CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 22011011264645204

Job options:

ID        	=	 22011011264645204
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   THR A   6      12.553   8.193 -19.771  1.00 76.56           N  
ANISOU    1  N   THR A   6     8266  13324   7500  -1948   2707  -3829       N  
ATOM      2  CA  THR A   6      12.157   8.234 -18.369  1.00 79.27           C  
ANISOU    2  CA  THR A   6     8585  13233   8300  -1828   2565  -3489       C  
ATOM      3  C   THR A   6      11.538   9.584 -18.015  1.00 83.03           C  
ANISOU    3  C   THR A   6     8913  14099   8534  -1640   2206  -2940       C  
ATOM      4  O   THR A   6      11.471  10.484 -18.852  1.00 82.23           O  
ANISOU    4  O   THR A   6     8753  14539   7950  -1580   2070  -2776       O  
ATOM      5  CB  THR A   6      13.352   7.954 -17.436  1.00 88.95           C  
ANISOU    5  CB  THR A   6     9929  13751  10116  -1525   2777  -3294       C  
ATOM      7  CG2 THR A   6      14.397   9.050 -17.564  1.00 66.94           C  
ANISOU    7  CG2 THR A   6     7103  11098   7232  -1220   2764  -2894       C  
ATOM      6  OG1 THR A   6      12.898   7.889 -16.079  1.00103.22           O  
ANISOU    6  OG1 THR A   6    11726  15188  12305  -1447   2644  -2997       O  
ATOM      8  N   ARG A   7      11.091   9.720 -16.771  1.00 82.77           N  
ANISOU    8  N   ARG A   7     8842  13777   8832  -1525   2070  -2648       N  
ATOM      9  CA  ARG A   7      10.418  10.935 -16.329  1.00 62.80           C  
ANISOU    9  CA  ARG A   7     6189  11552   6118  -1310   1758  -2182       C  
ATOM     10  C   ARG A   7      11.177  11.624 -15.202  1.00 82.95           C  
ANISOU   10  C   ARG A   7     8836  13650   9031   -967   1739  -1735       C  
ATOM     11  O   ARG A   7      12.042  11.024 -14.565  1.00 98.31           O  
ANISOU   11  O   ARG A   7    10882  15073  11398   -915   1929  -1764       O  
ATOM     12  CB  ARG A   7       8.996  10.612 -15.868  1.00 65.79           C  
ANISOU   12  CB  ARG A   7     6378  12159   6460  -1495   1588  -2262       C  
ATOM     13  CG  ARG A   7       8.135   9.953 -16.930  1.00 72.04           C  
ANISOU   13  CG  ARG A   7     7023  13484   6864  -1906   1560  -2730       C  
ATOM     14  CD  ARG A   7       7.760  10.931 -18.030  1.00 74.83           C  
ANISOU   14  CD  ARG A   7     7240  14600   6591  -1808   1331  -2595       C  
ATOM     15  NE  ARG A   7       6.945  12.035 -17.532  1.00 78.69           N  
ANISOU   15  NE  ARG A   7     7549  15408   6941  -1495   1031  -2123       N  
ATOM     16  CZ  ARG A   7       6.351  12.933 -18.310  1.00 76.46           C  
ANISOU   16  CZ  ARG A   7     7110  15807   6134  -1337    780  -1908       C  
ATOM     17  NH1 ARG A   7       6.478  12.856 -19.627  1.00 75.61           N1+
ANISOU   17  NH1 ARG A   7     6995  16191   5542  -1507    778  -2112       N1+
ATOM     18  NH2 ARG A   7       5.628  13.905 -17.775  1.00 70.66           N  
ANISOU   18  NH2 ARG A   7     6233  15276   5340   -980    541  -1484       N  
ATOM     19  N   VAL A   8      10.846  12.889 -14.964  1.00 56.53           N  
ANISOU   19  N   VAL A   8     5460  10514   5507   -724   1504  -1329       N  
ATOM     20  CA  VAL A   8      11.413  13.643 -13.853  1.00 63.04           C  
ANISOU   20  CA  VAL A   8     6379  10951   6620   -444   1450   -948       C  
ATOM     21  C   VAL A   8      10.335  14.484 -13.185  1.00 59.03           C  
ANISOU   21  C   VAL A   8     5795  10624   6009   -249   1198   -681       C  
ATOM     22  O   VAL A   8       9.283  14.741 -13.773  1.00 71.88           O  
ANISOU   22  O   VAL A   8     7278  12747   7288   -260   1044   -700       O  
ATOM     23  CB  VAL A   8      12.553  14.581 -14.308  1.00 70.76           C  
ANISOU   23  CB  VAL A   8     7489  11874   7522   -308   1491   -705       C  
ATOM     24  CG1 VAL A   8      13.789  13.784 -14.702  1.00 54.43           C  
ANISOU   24  CG1 VAL A   8     5452   9592   5637   -423   1775   -934       C  
ATOM     25  CG2 VAL A   8      12.088  15.473 -15.450  1.00 82.91           C  
ANISOU   25  CG2 VAL A   8     9032  13917   8555   -278   1359   -564       C  
ATOM     26  N   PHE A   9      10.605  14.908 -11.954  1.00 54.19           N  
ANISOU   26  N   PHE A   9     5259   9653   5678    -51   1159   -447       N  
ATOM     27  CA  PHE A   9       9.704  15.793 -11.227  1.00 57.45           C  
ANISOU   27  CA  PHE A   9     5632  10185   6013    197    960   -211       C  
ATOM     28  C   PHE A   9      10.074  17.246 -11.476  1.00 57.13           C  
ANISOU   28  C   PHE A   9     5770  10114   5824    463    845    108       C  
ATOM     29  O   PHE A   9      11.255  17.589 -11.573  1.00 55.78           O  
ANISOU   29  O   PHE A   9     5772   9655   5768    442    930    205       O  
ATOM     30  CB  PHE A   9       9.770  15.521  -9.723  1.00 68.29           C  
ANISOU   30  CB  PHE A   9     7021  11206   7717    263    987   -150       C  
ATOM     31  CG  PHE A   9       9.293  14.157  -9.328  1.00 78.20           C  
ANISOU   31  CG  PHE A   9     8140  12431   9140      9   1106   -379       C  
ATOM     32  CD1 PHE A   9      10.176  13.093  -9.257  1.00 84.01           C  
ANISOU   32  CD1 PHE A   9     8959  12799  10164   -168   1306   -526       C  
ATOM     33  CD2 PHE A   9       7.962  13.941  -9.013  1.00 65.48           C  
ANISOU   33  CD2 PHE A   9     6319  11148   7414    -47   1037   -430       C  
ATOM     34  CE1 PHE A   9       9.740  11.837  -8.887  1.00 83.84           C  
ANISOU   34  CE1 PHE A   9     8880  12647  10329   -409   1439   -705       C  
ATOM     35  CE2 PHE A   9       7.520  12.687  -8.641  1.00 73.73           C  
ANISOU   35  CE2 PHE A   9     7262  12126   8625   -353   1170   -620       C  
ATOM     36  CZ  PHE A   9       8.410  11.633  -8.579  1.00 82.99           C  
ANISOU   36  CZ  PHE A   9     8589  12840  10104   -540   1374   -750       C  
ATOM     37  N   LYS A  10       9.062  18.099 -11.571  1.00 55.47           N  
ANISOU   37  N   LYS A  10     5512  10195   5369    713    665    281       N  
ATOM     38  CA  LYS A  10       9.294  19.532 -11.660  1.00 61.49           C  
ANISOU   38  CA  LYS A  10     6509  10817   6039   1008    565    616       C  
ATOM     39  C   LYS A  10       8.251  20.316 -10.875  1.00 68.65           C  
ANISOU   39  C   LYS A  10     7390  11777   6915   1384    415    767       C  
ATOM     40  O   LYS A  10       7.107  19.884 -10.731  1.00 70.29           O  
ANISOU   40  O   LYS A  10     7312  12385   7011   1437    347    659       O  
ATOM     41  CB  LYS A  10       9.338  20.002 -13.116  1.00 71.73           C  
ANISOU   41  CB  LYS A  10     7855  12432   6966   1006    527    757       C  
ATOM     42  CG  LYS A  10       7.990  20.071 -13.809  1.00 56.74           C  
ANISOU   42  CG  LYS A  10     5717  11162   4680   1156    352    785       C  
ATOM     43  CD  LYS A  10       8.118  20.731 -15.170  1.00 60.25           C  
ANISOU   43  CD  LYS A  10     6264  11912   4717   1216    293   1027       C  
ATOM     44  CE  LYS A  10       6.761  20.937 -15.818  1.00 71.38           C  
ANISOU   44  CE  LYS A  10     7406  14015   5701   1439     69   1123       C  
ATOM     45  NZ  LYS A  10       6.884  21.504 -17.194  1.00 74.43           N1+
ANISOU   45  NZ  LYS A  10     7885  14775   5622   1491      1   1394       N1+
ATOM     46  N   LYS A  11       8.660  21.466 -10.353  1.00 63.28           N  
ANISOU   46  N   LYS A  11     7005  10698   6341   1630    381    991       N  
ATOM     47  CA  LYS A  11       7.741  22.331  -9.626  1.00 69.30           C  
ANISOU   47  CA  LYS A  11     7801  11451   7080   2055    271   1114       C  
ATOM     48  C   LYS A  11       8.154  23.787  -9.774  1.00 71.53           C  
ANISOU   48  C   LYS A  11     8488  11330   7359   2325    230   1409       C  
ATOM     49  O   LYS A  11       9.320  24.131  -9.599  1.00 77.47           O  
ANISOU   49  O   LYS A  11     9522  11619   8292   2131    307   1449       O  
ATOM     50  CB  LYS A  11       7.680  21.942  -8.150  1.00 71.72           C  
ANISOU   50  CB  LYS A  11     8054  11564   7631   2045    325    940       C  
ATOM     51  CG  LYS A  11       6.618  22.689  -7.361  1.00 69.82           C  
ANISOU   51  CG  LYS A  11     7787  11409   7334   2493    253    992       C  
ATOM     52  CD  LYS A  11       6.516  22.148  -5.947  1.00 78.04           C  
ANISOU   52  CD  LYS A  11     8732  12378   8540   2429    329    808       C  
ATOM     53  CE  LYS A  11       5.433  22.855  -5.155  1.00 52.22           C  
ANISOU   53  CE  LYS A  11     5401   9258   5182   2888    299    816       C  
ATOM     54  NZ  LYS A  11       5.292  22.267  -3.799  1.00 65.43           N1+
ANISOU   54  NZ  LYS A  11     6958  10955   6947   2795    392    650       N1+
ATOM     55  N   ALA A  12       7.189  24.640 -10.094  1.00 65.02           N  
ANISOU   55  N   ALA A  12     7685  10684   6336   2773    112   1625       N  
ATOM     56  CA  ALA A  12       7.485  26.037 -10.379  1.00 80.03           C  
ANISOU   56  CA  ALA A  12    10023  12154   8230   3057     85   1954       C  
ATOM     57  C   ALA A  12       7.059  26.967  -9.249  1.00 79.44           C  
ANISOU   57  C   ALA A  12    10176  11683   8324   3483     74   1954       C  
ATOM     58  O   ALA A  12       6.122  26.675  -8.509  1.00 96.12           O  
ANISOU   58  O   ALA A  12    12018  14076  10428   3724     48   1787       O  
ATOM     59  CB  ALA A  12       6.830  26.457 -11.686  1.00 65.18           C  
ANISOU   59  CB  ALA A  12     8089  10688   5990   3320    -31   2275       C  
ATOM     60  N   SER A  13       7.765  28.084  -9.123  1.00 73.73           N  
ANISOU   60  N   SER A  13     9959  10307   7749   3544    115   2122       N  
ATOM     61  CA  SER A  13       7.376  29.145  -8.208  1.00 81.83           C  
ANISOU   61  CA  SER A  13    11303  10872   8916   3984    121   2116       C  
ATOM     62  C   SER A  13       6.061  29.743  -8.697  1.00 98.53           C  
ANISOU   62  C   SER A  13    13334  13281  10821   4654     24   2370       C  
ATOM     63  O   SER A  13       5.757  29.664  -9.887  1.00113.78           O  
ANISOU   63  O   SER A  13    15121  15611  12500   4724    -63   2654       O  
ATOM     64  CB  SER A  13       8.463  30.219  -8.166  1.00 89.07           C  
ANISOU   64  CB  SER A  13    12821  10991  10032   3819    194   2248       C  
ATOM     65  OG  SER A  13       8.632  30.820  -9.438  1.00 98.78           O  
ANISOU   65  OG  SER A  13    14275  12136  11121   3865    181   2674       O  
ATOM     66  N   PRO A  14       5.272  30.332  -7.781  1.00 95.14           N  
ANISOU   66  N   PRO A  14    12966  12714  10468   5174     37   2265       N  
ATOM     67  CA  PRO A  14       3.985  30.948  -8.132  1.00 93.55           C  
ANISOU   67  CA  PRO A  14    12636  12806  10103   5843    -36   2469       C  
ATOM     68  C   PRO A  14       4.083  31.917  -9.310  1.00100.90           C  
ANISOU   68  C   PRO A  14    13907  13469  10961   5981    -80   2900       C  
ATOM     69  O   PRO A  14       3.175  31.975 -10.140  1.00104.67           O  
ANISOU   69  O   PRO A  14    14088  14470  11210   6209   -177   3082       O  
ATOM     70  CB  PRO A  14       3.611  31.709  -6.860  1.00 81.85           C  
ANISOU   70  CB  PRO A  14    11389  10890   8820   6172     73   2204       C  
ATOM     71  CG  PRO A  14       4.234  30.916  -5.769  1.00 76.45           C  
ANISOU   71  CG  PRO A  14    10631  10160   8258   5830    143   1847       C  
ATOM     72  CD  PRO A  14       5.525  30.383  -6.328  1.00 72.36           C  
ANISOU   72  CD  PRO A  14    10217   9473   7802   5106    138   1889       C  
ATOM     73  N   ASN A  15       5.183  32.658  -9.381  1.00 96.62           N  
ANISOU   73  N   ASN A  15    13974  12134  10603   5806     -4   3065       N  
ATOM     74  CA  ASN A  15       5.389  33.627 -10.452  1.00101.60           C  
ANISOU   74  CA  ASN A  15    14982  12429  11191   5868    -16   3504       C  
ATOM     75  C   ASN A  15       6.063  33.032 -11.690  1.00 97.05           C  
ANISOU   75  C   ASN A  15    14305  12207  10362   5449    -61   3795       C  
ATOM     76  O   ASN A  15       6.285  33.726 -12.683  1.00103.37           O  
ANISOU   76  O   ASN A  15    15376  12828  11071   5431    -68   4189       O  
ATOM     77  CB  ASN A  15       6.150  34.859  -9.935  1.00 93.90           C  
ANISOU   77  CB  ASN A  15    14741  10389  10548   5840    116   3539       C  
ATOM     78  CG  ASN A  15       7.593  34.555  -9.544  1.00 89.40           C  
ANISOU   78  CG  ASN A  15    14486   9346  10138   5256    220   3436       C  
ATOM     80  ND2 ASN A  15       7.899  33.287  -9.300  1.00 82.95           N  
ANISOU   80  ND2 ASN A  15    13173   9086   9258   4803    198   3119       N  
ATOM     79  OD1 ASN A  15       8.422  35.461  -9.468  1.00129.70           O  
ANISOU   79  OD1 ASN A  15    20176  13644  15461   5026    325   3531       O  
ATOM     81  N   GLY A  16       6.390  31.745 -11.618  1.00 91.55           N  
ANISOU   81  N   GLY A  16    13204  12023   9559   5057    -72   3559       N  
ATOM     82  CA  GLY A  16       6.963  31.033 -12.747  1.00 84.78           C  
ANISOU   82  CA  GLY A  16    12153  11607   8454   4567    -81   3671       C  
ATOM     83  C   GLY A  16       8.437  31.302 -12.987  1.00 90.96           C  
ANISOU   83  C   GLY A  16    13338  11831   9393   3992     76   3749       C  
ATOM     84  O   GLY A  16       9.072  30.615 -13.787  1.00110.96           O  
ANISOU   84  O   GLY A  16    15691  14715  11753   3529    121   3751       O  
ATOM     85  N   LYS A  17       8.984  32.292 -12.289  1.00 89.79           N  
ANISOU   85  N   LYS A  17    13716  10837   9563   4001    172   3780       N  
ATOM     86  CA  LYS A  17      10.372  32.707 -12.484  1.00 91.07           C  
ANISOU   86  CA  LYS A  17    14266  10450   9887   3433    323   3881       C  
ATOM     87  C   LYS A  17      11.376  31.594 -12.197  1.00 85.48           C  
ANISOU   87  C   LYS A  17    13220   9983   9275   2769    402   3488       C  
ATOM     88  O   LYS A  17      12.483  31.592 -12.737  1.00 76.55           O  
ANISOU   88  O   LYS A  17    12185   8750   8152   2263    523   3595       O  
ATOM     89  CB  LYS A  17      10.688  33.926 -11.615  1.00 93.41           C  
ANISOU   89  CB  LYS A  17    15169   9791  10532   3523    400   3878       C  
ATOM     90  N   LEU A  18      10.984  30.650 -11.349  1.00 85.77           N  
ANISOU   90  N   LEU A  18    12853  10352   9384   2794    348   3060       N  
ATOM     91  CA  LEU A  18      11.873  29.571 -10.941  1.00 66.75           C  
ANISOU   91  CA  LEU A  18    10136   8123   7103   2264    418   2703       C  
ATOM     92  C   LEU A  18      11.191  28.222 -11.124  1.00 73.00           C  
ANISOU   92  C   LEU A  18    10378   9640   7721   2297    362   2479       C  
ATOM     93  O   LEU A  18      10.014  28.072 -10.802  1.00 72.06           O  
ANISOU   93  O   LEU A  18    10069   9796   7516   2696    259   2409       O  
ATOM     94  CB  LEU A  18      12.265  29.755  -9.477  1.00 79.15           C  
ANISOU   94  CB  LEU A  18    11836   9248   8989   2169    429   2384       C  
ATOM     95  CG  LEU A  18      13.744  29.599  -9.134  1.00 90.02           C  
ANISOU   95  CG  LEU A  18    13249  10381  10574   1572    523   2239       C  
ATOM     96  CD1 LEU A  18      14.569  30.594  -9.924  1.00 98.16           C  
ANISOU   96  CD1 LEU A  18    14675  11003  11617   1305    620   2572       C  
ATOM     97  CD2 LEU A  18      13.961  29.782  -7.642  1.00101.47           C  
ANISOU   97  CD2 LEU A  18    14796  11505  12255   1529    486   1912       C  
ATOM     98  N   THR A  19      11.923  27.241 -11.643  1.00 65.98           N  
ANISOU   98  N   THR A  19     9228   9054   6787   1869    449   2350       N  
ATOM     99  CA  THR A  19      11.370  25.896 -11.785  1.00 76.54           C  
ANISOU   99  CA  THR A  19    10098  10976   8006   1819    427   2082       C  
ATOM    100  C   THR A  19      12.381  24.813 -11.411  1.00 79.46           C  
ANISOU  100  C   THR A  19    10264  11343   8585   1386    554   1780       C  
ATOM    101  O   THR A  19      13.370  24.605 -12.112  1.00 83.41           O  
ANISOU  101  O   THR A  19    10763  11867   9061   1068    681   1811       O  
ATOM    102  CB  THR A  19      10.850  25.636 -13.213  1.00 83.27           C  
ANISOU  102  CB  THR A  19    10788  12394   8456   1859    392   2239       C  
ATOM    104  CG2 THR A  19      10.060  24.337 -13.260  1.00 75.95           C  
ANISOU  104  CG2 THR A  19     9406  12038   7415   1810    349   1914       C  
ATOM    103  OG1 THR A  19      10.004  26.718 -13.624  1.00 93.34           O  
ANISOU  103  OG1 THR A  19    12261  13679   9525   2312    263   2609       O  
ATOM    105  N   VAL A  20      12.119  24.123 -10.305  1.00 61.87           N  
ANISOU  105  N   VAL A  20     7853   9107   6548   1407    533   1511       N  
ATOM    106  CA  VAL A  20      13.004  23.066  -9.823  1.00 51.03           C  
ANISOU  106  CA  VAL A  20     6290   7707   5394   1088    639   1268       C  
ATOM    107  C   VAL A  20      12.728  21.734 -10.507  1.00 63.45           C  
ANISOU  107  C   VAL A  20     7545   9702   6862    945    712   1071       C  
ATOM    108  O   VAL A  20      11.577  21.312 -10.624  1.00 59.68           O  
ANISOU  108  O   VAL A  20     6891   9550   6234   1081    642    988       O  
ATOM    109  CB  VAL A  20      12.865  22.864  -8.304  1.00 61.07           C  
ANISOU  109  CB  VAL A  20     7527   8790   6886   1167    590   1109       C  
ATOM    110  CG1 VAL A  20      13.785  21.749  -7.826  1.00 77.88           C  
ANISOU  110  CG1 VAL A  20     9457  10903   9230    895    686    931       C  
ATOM    111  CG2 VAL A  20      13.180  24.144  -7.579  1.00 72.51           C  
ANISOU  111  CG2 VAL A  20     9313   9807   8430   1264    528   1211       C  
ATOM    112  N   TYR A  21      13.799  21.081 -10.949  1.00 54.99           N  
ANISOU  112  N   TYR A  21     6392   8626   5874    660    865    972       N  
ATOM    113  CA  TYR A  21      13.720  19.751 -11.539  1.00 57.44           C  
ANISOU  113  CA  TYR A  21     6457   9226   6142    498    982    714       C  
ATOM    114  C   TYR A  21      14.536  18.752 -10.720  1.00 64.20           C  
ANISOU  114  C   TYR A  21     7190   9864   7341    369   1100    526       C  
ATOM    115  O   TYR A  21      15.722  18.978 -10.447  1.00 75.56           O  
ANISOU  115  O   TYR A  21     8664  11089   8957    277   1168    593       O  
ATOM    116  CB  TYR A  21      14.244  19.770 -12.976  1.00 49.35           C  
ANISOU  116  CB  TYR A  21     5440   8446   4866    335   1105    739       C  
ATOM    117  CG  TYR A  21      13.332  20.435 -13.981  1.00 74.93           C  
ANISOU  117  CG  TYR A  21     8743  12039   7689    463    989    920       C  
ATOM    118  CD1 TYR A  21      13.262  21.819 -14.080  1.00 72.00           C  
ANISOU  118  CD1 TYR A  21     8631  11518   7208    642    886   1296       C  
ATOM    119  CD2 TYR A  21      12.557  19.678 -14.850  1.00 70.08           C  
ANISOU  119  CD2 TYR A  21     7938  11911   6779    401    980    719       C  
ATOM    120  CE1 TYR A  21      12.435  22.428 -15.007  1.00 73.92           C  
ANISOU  120  CE1 TYR A  21     8930  12098   7057    825    769   1529       C  
ATOM    121  CE2 TYR A  21      11.730  20.277 -15.780  1.00 68.00           C  
ANISOU  121  CE2 TYR A  21     7685  12069   6083    538    840    912       C  
ATOM    122  CZ  TYR A  21      11.673  21.652 -15.855  1.00 71.13           C  
ANISOU  122  CZ  TYR A  21     8329  12320   6375    784    732   1349       C  
ATOM    123  OH  TYR A  21      10.849  22.252 -16.781  1.00 77.40           O  
ANISOU  123  OH  TYR A  21     9134  13545   6730    986    582   1607       O  
ATOM    124  N   LEU A  22      13.895  17.649 -10.338  1.00 67.08           N  
ANISOU  124  N   LEU A  22     7398  10298   7793    355   1124    317       N  
ATOM    125  CA  LEU A  22      14.562  16.571  -9.611  1.00 61.08           C  
ANISOU  125  CA  LEU A  22     6539   9314   7353    280   1246    182       C  
ATOM    126  C   LEU A  22      14.315  15.223 -10.277  1.00 56.89           C  
ANISOU  126  C   LEU A  22     5888   8890   6837    128   1412   -110       C  
ATOM    127  O   LEU A  22      13.318  15.039 -10.973  1.00 64.32           O  
ANISOU  127  O   LEU A  22     6780  10121   7538     56   1380   -242       O  
ATOM    128  CB  LEU A  22      14.080  16.513  -8.160  1.00 58.98           C  
ANISOU  128  CB  LEU A  22     6271   8893   7245    402   1138    248       C  
ATOM    129  CG  LEU A  22      14.595  17.581  -7.198  1.00 58.81           C  
ANISOU  129  CG  LEU A  22     6379   8678   7289    515   1010    443       C  
ATOM    130  CD1 LEU A  22      13.945  17.405  -5.841  1.00 50.96           C  
ANISOU  130  CD1 LEU A  22     5367   7634   6362    634    926    462       C  
ATOM    131  CD2 LEU A  22      16.107  17.509  -7.081  1.00 49.17           C  
ANISOU  131  CD2 LEU A  22     5125   7294   6262    414   1084    482       C  
ATOM    132  N   GLY A  23      15.222  14.279 -10.050  1.00 59.83           N  
ANISOU  132  N   GLY A  23     6210   9031   7493     86   1586   -221       N  
ATOM    133  CA  GLY A  23      15.102  12.949 -10.620  1.00 54.90           C  
ANISOU  133  CA  GLY A  23     5536   8378   6947    -49   1786   -537       C  
ATOM    134  C   GLY A  23      14.188  12.042  -9.818  1.00 51.13           C  
ANISOU  134  C   GLY A  23     5044   7751   6631   -103   1781   -616       C  
ATOM    135  O   GLY A  23      13.557  11.140 -10.367  1.00 75.21           O  
ANISOU  135  O   GLY A  23     8082  10846   9650   -299   1889   -902       O  
ATOM    136  N   LYS A  24      14.115  12.283  -8.514  1.00 63.51           N  
ANISOU  136  N   LYS A  24     6621   9161   8351     32   1665   -374       N  
ATOM    137  CA  LYS A  24      13.278  11.474  -7.637  1.00 70.21           C  
ANISOU  137  CA  LYS A  24     7455   9885   9335    -32   1678   -378       C  
ATOM    138  C   LYS A  24      13.012  12.187  -6.317  1.00 59.21           C  
ANISOU  138  C   LYS A  24     6062   8503   7932    134   1503    -93       C  
ATOM    139  O   LYS A  24      13.706  13.142  -5.971  1.00 72.42           O  
ANISOU  139  O   LYS A  24     7774  10168   9575    293   1389     80       O  
ATOM    140  CB  LYS A  24      13.930  10.114  -7.385  1.00 77.70           C  
ANISOU  140  CB  LYS A  24     8453  10426  10643    -59   1902   -460       C  
ATOM    141  CG  LYS A  24      15.381  10.186  -6.941  1.00 51.04           C  
ANISOU  141  CG  LYS A  24     5069   6833   7490    176   1937   -277       C  
ATOM    142  CD  LYS A  24      15.935   8.793  -6.706  1.00 69.52           C  
ANISOU  142  CD  LYS A  24     7461   8755  10199    235   2166   -328       C  
ATOM    143  CE  LYS A  24      17.338   8.836  -6.130  1.00 65.42           C  
ANISOU  143  CE  LYS A  24     6856   8105   9894    523   2169    -95       C  
ATOM    144  NZ  LYS A  24      17.776   7.488  -5.676  1.00 77.99           N1+
ANISOU  144  NZ  LYS A  24     8511   9259  11864    678   2367    -44       N1+
ATOM    145  N   ARG A  25      12.005  11.720  -5.586  1.00 58.17           N  
ANISOU  145  N   ARG A  25     5888   8405   7807     62   1498    -68       N  
ATOM    146  CA  ARG A  25      11.628  12.337  -4.318  1.00 52.46           C  
ANISOU  146  CA  ARG A  25     5158   7755   7019    217   1363    160       C  
ATOM    147  C   ARG A  25      12.196  11.560  -3.134  1.00 71.57           C  
ANISOU  147  C   ARG A  25     7624   9887   9683    264   1433    347       C  
ATOM    148  O   ARG A  25      12.468  12.131  -2.078  1.00 80.90           O  
ANISOU  148  O   ARG A  25     8828  11093  10816    428   1316    546       O  
ATOM    149  CB  ARG A  25      10.105  12.422  -4.196  1.00 58.23           C  
ANISOU  149  CB  ARG A  25     5761   8820   7545    136   1320    107       C  
ATOM    150  CG  ARG A  25       9.414  13.124  -5.357  1.00 63.25           C  
ANISOU  150  CG  ARG A  25     6306   9820   7904    131   1225    -35       C  
ATOM    151  CD  ARG A  25       9.567  14.636  -5.282  1.00 53.37           C  
ANISOU  151  CD  ARG A  25     5136   8667   6477    433   1050    116       C  
ATOM    152  NE  ARG A  25       8.869  15.207  -4.131  1.00 60.25           N  
ANISOU  152  NE  ARG A  25     5973   9657   7261    628    970    239       N  
ATOM    153  CZ  ARG A  25       7.577  15.526  -4.120  1.00 67.10           C  
ANISOU  153  CZ  ARG A  25     6662  10911   7920    715    916    215       C  
ATOM    154  NH1 ARG A  25       7.032  16.047  -3.032  1.00 54.24           N1+
ANISOU  154  NH1 ARG A  25     5006   9390   6212    926    881    303       N1+
ATOM    155  NH2 ARG A  25       6.828  15.329  -5.196  1.00 86.26           N  
ANISOU  155  NH2 ARG A  25     8911  13675  10190    601    895     88       N  
ATOM    156  N   ASP A  26      12.366  10.253  -3.310  1.00 59.63           N  
ANISOU  156  N   ASP A  26     6144   8096   8416    125   1626    284       N  
ATOM    157  CA  ASP A  26      12.877   9.403  -2.239  1.00 53.22           C  
ANISOU  157  CA  ASP A  26     5395   6979   7845    204   1707    524       C  
ATOM    158  C   ASP A  26      14.363   9.101  -2.410  1.00 51.68           C  
ANISOU  158  C   ASP A  26     5229   6518   7891    394   1761    584       C  
ATOM    159  O   ASP A  26      14.796   8.584  -3.443  1.00 52.25           O  
ANISOU  159  O   ASP A  26     5323   6424   8107    349   1915    363       O  
ATOM    160  CB  ASP A  26      12.074   8.105  -2.145  1.00 48.71           C  
ANISOU  160  CB  ASP A  26     4880   6192   7436    -50   1910    482       C  
ATOM    161  CG  ASP A  26      10.622   8.345  -1.781  1.00 68.86           C  
ANISOU  161  CG  ASP A  26     7325   9089   9751   -246   1866    471       C  
ATOM    162  OD1 ASP A  26      10.339   9.343  -1.082  1.00 59.47           O  
ANISOU  162  OD1 ASP A  26     6057   8218   8322    -81   1699    611       O  
ATOM    163  OD2 ASP A  26       9.763   7.540  -2.194  1.00 75.12           O1-
ANISOU  163  OD2 ASP A  26     8099   9851  10594   -575   2010    298       O1-
ATOM    164  N   PHE A  27      15.139   9.434  -1.387  1.00 51.13           N  
ANISOU  164  N   PHE A  27     5126   6464   7835    612   1634    864       N  
ATOM    165  CA  PHE A  27      16.575   9.201  -1.419  1.00 56.57           C  
ANISOU  165  CA  PHE A  27     5755   7007   8734    824   1655    962       C  
ATOM    166  C   PHE A  27      16.981   8.157  -0.384  1.00 67.00           C  
ANISOU  166  C   PHE A  27     7106   8073  10279   1003   1718   1282       C  
ATOM    167  O   PHE A  27      16.715   8.299   0.814  1.00 49.74           O  
ANISOU  167  O   PHE A  27     4927   6014   7958   1052   1590   1553       O  
ATOM    168  CB  PHE A  27      17.337  10.518  -1.247  1.00 55.04           C  
ANISOU  168  CB  PHE A  27     5450   7103   8358    908   1434   1010       C  
ATOM    169  CG  PHE A  27      17.085  11.499  -2.358  1.00 53.92           C  
ANISOU  169  CG  PHE A  27     5321   7135   8032    767   1403    764       C  
ATOM    170  CD1 PHE A  27      15.997  12.356  -2.312  1.00 50.23           C  
ANISOU  170  CD1 PHE A  27     4927   6859   7301    675   1288    703       C  
ATOM    171  CD2 PHE A  27      17.922  11.545  -3.462  1.00 64.33           C  
ANISOU  171  CD2 PHE A  27     6570   8445   9427    755   1508    617       C  
ATOM    172  CE1 PHE A  27      15.758  13.250  -3.339  1.00 51.92           C  
ANISOU  172  CE1 PHE A  27     5171   7217   7339    595   1254    546       C  
ATOM    173  CE2 PHE A  27      17.688  12.437  -4.494  1.00 49.19           C  
ANISOU  173  CE2 PHE A  27     4685   6703   7303    622   1487    453       C  
ATOM    174  CZ  PHE A  27      16.606  13.290  -4.432  1.00 50.71           C  
ANISOU  174  CZ  PHE A  27     4976   7049   7241    552   1349    439       C  
ATOM    175  N   VAL A  28      17.616   7.097  -0.870  1.00 52.49           N  
ANISOU  175  N   VAL A  28     5302   5875   8768   1123   1930   1253       N  
ATOM    176  CA  VAL A  28      17.902   5.932  -0.050  1.00 61.76           C  
ANISOU  176  CA  VAL A  28     6564   6693  10208   1322   2041   1577       C  
ATOM    177  C   VAL A  28      19.160   6.094   0.793  1.00 60.94           C  
ANISOU  177  C   VAL A  28     6275   6742  10136   1688   1877   1928       C  
ATOM    178  O   VAL A  28      20.241   6.379   0.276  1.00 63.73           O  
ANISOU  178  O   VAL A  28     6434   7212  10568   1862   1857   1843       O  
ATOM    179  CB  VAL A  28      18.031   4.663  -0.913  1.00 59.84           C  
ANISOU  179  CB  VAL A  28     6482   5913  10341   1342   2369   1381       C  
ATOM    180  CG1 VAL A  28      18.331   3.454  -0.039  1.00 64.52           C  
ANISOU  180  CG1 VAL A  28     7223   6045  11247   1593   2500   1778       C  
ATOM    181  CG2 VAL A  28      16.762   4.447  -1.724  1.00 59.40           C  
ANISOU  181  CG2 VAL A  28     6584   5766  10220    913   2510   1004       C  
ATOM    182  N   ASP A  29      19.002   5.916   2.100  1.00 61.85           N  
ANISOU  182  N   ASP A  29     6420   6927  10155   1784   1756   2329       N  
ATOM    183  CA  ASP A  29      20.132   5.885   3.012  1.00 62.89           C  
ANISOU  183  CA  ASP A  29     6363   7240  10290   2140   1584   2715       C  
ATOM    184  C   ASP A  29      20.662   4.462   3.103  1.00 66.42           C  
ANISOU  184  C   ASP A  29     6900   7195  11141   2479   1800   2998       C  
ATOM    185  O   ASP A  29      19.998   3.575   3.638  1.00 79.92           O  
ANISOU  185  O   ASP A  29     8860   8550  12954   2455   1938   3251       O  
ATOM    186  CB  ASP A  29      19.713   6.382   4.396  1.00 64.16           C  
ANISOU  186  CB  ASP A  29     6522   7770  10085   2094   1344   3017       C  
ATOM    187  CG  ASP A  29      20.847   6.334   5.405  1.00 80.60           C  
ANISOU  187  CG  ASP A  29     8387  10137  12098   2440   1125   3430       C  
ATOM    188  OD1 ASP A  29      20.560   6.296   6.618  1.00 75.05           O  
ANISOU  188  OD1 ASP A  29     7726   9653  11136   2473    989   3773       O  
ATOM    189  OD2 ASP A  29      22.024   6.335   4.989  1.00115.54           O1-
ANISOU  189  OD2 ASP A  29    12570  14634  16698   2676   1087   3415       O1-
ATOM    190  N   HIS A  30      21.861   4.248   2.573  1.00 68.50           N  
ANISOU  190  N   HIS A  30     6960   7424  11643   2803   1850   2963       N  
ATOM    191  CA  HIS A  30      22.493   2.936   2.614  1.00 74.27           C  
ANISOU  191  CA  HIS A  30     7760   7665  12792   3237   2068   3226       C  
ATOM    192  C   HIS A  30      23.411   2.831   3.823  1.00 77.85           C  
ANISOU  192  C   HIS A  30     7976   8421  13181   3671   1829   3796       C  
ATOM    193  O   HIS A  30      24.380   2.071   3.810  1.00 82.83           O  
ANISOU  193  O   HIS A  30     8528   8916  14027   4054   1891   3939       O  
ATOM    194  CB  HIS A  30      23.293   2.690   1.333  1.00 75.53           C  
ANISOU  194  CB  HIS A  30     7799   7653  13248   3417   2295   2854       C  
ATOM    195  CG  HIS A  30      22.526   2.968   0.079  1.00 72.16           C  
ANISOU  195  CG  HIS A  30     7535   7103  12779   2984   2474   2272       C  
ATOM    197  CD2 HIS A  30      22.331   4.116  -0.610  1.00 67.41           C  
ANISOU  197  CD2 HIS A  30     6802   6929  11883   2651   2359   1915       C  
ATOM    196  ND1 HIS A  30      21.844   1.987  -0.609  1.00 83.97           N  
ANISOU  196  ND1 HIS A  30     9380   7987  14538   2850   2806   2010       N  
ATOM    198  CE1 HIS A  30      21.264   2.521  -1.669  1.00 79.64           C  
ANISOU  198  CE1 HIS A  30     8866   7576  13819   2455   2863   1509       C  
ATOM    199  NE2 HIS A  30      21.543   3.811  -1.693  1.00 68.89           N  
ANISOU  199  NE2 HIS A  30     7225   6829  12123   2356   2599   1474       N  
ATOM    200  N   ILE A  31      23.094   3.605   4.860  1.00 89.61           N  
ANISOU  200  N   ILE A  31     9393  10411  14246   3499   1521   4006       N  
ATOM    201  CA  ILE A  31      23.893   3.688   6.086  1.00 98.26           C  
ANISOU  201  CA  ILE A  31    10248  11973  15112   3790   1219   4479       C  
ATOM    202  C   ILE A  31      25.289   4.271   5.858  1.00 95.25           C  
ANISOU  202  C   ILE A  31     9438  12102  14651   3918   1013   4319       C  
ATOM    203  O   ILE A  31      25.633   5.306   6.426  1.00 78.57           O  
ANISOU  203  O   ILE A  31     7066  10615  12173   3775    690   4313       O  
ATOM    204  CB  ILE A  31      24.013   2.328   6.812  1.00 85.63           C  
ANISOU  204  CB  ILE A  31     8885   9998  13655   4066   1329   4920       C  
ATOM    205  CG1 ILE A  31      22.634   1.696   7.000  1.00 85.51           C  
ANISOU  205  CG1 ILE A  31     9310   9442  13738   3851   1573   5077       C  
ATOM    206  CG2 ILE A  31      24.711   2.501   8.151  1.00138.77           C  
ANISOU  206  CG2 ILE A  31    15403  17327  19997   4227    981   5311       C  
ATOM    207  CD1 ILE A  31      22.673   0.355   7.694  1.00 92.47           C  
ANISOU  207  CD1 ILE A  31    10467   9900  14766   4059   1706   5508       C  
ATOM    208  N   ASP A  32      26.089   3.605   5.030  1.00 99.11           N  
ANISOU  208  N   ASP A  32     9858  12326  15471   4162   1210   4171       N  
ATOM    209  CA  ASP A  32      27.420   4.101   4.696  1.00 92.14           C  
ANISOU  209  CA  ASP A  32     8545  11923  14540   4267   1063   4011       C  
ATOM    210  C   ASP A  32      27.344   5.375   3.853  1.00 96.90           C  
ANISOU  210  C   ASP A  32     8959  12828  15029   3900   1027   3582       C  
ATOM    211  O   ASP A  32      28.179   6.267   3.986  1.00108.99           O  
ANISOU  211  O   ASP A  32    10127  14936  16349   3790    784   3509       O  
ATOM    212  CB  ASP A  32      28.243   3.022   3.983  1.00 97.64           C  
ANISOU  212  CB  ASP A  32     9226  12264  15611   4651   1317   3946       C  
ATOM    213  CG  ASP A  32      27.489   2.364   2.840  1.00118.64           C  
ANISOU  213  CG  ASP A  32    12240  14214  18623   4598   1734   3629       C  
ATOM    214  OD1 ASP A  32      26.877   3.085   2.025  1.00117.63           O  
ANISOU  214  OD1 ASP A  32    12143  14089  18464   4260   1830   3261       O  
ATOM    215  OD2 ASP A  32      27.511   1.118   2.757  1.00141.11           O1-
ANISOU  215  OD2 ASP A  32    15347  16498  21771   4885   1968   3732       O1-
ATOM    216  N   LEU A  33      26.337   5.452   2.988  1.00 83.73           N  
ANISOU  216  N   LEU A  33     7542  10769  13504   3689   1277   3302       N  
ATOM    217  CA  LEU A  33      26.135   6.633   2.158  1.00 70.00           C  
ANISOU  217  CA  LEU A  33     5707   9271  11619   3301   1263   2895       C  
ATOM    218  C   LEU A  33      24.656   6.841   1.841  1.00 70.43           C  
ANISOU  218  C   LEU A  33     6201   9011  11547   2896   1360   2640       C  
ATOM    219  O   LEU A  33      23.872   5.894   1.826  1.00 81.84           O  
ANISOU  219  O   LEU A  33     7961   9968  13167   2938   1566   2689       O  
ATOM    220  CB  LEU A  33      26.949   6.533   0.862  1.00 81.17           C  
ANISOU  220  CB  LEU A  33     6925  10664  13252   3378   1500   2577       C  
ATOM    221  CG  LEU A  33      26.461   5.594  -0.248  1.00 77.89           C  
ANISOU  221  CG  LEU A  33     6796   9648  13152   3452   1917   2297       C  
ATOM    222  CD1 LEU A  33      25.651   6.350  -1.297  1.00 87.58           C  
ANISOU  222  CD1 LEU A  33     8214  10866  14195   2965   2008   1842       C  
ATOM    223  CD2 LEU A  33      27.629   4.871  -0.900  1.00 76.86           C  
ANISOU  223  CD2 LEU A  33     6507   9476  13219   3761   2088   2173       C  
ATOM    224  N   VAL A  34      24.281   8.090   1.591  1.00 65.77           N  
ANISOU  224  N   VAL A  34     5622   8708  10661   2501   1213   2377       N  
ATOM    225  CA  VAL A  34      22.925   8.407   1.171  1.00 76.92           C  
