILE A 293       3.990 -17.608  26.532  1.00 36.84           C  
ANISOU 2136  CD1 ILE A 293     6336   2972   4691     59   -290   -136       C  
ATOM   2137  N   GLN A 294       5.288 -15.684  31.730  1.00 39.19           N  
ANISOU 2137  N   GLN A 294     7382   3102   4408    162   -868    -18       N  
ATOM   2138  CA  GLN A 294       5.809 -14.622  32.578  1.00 40.01           C  
ANISOU 2138  CA  GLN A 294     7613   3204   4384    125  -1057    -46       C  
ATOM   2139  C   GLN A 294       6.194 -15.095  33.970  1.00 44.81           C  
ANISOU 2139  C   GLN A 294     8515   3729   4782    185  -1238     17       C  
ATOM   2140  O   GLN A 294       6.631 -14.270  34.784  1.00 47.00           O  
ANISOU 2140  O   GLN A 294     8950   3994   4913    140  -1424    -13       O  
ATOM   2141  CB  GLN A 294       4.783 -13.512  32.677  1.00 37.83           C  
ANISOU 2141  CB  GLN A 294     7452   2911   4011     54   -882   -107       C  
ATOM   2142  CG  GLN A 294       4.619 -12.815  31.370  1.00 37.93           C  
ANISOU 2142  CG  GLN A 294     7190   3008   4212     -4   -779   -158       C  
ATOM   2143  CD  GLN A 294       3.578 -11.741  31.449  1.00 42.38           C  
ANISOU 2143  CD  GLN A 294     7863   3544   4696    -35   -604   -201       C  
ATOM   2144  NE2 GLN A 294       2.356 -12.071  31.047  1.00 37.10           N  
ANISOU 2144  NE2 GLN A 294     7151   2892   4051    -14   -356   -177       N  
ATOM   2145  OE1 GLN A 294       3.862 -10.632  31.870  1.00 40.87           O  
ANISOU 2145  OE1 GLN A 294     7791   3311   4428    -76   -691   -252       O  
ATOM   2146  N   GLY A 295       6.036 -16.381  34.263  1.00 42.25           N  
ANISOU 2146  N   GLY A 295     8296   3334   4422    276  -1196    105       N  
ATOM   2147  CA  GLY A 295       6.459 -16.953  35.524  1.00 46.65           C  
ANISOU 2147  CA  GLY A 295     9142   3807   4776    353  -1382    193       C  
ATOM   2148  C   GLY A 295       5.437 -16.922  36.634  1.00 43.55           C  
ANISOU 2148  C   GLY A 295     9151   3309   4089    332  -1229    220       C  
ATOM   2149  O   GLY A 295       5.781 -17.244  37.776  1.00 49.55           O  
ANISOU 2149  O   GLY A 295    10209   3995   4622    384  -1396    291       O  
ATOM   2150  N   TYR A 296       4.201 -16.528  36.352  1.00 45.68           N  
ANISOU 2150  N   TYR A 296     9437   3574   4346    264   -918    172       N  
ATOM   2151  CA  TYR A 296       3.181 -16.536  37.396  1.00 43.20           C  
ANISOU 2151  CA  TYR A 296     9483   3168   3765    255   -717    206       C  
ATOM   2152  C   TYR A 296       2.823 -17.963  37.774  1.00 51.12           C  
ANISOU 2152  C   TYR A 296    10650   4069   4706    301   -611    333       C  
ATOM   2153  O   TYR A 296       2.712 -18.825  36.906  1.00 45.10           O  
ANISOU 2153  O   TYR A 296     9679   3306   4150    303   -528    362       O  
ATOM   2154  CB  TYR A 296       1.923 -15.846  36.900  1.00 41.53           C  
ANISOU 2154  CB  TYR A 296     9175   2996   3608    194   -391    143       C  
ATOM   2155  CG  TYR A 296       2.031 -14.352  36.810  1.00 40.86           C  
ANISOU 2155  CG  TYR A 296     9062   2954   3510    160   -436     30       C  
ATOM   2156  CD1 TYR A 296       2.017 -13.571  37.962  1.00 44.81           C  
ANISOU 2156  CD1 TYR A 296     9919   3378   3730    164   -474    -10       C  
ATOM   2157  CD2 TYR A 296       2.144 -13.731  35.570  1.00 41.11           C  