ANISOU  225  CA  VAL A  34     7370   9921  11934   2158   1291   2120       C  
ATOM    226  C   VAL A  34      22.965   8.822  -0.295  1.00 66.56           C  
ANISOU  226  C   VAL A  34     6054   8577  10658   1967   1460   1717       C  
ATOM    227  O   VAL A  34      23.954   9.398  -0.747  1.00 57.51           O  
ANISOU  227  O   VAL A  34     4646   7703   9502   1967   1424   1641       O  
ATOM    228  CB  VAL A  34      22.323   9.544   2.028  1.00 61.24           C  
ANISOU  228  CB  VAL A  34     5450   8260   9558   1912   1007   2144       C  
ATOM    229  CG1 VAL A  34      20.872   9.808   1.645  1.00 51.59           C  
ANISOU  229  CG1 VAL A  34     4523   6878   8202   1639   1094   1917       C  
ATOM    230  CG2 VAL A  34      22.430   9.205   3.510  1.00 57.24           C  
ANISOU  230  CG2 VAL A  34     4906   7912   8932   2098    823   2545       C  
ATOM    231  N   ASP A  35      21.911   8.501  -1.041  1.00 70.98           N  
ANISOU  231  N   ASP A  35     6880   8854  11236   1785   1648   1473       N  
ATOM    232  CA  ASP A  35      21.784   8.980  -2.411  1.00 65.80           C  
ANISOU  232  CA  ASP A  35     6245   8247  10509   1573   1777   1107       C  
ATOM    233  C   ASP A  35      21.894  10.495  -2.400  1.00 63.11           C  
ANISOU  233  C   ASP A  35     5827   8284   9868   1358   1544   1077       C  
ATOM    234  O   ASP A  35      21.235  11.161  -1.603  1.00 58.98           O  
ANISOU  234  O   ASP A  35     5409   7865   9134   1250   1338   1169       O  
ATOM    235  CB  ASP A  35      20.439   8.574  -3.017  1.00 55.22           C  
ANISOU  235  CB  ASP A  35     5181   6672   9127   1350   1923    868       C  
ATOM    236  CG  ASP A  35      20.292   7.075  -3.173  1.00 67.94           C  
ANISOU  236  CG  ASP A  35     6935   7818  11060   1472   2196    823       C  
ATOM    237  OD1 ASP A  35      21.313   6.362  -3.096  1.00 71.71           O  
ANISOU  237  OD1 ASP A  35     7306   8123  11816   1791   2321    931       O  
ATOM    238  OD2 ASP A  35      19.150   6.613  -3.385  1.00 71.86           O1-
ANISOU  238  OD2 ASP A  35     7648   8117  11540   1245   2294    671       O1-
ATOM    239  N   PRO A  36      22.747  11.046  -3.271  1.00 58.22           N  
ANISOU  239  N   PRO A  36     5035   7855   9230   1294   1599    947       N  
ATOM    240  CA  PRO A  36      22.886  12.502  -3.344  1.00 56.24           C  
ANISOU  240  CA  PRO A  36     4765   7876   8727   1046   1412    928       C  
ATOM    241  C   PRO A  36      21.615  13.132  -3.893  1.00 56.71           C  
ANISOU  241  C   PRO A  36     5112   7878   8559    834   1397    771       C  
ATOM    242  O   PRO A  36      20.909  12.500  -4.679  1.00 58.34           O  
ANISOU  242  O   PRO A  36     5437   7947   8782    816   1573    600       O  
ATOM    243  CB  PRO A  36      24.043  12.691  -4.328  1.00 62.51           C  
ANISOU  243  CB  PRO A  36     5312   8856   9584   1009   1563    835       C  
ATOM    244  CG  PRO A  36      24.046  11.448  -5.153  1.00 58.12           C  
ANISOU  244  CG  PRO A  36     4756   8098   9229   1196   1874    671       C  
ATOM    245  CD  PRO A  36      23.623  10.351  -4.229  1.00 53.18           C  
ANISOU  245  CD  PRO A  36     4227   7178   8803   1442   1869    811       C  
ATOM    246  N   VAL A  37      21.318  14.354  -3.465  1.00 54.58           N  
ANISOU  246  N   VAL A  37     4948   7717   8074    687   1186    817       N  
ATOM    247  CA  VAL A  37      20.172  15.079  -3.993  1.00 42.47           C  
ANISOU  247  CA  VAL A  37     3657   6160   6321    561   1158    711       C  
ATOM    248  C   VAL A  37      20.626  15.978  -5.135  1.00 55.92           C  
ANISOU  248  C   VAL A  37     5377   7960   7910    386   1213    650       C  
ATOM    249  O   VAL A  37      21.046  17.116  -4.922  1.00 53.67           O  
ANISOU  249  O   VAL A  37     5141   7716   7535    251   1084    722       O  
ATOM    250  CB  VAL A  37      19.469  15.908  -2.908  1.00 44.05           C  
ANISOU  250  CB  VAL A  37     4015   6369   6354    563    935    784       C  
ATOM    251  CG1 VAL A  37      18.287  16.663  -3.500  1.00 44.78           C  
ANISOU  251  CG1 VAL A  37     4323   6455   6236    520    916    696       C  
ATOM    252  CG2 VAL A  37      19.006  15.005  -1.773  1.00 53.41           C  
ANISOU  252  CG2 VAL A  37     5179   7516   7601    712    905    884       C  
ATOM    253  N   ASP A  38      20.555  15.442  -6.348  1.00 73.18           N  
ANISOU  253  N   ASP A  38     7540  10176  10088    362   1422    511       N  
ATOM    254  CA  ASP A  38      20.973  16.167  -7.540  1.00 73.56           C  
ANISOU  254  CA  ASP A  38     7601  10366   9984    194   1517    483       C  
ATOM    255  C   ASP A  38      19.762  16.641  -8.329  1.00 69.19           C  
ANISOU  255  C   ASP A  38     7274   9855   9160    144   1493    432       C  
ATOM    256  O   ASP A  38      18.783  15.912  -8.476  1.00 70.76           O  
ANISOU  256  O   ASP A  38     7514  10049   9323    210   1524    302       O  
ATOM    257  CB  ASP A  38      21.860  15.283  -8.422  1.00 66.28           C  
ANISOU  257  CB  ASP A  38     6463   9546   9175    216   1786    349       C  
ATOM    258  CG  ASP A  38      21.199  13.961  -8.777  1.00 59.31           C  
ANISOU  258  CG  ASP A  38     5615   8549   8372    339   1950    131       C  
ATOM    259  OD1 ASP A  38      20.379  13.469  -7.976  1.00 73.38           O  
ANISOU  259  OD1 ASP A  38     7492  10155  10235    425   1855    146       O  
ATOM    260  OD2 ASP A  38      21.504  13.410  -9.856  1.00 66.22           O1-
ANISOU  260  OD2 ASP A  38     6430   9512   9218    320   2192    -72       O1-
ATOM    261  N   GLY A  39      19.832  17.870  -8.828  1.00 71.69           N  
ANISOU  261  N   GLY A  39     7729  10224   9285     17   1435    556       N  
ATOM    262  CA  GLY A  39      18.762  18.414  -9.643  1.00 71.91           C  
ANISOU  262  CA  GLY A  39     7953  10340   9029     25   1396    577       C  
ATOM    263  C   GLY A  39      19.208  19.664 -10.370  1.00 70.58           C  
ANISOU  263  C   GLY A  39     7935  10196   8684   -126   1402    772       C  
ATOM    264  O   GLY A  39      20.387  20.011 -10.340  1.00 59.46           O  
ANISOU  264  O   GLY A  39     6447   8765   7379   -300   1472    848       O  
ATOM    265  N   VAL A  40      18.278  20.339 -11.037  1.00 63.59           N  
ANISOU  265  N   VAL A  40     7254   9380   7528    -65   1335    881       N  
ATOM    266  CA  VAL A  40      18.601  21.627 -11.650  1.00 62.98           C  
ANISOU  266  CA  VAL A  40     7401   9240   7289   -184   1334   1146       C  
ATOM    267  C   VAL A  40      17.525  22.656 -11.350  1.00 71.92           C  
ANISOU  267  C   VAL A  40     8830  10187   8307     26   1140   1321       C  
ATOM    268  O   VAL A  40      16.420  22.313 -10.934  1.00 63.46           O  
ANISOU  268  O   VAL A  40     7730   9179   7204    266   1025   1224       O  
ATOM    269  CB  VAL A  40      18.783  21.542 -13.187  1.00 59.86           C  
ANISOU  269  CB  VAL A  40     6977   9174   6594   -306   1510   1200       C  
ATOM    270  CG1 VAL A  40      19.883  20.555 -13.558  1.00 62.04           C  
ANISOU  270  CG1 VAL A  40     6955   9642   6973   -470   1751    994       C  
ATOM    271  CG2 VAL A  40      17.471  21.182 -13.863  1.00 64.65           C  
ANISOU  271  CG2 VAL A  40     7598  10061   6905   -123   1440   1134       C  
ATOM    272  N   VAL A  41      17.860  23.923 -11.559  1.00 71.37           N  
ANISOU  272  N   VAL A  41     9047   9880   8190    -63   1125   1584       N  
ATOM    273  CA  VAL A  41      16.897  25.001 -11.411  1.00 75.47           C  
ANISOU  273  CA  VAL A  41     9901  10166   8610    195    976   1782       C  
ATOM    274  C   VAL A  41      16.844  25.817 -12.692  1.00 57.97           C  
ANISOU  274  C   VAL A  41     7913   7999   6113    171   1036   2125       C  
ATOM    275  O   VAL A  41      17.830  26.439 -13.086  1.00 72.33           O  
ANISOU  275  O   VAL A  41     9874   9655   7952   -133   1158   2312       O  
ATOM    276  CB  VAL A  41      17.244  25.926 -10.232  1.00 56.05           C  
ANISOU  276  CB  VAL A  41     7696   7211   6391    155    888   1788       C  
ATOM    277  CG1 VAL A  41      16.234  27.056 -10.136  1.00 62.84           C  
ANISOU  277  CG1 VAL A  41     8939   7771   7165    491    773   1976       C  
ATOM    278  CG2 VAL A  41      17.269  25.141  -8.944  1.00 67.38           C  
ANISOU  278  CG2 VAL A  41     8906   8664   8030    195    814   1493       C  
ATOM    279  N   LEU A  42      15.691  25.796 -13.347  1.00 79.45           N  
ANISOU  279  N   LEU A  42    10642  10996   8549    477    950   2228       N  
ATOM    280  CA  LEU A  42      15.483  26.596 -14.542  1.00 72.46           C  
ANISOU  280  CA  LEU A  42     9986  10207   7338    536    970   2620       C  
ATOM    281  C   LEU A  42      15.053  27.996 -14.135  1.00 66.23           C  
ANISOU  281  C   LEU A  42     9646   8890   6628    799    864   2932       C  
ATOM    282  O   LEU A  42      14.063  28.172 -13.418  1.00 79.82           O  
ANISOU  282  O   LEU A  42    11405  10507   8417   1190    711   2860       O  
ATOM    283  CB  LEU A  42      14.434  25.953 -15.450  1.00 68.10           C  
ANISOU  283  CB  LEU A  42     9208  10268   6399    755    894   2598       C  
ATOM    284  CG  LEU A  42      14.183  26.642 -16.793  1.00 68.91           C  
ANISOU  284  CG  LEU A  42     9491  10629   6063    837    894   3028       C  
ATOM    285  CD1 LEU A  42      15.470  26.748 -17.596  1.00 70.93           C  
ANISOU  285  CD1 LEU A  42     9812  10913   6223    402   1135   3167       C  
ATOM    286  CD2 LEU A  42      13.117  25.897 -17.581  1.00 75.96           C  
ANISOU  286  CD2 LEU A  42    10084  12231   6545   1020    778   2922       C  
ATOM    287  N   VAL A  43      15.816  28.986 -14.585  1.00 71.38           N  
ANISOU  287  N   VAL A  43    10647   9193   7282    574    974   3269       N  
ATOM    288  CA  VAL A  43      15.548  30.380 -14.264  1.00 76.67           C  
ANISOU  288  CA  VAL A  43    11838   9226   8068    778    920   3577       C  
ATOM    289  C   VAL A  43      15.069  31.134 -15.495  1.00 79.41           C  
ANISOU  289  C   VAL A  43    12461   9647   8065   1002    922   4119       C  
ATOM    290  O   VAL A  43      15.781  31.223 -16.496  1.00 93.33           O  
ANISOU  290  O   VAL A  43    14261  11581   9618    669   1075   4383       O  
ATOM    291  CB  VAL A  43      16.804  31.080 -13.717  1.00 88.19           C  
ANISOU  291  CB  VAL A  43    13569  10097   9842    295   1046   3575       C  
ATOM    292  CG1 VAL A  43      16.554  32.573 -13.561  1.00 80.86           C  
ANISOU  292  CG1 VAL A  43    13273   8425   9027    461   1031   3908       C  
ATOM    293  CG2 VAL A  43      17.230  30.454 -12.398  1.00 70.95           C  
ANISOU  293  CG2 VAL A  43    11131   7855   7971    133    998   3081       C  
ATOM    294  N   ASP A  44      13.857  31.671 -15.417  1.00 92.11           N  
ANISOU  294  N   ASP A  44    14240  11171   9589   1593    758   4305       N  
ATOM    295  CA  ASP A  44      13.304  32.463 -16.506  1.00100.32           C  
ANISOU  295  CA  ASP A  44    15558  12267  10291   1917    722   4888       C  
ATOM    296  C   ASP A  44      13.871  33.877 -16.438  1.00110.77           C  
ANISOU  296  C   ASP A  44    17549  12708  11832   1823    840   5295       C  
ATOM    297  O   ASP A  44      13.583  34.620 -15.498  1.00115.24           O  
ANISOU  297  O   ASP A  44    18458  12603  12723   2080    799   5226       O  
ATOM    298  CB  ASP A  44      11.776  32.493 -16.420  1.00 99.94           C  
ANISOU  298  CB  ASP A  44    15382  12509  10080   2642    494   4943       C  
ATOM    299  CG  ASP A  44      11.119  32.763 -17.763  1.00121.96           C  
ANISOU  299  CG  ASP A  44    18177  15804  12359   2966    402   5474       C  
ATOM    300  OD1 ASP A  44      11.699  33.508 -18.583  1.00109.02           O  
ANISOU  300  OD1 ASP A  44    16871  13920  10631   2736    495   5866       O  
ATOM    301  OD2 ASP A  44      10.017  32.224 -18.000  1.00144.15           O1-
ANISOU  301  OD2 ASP A  44    20567  19280  14925   3320    203   5345       O1-
ATOM    302  N   PRO A  45      14.683  34.254 -17.437  1.00113.61           N  
ANISOU  302  N   PRO A  45    18109  13053  12003   1428   1010   5707       N  
ATOM    303  CA  PRO A  45      15.330  35.570 -17.474  1.00123.60           C  
ANISOU  303  CA  PRO A  45    20030  13458  13474   1204   1165   6129       C  
ATOM    304  C   PRO A  45      14.330  36.695 -17.719  1.00141.25           C  
ANISOU  304  C   PRO A  45    22602  15326  15741   1753    967   6438       C  
ATOM    305  O   PRO A  45      14.664  37.865 -17.529  1.00162.11           O  
ANISOU  305  O   PRO A  45    25738  17168  18688   1622   1018   6626       O  
ATOM    306  CB  PRO A  45      16.286  35.449 -18.663  1.00125.36           C  
ANISOU  306  CB  PRO A  45    20172  14060  13398    632   1357   6423       C  
ATOM    307  CG  PRO A  45      15.642  34.446 -19.553  1.00103.54           C  
ANISOU  307  CG  PRO A  45    16913  12302  10126    882   1256   6397       C  
ATOM    308  CD  PRO A  45      14.996  33.451 -18.632  1.00115.96           C  
ANISOU  308  CD  PRO A  45    18036  14174  11848   1159   1088   5796       C  
ATOM    309  N   GLU A  46      13.118  36.339 -18.135  1.00134.53           N  
ANISOU  309  N   GLU A  46    21443  15077  14595   2339    749   6468       N  
ATOM    310  CA  GLU A  46      12.070  37.321 -18.385  1.00133.01           C  
ANISOU  310  CA  GLU A  46    21468  14651  14420   2927    565   6749       C  
ATOM    311  C   GLU A  46      11.530  37.910 -17.086  1.00139.50           C  
ANISOU  311  C   GLU A  46    22512  14797  15696   3341    521   6467       C  
ATOM    312  O   GLU A  46      10.967  39.006 -17.080  1.00132.78           O  
ANISOU  312  O   GLU A  46    21994  13444  15013   3733    458   6687       O  
ATOM    313  CB  GLU A  46      10.924  36.687 -19.176  1.00130.58           C  
ANISOU  313  CB  GLU A  46    20672  15289  13654   3384    347   6797       C  
ATOM    314  CG  GLU A  46      11.306  36.214 -20.569  1.00148.34           C  
ANISOU  314  CG  GLU A  46    22733  18241  15388   3038    373   7051       C  
ATOM    315  CD  GLU A  46      10.177  35.471 -21.258  1.00156.96           C  
ANISOU  315  CD  GLU A  46    23292  20313  16033   3417    151   6973       C  
ATOM    316  OE1 GLU A  46       9.886  34.325 -20.856  1.00146.41           O  
ANISOU  316  OE1 GLU A  46    21469  19536  14625   3419    110   6525       O  
ATOM    317  OE2 GLU A  46       9.578  36.033 -22.198  1.00124.81           O1-
ANISOU  317  OE2 GLU A  46    19283  16457  11684   3689     13   7359       O1-
ATOM    318  N   TYR A  47      11.703  37.180 -15.989  1.00133.27           N  
ANISOU  318  N   TYR A  47    21542  14005  15088   3261    565   5974       N  
ATOM    319  CA  TYR A  47      11.139  37.589 -14.707  1.00138.22           C  
ANISOU  319  CA  TYR A  47    22320  14125  16073   3657    527   5618       C  
ATOM    320  C   TYR A  47      12.203  37.747 -13.621  1.00124.15           C  
ANISOU  320  C   TYR A  47    20872  11632  14668   3161    694   5285       C  
ATOM    321  O   TYR A  47      11.939  38.313 -12.561  1.00125.71           O  
ANISOU  321  O   TYR A  47    21326  11262  15177   3379    696   4980       O  
ATOM    322  CB  TYR A  47      10.069  36.591 -14.258  1.00148.83           C  
ANISOU  322  CB  TYR A  47    23093  16201  17254   4128    375   5283       C  
ATOM    323  CG  TYR A  47       9.062  36.253 -15.336  1.00148.58           C  
ANISOU  323  CG  TYR A  47    22631  17012  16811   4493    199   5526       C  
ATOM    324  CD1 TYR A  47       8.090  37.169 -15.719  1.00158.92           C  
ANISOU  324  CD1 TYR A  47    24043  18237  18100   5038     87   5793       C  
ATOM    325  CD2 TYR A  47       9.083  35.016 -15.969  1.00136.76           C  
ANISOU  325  CD2 TYR A  47    20618  16406  14939   4277    149   5463       C  
ATOM    326  CE1 TYR A  47       7.168  36.864 -16.705  1.00157.95           C  
ANISOU  326  CE1 TYR A  47    23509  18922  17582   5343    -86   6002       C  
ATOM    327  CE2 TYR A  47       8.165  34.702 -16.954  1.00140.73           C  
ANISOU  327  CE2 TYR A  47    20721  17703  15045   4543    -23   5619       C  
ATOM    328  CZ  TYR A  47       7.210  35.630 -17.318  1.00151.59           C  
ANISOU  328  CZ  TYR A  47    22195  19005  16397   5070   -146   5895       C  
ATOM    329  OH  TYR A  47       6.294  35.322 -18.299  1.00150.78           O  
ANISOU  329  OH  TYR A  47    21677  19728  15885   5316   -324   6046       O  
ATOM    330  N   LEU A  48      13.403  37.245 -13.889  1.00115.43           N  
ANISOU  330  N   LEU A  48    19738  10606  13513   2472    844   5311       N  
ATOM    331  CA  LEU A  48      14.498  37.333 -12.929  1.00102.07           C  
ANISOU  331  CA  LEU A  48    18247   8376  12159   1869    976   4946       C  
ATOM    332  C   LEU A  48      15.113  38.731 -12.922  1.00126.51           C  
ANISOU  332  C   LEU A  48    21966  10548  15553   1548   1088   5135       C  
ATOM    333  O   LEU A  48      15.319  39.337 -13.974  1.00114.99           O  
ANISOU  333  O   LEU A  48    20654   9037  14000   1410   1131   5610       O  
ATOM    334  CB  LEU A  48      15.564  36.273 -13.237  1.00 96.97           C  
ANISOU  334  CB  LEU A  48    17069   8364  11412   1163   1043   4749       C  
ATOM    335  CG  LEU A  48      16.748  36.067 -12.281  1.00106.42           C  
ANISOU  335  CG  LEU A  48    18165   9357  12914    481   1108   4277       C  
ATOM    336  CD1 LEU A  48      17.921  36.996 -12.597  1.00121.37           C  
ANISOU  336  CD1 LEU A  48    20495  10656  14963   -190   1302   4534       C  
ATOM    337  CD2 LEU A  48      16.320  36.189 -10.820  1.00104.90           C  
ANISOU  337  CD2 LEU A  48    18056   8821  12981    726    993   3778       C  
ATOM    338  N   LYS A  49      15.402  39.233 -11.726  1.00110.34           N  
ANISOU  338  N   LYS A  49    20230   7835  13861   1392   1116   4718       N  
ATOM    339  CA  LYS A  49      16.049  40.528 -11.565  1.00137.39           C  
ANISOU  339  CA  LYS A  49    24179  10404  17620    989   1215   4756       C  
ATOM    340  C   LYS A  49      16.944  40.445 -10.333  1.00139.55           C  
ANISOU  340  C   LYS A  49    24552  10318  18150    397   1267   4187       C  
ATOM    341  O   LYS A  49      17.930  41.173 -10.215  1.00139.20           O  
ANISOU  341  O   LYS A  49    24772   9775  18341   -270   1370   4139       O  
ATOM    342  CB  LYS A  49      15.020  41.657 -11.638  1.00138.56           C  
ANISOU  342  CB  LYS A  49    24683  10065  17899   1660   1151   4937       C  
ATOM    343  N   GLU A  50      16.584  39.548  -9.418  1.00133.40           N  
ANISOU  343  N   GLU A  50    23513   9862  17311    629   1176   3749       N  
ATOM    344  CA  GLU A  50      17.172  39.476  -8.084  1.00132.75           C  
ANISOU  344  CA  GLU A  50    23382   9617  17439    210   1131   3103       C  
ATOM    345  C   GLU A  50      18.664  39.158  -8.148  1.00136.44           C  
ANISOU  345  C   GLU A  50    23575  10304  17963   -761   1189   3003       C  
ATOM    346  O   GLU A  50      19.385  39.307  -7.160  1.00142.08           O  
ANISOU  346  O   GLU A  50    24314  10820  18849  -1265   1157   2540       O  
ATOM    347  CB  GLU A  50      16.442  38.425  -7.245  1.00112.43           C  
ANISOU  347  CB  GLU A  50    20241   7737  14740    658    962   2662       C  
ATOM    348  CG  GLU A  50      15.050  38.083  -7.760  1.00109.26           C  
ANISOU  348  CG  GLU A  50    19654   7739  14120   1531    893   2921       C  
ATOM    349  CD  GLU A  50      14.044  39.201  -7.565  1.00127.18           C  
ANISOU  349  CD  GLU A  50    22532   9294  16495   2244    928   3033       C  
ATOM    350  OE1 GLU A  50      14.297  40.099  -6.734  1.00143.72           O  
ANISOU  350  OE1 GLU A  50    25105  10657  18847   2099    985   2715       O  
ATOM    351  OE2 GLU A  50      12.996  39.178  -8.244  1.00121.05           O1-
ANISOU  351  OE2 GLU A  50    21598   8850  15547   2904    869   3363       O1-
ATOM    352  N   ARG A  51      19.106  38.699  -9.316  1.00134.97           N  
ANISOU  352  N   ARG A  51    23084  10603  17594  -1001   1271   3424       N  
ATOM    353  CA  ARG A  51      20.525  38.515  -9.624  1.00138.73           C  
ANISOU  353  CA  ARG A  51    23306  11298  18106  -1887   1383   3446       C  
ATOM    354  C   ARG A  51      21.238  37.419  -8.830  1.00117.73           C  
ANISOU  354  C   ARG A  51    19944   9333  15456  -2234   1271   2939       C  
ATOM    355  O   ARG A  51      22.466  37.334  -8.865  1.00131.76           O  
ANISOU  355  O   ARG A  51    21479  11284  17301  -2965   1346   2879       O  
ATOM    356  CB  ARG A  51      21.288  39.841  -9.501  1.00149.96           C  
ANISOU  356  CB  ARG A  51    25388  11795  19795  -2514   1529   3527       C  
ATOM    357  N   ARG A  52      20.478  36.580  -8.128  1.00103.34           N  
ANISOU  357  N   ARG A  52    17776   7932  13558  -1708   1100   2609       N  
ATOM    358  CA  ARG A  52      21.067  35.452  -7.406  1.00 97.12           C  
ANISOU  358  CA  ARG A  52    16327   7815  12760  -1936    991   2207       C  
ATOM    359  C   ARG A  52      20.025  34.424  -6.954  1.00 93.01           C  
ANISOU  359  C   ARG A  52    15440   7795  12103  -1278    848   2007       C  
ATOM    360  O   ARG A  52      19.121  34.735  -6.176  1.00 97.08           O  
ANISOU  360  O   ARG A  52    16205   8038  12641   -829    757   1804       O  
ATOM    361  CB  ARG A  52      21.892  35.941  -6.210  1.00 96.10           C  
ANISOU  361  CB  ARG A  52    16310   7376  12827  -2474    918   1780       C  
ATOM    362  CG  ARG A  52      23.144  35.124  -5.945  1.00 96.97           C  
ANISOU  362  CG  ARG A  52    15773   8125  12946  -3046    881   1593       C  
ATOM    363  CD  ARG A  52      24.065  35.824  -4.961  1.00 93.44           C  
ANISOU  363  CD  ARG A  52    15471   7374  12659  -3702    809   1236       C  
ATOM    364  NE  ARG A  52      24.525  37.118  -5.453  1.00100.90           N  
ANISOU  364  NE  ARG A  52    16996   7590  13753  -4227    970   1434       N  
ATOM    365  CZ  ARG A  52      25.331  37.929  -4.775  1.00119.05           C  
ANISOU  365  CZ  ARG A  52    19530   9497  16207  -4917    944   1147       C  
ATOM    366  NH1 ARG A  52      25.766  37.578  -3.572  1.00121.80           N1+
ANISOU  366  NH1 ARG A  52    19550  10192  16538  -5134    737    648       N1+
ATOM    367  NH2 ARG A  52      25.700  39.091  -5.298  1.00124.96           N  
ANISOU  367  NH2 ARG A  52    20852   9516  17111  -5416   1124   1367       N  
ATOM    368  N   VAL A  53      20.167  33.198  -7.451  1.00 80.19           N  
ANISOU  368  N   VAL A  53    12526   6399  11544   -448    773   3178       N  
ATOM    369  CA  VAL A  53      19.283  32.095  -7.092  1.00 91.87           C  
ANISOU  369  CA  VAL A  53    13753   8187  12967    -68    586   3039       C  
ATOM    370  C   VAL A  53      20.004  31.034  -6.262  1.00 91.32           C  
ANISOU  370  C   VAL A  53    13316   8459  12924   -259    432   2743       C  
ATOM    371  O   VAL A  53      21.020  30.474  -6.692  1.00 96.94           O  
ANISOU  371  O   VAL A  53    13739   9500  13593   -477    431   2738       O  
ATOM    372  CB  VAL A  53      18.693  31.416  -8.341  1.00 85.07           C  
ANISOU  372  CB  VAL A  53    12709   7682  11931    260    568   3248       C  
ATOM    373  CG1 VAL A  53      17.836  30.222  -7.942  1.00 76.97           C  
ANISOU  373  CG1 VAL A  53    11425   6977  10843    557    392   3067       C  
ATOM    374  CG2 VAL A  53      17.885  32.412  -9.153  1.00103.95           C  
ANISOU  374  CG2 VAL A  53    15441   9803  14252    538    698   3567       C  
ATOM    375  N   TYR A  54      19.459  30.762  -5.077  1.00 86.44           N  
ANISOU  375  N   TYR A  54    12712   7774  12355   -139    314   2512       N  
ATOM    376  CA  TYR A  54      20.007  29.764  -4.163  1.00 75.92           C  
ANISOU  376  CA  TYR A  54    11084   6737  11026   -246    164   2249       C  
ATOM    377  C   TYR A  54      19.131  28.521  -4.067  1.00 68.83           C  
ANISOU  377  C   TYR A  54     9997   6115  10041    107     46   2182       C  
ATOM    378  O   TYR A  54      17.926  28.573  -4.309  1.00 69.25           O  
ANISOU  378  O   TYR A  54    10162   6096  10054    416     53   2261       O  
ATOM    379  CB  TYR A  54      20.141  30.346  -2.758  1.00 69.90           C  
ANISOU  379  CB  TYR A  54    10492   5709  10356   -428    123   2013       C  
ATOM    380  CG  TYR A  54      21.157  31.447  -2.618  1.00 80.14           C  
ANISOU  380  CG  TYR A  54    11954   6765  11731   -892    226   1987       C  
ATOM    381  CD1 TYR A  54      20.760  32.774  -2.516  1.00 69.95           C  
ANISOU  381  CD1 TYR A  54    11125   4936  10519   -956    369   2040       C  
ATOM    382  CD2 TYR A  54      22.514  31.161  -2.576  1.00 64.90           C  
ANISOU  382  CD2 TYR A  54     9724   5153   9783  -1272    194   1902       C  
ATOM    383  CE1 TYR A  54      21.690  33.784  -2.376  1.00 78.33           C  
ANISOU  383  CE1 TYR A  54    12381   5736  11645  -1450    487   1994       C  
ATOM    384  CE2 TYR A  54      23.448  32.164  -2.442  1.00 69.03           C  
ANISOU  384  CE2 TYR A  54    10367   5500  10361  -1770    295   1855       C  
ATOM    385  CZ  TYR A  54      23.031  33.472  -2.341  1.00 74.22           C  
ANISOU  385  CZ  TYR A  54    11521   5575  11102  -1889    446   1893       C  
ATOM    386  OH  TYR A  54      23.966  34.471  -2.208  1.00100.40           O  
ANISOU  386  OH  TYR A  54    15000   8680  14469  -2451    570   1825       O  
ATOM    387  N   VAL A  55      19.747  27.404  -3.697  1.00 61.88           N  
ANISOU  387  N   VAL A  55     8832   5560   9118     58    -53   2034       N  
ATOM    388  CA  VAL A  55      19.011  26.190  -3.375  1.00 66.10           C  
ANISOU  388  CA  VAL A  55     9245   6294   9578    322   -148   1930       C  
ATOM    389  C   VAL A  55      19.444  25.696  -1.998  1.00 73.99           C  
ANISOU  389  C   VAL A  55    10171   7348  10594    246   -256   1700       C  
ATOM    390  O   VAL A  55      20.630  25.714  -1.667  1.00 68.47           O  
ANISOU  390  O   VAL A  55     9335   6772   9906     19   -286   1632       O  
ATOM    391  CB  VAL A  55      19.242  25.081  -4.417  1.00 72.43           C  
ANISOU  391  CB  VAL A  55     9820   7438  10261    417   -137   2001       C  
ATOM    392  CG1 VAL A  55      18.315  23.905  -4.149  1.00 73.21           C  
ANISOU  392  CG1 VAL A  55     9872   7668  10278    651   -201   1893       C  
ATOM    393  CG2 VAL A  55      19.015  25.616  -5.817  1.00 63.66           C  
ANISOU  393  CG2 VAL A  55     8760   6330   9098    456    -33   2237       C  
ATOM    394  N   THR A  56      18.479  25.258  -1.196  1.00 75.96           N  
ANISOU  394  N   THR A  56    10492   7548  10821    437   -313   1586       N  
ATOM    395  CA  THR A  56      18.756  24.848   0.174  1.00 57.61           C  
ANISOU  395  CA  THR A  56     8144   5261   8485    398   -410   1386       C  
ATOM    396  C   THR A  56      18.143  23.491   0.500  1.00 64.44           C  
ANISOU  396  C   THR A  56     8937   6294   9251    614   -453   1321       C  
ATOM    397  O   THR A  56      16.975  23.238   0.206  1.00 74.00           O  
ANISOU  397  O   THR A  56    10210   7477  10431    785   -417   1352       O  
ATOM    398  CB  THR A  56      18.224  25.889   1.177  1.00 61.06           C  
ANISOU  398  CB  THR A  56     8824   5389   8986    359   -410   1278       C  
ATOM    400  CG2 THR A  56      18.513  25.455   2.603  1.00 83.91           C  
ANISOU  400  CG2 THR A  56    11690   8362  11829    318   -516   1070       C  
ATOM    399  OG1 THR A  56      18.853  27.153   0.934  1.00 69.75           O  
ANISOU  399  OG1 THR A  56    10056   6271  10176    109   -346   1319       O  
ATOM    401  N   LEU A  57      18.942  22.615   1.101  1.00 59.02           N  
ANISOU  401  N   LEU A  57     8124   5800   8502    603   -521   1234       N  
ATOM    402  CA  LEU A  57      18.436  21.348   1.611  1.00 56.23           C  
ANISOU  402  CA  LEU A  57     7779   5536   8049    786   -541   1168       C  
ATOM    403  C   LEU A  57      18.227  21.457   3.114  1.00 63.17           C  
ANISOU  403  C   LEU A  57     8761   6338   8902    787   -610   1025       C  
ATOM    404  O   LEU A  57      19.145  21.815   3.852  1.00 60.35           O  
ANISOU  404  O   LEU A  57     8351   6042   8536    667   -690    949       O  
ATOM    405  CB  LEU A  57      19.405  20.209   1.305  1.00 62.21           C  
ANISOU  405  CB  LEU A  57     8381   6534   8720    855   -548   1191       C  
ATOM    406  CG  LEU A  57      18.930  18.838   1.790  1.00 65.34           C  
ANISOU  406  CG  LEU A  57     8863   6958   9005   1042   -533   1140       C  
ATOM    407  CD1 LEU A  57      17.667  18.428   1.051  1.00 55.97           C  
ANISOU  407  CD1 LEU A  57     7774   5692   7799   1094   -443   1161       C  
ATOM    408  CD2 LEU A  57      20.018  17.788   1.633  1.00 63.77           C  
ANISOU  408  CD2 LEU A  57     8557   6960   8713   1169   -530   1165       C  
ATOM    409  N   THR A  58      17.019  21.143   3.567  1.00 63.38           N  
ANISOU  409  N   THR A  58     8915   6275   8892    908   -578    979       N  
ATOM    410  CA  THR A  58      16.682  21.289   4.976  1.00 45.63           C  
ANISOU  410  CA  THR A  58     6782   3956   6599    921   -621    846       C  
ATOM    411  C   THR A  58      16.083  20.024   5.571  1.00 44.77           C  
ANISOU  411  C   THR A  58     6730   3916   6365   1055   -595    814       C  
ATOM    412  O   THR A  58      15.085  19.505   5.074  1.00 68.75           O  
ANISOU  412  O   THR A  58     9794   6946   9381   1118   -511    846       O  
ATOM    413  CB  THR A  58      15.698  22.451   5.192  1.00 55.94           C  
ANISOU  413  CB  THR A  58     8231   5048   7976    924   -577    805       C  
ATOM    415  CG2 THR A  58      15.235  22.500   6.640  1.00 68.90           C  
ANISOU  415  CG2 THR A  58     9997   6641   9542    961   -599    654       C  
ATOM    414  OG1 THR A  58      16.340  23.687   4.860  1.00 72.54           O  
ANISOU  414  OG1 THR A  58    10367   7010  10185    771   -583    823       O  
ATOM    416  N   CYS A  59      16.710  19.527   6.632  1.00 55.36           N  
ANISOU  416  N   CYS A  59     8090   5341   7603   1082   -663    754       N  
ATOM    417  CA  CYS A  59      16.120  18.473   7.447  1.00 57.66           C  
ANISOU  417  CA  CYS A  59     8506   5644   7759   1197   -621    728       C  
ATOM    418  C   CYS A  59      15.509  19.125   8.670  1.00 62.40           C  
ANISOU  418  C   CYS A  59     9219   6174   8318   1176   -639    609       C  
ATOM    419  O   CYS A  59      16.222  19.698   9.495  1.00 71.66           O  
ANISOU  419  O   CYS A  59    10385   7388   9453   1123   -741    526       O  
ATOM    420  CB  CYS A  59      17.173  17.462   7.891  1.00 46.82           C  
ANISOU  420  CB  CYS A  59     7116   4417   6256   1308   -673    768       C  
ATOM    421  SG  CYS A  59      16.512  16.177   8.981  1.00 62.64           S  
ANISOU  421  SG  CYS A  59     9353   6379   8069   1450   -594    771       S  
ATOM    422  N   ALA A  60      14.191  19.046   8.798  1.00 64.83           N  
ANISOU  422  N   ALA A  60     9613   6410   8611   1208   -537    583       N  
ATOM    423  CA  ALA A  60      13.543  19.763   9.885  1.00 45.12           C  
ANISOU  423  CA  ALA A  60     7217   3853   6072   1214   -529    462       C  
ATOM    424  C   ALA A  60      12.602  18.910  10.717  1.00 49.76           C  
ANISOU  424  C   ALA A  60     7911   4485   6510   1271   -433    436       C  
ATOM    425  O   ALA A  60      11.998  17.947  10.225  1.00 57.71           O  
ANISOU  425  O   ALA A  60     8919   5526   7483   1270   -332    502       O  
ATOM    426  CB  ALA A  60      12.818  20.990   9.354  1.00 42.57           C  
ANISOU  426  CB  ALA A  60     6886   3407   5880   1215   -485    438       C  
ATOM    427  N   PHE A  61      12.498  19.277  11.990  1.00 52.41           N  
ANISOU  427  N   PHE A  61     8349   4825   6740   1291   -454    326       N  
ATOM    428  CA  PHE A  61      11.491  18.719  12.875  1.00 52.03           C  
ANISOU  428  CA  PHE A  61     8406   4824   6541   1329   -339    291       C  
ATOM    429  C   PHE A  61      10.327  19.687  12.955  1.00 44.48           C  
ANISOU  429  C   PHE A  61     7431   3836   5633   1364   -254    196       C  
ATOM    430  O   PHE A  61      10.483  20.821  13.405  1.00 55.49           O  
ANISOU  430  O   PHE A  61     8877   5146   7061   1390   -302     83       O  
ATOM    431  CB  PHE A  61      12.060  18.481  14.273  1.00 54.12           C  
ANISOU  431  CB  PHE A  61     8797   5154   6610   1363   -402    237       C  
ATOM    432  CG  PHE A  61      11.151  17.684  15.164  1.00 54.72           C  
ANISOU  432  CG  PHE A  61     9007   5285   6498   1390   -263    242       C  
ATOM    433  CD1 PHE A  61      10.969  16.328  14.949  1.00 87.87           C  
ANISOU  433  CD1 PHE A  61    13286   9482  10617   1379   -158    374       C  
ATOM    434  CD2 PHE A  61      10.481  18.283  16.214  1.00 94.27           C  
ANISOU  434  CD2 PHE A  61    14088  10332  11397   1414   -214    112       C  
ATOM    435  CE1 PHE A  61      10.132  15.590  15.756  1.00 87.08           C  
ANISOU  435  CE1 PHE A  61    13336   9414  10338   1356     -1    390       C  
ATOM    436  CE2 PHE A  61       9.644  17.541  17.027  1.00111.13           C  
ANISOU  436  CE2 PHE A  61    16336  12544  13343   1417    -65    128       C  
ATOM    437  CZ  PHE A  61       9.470  16.191  16.797  1.00 86.37           C  
ANISOU  437  CZ  PHE A  61    13280   9402  10134   1370     45    275       C  
ATOM    438  N   ARG A  62       9.165  19.244  12.494  1.00 54.57           N  
ANISOU  438  N   ARG A  62     8636   5194   6903   1367   -120    234       N  
ATOM    439  CA  ARG A  62       7.978  20.083  12.522  1.00 45.09           C  
ANISOU  439  CA  ARG A  62     7370   4039   5723   1461    -28    163       C  
ATOM    440  C   ARG A  62       7.104  19.689  13.699  1.00 50.02           C  
ANISOU  440  C   ARG A  62     8054   4791   6160   1471     96     84       C  
ATOM    441  O   ARG A  62       6.939  18.506  13.986  1.00 54.71           O  
ANISOU  441  O   ARG A  62     8690   5468   6630   1363    170    134       O  
ATOM    442  CB  ARG A  62       7.197  19.973  11.211  1.00 50.29           C  
ANISOU  442  CB  ARG A  62     7837   4807   6463   1466     29    247       C  
ATOM    443  CG  ARG A  62       6.036  20.949  11.104  1.00 68.88           C  
ANISOU  443  CG  ARG A  62    10085   7253   8835   1641    108    203       C  
ATOM    444  CD  ARG A  62       5.168  20.656   9.895  1.00 76.89           C  
ANISOU  444  CD  ARG A  62    10863   8491   9862   1644    157    287       C  
ATOM    445  NE  ARG A  62       5.695  21.232   8.661  1.00 88.50           N  
ANISOU  445  NE  ARG A  62    12287   9863  11475   1702     67    394       N  
ATOM    446  CZ  ARG A  62       5.397  22.452   8.226  1.00120.51           C  
ANISOU  446  CZ  ARG A  62    16323  13859  15608   1924     63    433       C  
ATOM    447  NH1 ARG A  62       4.585  23.227   8.931  1.00139.26           N1+
ANISOU  447  NH1 ARG A  62    18718  16256  17937   2137    144    356       N1+
ATOM    448  NH2 ARG A  62       5.908  22.900   7.087  1.00129.14           N  
ANISOU  448  NH2 ARG A  62    17399  14860  16809   1956     -3    557       N  
ATOM    449  N   TYR A  63       6.549  20.682  14.384  1.00 59.04           N  
ANISOU  449  N   TYR A  63     9229   5931   7273   1604    141    -38       N  
ATOM    450  CA  TYR A  63       5.746  20.413  15.570  1.00 49.49           C  
ANISOU  450  CA  TYR A  63     8071   4867   5865   1626    272   -124       C  
ATOM    451  C   TYR A  63       4.729  21.514  15.827  1.00 54.95           C  
ANISOU  451  C   TYR A  63     8709   5617   6553   1831    373   -239       C  
ATOM    452  O   TYR A  63       4.887  22.638  15.358  1.00 56.29           O  
ANISOU  452  O   TYR A  63     8900   5624   6864   1974    323   -270       O  
ATOM    453  CB  TYR A  63       6.650  20.247  16.797  1.00 59.21           C  
ANISOU  453  CB  TYR A  63     9517   6031   6951   1589    196   -187       C  
ATOM    454  CG  TYR A  63       7.544  21.439  17.063  1.00 50.77           C  
ANISOU  454  CG  TYR A  63     8557   4780   5953   1641     55   -308       C  
ATOM    455  CD1 TYR A  63       7.145  22.452  17.923  1.00 52.91           C  
ANISOU  455  CD1 TYR A  63     8941   5010   6154   1753    105   -492       C  
ATOM    456  CD2 TYR A  63       8.788  21.550  16.451  1.00 78.51           C  
ANISOU  456  CD2 TYR A  63    12067   8169   9593   1554   -112   -255       C  
ATOM    457  CE1 TYR A  63       7.957  23.544  18.167  1.00 57.13           C  
ANISOU  457  CE1 TYR A  63     9618   5345   6743   1741     -5   -634       C  
ATOM    458  CE2 TYR A  63       9.607  22.638  16.688  1.00 50.83           C  
ANISOU  458  CE2 TYR A  63     8657   4513   6143   1525   -226   -384       C  
ATOM    459  CZ  TYR A  63       9.187  23.632  17.547  1.00 66.64           C  
ANISOU  459  CZ  TYR A  63    10808   6438   8076   1600   -171   -581       C  
ATOM    460  OH  TYR A  63       9.999  24.717  17.787  1.00 63.53           O  
ANISOU  460  OH  TYR A  63    10551   5860   7727   1514   -267   -740       O  
ATOM    461  N   GLY A  64       3.682  21.184  16.574  1.00 56.85           N  
ANISOU  461  N   GLY A  64     8894   6086   6620   1856    537   -294       N  
ATOM    462  CA  GLY A  64       2.734  22.182  17.029  1.00 55.33           C  
ANISOU  462  CA  GLY A  64     8661   5983   6378   2100    655   -419       C  
ATOM    463  C   GLY A  64       3.010  22.502  18.485  1.00 73.77           C  
ANISOU  463  C   GLY A  64    11233   8253   8545   2138    678   -577       C  
ATOM    464  O   GLY A  64       3.523  21.659  19.219  1.00 83.02           O  
ANISOU  464  O   GLY A  64    12523   9449   9572   1967    653   -559       O  
ATOM    465  N   ARG A  65       2.684  23.720  18.904  1.00 75.46           N  
ANISOU  465  N   ARG A  65    11540   8376   8756   2381    731   -732       N  
ATOM    466  CA  ARG A  65       2.867  24.111  20.299  1.00 82.66           C  
ANISOU  466  CA  ARG A  65    12685   9244   9478   2423    765   -923       C  
ATOM    467  C   ARG A  65       1.684  23.674  21.155  1.00 89.90           C  
ANISOU  467  C   ARG A  65    13498  10504  10157   2491    983   -971       C  
ATOM    468  O   ARG A  65       0.528  23.898  20.795  1.00 72.73           O  
ANISOU  468  O   ARG A  65    11099   8547   7987   2673   1136   -960       O  
ATOM    469  CB  ARG A  65       3.091  25.618  20.423  1.00 69.04           C  
ANISOU  469  CB  ARG A  65    11176   7218   7839   2629    751  -1102       C  
ATOM    470  CG  ARG A  65       4.512  26.059  20.114  1.00 83.99           C  
ANISOU  470  CG  ARG A  65    13260   8776   9879   2456    542  -1126       C  
ATOM    471  CD  ARG A  65       5.501  25.419  21.074  1.00112.33           C  
ANISOU  471  CD  ARG A  65    16965  12424  13291   2216    412  -1185       C  
ATOM    472  NE  ARG A  65       6.873  25.850  20.824  1.00136.15           N  
ANISOU  472  NE  ARG A  65    20104  15209  16419   2030    210  -1227       N  
ATOM    473  CZ  ARG A  65       7.927  25.426  21.515  1.00131.39           C  
ANISOU  473  CZ  ARG A  65    19567  14684  15672   1834     53  -1275       C  
ATOM    474  NH1 ARG A  65       9.141  25.871  21.220  1.00123.52           N1+
ANISOU  474  NH1 ARG A  65    18622  13537  14774   1649   -124  -1323       N1+
ATOM    475  NH2 ARG A  65       7.766  24.556  22.503  1.00125.13           N  
ANISOU  475  NH2 ARG A  65    18778  14151  14616   1827     78  -1265       N  
ATOM    476  N   GLU A  66       1.988  23.052  22.290  1.00112.69           N  
ANISOU  476  N   GLU A  66    16530  13475  12813   2352    997  -1014       N  
ATOM    477  CA  GLU A  66       0.966  22.514  23.182  1.00129.50           C  
ANISOU  477  CA  GLU A  66    18585  15937  14682   2358   1218  -1040       C  
ATOM    478  C   GLU A  66       0.200  23.624  23.900  1.00129.57           C  
ANISOU  478  C   GLU A  66    18637  16016  14579   2661   1372  -1259       C  
ATOM    479  O   GLU A  66      -0.933  23.426  24.338  1.00141.62           O  
ANISOU  479  O   GLU A  66    19996  17878  15935   2745   1595  -1285       O  
ATOM    480  CB  GLU A  66       1.605  21.572  24.208  1.00131.45           C  
ANISOU  480  CB  GLU A  66    19031  16225  14689   2152   1188   -997       C  
ATOM    481  CG  GLU A  66       0.612  20.706  24.971  1.00135.25           C  
ANISOU  481  CG  GLU A  66    19443  17042  14902   2065   1435   -948       C  
ATOM    482  CD  GLU A  66       0.999  20.515  26.426  1.00138.09           C  
ANISOU  482  CD  GLU A  66    20070  17459  14940   2048   1456  -1019       C  
ATOM    483  OE1 GLU A  66       1.371  19.384  26.804  1.00146.41           O  
ANISOU  483  OE1 GLU A  66    21245  18547  15837   1858   1461   -851       O  
ATOM    484  OE2 GLU A  66       0.922  21.497  27.194  1.00131.44           O1-
ANISOU  484  OE2 GLU A  66    19339  16620  13982   2240   1478  -1243       O1-
ATOM    485  N   ASP A  67       0.820  24.795  24.011  1.00102.87           N  
ANISOU  485  N   ASP A  67    15486  12315  11283   2815   1271  -1428       N  
ATOM    486  CA  ASP A  67       0.236  25.899  24.766  1.00 91.07           C  
ANISOU  486  CA  ASP A  67    14130  10802   9670   3118   1422  -1670       C  
ATOM    487  C   ASP A  67      -0.533  26.893  23.895  1.00 94.65           C  
ANISOU  487  C   ASP A  67    14472  11179  10312   3472   1519  -1679       C  
ATOM    488  O   ASP A  67      -1.161  27.817  24.410  1.00100.12           O  
ANISOU  488  O   ASP A  67    15271  11856  10913   3801   1683  -1863       O  
ATOM    489  CB  ASP A  67       1.320  26.628  25.563  1.00 88.58           C  
ANISOU  489  CB  ASP A  67    14199  10172   9284   3061   1288  -1896       C  
ATOM    490  CG  ASP A  67       2.494  27.044  24.702  1.00101.42           C  
ANISOU  490  CG  ASP A  67    15941  11419  11176   2915   1054  -1858       C  
ATOM    491  OD1 ASP A  67       2.845  26.289  23.771  1.00109.96           O  
ANISOU  491  OD1 ASP A  67    16832  12525  12421   2747    938  -1623       O  
ATOM    492  OD2 ASP A  67       3.064  28.125  24.954  1.00117.36           O1-
ANISOU  492  OD2 ASP A  67    18248  13115  13229   2948   1002  -2074       O1-
ATOM    493  N   LEU A  68      -0.485  26.702  22.581  1.00104.69           N  
ANISOU  493  N   LEU A  68    15544  12410  11824   3437   1426  -1476       N  
ATOM    494  CA  LEU A  68      -1.176  27.599  21.659  1.00107.10           C  
ANISOU  494  CA  LEU A  68    15735  12667  12289   3802   1499  -1435       C  
ATOM    495  C   LEU A  68      -2.462  26.972  21.128  1.00108.94           C  
ANISOU  495  C   LEU A  68    15500  13426  12466   3903   1638  -1288       C  
ATOM    496  O   LEU A  68      -2.484  25.799  20.758  1.00114.04           O  
ANISOU  496  O   LEU A  68    15912  14317  13104   3581   1591  -1138       O  
ATOM    497  CB  LEU A  68      -0.263  27.986  20.494  1.00104.99           C  
ANISOU  497  CB  LEU A  68    15570  12016  12306   3726   1305  -1313       C  
ATOM    498  CG  LEU A  68       1.093  28.595  20.855  1.00 94.06           C  
ANISOU  498  CG  LEU A  68    14597  10147  10993   3546   1153  -1453       C  
ATOM    499  CD1 LEU A  68       1.820  29.073  19.606  1.00 74.29           C  
ANISOU  499  CD1 LEU A  68    12158   7305   8766   3500   1013  -1316       C  
ATOM    500  CD2 LEU A  68       0.933  29.725  21.853  1.00 94.99           C  
ANISOU  500  CD2 LEU A  68    15058  10041  10992   3784   1284  -1735       C  
ATOM    501  N   ASP A  69      -3.529  27.763  21.090  1.00 97.12           N  
ANISOU  501  N   ASP A  69    13873  12111  10918   4352   1817  -1342       N  
ATOM    502  CA  ASP A  69      -4.821  27.283  20.612  1.00100.09           C  
ANISOU  502  CA  ASP A  69    13743  13081  11206   4474   1952  -1228       C  
ATOM    503  C   ASP A  69      -5.112  27.781  19.199  1.00 86.12           C  
ANISOU  503  C   ASP A  69    11773  11327   9622   4743   1883  -1058       C  
ATOM    504  O   ASP A  69      -6.222  28.221  18.903  1.00 99.94           O  
ANISOU  504  O   ASP A  69    13225  13452  11296   5155   2021  -1031       O  
ATOM    505  CB  ASP A  69      -5.940  27.717  21.563  1.00108.69           C  
ANISOU  505  CB  ASP A  69    14723  14523  12052   4834   2218  -1388       C  
ATOM    506  N   VAL A  70      -4.109  27.709  18.332  1.00 79.75           N  
ANISOU  506  N   VAL A  70    11116  10151   9033   4528   1671   -935       N  
ATOM    507  CA  VAL A  70      -4.256  28.159  16.953  1.00 80.42           C  
ANISOU  507  CA  VAL A  70    11053  10222   9280   4754   1591   -751       C  
ATOM    508  C   VAL A  70      -4.255  26.979  15.987  1.00 72.99           C  
ANISOU  508  C   VAL A  70     9759   9597   8378   4373   1470   -577       C  
ATOM    509  O   VAL A  70      -3.229  26.331  15.782  1.00 75.06           O  
ANISOU  509  O   VAL A  70    10174   9600   8746   3964   1317   -532       O  
ATOM    510  CB  VAL A  70      -3.141  29.143  16.560  1.00 80.38           C  
ANISOU  510  CB  VAL A  70    11509   9538   9493   4833   1469   -738       C  
ATOM    511  CG1 VAL A  70      -3.312  29.586  15.118  1.00 75.47           C  
ANISOU  511  CG1 VAL A  70    10750   8913   9010   5077   1402   -514       C  
ATOM    512  CG2 VAL A  70      -3.145  30.344  17.495  1.00 78.74           C  
ANISOU  512  CG2 VAL A  70    11710   8967   9240   5180   1608   -944       C  
ATOM    513  N   LEU A  71      -5.413  26.708  15.395  1.00105.12           N  
ANISOU  513  N   LEU A  71    13349  14250  12342   4516   1544   -494       N  
ATOM    514  CA  LEU A  71      -5.570  25.571  14.494  1.00 93.46           C  
ANISOU  514  CA  LEU A  71    11519  13133  10860   4130   1456   -372       C  
ATOM    515  C   LEU A  71      -4.686  25.682  13.255  1.00 83.51           C  
ANISOU  515  C   LEU A  71    10378  11545   9809   4055   1252   -213       C  
ATOM    516  O   LEU A  71      -4.692  26.700  12.564  1.00 96.94           O  
ANISOU  516  O   LEU A  71    12141  13092  11600   4458   1214   -115       O  
ATOM    517  CB  LEU A  71      -7.035  25.424  14.074  1.00 82.89           C  
ANISOU  517  CB  LEU A  71     9606  12551   9339   4321   1571   -339       C  
ATOM    518  N   GLY A  72      -3.925  24.627  12.986  1.00 78.51           N  
ANISOU  518  N   GLY A  72     9798  10797   9235   3556   1140   -177       N  
ATOM    519  CA  GLY A  72      -3.120  24.548  11.781  1.00 73.09           C  
ANISOU  519  CA  GLY A  72     9172   9883   8716   3436    963    -32       C  
ATOM    520  C   GLY A  72      -1.747  25.172  11.920  1.00 64.40           C  
ANISOU  520  C   GLY A  72     8536   8128   7803   3431    852    -28       C  
ATOM    521  O   GLY A  72      -0.953  25.158  10.982  1.00 67.57           O  
ANISOU  521  O   GLY A  72     9016   8311   8346   3322    716     90       O  
ATOM    522  N   LEU A  73      -1.467  25.720  13.096  1.00 66.89           N  
ANISOU  522  N   LEU A  73     9148   8166   8102   3525    916   -172       N  
ATOM    523  CA  LEU A  73      -0.198  26.388  13.336  1.00 64.47           C  
ANISOU  523  CA  LEU A  73     9267   7283   7944   3484    819   -210       C  
ATOM    524  C   LEU A  73       0.902  25.383  13.654  1.00 69.79           C  
ANISOU  524  C   LEU A  73    10062   7816   8640   3029    702   -228       C  
ATOM    525  O   LEU A  73       0.785  24.594  14.592  1.00 85.80           O  
ANISOU  525  O   LEU A  73    12083   9992  10524   2842    755   -315       O  
ATOM    526  CB  LEU A  73      -0.340  27.397  14.475  1.00 64.79           C  
ANISOU  526  CB  LEU A  73     9589   7101   7928   3751    934   -392       C  
ATOM    527  CG  LEU A  73       0.875  28.284  14.741  1.00 80.00           C  
ANISOU  527  CG  LEU A  73    11966   8441   9989   3700    854   -475       C  
ATOM    528  CD1 LEU A  73       1.291  29.006  13.472  1.00 64.70           C  
ANISOU  528  CD1 LEU A  73    10112   6229   8242   3815    783   -305       C  
ATOM    529  CD2 LEU A  73       0.564  29.278  15.845  1.00 73.31           C  
ANISOU  529  CD2 LEU A  73    11403   7399   9052   3974    997   -689       C  
ATOM    530  N   THR A  74       1.968  25.408  12.862  1.00 60.18           N  
ANISOU  530  N   THR A  74     8955   6327   7584   2877    554   -130       N  
ATOM    531  CA  THR A  74       3.122  24.554  13.112  1.00 67.03           C  
ANISOU  531  CA  THR A  74     9938   7060   8471   2519    436   -133       C  
ATOM    532  C   THR A  74       4.414  25.358  13.055  1.00 62.96           C  
ANISOU  532  C   THR A  74     9699   6123   8099   2466    316   -156       C  
ATOM    533  O   THR A  74       4.419  26.519  12.641  1.00 63.74           O  
ANISOU  533  O   THR A  74     9924   5990   8305   2664    333   -144       O  
ATOM    534  CB  THR A  74       3.205  23.383  12.108  1.00 61.61           C  
ANISOU  534  CB  THR A  74     9035   6570   7804   2292    380     11       C  
ATOM    536  CG2 THR A  74       2.062  22.402  12.328  1.00 56.49           C  
ANISOU  536  CG2 THR A  74     8146   6330   6988   2206    507     -5       C  
ATOM    535  OG1 THR A  74       3.143  23.889  10.770  1.00 73.98           O  
ANISOU  535  OG1 THR A  74    10489   8128   9493   2417    333    145       O  
ATOM    537  N   PHE A  75       5.503  24.728  13.480  1.00 52.40           N  
ANISOU  537  N   PHE A  75     8459   4703   6749   2198    207   -183       N  
ATOM    538  CA  PHE A  75       6.822  25.345  13.486  1.00 55.70           C  
ANISOU  538  CA  PHE A  75     9077   4814   7272   2069     82   -223       C  
ATOM    539  C   PHE A  75       7.843  24.323  13.008  1.00 49.66           C  
ANISOU  539  C   PHE A  75     8219   4114   6536   1825    -46   -112       C  
ATOM    540  O   PHE A  75       7.708  23.130  13.283  1.00 64.02           O  
ANISOU  540  O   PHE A  75     9947   6135   8241   1740    -37    -75       O  
ATOM    541  CB  PHE A  75       7.193  25.810  14.895  1.00 65.12           C  
ANISOU  541  CB  PHE A  75    10503   5892   8350   2032     76   -439       C  
ATOM    542  CG  PHE A  75       6.218  26.784  15.494  1.00 70.70           C  
ANISOU  542  CG  PHE A  75    11342   6521   9001   2295    225   -580       C  
ATOM    543  CD1 PHE A  75       6.410  28.148  15.356  1.00 59.01           C  
ANISOU  543  CD1 PHE A  75    10108   4687   7628   2404    257   -663       C  
ATOM    544  CD2 PHE A  75       5.114  26.336  16.203  1.00 57.48           C  
ANISOU  544  CD2 PHE A  75     9566   5118   7154   2436    357   -631       C  
ATOM    545  CE1 PHE A  75       5.517  29.046  15.907  1.00 63.26           C  
ANISOU  545  CE1 PHE A  75    10807   5123   8105   2700    417   -797       C  
ATOM    546  CE2 PHE A  75       4.217  27.231  16.755  1.00 72.60           C  
ANISOU  546  CE2 PHE A  75    11587   6996   9003   2723    510   -765       C  
ATOM    547  CZ  PHE A  75       4.420  28.588  16.608  1.00 62.73           C  
ANISOU  547  CZ  PHE A  75    10601   5371   7862   2882    540   -850       C  
ATOM    548  N   ARG A  76       8.864  24.792  12.299  1.00 88.79           N  
ANISOU  548  N   ARG A  76    13215   8887  11633   1721   -146    -58       N  
ATOM    549  CA  ARG A  76       9.915  23.913  11.798  1.00 81.05           C  
ANISOU  549  CA  ARG A  76    12134   7983  10678   1533   -259     44       C  
ATOM    550  C   ARG A  76      11.281  24.275  12.366  1.00 79.57           C  
ANISOU  550  C   ARG A  76    12049   7695  10487   1356   -388    -53       C  
ATOM    551  O   ARG A  76      11.830  25.331  12.056  1.00 96.52           O  
ANISOU  551  O   ARG A  76    14289   9636  12749   1278   -414    -90       O  
ATOM    552  CB  ARG A  76       9.967  23.955  10.272  1.00 86.24           C  
ANISOU  552  CB  ARG A  76    12664   8627  11478   1541   -262    217       C  
ATOM    553  CG  ARG A  76       8.887  23.142   9.592  1.00106.07           C  
ANISOU  553  CG  ARG A  76    14996  11361  13946   1628   -181    318       C  
ATOM    554  CD  ARG A  76       8.846  23.440   8.109  1.00122.94           C  
ANISOU  554  CD  ARG A  76    17022  13497  16191   1671   -185    472       C  
ATOM    555  NE  ARG A  76      10.143  23.252   7.471  1.00116.25           N  
ANISOU  555  NE  ARG A  76    16168  12579  15424   1510   -278    547       N  
ATOM    556  CZ  ARG A  76      10.567  22.094   6.979  1.00100.22           C  
ANISOU  556  CZ  ARG A  76    14029  10692  13357   1407   -307    609       C  
ATOM    557  NH1 ARG A  76      11.763  22.011   6.411  1.00 81.56           N1+
ANISOU  557  NH1 ARG A  76    11641   8291  11056   1298   -378    674       N1+
ATOM    558  NH2 ARG A  76       9.796  21.018   7.058  1.00 87.87           N  
ANISOU  558  NH2 ARG A  76    12395   9307  11684   1403   -246    599       N  
ATOM    559  N   LYS A  77      11.825  23.391  13.196  1.00 59.51           N  
ANISOU  559  N   LYS A  77     9494   5321   7798   1285   -460    -88       N  
ATOM    560  CA  LYS A  77      13.160  23.586  13.746  1.00 69.42           C  
ANISOU  560  CA  LYS A  77    10771   6603   9003   1122   -607   -176       C  
ATOM    561  C   LYS A  77      14.180  22.826  12.904  1.00 73.24           C  
ANISOU  561  C   LYS A  77    11078   7215   9534   1048   -697    -22       C  
ATOM    562  O   LYS A  77      14.059  21.616  12.709  1.00 77.27           O  
ANISOU  562  O   LYS A  77    11519   7861   9981   1132   -675    102       O  
ATOM    563  CB  LYS A  77      13.218  23.116  15.200  1.00 64.85           C  
ANISOU  563  CB  LYS A  77    10272   6182   8187   1142   -647   -292       C  
ATOM    564  CG  LYS A  77      14.532  23.425  15.905  1.00 91.99           C  
ANISOU  564  CG  LYS A  77    13706   9726  11521    977   -817   -418       C  
ATOM    565  CD  LYS A  77      14.683  24.914  16.192  1.00 87.06           C  
ANISOU  565  CD  LYS A  77    13234   8889  10957    825   -823   -637       C  
ATOM    566  CE  LYS A  77      13.659  25.393  17.211  1.00 84.69           C  
ANISOU  566  CE  LYS A  77    13147   8493  10540    940   -715   -811       C  
ATOM    567  NZ  LYS A  77      13.799  26.847  17.510  1.00 84.36           N1+
ANISOU  567  NZ  LYS A  77    13324   8182  10546    803   -694  -1048       N1+
ATOM    568  N   ASP A  78      15.181  23.544  12.402  1.00 70.68           N  
ANISOU  568  N   ASP A  78    10701   6837   9316    882   -777    -37       N  
ATOM    569  CA  ASP A  78      16.203  22.948  11.547  1.00 63.91           C  
ANISOU  569  CA  ASP A  78     9650   6131   8503    822   -849    100       C  
ATOM    570  C   ASP A  78      17.145  22.030  12.321  1.00 61.88           C  
ANISOU  570  C   ASP A  78     9292   6161   8060    843   -973     94       C  
ATOM    571  O   ASP A  78      17.594  22.365  13.416  1.00 72.12           O  
ANISOU  571  O   ASP A  78    10624   7560   9219    767  -1069    -56       O  
ATOM    572  CB  ASP A  78      17.010  24.039  10.842  1.00 63.75           C  
ANISOU  572  CB  ASP A  78     9590   6003   8630    604   -879     83       C  
ATOM    573  CG  ASP A  78      16.174  24.853   9.878  1.00 71.12           C  
ANISOU  573  CG  ASP A  78    10633   6656   9735    643   -749    158       C  
ATOM    574  OD1 ASP A  78      15.154  24.328   9.386  1.00 75.13           O  
ANISOU  574  OD1 ASP A  78    11129   7160  10256    840   -662    267       O  
ATOM    575  OD2 ASP A  78      16.539  26.018   9.608  1.00 68.87           O1-
ANISOU  575  OD2 ASP A  78    10449   6164   9554    471   -728    112       O1-
ATOM    576  N   LEU A  79      17.441  20.872  11.741  1.00 54.32           N  
ANISOU  576  N   LEU A  79     8224   5340   7076    967   -965    257       N  
ATOM    577  CA  LEU A  79      18.393  19.935  12.326  1.00 57.29           C  
ANISOU  577  CA  LEU A  79     8508   5991   7268   1070  -1069    301       C  
ATOM    578  C   LEU A  79      19.616  19.848  11.429  1.00 67.26           C  
ANISOU  578  C   LEU A  79     9532   7432   8592   1023  -1137    384       C  
ATOM    579  O   LEU A  79      20.701  19.466  11.868  1.00 72.38           O  
ANISOU  579  O   LEU A  79    10024   8381   9096   1075  -1259    392       O  
ATOM    580  CB  LEU A  79      17.770  18.546  12.461  1.00 55.79           C  
ANISOU  580  CB  LEU A  79     8440   5789   6968   1296   -969    428       C  
ATOM    581  CG  LEU A  79      16.402  18.457  13.136  1.00 60.85           C  
ANISOU  581  CG  LEU A  79     9289   6276   7553   1330   -851    377       C  
ATOM    582  CD1 LEU A  79      15.955  17.004  13.228  1.00 46.63           C  
ANISOU  582  CD1 LEU A  79     7623   4463   5630   1488   -736    510       C  
ATOM    583  CD2 LEU A  79      16.442  19.111  14.505  1.00 57.91           C  
ANISOU  583  CD2 LEU A  79     8994   5975   7035   1288   -932    217       C  
ATOM    584  N   PHE A  80      19.422  20.199  10.163  1.00 55.82           N  
ANISOU  584  N   PHE A  80     8038   5836   7334    944  -1054    454       N  
ATOM    585  CA  PHE A  80      20.487  20.162   9.175  1.00 55.05           C  
ANISOU  585  CA  PHE A  80     7713   5903   7299    888  -1082    541       C  
ATOM    586  C   PHE A  80      20.149  21.083   8.012  1.00 65.09           C  
ANISOU  586  C   PHE A  80     8992   6963   8775    722   -994    577       C  
ATOM    587  O   PHE A  80      19.098  20.949   7.386  1.00 60.89           O  
ANISOU  587  O   PHE A  80     8580   6237   8320    806   -882    643       O  
ATOM    588  CB  PHE A  80      20.697  18.735   8.666  1.00 59.06           C  
ANISOU  588  CB  PHE A  80     8178   6529   7733   1147  -1032    692       C  
ATOM    589  CG  PHE A  80      21.550  18.651   7.431  1.00 77.33           C  
ANISOU  589  CG  PHE A  80    10279   8981  10121   1127  -1011    790       C  
ATOM    590  CD1 PHE A  80      22.929  18.763   7.515  1.00 83.49           C  
ANISOU  590  CD1 PHE A  80    10786  10102  10833   1088  -1118    786       C  
ATOM    591  CD2 PHE A  80      20.973  18.454   6.186  1.00 69.16           C  
ANISOU  591  CD2 PHE A  80     9291   7787   9199   1144   -882    880       C  
ATOM    592  CE1 PHE A  80      23.717  18.685   6.380  1.00 78.28           C  
ANISOU  592  CE1 PHE A  80     9910   9608  10227   1072  -1078    876       C  
ATOM    593  CE2 PHE A  80      21.755  18.375   5.047  1.00 68.58           C  
ANISOU  593  CE2 PHE A  80     9029   7857   9170   1131   -849    968       C  
ATOM    594  CZ  PHE A  80      23.129  18.491   5.145  1.00 68.75           C  
ANISOU  594  CZ  PHE A  80     8785   8204   9134   1099   -938    969       C  
ATOM    595  N   VAL A  81      21.040  22.025   7.730  1.00 67.66           N  
ANISOU  595  N   VAL A  81     9189   7350   9168    474  -1041    536       N  
ATOM    596  CA  VAL A  81      20.839  22.941   6.616  1.00 66.19           C  
ANISOU  596  CA  VAL A  81     9041   6954   9156    317   -944    603       C  
ATOM    597  C   VAL A  81      22.076  22.998   5.725  1.00 72.36           C  
ANISOU  597  C   VAL A  81     9565   7967   9963    169   -953    686       C  
ATOM    598  O   VAL A  81      23.193  23.189   6.207  1.00 74.92           O  
ANISOU  598  O   VAL A  81     9695   8556  10216     -3  -1053    602       O  
ATOM    599  CB  VAL A  81      20.489  24.362   7.101  1.00 60.54           C  
ANISOU  599  CB  VAL A  81     8533   5950   8521     97   -926    469       C  
ATOM    600  CG1 VAL A  81      20.232  25.272   5.914  1.00 61.61           C  
ANISOU  600  CG1 VAL A  81     8762   5829   8819     -8   -802    585       C  
ATOM    601  CG2 VAL A  81      19.274  24.333   8.013  1.00 57.29           C  
ANISOU  601  CG2 VAL A  81     8351   5353   8065    268   -903    377       C  
ATOM    602  N   ALA A  82      21.867  22.817   4.426  1.00 64.07           N  
ANISOU  602  N   ALA A  82     8488   6865   8991    233   -847    844       N  
ATOM    603  CA  ALA A  82      22.942  22.935   3.448  1.00 67.66           C  
ANISOU  603  CA  ALA A  82     8708   7530   9469     92   -819    938       C  
ATOM    604  C   ALA A  82      22.503  23.835   2.299  1.00 58.57           C  
ANISOU  604  C   ALA A  82     7679   6123   8450    -34   -690   1058       C  
ATOM    605  O   ALA A  82      21.364  23.757   1.841  1.00 63.71           O  
ANISOU  605  O   ALA A  82     8507   6560   9138    139   -619   1132       O  
ATOM    606  CB  ALA A  82      23.347  21.567   2.931  1.00 66.89           C  
ANISOU  606  CB  ALA A  82     8432   7712   9273    359   -808   1032       C  
ATOM    607  N   ASN A  83      23.409  24.690   1.837  1.00 73.24           N  
ANISOU  607  N   ASN A  83     9437   8032  10359   -341   -654   1085       N  
ATOM    608  CA  ASN A  83      23.088  25.647   0.783  1.00 68.64           C  
ANISOU  608  CA  ASN A  83     9012   7184   9884   -474   -516   1227       C  
ATOM    609  C   ASN A  83      24.028  25.573  -0.412  1.00 74.06           C  
ANISOU  609  C   ASN A  83     9467   8118  10555   -598   -435   1375       C  
ATOM    610  O   ASN A  83      25.209  25.257  -0.273  1.00 85.00           O  
ANISOU  610  O   ASN A  83    10551   9872  11875   -730   -483   1326       O  
ATOM    611  CB  ASN A  83      23.069  27.074   1.334  1.00 79.36           C  
ANISOU  611  CB  ASN A  83    10616   8205  11331   -785   -485   1133       C  
ATOM    612  CG  ASN A  83      24.463  27.626   1.590  1.00120.48           C  
ANISOU  612  CG  ASN A  83    15635  13616  16524  -1221   -509   1034       C  
ATOM    614  ND2 ASN A  83      25.347  26.791   2.124  1.00143.13           N  
ANISOU  614  ND2 ASN A  83    18159  16948  19276  -1210   -640    938       N  
ATOM    613  OD1 ASN A  83      24.740  28.793   1.307  1.00136.56           O  
ANISOU  613  OD1 ASN A  83    17839  15406  18641  -1567   -403   1048       O  
ATOM    615  N   VAL A  84      23.488  25.867  -1.588  1.00 85.77           N  
ANISOU  615  N   VAL A  84    11074   9439  12076   -534   -310   1561       N  
ATOM    616  CA  VAL A  84      24.277  25.934  -2.807  1.00 55.98           C  
ANISOU  616  CA  VAL A  84     7127   5867   8276   -662   -202   1721       C  
ATOM    617  C   VAL A  84      23.820  27.131  -3.628  1.00 87.08           C  
ANISOU  617  C   VAL A  84    11342   9456  12289   -796    -56   1898       C  
ATOM    618  O   VAL A  84      22.623  27.335  -3.827  1.00 83.80           O  
ANISOU  618  O   VAL A  84    11180   8766  11895   -565    -32   1974       O  
ATOM    619  CB  VAL A  84      24.140  24.647  -3.654  1.00 64.96           C  
ANISOU  619  CB  VAL A  84     8099   7278   9306   -340   -186   1803       C  
ATOM    620  CG1 VAL A  84      24.749  24.842  -5.033  1.00 78.14           C  
ANISOU  620  CG1 VAL A  84     9642   9114  10931   -446    -47   1986       C  
ATOM    621  CG2 VAL A  84      24.792  23.468  -2.950  1.00 80.29           C  
ANISOU  621  CG2 VAL A  84     9793   9557  11159   -188   -292   1667       C  
ATOM    622  N   GLN A  85      24.775  27.933  -4.085  1.00 83.36           N  
ANISOU  622  N   GLN A  85    10822   9010  11842  -1165     49   1971       N  
ATOM    623  CA  GLN A  85      24.467  29.035  -4.982  1.00 76.69           C  
ANISOU  623  CA  GLN A  85    10267   7829  11043  -1290    221   2186       C  
ATOM    624  C   GLN A  85      24.476  28.539  -6.422  1.00 67.61           C  
ANISOU  624  C   GLN A  85     8987   6914   9789  -1121    316   2413       C  
ATOM    625  O   GLN A  85      25.533  28.426  -7.042  1.00 91.49           O  
ANISOU  625  O   GLN A  85    11760  10247  12756  -1332    394   2476       O  
ATOM    626  CB  GLN A  85      25.475  30.169  -4.806  1.00 67.53           C  
ANISOU  626  CB  GLN A  85     9166   6547   9946  -1829    324   2160       C  
ATOM    627  CG  GLN A  85      25.252  31.342  -5.746  1.00 91.63           C  
ANISOU  627  CG  GLN A  85    12577   9201  13036  -1981    540   2413       C  
ATOM    628  CD  GLN A  85      26.299  32.424  -5.586  1.00 75.46           C  
ANISOU  628  CD  GLN A  85    10612   7016  11043  -2593    673   2373       C  
ATOM    630  NE2 GLN A  85      26.679  33.046  -6.693  1.00 88.36           N  
ANISOU  630  NE2 GLN A  85    12351   8570  12651  -2810    884   2625       N  
ATOM    629  OE1 GLN A  85      26.768  32.693  -4.480  1.00128.42           O  
ANISOU  629  OE1 GLN A  85    17290  13708  17796  -2895    592   2113       O  
ATOM    631  N   SER A  86      23.295  28.231  -6.945  1.00 65.49           N  
ANISOU  631  N   SER A  86     8866   6543   9474   -745    309   2523       N  
ATOM    632  CA  SER A  86      23.174  27.760  -8.319  1.00 67.42           C  
ANISOU  632  CA  SER A  86     9013   7018   9585   -571    388   2719       C  
ATOM    633  C   SER A  86      23.380  28.898  -9.306  1.00 79.94           C  
ANISOU  633  C   SER A  86    10798   8419  11157   -760    575   2989       C  
ATOM    634  O   SER A  86      24.050  28.728 -10.324  1.00 79.86           O  
ANISOU  634  O   SER A  86    10624   8679  11042   -850    682   3129       O  
ATOM    635  CB  SER A  86      21.817  27.095  -8.554  1.00 68.15           C  
ANISOU  635  CB  SER A  86     9181   7113   9602   -154    312   2729       C  
ATOM    636  OG  SER A  86      21.732  25.861  -7.863  1.00 79.70           O  
ANISOU  636  OG  SER A  86    10457   8784  11042     -1    181   2508       O  
ATOM    637  N   PHE A  87      22.806  30.060  -9.007  1.00 80.78           N  
ANISOU  637  N   PHE A  87    11286   8050  11356   -804    635   3070       N  
ATOM    638  CA  PHE A  87      22.970  31.210  -9.891  1.00 85.15           C  
ANISOU  638  CA  PHE A  87    12118   8342  11894   -972    840   3355       C  
ATOM    639  C   PHE A  87      23.472  32.450  -9.153  1.00 87.66           C  
ANISOU  639  C   PHE A  87    12732   8213  12361  -1387    943   3303       C  
ATOM    640  O   PHE A  87      22.924  32.824  -8.122  1.00 80.85           O  
ANISOU  640  O   PHE A  87    12091   7023  11606  -1332    875   3144       O  
ATOM    641  CB  PHE A  87      21.667  31.520 -10.633  1.00 90.78           C  
ANISOU  641  CB  PHE A  87    13103   8874  12515   -546    873   3598       C  
ATOM    642  CG  PHE A  87      21.764  32.702 -11.557  1.00 92.10           C  
ANISOU  642  CG  PHE A  87    13615   8741  12639   -648   1096   3937       C  
ATOM    643  CD1 PHE A  87      21.200  33.918 -11.208  1.00 93.12           C  
ANISOU  643  CD1 PHE A  87    14232   8293  12856   -603   1197   4048       C  
ATOM    644  CD2 PHE A  87      22.427  32.599 -12.769  1.00 85.86           C  
ANISOU  644  CD2 PHE A  87    12692   8229  11704   -773   1224   4152       C  
ATOM    645  CE1 PHE A  87      21.290  35.009 -12.055  1.00102.78           C  
ANISOU  645  CE1 PHE A  87    15837   9185  14028   -677   1428   4387       C  
ATOM    646  CE2 PHE A  87      22.523  33.687 -13.620  1.00 86.99           C  
ANISOU  646  CE2 PHE A  87    13184   8082  11786   -873   1450   4493       C  
ATOM    647  CZ  PHE A  87      21.953  34.893 -13.262  1.00 95.81           C  
ANISOU  647  CZ  PHE A  87    14819   8587  12996   -823   1554   4621       C  
ATOM    648  N   PRO A  88      24.544  33.072  -9.666  1.00 92.79           N  
ANISOU  648  N   PRO A  88    13385   8864  13006  -1838   1120   3417       N  
ATOM    649  CA  PRO A  88      25.353  32.564 -10.779  1.00102.05           C  
ANISOU  649  CA  PRO A  88    14232  10502  14042  -1942   1206   3565       C  
ATOM    650  C   PRO A  88      26.300  31.474 -10.285  1.00104.36           C  
ANISOU  650  C   PRO A  88    13987  11348  14316  -2059   1069   3302       C  
ATOM    651  O   PRO A  88      26.466  31.338  -9.073  1.00101.07           O  
ANISOU  651  O   PRO A  88    13490  10914  13997  -2160    929   3032       O  
ATOM    652  CB  PRO A  88      26.143  33.800 -11.216  1.00 92.48           C  
ANISOU  652  CB  PRO A  88    13267   9016  12853  -2456   1463   3747       C  
ATOM    653  CG  PRO A  88      26.275  34.607  -9.979  1.00 93.54           C  
ANISOU  653  CG  PRO A  88    13655   8729  13159  -2788   1452   3526       C  
ATOM    654  CD  PRO A  88      24.988  34.408  -9.229  1.00 89.11           C  
ANISOU  654  CD  PRO A  88    13294   7905  12657  -2300   1282   3414       C  
ATOM    655  N   PRO A  89      26.889  30.692 -11.205  1.00119.07           N  
ANISOU  655  N   PRO A  89    15499  13709  16035  -2003   1111   3383       N  
ATOM    656  CA  PRO A  89      27.874  29.672 -10.827  1.00129.55           C  
ANISOU  656  CA  PRO A  89    16318  15583  17321  -2060   1012   3166       C  
ATOM    657  C   PRO A  89      28.996  30.251  -9.970  1.00131.82           C  
ANISOU  657  C   PRO A  89    16449  15941  17696  -2592   1024   2998       C  
ATOM    658  O   PRO A  89      29.583  31.271 -10.333  1.00126.95           O  
ANISOU  658  O   PRO A  89    15950  15189  17098  -3053   1213   3120       O  
ATOM    659  CB  PRO A  89      28.422  29.212 -12.177  1.00128.57           C  
ANISOU  659  CB  PRO A  89    15955  15878  17020  -2014   1157   3350       C  
ATOM    660  CG  PRO A  89      27.276  29.392 -13.109  1.00120.55           C  
ANISOU  660  CG  PRO A  89    15271  14611  15922  -1691   1211   3589       C  
ATOM    661  CD  PRO A  89      26.562  30.633 -12.642  1.00116.46           C  
ANISOU  661  CD  PRO A  89    15234  13475  15541  -1797   1244   3677       C  
ATOM    662  N   ALA A  90      29.272  29.604  -8.842  1.00134.20           N  
ANISOU  662  N   ALA A  90    16498  16460  18030  -2540    828   2721       N  
ATOM    663  CA  ALA A  90      30.287  30.070  -7.903  1.00139.81           C  
ANISOU  663  CA  ALA A  90    17013  17319  18790  -3025    792   2517       C  
ATOM    664  C   ALA A  90      31.659  30.178  -8.562  1.00148.21           C  
ANISOU  664  C   ALA A  90    17671  18885  19756  -3425    942   2578       C  
ATOM    665  O   ALA A  90      32.057  29.295  -9.322  1.00148.12           O  
ANISOU  665  O   ALA A  90    17322  19341  19615  -3176    974   2658       O  
ATOM    666  CB  ALA A  90      30.348  29.149  -6.691  1.00135.79           C  
ANISOU  666  CB  ALA A  90    16248  17074  18272  -2792    542   2244       C  
ATOM    667  N   PRO A  91      32.385  31.268  -8.270  1.00160.33           N  
ANISOU  667  N   PRO A  91    19246  20330  21341  -4065   1050   2527       N  
ATOM    668  CA  PRO A  91      33.699  31.522  -8.871  1.00164.91           C  
ANISOU  668  CA  PRO A  91    19437  21397  21825  -4549   1222   2582       C  
ATOM    669  C   PRO A  91      34.730  30.491  -8.430  1.00155.03           C  
ANISOU  669  C   PRO A  91    17492  20960  20450  -4461   1071   2388       C  
ATOM    670  O   PRO A  91      35.645  30.164  -9.186  1.00148.44           O  
ANISOU  670  O   PRO A  91    16228  20689  19485  -4547   1194   2474       O  
ATOM    671  CB  PRO A  91      34.069  32.905  -8.325  1.00173.08           C  
ANISOU  671  CB  PRO A  91    20737  22068  22957  -5279   1331   2490       C  
ATOM    672  CG  PRO A  91      33.306  33.023  -7.050  1.00171.04           C  
ANISOU  672  CG  PRO A  91    20772  21401  22813  -5139   1123   2257       C  
ATOM    673  CD  PRO A  91      32.011  32.310  -7.298  1.00163.43           C  
ANISOU  673  CD  PRO A  91    20056  20167  21873  -4394   1025   2382       C  
ATOM    674  N   GLU A  92      34.573  29.982  -7.214  1.00146.61           N  
ANISOU  674  N   GLU A  92    16325  19971  19407  -4254    817   2141       N  
ATOM    675  CA  GLU A  92      35.505  29.006  -6.669  1.00139.61           C  
ANISOU  675  CA  GLU A  92    14815  19844  18385  -4096    655   1968       C  
ATOM    676  C   GLU A  92      35.101  27.589  -7.049  1.00131.17           C  
ANISOU  676  C   GLU A  92    13628  18976  17234  -3338    579   2040       C  