ANISOU 2157  CD2 TYR A 296     8748   3081   3790    121   -435    -36       C  
ATOM   2158  CE1 TYR A 296       2.098 -12.179  37.865  1.00 48.53           C  
ANISOU 2158  CE1 TYR A 296    10402   3849   4188    127   -504   -124       C  
ATOM   2159  CE2 TYR A 296       2.235 -12.352  35.473  1.00 45.13           C  
ANISOU 2159  CE2 TYR A 296     9259   3598   4290     86   -467   -130       C  
ATOM   2160  CZ  TYR A 296       2.216 -11.594  36.628  1.00 45.84           C  
ANISOU 2160  CZ  TYR A 296     9709   3594   4116     88   -503   -176       C  
ATOM   2161  OH  TYR A 296       2.296 -10.206  36.515  1.00 45.42           O  
ANISOU 2161  OH  TYR A 296     9693   3512   4053     48   -526   -277       O  
ATOM   2162  N   ARG A 297       2.632 -18.198  39.071  1.00 46.99           N  
ANISOU 2162  N   ARG A 297    10532   3443   3879    328   -607    406       N  
ATOM   2163  CA  ARG A 297       2.017 -19.407  39.591  1.00 53.51           C  
ANISOU 2163  CA  ARG A 297    11594   4146   4593    343   -428    538       C  
ATOM   2164  C   ARG A 297       0.506 -19.227  39.651  1.00 53.79           C  
ANISOU 2164  C   ARG A 297    11677   4178   4582    254    -10    530       C  
ATOM   2165  O   ARG A 297       0.000 -18.106  39.738  1.00 53.21           O  
ANISOU 2165  O   ARG A 297    11593   4168   4455    226    113    440       O  
ATOM   2166  CB  ARG A 297       2.565 -19.730  40.985  1.00 52.33           C  
ANISOU 2166  CB  ARG A 297    11883   3889   4112    417   -626    638       C  
ATOM   2167  CG  ARG A 297       3.969 -20.299  40.945  1.00 61.93           C  
ANISOU 2167  CG  ARG A 297    13029   5098   5403    531  -1025    701       C  
ATOM   2168  CD  ARG A 297       4.770 -20.005  42.215  1.00 89.84           C  
ANISOU 2168  CD  ARG A 297    16890   8615   8631    585  -1350    738       C  
ATOM   2169  NE  ARG A 297       6.102 -19.511  41.873  1.00110.34           N  
ANISOU 2169  NE  ARG A 297    19238  11319  11368    626  -1758    698       N  
ATOM   2170  CZ  ARG A 297       7.118 -20.279  41.497  1.00105.55           C  
ANISOU 2170  CZ  ARG A 297    18419  10729  10954    749  -2009    780       C  
ATOM   2171  NH1 ARG A 297       7.019 -21.600  41.475  1.00 99.25           N1+
ANISOU 2171  NH1 ARG A 297    17663   9832  10217    852  -1912    896       N1+
ATOM   2172  NH2 ARG A 297       8.260 -19.706  41.124  1.00 96.16           N  
ANISOU 2172  NH2 ARG A 297    16925   9677   9934    761  -2333    727       N  
ATOM   2173  N   LYS A 298      -0.218 -20.347  39.604  1.00 52.66           N  
ANISOU 2173  N   LYS A 298    11582   3954   4472    209    215    632       N  
ATOM   2174  CA  LYS A 298      -1.673 -20.277  39.688  1.00 60.59           C  
ANISOU 2174  CA  LYS A 298    12591   4973   5457    109    619    648       C  
ATOM   2175  C   LYS A 298      -2.136 -19.583  40.974  1.00 64.40           C  
ANISOU 2175  C   LYS A 298    13442   5423   5606    136    766    658       C  
ATOM   2176  O   LYS A 298      -3.171 -18.907  40.966  1.00 58.63           O  
ANISOU 2176  O   LYS A 298    12637   4759   4879    100   1066    616       O  
ATOM   2177  CB  LYS A 298      -2.279 -21.688  39.575  1.00 68.31           C  
ANISOU 2177  CB  LYS A 298    13604   5848   6503     24    809    767       C  
ATOM   2178  CG  LYS A 298      -3.770 -21.668  39.234  1.00 67.07           C  
ANISOU 2178  CG  LYS A 298    13278   5753   6452   -120   1204    778       C  
ATOM   2179  CD  LYS A 298      -4.177 -22.649  38.140  1.00 75.34           C  
ANISOU 2179  CD  LYS A 298    14059   6790   7777   -252   1278    795       C  
ATOM   2180  CE  LYS A 298      -4.989 -23.794  38.738  1.00 86.55           C  
ANISOU 2180  CE  LYS A 298    15605   8140   9140   -366   1507    891       C  
ATOM   2181  NZ  LYS A 298      -5.165 -24.943  37.806  1.00 71.36           N1+
ANISOU 2181  NZ  LYS A 298    13502   6166   7446   -496   1510    899       N1+
ATOM   2182  N   ALA A 299      -1.380 -19.710  42.077  1.00 57.05           N  
ANISOU 2182  N   ALA A 299    12862   4415   4400    210    554    687       N  
ATOM   2183  CA  ALA A 299      -1.709 -18.983  43.307  1.00 62.34           C  
ANISOU 2183  CA  ALA A 299    13863   5065   4759    238    659    639       C  
ATOM   2184  C   ALA A 299      -1.708 -17.463  43.125  1.00 67.88           C  
ANISOU 2184  C   ALA A 299    14563   5821   5408    259    650    519       C  
ATOM   2185  O   ALA A 299      -2.359 -16.753  43.902  1.00 66.38           O  
ANISOU 2185  O   ALA A 299    14574   5614   5033    278    870    455       O  
ATOM   2186  CB  ALA A 299      -0.730 -19.358  44.422  1.00 68.39           C  
ANISOU 2186  CB  ALA A 299    14942   5756   5287    303    349    660       C  
ATOM   2187  N   ASP A 300      -0.973 -16.945  42.146  1.00 53.29           N  
ANISOU 2187  N   ASP A 300    12392   4057   3800    259    396    431       N  
ATOM   2188  CA  ASP A 300      -0.976 -15.514  41.842  1.00 56.03           C  
ANISOU 2188  CA  ASP A 300    12629   4469   4190    264    383    279       C  
ATOM   2189  C   ASP A 300      -2.204 -15.055  41.062  1.00 61.23           C  
ANISOU 2189  C   ASP A 300    12989   5211   5063    248    751    241       C  
ATOM   2190  O   ASP A 300      -2.418 -13.843  40.957  1.00 57.25           O  
ANISOU 2190  O   ASP A 300    12464   4729   4558    279    813    132       O  
ATOM   2191  CB  ASP A 300       0.259 -15.120  41.010  1.00 59.79           C  
ANISOU 2191  CB  ASP A 300    12821   5017   4881    252     -6    202       C  
ATOM   2192  CG  ASP A 300       1.569 -15.560  41.634  1.00 70.94           C  
ANISOU 2192  CG  ASP A 300    14420   6385   6150    277   -417    249       C  
ATOM   2193  OD1 ASP A 300       1.644 -15.563  42.874  1.00 71.48           O  
ANISOU 2193  OD1 ASP A 300    14932   6362   5867    299   -471    281       O  
ATOM   2194  OD2 ASP A 300       2.527 -15.879  40.882  1.00 55.07           O1-
ANISOU 2194  OD2 ASP A 300    12111   4438   4374    283   -686    256       O1-
ATOM   2195  N   PHE A 301      -2.975 -15.969  40.469  1.00 51.56           N  
ANISOU 2195  N   PHE A 301    11526   4030   4035    198    969    329       N  
ATOM   2196  CA  PHE A 301      -3.998 -15.572  39.503  1.00 53.33           C  
ANISOU 2196  CA  PHE A 301    11371   4372   4521    172   1226    299       C  
ATOM   2197  C   PHE A 301      -5.160 -14.873  40.200  1.00 55.53           C  
ANISOU 2197  C   PHE A 301    11797   4648   4653    226   1605    295       C  
ATOM   2198  O   PHE A 301      -5.495 -15.180  41.344  1.00 56.41           O  
ANISOU 2198  O   PHE A 301    12274   4672   4490    243   1782    356       O  
ATOM   2199  CB  PHE A 301      -4.568 -16.787  38.759  1.00 55.60           C  
ANISOU 2199  CB  PHE A 301    11389   4701   5033     71   1349    394       C  