ATOM    677  O   GLU A  92      35.897  26.833  -7.603  1.00126.15           O  
ANISOU  677  O   GLU A  92    12540  18938  16452  -3150    631   2084       O  
ATOM    678  CB  GLU A  92      35.566  29.132  -5.148  1.00131.10           C  
ANISOU  678  CB  GLU A  92    13700  18777  17333  -4232    419   1678       C  
ATOM    679  CG  GLU A  92      36.444  28.094  -4.481  1.00132.26           C  
ANISOU  679  CG  GLU A  92    13230  19709  17313  -3977    224   1519       C  
ATOM    680  CD  GLU A  92      37.735  28.677  -3.941  1.00151.32           C  
ANISOU  680  CD  GLU A  92    15161  22706  19627  -4610    195   1333       C  
ATOM    681  OE1 GLU A  92      38.291  29.596  -4.580  1.00153.08           O  
ANISOU  681  OE1 GLU A  92    15347  22948  19866  -5221    406   1394       O  
ATOM    682  OE2 GLU A  92      38.188  28.220  -2.871  1.00163.15           O1-
ANISOU  682  OE2 GLU A  92    16317  24660  21011  -4511    -35   1126       O1-
ATOM    683  N   ASP A  93      33.852  27.245  -6.752  1.00125.10           N  
ANISOU  683  N   ASP A  93    13280  17702  16549  -2917    474   2040       N  
ATOM    684  CA  ASP A  93      33.343  25.891  -6.941  1.00112.80           C  
ANISOU  684  CA  ASP A  93    11692  16246  14920  -2245    394   2063       C  
ATOM    685  C   ASP A  93      33.425  25.387  -8.380  1.00100.86           C  
ANISOU  685  C   ASP A  93    10102  14915  13306  -2016    578   2261       C  
ATOM    686  O   ASP A  93      32.852  25.978  -9.294  1.00115.76           O  
ANISOU  686  O   ASP A  93    12299  16456  15228  -2116    729   2445       O  
ATOM    687  CB  ASP A  93      31.901  25.797  -6.438  1.00123.73           C  
ANISOU  687  CB  ASP A  93    13570  17025  16415  -1950    284   2034       C  
ATOM    688  CG  ASP A  93      31.802  25.914  -4.931  1.00151.06           C  
ANISOU  688  CG  ASP A  93    17070  20400  19928  -2015     80   1811       C  
ATOM    689  OD1 ASP A  93      32.788  25.575  -4.243  1.00156.91           O  
ANISOU  689  OD1 ASP A  93    17401  21645  20573  -2079    -28   1670       O  
ATOM    690  OD2 ASP A  93      30.739  26.343  -4.435  1.00160.41           O1-
ANISOU  690  OD2 ASP A  93    18676  21050  21223  -1982     29   1777       O1-
ATOM    691  N   LYS A  94      34.151  24.289  -8.565  1.00 92.49           N  
ANISOU  691  N   LYS A  94     8634  14412  12096  -1681    570   2225       N  
ATOM    692  CA  LYS A  94      34.199  23.595  -9.845  1.00 77.25           C  
ANISOU  692  CA  LYS A  94     6638  12675  10038  -1374    734   2365       C  
ATOM    693  C   LYS A  94      33.950  22.112  -9.598  1.00 82.03           C  
ANISOU  693  C   LYS A  94     7213  13400  10555   -737    635   2267       C  
ATOM    694  O   LYS A  94      34.846  21.388  -9.167  1.00 76.23           O  
ANISOU  694  O   LYS A  94     6089  13162   9711   -522    585   2174       O  
ATOM    695  CB  LYS A  94      35.553  23.801 -10.525  1.00 82.03           C  
ANISOU  695  CB  LYS A  94     6754  13901  10514  -1640    907   2431       C  
ATOM    696  CG  LYS A  94      35.904  25.259 -10.784  1.00113.98           C  
ANISOU  696  CG  LYS A  94    10842  17833  14632  -2339   1044   2530       C  
ATOM    697  CD  LYS A  94      37.327  25.401 -11.302  1.00 90.85           C  
ANISOU  697  CD  LYS A  94     7350  15611  11559  -2647   1210   2565       C  
ATOM    698  CE  LYS A  94      37.726  26.861 -11.432  1.00112.57           C  
ANISOU  698  CE  LYS A  94    10163  18228  14380  -3428   1360   2640       C  
ATOM    699  NZ  LYS A  94      39.154  27.014 -11.840  1.00103.10           N1+
ANISOU  699  NZ  LYS A  94     8357  17786  13029  -3801   1523   2650       N1+
ATOM    700  N   LYS A  95      32.725  21.666  -9.860  1.00 70.65           N  
ANISOU  700  N   LYS A  95     6190  11508   9147   -437    615   2290       N  
ATOM    701  CA  LYS A  95      32.326  20.301  -9.533  1.00 85.82           C  
ANISOU  701  CA  LYS A  95     8194  13412  11000    104    534   2182       C  
ATOM    702  C   LYS A  95      31.753  19.566 -10.744  1.00 84.77           C  
ANISOU  702  C   LYS A  95     8256  13196  10758    405    672   2245       C  
ATOM    703  O   LYS A  95      31.133  20.178 -11.612  1.00 86.86           O  
ANISOU  703  O   LYS A  95     8731  13237  11034    232    760   2370       O  
ATOM    704  CB  LYS A  95      31.319  20.292  -8.371  1.00 88.35           C  
ANISOU  704  CB  LYS A  95     8839  13281  11449    166    345   2077       C  
ATOM    705  CG  LYS A  95      30.864  21.672  -7.893  1.00 98.39           C  
ANISOU  705  CG  LYS A  95    10302  14195  12886   -285    288   2098       C  
ATOM    706  CD  LYS A  95      31.854  22.326  -6.921  1.00 93.61           C  
ANISOU  706  CD  LYS A  95     9404  13851  12312   -629    198   2002       C  
ATOM    707  CE  LYS A  95      31.645  21.887  -5.476  1.00 72.90           C  
ANISOU  707  CE  LYS A  95     6817  11175   9706   -455    -11   1832       C  
ATOM    708  NZ  LYS A  95      32.085  20.491  -5.228  1.00 70.76           N1+
ANISOU  708  NZ  LYS A  95     6342  11256   9289     43    -58   1781       N1+
ATOM    709  N   PRO A  96      31.967  18.241 -10.809  1.00 86.88           N  
ANISOU  709  N   PRO A  96     8470  13646  10894    868    697   2157       N  
ATOM    710  CA  PRO A  96      31.439  17.434 -11.915  1.00 65.62           C  
ANISOU  710  CA  PRO A  96     5986  10877   8071   1145    832   2163       C  
ATOM    711  C   PRO A  96      29.927  17.259 -11.828  1.00 70.89           C  
ANISOU  711  C   PRO A  96     7111  11021   8803   1194    752   2119       C  
ATOM    712  O   PRO A  96      29.377  17.149 -10.733  1.00 78.73           O  
ANISOU  712  O   PRO A  96     8262  11744   9906   1231    601   2035       O  
ATOM    713  CB  PRO A  96      32.136  16.083 -11.725  1.00 85.15           C  
ANISOU  713  CB  PRO A  96     8319  13631  10402   1630    877   2052       C  
ATOM    714  CG  PRO A  96      32.427  16.019 -10.269  1.00 93.18           C  
ANISOU  714  CG  PRO A  96     9234  14665  11505   1687    696   1981       C  
ATOM    715  CD  PRO A  96      32.757  17.428  -9.868  1.00 93.12           C  
ANISOU  715  CD  PRO A  96     9018  14737  11627   1171    614   2048       C  
ATOM    716  N   LEU A  97      29.266  17.236 -12.979  1.00 73.21           N  
ANISOU  716  N   LEU A  97     7589  11223   9005   1190    855   2174       N  
ATOM    717  CA  LEU A  97      27.819  17.065 -13.035  1.00 78.34           C  
ANISOU  717  CA  LEU A  97     8611  11478   9675   1223    786   2129       C  
ATOM    718  C   LEU A  97      27.444  15.589 -13.013  1.00 73.08           C  
ANISOU  718  C   LEU A  97     8135  10734   8896   1573    813   1946       C  
ATOM    719  O   LEU A  97      28.185  14.745 -13.516  1.00 74.70           O  
ANISOU  719  O   LEU A  97     8247  11183   8954   1816    945   1889       O  
ATOM    720  CB  LEU A  97      27.251  17.715 -14.301  1.00 65.26           C  
ANISOU  720  CB  LEU A  97     7053   9815   7929   1064    871   2273       C  
ATOM    721  CG  LEU A  97      26.928  19.213 -14.307  1.00 73.43           C  
ANISOU  721  CG  LEU A  97     8134  10682   9085    734    833   2466       C  
ATOM    722  CD1 LEU A  97      28.146  20.064 -13.978  1.00 97.35           C  
ANISOU  722  CD1 LEU A  97    10893  13891  12204    468    877   2561       C  
ATOM    723  CD2 LEU A  97      26.351  19.614 -15.656  1.00 74.48           C  
ANISOU  723  CD2 LEU A  97     8386  10851   9062    691    929   2624       C  
ATOM    724  N   THR A  98      26.295  15.279 -12.423  1.00 67.33           N  
ANISOU  724  N   THR A  98     7692   9658   8230   1595    708   1850       N  
ATOM    725  CA  THR A  98      25.752  13.929 -12.497  1.00 66.64           C  
ANISOU  725  CA  THR A  98     7864   9428   8029   1840    760   1672       C  
ATOM    726  C   THR A  98      25.149  13.743 -13.883  1.00 74.12           C  
ANISOU  726  C   THR A  98     8929  10437   8797   1799    863   1652       C  
ATOM    727  O   THR A  98      24.867  14.723 -14.571  1.00 69.67           O  
ANISOU  727  O   THR A  98     8289   9959   8223   1594    851   1797       O  
ATOM    728  CB  THR A  98      24.670  13.686 -11.425  1.00 69.36           C  
ANISOU  728  CB  THR A  98     8462   9410   8482   1814    631   1576       C  
ATOM    730  CG2 THR A  98      25.201  14.024 -10.041  1.00 54.05           C  
ANISOU  730  CG2 THR A  98     6407   7432   6698   1825    510   1605       C  
ATOM    729  OG1 THR A  98      23.521  14.497 -11.702  1.00 70.95           O  
ANISOU  729  OG1 THR A  98     8750   9481   8727   1578    554   1631       O  
ATOM    731  N   ARG A  99      24.960  12.492 -14.294  1.00 73.15           N  
ANISOU  731  N   ARG A  99     9013  10266   8513   1995    972   1472       N  
ATOM    732  CA  ARG A  99      24.382  12.198 -15.604  1.00 66.88           C  
ANISOU  732  CA  ARG A  99     8341   9565   7506   1945   1067   1403       C  
ATOM    733  C   ARG A  99      22.979  12.789 -15.731  1.00 74.34           C  
ANISOU  733  C   ARG A  99     9393  10387   8465   1699    938   1426       C  
ATOM    734  O   ARG A  99      22.617  13.343 -16.772  1.00 66.80           O  
ANISOU  734  O   ARG A  99     8383   9620   7377   1582    950   1515       O  
ATOM    735  CB  ARG A  99      24.349  10.690 -15.856  1.00 74.04           C  
ANISOU  735  CB  ARG A  99     9525  10364   8244   2168   1212   1157       C  
ATOM    736  N   LEU A 100      22.201  12.671 -14.658  1.00 66.38           N  
ANISOU  736  N   LEU A 100     8525   9098   7598   1647    820   1356       N  
ATOM    737  CA  LEU A 100      20.869  13.259 -14.600  1.00 63.03           C  
ANISOU  737  CA  LEU A 100     8158   8590   7199   1453    692   1381       C  
ATOM    738  C   LEU A 100      20.944  14.755 -14.864  1.00 63.03           C  
ANISOU  738  C   LEU A 100     7963   8704   7280   1337    621   1642       C  
ATOM    739  O   LEU A 100      20.166  15.302 -15.649  1.00 72.44           O  
ANISOU  739  O   LEU A 100     9149  10016   8361   1252    588   1726       O  
ATOM    740  CB  LEU A 100      20.238  13.013 -13.227  1.00 60.67           C  
ANISOU  740  CB  LEU A 100     7993   7994   7064   1431    592   1293       C  
ATOM    741  CG  LEU A 100      18.921  13.745 -12.958  1.00 59.23           C  
ANISOU  741  CG  LEU A 100     7817   7752   6935   1266    457   1335       C  
ATOM    742  CD1 LEU A 100      17.798  13.175 -13.810  1.00 58.76           C  
ANISOU  742  CD1 LEU A 100     7855   7815   6657   1163    475   1187       C  
ATOM    743  CD2 LEU A 100      18.559  13.698 -11.481  1.00 63.79           C  
ANISOU  743  CD2 LEU A 100     8480   8064   7694   1259    373   1287       C  
ATOM    744  N   GLN A 101      21.896  15.409 -14.206  1.00 67.14           N  
ANISOU  744  N   GLN A 101     8338   9195   7976   1334    605   1770       N  
ATOM    745  CA  GLN A 101      22.071  16.847 -14.344  1.00 56.94           C  
ANISOU  745  CA  GLN A 101     6921   7933   6779   1186    569   2010       C  
ATOM    746  C   GLN A 101      22.427  17.244 -15.768  1.00 69.57           C  
ANISOU  746  C   GLN A 101     8430   9805   8196   1151    684   2161       C  
ATOM    747  O   GLN A 101      21.833  18.163 -16.316  1.00 74.05           O  
ANISOU  747  O   GLN A 101     9028  10383   8724   1066    659   2338       O  
ATOM    748  CB  GLN A 101      23.125  17.367 -13.368  1.00 71.18           C  
ANISOU  748  CB  GLN A 101     8581   9685   8778   1130    544   2069       C  
ATOM    749  CG  GLN A 101      22.602  17.564 -11.957  1.00 79.45           C  
ANISOU  749  CG  GLN A 101     9723  10449  10014   1101    404   2001       C  
ATOM    750  CD  GLN A 101      23.697  17.923 -10.976  1.00 74.00           C  
ANISOU  750  CD  GLN A 101     8876   9773   9469   1043    368   2013       C  
ATOM    752  NE2 GLN A 101      23.319  18.582  -9.887  1.00 70.11           N  
ANISOU  752  NE2 GLN A 101     8450   9053   9136    940    252   2006       N  
ATOM    751  OE1 GLN A 101      24.870  17.616 -11.195  1.00 70.81           O  
ANISOU  751  OE1 GLN A 101     8274   9618   9013   1092    445   2018       O  
ATOM    753  N   GLU A 102      23.384  16.550 -16.372  1.00 73.36           N  
ANISOU  753  N   GLU A 102     8811  10516   8546   1248    821   2104       N  
ATOM    754  CA  GLU A 102      23.790  16.893 -17.731  1.00 82.69           C  
ANISOU  754  CA  GLU A 102     9900  11991   9528   1214    952   2247       C  
ATOM    755  C   GLU A 102      22.675  16.622 -18.747  1.00 74.33           C  
ANISOU  755  C   GLU A 102     8986  11028   8228   1236    942   2207       C  
ATOM    756  O   GLU A 102      22.536  17.350 -19.731  1.00 76.99           O  
ANISOU  756  O   GLU A 102     9293  11543   8416   1174    983   2404       O  
ATOM    757  CB  GLU A 102      25.108  16.208 -18.122  1.00 67.86           C  
ANISOU  757  CB  GLU A 102     7854  10380   7548   1340   1119   2184       C  
ATOM    758  CG  GLU A 102      25.080  14.696 -18.129  1.00 84.30           C  
ANISOU  758  CG  GLU A 102    10068  12453   9508   1580   1179   1907       C  
ATOM    759  CD  GLU A 102      26.469  14.094 -18.235  1.00107.27           C  
ANISOU  759  CD  GLU A 102    12796  15605  12358   1780   1337   1861       C  
ATOM    760  OE1 GLU A 102      26.578  12.896 -18.573  1.00121.58           O  
ANISOU  760  OE1 GLU A 102    14744  17442  14010   2015   1450   1658       O  
ATOM    761  OE2 GLU A 102      27.453  14.819 -17.975  1.00101.54           O1-
ANISOU  761  OE2 GLU A 102    11793  15053  11735   1702   1359   2019       O1-
ATOM    762  N   ARG A 103      21.869  15.593 -18.497  1.00 77.28           N  
ANISOU  762  N   ARG A 103     9520  11299   8544   1306    890   1955       N  
ATOM    763  CA  ARG A 103      20.694  15.347 -19.328  1.00 57.62           C  
ANISOU  763  CA  ARG A 103     7136   8937   5819   1273    848   1880       C  
ATOM    764  C   ARG A 103      19.695  16.493 -19.190  1.00 77.09           C  
ANISOU  764  C   ARG A 103     9591  11353   8347   1194    702   2082       C  
ATOM    765  O   ARG A 103      19.134  16.964 -20.183  1.00 75.31           O  
ANISOU  765  O   ARG A 103     9347  11361   7907   1188    688   2212       O  
ATOM    766  CB  ARG A 103      20.031  14.019 -18.963  1.00 70.56           C  
ANISOU  766  CB  ARG A 103     8961  10448   7400   1291    835   1548       C  
ATOM    767  CG  ARG A 103      20.850  12.793 -19.334  1.00 73.73           C  
ANISOU  767  CG  ARG A 103     9456  10889   7669   1419   1009   1332       C  
ATOM    768  CD  ARG A 103      20.256  11.525 -18.744  1.00 73.19           C  
ANISOU  768  CD  ARG A 103     9648  10568   7593   1419   1021   1022       C  
ATOM    769  NE  ARG A 103      18.948  11.214 -19.310  1.00 98.00           N  
ANISOU  769  NE  ARG A 103    12898  13811  10528   1236    962    858       N  
ATOM    770  CZ  ARG A 103      18.192  10.191 -18.922  1.00113.96           C  
ANISOU  770  CZ  ARG A 103    15154  15640  12505   1130    974    577       C  
ATOM    771  NH1 ARG A 103      18.613   9.380 -17.962  1.00 98.96           N1+
ANISOU  771  NH1 ARG A 103    13453  13391  10757   1230   1052    457       N1+
ATOM    772  NH2 ARG A 103      17.014   9.980 -19.493  1.00134.95           N  
ANISOU  772  NH2 ARG A 103    17849  18477  14949    914    913    422       N  
ATOM    773  N   LEU A 104      19.483  16.943 -17.955  1.00 61.46           N  
ANISOU  773  N   LEU A 104     7631   9081   6638   1167    601   2112       N  
ATOM    774  CA  LEU A 104      18.578  18.060 -17.694  1.00 68.47           C  
ANISOU  774  CA  LEU A 104     8535   9876   7606   1144    482   2300       C  
ATOM    775  C   LEU A 104      19.060  19.350 -18.351  1.00 69.76           C  
ANISOU  775  C   LEU A 104     8656  10096   7755   1124    542   2635       C  
ATOM    776  O   LEU A 104      18.256  20.131 -18.852  1.00 84.67           O  
ANISOU  776  O   LEU A 104    10581  12051   9539   1176    493   2825       O  
ATOM    777  CB  LEU A 104      18.391  18.274 -16.189  1.00 61.07           C  
ANISOU  777  CB  LEU A 104     7645   8601   6958   1123    388   2245       C  
ATOM    778  CG  LEU A 104      17.466  17.297 -15.460  1.00 73.81           C  
ANISOU  778  CG  LEU A 104     9339  10125   8579   1126    311   1980       C  
ATOM    779  CD1 LEU A 104      17.642  17.415 -13.955  1.00 55.42           C  
ANISOU  779  CD1 LEU A 104     7055   7481   6521   1115    254   1930       C  
ATOM    780  CD2 LEU A 104      16.017  17.543 -15.845  1.00 53.22           C  
ANISOU  780  CD2 LEU A 104     6724   7673   5823   1135    214   1991       C  
ATOM    781  N   ILE A 105      20.371  19.571 -18.341  1.00 57.14           N  
ANISOU  781  N   ILE A 105     6980   8483   6246   1052    658   2716       N  
ATOM    782  CA  ILE A 105      20.951  20.744 -18.982  1.00 67.81           C  
ANISOU  782  CA  ILE A 105     8312   9875   7577    967    758   3030       C  
ATOM    783  C   ILE A 105      20.763  20.636 -20.488  1.00 70.21           C  
ANISOU  783  C   ILE A 105     8603  10531   7541   1033    838   3137       C  
ATOM    784  O   ILE A 105      20.440  21.619 -21.158  1.00 82.45           O  
ANISOU  784  O   ILE A 105    10224  12119   8984   1045    863   3424       O  
ATOM    785  CB  ILE A 105      22.457  20.890 -18.670  1.00 85.38           C  
ANISOU  785  CB  ILE A 105    10400  12100   9942    825    879   3057       C  
ATOM    786  CG1 ILE A 105      22.695  20.969 -17.160  1.00 74.90           C  
ANISOU  786  CG1 ILE A 105     9064  10482   8911    756    785   2935       C  
ATOM    787  CG2 ILE A 105      23.034  22.119 -19.357  1.00 70.93           C  
ANISOU  787  CG2 ILE A 105     8572  10299   8079    667   1013   3384       C  
ATOM    788  CD1 ILE A 105      21.835  21.983 -16.458  1.00 77.63           C  
ANISOU  788  CD1 ILE A 105     9581  10492   9422    716    679   3042       C  
ATOM    789  N   LYS A 106      20.956  19.429 -21.011  1.00 66.81           N  
ANISOU  789  N   LYS A 106     8114  10348   6923   1093    888   2905       N  
ATOM    790  CA  LYS A 106      20.776  19.174 -22.434  1.00 72.45           C  
ANISOU  790  CA  LYS A 106     8818  11435   7274   1149    961   2945       C  
ATOM    791  C   LYS A 106      19.335  19.429 -22.868  1.00 81.20           C  
ANISOU  791  C   LYS A 106    10000  12658   8194   1227    819   2999       C  
ATOM    792  O   LYS A 106      19.088  19.889 -23.983  1.00 78.24           O  
ANISOU  792  O   LYS A 106     9627  12561   7540   1279    851   3201       O  
ATOM    793  CB  LYS A 106      21.191  17.742 -22.784  1.00 79.19           C  
ANISOU  793  CB  LYS A 106     9645  12474   7969   1204   1047   2622       C  
ATOM    794  CG  LYS A 106      21.216  17.452 -24.277  1.00 97.32           C  
ANISOU  794  CG  LYS A 106    11930  15181   9869   1245   1154   2633       C  
ATOM    795  CD  LYS A 106      21.720  16.048 -24.571  1.00120.16           C  
ANISOU  795  CD  LYS A 106    14844  18196  12615   1315   1273   2293       C  
ATOM    796  CE  LYS A 106      20.786  14.991 -24.005  1.00138.29           C  
ANISOU  796  CE  LYS A 106    17291  20328  14925   1315   1161   1945       C  
ATOM    797  NZ  LYS A 106      21.252  13.610 -24.317  1.00149.57           N1+
ANISOU  797  NZ  LYS A 106    18828  21804  16199   1394   1308   1609       N1+
ATOM    798  N   LYS A 107      18.385  19.138 -21.984  1.00 77.14           N  
ANISOU  798  N   LYS A 107     9527  11972   7810   1245    664   2828       N  
ATOM    799  CA  LYS A 107      16.974  19.328 -22.308  1.00 85.21           C  
ANISOU  799  CA  LYS A 107    10556  13174   8646   1327    518   2854       C  
ATOM    800  C   LYS A 107      16.519  20.779 -22.163  1.00 77.20           C  
ANISOU  800  C   LYS A 107     9591  12024   7717   1433    463   3218       C  
ATOM    801  O   LYS A 107      15.844  21.321 -23.038  1.00 70.11           O  
ANISOU  801  O   LYS A 107     8687  11394   6556   1567    424   3427       O  
ATOM    802  CB  LYS A 107      16.087  18.427 -21.446  1.00 77.81           C  
ANISOU  802  CB  LYS A 107     9626  12152   7789   1284    395   2523       C  
ATOM    803  CG  LYS A 107      14.614  18.782 -21.540  1.00 85.44           C  
ANISOU  803  CG  LYS A 107    10535  13317   8610   1364    232   2565       C  
ATOM    804  CD  LYS A 107      13.746  17.917 -20.644  1.00 82.24           C  
ANISOU  804  CD  LYS A 107    10120  12844   8286   1268    135   2241       C  
ATOM    805  CE  LYS A 107      12.320  18.443 -20.631  1.00 61.17           C  
ANISOU  805  CE  LYS A 107     7334  10413   5495   1368    -24   2318       C  
ATOM    806  NZ  LYS A 107      11.369  17.478 -20.035  1.00 84.36           N1+
ANISOU  806  NZ  LYS A 107    10218  13427   8410   1214   -102   1976       N1+
ATOM    807  N   LEU A 108      16.896  21.403 -21.053  1.00 74.45           N  
ANISOU  807  N   LEU A 108     9312  11258   7718   1390    468   3290       N  
ATOM    808  CA  LEU A 108      16.392  22.726 -20.705  1.00 69.62           C  
ANISOU  808  CA  LEU A 108     8814  10414   7224   1500    428   3582       C  
ATOM    809  C   LEU A 108      17.194  23.844 -21.357  1.00 80.53           C  
ANISOU  809  C   LEU A 108    10307  11706   8584   1473    583   3954       C  
ATOM    810  O   LEU A 108      16.629  24.839 -21.811  1.00 88.06           O  
ANISOU  810  O   LEU A 108    11387  12645   9428   1640    585   4265       O  
ATOM    811  CB  LEU A 108      16.376  22.908 -19.185  1.00 80.06           C  
ANISOU  811  CB  LEU A 108    10197  11314   8910   1444    371   3462       C  
ATOM    812  CG  LEU A 108      15.153  22.417 -18.403  1.00 88.89           C  
ANISOU  812  CG  LEU A 108    11273  12439  10064   1532    213   3242       C  
ATOM    813  CD1 LEU A 108      14.834  20.958 -18.683  1.00 83.60           C  
ANISOU  813  CD1 LEU A 108    10479  12071   9214   1461    170   2913       C  
ATOM    814  CD2 LEU A 108      15.370  22.632 -16.916  1.00 92.11           C  
ANISOU  814  CD2 LEU A 108    11757  12425  10817   1460    188   3140       C  
ATOM    815  N   GLY A 109      18.511  23.681 -21.397  1.00 71.99           N  
ANISOU  815  N   GLY A 109     9184  10576   7594   1271    726   3930       N  
ATOM    816  CA  GLY A 109      19.378  24.684 -21.987  1.00 71.95           C  
ANISOU  816  CA  GLY A 109     9271  10497   7570   1164    906   4261       C  
ATOM    817  C   GLY A 109      20.297  25.327 -20.967  1.00 73.11           C  
ANISOU  817  C   GLY A 109     9476  10239   8064    928    981   4283       C  
ATOM    818  O   GLY A 109      20.455  24.823 -19.855  1.00 73.24           O  
ANISOU  818  O   GLY A 109     9418  10100   8311    859    896   4016       O  
ATOM    819  N   GLU A 110      20.896  26.451 -21.346  1.00 90.30           N  
ANISOU  819  N   GLU A 110    11800  12253  10256    786   1147   4601       N  
ATOM    820  CA  GLU A 110      21.876  27.129 -20.503  1.00 77.93           C  
ANISOU  820  CA  GLU A 110    10282  10348   8980    476   1244   4617       C  
ATOM    821  C   GLU A 110      21.259  27.770 -19.260  1.00 81.07           C  
ANISOU  821  C   GLU A 110    10879  10275   9649    498   1135   4567       C  
ATOM    822  O   GLU A 110      21.960  28.038 -18.284  1.00 85.09           O  
ANISOU  822  O   GLU A 110    11381  10539  10409    242   1153   4448       O  
ATOM    823  CB  GLU A 110      22.633  28.185 -21.315  1.00 76.38           C  
ANISOU  823  CB  GLU A 110    10230  10091   8701    263   1482   4976       C  
ATOM    824  N   HIS A 111      19.952  28.011 -19.296  1.00 84.83           N  
ANISOU  824  N   HIS A 111    11511  10669  10051    810   1024   4648       N  
ATOM    825  CA  HIS A 111      19.268  28.678 -18.189  1.00 88.37           C  
ANISOU  825  CA  HIS A 111    12168  10683  10724    891    943   4618       C  
ATOM    826  C   HIS A 111      18.994  27.753 -17.000  1.00 91.72           C  
ANISOU  826  C   HIS A 111    12419  11114  11318    902    767   4232       C  
ATOM    827  O   HIS A 111      18.491  28.192 -15.964  1.00 84.90           O  
ANISOU  827  O   HIS A 111    11696   9921  10641    951    698   4158       O  
ATOM    828  CB  HIS A 111      17.970  29.327 -18.671  1.00 78.22           C  
ANISOU  828  CB  HIS A 111    11092   9353   9275   1273    904   4871       C  
ATOM    829  CG  HIS A 111      18.184  30.511 -19.561  1.00 88.98           C  
ANISOU  829  CG  HIS A 111    12736  10547  10527   1264   1073   5212       C  
ATOM    831  CD2 HIS A 111      17.476  30.971 -20.620  1.00 87.81           C  
ANISOU  831  CD2 HIS A 111    12686  10557  10120   1522   1061   5375       C  
ATOM    830  ND1 HIS A 111      19.245  31.377 -19.405  1.00101.57           N  
ANISOU  830  ND1 HIS A 111    14537  11778  12277    911   1265   5335       N  
ATOM    832  CE1 HIS A 111      19.180  32.321 -20.327  1.00 83.08           C  
ANISOU  832  CE1 HIS A 111    12449   9338   9778    952   1371   5567       C  
ATOM    833  NE2 HIS A 111      18.116  32.097 -21.077  1.00 92.93           N  
ANISOU  833  NE2 HIS A 111    13633  10900  10777   1344   1246   5606       N  
ATOM    834  N   ALA A 112      19.327  26.475 -17.151  1.00 76.61           N  
ANISOU  834  N   ALA A 112    10230   9555   9323    870    712   3993       N  
ATOM    835  CA  ALA A 112      19.188  25.523 -16.057  1.00 76.87           C  
ANISOU  835  CA  ALA A 112    10129   9580   9497    869    576   3650       C  
ATOM    836  C   ALA A 112      20.507  25.392 -15.303  1.00 78.14           C  
ANISOU  836  C   ALA A 112    10184   9656   9850    593    624   3513       C  
ATOM    837  O   ALA A 112      21.529  25.039 -15.887  1.00 87.36           O  
ANISOU  837  O   ALA A 112    11188  11064  10940    462    726   3523       O  
ATOM    838  CB  ALA A 112      18.737  24.172 -16.581  1.00 58.62           C  
ANISOU  838  CB  ALA A 112     7639   7653   6981   1007    504   3455       C  
ATOM    839  N   TYR A 113      20.483  25.687 -14.007  1.00 67.71           N  
ANISOU  839  N   TYR A 113     8934   8038   8755    515    551   3381       N  
ATOM    840  CA  TYR A 113      21.693  25.627 -13.195  1.00 68.92           C  
ANISOU  840  CA  TYR A 113     8961   8157   9068    254    569   3244       C  
ATOM    841  C   TYR A 113      21.615  24.515 -12.161  1.00 63.65           C  
ANISOU  841  C   TYR A 113     8161   7556   8466    344    431   2945       C  
ATOM    842  O   TYR A 113      20.686  24.470 -11.356  1.00 71.06           O  
ANISOU  842  O   TYR A 113     9216   8306   9477    468    323   2840       O  
ATOM    843  CB  TYR A 113      21.955  26.974 -12.521  1.00 67.30           C  
ANISOU  843  CB  TYR A 113     8966   7558   9047     20    618   3334       C  
ATOM    844  CG  TYR A 113      22.158  28.096 -13.508  1.00 70.60           C  
ANISOU  844  CG  TYR A 113     9572   7849   9402   -103    795   3652       C  
ATOM    845  CD1 TYR A 113      21.097  28.895 -13.907  1.00 80.22           C  
ANISOU  845  CD1 TYR A 113    11094   8816  10572    111    822   3871       C  
ATOM    846  CD2 TYR A 113      23.410  28.346 -14.054  1.00 78.31           C  
ANISOU  846  CD2 TYR A 113    10422   8983  10348   -416    947   3749       C  
ATOM    847  CE1 TYR A 113      21.277  29.919 -14.817  1.00 78.60           C  
ANISOU  847  CE1 TYR A 113    11114   8463  10288     31   1001   4198       C  
ATOM    848  CE2 TYR A 113      23.600  29.367 -14.963  1.00 82.79           C  
ANISOU  848  CE2 TYR A 113    11197   9415  10844   -554   1136   4060       C  
ATOM    849  CZ  TYR A 113      22.531  30.150 -15.341  1.00 74.38           C  
ANISOU  849  CZ  TYR A 113    10485   8045   9730   -323   1164   4294       C  
ATOM    850  OH  TYR A 113      22.717  31.170 -16.247  1.00 95.18           O  
ANISOU  850  OH  TYR A 113    13378  10512  12275   -429   1369   4638       O  
ATOM    851  N   PRO A 114      22.606  23.615 -12.176  1.00 66.21           N  
ANISOU  851  N   PRO A 114     8249   8159   8750    303    451   2819       N  
ATOM    852  CA  PRO A 114      22.598  22.415 -11.336  1.00 54.20           C  
ANISOU  852  CA  PRO A 114     6632   6714   7247    441    349   2568       C  
ATOM    853  C   PRO A 114      22.764  22.712  -9.849  1.00 58.66           C  
ANISOU  853  C   PRO A 114     7223   7070   7993    343    246   2438       C  
ATOM    854  O   PRO A 114      23.368  23.714  -9.470  1.00 66.61           O  
ANISOU  854  O   PRO A 114     8237   7962   9111     99    268   2496       O  
ATOM    855  CB  PRO A 114      23.814  21.635 -11.844  1.00 57.31           C  
ANISOU  855  CB  PRO A 114     6778   7459   7539    442    436   2528       C  
ATOM    856  CG  PRO A 114      24.735  22.684 -12.357  1.00 56.96           C  
ANISOU  856  CG  PRO A 114     6643   7487   7513    176    554   2714       C  
ATOM    857  CD  PRO A 114      23.842  23.726 -12.970  1.00 58.79           C  
ANISOU  857  CD  PRO A 114     7123   7479   7734    136    592   2926       C  
ATOM    858  N   PHE A 115      22.208  21.836  -9.019  1.00 57.74           N  
ANISOU  858  N   PHE A 115     7144   6907   7889    511    143   2257       N  
ATOM    859  CA  PHE A 115      22.490  21.829  -7.590  1.00 60.24           C  
ANISOU  859  CA  PHE A 115     7451   7114   8323    460     42   2110       C  
ATOM    860  C   PHE A 115      22.649  20.388  -7.128  1.00 59.23           C  
ANISOU  860  C   PHE A 115     7250   7135   8122    666      0   1948       C  
ATOM    861  O   PHE A 115      21.939  19.493  -7.599  1.00 60.81           O  
ANISOU  861  O   PHE A 115     7530   7354   8220    839     25   1903       O  
ATOM    862  CB  PHE A 115      21.396  22.543  -6.784  1.00 63.41           C  
ANISOU  862  CB  PHE A 115     8079   7184   8829    458    -31   2084       C  
ATOM    863  CG  PHE A 115      20.032  21.921  -6.910  1.00 60.12           C  
ANISOU  863  CG  PHE A 115     7781   6720   8343    675    -61   2040       C  
ATOM    864  CD1 PHE A 115      19.629  20.914  -6.048  1.00 56.50           C  
ANISOU  864  CD1 PHE A 115     7344   6257   7866    794   -127   1866       C  
ATOM    865  CD2 PHE A 115      19.145  22.357  -7.881  1.00 60.45           C  
ANISOU  865  CD2 PHE A 115     7906   6747   8317    748    -18   2180       C  
ATOM    866  CE1 PHE A 115      18.373  20.345  -6.161  1.00 60.70           C  
ANISOU  866  CE1 PHE A 115     7966   6773   8324    924   -139   1810       C  
ATOM    867  CE2 PHE A 115      17.887  21.794  -7.997  1.00 55.33           C  
ANISOU  867  CE2 PHE A 115     7309   6136   7579    911    -54   2121       C  
ATOM    868  CZ  PHE A 115      17.502  20.786  -7.136  1.00 62.41           C  
ANISOU  868  CZ  PHE A 115     8214   7031   8470    970   -109   1925       C  
ATOM    869  N   THR A 116      23.589  20.170  -6.214  1.00 58.33           N  
ANISOU  869  N   THR A 116     6996   7130   8039    642    -56   1860       N  
ATOM    870  CA  THR A 116      23.858  18.839  -5.690  1.00 60.14           C  
ANISOU  870  CA  THR A 116     7186   7478   8185    884    -82   1739       C  
ATOM    871  C   THR A 116      24.125  18.894  -4.191  1.00 64.28           C  
ANISOU  871  C   THR A 116     7696   7962   8764    872   -208   1636       C  
ATOM    872  O   THR A 116      25.084  19.527  -3.747  1.00 58.33           O  
ANISOU  872  O   THR A 116     6751   7367   8046    704   -256   1634       O  
ATOM    873  CB  THR A 116      25.070  18.195  -6.386  1.00 58.12           C  
ANISOU  873  CB  THR A 116     6693   7573   7818    992      6   1767       C  
ATOM    875  CG2 THR A 116      25.316  16.798  -5.846  1.00 70.00           C  
ANISOU  875  CG2 THR A 116     8223   9149   9224   1311      1   1661       C  
ATOM    874  OG1 THR A 116      24.830  18.119  -7.796  1.00 81.78           O  
ANISOU  874  OG1 THR A 116     9712  10629  10732   1003    130   1851       O  
ATOM    876  N   PHE A 117      23.271  18.233  -3.416  1.00 60.68           N  
ANISOU  876  N   PHE A 117     7438   7322   8295   1024   -257   1544       N  
ATOM    877  CA  PHE A 117      23.463  18.150  -1.973  1.00 60.30           C  
ANISOU  877  CA  PHE A 117     7402   7253   8256   1055   -372   1451       C  
ATOM    878  C   PHE A 117      23.918  16.760  -1.561  1.00 62.05           C  
ANISOU  878  C   PHE A 117     7621   7607   8348   1358   -365   1410       C  
ATOM    879  O   PHE A 117      23.435  15.753  -2.078  1.00 66.08           O  
ANISOU  879  O   PHE A 117     8290   8032   8787   1539   -270   1402       O  
ATOM    880  CB  PHE A 117      22.179  18.504  -1.223  1.00 44.63           C  
ANISOU  880  CB  PHE A 117     5661   4962   6336   1008   -420   1390       C  
ATOM    881  CG  PHE A 117      21.725  19.917  -1.429  1.00 54.71           C  
ANISOU  881  CG  PHE A 117     6990   6065   7732    777   -423   1432       C  
ATOM    882  CD1 PHE A 117      20.628  20.194  -2.225  1.00 43.85           C  
ANISOU  882  CD1 PHE A 117     5748   4533   6379    789   -358   1497       C  
ATOM    883  CD2 PHE A 117      22.396  20.969  -0.828  1.00 54.00           C  
ANISOU  883  CD2 PHE A 117     6829   5974   7713    553   -484   1403       C  
ATOM    884  CE1 PHE A 117      20.205  21.492  -2.416  1.00 52.38           C  
ANISOU  884  CE1 PHE A 117     6916   5431   7553    649   -345   1565       C  
ATOM    885  CE2 PHE A 117      21.978  22.272  -1.017  1.00 60.87           C  
ANISOU  885  CE2 PHE A 117     7827   6610   8691    356   -454   1445       C  
ATOM    886  CZ  PHE A 117      20.880  22.534  -1.812  1.00 58.11           C  
ANISOU  886  CZ  PHE A 117     7637   6077   8367    437   -379   1542       C  
ATOM    887  N   GLU A 118      24.855  16.713  -0.624  1.00 68.07           N  
ANISOU  887  N   GLU A 118     7019   8411  10434   -211    256   2345       N  
ATOM    888  CA  GLU A 118      25.304  15.452  -0.068  1.00 60.47           C  
ANISOU  888  CA  GLU A 118     5742   7593   9641   -150    299   2446       C  
ATOM    889  C   GLU A 118      24.731  15.314   1.334  1.00 59.96           C  
ANISOU  889  C   GLU A 118     5741   7525   9518   -314    -43   2246       C  
ATOM    890  O   GLU A 118      24.998  16.142   2.204  1.00 78.35           O  
ANISOU  890  O   GLU A 118     8097   9795  11878   -638   -336   2313       O  
ATOM    891  CB  GLU A 118      26.831  15.401  -0.024  1.00 81.49           C  
ANISOU  891  CB  GLU A 118     7956  10359  12648   -302    380   2922       C  
ATOM    892  CG  GLU A 118      27.396  14.066   0.426  1.00107.05           C  
ANISOU  892  CG  GLU A 118    10833  13745  16095   -186    480   3093       C  
ATOM    893  CD  GLU A 118      27.168  12.964  -0.589  1.00133.53           C  
ANISOU  893  CD  GLU A 118    14252  17108  19376    233    913   3019       C  
ATOM    894  OE1 GLU A 118      27.050  13.275  -1.793  1.00122.78           O  
ANISOU  894  OE1 GLU A 118    13095  15666  17892    401   1188   2996       O  
ATOM    895  OE2 GLU A 118      27.106  11.784  -0.182  1.00159.94           O1-
ANISOU  895  OE2 GLU A 118    17487  20520  22763    385    979   2983       O1-
ATOM    896  N   ILE A 119      23.928  14.279   1.547  1.00 66.58           N  
ANISOU  896  N   ILE A 119     6645   8403  10248   -103     -2   1999       N  
ATOM    897  CA  ILE A 119      23.372  14.016   2.866  1.00 59.99           C  
ANISOU  897  CA  ILE A 119     5873   7565   9357   -225   -274   1815       C  
ATOM    898  C   ILE A 119      24.343  13.189   3.698  1.00 50.80           C  
ANISOU  898  C   ILE A 119     4345   6528   8429   -340   -348   2070       C  
ATOM    899  O   ILE A 119      24.626  12.038   3.370  1.00 69.15           O  
ANISOU  899  O   ILE A 119     6466   8952  10855   -119   -123   2152       O  
ATOM    900  CB  ILE A 119      22.025  13.281   2.781  1.00 72.01           C  
ANISOU  900  CB  ILE A 119     7613   9076  10671     30   -212   1454       C  
ATOM    901  CG1 ILE A 119      21.017  14.112   1.986  1.00 59.59           C  
ANISOU  901  CG1 ILE A 119     6365   7393   8884    143   -177   1242       C  
ATOM    902  CG2 ILE A 119      21.493  12.988   4.176  1.00 66.22           C  
ANISOU  902  CG2 ILE A 119     6937   8332   9891    -90   -451   1289       C  
ATOM    903  CD1 ILE A 119      19.652  13.476   1.889  1.00 48.63           C  
ANISOU  903  CD1 ILE A 119     5154   6008   7316    356   -158    932       C  
ATOM    904  N   PRO A 120      24.864  13.782   4.780  1.00 62.54           N  
ANISOU  904  N   PRO A 120     5775   7994   9991   -693   -672   2210       N  
ATOM    905  CA  PRO A 120      25.791  13.083   5.672  1.00 69.01           C  
ANISOU  905  CA  PRO A 120     6245   8941  11037   -848   -819   2489       C  
ATOM    906  C   PRO A 120      25.088  11.970   6.437  1.00 63.50           C  
ANISOU  906  C   PRO A 120     5607   8275  10245   -708   -851   2258       C  
ATOM    907  O   PRO A 120      23.876  12.047   6.646  1.00 63.19           O  
ANISOU  907  O   PRO A 120     5914   8136   9958   -622   -879   1885       O  
ATOM    908  CB  PRO A 120      26.237  14.183   6.638  1.00 79.32           C  
ANISOU  908  CB  PRO A 120     7638  10161  12338  -1310  -1223   2616       C  
ATOM    909  CG  PRO A 120      25.117  15.157   6.639  1.00 75.44           C  
ANISOU  909  CG  PRO A 120     7656   9467  11540  -1327  -1282   2252       C  
ATOM    910  CD  PRO A 120      24.582  15.153   5.238  1.00 62.06           C  
ANISOU  910  CD  PRO A 120     6029   7768   9782   -977   -930   2119       C  
ATOM    911  N   PRO A 121      25.841  10.942   6.851  1.00 66.29           N  
ANISOU  911  N   PRO A 121     5611   8766  10812   -677   -835   2504       N  
ATOM    912  CA  PRO A 121      25.288   9.848   7.654  1.00 64.94           C  
ANISOU  912  CA  PRO A 121     5485   8622  10569   -569   -876   2324       C  
ATOM    913  C   PRO A 121      24.821  10.336   9.023  1.00 72.78           C  
ANISOU  913  C   PRO A 121     6742   9520  11392   -871  -1262   2159       C  
ATOM    914  O   PRO A 121      25.110  11.474   9.403  1.00 63.65           O  
ANISOU  914  O   PRO A 121     5710   8277  10195  -1192  -1518   2237       O  
ATOM    915  CB  PRO A 121      26.477   8.896   7.811  1.00 79.05           C  
ANISOU  915  CB  PRO A 121     6800  10566  12669   -522   -805   2735       C  
ATOM    916  CG  PRO A 121      27.676   9.763   7.653  1.00 86.60           C  
ANISOU  916  CG  PRO A 121     7462  11578  13863   -779   -922   3157       C  
ATOM    917  CD  PRO A 121      27.285  10.777   6.618  1.00 80.62           C  
ANISOU  917  CD  PRO A 121     6945  10716  12972   -743   -775   3006       C  
ATOM    918  N   ASN A 122      24.103   9.476   9.742  1.00 68.42           N  
ANISOU  918  N   ASN A 122     6314   8960  10722   -771  -1284   1936       N  
ATOM    919  CA  ASN A 122      23.611   9.776  11.086  1.00 72.90           C  
ANISOU  919  CA  ASN A 122     7174   9419  11104  -1015  -1592   1771       C  
ATOM    920  C   ASN A 122      22.560  10.877  11.137  1.00 68.93           C  
ANISOU  920  C   ASN A 122     7130   8726  10334  -1069  -1632   1450       C  
ATOM    921  O   ASN A 122      22.322  11.471  12.188  1.00 73.18           O  
ANISOU  921  O   ASN A 122     7977   9122  10705  -1320  -1877   1362       O  
ATOM    922  CB  ASN A 122      24.764  10.088  12.045  1.00 76.14           C  
ANISOU  922  CB  ASN A 122     7428   9862  11641  -1409  -1960   2122       C  
ATOM    923  CG  ASN A 122      25.637   8.885  12.310  1.00105.29           C  
ANISOU  923  CG  ASN A 122    10684  13735  15587  -1340  -1955   2437       C  
ATOM    925  ND2 ASN A 122      26.946   9.104  12.373  1.00119.55           N  
ANISOU  925  ND2 ASN A 122    12114  15653  17658  -1565  -2131   2897       N  
ATOM    924  OD1 ASN A 122      25.143   7.767  12.454  1.00116.20           O  
ANISOU  924  OD1 ASN A 122    12057  15153  16940  -1088  -1791   2290       O  
ATOM    926  N   LEU A 123      21.933  11.148   9.999  1.00 65.73           N  
ANISOU  926  N   LEU A 123     6796   8301   9878   -825  -1380   1291       N  
ATOM    927  CA  LEU A 123      20.797  12.059   9.968  1.00 63.01           C  
ANISOU  927  CA  LEU A 123     6851   7786   9302   -791  -1366    996       C  
ATOM    928  C   LEU A 123      19.501  11.265  10.100  1.00 62.25           C  
ANISOU  928  C   LEU A 123     6880   7689   9082   -530  -1218    687       C  
ATOM    929  O   LEU A 123      19.436  10.106   9.692  1.00 53.12           O  
ANISOU  929  O   LEU A 123     5516   6662   8007   -326  -1060    678       O  
ATOM    930  CB  LEU A 123      20.797  12.890   8.684  1.00 57.97           C  
ANISOU  930  CB  LEU A 123     6230   7122   8673   -693  -1215   1022       C  
ATOM    931  CG  LEU A 123      21.875  13.971   8.597  1.00 65.82           C  
ANISOU  931  CG  LEU A 123     7190   8066   9753   -990  -1368   1294       C  
ATOM    932  CD1 LEU A 123      21.597  14.903   7.427  1.00 66.81           C  
ANISOU  932  CD1 LEU A 123     7445   8118   9824   -878  -1211   1253       C  
ATOM    933  CD2 LEU A 123      21.956  14.746   9.900  1.00 53.41           C  
ANISOU  933  CD2 LEU A 123     5919   6325   8048  -1347  -1683   1282       C  
ATOM    934  N   PRO A 124      18.465  11.883  10.684  1.00 51.91           N  
ANISOU  934  N   PRO A 124     5923   6221   7581   -538  -1253    451       N  
ATOM    935  CA  PRO A 124      17.190  11.187  10.876  1.00 49.36           C  
ANISOU  935  CA  PRO A 124     5688   5901   7168   -312  -1117    193       C  
ATOM    936  C   PRO A 124      16.531  10.854   9.545  1.00 47.59           C  
ANISOU  936  C   PRO A 124     5345   5768   6968    -27   -905    103       C  
ATOM    937  O   PRO A 124      16.633  11.637   8.603  1.00 70.48           O  
ANISOU  937  O   PRO A 124     8267   8645   9867     13   -857    153       O  
ATOM    938  CB  PRO A 124      16.332  12.217  11.619  1.00 56.61           C  
ANISOU  938  CB  PRO A 124     7008   6602   7898   -368  -1155     26       C  
ATOM    939  CG  PRO A 124      17.285  13.232  12.142  1.00 72.15           C  
ANISOU  939  CG  PRO A 124     9153   8437   9823   -690  -1367    184       C  
ATOM    940  CD  PRO A 124      18.427  13.263  11.193  1.00 49.49           C  
ANISOU  940  CD  PRO A 124     5964   5705   7134   -754  -1396    433       C  
ATOM    941  N   CYS A 125      15.868   9.707   9.466  1.00 43.21           N  
ANISOU  941  N   CYS A 125     4697   5303   6417    144   -797    -20       N  
ATOM    942  CA  CYS A 125      15.072   9.384   8.291  1.00 50.74           C  
ANISOU  942  CA  CYS A 125     5611   6321   7348    371   -645   -124       C  
ATOM    943  C   CYS A 125      13.733  10.109   8.375  1.00 55.30           C  
ANISOU  943  C   CYS A 125     6381   6810   7823    463   -633   -295       C  
ATOM    944  O   CYS A 125      13.366  10.621   9.432  1.00 53.76           O  
ANISOU  944  O   CYS A 125     6361   6496   7570    389   -684   -359       O  
ATOM    945  CB  CYS A 125      14.868   7.875   8.167  1.00 38.83           C  
ANISOU  945  CB  CYS A 125     3964   4920   5870    482   -551   -179       C  
ATOM    946  SG  CYS A 125      16.369   6.969   7.719  1.00 76.35           S  
ANISOU  946  SG  CYS A 125     8481   9766  10762    482   -463     58       S  
ATOM    947  N   SER A 126      13.017  10.171   7.257  1.00 53.73           N  
ANISOU  947  N   SER A 126     6165   6655   7596    628   -558   -347       N  
ATOM    948  CA  SER A 126      11.727  10.851   7.221  1.00 34.97           C  
ANISOU  948  CA  SER A 126     3907   4217   5164    748   -541   -452       C  
ATOM    949  C   SER A 126      10.674  10.088   8.013  1.00 44.76           C  
ANISOU  949  C   SER A 126     5116   5481   6409    808   -510   -582       C  
ATOM    950  O   SER A 126      10.290   8.976   7.655  1.00 50.39           O  
ANISOU  950  O   SER A 126     5695   6311   7142    859   -489   -630       O  
ATOM    951  CB  SER A 126      11.263  11.071   5.783  1.00 39.44           C  
ANISOU  951  CB  SER A 126     4444   4841   5701    888   -514   -434       C  
ATOM    952  OG  SER A 126      11.942  12.168   5.200  1.00 54.81           O  
ANISOU  952  OG  SER A 126     6484   6713   7627    855   -521   -323       O  
ATOM    953  N   VAL A 127      10.222  10.695   9.104  1.00 45.05           N  
ANISOU  953  N   VAL A 127     5315   5386   6416    791   -490   -631       N  
ATOM    954  CA  VAL A 127       9.238  10.082   9.978  1.00 44.22           C  
ANISOU  954  CA  VAL A 127     5201   5280   6323    850   -420   -733       C  
ATOM    955  C   VAL A 127       8.155  11.101  10.313  1.00 48.52           C  
ANISOU  955  C   VAL A 127     5894   5692   6851    993   -313   -756       C  
ATOM    956  O   VAL A 127       8.447  12.251  10.645  1.00 46.40           O  
ANISOU  956  O   VAL A 127     5873   5245   6510    962   -296   -727       O  
ATOM    957  CB  VAL A 127       9.888   9.560  11.285  1.00 45.61           C  
ANISOU  957  CB  VAL A 127     5468   5397   6465    687   -453   -754       C  
ATOM    958  CG1 VAL A 127       8.837   8.960  12.210  1.00 42.18           C  
ANISOU  958  CG1 VAL A 127     5053   4942   6031    755   -346   -856       C  
ATOM    959  CG2 VAL A 127      10.965   8.534  10.974  1.00 33.66           C  
ANISOU  959  CG2 VAL A 127     3777   4013   5000    587   -530   -688       C  
ATOM    960  N   THR A 128       6.902  10.678  10.207  1.00 41.65           N  
ANISOU  960  N   THR A 128     4873   4898   6054   1147   -232   -785       N  
ATOM    961  CA  THR A 128       5.774  11.535  10.534  1.00 39.57           C  
ANISOU  961  CA  THR A 128     4691   4522   5821   1334    -81   -763       C  
ATOM    962  C   THR A 128       5.031  10.957  11.727  1.00 46.82           C  
ANISOU  962  C   THR A 128     5624   5398   6769   1370     67   -822       C  
ATOM    963  O   THR A 128       4.721   9.772  11.752  1.00 45.19           O  
ANISOU  963  O   THR A 128     5203   5340   6627   1333     39   -856       O  
ATOM    964  CB  THR A 128       4.808  11.665   9.340  1.00 45.01           C  
ANISOU  964  CB  THR A 128     5141   5347   6613   1506   -106   -678       C  
ATOM    966  CG2 THR A 128       3.556  12.428   9.741  1.00 43.29           C  
ANISOU  966  CG2 THR A 128     4933   5032   6481   1738     82   -606       C  
ATOM    965  OG1 THR A 128       5.461  12.361   8.271  1.00 51.97           O  
ANISOU  965  OG1 THR A 128     6076   6229   7441   1491   -212   -619       O  
ATOM    967  N   LEU A 129       4.756  11.791  12.722  1.00 48.37           N  
ANISOU  967  N   LEU A 129     6114   5367   6899   1438    244   -833       N  
ATOM    968  CA  LEU A 129       3.996  11.352  13.885  1.00 40.54           C  
ANISOU  968  CA  LEU A 129     5185   4298   5920   1501    443   -875       C  
ATOM    969  C   LEU A 129       2.509  11.447  13.582  1.00 50.79           C  
ANISOU  969  C   LEU A 129     6232   5665   7402   1767    624   -776       C  
ATOM    970  O   LEU A 129       2.053  12.433  13.006  1.00 49.52           O  
ANISOU  970  O   LEU A 129     6069   5454   7294   1947    690   -675       O  
ATOM    971  CB  LEU A 129       4.355  12.199  15.102  1.00 42.05           C  
ANISOU  971  CB  LEU A 129     5878   4177   5924   1455    580   -923       C  
ATOM    972  CG  LEU A 129       5.835  12.146  15.472  1.00 43.16           C  
ANISOU  972  CG  LEU A 129     6247   4256   5896   1150    352   -973       C  
ATOM    973  CD1 LEU A 129       6.134  13.029  16.670  1.00 58.88           C  
ANISOU  973  CD1 LEU A 129     8800   5912   7662   1058    445  -1014       C  
ATOM    974  CD2 LEU A 129       6.249  10.710  15.738  1.00 39.32           C  
ANISOU  974  CD2 LEU A 129     5545   3951   5444    999    223  -1017       C  
ATOM    975  N   GLN A 130       1.756  10.420  13.964  1.00 47.16           N  
ANISOU  975  N   GLN A 130     5541   5323   7054   1787    699   -778       N  
ATOM    976  CA  GLN A 130       0.341  10.352  13.613  1.00 49.49           C  
ANISOU  976  CA  GLN A 130     5496   5735   7573   2000    826   -635       C  
ATOM    977  C   GLN A 130      -0.475  11.481  14.238  1.00 46.82           C  
ANISOU  977  C   GLN A 130     5334   5177   7280   2282   1169   -530       C  
ATOM    978  O   GLN A 130      -0.474  11.657  15.453  1.00 65.63           O  
ANISOU  978  O   GLN A 130     8048   7332   9554   2314   1418   -592       O  
ATOM    979  CB  GLN A 130      -0.259   8.999  13.997  1.00 43.59           C  
ANISOU  979  CB  GLN A 130     4484   5142   6938   1926    843   -647       C  
ATOM    980  CG  GLN A 130      -1.651   8.784  13.423  1.00 58.93           C  
ANISOU  980  CG  GLN A 130     5980   7267   9143   2074    878   -458       C  
ATOM    981  CD  GLN A 130      -2.236   7.441  13.788  1.00 55.88           C  
ANISOU  981  CD  GLN A 130     5340   7024   8868   1958    880   -460       C  
ATOM    983  NE2 GLN A 130      -1.811   6.901  14.924  1.00 61.78           N  
ANISOU  983  NE2 GLN A 130     6328   7648   9496   1866   1012   -596       N  
ATOM    982  OE1 GLN A 130      -3.063   6.893  13.057  1.00 54.56           O  
ANISOU  982  OE1 GLN A 130     4779   7069   8883   1931    746   -329       O  
ATOM    984  N   PRO A 131      -1.187  12.244  13.397  1.00 69.68           N  
ANISOU  984  N   PRO A 131     8031   8120  10323   2499   1197   -357       N  
ATOM    985  CA  PRO A 131      -2.015  13.357  13.865  1.00 56.50           C  
ANISOU  985  CA  PRO A 131     6506   6234   8726   2824   1561   -215       C  
ATOM    986  C   PRO A 131      -3.288  12.861  14.531  1.00 61.93           C  
ANISOU  986  C   PRO A 131     6926   6966   9637   3012   1856    -75       C  
ATOM    987  O   PRO A 131      -3.672  11.706  14.345  1.00 62.60           O  
ANISOU  987  O   PRO A 131     6621   7300   9862   2884   1711    -53       O  
ATOM    988  CB  PRO A 131      -2.372  14.083  12.568  1.00 52.80           C  
ANISOU  988  CB  PRO A 131     5796   5880   8386   2976   1425    -38       C  
ATOM    989  CG  PRO A 131      -2.390  13.004  11.550  1.00 51.01           C  
ANISOU  989  CG  PRO A 131     5133   5993   8253   2776   1056    -25       C  
ATOM    990  CD  PRO A 131      -1.277  12.071  11.935  1.00 49.59           C  
ANISOU  990  CD  PRO A 131     5131   5829   7881   2459    892   -266       C  
ATOM    991  N   GLY A 132      -3.929  13.730  15.304  1.00 66.81           N  
ANISOU  991  N   GLY A 132     7790   7362  10232   3214   2207     15       N  
ATOM    992  CA  GLY A 132      -5.228  13.429  15.871  1.00 86.57           C  
ANISOU  992  CA  GLY A 132    10046   9941  12904   3313   2435    187       C  
ATOM    993  C   GLY A 132      -6.318  13.744  14.865  1.00 94.78           C  
ANISOU  993  C   GLY A 132    10595  11204  14212   3459   2348    466       C  
ATOM    994  O   GLY A 132      -6.041  14.316  13.810  1.00 97.48           O  
ANISOU  994  O   GLY A 132    10863  11605  14569   3496   2136    512       O  
ATOM    995  N   PRO A 133      -7.566  13.369  15.182  1.00 96.27           N  
ANISOU  995  N   PRO A 133    10453  11514  14610   3531   2504    671       N  
ATOM    996  CA  PRO A 133      -8.709  13.598  14.290  1.00100.55           C  
ANISOU  996  CA  PRO A 133    10505  12276  15423   3645   2408    974       C  
ATOM    997  C   PRO A 133      -8.907  15.074  13.949  1.00105.28           C  
ANISOU  997  C   PRO A 133    11287  12711  16003   3887   2550   1116       C  
ATOM    998  O   PRO A 133      -9.407  15.389  12.869  1.00112.88           O  
ANISOU  998  O   PRO A 133    11913  13851  17127   3947   2343   1311       O  
ATOM    999  CB  PRO A 133      -9.895  13.082  15.108  1.00111.65           C  
ANISOU  999  CB  PRO A 133    11682  13728  17012   3698   2677   1158       C  
ATOM   1000  CG  PRO A 133      -9.300  12.074  16.034  1.00117.56           C  
ANISOU 1000  CG  PRO A 133    12625  14420  17623   3517   2732    921       C  
ATOM   1001  CD  PRO A 133      -7.950  12.622  16.392  1.00102.02           C  
ANISOU 1001  CD  PRO A 133    11244  12185  15336   3487   2759    641       C  
ATOM   1002  N   GLU A 134      -8.509  15.963  14.855  1.00 98.76           N  
ANISOU 1002  N   GLU A 134    11022  11540  14962   4005   2887   1022       N  
ATOM   1003  CA  GLU A 134      -8.712  17.394  14.655  1.00102.33           C  
ANISOU 1003  CA  GLU A 134    11713  11796  15373   4238   3078   1159       C  
ATOM   1004  C   GLU A 134      -7.410  18.163  14.426  1.00119.22           C  
ANISOU 1004  C   GLU A 134    14352  13714  17231   4180   2977    938       C  
ATOM   1005  O   GLU A 134      -7.167  19.186  15.065  1.00122.21           O  
ANISOU 1005  O   GLU A 134    15262  13767  17404   4281   3262    904       O  
ATOM   1006  CB  GLU A 134      -9.469  17.996  15.841  1.00112.86           C  
ANISOU 1006  CB  GLU A 134    13331  12873  16677   4442   3595   1297       C  
ATOM   1007  N   ASP A 135      -6.577  17.668  13.517  1.00125.74           N  
ANISOU 1007  N   ASP A 135    15028  14707  18040   4005   2577    802       N  
ATOM   1008  CA  ASP A 135      -5.374  18.393  13.121  1.00112.05           C  
ANISOU 1008  CA  ASP A 135    13702  12790  16081   3951   2453    639       C  
ATOM   1009  C   ASP A 135      -5.497  18.825  11.667  1.00 97.65           C  
ANISOU 1009  C   ASP A 135    11575  11143  14386   4025   2181    793       C  
ATOM   1010  O   ASP A 135      -5.807  18.015  10.795  1.00104.84           O  
ANISOU 1010  O   ASP A 135    11987  12372  15473   3945   1876    876       O  
ATOM   1011  CB  ASP A 135      -4.121  17.538  13.321  1.00101.00           C  
ANISOU 1011  CB  ASP A 135    12471  11388  14517   3692   2248    360       C  
ATOM   1012  CG  ASP A 135      -3.888  17.175  14.774  1.00107.27           C  
ANISOU 1012  CG  ASP A 135    13643  11978  15137   3594   2488    198       C  
ATOM   1013  OD1 ASP A 135      -4.550  17.771  15.651  1.00129.46           O  
ANISOU 1013  OD1 ASP A 135    16697  14593  17897   3727   2835    283       O  
ATOM   1014  OD2 ASP A 135      -3.037  16.300  15.043  1.00 86.38           O1-
ANISOU 1014  OD2 ASP A 135    11072   9358  12392   3385   2336     -2       O1-
ATOM   1015  N   THR A 136      -5.261  20.104  11.409  1.00 94.46           N  
ANISOU 1015  N   THR A 136    11503  10518  13870   4158   2282    837       N  
ATOM   1016  CA  THR A 136      -5.424  20.634  10.063  1.00 96.10           C  
ANISOU 1016  CA  THR A 136    11472  10862  14181   4249   2052   1004       C  
ATOM   1017  C   THR A 136      -4.115  21.161   9.481  1.00101.92           C  
ANISOU 1017  C   THR A 136    12569  11452  14704   4156   1877    849       C  
ATOM   1018  O   THR A 136      -4.041  21.495   8.299  1.00122.67           O  
ANISOU 1018  O   THR A 136    15038  14194  17379   4196   1644    959       O  
ATOM   1019  CB  THR A 136      -6.502  21.734  10.017  1.00104.71           C  
ANISOU 1019  CB  THR A 136    12540  11863  15383   4531   2314   1274       C  
ATOM   1021  CG2 THR A 136      -6.197  22.828  11.025  1.00 91.26           C  
ANISOU 1021  CG2 THR A 136    11483   9748  13444   4630   2716   1196       C  
ATOM   1020  OG1 THR A 136      -6.554  22.300   8.702  1.00145.33           O  
ANISOU 1020  OG1 THR A 136    17509  17115  20596   4607   2072   1425       O  
ATOM   1022  N   GLY A 137      -3.080  21.221  10.310  1.00 82.11           N  
ANISOU 1022  N   GLY A 137    10561   8687  11951   4014   1975    607       N  
ATOM   1023  CA  GLY A 137      -1.792  21.721   9.871  1.00 62.54           C  
ANISOU 1023  CA  GLY A 137     8464   6038   9261   3897   1822    468       C  
ATOM   1024  C   GLY A 137      -0.990  20.680   9.116  1.00 95.75           C  
ANISOU 1024  C   GLY A 137    12402  10525  13454   3624   1417    354       C  
ATOM   1025  O   GLY A 137      -1.453  19.557   8.908  1.00 72.22           O  
ANISOU 1025  O   GLY A 137     8962   7848  10631   3561   1267    382       O  
ATOM   1026  N   LYS A 138       0.215  21.058   8.701  1.00 56.95           N  
ANISOU 1026  N   LYS A 138     7776   5534   8329   3376   1215    226       N  
ATOM   1027  CA  LYS A 138       1.114  20.134   8.026  1.00 58.05           C  
ANISOU 1027  CA  LYS A 138     7713   5934   8409   3041    845    108       C  
ATOM   1028  C   LYS A 138       1.454  18.968   8.945  1.00 73.05           C  
ANISOU 1028  C   LYS A 138     9568   7912  10275   2816    816    -63       C  
ATOM   1029  O   LYS A 138       1.281  19.053  10.161  1.00 65.29           O  
ANISOU 1029  O   LYS A 138     8839   6727   9242   2856   1058   -128       O  
ATOM   1030  CB  LYS A 138       2.399  20.845   7.596  1.00 65.73           C  
ANISOU 1030  CB  LYS A 138     9030   6767   9178   2827    706     31       C  
ATOM   1031  CG  LYS A 138       2.222  21.870   6.491  1.00 62.61           C  
ANISOU 1031  CG  LYS A 138     8665   6329   8795   3000    677    192       C  
ATOM   1032  CD  LYS A 138       1.922  21.206   5.158  1.00 89.29           C  
ANISOU 1032  CD  LYS A 138    11593  10049  12283   3001    406    293       C  
ATOM   1033  CE  LYS A 138       1.932  22.223   4.029  1.00101.44           C  
ANISOU 1033  CE  LYS A 138    13217  11534  13790   3128    343    444       C  
ATOM   1034  NZ  LYS A 138       3.236  22.939   3.947  1.00 94.44           N1+
ANISOU 1034  NZ  LYS A 138    12736  10445  12701   2915    319    348       N1+
ATOM   1035  N   ALA A 139       1.934  17.879   8.355  1.00 77.26           N  
ANISOU 1035  N   ALA A 139     9817   8719  10820   2590    536   -130       N  
ATOM   1036  CA  ALA A 139       2.291  16.692   9.118  1.00 73.07           C  
ANISOU 1036  CA  ALA A 139     9221   8278  10265   2381    489   -276       C  
ATOM   1037  C   ALA A 139       3.502  16.962  10.002  1.00 75.60           C  
ANISOU 1037  C   ALA A 139     9964   8382  10381   2148    496   -421       C  
ATOM   1038  O   ALA A 139       4.512  17.494   9.541  1.00 60.15           O  
ANISOU 1038  O   ALA A 139     8181   6363   8311   1993    360   -433       O  
ATOM   1039  CB  ALA A 139       2.564  15.528   8.182  1.00 71.69           C  
ANISOU 1039  CB  ALA A 139     8701   8407  10130   2213    211   -299       C  
ATOM   1040  N   CYS A 140       3.393  16.594  11.275  1.00 62.97           N  
ANISOU 1040  N   CYS A 140     8527   6665   8733   2107    643   -509       N  
ATOM   1041  CA  CYS A 140       4.481  16.804  12.224  1.00 67.64           C  
ANISOU 1041  CA  CYS A 140     9538   7046   9115   1852    611   -625       C  
ATOM   1042  C   CYS A 140       5.459  15.633  12.258  1.00 43.70           C  
ANISOU 1042  C   CYS A 140     6331   4211   6064   1561    362   -705       C  
ATOM   1043  O   CYS A 140       5.108  14.503  11.919  1.00 66.72           O  
ANISOU 1043  O   CYS A 140     8872   7374   9105   1578    298   -712       O  
ATOM   1044  CB  CYS A 140       3.927  17.087  13.620  1.00 48.32           C  
ANISOU 1044  CB  CYS A 140     7459   4326   6575   1946    902   -674       C  
ATOM   1045  SG  CYS A 140       3.094  18.685  13.745  1.00 73.37           S  
ANISOU 1045  SG  CYS A 140    11018   7151   9709   2278   1254   -573       S  
ATOM   1046  N   GLY A 141       6.689  15.915  12.669  1.00 45.84           N  
ANISOU 1046  N   GLY A 141     6877   4358   6181   1290    221   -742       N  
ATOM   1047  CA  GLY A 141       7.736  14.912  12.687  1.00 41.58           C  
ANISOU 1047  CA  GLY A 141     6163   3991   5644   1032     -4   -766       C  
ATOM   1048  C   GLY A 141       8.987  15.417  11.995  1.00 54.14           C  
ANISOU 1048  C   GLY A 141     7779   5592   7200    834   -202   -690       C  
ATOM   1049  O   GLY A 141       9.286  16.608  12.037  1.00 57.85           O  
ANISOU 1049  O   GLY A 141     8566   5849   7567    780   -194   -654       O  
ATOM   1050  N   VAL A 142       9.713  14.510  11.351  1.00 52.23           N  
ANISOU 1050  N   VAL A 142     7216   5582   7046    731   -353   -651       N  
ATOM   1051  CA  VAL A 142      10.959  14.856  10.677  1.00 56.83           C  
ANISOU 1051  CA  VAL A 142     7760   6199   7632    552   -508   -542       C  
ATOM   1052  C   VAL A 142      10.802  14.723   9.166  1.00 49.18           C  
ANISOU 1052  C   VAL A 142     6523   5406   6756    706   -496   -487       C  
ATOM   1053  O   VAL A 142      10.383  13.678   8.669  1.00 49.67           O  
ANISOU 1053  O   VAL A 142     6321   5657   6893    811   -480   -519       O  
ATOM   1054  CB  VAL A 142      12.118  13.960  11.164  1.00 48.81           C  
ANISOU 1054  CB  VAL A 142     6614   5285   6645    310   -664   -489       C  
ATOM   1055  CG1 VAL A 142      13.420  14.334  10.475  1.00 43.25           C  
ANISOU 1055  CG1 VAL A 142     5819   4626   5989    134   -795   -323       C  
ATOM   1056  CG2 VAL A 142      12.268  14.077  12.669  1.00 51.53           C  
ANISOU 1056  CG2 VAL A 142     7265   5449   6863    129   -717   -533       C  
ATOM   1057  N   ASP A 143      11.132  15.782   8.435  1.00 44.74           N  
ANISOU 1057  N   ASP A 143     6073   4761   6166    703   -508   -405       N  
ATOM   1058  CA  ASP A 143      10.953  15.767   6.984  1.00 46.34           C  
ANISOU 1058  CA  ASP A 143     6092   5099   6417    848   -495   -348       C  
ATOM   1059  C   ASP A 143      12.092  16.479   6.265  1.00 53.11           C  
ANISOU 1059  C   ASP A 143     7001   5918   7261    711   -552   -216       C  
ATOM   1060  O   ASP A 143      12.781  17.315   6.865  1.00 52.34           O  
ANISOU 1060  O   ASP A 143     7123   5650   7112    520   -604   -165       O  
ATOM   1061  CB  ASP A 143       9.619  16.411   6.607  1.00 43.44           C  
ANISOU 1061  CB  ASP A 143     5785   4677   6044   1106   -397   -367       C  
ATOM   1062  CG  ASP A 143       9.580  17.892   6.918  1.00 72.37           C  
ANISOU 1062  CG  ASP A 143     9793   8078   9626   1121   -332   -332       C  
ATOM   1063  OD1 ASP A 143       9.233  18.258   8.061  1.00 66.58           O  
ANISOU 1063  OD1 ASP A 143     9303   7158   8835   1118   -245   -392       O  
ATOM   1064  OD2 ASP A 143       9.898  18.695   6.014  1.00 96.99           O1-
ANISOU 1064  OD2 ASP A 143    12982  11152  12719   1136   -349   -242       O1-
ATOM   1065  N   TYR A 144      12.303  16.150   4.989  1.00 52.05           N  
ANISOU 1065  N   TYR A 144     6694   5926   7159    787   -542   -151       N  
ATOM   1066  CA  TYR A 144      13.324  16.863   4.236  1.00 57.40           C  
ANISOU 1066  CA  TYR A 144     7417   6562   7832    680   -553     -7       C  
ATOM   1067  C   TYR A 144      12.670  17.777   3.210  1.00 50.99           C  
ANISOU 1067  C   TYR A 144     6730   5687   6956    856   -505     19       C  
ATOM   1068  O   TYR A 144      11.542  17.539   2.783  1.00 65.43           O  
ANISOU 1068  O   TYR A 144     8512   7581   8769   1065   -485    -43       O  
ATOM   1069  CB  TYR A 144      14.322  15.895   3.589  1.00 57.31           C  
ANISOU 1069  CB  TYR A 144     7163   6716   7894    620   -533     91       C  
ATOM   1070  CG  TYR A 144      15.258  15.223   4.573  1.00 53.76           C  
ANISOU 1070  CG  TYR A 144     6582   6310   7535    422   -594    145       C  
ATOM   1071  CD1 TYR A 144      14.809  14.214   5.414  1.00 51.95           C  
ANISOU 1071  CD1 TYR A 144     6271   6147   7321    444   -614     29       C  
ATOM   1072  CD2 TYR A 144      16.594  15.593   4.653  1.00 55.42           C  
ANISOU 1072  CD2 TYR A 144     6731   6501   7826    204   -643    342       C  
ATOM   1073  CE1 TYR A 144      15.661  13.597   6.310  1.00 54.17           C  
ANISOU 1073  CE1 TYR A 144     6437   6467   7679    270   -687    100       C  
ATOM   1074  CE2 TYR A 144      17.455  14.979   5.544  1.00 50.41           C  
ANISOU 1074  CE2 TYR A 144     5942   5922   7291     17   -734    438       C  
ATOM   1075  CZ  TYR A 144      16.983  13.984   6.370  1.00 60.22           C  
ANISOU 1075  CZ  TYR A 144     7127   7222   8530     59   -758    313       C  
ATOM   1076  OH  TYR A 144      17.838  13.374   7.260  1.00 68.06           O  
ANISOU 1076  OH  TYR A 144     7973   8270   9618   -122   -865    428       O  
ATOM   1077  N   GLU A 145      13.373  18.836   2.831  1.00 48.22           N  
ANISOU 1077  N   GLU A 145     6535   5211   6576    757   -504    134       N  
ATOM   1078  CA  GLU A 145      12.811  19.820   1.921  1.00 55.94           C  
ANISOU 1078  CA  GLU A 145     7673   6099   7484    918   -459    177       C  
ATOM   1079  C   GLU A 145      13.886  20.493   1.080  1.00 56.37           C  
ANISOU 1079  C   GLU A 145     7790   6103   7525    793   -439    334       C  
ATOM   1080  O   GLU A 145      14.912  20.928   1.597  1.00 68.21           O  
ANISOU 1080  O   GLU A 145     9349   7511   9057    545   -477    421       O  
ATOM   1081  CB  GLU A 145      12.020  20.866   2.712  1.00 56.80           C  
ANISOU 1081  CB  GLU A 145     8060   5985   7538    991   -428    124       C  
ATOM   1082  CG  GLU A 145      11.555  22.063   1.901  1.00 63.89           C  
ANISOU 1082  CG  GLU A 145     9163   6743   8370   1152   -371    201       C  
ATOM   1083  CD  GLU A 145      10.757  23.048   2.734  1.00 83.34           C  
ANISOU 1083  CD  GLU A 145    11928   8954  10784   1267   -283    162       C  
ATOM   1084  OE1 GLU A 145      10.905  24.270   2.520  1.00 86.81           O  
ANISOU 1084  OE1 GLU A 145    12665   9170  11147   1266   -232    234       O  
ATOM   1085  OE2 GLU A 145       9.979  22.598   3.603  1.00 83.80           O1-
ANISOU 1085  OE2 GLU A 145    11949   9019  10874   1367   -236     67       O1-
ATOM   1086  N   VAL A 146      13.649  20.562  -0.224  1.00 61.69           N  
ANISOU 1086  N   VAL A 146     8455   6837   8148    949   -391    389       N  
ATOM   1087  CA  VAL A 146      14.504  21.334  -1.113  1.00 51.80           C  
ANISOU 1087  CA  VAL A 146     7306   5511   6866    871   -336    546       C  
ATOM   1088  C   VAL A 146      13.806  22.649  -1.435  1.00 59.56           C  
ANISOU 1088  C   VAL A 146     8569   6307   7756    996   -328    566       C  
ATOM   1089  O   VAL A 146      12.708  22.654  -1.985  1.00 66.58           O  
ANISOU 1089  O   VAL A 146     9479   7233   8587   1237   -337    529       O  
ATOM   1090  CB  VAL A 146      14.801  20.573  -2.420  1.00 49.50           C  
ANISOU 1090  CB  VAL A 146     6892   5372   6542    960   -255    610       C  
ATOM   1091  CG1 VAL A 146      15.436  21.498  -3.443  1.00 51.57           C  
ANISOU 1091  CG1 VAL A 146     7310   5536   6748    934   -168    772       C  
ATOM   1092  CG2 VAL A 146      15.701  19.375  -2.147  1.00 53.19           C  
ANISOU 1092  CG2 VAL A 146     7111   5983   7115    847   -206    637       C  
ATOM   1093  N   LYS A 147      14.434  23.764  -1.079  1.00 53.44           N  
ANISOU 1093  N   LYS A 147     8012   5324   6967    823   -321    645       N  
ATOM   1094  CA  LYS A 147      13.846  25.073  -1.337  1.00 60.73           C  
ANISOU 1094  CA  LYS A 147     9251   6027   7795    944   -284    676       C  
ATOM   1095  C   LYS A 147      14.740  25.924  -2.237  1.00 62.76           C  
ANISOU 1095  C   LYS A 147     9649   6184   8013    824   -233    844       C  
ATOM   1096  O   LYS A 147      15.856  26.273  -1.862  1.00 71.87           O  
ANISOU 1096  O   LYS A 147    10840   7256   9212    527   -252    936       O  
ATOM   1097  CB  LYS A 147      13.566  25.806  -0.022  1.00 52.86           C  
ANISOU 1097  CB  LYS A 147     8525   4790   6770    868   -291    601       C  
ATOM   1098  CG  LYS A 147      12.681  27.031  -0.173  1.00 54.77           C  
ANISOU 1098  CG  LYS A 147     9104   4789   6918   1085   -203    618       C  
ATOM   1099  CD  LYS A 147      12.298  27.624   1.173  1.00 66.25           C  
ANISOU 1099  CD  LYS A 147    10878   5977   8316   1054   -154    527       C  
ATOM   1100  CE  LYS A 147      13.493  28.254   1.872  1.00 95.91           C  
ANISOU 1100  CE  LYS A 147    14913   9518  12009    646   -223    560       C  
ATOM   1101  NZ  LYS A 147      13.098  28.945   3.134  1.00102.44           N1+
ANISOU 1101  NZ  LYS A 147    16188  10019  12715    606   -162    466       N1+
ATOM   1102  N   ALA A 148      14.246  26.250  -3.426  1.00 66.90           N  
ANISOU 1102  N   ALA A 148    10247   6717   8455   1040   -184    904       N  
ATOM   1103  CA  ALA A 148      14.988  27.110  -4.343  1.00 64.96           C  
ANISOU 1103  CA  ALA A 148    10171   6358   8154    957   -111   1067       C  
ATOM   1104  C   ALA A 148      14.358  28.492  -4.383  1.00 66.17           C  
ANISOU 1104  C   ALA A 148    10689   6243   8209   1076    -85   1098       C  
ATOM   1105  O   ALA A 148      13.146  28.622  -4.543  1.00 73.35           O  
ANISOU 1105  O   ALA A 148    11652   7146   9073   1369    -95   1052       O  
ATOM   1106  CB  ALA A 148      15.026  26.507  -5.732  1.00 56.09           C  
ANISOU 1106  CB  ALA A 148     8936   5405   6971   1095    -55   1134       C  
ATOM   1107  N   PHE A 149      15.180  29.525  -4.243  1.00 64.55           N  
ANISOU 1107  N   PHE A 149    10730   5813   7982    846    -49   1199       N  
ATOM   1108  CA  PHE A 149      14.657  30.878  -4.132  1.00 64.46           C  
ANISOU 1108  CA  PHE A 149    11133   5493   7868    938     -1   1223       C  
ATOM   1109  C   PHE A 149      15.557  31.928  -4.771  1.00 88.51           C  
ANISOU 1109  C   PHE A 149    14428   8346  10857    745     60   1392       C  
ATOM   1110  O   PHE A 149      16.701  31.651  -5.132  1.00 73.16           O  
ANISOU 1110  O   PHE A 149    12314   6501   8981    491     66   1505       O  
ATOM   1111  CB  PHE A 149      14.386  31.230  -2.667  1.00 62.69           C  
ANISOU 1111  CB  PHE A 149    11123   5062   7635    846    -23   1104       C  
ATOM   1112  CG  PHE A 149      15.608  31.190  -1.791  1.00 63.04           C  
ANISOU 1112  CG  PHE A 149    11180   5049   7723    396   -114   1119       C  
ATOM   1113  CD1 PHE A 149      16.049  29.994  -1.245  1.00 66.44           C  
ANISOU 1113  CD1 PHE A 149    11248   5726   8271    250   -211   1066       C  
ATOM   1114  CD2 PHE A 149      16.305  32.351  -1.498  1.00 80.12           C  
ANISOU 1114  CD2 PHE A 149    13728   6904   9809    102   -125   1206       C  
ATOM   1115  CE1 PHE A 149      17.170  29.955  -0.434  1.00 62.95           C  
ANISOU 1115  CE1 PHE A 149    10787   5246   7884   -172   -333   1123       C  
ATOM   1116  CE2 PHE A 149      17.426  32.318  -0.687  1.00 77.02           C  
ANISOU 1116  CE2 PHE A 149    13334   6469   9461   -357   -265   1256       C  
ATOM   1117  CZ  PHE A 149      17.858  31.119  -0.154  1.00 67.64           C  
ANISOU 1117  CZ  PHE A 149    11743   5550   8406   -490   -378   1226       C  
ATOM   1118  N   CYS A 150      15.021  33.137  -4.903  1.00 83.61           N  
ANISOU 1118  N   CYS A 150    14204   7440  10123    880    127   1429       N  
ATOM   1119  CA  CYS A 150      15.741  34.241  -5.515  1.00 69.38           C  
ANISOU 1119  CA  CYS A 150    12699   5415   8249    715    195   1589       C  
ATOM   1120  C   CYS A 150      15.934  35.358  -4.497  1.00 90.52           C  
ANISOU 1120  C   CYS A 150    15831   7709  10852    495    200   1569       C  
ATOM   1121  O   CYS A 150      14.977  35.790  -3.854  1.00 88.34           O  
ANISOU 1121  O   CYS A 150    15823   7237  10504    711    251   1469       O  
ATOM   1122  CB  CYS A 150      14.957  34.770  -6.714  1.00 76.86           C  
ANISOU 1122  CB  CYS A 150    13795   6321   9090   1072    276   1676       C  
ATOM   1123  SG  CYS A 150      14.346  33.498  -7.833  1.00107.98           S  
ANISOU 1123  SG  CYS A 150    17332  10656  13041   1372    229   1670       S  
ATOM   1124  N   ALA A 151      17.170  35.826  -4.355  1.00 80.41           N  
ANISOU 1124  N   ALA A 151    14656   6309   9588     58    158   1683       N  
ATOM   1125  CA  ALA A 151      17.483  36.881  -3.397  1.00 76.00           C  
ANISOU 1125  CA  ALA A 151    14590   5361   8926   -243    124   1673       C  
ATOM   1126  C   ALA A 151      18.797  37.573  -3.741  1.00 78.56           C  
ANISOU 1126  C   ALA A 151    15023   5559   9266   -695     84   1877       C  
ATOM   1127  O   ALA A 151      19.533  37.122  -4.613  1.00 86.38           O  
ANISOU 1127  O   ALA A 151    15646   6793  10382   -773    104   2031       O  