ATOM   2200  CG  PHE A 301      -3.634 -17.426  37.770  1.00 49.55           C  
ANISOU 2200  CG  PHE A 301    10400   3951   4477     34   1054    381       C  
ATOM   2201  CD1 PHE A 301      -2.299 -17.075  37.694  1.00 48.85           C  
ANISOU 2201  CD1 PHE A 301    10344   3847   4370     94    702    320       C  
ATOM   2202  CD2 PHE A 301      -4.113 -18.417  36.914  1.00 50.95           C  
ANISOU 2202  CD2 PHE A 301    10332   4156   4871    -69   1144    432       C  
ATOM   2203  CE1 PHE A 301      -1.455 -17.715  36.769  1.00 47.11           C  
ANISOU 2203  CE1 PHE A 301     9901   3645   4355     81    477    315       C  
ATOM   2204  CE2 PHE A 301      -3.281 -19.042  35.987  1.00 47.16           C  
ANISOU 2204  CE2 PHE A 301     9677   3672   4569    -87    911    410       C  
ATOM   2205  CZ  PHE A 301      -1.956 -18.687  35.913  1.00 47.44           C  
ANISOU 2205  CZ  PHE A 301     9732   3699   4593      3    595    355       C  
ATOM   2206  N   VAL A 302      -5.798 -13.947  39.482  1.00 53.74           N  
ANISOU 2206  N   VAL A 302    11286   4519   4614    267   1747    232       N  
ATOM   2207  CA  VAL A 302      -7.105 -13.450  39.903  1.00 64.78           C  
ANISOU 2207  CA  VAL A 302    12696   5947   5969    337   2169    253       C  
ATOM   2208  C   VAL A 302      -8.147 -14.523  39.614  1.00 74.35           C  
ANISOU 2208  C   VAL A 302    13657   7246   7347    234   2434    384       C  
ATOM   2209  O   VAL A 302      -8.353 -14.912  38.459  1.00 74.23           O  
ANISOU 2209  O   VAL A 302    13233   7343   7629    147   2368    404       O  
ATOM   2210  CB  VAL A 302      -7.455 -12.144  39.182  1.00 63.22           C  
ANISOU 2210  CB  VAL A 302    12258   5821   5943    437   2220    164       C  
ATOM   2211  CG1 VAL A 302      -8.915 -11.773  39.452  1.00 69.56           C  
ANISOU 2211  CG1 VAL A 302    12967   6686   6778    533   2680    213       C  
ATOM   2212  CG2 VAL A 302      -6.505 -11.031  39.616  1.00 53.09           C  
ANISOU 2212  CG2 VAL A 302    11289   4416   4467    512   1997     31       C  
ATOM   2213  N   GLN A 303      -8.807 -15.013  40.659  1.00 77.10           N  
ANISOU 2213  N   GLN A 303    14263   7538   7492    224   2737    474       N  
ATOM   2214  CA  GLN A 303      -9.827 -16.042  40.476  1.00 90.60           C  
ANISOU 2214  CA  GLN A 303    15749   9320   9354     89   3011    608       C  
ATOM   2215  C   GLN A 303     -11.224 -15.450  40.610  1.00104.24           C  
ANISOU 2215  C   GLN A 303    17277  11165  11165    155   3454    643       C  
ATOM   2216  O   GLN A 303     -11.963 -15.360  39.630  1.00103.30           O  
ANISOU 2216  O   GLN A 303    16679  11209  11362    116   3528    664       O  
ATOM   2217  CB  GLN A 303      -9.638 -17.192  41.476  1.00100.97           C  
ANISOU 2217  CB  GLN A 303    17443  10494  10428      1   3057    715       C  
ATOM   2218  CG  GLN A 303      -8.210 -17.725  41.555  1.00 97.10           C  
ANISOU 2218  CG  GLN A 303    17212   9872   9808    -10   2632    701       C  
ATOM   2219  CD  GLN A 303      -7.949 -18.855  40.565  1.00106.88           C  
ANISOU 2219  CD  GLN A 303    18181  11118  11308   -152   2451    750       C  
ATOM   2220  NE2 GLN A 303      -6.728 -19.382  40.573  1.00 89.95           N  
ANISOU 2220  NE2 GLN A 303    16211   8868   9100   -134   2096    746       N  
ATOM   2221  OE1 GLN A 303      -8.832 -19.242  39.798  1.00113.14           O  
ANISOU 2221  OE1 GLN A 303    18616  12012  12360   -274   2625    789       O  
TER   
HETATM 2222  C1  PEG A 401     -10.856  -0.038  37.765  0.58 82.55           C  
HETATM 2223  O1  PEG A 401      -9.468  -0.217  37.714  0.58 72.50           O  
HETATM 2224  C2  PEG A 401     -11.496  -0.666  36.529  0.58 84.54           C  
HETATM 2225  O2  PEG A 401     -11.872   0.344  35.637  0.58 87.24           O  
HETATM 2226  C3  PEG A 401     -11.128   0.367  34.452  0.58 83.26           C  
HETATM 2227  C4  PEG A 401     -11.499  -0.834  33.583  0.58 79.95           C  
HETATM 2228  O4  PEG A 401     -10.945  -0.665  32.307  0.58 75.24           O  
HETATM 2229  C1  GOL A 402      -9.717 -18.982  17.940  0.82 57.01           C  
HETATM 2230  O1  GOL A 402      -9.006 -19.746  17.001  0.82 79.10           O  
HETATM 2231  C2  GOL A 402      -8.813 -18.692  19.140  0.82 60.08           C  
HETATM 2232  O2  GOL A 402      -9.597 -18.370  20.263  0.82 58.51           O  
HETATM 2233  C3  GOL A 402      -7.944 -19.917  19.436  0.82 68.82           C  
HETATM 2234  O3  GOL A 402      -6.987 -19.593  20.413  0.82 62.76           O  
HETATM 2235  C   FMT A 403       0.788 -27.592  16.419  0.74 65.89           C  
HETATM 2236  O1  FMT A 403       1.774 -28.060  17.055  0.74 64.89           O  
HETATM 2237  O2  FMT A 403      -0.392 -27.880  16.767  0.74 57.89           O  
HETATM 2238  C1  GOL A 404      12.136 -14.589  14.701  0.87 82.73           C  
HETATM 2239  O1  GOL A 404      11.105 -13.664  14.959  0.87 63.34           O  
HETATM 2240  C2  GOL A 404      11.686 -15.652  13.692  0.87 77.30           C  
HETATM 2241  O2  GOL A 404      11.976 -15.245  12.378  0.87 86.91           O  
HETATM 2242  C3  GOL A 404      12.380 -16.985  13.984  0.87 82.02           C  
HETATM 2243  O3  GOL A 404      11.595 -17.751  14.859  0.87 73.40           O  
HETATM 2244  C   FMT A 405      -3.787   6.414  19.968  0.95 78.89           C  
HETATM 2245  O1  FMT A 405      -2.701   5.814  19.745  0.95 68.06           O  
HETATM 2246  O2  FMT A 405      -4.699   5.844  20.626  0.95 74.26           O  
HETATM 2247  C   FMT A 406      -9.984   3.430  18.839  0.80 65.77           C  
HETATM 2248  O1  FMT A 406      -9.534   4.000  17.809  0.80 72.68           O  
HETATM 2249  O2  FMT A 406     -10.471   2.268  18.763  0.80 52.47           O  
HETATM 2250  C   FMT A 407      12.342   5.143  28.337  0.85 75.40           C  
HETATM 2251  O1  FMT A 407      12.937   4.513  29.257  0.85 77.69           O  
HETATM 2252  O2  FMT A 407      11.080   5.240  28.335  0.85 71.33           O  
HETATM 2253  C1  GOL A 408       1.299 -23.682  42.619  1.00 80.11           C  
HETATM 2254  O1  GOL A 408       0.387 -22.632  42.396  1.00 72.67           O  
HETATM 2255  C2  GOL A 408       0.835 -25.017  42.014  1.00 79.29           C  
HETATM 2256  O2  GOL A 408       1.541 -26.066  42.624  1.00 77.38           O  
HETATM 2257  C3  GOL A 408      -0.680 -25.234  42.148  1.00 82.03           C  
HETATM 2258  O3  GOL A 408      -1.208 -25.907  41.019  1.00 54.83           O  
HETATM 2259  C1  GOL A 409     -12.148 -13.173  37.391  0.86 72.94           C  
HETATM 2260  O1  GOL A 409     -11.577 -11.915  37.627  0.86 71.03           O  
HETATM 2261  C2  GOL A 409     -11.389 -13.882  36.269  0.86 75.45           C  
HETATM 2262  O2  GOL A 409     -10.021 -13.940  36.583  0.86 64.19           O  