ATOM   1128  CB  ALA A 151      17.536  36.317  -1.990  1.00 75.06           C  
ANISOU 1128  CB  ALA A 151    14436   5253   8831   -444    -10   1528       C  
ATOM   1129  N   GLU A 152      19.086  38.669  -3.048  1.00 91.59           N  
ANISOU 1129  N   GLU A 152    17203   6811  10786   -998     44   1891       N  
ATOM   1130  CA  GLU A 152      20.355  39.366  -3.213  1.00 93.92           C  
ANISOU 1130  CA  GLU A 152    17619   6964  11104  -1508    -35   2101       C  
ATOM   1131  C   GLU A 152      21.444  38.647  -2.427  1.00110.62           C  
ANISOU 1131  C   GLU A 152    19374   9273  13382  -1996   -270   2175       C  
ATOM   1132  O   GLU A 152      22.570  38.495  -2.900  1.00112.60           O  
ANISOU 1132  O   GLU A 152    19287   9689  13806  -2308   -322   2411       O  
ATOM   1133  CB  GLU A 152      20.239  40.814  -2.734  1.00 88.36           C  
ANISOU 1133  CB  GLU A 152    17678   5724  10170  -1687    -12   2088       C  
ATOM   1134  N   ASN A 153      21.092  38.208  -1.222  1.00112.62           N  
ANISOU 1134  N   ASN A 153    19697   9505  13589  -2047   -401   1997       N  
ATOM   1135  CA  ASN A 153      22.005  37.475  -0.353  1.00107.31           C  
ANISOU 1135  CA  ASN A 153    18703   9016  13056  -2485   -657   2061       C  
ATOM   1136  C   ASN A 153      21.233  36.531   0.571  1.00112.64           C  
ANISOU 1136  C   ASN A 153    19268   9821  13709  -2264   -703   1824       C  
ATOM   1137  O   ASN A 153      20.009  36.448   0.489  1.00112.31           O  
ANISOU 1137  O   ASN A 153    19361   9741  13569  -1778   -524   1630       O  
ATOM   1138  CB  ASN A 153      22.860  38.447   0.462  1.00100.82           C  
ANISOU 1138  CB  ASN A 153    18340   7844  12124  -3116   -886   2174       C  
ATOM   1139  N   LEU A 154      21.938  35.816   1.444  1.00104.85           N  
ANISOU 1139  N   LEU A 154    18017   8993  12827  -2618   -942   1865       N  
ATOM   1140  CA  LEU A 154      21.285  34.874   2.358  1.00 95.05           C  
ANISOU 1140  CA  LEU A 154    16670   7878  11567  -2442   -989   1654       C  
ATOM   1141  C   LEU A 154      20.556  35.566   3.505  1.00105.75           C  
ANISOU 1141  C   LEU A 154    18731   8815  12633  -2474  -1001   1444       C  
ATOM   1142  O   LEU A 154      19.780  34.941   4.230  1.00 99.23           O  
ANISOU 1142  O   LEU A 154    17920   8029  11753  -2244   -964   1247       O  
ATOM   1143  CB  LEU A 154      22.293  33.877   2.932  1.00 77.32           C  
ANISOU 1143  CB  LEU A 154    13926   5930   9523  -2803  -1243   1789       C  
ATOM   1144  CG  LEU A 154      22.674  32.663   2.084  1.00108.42           C  
ANISOU 1144  CG  LEU A 154    17106  10339  13751  -2597  -1160   1913       C  
ATOM   1145  CD1 LEU A 154      21.437  32.089   1.392  1.00 71.14           C  
ANISOU 1145  CD1 LEU A 154    12269   5762   9000  -1972   -897   1705       C  
ATOM   1146  CD2 LEU A 154      23.758  33.007   1.068  1.00117.99           C  
ANISOU 1146  CD2 LEU A 154    18047  11641  15141  -2802  -1121   2229       C  
ATOM   1147  N   GLU A 155      20.818  36.855   3.670  1.00119.26           N  
ANISOU 1147  N   GLU A 155    21060  10104  14150  -2762  -1030   1495       N  
ATOM   1148  CA  GLU A 155      20.175  37.628   4.718  1.00125.77           C  
ANISOU 1148  CA  GLU A 155    22620  10507  14661  -2773   -986   1295       C  
ATOM   1149  C   GLU A 155      18.765  38.016   4.299  1.00131.11           C  
ANISOU 1149  C   GLU A 155    23589  10995  15232  -2140   -619   1141       C  
ATOM   1150  O   GLU A 155      17.864  38.103   5.133  1.00136.47           O  
ANISOU 1150  O   GLU A 155    24572  11542  15739  -1887   -476    932       O  
ATOM   1151  CB  GLU A 155      20.997  38.877   5.033  1.00137.70           C  
ANISOU 1151  CB  GLU A 155    24484  11850  15984  -3213  -1124   1346       C  
ATOM   1152  CG  GLU A 155      22.400  38.573   5.522  1.00147.63           C  
ANISOU 1152  CG  GLU A 155    25419  13323  17350  -3832  -1514   1529       C  
ATOM   1153  CD  GLU A 155      22.401  37.774   6.811  1.00156.77           C  
ANISOU 1153  CD  GLU A 155    26540  14590  18435  -3976  -1720   1412       C  
ATOM   1154  OE1 GLU A 155      21.489  37.980   7.639  1.00162.63           O  
ANISOU 1154  OE1 GLU A 155    27757  15131  18906  -3749  -1585   1161       O  
ATOM   1155  OE2 GLU A 155      23.310  36.938   6.994  1.00158.69           O1-
ANISOU 1155  OE2 GLU A 155    26268  15131  18896  -4295  -1995   1589       O1-
ATOM   1156  N   GLU A 156      18.584  38.234   2.999  1.00135.26           N  
ANISOU 1156  N   GLU A 156    23896  11624  15873  -1844   -454   1249       N  
ATOM   1157  CA  GLU A 156      17.313  38.702   2.449  1.00122.63           C  
ANISOU 1157  CA  GLU A 156    22509   9884  14201  -1245   -135   1167       C  
ATOM   1158  C   GLU A 156      16.114  37.853   2.867  1.00107.37           C  
ANISOU 1158  C   GLU A 156    20366   8119  12312   -760      6    991       C  
ATOM   1159  O   GLU A 156      16.172  36.622   2.859  1.00 98.93           O  
ANISOU 1159  O   GLU A 156    18699   7465  11423   -714    -98    961       O  
ATOM   1160  CB  GLU A 156      17.385  38.766   0.920  1.00122.98           C  
ANISOU 1160  CB  GLU A 156    22184  10151  14391  -1015    -44   1325       C  
ATOM   1161  CG  GLU A 156      18.433  39.726   0.374  1.00138.99           C  
ANISOU 1161  CG  GLU A 156    24445  11984  16380  -1423   -113   1521       C  
ATOM   1162  CD  GLU A 156      18.013  41.181   0.482  1.00160.15           C  
ANISOU 1162  CD  GLU A 156    27774  14256  18819  -1344     51   1467       C  
ATOM   1163  OE1 GLU A 156      16.813  41.443   0.709  1.00168.26           O  
ANISOU 1163  OE1 GLU A 156    29020  15169  19741   -874    272   1322       O  
ATOM   1164  OE2 GLU A 156      18.885  42.063   0.338  1.00167.80           O1-
ANISOU 1164  OE2 GLU A 156    28926  15109  19722  -1730    -31   1562       O1-
ATOM   1165  N   LYS A 157      15.032  38.527   3.243  1.00104.04           N  
ANISOU 1165  N   LYS A 157    20445   7354  11731   -397    265    895       N  
ATOM   1166  CA  LYS A 157      13.779  37.856   3.560  1.00 94.69           C  
ANISOU 1166  CA  LYS A 157    19062   6304  10613    109    448    773       C  
ATOM   1167  C   LYS A 157      13.180  37.289   2.280  1.00103.49           C  
ANISOU 1167  C   LYS A 157    19557   7819  11945    548    506    859       C  
ATOM   1168  O   LYS A 157      12.833  38.034   1.364  1.00109.79           O  
ANISOU 1168  O   LYS A 157    20472   8512  12730    799    637    973       O  
ATOM   1169  CB  LYS A 157      12.798  38.830   4.212  1.00 89.28           C  
ANISOU 1169  CB  LYS A 157    18845   5350   9726    405    747    671       C  
ATOM   1170  N   ILE A 158      13.064  35.968   2.222  1.00 95.05           N  
ANISOU 1170  N   ILE A 158    17867   7191  11055    621    395    810       N  
ATOM   1171  CA  ILE A 158      12.598  35.297   1.017  1.00 83.89           C  
ANISOU 1171  CA  ILE A 158    15888   6169   9817    952    394    885       C  
ATOM   1172  C   ILE A 158      11.119  35.542   0.754  1.00 87.83           C  
ANISOU 1172  C   ILE A 158    16409   6620  10344   1525    614    905       C  
ATOM   1173  O   ILE A 158      10.270  35.196   1.573  1.00 93.01           O  
ANISOU 1173  O   ILE A 158    17062   7253  11024   1746    728    814       O  
ATOM   1174  CB  ILE A 158      12.825  33.781   1.100  1.00 82.78           C  
ANISOU 1174  CB  ILE A 158    15139   6475   9839    871    229    819       C  
ATOM   1175  CG1 ILE A 158      14.291  33.474   1.409  1.00 76.70           C  
ANISOU 1175  CG1 ILE A 158    14278   5776   9086    330     17    847       C  
ATOM   1176  CG2 ILE A 158      12.385  33.110  -0.192  1.00 81.30           C  
ANISOU 1176  CG2 ILE A 158    14460   6648   9781   1167    214    894       C  
ATOM   1177  CD1 ILE A 158      14.574  31.999   1.594  1.00 79.48           C  
ANISOU 1177  CD1 ILE A 158    14077   6527   9594    255   -119    794       C  
ATOM   1178  N   HIS A 159      10.817  36.141  -0.393  1.00101.89           N  
ANISOU 1178  N   HIS A 159    18197   8389  12130   1765    674   1053       N  
ATOM   1179  CA  HIS A 159       9.438  36.261  -0.844  1.00108.65           C  
ANISOU 1179  CA  HIS A 159    18937   9283  13061   2312    826   1139       C  
ATOM   1180  C   HIS A 159       8.962  34.895  -1.321  1.00103.78           C  
ANISOU 1180  C   HIS A 159    17656   9158  12620   2457    677   1127       C  
ATOM   1181  O   HIS A 159       9.636  34.239  -2.116  1.00111.78           O  
ANISOU 1181  O   HIS A 159    18351  10456  13666   2266    494   1144       O  
ATOM   1182  CB  HIS A 159       9.322  37.288  -1.971  1.00123.30           C  
ANISOU 1182  CB  HIS A 159    21002  10988  14858   2495    892   1323       C  
ATOM   1183  CG  HIS A 159       9.595  38.694  -1.536  1.00137.78           C  
ANISOU 1183  CG  HIS A 159    23543  12296  16512   2414   1075   1347       C  
ATOM   1185  CD2 HIS A 159       9.899  39.209  -0.321  1.00136.89           C  
ANISOU 1185  CD2 HIS A 159    23866  11889  16257   2166   1170   1208       C  
ATOM   1184  ND1 HIS A 159       9.567  39.762  -2.408  1.00143.81           N  
ANISOU 1184  ND1 HIS A 159    24528  12917  17198   2518   1153   1486       N  
ATOM   1186  CE1 HIS A 159       9.844  40.873  -1.750  1.00145.49           C  
ANISOU 1186  CE1 HIS A 159    25235  12807  17238   2329   1291   1417       C  
ATOM   1187  NE2 HIS A 159      10.049  40.565  -0.481  1.00139.97           N  
ANISOU 1187  NE2 HIS A 159    24684  12015  16484   2108   1297   1248       N  
ATOM   1188  N   LYS A 160       7.804  34.467  -0.829  1.00 94.90           N  
ANISOU 1188  N   LYS A 160    16344   8110  11602   2791    774   1111       N  
ATOM   1189  CA  LYS A 160       7.295  33.132  -1.123  1.00 86.78           C  
ANISOU 1189  CA  LYS A 160    14720   7521  10732   2890    623   1090       C  
ATOM   1190  C   LYS A 160       7.009  32.939  -2.611  1.00 90.42           C  
ANISOU 1190  C   LYS A 160    14882   8242  11234   3047    472   1247       C  
ATOM   1191  O   LYS A 160       7.102  31.826  -3.129  1.00 97.08           O  
ANISOU 1191  O   LYS A 160    15318   9435  12133   2959    282   1215       O  
ATOM   1192  CB  LYS A 160       6.043  32.840  -0.293  1.00 80.36           C  
ANISOU 1192  CB  LYS A 160    13781   6710  10042   3224    782   1083       C  
ATOM   1193  CG  LYS A 160       5.745  31.359  -0.123  1.00 88.14           C  
ANISOU 1193  CG  LYS A 160    14232   8089  11167   3184    629    997       C  
ATOM   1194  CD  LYS A 160       4.606  31.131   0.859  1.00112.28           C  
ANISOU 1194  CD  LYS A 160    17204  11109  14349   3473    826    995       C  
ATOM   1195  CE  LYS A 160       4.414  29.650   1.151  1.00113.85           C  
ANISOU 1195  CE  LYS A 160    16921  11668  14671   3373    677    891       C  
ATOM   1196  NZ  LYS A 160       5.622  29.045   1.776  1.00118.31           N1+
ANISOU 1196  NZ  LYS A 160    17566  12252  15133   2939    567    683       N1+
ATOM   1197  N   ARG A 161       6.669  34.026  -3.297  1.00 99.34           N  
ANISOU 1197  N   ARG A 161    16261   9175  12310   3272    558   1419       N  
ATOM   1198  CA  ARG A 161       6.413  33.966  -4.732  1.00 90.11           C  
ANISOU 1198  CA  ARG A 161    14892   8210  11136   3409    403   1586       C  
ATOM   1199  C   ARG A 161       7.710  33.788  -5.514  1.00 90.83           C  
ANISOU 1199  C   ARG A 161    15025   8381  11107   3048    275   1549       C  
ATOM   1200  O   ARG A 161       7.724  33.166  -6.576  1.00 69.54           O  
ANISOU 1200  O   ARG A 161    12084   5948   8389   3045    109   1608       O  
ATOM   1201  CB  ARG A 161       5.665  35.215  -5.207  1.00 90.67           C  
ANISOU 1201  CB  ARG A 161    15230   8032  11188   3773    539   1807       C  
ATOM   1202  CG  ARG A 161       4.289  35.380  -4.581  1.00100.92           C  
ANISOU 1202  CG  ARG A 161    16421   9275  12648   4204    701   1916       C  
ATOM   1203  CD  ARG A 161       3.503  36.505  -5.237  1.00119.50           C  
ANISOU 1203  CD  ARG A 161    18850  11540  15017   4485    794   2133       C  
ATOM   1204  NE  ARG A 161       3.232  36.236  -6.648  1.00129.54           N  
ANISOU 1204  NE  ARG A 161    19863  13068  16289   4579    527   2323       N  
ATOM   1205  CZ  ARG A 161       2.214  35.503  -7.087  1.00116.24           C  
ANISOU 1205  CZ  ARG A 161    17684  11721  14762   4758    331   2462       C  
ATOM   1206  NH1 ARG A 161       1.366  34.956  -6.227  1.00125.87           N1+
ANISOU 1206  NH1 ARG A 161    18573  13071  16181   4875    398   2439       N1+
ATOM   1207  NH2 ARG A 161       2.044  35.313  -8.388  1.00 88.85           N  
ANISOU 1207  NH2 ARG A 161    14068   8453  11237   4790     59   2630       N  
ATOM   1208  N   ASN A 162       8.800  34.330  -4.978  1.00 87.49           N  
ANISOU 1208  N   ASN A 162    14925   7717  10599   2734    360   1469       N  
ATOM   1209  CA  ASN A 162      10.116  34.173  -5.588  1.00 85.71           C  
ANISOU 1209  CA  ASN A 162    14703   7560  10304   2375    279   1468       C  
ATOM   1210  C   ASN A 162      10.821  32.905  -5.125  1.00 78.09           C  
ANISOU 1210  C   ASN A 162    13400   6856   9415   2089    172   1326       C  
ATOM   1211  O   ASN A 162      12.050  32.844  -5.105  1.00 75.43           O  
ANISOU 1211  O   ASN A 162    13087   6510   9063   1741    154   1320       O  
ATOM   1212  CB  ASN A 162      11.001  35.383  -5.285  1.00 82.87           C  
ANISOU 1212  CB  ASN A 162    14822   6825   9840   2131    390   1499       C  
ATOM   1213  CG  ASN A 162      10.547  36.633  -6.003  1.00 90.55           C  
ANISOU 1213  CG  ASN A 162    16153   7536  10715   2378    501   1664       C  
ATOM   1215  ND2 ASN A 162      10.329  36.519  -7.308  1.00 90.54           N  
ANISOU 1215  ND2 ASN A 162    16007   7709  10685   2541    430   1798       N  
ATOM   1214  OD1 ASN A 162      10.392  37.692  -5.394  1.00112.00           O  
ANISOU 1214  OD1 ASN A 162    19312   9878  13364   2422    654   1676       O  
ATOM   1216  N   SER A 163      10.043  31.895  -4.750  1.00 73.35           N  
ANISOU 1216  N   SER A 163    12471   6488   8912   2238    107   1238       N  
ATOM   1217  CA  SER A 163      10.611  30.656  -4.231  1.00 77.71           C  
ANISOU 1217  CA  SER A 163    12716   7272   9538   2004     21   1104       C  
ATOM   1218  C   SER A 163       9.739  29.448  -4.543  1.00 63.07           C  
ANISOU 1218  C   SER A 163    10468   5739   7756   2194    -88   1065       C  
ATOM   1219  O   SER A 163       8.598  29.583  -4.983  1.00 78.86           O  
ANISOU 1219  O   SER A 163    12406   7786   9773   2498   -116   1148       O  
ATOM   1220  CB  SER A 163      10.827  30.756  -2.718  1.00 61.91           C  
ANISOU 1220  CB  SER A 163    10856   5101   7566   1836     74    977       C  
ATOM   1221  OG  SER A 163       9.590  30.807  -2.030  1.00 91.32           O  
ANISOU 1221  OG  SER A 163    14596   8763  11336   2131    157    933       O  
ATOM   1222  N   VAL A 164      10.290  28.266  -4.303  1.00 58.13           N  
ANISOU 1222  N   VAL A 164     9576   5330   7181   1999   -158    961       N  
ATOM   1223  CA  VAL A 164       9.573  27.020  -4.518  1.00 64.44           C  
ANISOU 1223  CA  VAL A 164    10035   6416   8034   2114   -268    906       C  
ATOM   1224  C   VAL A 164      10.158  25.931  -3.625  1.00 66.64           C  
ANISOU 1224  C   VAL A 164    10108   6823   8390   1897   -285    761       C  
ATOM   1225  O   VAL A 164      11.376  25.746  -3.567  1.00 67.31           O  
ANISOU 1225  O   VAL A 164    10196   6907   8471   1641   -263    757       O  
ATOM   1226  CB  VAL A 164       9.628  26.589  -5.998  1.00 73.14           C  
ANISOU 1226  CB  VAL A 164    11068   7686   9034   2153   -360    993       C  
ATOM   1227  CG1 VAL A 164      11.030  26.773  -6.554  1.00 76.60           C  
ANISOU 1227  CG1 VAL A 164    11636   8069   9400   1922   -280   1041       C  
ATOM   1228  CG2 VAL A 164       9.159  25.151  -6.163  1.00 82.21           C  
ANISOU 1228  CG2 VAL A 164    11918   9112  10207   2165   -486    913       C  
ATOM   1229  N   ARG A 165       9.289  25.227  -2.908  1.00 68.85           N  
ANISOU 1229  N   ARG A 165    10194   7211   8756   2005   -317    670       N  
ATOM   1230  CA  ARG A 165       9.732  24.159  -2.024  1.00 63.11           C  
ANISOU 1230  CA  ARG A 165     9280   6601   8098   1824   -336    536       C  
ATOM   1231  C   ARG A 165       9.170  22.811  -2.457  1.00 66.84           C  
ANISOU 1231  C   ARG A 165     9448   7349   8601   1889   -440    488       C  
ATOM   1232  O   ARG A 165       8.037  22.713  -2.930  1.00 71.32           O  
ANISOU 1232  O   ARG A 165     9916   8005   9178   2096   -513    537       O  
ATOM   1233  CB  ARG A 165       9.355  24.455  -0.571  1.00 54.64           C  
ANISOU 1233  CB  ARG A 165     8309   5371   7080   1832   -258    449       C  
ATOM   1234  CG  ARG A 165       7.861  24.541  -0.311  1.00 83.36           C  
ANISOU 1234  CG  ARG A 165    11875   9013  10786   2142   -212    464       C  
ATOM   1235  CD  ARG A 165       7.573  24.712   1.172  1.00110.92           C  
ANISOU 1235  CD  ARG A 165    15504  12330  14309   2148    -80    370       C  
ATOM   1236  NE  ARG A 165       8.261  25.872   1.730  1.00121.59           N  
ANISOU 1236  NE  ARG A 165    17287  13357  15555   2016     19    369       N  
ATOM   1237  CZ  ARG A 165       8.213  26.223   3.011  1.00123.05           C  
ANISOU 1237  CZ  ARG A 165    17748  13309  15696   1966    139    286       C  
ATOM   1238  NH1 ARG A 165       8.871  27.294   3.432  1.00134.15           N1+
ANISOU 1238  NH1 ARG A 165    19604  14396  16970   1801    196    290       N1+
ATOM   1239  NH2 ARG A 165       7.508  25.502   3.871  1.00115.11           N  
ANISOU 1239  NH2 ARG A 165    16606  12372  14761   2064    203    202       N  
ATOM   1240  N   LEU A 166       9.981  21.775  -2.298  1.00 59.63           N  
ANISOU 1240  N   LEU A 166     8391   6563   7704   1701   -454    415       N  
ATOM   1241  CA  LEU A 166       9.579  20.426  -2.649  1.00 52.63           C  
ANISOU 1241  CA  LEU A 166     7276   5900   6819   1723   -537    353       C  
ATOM   1242  C   LEU A 166       9.965  19.491  -1.512  1.00 61.03           C  
ANISOU 1242  C   LEU A 166     8189   7025   7974   1582   -514    233       C  
ATOM   1243  O   LEU A 166      11.134  19.402  -1.136  1.00 60.91           O  
ANISOU 1243  O   LEU A 166     8187   6975   7983   1396   -461    237       O  
ATOM   1244  CB  LEU A 166      10.250  19.995  -3.955  1.00 47.18           C  
ANISOU 1244  CB  LEU A 166     6626   5289   6012   1669   -540    412       C  
ATOM   1245  CG  LEU A 166       9.670  18.767  -4.656  1.00101.62           C  
ANISOU 1245  CG  LEU A 166    13414  12365  12833   1707   -643    368       C  
ATOM   1246  CD1 LEU A 166       8.178  18.943  -4.887  1.00119.80           C  
ANISOU 1246  CD1 LEU A 166    15657  14726  15137   1875   -806    404       C  
ATOM   1247  CD2 LEU A 166      10.390  18.508  -5.969  1.00 84.05           C  
ANISOU 1247  CD2 LEU A 166    11345  10148  10442   1667   -593    433       C  
ATOM   1248  N   VAL A 167       8.970  18.815  -0.949  1.00 65.15           N  
ANISOU 1248  N   VAL A 167     8553   7642   8560   1668   -562    153       N  
ATOM   1249  CA  VAL A 167       9.205  17.876   0.136  1.00 46.82           C  
ANISOU 1249  CA  VAL A 167     6099   5377   6312   1552   -543     38       C  
ATOM   1250  C   VAL A 167       9.903  16.637  -0.389  1.00 58.55           C  
ANISOU 1250  C   VAL A 167     7467   7010   7768   1442   -560     10       C  
ATOM   1251  O   VAL A 167       9.476  16.049  -1.381  1.00 60.68           O  
ANISOU 1251  O   VAL A 167     7703   7389   7964   1501   -621     20       O  
ATOM   1252  CB  VAL A 167       7.888  17.446   0.804  1.00 49.04           C  
ANISOU 1252  CB  VAL A 167     6236   5720   6675   1683   -565    -22       C  
ATOM   1253  CG1 VAL A 167       8.136  16.315   1.796  1.00 41.28           C  
ANISOU 1253  CG1 VAL A 167     5125   4810   5748   1558   -550   -140       C  
ATOM   1254  CG2 VAL A 167       7.216  18.636   1.481  1.00 44.38           C  
ANISOU 1254  CG2 VAL A 167     5786   4950   6128   1831   -472     18       C  
ATOM   1255  N   ILE A 168      10.991  16.253   0.266  1.00 61.67           N  
ANISOU 1255  N   ILE A 168     7826   7394   8211   1278   -505     -5       N  
ATOM   1256  CA  ILE A 168      11.640  14.989  -0.037  1.00 54.07           C  
ANISOU 1256  CA  ILE A 168     6742   6553   7247   1209   -472    -19       C  
ATOM   1257  C   ILE A 168      11.836  14.147   1.218  1.00 47.33           C  
ANISOU 1257  C   ILE A 168     5756   5739   6487   1114   -472   -100       C  
ATOM   1258  O   ILE A 168      11.811  14.652   2.364  1.00 64.27           O  
ANISOU 1258  O   ILE A 168     7938   7796   8685   1049   -493   -127       O  
ATOM   1259  CB  ILE A 168      12.993  15.165  -0.772  1.00 60.28           C  
ANISOU 1259  CB  ILE A 168     7569   7315   8020   1129   -369    116       C  
ATOM   1260  CG1 ILE A 168      13.985  15.937   0.094  1.00 51.42           C  
ANISOU 1260  CG1 ILE A 168     6448   6093   6998    959   -359    204       C  
ATOM   1261  CG2 ILE A 168      12.794  15.856  -2.115  1.00 49.44           C  
ANISOU 1261  CG2 ILE A 168     6360   5902   6522   1227   -354    193       C  
ATOM   1262  CD1 ILE A 168      15.406  15.859  -0.402  1.00 48.97           C  
ANISOU 1262  CD1 ILE A 168     6065   5797   6745    853   -250    378       C  
ATOM   1263  N   ARG A 169      12.035  12.856   0.976  1.00 46.46           N  
ANISOU 1263  N   ARG A 169     5542   5738   6372   1107   -439   -134       N  
ATOM   1264  CA  ARG A 169      12.155  11.867   2.032  1.00 65.17           C  
ANISOU 1264  CA  ARG A 169     7787   8158   8818   1037   -437   -206       C  
ATOM   1265  C   ARG A 169      13.486  11.130   1.983  1.00 57.94           C  
ANISOU 1265  C   ARG A 169     6780   7277   7957    959   -338   -110       C  
ATOM   1266  O   ARG A 169      13.973  10.768   0.912  1.00 58.58           O  
ANISOU 1266  O   ARG A 169     6891   7380   7987   1011   -231    -40       O  
ATOM   1267  CB  ARG A 169      11.014  10.855   1.931  1.00 55.59           C  
ANISOU 1267  CB  ARG A 169     6522   7035   7566   1111   -481   -328       C  
ATOM   1268  CG  ARG A 169       9.640  11.449   2.166  1.00 50.17           C  
ANISOU 1268  CG  ARG A 169     5836   6339   6888   1201   -566   -378       C  
ATOM   1269  CD  ARG A 169       8.597  10.359   2.247  1.00 44.04           C  
ANISOU 1269  CD  ARG A 169     4951   5666   6116   1223   -624   -465       C  
ATOM   1270  NE  ARG A 169       8.324   9.765   0.944  1.00 45.91           N  
ANISOU 1270  NE  ARG A 169     5238   5973   6234   1232   -690   -454       N  
ATOM   1271  CZ  ARG A 169       7.821   8.548   0.770  1.00 94.29           C  
ANISOU 1271  CZ  ARG A 169    11334  12174  12317   1182   -742   -523       C  
ATOM   1272  NH1 ARG A 169       7.551   7.785   1.820  1.00118.21           N1+
ANISOU 1272  NH1 ARG A 169    14246  15233  15434   1136   -719   -602       N1+
ATOM   1273  NH2 ARG A 169       7.600   8.089  -0.455  1.00105.08           N  
ANISOU 1273  NH2 ARG A 169    12831  13567  13528   1159   -819   -511       N  
ATOM   1274  N   LYS A 170      14.070  10.919   3.156  1.00 53.61           N  
ANISOU 1274  N   LYS A 170     6136   6722   7510    841   -364    -87       N  
ATOM   1275  CA  LYS A 170      15.233  10.057   3.289  1.00 44.10           C  
ANISOU 1275  CA  LYS A 170     4785   5573   6400    786   -279     33       C  
ATOM   1276  C   LYS A 170      14.743   8.720   3.825  1.00 48.72           C  
ANISOU 1276  C   LYS A 170     5309   6218   6983    825   -268    -88       C  
ATOM   1277  O   LYS A 170      14.167   8.656   4.910  1.00 60.75           O  
ANISOU 1277  O   LYS A 170     6834   7731   8519    773   -364   -191       O  
ATOM   1278  CB  LYS A 170      16.253  10.683   4.238  1.00 49.56           C  
ANISOU 1278  CB  LYS A 170     5398   6224   7209    597   -363    181       C  
ATOM   1279  CG  LYS A 170      17.490   9.837   4.486  1.00 38.18           C  
ANISOU 1279  CG  LYS A 170     3737   4857   5914    540   -299    369       C  
ATOM   1280  CD  LYS A 170      18.465  10.567   5.393  1.00 60.09           C  
ANISOU 1280  CD  LYS A 170     6428   7599   8803    299   -454    553       C  
ATOM   1281  CE  LYS A 170      19.513   9.623   5.946  1.00 73.17           C  
ANISOU 1281  CE  LYS A 170     7825   9349  10629    238   -446    752       C  
ATOM   1282  NZ  LYS A 170      18.899   8.558   6.781  1.00 77.58           N1+
ANISOU 1282  NZ  LYS A 170     8395   9935  11149    287   -477    592       N1+
ATOM   1283  N   VAL A 171      14.950   7.655   3.059  1.00 59.90           N  
ANISOU 1283  N   VAL A 171     6718   7677   8366    920   -129    -77       N  
ATOM   1284  CA  VAL A 171      14.389   6.359   3.423  1.00 42.02           C  
ANISOU 1284  CA  VAL A 171     4448   5447   6072    953   -111   -204       C  
ATOM   1285  C   VAL A 171      15.434   5.260   3.545  1.00 44.07           C  
ANISOU 1285  C   VAL A 171     4609   5722   6413    983     47    -85       C  
ATOM   1286  O   VAL A 171      16.564   5.403   3.081  1.00 57.54           O  
ANISOU 1286  O   VAL A 171     6242   7423   8198   1013    181    113       O  
ATOM   1287  CB  VAL A 171      13.318   5.898   2.409  1.00 43.48           C  
ANISOU 1287  CB  VAL A 171     4794   5636   6092   1034   -110   -339       C  
ATOM   1288  CG1 VAL A 171      12.172   6.891   2.357  1.00 35.00           C  
ANISOU 1288  CG1 VAL A 171     3761   4564   4974   1031   -271   -420       C  
ATOM   1289  CG2 VAL A 171      13.937   5.713   1.034  1.00 48.30           C  
ANISOU 1289  CG2 VAL A 171     5543   6208   6602   1117     56   -250       C  
ATOM   1290  N   GLN A 172      15.035   4.158   4.173  1.00 36.30           N  
ANISOU 1290  N   GLN A 172     3616   4753   5422    986     48   -186       N  
ATOM   1291  CA  GLN A 172      15.891   2.992   4.313  1.00 45.40           C  
ANISOU 1291  CA  GLN A 172     4701   5905   6646   1048    216    -78       C  
ATOM   1292  C   GLN A 172      15.089   1.748   3.980  1.00 48.36           C  
ANISOU 1292  C   GLN A 172     5249   6244   6881   1109    290   -246       C  
ATOM   1293  O   GLN A 172      13.877   1.718   4.170  1.00 37.33           O  
ANISOU 1293  O   GLN A 172     3928   4860   5397   1049    147   -431       O  
ATOM   1294  CB  GLN A 172      16.429   2.881   5.739  1.00 44.63           C  
ANISOU 1294  CB  GLN A 172     4414   5842   6701    949    114     11       C  
ATOM   1295  CG  GLN A 172      17.414   3.961   6.134  1.00 52.93           C  
ANISOU 1295  CG  GLN A 172     5304   6915   7891    835     16    221       C  
ATOM   1296  CD  GLN A 172      17.935   3.769   7.544  1.00 55.36           C  
ANISOU 1296  CD  GLN A 172     5469   7249   8315    700   -130    321       C  
ATOM   1298  NE2 GLN A 172      19.145   4.256   7.802  1.00 51.61           N  
ANISOU 1298  NE2 GLN A 172     4801   6808   8000    598   -191    597       N  
ATOM   1297  OE1 GLN A 172      17.261   3.181   8.390  1.00 58.02           O  
ANISOU 1297  OE1 GLN A 172     5871   7575   8598    673   -199    172       O  
ATOM   1299  N   TYR A 173      15.765   0.717   3.487  1.00 39.55           N  
ANISOU 1299  N   TYR A 173     4203   5073   5751   1225    525   -161       N  
ATOM   1300  CA  TYR A 173      15.095  -0.540   3.192  1.00 48.17           C  
ANISOU 1300  CA  TYR A 173     5521   6093   6687   1257    604   -315       C  
ATOM   1301  C   TYR A 173      15.705  -1.698   3.969  1.00 45.09           C  
ANISOU 1301  C   TYR A 173     5061   5675   6397   1317    743   -238       C  
ATOM   1302  O   TYR A 173      16.801  -1.581   4.514  1.00 43.86           O  
ANISOU 1302  O   TYR A 173     4673   5557   6434   1364    811    -20       O  
ATOM   1303  CB  TYR A 173      15.098  -0.813   1.689  1.00 41.77           C  
ANISOU 1303  CB  TYR A 173     5020   5176   5673   1347    782   -330       C  
ATOM   1304  CG  TYR A 173      14.354   0.244   0.908  1.00 60.35           C  
ANISOU 1304  CG  TYR A 173     7468   7557   7904   1281    609   -408       C  
ATOM   1305  CD1 TYR A 173      15.035   1.174   0.135  1.00 56.50           C  
ANISOU 1305  CD1 TYR A 173     6982   7060   7425   1346    700   -268       C  
ATOM   1306  CD2 TYR A 173      12.970   0.329   0.969  1.00 53.29           C  
ANISOU 1306  CD2 TYR A 173     6635   6704   6909   1156    357   -592       C  
ATOM   1307  CE1 TYR A 173      14.356   2.148  -0.569  1.00 62.27           C  
ANISOU 1307  CE1 TYR A 173     7811   7808   8042   1296    539   -326       C  
ATOM   1308  CE2 TYR A 173      12.284   1.298   0.268  1.00 69.32           C  
ANISOU 1308  CE2 TYR A 173     8723   8766   8850   1115    191   -625       C  
ATOM   1309  CZ  TYR A 173      12.980   2.206  -0.500  1.00 73.47           C  
ANISOU 1309  CZ  TYR A 173     9285   9269   9362   1188    279   -500       C  
ATOM   1310  OH  TYR A 173      12.295   3.173  -1.200  1.00 81.76           O  
ANISOU 1310  OH  TYR A 173    10407  10342  10317   1158    112   -520       O  
ATOM   1311  N   ALA A 174      14.974  -2.804   4.034  1.00 48.66           N  
ANISOU 1311  N   ALA A 174     5707   6060   6722   1298    765   -398       N  
ATOM   1312  CA  ALA A 174      15.411  -3.973   4.781  1.00 49.45           C  
ANISOU 1312  CA  ALA A 174     5783   6113   6894   1359    896   -344       C  
ATOM   1313  C   ALA A 174      16.728  -4.515   4.235  1.00 58.29           C  
ANISOU 1313  C   ALA A 174     6923   7145   8078   1574   1237   -108       C  
ATOM   1314  O   ALA A 174      16.935  -4.543   3.021  1.00 71.65           O  
ANISOU 1314  O   ALA A 174     8847   8738   9639   1677   1439    -87       O  
ATOM   1315  CB  ALA A 174      14.337  -5.049   4.747  1.00 37.26           C  
ANISOU 1315  CB  ALA A 174     4505   4483   5170   1284    875   -563       C  
ATOM   1316  N   PRO A 175      17.627  -4.935   5.137  1.00 53.87           N  
ANISOU 1316  N   PRO A 175     6125   6617   7726   1649   1311     95       N  
ATOM   1317  CA  PRO A 175      18.897  -5.557   4.747  1.00 48.83           C  
ANISOU 1317  CA  PRO A 175     5444   5902   7206   1891   1668    377       C  
ATOM   1318  C   PRO A 175      18.634  -6.822   3.945  1.00 43.97           C  
ANISOU 1318  C   PRO A 175     5265   5071   6370   2034   1975    268       C  
ATOM   1319  O   PRO A 175      17.665  -7.527   4.229  1.00 96.72           O  
ANISOU 1319  O   PRO A 175    12173  11689  12889   1924   1870     29       O  
ATOM   1320  CB  PRO A 175      19.536  -5.920   6.092  1.00 44.66           C  
ANISOU 1320  CB  PRO A 175     4596   5457   6915   1892   1588    570       C  
ATOM   1321  CG  PRO A 175      18.891  -5.016   7.086  1.00 44.34           C  
ANISOU 1321  CG  PRO A 175     4394   5554   6898   1634   1179    438       C  
ATOM   1322  CD  PRO A 175      17.489  -4.825   6.600  1.00 61.76           C  
ANISOU 1322  CD  PRO A 175     6884   7722   8860   1514   1060     95       C  
ATOM   1323  N   GLU A 176      19.474  -7.102   2.956  1.00 57.78           N  
ANISOU 1323  N   GLU A 176     7160   6691   8104   2268   2363    448       N  
ATOM   1324  CA  GLU A 176      19.290  -8.280   2.114  1.00 66.88           C  
ANISOU 1324  CA  GLU A 176     8830   7583   9000   2410   2698    348       C  
ATOM   1325  C   GLU A 176      19.452  -9.567   2.912  1.00 65.79           C  
ANISOU 1325  C   GLU A 176     8731   7349   8917   2510   2836    390       C  
ATOM   1326  O   GLU A 176      18.758 -10.552   2.665  1.00 68.46           O  
ANISOU 1326  O   GLU A 176     9514   7495   9000   2477   2914    178       O  
ATOM   1327  CB  GLU A 176      20.271  -8.265   0.939  1.00 78.52           C  
ANISOU 1327  CB  GLU A 176    10466   8913  10454   2681   3154    571       C  
ATOM   1328  CG  GLU A 176      19.889  -7.319  -0.194  1.00106.03           C  
ANISOU 1328  CG  GLU A 176    14163  12388  13737   2592   3092    457       C  
ATOM   1329  CD  GLU A 176      20.109  -5.857   0.150  1.00136.14           C  
ANISOU 1329  CD  GLU A 176    17494  16455  17779   2465   2801    564       C  
ATOM   1330  OE1 GLU A 176      20.674  -5.571   1.227  1.00159.29           O  
ANISOU 1330  OE1 GLU A 176    19941  19559  21024   2443   2665    752       O  
ATOM   1331  OE2 GLU A 176      19.719  -4.991  -0.661  1.00136.68           O1-
ANISOU 1331  OE2 GLU A 176    17702  16534  17697   2374   2698    466       O1-
ATOM   1332  N   ARG A 177      20.369  -9.548   3.874  1.00 67.26           N  
ANISOU 1332  N   ARG A 177     8460   7664   9431   2612   2845    678       N  
ATOM   1333  CA  ARG A 177      20.676 -10.739   4.655  1.00 74.80           C  
ANISOU 1333  CA  ARG A 177     9423   8553  10443   2671   2923    775       C  
ATOM   1334  C   ARG A 177      19.987 -10.697   6.011  1.00 68.50           C  
ANISOU 1334  C   ARG A 177     8411   7886   9730   2496   2572    637       C  
ATOM   1335  O   ARG A 177      20.189  -9.762   6.787  1.00 72.31           O  
ANISOU 1335  O   ARG A 177     8484   8586  10407   2356   2265    734       O  
ATOM   1336  CB  ARG A 177      22.189 -10.893   4.829  1.00 76.18           C  
ANISOU 1336  CB  ARG A 177     9283   8787  10874   2816   3089   1219       C  
ATOM   1337  N   PRO A 178      19.173 -11.722   6.303  1.00 84.45           N  
ANISOU 1337  N   PRO A 178    10756   9767  11564   2430   2570    410       N  
ATOM   1338  CA  PRO A 178      18.419 -11.785   7.559  1.00 78.29           C  
ANISOU 1338  CA  PRO A 178     9843   9096  10806   2202   2221    258       C  
ATOM   1339  C   PRO A 178      19.340 -11.958   8.758  1.00 78.99           C  
ANISOU 1339  C   PRO A 178     9548   9290  11176   2293   2182    557       C  
ATOM   1340  O   PRO A 178      20.320 -12.701   8.686  1.00 72.02           O  
ANISOU 1340  O   PRO A 178     8629   8313  10422   2565   2497    835       O  
ATOM   1341  CB  PRO A 178      17.551 -13.033   7.378  1.00 62.29           C  
ANISOU 1341  CB  PRO A 178     8296   6849   8523   2160   2338     13       C  
ATOM   1342  CG  PRO A 178      18.315 -13.886   6.428  1.00 77.58           C  
ANISOU 1342  CG  PRO A 178    10553   8540  10384   2456   2814    156       C  
ATOM   1343  CD  PRO A 178      18.978 -12.928   5.480  1.00 95.77           C  
ANISOU 1343  CD  PRO A 178    12734  10911  12742   2551   2910    307       C  
ATOM   1344  N   GLY A 179      19.026 -11.270   9.850  1.00 79.29           N  
ANISOU 1344  N   GLY A 179     9319   9509  11301   2071   1801    517       N  
ATOM   1345  CA  GLY A 179      19.782 -11.412  11.079  1.00 65.19           C  
ANISOU 1345  CA  GLY A 179     7217   7820   9734   2091   1681    781       C  
ATOM   1346  C   GLY A 179      19.501 -12.748  11.740  1.00 69.53           C  
ANISOU 1346  C   GLY A 179     7969   8231  10217   2149   1784    731       C  
ATOM   1347  O   GLY A 179      18.704 -13.539  11.234  1.00 73.73           O  
ANISOU 1347  O   GLY A 179     8893   8590  10532   2152   1946    482       O  
ATOM   1348  N   PRO A 180      20.158 -13.011  12.877  1.00 63.84           N  
ANISOU 1348  N   PRO A 180     7002   7581   9673   2174   1673    980       N  
ATOM   1349  CA  PRO A 180      19.927 -14.265  13.598  1.00 54.16           C  
ANISOU 1349  CA  PRO A 180     5965   6223   8389   2231   1761    955       C  
ATOM   1350  C   PRO A 180      18.507 -14.315  14.143  1.00 60.04           C  
ANISOU 1350  C   PRO A 180     6957   6945   8912   1956   1550    563       C  
ATOM   1351  O   PRO A 180      17.928 -13.268  14.438  1.00 54.22           O  
ANISOU 1351  O   PRO A 180     6121   6341   8138   1725   1261    410       O  
ATOM   1352  CB  PRO A 180      20.939 -14.202  14.743  1.00 53.33           C  
ANISOU 1352  CB  PRO A 180     5485   6249   8528   2259   1581   1332       C  
ATOM   1353  CG  PRO A 180      21.216 -12.754  14.927  1.00 59.95           C  
ANISOU 1353  CG  PRO A 180     6010   7298   9468   2060   1252   1409       C  
ATOM   1354  CD  PRO A 180      21.123 -12.140  13.568  1.00 54.88           C  
ANISOU 1354  CD  PRO A 180     5422   6646   8784   2116   1422   1306       C  
ATOM   1355  N   GLN A 181      17.952 -15.516  14.257  1.00 49.95           N  
ANISOU 1355  N   GLN A 181     6001   5485   7494   1988   1717    422       N  
ATOM   1356  CA  GLN A 181      16.594 -15.678  14.754  1.00 42.58           C  
ANISOU 1356  CA  GLN A 181     5280   4522   6375   1732   1554     87       C  
ATOM   1357  C   GLN A 181      16.469 -15.142  16.171  1.00 49.39           C  
ANISOU 1357  C   GLN A 181     5936   5527   7302   1557   1239    118       C  
ATOM   1358  O   GLN A 181      17.169 -15.599  17.073  1.00 68.99           O  
ANISOU 1358  O   GLN A 181     8319   8009   9885   1636   1214    346       O  
ATOM   1359  CB  GLN A 181      16.176 -17.146  14.720  1.00 51.28           C  
ANISOU 1359  CB  GLN A 181     6759   5389   7336   1790   1794    -16       C  
ATOM   1360  CG  GLN A 181      14.766 -17.377  15.222  1.00 52.29           C  
ANISOU 1360  CG  GLN A 181     7077   5489   7301   1511   1642   -326       C  
ATOM   1361  CD  GLN A 181      14.423 -18.844  15.343  1.00 63.42           C  
ANISOU 1361  CD  GLN A 181     8855   6660   8582   1537   1854   -398       C  
ATOM   1363  NE2 GLN A 181      13.151 -19.137  15.592  1.00 67.60           N  
ANISOU 1363  NE2 GLN A 181     9565   7148   8972   1279   1756   -658       N  
ATOM   1362  OE1 GLN A 181      15.290 -19.708  15.214  1.00 76.90           O  
ANISOU 1362  OE1 GLN A 181    10679   8213  10325   1790   2119   -202       O  
ATOM   1364  N   PRO A 182      15.576 -14.162  16.368  1.00 46.27           N  
ANISOU 1364  N   PRO A 182     5503   5239   6837   1326   1007    -97       N  
ATOM   1365  CA  PRO A 182      15.333 -13.581  17.693  1.00 60.31           C  
ANISOU 1365  CA  PRO A 182     7183   7110   8622   1148    739   -104       C  
ATOM   1366  C   PRO A 182      14.776 -14.607  18.671  1.00 40.48           C  
ANISOU 1366  C   PRO A 182     4869   4489   6021   1092    775   -183       C  
ATOM   1367  O   PRO A 182      13.648 -15.067  18.517  1.00 57.90           O  
ANISOU 1367  O   PRO A 182     7278   6615   8105    992    853   -430       O  
ATOM   1368  CB  PRO A 182      14.295 -12.487  17.418  1.00 36.49           C  
ANISOU 1368  CB  PRO A 182     4165   4172   5527    967    601   -350       C  
ATOM   1369  CG  PRO A 182      13.695 -12.838  16.105  1.00 59.16           C  
ANISOU 1369  CG  PRO A 182     7182   6977   8318   1004    771   -516       C  
ATOM   1370  CD  PRO A 182      14.762 -13.524  15.323  1.00 52.28           C  
ANISOU 1370  CD  PRO A 182     6336   6024   7503   1235    998   -324       C  
ATOM   1371  N   THR A 183      15.584 -14.975  19.658  1.00 66.06           N  
ANISOU 1371  N   THR A 183     8042   7727   9331   1145    707     52       N  
ATOM   1372  CA  THR A 183      15.150 -15.872  20.717  1.00 48.17           C  
ANISOU 1372  CA  THR A 183     5968   5358   6976   1089    720      8       C  
ATOM   1373  C   THR A 183      15.431 -15.197  22.049  1.00 40.56           C  
ANISOU 1373  C   THR A 183     4928   4476   6006    945    433    123       C  
ATOM   1374  O   THR A 183      16.315 -14.346  22.144  1.00 66.96           O  
ANISOU 1374  O   THR A 183     8054   7938   9451    934    239    331       O  
ATOM   1375  CB  THR A 183      15.905 -17.208  20.670  1.00 53.85           C  
ANISOU 1375  CB  THR A 183     6762   5946   7753   1317    938    215       C  
ATOM   1377  CG2 THR A 183      15.829 -17.823  19.276  1.00 54.39           C  
ANISOU 1377  CG2 THR A 183     6971   5894   7800   1475   1243    134       C  
ATOM   1376  OG1 THR A 183      17.277 -16.993  21.023  1.00 63.95           O  
ANISOU 1376  OG1 THR A 183     7771   7316   9209   1449    830    596       O  
ATOM   1378  N   ALA A 184      14.676 -15.569  23.075  1.00 48.60           N  
ANISOU 1378  N   ALA A 184     6156   5417   6891    817    406     -6       N  
ATOM   1379  CA  ALA A 184      14.896 -15.020  24.407  1.00 49.98           C  
ANISOU 1379  CA  ALA A 184     6368   5623   7000    667    149     90       C  
ATOM   1380  C   ALA A 184      14.296 -15.912  25.484  1.00 48.84           C  
ANISOU 1380  C   ALA A 184     6495   5346   6716    605    211     18       C  
ATOM   1381  O   ALA A 184      13.235 -16.505  25.300  1.00 65.38           O  
ANISOU 1381  O   ALA A 184     8751   7351   8740    580    416   -213       O  
ATOM   1382  CB  ALA A 184      14.328 -13.617  24.503  1.00 39.60           C  
ANISOU 1382  CB  ALA A 184     5052   4380   5615    490     -3    -72       C  
ATOM   1383  N   GLU A 185      14.989 -16.005  26.612  1.00 60.94           N  
ANISOU 1383  N   GLU A 185     8079   6866   8209    560     15    237       N  
ATOM   1384  CA  GLU A 185      14.551 -16.862  27.701  1.00 44.14           C  
ANISOU 1384  CA  GLU A 185     6230   4603   5938    508     65    207       C  
ATOM   1385  C   GLU A 185      14.730 -16.177  29.048  1.00 45.23           C  
ANISOU 1385  C   GLU A 185     6535   4734   5918    313   -220    289       C  
ATOM   1386  O   GLU A 185      15.523 -15.248  29.184  1.00 63.75           O  
ANISOU 1386  O   GLU A 185     8753   7178   8292    231   -501    460       O  
ATOM   1387  CB  GLU A 185      15.327 -18.178  27.681  1.00 51.64           C  
ANISOU 1387  CB  GLU A 185     7157   5482   6980    711    174    446       C  
ATOM   1388  CG  GLU A 185      16.819 -18.024  27.928  1.00 66.72           C  
ANISOU 1388  CG  GLU A 185     8825   7493   9034    797    -69    863       C  
ATOM   1389  CD  GLU A 185      17.524 -19.358  28.046  1.00 98.13           C  
ANISOU 1389  CD  GLU A 185    12794  11383  13109   1028     67   1132       C  
ATOM   1390  OE1 GLU A 185      18.769 -19.371  28.152  1.00115.33           O  
ANISOU 1390  OE1 GLU A 185    14712  13649  15458   1143    -94   1530       O  
ATOM   1391  OE2 GLU A 185      16.831 -20.397  28.034  1.00105.36           O1-
ANISOU 1391  OE2 GLU A 185    13956  12135  13939   1094    337    966       O1-
ATOM   1392  N   THR A 186      13.980 -16.637  30.042  1.00 60.02           N  
ANISOU 1392  N   THR A 186     8728   6473   7606    220   -145    169       N  
ATOM   1393  CA  THR A 186      14.163 -16.164  31.409  1.00 58.21           C  
ANISOU 1393  CA  THR A 186     8763   6184   7169     36   -391    255       C  
ATOM   1394  C   THR A 186      13.699 -17.212  32.409  1.00 61.57           C  
ANISOU 1394  C   THR A 186     9512   6447   7437     21   -264    233       C  
ATOM   1395  O   THR A 186      12.781 -17.989  32.136  1.00 66.08           O  
ANISOU 1395  O   THR A 186    10153   6936   8017     83     49     41       O  
ATOM   1396  CB  THR A 186      13.443 -14.828  31.672  1.00 61.27           C  
ANISOU 1396  CB  THR A 186     9314   6559   7408   -141   -437     42       C  
ATOM   1398  CG2 THR A 186      11.940 -14.993  31.559  1.00 52.45           C  
ANISOU 1398  CG2 THR A 186     8335   5358   6237   -135    -88   -276       C  
ATOM   1397  OG1 THR A 186      13.771 -14.361  32.985  1.00 81.44           O  
ANISOU 1397  OG1 THR A 186    12199   9023   9721   -333   -696    148       O  
ATOM   1399  N   THR A 187      14.354 -17.236  33.563  1.00 67.80           N  
ANISOU 1399  N   THR A 187    10505   7183   8073    -84   -530    448       N  
ATOM   1400  CA  THR A 187      14.067 -18.223  34.591  1.00 60.02           C  
ANISOU 1400  CA  THR A 187     9850   6035   6919    -99   -445    474       C  
ATOM   1401  C   THR A 187      13.762 -17.539  35.915  1.00 66.82           C  
ANISOU 1401  C   THR A 187    11156   6774   7457   -334   -604    427       C  
ATOM   1402  O   THR A 187      14.623 -16.882  36.499  1.00 73.75           O  
ANISOU 1402  O   THR A 187    12111   7681   8230   -482   -989    637       O  
ATOM   1403  CB  THR A 187      15.249 -19.187  34.779  1.00 75.77           C  
ANISOU 1403  CB  THR A 187    11717   8049   9022     35   -603    845       C  
ATOM   1405  CG2 THR A 187      14.985 -20.134  35.936  1.00 62.67           C  
ANISOU 1405  CG2 THR A 187    10442   6211   7158      3   -550    888       C  
ATOM   1404  OG1 THR A 187      15.443 -19.946  33.579  1.00 82.67           O  
ANISOU 1404  OG1 THR A 187    12276   8975  10161    285   -363    872       O  
ATOM   1406  N   ARG A 188      12.529 -17.695  36.381  1.00 65.93           N  
ANISOU 1406  N   ARG A 188    11353   6513   7183   -380   -300    165       N  
ATOM   1407  CA  ARG A 188      12.099 -17.067  37.621  1.00 62.33           C  
ANISOU 1407  CA  ARG A 188    11395   5895   6392   -575   -349     91       C  
ATOM   1408  C   ARG A 188      12.014 -18.089  38.749  1.00 67.80           C  
ANISOU 1408  C   ARG A 188    12467   6414   6881   -602   -297    178       C  
ATOM   1409  O   ARG A 188      11.266 -19.061  38.659  1.00 71.23           O  
ANISOU 1409  O   ARG A 188    12916   6776   7372   -502     42     65       O  
ATOM   1410  CB  ARG A 188      10.741 -16.392  37.424  1.00 58.56           C  
ANISOU 1410  CB  ARG A 188    11013   5359   5877   -590      1   -231       C  
ATOM   1411  CG  ARG A 188      10.220 -15.641  38.641  1.00 63.83           C  
ANISOU 1411  CG  ARG A 188    12238   5821   6191   -752     41   -322       C  
ATOM   1412  CD  ARG A 188      10.981 -14.346  38.863  1.00 60.85           C  
ANISOU 1412  CD  ARG A 188    12004   5453   5664   -914   -331   -238       C  
ATOM   1413  NE  ARG A 188      10.398 -13.549  39.938  1.00 86.30           N  
ANISOU 1413  NE  ARG A 188    15835   8435   8518  -1059   -236   -357       N  
ATOM   1414  CZ  ARG A 188       9.425 -12.660  39.765  1.00 82.79           C  
ANISOU 1414  CZ  ARG A 188    15494   7917   8044  -1023     72   -579       C  
ATOM   1415  NH1 ARG A 188       8.921 -12.449  38.557  1.00 72.41           N1+
ANISOU 1415  NH1 ARG A 188    13688   6772   7051   -870    266   -700       N1+
ATOM   1416  NH2 ARG A 188       8.956 -11.981  40.803  1.00 77.71           N  
ANISOU 1416  NH2 ARG A 188    15471   7014   7040  -1131    197   -664       N  
ATOM   1417  N   GLN A 189      12.790 -17.870  39.804  1.00 66.87           N  
ANISOU 1417  N   GLN A 189    12669   6222   6517   -759   -656    391       N  
ATOM   1418  CA  GLN A 189      12.712 -18.709  40.993  1.00 74.00           C  
ANISOU 1418  CA  GLN A 189    14011   6937   7167   -812   -640    481       C  
ATOM   1419  C   GLN A 189      11.959 -17.973  42.092  1.00 68.27           C  
ANISOU 1419  C   GLN A 189    13904   5990   6047  -1004   -547    309       C  
ATOM   1420  O   GLN A 189      12.317 -16.857  42.460  1.00 77.38           O  
ANISOU 1420  O   GLN A 189    15286   7113   7003  -1187   -823    334       O  
ATOM   1421  CB  GLN A 189      14.105 -19.114  41.478  1.00 75.72           C  
ANISOU 1421  CB  GLN A 189    14198   7208   7363   -855  -1116    885       C  
ATOM   1422  CG  GLN A 189      14.794 -20.143  40.594  1.00 93.98           C  
ANISOU 1422  CG  GLN A 189    15993   9672  10042   -603  -1098   1096       C  
ATOM   1423  CD  GLN A 189      16.011 -20.761  41.255  1.00121.78           C  
ANISOU 1423  CD  GLN A 189    19515  13211  13544   -605  -1491   1534       C  
ATOM   1425  NE2 GLN A 189      16.402 -21.942  40.788  1.00130.17           N  
ANISOU 1425  NE2 GLN A 189    20295  14310  14855   -347  -1353   1712       N  
ATOM   1424  OE1 GLN A 189      16.590 -20.188  42.178  1.00138.30           O  
ANISOU 1424  OE1 GLN A 189    21881  15272  15393   -840  -1917   1725       O  
ATOM   1426  N   PHE A 190      10.909 -18.600  42.610  1.00 71.35           N  
ANISOU 1426  N   PHE A 190    14590   6205   6315   -964   -134    142       N  
ATOM   1427  CA  PHE A 190      10.061 -17.951  43.600  1.00 68.87           C  
ANISOU 1427  CA  PHE A 190    14870   5653   5643  -1094     79    -29       C  
ATOM   1428  C   PHE A 190      10.481 -18.263  45.027  1.00 75.01           C  
ANISOU 1428  C   PHE A 190    16279   6215   6008  -1256   -131    137       C  
ATOM   1429  O   PHE A 190      11.199 -19.229  45.279  1.00 77.87           O  
ANISOU 1429  O   PHE A 190    16591   6604   6393  -1234   -351    370       O  
ATOM   1430  CB  PHE A 190       8.594 -18.319  43.380  1.00 71.77           C  
ANISOU 1430  CB  PHE A 190    15202   5949   6119   -970    683   -284       C  
ATOM   1431  CG  PHE A 190       8.049 -17.843  42.068  1.00 83.16           C  
ANISOU 1431  CG  PHE A 190    16105   7581   7911   -852    872   -452       C  
ATOM   1432  CD1 PHE A 190       7.839 -16.493  41.842  1.00 78.55           C  
ANISOU 1432  CD1 PHE A 190    15546   7011   7289   -891    864   -565       C  
ATOM   1433  CD2 PHE A 190       7.754 -18.741  41.058  1.00 59.50           C  
ANISOU 1433  CD2 PHE A 190    12619   4729   5260   -713   1047   -489       C  
ATOM   1434  CE1 PHE A 190       7.342 -16.047  40.635  1.00 82.89           C  
ANISOU 1434  CE1 PHE A 190    15604   7735   8154   -780   1018   -698       C  
ATOM   1435  CE2 PHE A 190       7.256 -18.302  39.847  1.00 73.09           C  
ANISOU 1435  CE2 PHE A 190    13879   6618   7274   -629   1183   -630       C  
ATOM   1436  CZ  PHE A 190       7.049 -16.953  39.636  1.00 78.51           C  
ANISOU 1436  CZ  PHE A 190    14558   7337   7935   -657   1163   -728       C  
ATOM   1437  N   LEU A 191      10.025 -17.424  45.951  1.00 83.67           N  
ANISOU 1437  N   LEU A 191    18000   7077   6713  -1411    -49     24       N  
ATOM   1438  CA  LEU A 191      10.353 -17.553  47.364  1.00 88.30           C  
ANISOU 1438  CA  LEU A 191    19312   7413   6823  -1604   -249    157       C  
ATOM   1439  C   LEU A 191       9.963 -18.915  47.927  1.00 98.07           C  
ANISOU 1439  C   LEU A 191    20707   8538   8017  -1513     11    203       C  
ATOM   1440  O   LEU A 191      10.811 -19.653  48.427  1.00100.98           O  
ANISOU 1440  O   LEU A 191    21172   8904   8293  -1569   -338    463       O  
ATOM   1441  CB  LEU A 191       9.662 -16.441  48.156  1.00 89.40           C  
ANISOU 1441  CB  LEU A 191    20151   7270   6548  -1739    -36    -34       C  
ATOM   1442  CG  LEU A 191       9.748 -16.491  49.681  1.00 87.34           C  
ANISOU 1442  CG  LEU A 191    20800   6674   5710  -1946   -129     43       C  
ATOM   1443  CD1 LEU A 191      11.193 -16.460  50.137  1.00101.41           C  
ANISOU 1443  CD1 LEU A 191    22664   8507   7361  -2190   -886    348       C  
ATOM   1444  CD2 LEU A 191       8.968 -15.338  50.287  1.00105.03           C  
ANISOU 1444  CD2 LEU A 191    23449   8616   7841  -1989    193   -125       C  
ATOM   1445  N   MET A 192       8.679 -19.245  47.831  1.00113.33           N  
ANISOU 1445  N   MET A 192    22644  10381  10036  -1375    622    -26       N  
ATOM   1446  CA  MET A 192       8.148 -20.463  48.437  1.00125.83           C  
ANISOU 1446  CA  MET A 192    24448  11815  11547  -1314    937     -8       C  
ATOM   1447  C   MET A 192       8.387 -21.718  47.601  1.00128.07           C  
ANISOU 1447  C   MET A 192    24142  12287  12230  -1150    945     85       C  
ATOM   1448  O   MET A 192       8.102 -22.829  48.049  1.00147.60           O  
ANISOU 1448  O   MET A 192    26777  14642  14661  -1107   1149    133       O  
ATOM   1449  CB  MET A 192       6.652 -20.305  48.724  1.00129.16           C  
ANISOU 1449  CB  MET A 192    25114  12054  11909  -1254   1606   -253       C  
ATOM   1450  CG  MET A 192       6.309 -19.225  49.745  1.00121.73           C  
ANISOU 1450  CG  MET A 192    24918  10831  10503  -1380   1725   -338       C  
ATOM   1451  SD  MET A 192       6.413 -19.776  51.463  1.00201.02           S  
ANISOU 1451  SD  MET A 192    35732  20501  20147  -1515   1688   -197       S  
ATOM   1452  CE  MET A 192       8.156 -19.561  51.819  1.00113.40           C  
ANISOU 1452  CE  MET A 192    24826   9475   8784  -1743    802     34       C  
ATOM   1453  N   SER A 193       8.909 -21.544  46.392  1.00107.05           N  
ANISOU 1453  N   SER A 193    20845   9894   9937  -1059    744    112       N  
ATOM   1454  CA  SER A 193       9.165 -22.676  45.506  1.00105.23           C  
ANISOU 1454  CA  SER A 193    20100   9813  10068   -889    778    193       C  
ATOM   1455  C   SER A 193      10.657 -22.975  45.390  1.00 96.80           C  
ANISOU 1455  C   SER A 193    18830   8876   9072   -861    250    519       C  
ATOM   1456  O   SER A 193      11.493 -22.082  45.516  1.00107.48           O  
ANISOU 1456  O   SER A 193    20192  10310  10334   -975   -180    654       O  
ATOM   1457  CB  SER A 193       8.576 -22.418  44.115  1.00110.15           C  
ANISOU 1457  CB  SER A 193    20146  10627  11080   -774   1016     -7       C  
ATOM   1458  OG  SER A 193       7.175 -22.205  44.176  1.00105.82           O  
ANISOU 1458  OG  SER A 193    19698   9983  10526   -788   1503   -255       O  
ATOM   1459  N   ASP A 194      10.985 -24.240  45.152  1.00 89.98           N  
ANISOU 1459  N   ASP A 194    17784   8025   8380   -710    293    669       N  
ATOM   1460  CA  ASP A 194      12.367 -24.637  44.924  1.00102.36           C  
ANISOU 1460  CA  ASP A 194    19071   9726  10094   -617   -132   1021       C  
ATOM   1461  C   ASP A 194      12.615 -24.754  43.426  1.00104.32           C  
ANISOU 1461  C   ASP A 194    18675  10188  10775   -420    -55    998       C  
ATOM   1462  O   ASP A 194      13.707 -24.461  42.938  1.00116.09           O  
ANISOU 1462  O   ASP A 194    19808  11857  12445   -358   -400   1237       O  
ATOM   1463  CB  ASP A 194      12.667 -25.968  45.614  1.00114.18           C  
ANISOU 1463  CB  ASP A 194    20805  11075  11501   -534   -118   1244       C  
ATOM   1464  N   LYS A 195      11.586 -25.182  42.704  1.00 79.12           N  
ANISOU 1464  N   LYS A 195    15349   6968   7744   -338    400    724       N  
ATOM   1465  CA  LYS A 195      11.664 -25.335  41.258  1.00 73.75           C  
ANISOU 1465  CA  LYS A 195    14149   6448   7424   -173    518    660       C  
ATOM   1466  C   LYS A 195      11.256 -24.040  40.558  1.00 83.76           C  
ANISOU 1466  C   LYS A 195    15180   7866   8778   -250    514    443       C  
ATOM   1467  O   LYS A 195      10.375 -23.324  41.034  1.00 80.80           O  
ANISOU 1467  O   LYS A 195    15047   7423   8230   -396    650    236       O  
ATOM   1468  CB  LYS A 195      10.780 -26.497  40.804  1.00 92.50           C  
ANISOU 1468  CB  LYS A 195    16536   8703   9909    -88    962    494       C  
ATOM   1469  N   PRO A 196      11.900 -23.736  39.421  1.00 72.75           N  
ANISOU 1469  N   PRO A 196    13325   6663   7653   -133    385    507       N  
ATOM   1470  CA  PRO A 196      11.730 -22.451  38.738  1.00 73.51           C  
ANISOU 1470  CA  PRO A 196    13182   6914   7835   -197    314    355       C  
ATOM   1471  C   PRO A 196      10.647 -22.438  37.661  1.00 77.58           C  
ANISOU 1471  C   PRO A 196    13474   7471   8532   -157    669     59       C  
ATOM   1472  O   PRO A 196      10.185 -23.487  37.210  1.00 65.10           O  
ANISOU 1472  O   PRO A 196    11855   5823   7056    -76    938    -10       O  
ATOM   1473  CB  PRO A 196      13.089 -22.255  38.077  1.00 85.21           C  
ANISOU 1473  CB  PRO A 196    14278   8575   9525    -82    -11    632       C  
ATOM   1474  CG  PRO A 196      13.494 -23.643  37.705  1.00 84.83           C  
ANISOU 1474  CG  PRO A 196    14119   8478   9636    135    135    792       C  
ATOM   1475  CD  PRO A 196      12.965 -24.544  38.799  1.00 83.05           C  
ANISOU 1475  CD  PRO A 196    14336   8036   9184     82    285    777       C  
ATOM   1476  N   LEU A 197      10.256 -21.232  37.260  1.00 72.56           N  
ANISOU 1476  N   LEU A 197    12710   6937   7921   -230    647   -100       N  
ATOM   1477  CA  LEU A 197       9.339 -21.030  36.145  1.00 64.72           C  
ANISOU 1477  CA  LEU A 197    11444   6025   7121   -202    900   -336       C  
ATOM   1478  C   LEU A 197      10.129 -20.544  34.935  1.00 66.44           C  
ANISOU 1478  C   LEU A 197    11254   6433   7558   -100    717   -270       C  
ATOM   1479  O   LEU A 197      10.714 -19.460  34.959  1.00 69.54           O  
ANISOU 1479  O   LEU A 197    11570   6924   7930   -143    461   -201       O  
ATOM   1480  CB  LEU A 197       8.263 -20.008  36.514  1.00 53.32           C  
ANISOU 1480  CB  LEU A 197    10135   4553   5570   -323   1051   -541       C  
ATOM   1481  CG  LEU A 197       7.345 -19.543  35.382  1.00 53.45           C  
ANISOU 1481  CG  LEU A 197     9827   4686   5795   -306   1245   -741       C  
ATOM   1482  CD1 LEU A 197       6.532 -20.702  34.833  1.00 72.76           C  
ANISOU 1482  CD1 LEU A 197    12171   7096   8380   -296   1523   -833       C  
ATOM   1483  CD2 LEU A 197       6.431 -18.425  35.853  1.00 51.57           C  
ANISOU 1483  CD2 LEU A 197     9724   4412   5458   -382   1389   -879       C  
ATOM   1484  N   HIS A 198      10.148 -21.350  33.880  1.00 54.79           N  
ANISOU 1484  N   HIS A 198     9555   4987   6274     26    861   -287       N  
ATOM   1485  CA  HIS A 198      10.968 -21.052  32.714  1.00 61.23           C  
ANISOU 1485  CA  HIS A 198    10022   5953   7289    154    738   -197       C  
ATOM   1486  C   HIS A 198      10.137 -20.562  31.534  1.00 57.64           C  
ANISOU 1486  C   HIS A 198     9352   5588   6961    134    886   -432       C  
ATOM   1487  O   HIS A 198       9.162 -21.199  31.142  1.00 73.02           O  
ANISOU 1487  O   HIS A 198    11341   7469   8935     95   1130   -602       O  
ATOM   1488  CB  HIS A 198      11.780 -22.282  32.308  1.00 60.55           C  
ANISOU 1488  CB  HIS A 198     9884   5811   7312    347    796     -3       C  
ATOM   1489  CG  HIS A 198      12.876 -21.985  31.333  1.00 77.98           C  
ANISOU 1489  CG  HIS A 198    11761   8154   9713    513    671    178       C  
ATOM   1491  CD2 HIS A 198      13.268 -22.626  30.207  1.00 95.27           C  
ANISOU 1491  CD2 HIS A 198    13801  10333  12063    706    834    229       C  
ATOM   1490  ND1 HIS A 198      13.721 -20.906  31.473  1.00 93.51           N  
ANISOU 1490  ND1 HIS A 198    13540  10273  11718    484    362    346       N  
ATOM   1492  CE1 HIS A 198      14.585 -20.893  30.474  1.00 97.58           C  
ANISOU 1492  CE1 HIS A 198    13753  10885  12437    660    348    508       C  
ATOM   1493  NE2 HIS A 198      14.333 -21.928  29.692  1.00 98.57           N  
ANISOU 1493  NE2 HIS A 198    13912  10907  12631    813    650    437       N  
ATOM   1494  N   LEU A 199      10.532 -19.425  30.973  1.00 55.31           N  
ANISOU 1494  N   LEU A 199     8831   5443   6742    141    715   -422       N  
ATOM   1495  CA  LEU A 199       9.861 -18.878  29.802  1.00 43.55           C  
ANISOU 1495  CA  LEU A 199     7123   4051   5371    133    812   -610       C  
ATOM   1496  C   LEU A 199      10.824 -18.774  28.625  1.00 46.15           C  
ANISOU 1496  C   LEU A 199     7184   4489   5863    280    725   -493       C  
ATOM   1497  O   LEU A 199      11.851 -18.103  28.713  1.00 60.06           O  
ANISOU 1497  O   LEU A 199     8817   6342   7661    320    499   -309       O  
ATOM   1498  CB  LEU A 199       9.270 -17.503  30.112  1.00 51.49           C  
ANISOU 1498  CB  LEU A 199     8128   5119   6316     17    748   -729       C  
ATOM   1499  CG  LEU A 199       8.768 -16.705  28.907  1.00 48.07           C  
ANISOU 1499  CG  LEU A 199     7434   4813   6016     26    780   -868       C  
ATOM   1500  CD1 LEU A 199       7.630 -17.434  28.207  1.00 51.29           C  
ANISOU 1500  CD1 LEU A 199     7789   5198   6501     -6   1016  -1032       C  
ATOM   1501  CD2 LEU A 199       8.337 -15.308  29.325  1.00 53.10           C  
ANISOU 1501  CD2 LEU A 199     8106   5483   6585    -53    723   -943       C  
ATOM   1502  N   GLU A 200      10.489 -19.452  27.531  1.00 42.47           N  
ANISOU 1502  N   GLU A 200     6657   3999   5483    345    909   -588       N  
ATOM   1503  CA  GLU A 200      11.257 -19.357  26.296  1.00 43.07           C  
ANISOU 1503  CA  GLU A 200     6527   4148   5691    494    898   -506       C  
ATOM   1504  C   GLU A 200      10.359 -18.847  25.182  1.00 42.14           C  
ANISOU 1504  C   GLU A 200     6304   4096   5610    421    966   -728       C  
ATOM   1505  O   GLU A 200       9.224 -19.292  25.037  1.00 57.59           O  
ANISOU 1505  O   GLU A 200     8365   5990   7526    300   1102   -911       O  
ATOM   1506  CB  GLU A 200      11.823 -20.719  25.892  1.00 45.22           C  
ANISOU 1506  CB  GLU A 200     6902   4283   5995    667   1075   -387       C  
ATOM   1507  CG  GLU A 200      12.802 -21.320  26.880  1.00 76.75           C  
ANISOU 1507  CG  GLU A 200    10962   8215   9984    781   1010   -111       C  
ATOM   1508  CD  GLU A 200      13.306 -22.680  26.435  1.00100.06           C  
ANISOU 1508  CD  GLU A 200    14039  11004  12977    991   1242     14       C  
ATOM   1509  OE1 GLU A 200      13.525 -23.552  27.301  1.00108.98           O  
ANISOU 1509  OE1 GLU A 200    15346  12009  14053   1040   1283    144       O  
ATOM   1510  OE2 GLU A 200      13.485 -22.876  25.215  1.00 97.04           O1-
ANISOU 1510  OE2 GLU A 200    13614  10595  12663   1115   1401    -13       O1-
ATOM   1511  N   ALA A 201      10.869 -17.914  24.390  1.00 49.81           N  
ANISOU 1511  N   ALA A 201     7061   5198   6667    480    857   -688       N  
ATOM   1512  CA  ALA A 201      10.107 -17.383  23.271  1.00 43.31           C  
ANISOU 1512  CA  ALA A 201     6137   4444   5876    422    893   -868       C  
ATOM   1513  C   ALA A 201      11.019 -17.142  22.082  1.00 41.85           C  
ANISOU 1513  C   ALA A 201     5809   4315   5778    575    886   -768       C  
ATOM   1514  O   ALA A 201      12.208 -16.861  22.249  1.00 65.65           O  
ANISOU 1514  O   ALA A 201     8699   7379   8865    700    796   -547       O  
ATOM   1515  CB  ALA A 201       9.399 -16.099  23.672  1.00 53.41           C  
ANISOU 1515  CB  ALA A 201     7321   5828   7143    295    777   -972       C  
ATOM   1516  N   SER A 202      10.465 -17.260  20.880  1.00 55.23           N  
ANISOU 1516  N   SER A 202     7524   5998   7464    554    977   -908       N  
ATOM   1517  CA  SER A 202      11.229 -16.949  19.674  1.00 53.47           C  
ANISOU 1517  CA  SER A 202     7205   5813   7297    696   1002   -831       C  
ATOM   1518  C   SER A 202      10.314 -16.474  18.559  1.00 53.43           C  
ANISOU 1518  C   SER A 202     7191   5853   7255    586    988  -1023       C  
ATOM   1519  O   SER A 202       9.132 -16.796  18.541  1.00 52.05           O  
ANISOU 1519  O   SER A 202     7112   5645   7019    413    999  -1192       O  
ATOM   1520  CB  SER A 202      12.016 -18.169  19.201  1.00 56.03           C  
ANISOU 1520  CB  SER A 202     7699   5975   7614    886   1218   -707       C  
ATOM   1521  OG  SER A 202      11.145 -19.152  18.669  1.00 60.95           O  
ANISOU 1521  OG  SER A 202     8608   6438   8112    791   1369   -887       O  
ATOM   1522  N   LEU A 203      10.866 -15.702  17.631  1.00 41.54           N  
ANISOU 1522  N   LEU A 203     5557   4430   5797    676    951   -970       N  
ATOM   1523  CA  LEU A 203      10.123 -15.302  16.447  1.00 41.25           C  
ANISOU 1523  CA  LEU A 203     5539   4425   5709    588    928  -1121       C  
ATOM   1524  C   LEU A 203      10.576 -16.171  15.283  1.00 45.53           C  
ANISOU 1524  C   LEU A 203     6318   4815   6166    698   1116  -1105       C  
ATOM   1525  O   LEU A 203      11.668 -16.736  15.317  1.00 62.76           O  
ANISOU 1525  O   LEU A 203     8556   6909   8382    903   1275   -934       O  
ATOM   1526  CB  LEU A 203      10.355 -13.826  16.143  1.00 49.87           C  
ANISOU 1526  CB  LEU A 203     6388   5683   6877    608    776  -1085       C  
ATOM   1527  CG  LEU A 203      10.086 -12.874  17.310  1.00 40.43           C  
ANISOU 1527  CG  LEU A 203     5029   4593   5737    527    620  -1081       C  
ATOM   1528  CD1 LEU A 203      10.405 -11.436  16.931  1.00 39.20           C  
ANISOU 1528  CD1 LEU A 203     4689   4565   5641    550    488  -1037       C  
ATOM   1529  CD2 LEU A 203       8.647 -12.999  17.767  1.00 54.73           C  
ANISOU 1529  CD2 LEU A 203     6883   6402   7512    356    611  -1247       C  
ATOM   1530  N   ASP A 204       9.741 -16.295  14.259  1.00 43.18           N  
ANISOU 1530  N   ASP A 204     6180   4474   5752    563   1105  -1263       N  
ATOM   1531  CA  ASP A 204      10.094 -17.139  13.122  1.00 47.02           C  
ANISOU 1531  CA  ASP A 204     7003   4766   6096    641   1297  -1271       C  
ATOM   1532  C   ASP A 204      11.282 -16.569  12.342  1.00 56.80           C  
ANISOU 1532  C   ASP A 204     8172   6027   7383    885   1405  -1116       C  
ATOM   1533  O   ASP A 204      12.053 -17.318  11.742  1.00 54.23           O  
ANISOU 1533  O   ASP A 204     8092   5520   6991   1073   1664  -1026       O  
ATOM   1534  CB  ASP A 204       8.887 -17.394  12.211  1.00 41.19           C  
ANISOU 1534  CB  ASP A 204     6496   3967   5188    383   1205  -1467       C  
ATOM   1535  CG  ASP A 204       8.236 -16.114  11.720  1.00 75.57           C  
ANISOU 1535  CG  ASP A 204    10602   8525   9586    265    968  -1524       C  
ATOM   1536  OD1 ASP A 204       7.916 -15.243  12.555  1.00 62.63           O  
ANISOU 1536  OD1 ASP A 204     8628   7070   8099    235    826  -1507       O  
ATOM   1537  OD2 ASP A 204       8.039 -15.980  10.495  1.00 72.29           O1-
ANISOU 1537  OD2 ASP A 204    10362   8067   9037    206    933  -1580       O1-
ATOM   1538  N   LYS A 205      11.436 -15.247  12.367  1.00 46.50           N  
ANISOU 1538  N   LYS A 205     6544   4927   6196    891   1235  -1069       N  
ATOM   1539  CA  LYS A 205      12.601 -14.607  11.755  1.00 55.38           C  
ANISOU 1539  CA  LYS A 205     7540   6096   7404   1104   1325   -888       C  
ATOM   1540  C   LYS A 205      12.897 -13.227  12.339  1.00 51.30           C  
ANISOU 1540  C   LYS A 205     6635   5801   7054   1087   1111   -797       C  
ATOM   1541  O   LYS A 205      12.173 -12.738  13.206  1.00 49.67           O  
ANISOU 1541  O   LYS A 205     6296   5696   6878    928    914   -887       O  
ATOM   1542  CB  LYS A 205      12.448 -14.527  10.234  1.00 51.26           C  
ANISOU 1542  CB  LYS A 205     7265   5488   6724   1110   1414   -969       C  
ATOM   1543  CG  LYS A 205      11.189 -13.828   9.774  1.00 44.36           C  
ANISOU 1543  CG  LYS A 205     6380   4714   5759    860   1161  -1167       C  
ATOM   1544  CD  LYS A 205      10.885 -14.168   8.330  1.00 43.01           C  
ANISOU 1544  CD  LYS A 205     6590   4394   5357    810   1234  -1266       C  
ATOM   1545  CE  LYS A 205       9.479 -13.744   7.961  1.00 64.01           C  
ANISOU 1545  CE  LYS A 205     9249   7143   7928    520    946  -1439       C  
ATOM   1546  NZ  LYS A 205       9.151 -14.083   6.550  1.00 85.95           N1+
ANISOU 1546  NZ  LYS A 205    12445   9768  10444    421    958  -1527       N1+
ATOM   1547  N   GLU A 206      13.970 -12.608  11.852  1.00 48.70           N  
ANISOU 1547  N   GLU A 206     6152   5525   6826   1251   1174   -607       N  
ATOM   1548  CA  GLU A 206      14.435 -11.329  12.376  1.00 39.00           C  
ANISOU 1548  CA  GLU A 206     4592   4477   5749   1223    975   -486       C  
ATOM   1549  C   GLU A 206      13.863 -10.144  11.603  1.00 47.12           C  
ANISOU 1549  C   GLU A 206     5574   5598   6732   1124    839   -607       C  
ATOM   1550  O   GLU A 206      13.603  -9.085  12.177  1.00 57.60           O  
ANISOU 1550  O   GLU A 206     6723   7045   8115   1013    629   -627       O  
ATOM   1551  CB  GLU A 206      15.966 -11.283  12.359  1.00 45.46           C  
ANISOU 1551  CB  GLU A 206     5214   5318   6742   1429   1094   -160       C  
ATOM   1552  CG  GLU A 206      16.577 -10.224  13.265  1.00 49.86           C  
ANISOU 1552  CG  GLU A 206     5447   6037   7459   1350    847     14       C  
ATOM   1553  CD  GLU A 206      16.919  -8.947  12.529  1.00 70.50           C  
ANISOU 1553  CD  GLU A 206     7905   8752  10129   1333    773     74       C  
ATOM   1554  OE1 GLU A 206      17.399  -9.034  11.380  1.00 97.99           O  
ANISOU 1554  OE1 GLU A 206    11423  12189  13620   1490    989    154       O  
ATOM   1555  OE2 GLU A 206      16.707  -7.856  13.099  1.00 80.38           O1-
ANISOU 1555  OE2 GLU A 206     9035  10104  11400   1166    519     41       O1-
ATOM   1556  N   ILE A 207      13.665 -10.327  10.301  1.00 58.97           N  
ANISOU 1556  N   ILE A 207     7277   7020   8109   1167    965   -681       N  
ATOM   1557  CA  ILE A 207      13.170  -9.257   9.441  1.00 41.02           C  
ANISOU 1557  CA  ILE A 207     4981   4823   5780   1092    843   -770       C  
ATOM   1558  C   ILE A 207      11.752  -9.525   8.943  1.00 44.26           C  
ANISOU 1558  C   ILE A 207     5597   5199   6021    917    743  -1006       C  
ATOM   1559  O   ILE A 207      11.478 -10.559   8.334  1.00 52.89           O  
ANISOU 1559  O   ILE A 207     6995   6144   6958    900    864  -1085       O  
ATOM   1560  CB  ILE A 207      14.093  -9.035   8.221  1.00 45.21           C  
ANISOU 1560  CB  ILE A 207     5579   5305   6294   1262   1034   -635       C  
ATOM   1561  CG1 ILE A 207      15.512  -8.688   8.680  1.00 55.24           C  
ANISOU 1561  CG1 ILE A 207     6568   6639   7783   1418   1115   -344       C  
ATOM   1562  CG2 ILE A 207      13.540  -7.940   7.323  1.00 36.64           C  
ANISOU 1562  CG2 ILE A 207     4501   4290   5132   1179    895   -727       C  
ATOM   1563  CD1 ILE A 207      16.491  -8.470   7.541  1.00 60.34           C  
ANISOU 1563  CD1 ILE A 207     7235   7239   8453   1608   1353   -163       C  
ATOM   1564  N   TYR A 208      10.854  -8.584   9.209  1.00 39.41           N  
ANISOU 1564  N   TYR A 208     4822   4713   5439    780    520  -1096       N  
ATOM   1565  CA  TYR A 208       9.483  -8.671   8.721  1.00 39.21           C  
ANISOU 1565  CA  TYR A 208     4898   4697   5304    606    384  -1259       C  
ATOM   1566  C   TYR A 208       9.176  -7.493   7.810  1.00 44.98           C  
ANISOU 1566  C   TYR A 208     5562   5516   6013    590    252  -1261       C  
ATOM   1567  O   TYR A 208       9.773  -6.423   7.940  1.00 48.10           O  
ANISOU 1567  O   TYR A 208     5778   5990   6509    680    229  -1169       O  
ATOM   1568  CB  TYR A 208       8.491  -8.710   9.891  1.00 40.29           C  
ANISOU 1568  CB  TYR A 208     4885   4900   5524    473    268  -1333       C  
ATOM   1569  CG  TYR A 208       8.612  -9.954  10.741  1.00 43.49           C  
ANISOU 1569  CG  TYR A 208     5397   5204   5923    459    385  -1346       C  
ATOM   1570  CD1 TYR A 208       9.436  -9.978  11.859  1.00 41.91           C  
ANISOU 1570  CD1 TYR A 208     5091   5008   5827    557    447  -1245       C  
ATOM   1571  CD2 TYR A 208       7.912 -11.109  10.416  1.00 49.44           C  
ANISOU 1571  CD2 TYR A 208     6382   5849   6555    329    415  -1445       C  
ATOM   1572  CE1 TYR A 208       9.557 -11.117  12.634  1.00 45.99           C  
ANISOU 1572  CE1 TYR A 208     5716   5426   6332    556    551  -1240       C  
ATOM   1573  CE2 TYR A 208       8.025 -12.253  11.183  1.00 58.00           C  
ANISOU 1573  CE2 TYR A 208     7590   6822   7627    319    536  -1454       C  
ATOM   1574  CZ  TYR A 208       8.849 -12.251  12.290  1.00 57.99           C  
ANISOU 1574  CZ  TYR A 208     7467   6830   7735    449    612  -1349       C  
ATOM   1575  OH  TYR A 208       8.967 -13.386  13.054  1.00 58.51           O  
ANISOU 1575  OH  TYR A 208     7665   6781   7784    450    729  -1342       O  
ATOM   1576  N   TYR A 209       8.251  -7.696   6.880  1.00 35.78           N  
ANISOU 1576  N   TYR A 209     4558   4331   4707    458    147  -1353       N  
ATOM   1577  CA  TYR A 209       7.804  -6.619   6.006  1.00 42.73           C  
ANISOU 1577  CA  TYR A 209     5380   5297   5556    431    -10  -1346       C  
ATOM   1578  C   TYR A 209       6.485  -6.074   6.540  1.00 41.80           C  
ANISOU 1578  C   TYR A 209     5020   5315   5549    303   -217  -1382       C  