HETATM 2263  C3  GOL A 409     -11.944 -15.295  36.098  0.86 83.42           C  
HETATM 2264  O3  GOL A 409     -11.360 -15.893  34.972  0.86 71.50           O  
HETATM 2265  C1  GOL A 410      -7.893   2.872  32.908  0.74 70.29           C  
HETATM 2266  O1  GOL A 410      -8.297   1.565  32.616  0.74 69.86           O  
HETATM 2267  C2  GOL A 410      -6.542   3.152  32.254  0.74 63.99           C  
HETATM 2268  O2  GOL A 410      -6.434   4.519  31.957  0.74 62.48           O  
HETATM 2269  C3  GOL A 410      -5.418   2.800  33.218  0.74 65.57           C  
HETATM 2270  O3  GOL A 410      -5.960   2.315  34.417  0.74 66.96           O  
HETATM 2271  C1  EDO A 411      12.537 -19.952  39.062  1.00 78.63           C  
HETATM 2272  O1  EDO A 411      11.736 -18.974  39.665  1.00 85.60           O  
HETATM 2273  C2  EDO A 411      11.686 -20.695  38.034  1.00 60.28           C  
HETATM 2274  O2  EDO A 411      10.377 -20.819  38.532  1.00 65.80           O  
HETATM 2275  C1  EDO A 412      -2.560  -0.703  35.473  0.67 66.63           C  
HETATM 2276  O1  EDO A 412      -3.524  -1.482  34.809  0.67 63.69           O  
HETATM 2277  C2  EDO A 412      -2.721   0.767  35.095  0.67 67.85           C  
HETATM 2278  O2  EDO A 412      -3.996   1.196  35.490  0.67 70.27           O  
HETATM 2279  C1  GOL A 413     -18.527 -11.565  -5.157  0.84 76.50           C  
HETATM 2280  O1  GOL A 413     -18.393 -10.208  -4.829  0.84 81.06           O  
HETATM 2281  C2  GOL A 413     -19.910 -12.048  -4.726  0.84 79.76           C  
HETATM 2282  O2  GOL A 413     -19.883 -13.433  -4.489  0.84 73.32           O  
HETATM 2283  C3  GOL A 413     -20.325 -11.298  -3.462  0.84 68.32           C  
HETATM 2284  O3  GOL A 413     -21.633 -10.807  -3.610  0.84 80.14           O  
HETATM 2285  C   FMT A 414      -8.728   5.460  11.620  0.73 48.83           C  
HETATM 2286  O1  FMT A 414      -7.510   5.762  11.772  0.73 48.63           O  
HETATM 2287  O2  FMT A 414      -9.431   5.054  12.592  0.73 54.56           O  
HETATM 2288 MG    MG A 415      -6.321 -11.739  14.712  1.00 33.90          MG2+
CONECT 2222 2223 2224
CONECT 2223 2222
CONECT 2224 2222 2225
CONECT 2225 2224 2226
CONECT 2226 2225 2227
CONECT 2227 2226 2228
CONECT 2228 2227
CONECT 2229 2230 2231
CONECT 2230 2229
CONECT 2231 2229 2232 2233
CONECT 2232 2231
CONECT 2233 2231 2234
CONECT 2234 2233
CONECT 2235 2236 2237
CONECT 2236 2235
CONECT 2237 2235
CONECT 2238 2239 2240
CONECT 2239 2238
CONECT 2240 2238 2241 2242
CONECT 2241 2240
CONECT 2242 2240 2243
CONECT 2243 2242
CONECT 2244 2245 2246
CONECT 2245 2244
CONECT 2246 2244
CONECT 2247 2248 2249
CONECT 2248 2247
CONECT 2249 2247
CONECT 2250 2251 2252
CONECT 2251 2250
CONECT 2252 2250
CONECT 2253 2254 2255
CONECT 2254 2253
CONECT 2255 2253 2256 2257
CONECT 2256 2255
CONECT 2257 2255 2258
CONECT 2258 2257
CONECT 2259 2260 2261
CONECT 2260 2259
CONECT 2261 2259 2262 2263
CONECT 2262 2261
CONECT 2263 2261 2264
CONECT 2264 2263
CONECT 2265 2266 2267
CONECT 2266 2265
CONECT 2267 2265 2268 2269
CONECT 2268 2267
CONECT 2269 2267 2270
CONECT 2270 2269
CONECT 2271 2272 2273
CONECT 2272 2271
CONECT 2273 2271 2274
CONECT 2274 2273
CONECT 2275 2276 2277
CONECT 2276 2275
CONECT 2277 2275 2278
CONECT 2278 2277
CONECT 2279 2280 2281
CONECT 2280 2279
CONECT 2281 2279 2282 2283
CONECT 2282 2281
CONECT 2283 2281 2284
CONECT 2284 2283
CONECT 2285 2286 2287
CONECT 2286 2285
CONECT 2287 2285
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: April 25th, 2023.