ATOM   1579  O   TYR A 209       5.822  -6.725   7.344  1.00 52.82           O  
ANISOU 1579  O   TYR A 209     6355   6714   7000    202   -232  -1428       O  
ATOM   1580  CB  TYR A 209       7.649  -7.117   4.566  1.00 37.96           C  
ANISOU 1580  CB  TYR A 209     5130   4582   4710    359    -21  -1388       C  
ATOM   1581  CG  TYR A 209       8.936  -7.633   3.957  1.00 59.54           C  
ANISOU 1581  CG  TYR A 209     8140   7153   7330    528    256  -1332       C  
ATOM   1582  CD1 TYR A 209      10.171  -7.157   4.385  1.00 56.53           C  
ANISOU 1582  CD1 TYR A 209     7578   6799   7104    739    433  -1197       C  
ATOM   1583  CD2 TYR A 209       8.918  -8.602   2.959  1.00 65.13           C  
ANISOU 1583  CD2 TYR A 209     9304   7667   7775    473    352  -1392       C  
ATOM   1584  CE1 TYR A 209      11.350  -7.625   3.834  1.00 58.09           C  
ANISOU 1584  CE1 TYR A 209     7971   6856   7242    922    724  -1095       C  
ATOM   1585  CE2 TYR A 209      10.093  -9.076   2.401  1.00 62.33           C  
ANISOU 1585  CE2 TYR A 209     9224   7137   7320    671    675  -1319       C  
ATOM   1586  CZ  TYR A 209      11.306  -8.583   2.844  1.00 70.96           C  
ANISOU 1586  CZ  TYR A 209    10060   8284   8618    912    874  -1156       C  
ATOM   1587  OH  TYR A 209      12.480  -9.049   2.295  1.00 75.29           O  
ANISOU 1587  OH  TYR A 209    10825   8668   9113   1138   1230  -1033       O  
ATOM   1588  N   HIS A 210       6.106  -4.880   6.102  1.00 41.89           N  
ANISOU 1588  N   HIS A 210     4887   5425   5602    324   -350  -1339       N  
ATOM   1589  CA  HIS A 210       4.879  -4.261   6.588  1.00 44.52           C  
ANISOU 1589  CA  HIS A 210     4962   5881   6071    258   -500  -1327       C  
ATOM   1590  C   HIS A 210       3.630  -5.022   6.146  1.00 38.84           C  
ANISOU 1590  C   HIS A 210     4269   5188   5302     44   -667  -1354       C  
ATOM   1591  O   HIS A 210       3.418  -5.256   4.957  1.00 51.67           O  
ANISOU 1591  O   HIS A 210     6086   6785   6762    -63   -798  -1356       O  
ATOM   1592  CB  HIS A 210       4.802  -2.800   6.149  1.00 35.39           C  
ANISOU 1592  CB  HIS A 210     3673   4805   4970    356   -584  -1252       C  
ATOM   1593  CG  HIS A 210       5.889  -1.944   6.717  1.00 39.03           C  
ANISOU 1593  CG  HIS A 210     4086   5243   5499    513   -460  -1210       C  
ATOM   1595  CD2 HIS A 210       7.045  -1.494   6.174  1.00 37.84           C  
ANISOU 1595  CD2 HIS A 210     4030   5050   5296    608   -388  -1158       C  
ATOM   1594  ND1 HIS A 210       5.854  -1.454   8.004  1.00 41.14           N  
ANISOU 1594  ND1 HIS A 210     4209   5522   5901    560   -403  -1201       N  
ATOM   1596  CE1 HIS A 210       6.940  -0.737   8.230  1.00 32.06           C  
ANISOU 1596  CE1 HIS A 210     3077   4338   4765    647   -343  -1149       C  
ATOM   1597  NE2 HIS A 210       7.678  -0.745   7.135  1.00 42.28           N  
ANISOU 1597  NE2 HIS A 210     4482   5612   5970    680   -331  -1111       N  
ATOM   1598  N   GLY A 211       2.809  -5.408   7.117  1.00 50.49           N  
ANISOU 1598  N   GLY A 211     5566   6708   6911    -36   -667  -1359       N  
ATOM   1599  CA  GLY A 211       1.575  -6.118   6.839  1.00 46.57           C  
ANISOU 1599  CA  GLY A 211     5027   6253   6414   -271   -839  -1346       C  
ATOM   1600  C   GLY A 211       1.773  -7.617   6.866  1.00 51.26           C  
ANISOU 1600  C   GLY A 211     5906   6707   6862   -426   -780  -1440       C  
ATOM   1601  O   GLY A 211       0.853  -8.384   6.581  1.00 64.38           O  
ANISOU 1601  O   GLY A 211     7608   8370   8485   -675   -935  -1437       O  
ATOM   1602  N   GLU A 212       2.986  -8.032   7.213  1.00 39.03           N  
ANISOU 1602  N   GLU A 212     4557   5033   5240   -283   -560  -1501       N  
ATOM   1603  CA  GLU A 212       3.335  -9.445   7.272  1.00 48.39           C  
ANISOU 1603  CA  GLU A 212     6052   6051   6284   -371   -446  -1579       C  
ATOM   1604  C   GLU A 212       3.108  -9.996   8.676  1.00 47.70           C  
ANISOU 1604  C   GLU A 212     5828   5961   6335   -382   -330  -1594       C  
ATOM   1605  O   GLU A 212       3.398  -9.322   9.664  1.00 37.35           O  
ANISOU 1605  O   GLU A 212     4298   4717   5177   -226   -238  -1558       O  
ATOM   1606  CB  GLU A 212       4.795  -9.644   6.848  1.00 45.65           C  
ANISOU 1606  CB  GLU A 212     5979   5562   5803   -176   -239  -1588       C  
ATOM   1607  CG  GLU A 212       5.342 -11.048   7.066  1.00 74.23           C  
ANISOU 1607  CG  GLU A 212     9916   8985   9304   -181    -43  -1640       C  
ATOM   1608  CD  GLU A 212       6.789 -11.191   6.637  1.00 76.37           C  
ANISOU 1608  CD  GLU A 212    10404   9124   9489     57    203  -1593       C  
ATOM   1609  OE1 GLU A 212       7.211 -12.332   6.361  1.00 74.85           O  
ANISOU 1609  OE1 GLU A 212    10572   8728   9141     69    381  -1623       O  
ATOM   1610  OE2 GLU A 212       7.506 -10.170   6.579  1.00 68.24           O1-
ANISOU 1610  OE2 GLU A 212     9188   8185   8556    236    237  -1508       O1-
ATOM   1611  N   PRO A 213       2.579 -11.224   8.770  1.00 51.52           N  
ANISOU 1611  N   PRO A 213     6482   6348   6743   -584   -339  -1645       N  
ATOM   1612  CA  PRO A 213       2.375 -11.862  10.073  1.00 41.13           C  
ANISOU 1612  CA  PRO A 213     5086   5007   5536   -604   -210  -1658       C  
ATOM   1613  C   PRO A 213       3.684 -12.184  10.791  1.00 38.56           C  
ANISOU 1613  C   PRO A 213     4890   4571   5190   -383     26  -1667       C  
ATOM   1614  O   PRO A 213       4.685 -12.538  10.167  1.00 78.74           O  
ANISOU 1614  O   PRO A 213    10236   9538  10144   -272    130  -1673       O  
ATOM   1615  CB  PRO A 213       1.639 -13.156   9.716  1.00 42.55           C  
ANISOU 1615  CB  PRO A 213     5503   5074   5593   -896   -286  -1709       C  
ATOM   1616  CG  PRO A 213       2.005 -13.419   8.294  1.00 43.96           C  
ANISOU 1616  CG  PRO A 213     6046   5133   5523   -961   -365  -1751       C  
ATOM   1617  CD  PRO A 213       2.087 -12.064   7.665  1.00 43.13           C  
ANISOU 1617  CD  PRO A 213     5735   5181   5471   -838   -485  -1690       C  
ATOM   1618  N   ILE A 214       3.651 -12.052  12.111  1.00 46.84           N  
ANISOU 1618  N   ILE A 214     6170   5742   5884     87   -104  -1578       N  
ATOM   1619  CA  ILE A 214       4.769 -12.366  12.982  1.00 45.98           C  
ANISOU 1619  CA  ILE A 214     6028   5503   5939    222     93  -1497       C  
ATOM   1620  C   ILE A 214       4.380 -13.544  13.863  1.00 51.15           C  
ANISOU 1620  C   ILE A 214     6728   6057   6651     76    100  -1544       C  
ATOM   1621  O   ILE A 214       3.362 -13.500  14.561  1.00 49.56           O  
ANISOU 1621  O   ILE A 214     6364   5968   6498    -80    -27  -1567       O  
ATOM   1622  CB  ILE A 214       5.113 -11.165  13.876  1.00 55.04           C  
ANISOU 1622  CB  ILE A 214     6878   6779   7256    338     72  -1368       C  
ATOM   1623  CG1 ILE A 214       5.481  -9.959  13.010  1.00 56.42           C  
ANISOU 1623  CG1 ILE A 214     7027   7038   7374    469     74  -1315       C  
ATOM   1624  CG2 ILE A 214       6.239 -11.517  14.843  1.00 43.55           C  
ANISOU 1624  CG2 ILE A 214     5377   5197   5971    441    201  -1264       C  
ATOM   1625  CD1 ILE A 214       5.574  -8.662  13.774  1.00 40.34           C  
ANISOU 1625  CD1 ILE A 214     4743   5124   5462    539     22  -1211       C  
ATOM   1626  N   SER A 215       5.182 -14.603  13.816  1.00 47.10           N  
ANISOU 1626  N   SER A 215     6442   5313   6139    136    278  -1551       N  
ATOM   1627  CA  SER A 215       4.895 -15.807  14.584  1.00 46.51           C  
ANISOU 1627  CA  SER A 215     6478   5096   6098      6    305  -1589       C  
ATOM   1628  C   SER A 215       5.781 -15.912  15.819  1.00 54.82           C  
ANISOU 1628  C   SER A 215     7410   6072   7348    145    389  -1446       C  
ATOM   1629  O   SER A 215       7.007 -15.962  15.725  1.00 63.85           O  
ANISOU 1629  O   SER A 215     8571   7101   8590    361    532  -1342       O  
ATOM   1630  CB  SER A 215       5.028 -17.056  13.713  1.00 58.19           C  
ANISOU 1630  CB  SER A 215     8363   6328   7419    -45    432  -1701       C  
ATOM   1631  OG  SER A 215       3.989 -17.113  12.752  1.00 65.42           O  
ANISOU 1631  OG  SER A 215     9425   7307   8124   -266    275  -1841       O  
ATOM   1632  N   VAL A 216       5.132 -15.936  16.976  1.00 58.31           N  
ANISOU 1632  N   VAL A 216     7728   6577   7852     11    296  -1429       N  
ATOM   1633  CA  VAL A 216       5.790 -16.032  18.264  1.00 48.23           C  
ANISOU 1633  CA  VAL A 216     6383   5229   6713     88    315  -1294       C  
ATOM   1634  C   VAL A 216       5.611 -17.431  18.838  1.00 57.65           C  
ANISOU 1634  C   VAL A 216     7806   6209   7891    -18    379  -1319       C  
ATOM   1635  O   VAL A 216       4.531 -17.784  19.320  1.00 62.32           O  
ANISOU 1635  O   VAL A 216     8424   6825   8428   -244    335  -1396       O  
ATOM   1636  CB  VAL A 216       5.191 -15.026  19.260  1.00 56.62           C  
ANISOU 1636  CB  VAL A 216     7226   6475   7814     10    198  -1253       C  
ATOM   1637  CG1 VAL A 216       5.996 -15.013  20.546  1.00 50.85           C  
ANISOU 1637  CG1 VAL A 216     6482   5658   7179     81    181  -1102       C  
ATOM   1638  CG2 VAL A 216       5.134 -13.636  18.641  1.00 47.48           C  
ANISOU 1638  CG2 VAL A 216     5875   5515   6651     89    135  -1246       C  
ATOM   1639  N   ASN A 217       6.668 -18.231  18.759  1.00 53.43           N  
ANISOU 1639  N   ASN A 217     7429   5452   7418    152    504  -1242       N  
ATOM   1640  CA  ASN A 217       6.702 -19.529  19.410  1.00 58.67           C  
ANISOU 1640  CA  ASN A 217     8331   5874   8086    102    574  -1225       C  
ATOM   1641  C   ASN A 217       6.956 -19.343  20.899  1.00 60.98           C  
ANISOU 1641  C   ASN A 217     8523   6175   8472    110    475  -1072       C  
ATOM   1642  O   ASN A 217       7.975 -18.771  21.300  1.00 52.97           O  
ANISOU 1642  O   ASN A 217     7347   5189   7591    297    418   -905       O  
ATOM   1643  CB  ASN A 217       7.785 -20.412  18.793  1.00 53.45           C  
ANISOU 1643  CB  ASN A 217     7876   4952   7482    330    766  -1174       C  
ATOM   1644  CG  ASN A 217       7.808 -21.806  19.385  1.00 80.76           C  
ANISOU 1644  CG  ASN A 217    11627   8121  10936    298    852  -1154       C  
ATOM   1646  ND2 ASN A 217       8.545 -21.975  20.477  1.00106.29           N  
ANISOU 1646  ND2 ASN A 217    14795  11272  14318    434    806   -957       N  
ATOM   1645  OD1 ASN A 217       7.172 -22.723  18.867  1.00 79.98           O  
ANISOU 1645  OD1 ASN A 217    11836   7863  10692    139    942  -1306       O  
ATOM   1647  N   VAL A 218       6.015 -19.818  21.709  1.00 61.25           N  
ANISOU 1647  N   VAL A 218     8668   6177   8427   -118    450  -1125       N  
ATOM   1648  CA  VAL A 218       6.085 -19.672  23.157  1.00 54.71           C  
ANISOU 1648  CA  VAL A 218     7832   5333   7620   -156    369   -999       C  
ATOM   1649  C   VAL A 218       6.111 -21.030  23.849  1.00 58.04           C  
ANISOU 1649  C   VAL A 218     8563   5480   8011   -216    436   -956       C  
ATOM   1650  O   VAL A 218       5.245 -21.882  23.615  1.00 61.96           O  
ANISOU 1650  O   VAL A 218     9248   5876   8417   -414    532  -1088       O  
ATOM   1651  CB  VAL A 218       4.894 -18.855  23.699  1.00 54.37           C  
ANISOU 1651  CB  VAL A 218     7658   5495   7507   -370    326  -1077       C  
ATOM   1652  CG1 VAL A 218       4.924 -18.815  25.220  1.00 50.37           C  
ANISOU 1652  CG1 VAL A 218     7255   4920   6965   -433    286   -961       C  
ATOM   1653  CG2 VAL A 218       4.908 -17.449  23.122  1.00 47.44           C  
ANISOU 1653  CG2 VAL A 218     6499   4865   6661   -286    254  -1094       C  
ATOM   1654  N   HIS A 219       7.115 -21.220  24.698  1.00 50.54           N  
ANISOU 1654  N   HIS A 219     7666   4399   7137    -55    363   -756       N  
ATOM   1655  CA  HIS A 219       7.267 -22.443  25.471  1.00 47.18           C  
ANISOU 1655  CA  HIS A 219     7549   3693   6684    -73    400   -669       C  
ATOM   1656  C   HIS A 219       7.435 -22.104  26.949  1.00 61.13           C  
ANISOU 1656  C   HIS A 219     9365   5455   8406   -121    242   -509       C  
ATOM   1657  O   HIS A 219       8.387 -21.431  27.339  1.00 67.87           O  
ANISOU 1657  O   HIS A 219    10066   6371   9351     38     68   -337       O  
ATOM   1658  CB  HIS A 219       8.468 -23.248  24.972  1.00 48.99           C  
ANISOU 1658  CB  HIS A 219     7859   3697   7060    219    466   -544       C  
ATOM   1659  CG  HIS A 219       8.575 -24.615  25.574  1.00122.49           C  
ANISOU 1659  CG  HIS A 219    17525  12677  16340    225    534   -465       C  
ATOM   1661  CD2 HIS A 219       9.517 -25.166  26.376  1.00116.41           C  
ANISOU 1661  CD2 HIS A 219    16859  11704  15669    418    449   -222       C  
ATOM   1660  ND1 HIS A 219       7.629 -25.596  25.366  1.00117.26           N  
ANISOU 1660  ND1 HIS A 219    17174  11847  15534      5    695   -631       N  
ATOM   1662  CE1 HIS A 219       7.982 -26.691  26.015  1.00105.67           C  
ANISOU 1662  CE1 HIS A 219    16015  10070  14065     68    735   -505       C  
ATOM   1663  NE2 HIS A 219       9.124 -26.456  26.636  1.00101.07           N  
ANISOU 1663  NE2 HIS A 219    15310   9461  13629    333    581   -250       N  
ATOM   1664  N   VAL A 220       6.495 -22.566  27.763  1.00 54.52           N  
ANISOU 1664  N   VAL A 220     8762   4535   7417   -364    304   -563       N  
ATOM   1665  CA  VAL A 220       6.526 -22.328  29.197  1.00 63.12           C  
ANISOU 1665  CA  VAL A 220    10007   5579   8397   -447    191   -429       C  
ATOM   1666  C   VAL A 220       6.716 -23.635  29.952  1.00 51.27           C  
ANISOU 1666  C   VAL A 220     8892   3758   6828   -464    216   -314       C  
ATOM   1667  O   VAL A 220       5.954 -24.582  29.771  1.00 61.35           O  
ANISOU 1667  O   VAL A 220    10379   4890   8043   -623    403   -429       O  
ATOM   1668  CB  VAL A 220       5.220 -21.668  29.683  1.00 59.11           C  
ANISOU 1668  CB  VAL A 220     9485   5226   7750   -718    295   -569       C  
ATOM   1669  CG1 VAL A 220       5.275 -21.424  31.182  1.00 48.73           C  
ANISOU 1669  CG1 VAL A 220     8420   3823   6272   -807    217   -438       C  
ATOM   1670  CG2 VAL A 220       4.968 -20.371  28.933  1.00 53.53           C  
ANISOU 1670  CG2 VAL A 220     8412   4817   7111   -684    275   -674       C  
ATOM   1671  N   THR A 221       7.742 -23.689  30.791  1.00 67.33           N  
ANISOU 1671  N   THR A 221    11029   5675   8879   -313      5    -73       N  
ATOM   1672  CA  THR A 221       7.927 -24.826  31.678  1.00 65.08           C  
ANISOU 1672  CA  THR A 221    11146   5079   8505   -325    -12     74       C  
ATOM   1673  C   THR A 221       7.639 -24.376  33.102  1.00 64.53           C  
ANISOU 1673  C   THR A 221    11316   4997   8207   -511   -132    161       C  
ATOM   1674  O   THR A 221       8.449 -23.689  33.722  1.00 62.58           O  
ANISOU 1674  O   THR A 221    11022   4802   7952   -423   -411    339       O  
ATOM   1675  CB  THR A 221       9.350 -25.401  31.595  1.00 69.22           C  
ANISOU 1675  CB  THR A 221    11647   5427   9224      9   -180    327       C  
ATOM   1677  CG2 THR A 221       9.454 -26.671  32.425  1.00 73.10           C  
ANISOU 1677  CG2 THR A 221    12586   5568   9621     11   -179    478       C  
ATOM   1676  OG1 THR A 221       9.670 -25.704  30.232  1.00 65.04           O  
ANISOU 1676  OG1 THR A 221    10911   4902   8897    204    -18    241       O  
ATOM   1678  N   ASN A 222       6.472 -24.752  33.609  1.00 66.84           N  
ANISOU 1678  N   ASN A 222    11881   5210   8306   -788     88     36       N  
ATOM   1679  CA  ASN A 222       6.050 -24.331  34.936  1.00 71.37           C  
ANISOU 1679  CA  ASN A 222    12744   5747   8625   -986     65     89       C  
ATOM   1680  C   ASN A 222       6.246 -25.425  35.976  1.00 73.31           C  
ANISOU 1680  C   ASN A 222    13504   5652   8699  -1034     30    264       C  
ATOM   1681  O   ASN A 222       5.375 -26.268  36.176  1.00 82.60           O  
ANISOU 1681  O   ASN A 222    14952   6662   9771  -1231    293    177       O  
ATOM   1682  CB  ASN A 222       4.593 -23.866  34.907  1.00 56.54           C  
ANISOU 1682  CB  ASN A 222    10805   4017   6660  -1259    374   -144       C  
ATOM   1683  CG  ASN A 222       4.096 -23.411  36.265  1.00 64.20           C  
ANISOU 1683  CG  ASN A 222    12112   4923   7356  -1456    440   -104       C  
ATOM   1685  ND2 ASN A 222       4.998 -22.881  37.083  1.00 58.52           N  
ANISOU 1685  ND2 ASN A 222    11571   4159   6506  -1370    147     79       N  
ATOM   1684  OD1 ASN A 222       2.914 -23.540  36.576  1.00 77.96           O  
ANISOU 1684  OD1 ASN A 222    13966   6649   9006  -1695    756   -229       O  
ATOM   1686  N   ASN A 223       7.398 -25.400  36.638  1.00 74.38           N  
ANISOU 1686  N   ASN A 223    13768   5681   8810   -865   -315    525       N  
ATOM   1687  CA  ASN A 223       7.705 -26.371  37.679  1.00 77.91           C  
ANISOU 1687  CA  ASN A 223    14724   5797   9080   -881   -418    737       C  
ATOM   1688  C   ASN A 223       7.369 -25.844  39.069  1.00 67.34           C  
ANISOU 1688  C   ASN A 223    13802   4400   7384  -1112   -490    801       C  
ATOM   1689  O   ASN A 223       7.701 -26.471  40.071  1.00 86.74           O  
ANISOU 1689  O   ASN A 223    16731   6587   9637  -1139   -642   1006       O  
ATOM   1690  CB  ASN A 223       9.181 -26.770  37.621  1.00 72.38           C  
ANISOU 1690  CB  ASN A 223    13937   4985   8578   -549   -783   1031       C  
ATOM   1691  CG  ASN A 223       9.538 -27.513  36.349  1.00 83.18           C  
ANISOU 1691  CG  ASN A 223    15027   6313  10266   -300   -640    989       C  
ATOM   1693  ND2 ASN A 223      10.750 -27.290  35.855  1.00 84.43           N  
ANISOU 1693  ND2 ASN A 223    14827   6542  10709     15   -879   1165       N  
ATOM   1692  OD1 ASN A 223       8.736 -28.280  35.818  1.00 98.00           O  
ANISOU 1692  OD1 ASN A 223    17023   8082  12132   -402   -306    804       O  
ATOM   1694  N   THR A 224       6.710 -24.692  39.126  1.00 81.41           N  
ANISOU 1694  N   THR A 224    15445   6411   9076  -1271   -368    630       N  
ATOM   1695  CA  THR A 224       6.396 -24.062  40.405  1.00 80.72           C  
ANISOU 1695  CA  THR A 224    15784   6258   8628  -1482   -391    669       C  
ATOM   1696  C   THR A 224       5.028 -24.480  40.936  1.00 84.42           C  
ANISOU 1696  C   THR A 224    16602   6595   8878  -1765     74    517       C  
ATOM   1697  O   THR A 224       4.329 -25.288  40.325  1.00 83.08           O  
ANISOU 1697  O   THR A 224    16327   6391   8848  -1823    374    391       O  
ATOM   1698  CB  THR A 224       6.429 -22.527  40.306  1.00 77.82           C  
ANISOU 1698  CB  THR A 224    15151   6162   8255  -1497   -475    579       C  
ATOM   1700  CG2 THR A 224       7.659 -22.064  39.539  1.00 81.20           C  
ANISOU 1700  CG2 THR A 224    15116   6764   8972  -1238   -859    693       C  
ATOM   1699  OG1 THR A 224       5.246 -22.062  39.644  1.00 62.27           O  
ANISOU 1699  OG1 THR A 224    12891   4388   6379  -1598    -61    306       O  
ATOM   1701  N   ASN A 225       4.656 -23.917  42.081  1.00 95.07           N  
ANISOU 1701  N   ASN A 225    18383   7858   9882  -1958    143    535       N  
ATOM   1702  CA  ASN A 225       3.361 -24.186  42.691  1.00101.55           C  
ANISOU 1702  CA  ASN A 225    19540   8550  10493  -2231    634    408       C  
ATOM   1703  C   ASN A 225       2.305 -23.222  42.169  1.00 92.04           C  
ANISOU 1703  C   ASN A 225    17933   7619   9421  -2315   1004    159       C  
ATOM   1704  O   ASN A 225       1.105 -23.473  42.283  1.00 90.84           O  
ANISOU 1704  O   ASN A 225    17819   7438   9259  -2513   1469     25       O  
ATOM   1705  CB  ASN A 225       3.460 -24.070  44.213  1.00102.59           C  
ANISOU 1705  CB  ASN A 225    20354   8465  10160  -2372    575    540       C  
ATOM   1706  CG  ASN A 225       4.514 -24.989  44.800  1.00120.23           C  
ANISOU 1706  CG  ASN A 225    22896  10520  12265  -2247    152    788       C  
ATOM   1708  ND2 ASN A 225       5.264 -24.483  45.772  1.00125.34           N  
ANISOU 1708  ND2 ASN A 225    23882  11123  12618  -2245   -227    935       N  
ATOM   1707  OD1 ASN A 225       4.655 -26.138  44.382  1.00135.27           O  
ANISOU 1707  OD1 ASN A 225    24733  12324  14338  -2156    157    842       O  
ATOM   1709  N   LYS A 226       2.764 -22.117  41.593  1.00 69.01           N  
ANISOU 1709  N   LYS A 226    14612   4959   6648  -2161    793    115       N  
ATOM   1710  CA  LYS A 226       1.870 -21.079  41.103  1.00 64.45           C  
ANISOU 1710  CA  LYS A 226    13653   4636   6198  -2194   1092    -91       C  
ATOM   1711  C   LYS A 226       1.253 -21.449  39.758  1.00 77.32           C  
ANISOU 1711  C   LYS A 226    14702   6472   8204  -2154   1267   -249       C  
ATOM   1712  O   LYS A 226       1.595 -22.474  39.165  1.00 67.26           O  
ANISOU 1712  O   LYS A 226    13344   5135   7078  -2096   1156   -214       O  
ATOM   1713  CB  LYS A 226       2.614 -19.747  41.011  1.00 68.63           C  
ANISOU 1713  CB  LYS A 226    14026   5333   6716  -2057    793    -69       C  
ATOM   1714  CG  LYS A 226       3.198 -19.293  42.345  1.00 76.28           C  
ANISOU 1714  CG  LYS A 226    15609   6094   7278  -2144    580     78       C  
ATOM   1715  CD  LYS A 226       3.933 -17.969  42.225  1.00 80.48           C  
ANISOU 1715  CD  LYS A 226    15994   6780   7805  -2051    270     94       C  
ATOM   1716  CE  LYS A 226       4.509 -17.546  43.565  1.00 84.60           C  
ANISOU 1716  CE  LYS A 226    17185   7073   7887  -2186     16    240       C  
ATOM   1717  NZ  LYS A 226       3.452 -17.415  44.608  1.00103.14           N1+
ANISOU 1717  NZ  LYS A 226    20100   9217   9873  -2400    483    151       N1+
ATOM   1718  N   THR A 227       0.339 -20.610  39.284  1.00 72.51           N  
ANISOU 1718  N   THR A 227    13721   6090   7738  -2186   1537   -416       N  
ATOM   1719  CA  THR A 227      -0.385 -20.882  38.048  1.00 76.05           C  
ANISOU 1719  CA  THR A 227    13638   6741   8516  -2193   1687   -564       C  
ATOM   1720  C   THR A 227      -0.319 -19.700  37.087  1.00 67.68           C  
ANISOU 1720  C   THR A 227    12062   5991   7661  -2022   1579   -655       C  
ATOM   1721  O   THR A 227      -0.541 -18.554  37.482  1.00 69.71           O  
ANISOU 1721  O   THR A 227    12315   6330   7841  -1996   1671   -680       O  
ATOM   1722  CB  THR A 227      -1.864 -21.220  38.338  1.00 70.81           C  
ANISOU 1722  CB  THR A 227    12967   6051   7886  -2446   2176   -665       C  
ATOM   1724  CG2 THR A 227      -2.680 -21.254  37.056  1.00 60.41           C  
ANISOU 1724  CG2 THR A 227    11049   4988   6916  -2476   2276   -812       C  
ATOM   1723  OG1 THR A 227      -1.945 -22.498  38.976  1.00 82.67           O  
ANISOU 1723  OG1 THR A 227    14905   7264   9242  -2619   2280   -591       O  
ATOM   1725  N   VAL A 228       0.003 -19.980  35.828  1.00 59.47           N  
ANISOU 1725  N   VAL A 228    10637   5096   6862  -1903   1398   -701       N  
ATOM   1726  CA  VAL A 228      -0.073 -18.963  34.788  1.00 57.58           C  
ANISOU 1726  CA  VAL A 228     9909   5147   6823  -1762   1327   -794       C  
ATOM   1727  C   VAL A 228      -1.531 -18.805  34.380  1.00 62.11           C  
ANISOU 1727  C   VAL A 228    10161   5878   7561  -1906   1652   -934       C  
ATOM   1728  O   VAL A 228      -2.139 -19.731  33.847  1.00 66.05           O  
ANISOU 1728  O   VAL A 228    10539   6371   8186  -2048   1746   -997       O  
ATOM   1729  CB  VAL A 228       0.774 -19.334  33.561  1.00 50.10           C  
ANISOU 1729  CB  VAL A 228     8710   4278   6050  -1590   1049   -792       C  
ATOM   1730  CG1 VAL A 228       0.543 -18.339  32.439  1.00 51.75           C  
ANISOU 1730  CG1 VAL A 228     8446   4774   6443  -1476   1011   -895       C  
ATOM   1731  CG2 VAL A 228       2.246 -19.396  33.934  1.00 49.88           C  
ANISOU 1731  CG2 VAL A 228     8899   4120   5933  -1420    728   -622       C  
ATOM   1732  N   LYS A 229      -2.093 -17.632  34.648  1.00 58.34           N  
ANISOU 1732  N   LYS A 229     9549   5528   7090  -1875   1820   -971       N  
ATOM   1733  CA  LYS A 229      -3.516 -17.403  34.444  1.00 53.87           C  
ANISOU 1733  CA  LYS A 229     8658   5102   6707  -1994   2157  -1062       C  
ATOM   1734  C   LYS A 229      -3.801 -16.894  33.039  1.00 60.45           C  
ANISOU 1734  C   LYS A 229     8936   6223   7810  -1885   2019  -1141       C  
ATOM   1735  O   LYS A 229      -4.870 -17.140  32.483  1.00 80.64           O  
ANISOU 1735  O   LYS A 229    11144   8912  10582  -2012   2162  -1204       O  
ATOM   1736  CB  LYS A 229      -4.040 -16.396  35.469  1.00 55.34           C  
ANISOU 1736  CB  LYS A 229     9001   5247   6778  -1986   2468  -1049       C  
ATOM   1737  CG  LYS A 229      -3.766 -16.782  36.913  1.00 76.34           C  
ANISOU 1737  CG  LYS A 229    12295   7604   9108  -2104   2607   -968       C  
ATOM   1738  CD  LYS A 229      -4.103 -15.645  37.864  1.00 79.42           C  
ANISOU 1738  CD  LYS A 229    12923   7925   9328  -2066   2892   -966       C  
ATOM   1739  CE  LYS A 229      -5.561 -15.236  37.748  1.00 97.29           C  
ANISOU 1739  CE  LYS A 229    14813  10316  11838  -2106   3364  -1034       C  
ATOM   1740  NZ  LYS A 229      -5.885 -14.095  38.648  1.00105.29           N1+
ANISOU 1740  NZ  LYS A 229    16088  11230  12688  -2032   3701  -1035       N1+
ATOM   1741  N   LYS A 230      -2.836 -16.187  32.466  1.00 64.42           N  
ANISOU 1741  N   LYS A 230     9361   6819   8298  -1667   1727  -1125       N  
ATOM   1742  CA  LYS A 230      -3.046 -15.522  31.192  1.00 51.18           C  
ANISOU 1742  CA  LYS A 230     7221   5399   6826  -1542   1599  -1188       C  
ATOM   1743  C   LYS A 230      -1.719 -15.245  30.489  1.00 53.51           C  
ANISOU 1743  C   LYS A 230     7522   5726   7085  -1342   1257  -1156       C  
ATOM   1744  O   LYS A 230      -0.697 -14.992  31.135  1.00 53.99           O  
ANISOU 1744  O   LYS A 230     7863   5663   6987  -1255   1130  -1071       O  
ATOM   1745  CB  LYS A 230      -3.832 -14.224  31.412  1.00 53.40           C  
ANISOU 1745  CB  LYS A 230     7291   5814   7185  -1461   1811  -1201       C  
ATOM   1746  CG  LYS A 230      -4.190 -13.463  30.145  1.00 86.94           C  
ANISOU 1746  CG  LYS A 230    11062  10325  11647  -1327   1688  -1244       C  
ATOM   1747  CD  LYS A 230      -5.368 -12.527  30.378  1.00115.42           C  
ANISOU 1747  CD  LYS A 230    14398  14046  15410  -1286   1981  -1244       C  
ATOM   1748  CE  LYS A 230      -5.122 -11.598  31.556  1.00123.35           C  
ANISOU 1748  CE  LYS A 230    15737  14902  16229  -1187   2192  -1206       C  
ATOM   1749  NZ  LYS A 230      -6.283 -10.698  31.808  1.00117.56           N1+
ANISOU 1749  NZ  LYS A 230    14763  14243  15661  -1111   2548  -1200       N1+
ATOM   1750  N   ILE A 231      -1.741 -15.306  29.161  1.00 52.79           N  
ANISOU 1750  N   ILE A 231     7125   5793   7140  -1285   1106  -1215       N  
ATOM   1751  CA  ILE A 231      -0.560 -15.004  28.366  1.00 51.69           C  
ANISOU 1751  CA  ILE A 231     6951   5693   6996  -1090    843  -1187       C  
ATOM   1752  C   ILE A 231      -0.831 -13.818  27.451  1.00 49.74           C  
ANISOU 1752  C   ILE A 231     6366   5676   6856   -955    785  -1226       C  
ATOM   1753  O   ILE A 231      -1.699 -13.878  26.584  1.00 64.11           O  
ANISOU 1753  O   ILE A 231     7914   7643   8800  -1010    796  -1297       O  
ATOM   1754  CB  ILE A 231      -0.116 -16.218  27.529  1.00 61.40           C  
ANISOU 1754  CB  ILE A 231     8231   6846   8253  -1116    724  -1215       C  
ATOM   1755  CG1 ILE A 231       0.237 -17.390  28.447  1.00 64.87           C  
ANISOU 1755  CG1 ILE A 231     9035   7026   8586  -1217    772  -1154       C  
ATOM   1756  CG2 ILE A 231       1.068 -15.857  26.647  1.00 47.45           C  
ANISOU 1756  CG2 ILE A 231     6401   5120   6508   -896    519  -1180       C  
ATOM   1757  CD1 ILE A 231       0.756 -18.606  27.717  1.00 54.84           C  
ANISOU 1757  CD1 ILE A 231     7880   5621   7334  -1212    692  -1170       C  
ATOM   1758  N   LYS A 232      -0.089 -12.736  27.659  1.00 48.72           N  
ANISOU 1758  N   LYS A 232     6273   5567   6673   -793    705  -1168       N  
ATOM   1759  CA  LYS A 232      -0.251 -11.527  26.864  1.00 50.81           C  
ANISOU 1759  CA  LYS A 232     6273   6016   7017   -648    657  -1187       C  
ATOM   1760  C   LYS A 232       0.908 -11.360  25.892  1.00 41.89           C  
ANISOU 1760  C   LYS A 232     5100   4919   5895   -500    435  -1159       C  
ATOM   1761  O   LYS A 232       2.057 -11.224  26.306  1.00 53.95           O  
ANISOU 1761  O   LYS A 232     6793   6346   7358   -432    327  -1075       O  
ATOM   1762  CB  LYS A 232      -0.336 -10.296  27.769  1.00 41.43           C  
ANISOU 1762  CB  LYS A 232     5179   4805   5759   -584    771  -1149       C  
ATOM   1763  CG  LYS A 232      -1.509 -10.294  28.732  1.00 69.50           C  
ANISOU 1763  CG  LYS A 232     8782   8313   9311   -696   1071  -1171       C  
ATOM   1764  CD  LYS A 232      -1.496  -9.042  29.597  1.00 79.55           C  
ANISOU 1764  CD  LYS A 232    10233   9517  10476   -614   1210  -1141       C  
ATOM   1765  CE  LYS A 232      -2.712  -8.975  30.507  1.00 90.77           C  
ANISOU 1765  CE  LYS A 232    11701  10877  11910   -693   1588  -1161       C  
ATOM   1766  NZ  LYS A 232      -2.701  -7.750  31.357  1.00 99.92           N1+
ANISOU 1766  NZ  LYS A 232    13112  11922  12930   -606   1768  -1144       N1+
ATOM   1767  N   ILE A 233       0.599 -11.372  24.600  1.00 42.83           N  
ANISOU 1767  N   ILE A 233     5000   5176   6096   -461    366  -1218       N  
ATOM   1768  CA  ILE A 233       1.597 -11.142  23.564  1.00 35.99           C  
ANISOU 1768  CA  ILE A 233     4099   4341   5234   -315    216  -1197       C  
ATOM   1769  C   ILE A 233       1.367  -9.761  22.970  1.00 44.38           C  
ANISOU 1769  C   ILE A 233     4974   5561   6328   -188    186  -1193       C  
ATOM   1770  O   ILE A 233       0.228  -9.361  22.759  1.00 51.70           O  
ANISOU 1770  O   ILE A 233     5721   6611   7312   -214    237  -1234       O  
ATOM   1771  CB  ILE A 233       1.471 -12.169  22.428  1.00 42.48           C  
ANISOU 1771  CB  ILE A 233     4907   5166   6068   -367    166  -1272       C  
ATOM   1772  CG1 ILE A 233       1.242 -13.573  22.992  1.00 53.59           C  
ANISOU 1772  CG1 ILE A 233     6492   6416   7452   -534    236  -1300       C  
ATOM   1773  CG2 ILE A 233       2.703 -12.124  21.531  1.00 37.10           C  
ANISOU 1773  CG2 ILE A 233     4273   4449   5375   -206     85  -1236       C  
ATOM   1774  CD1 ILE A 233       2.431 -14.133  23.732  1.00 81.40           C  
ANISOU 1774  CD1 ILE A 233    10247   9743  10939   -470    226  -1205       C  
ATOM   1775  N   SER A 234       2.433  -9.021  22.698  1.00 43.69           N  
ANISOU 1775  N   SER A 234     4912   5466   6223    -50    103  -1128       N  
ATOM   1776  CA  SER A 234       2.243  -7.696  22.121  1.00 43.26           C  
ANISOU 1776  CA  SER A 234     4722   5532   6184     70     83  -1118       C  
ATOM   1777  C   SER A 234       3.401  -7.245  21.244  1.00 46.93           C  
ANISOU 1777  C   SER A 234     5188   6001   6644    196    -10  -1066       C  
ATOM   1778  O   SER A 234       4.559  -7.449  21.576  1.00 59.68           O  
ANISOU 1778  O   SER A 234     6896   7514   8266    214    -49   -992       O  
ATOM   1779  CB  SER A 234       1.974  -6.660  23.219  1.00 44.24           C  
ANISOU 1779  CB  SER A 234     4905   5624   6281     83    174  -1082       C  
ATOM   1780  OG  SER A 234       3.015  -6.645  24.179  1.00 62.57           O  
ANISOU 1780  OG  SER A 234     7440   7801   8533     48    132  -1010       O  
ATOM   1781  N   VAL A 235       3.070  -6.647  20.107  1.00 55.34           N  
ANISOU 1781  N   VAL A 235     6139   7181   7708    280    -45  -1089       N  
ATOM   1782  CA  VAL A 235       4.051  -5.953  19.296  1.00 50.02           C  
ANISOU 1782  CA  VAL A 235     5474   6510   7022    402    -86  -1032       C  
ATOM   1783  C   VAL A 235       4.047  -4.483  19.688  1.00 43.33           C  
ANISOU 1783  C   VAL A 235     4611   5681   6170    472    -75   -976       C  
ATOM   1784  O   VAL A 235       3.027  -3.782  19.552  1.00 38.26           O  
ANISOU 1784  O   VAL A 235     3887   5124   5528    517    -53   -999       O  
ATOM   1785  CB  VAL A 235       3.769  -6.099  17.797  1.00 53.01           C  
ANISOU 1785  CB  VAL A 235     5822   6969   7351    449   -128  -1081       C  
ATOM   1786  CG1 VAL A 235       4.831  -5.367  16.993  1.00 32.56           C  
ANISOU 1786  CG1 VAL A 235     3271   4359   4739    572   -117  -1012       C  
ATOM   1787  CG2 VAL A 235       3.728  -7.570  17.414  1.00 58.18           C  
ANISOU 1787  CG2 VAL A 235     6561   7565   7978    358   -124  -1153       C  
ATOM   1788  N   ARG A 236       5.200  -4.042  20.184  1.00 40.30           N  
ANISOU 1788  N   ARG A 236     4308   5208   5797    477    -96   -891       N  
ATOM   1789  CA  ARG A 236       5.389  -2.695  20.700  1.00 46.15           C  
ANISOU 1789  CA  ARG A 236     5110   5914   6512    500    -92   -837       C  
ATOM   1790  C   ARG A 236       6.370  -1.894  19.856  1.00 48.11           C  
ANISOU 1790  C   ARG A 236     5339   6160   6778    574   -124   -762       C  
ATOM   1791  O   ARG A 236       7.453  -2.382  19.493  1.00 46.62           O  
ANISOU 1791  O   ARG A 236     5117   5941   6655    571   -151   -702       O  
ATOM   1792  CB  ARG A 236       5.894  -2.752  22.144  1.00 49.50           C  
ANISOU 1792  CB  ARG A 236     5687   6211   6910    382   -124   -791       C  
ATOM   1793  CG  ARG A 236       4.804  -2.634  23.191  1.00 62.17           C  
ANISOU 1793  CG  ARG A 236     7399   7779   8445    327    -20   -850       C  
ATOM   1794  CD  ARG A 236       4.968  -3.670  24.288  1.00 59.18           C  
ANISOU 1794  CD  ARG A 236     7156   7301   8029    193    -39   -843       C  
ATOM   1795  NE  ARG A 236       6.275  -3.601  24.935  1.00 71.75           N  
ANISOU 1795  NE  ARG A 236     8883   8781   9597    112   -198   -735       N  
ATOM   1796  CZ  ARG A 236       6.526  -2.919  26.047  1.00 60.87           C  
ANISOU 1796  CZ  ARG A 236     7750   7278   8100      9   -242   -696       C  
ATOM   1797  NH1 ARG A 236       7.746  -2.922  26.565  1.00 47.94           N1+
ANISOU 1797  NH1 ARG A 236     6201   5554   6459    -90   -451   -577       N1+
ATOM   1798  NH2 ARG A 236       5.559  -2.236  26.642  1.00 64.08           N  
ANISOU 1798  NH2 ARG A 236     8320   7636   8393      2    -76   -766       N  
ATOM   1799  N   GLN A 237       5.974  -0.658  19.556  1.00 42.96           N  
ANISOU 1799  N   GLN A 237     4710   5530   6084    648    -95   -755       N  
ATOM   1800  CA  GLN A 237       6.831   0.299  18.874  1.00 36.04           C  
ANISOU 1800  CA  GLN A 237     3856   4628   5210    697   -103   -677       C  
ATOM   1801  C   GLN A 237       7.591   1.159  19.881  1.00 51.19           C  
ANISOU 1801  C   GLN A 237     5902   6424   7125    596   -141   -604       C  
ATOM   1802  O   GLN A 237       6.995   1.879  20.681  1.00 51.71           O  
ANISOU 1802  O   GLN A 237     6106   6425   7117    578   -108   -630       O  
ATOM   1803  CB  GLN A 237       6.015   1.200  17.943  1.00 35.05           C  
ANISOU 1803  CB  GLN A 237     3727   4567   5025    834    -66   -692       C  
ATOM   1804  CG  GLN A 237       6.860   2.219  17.183  1.00 32.44           C  
ANISOU 1804  CG  GLN A 237     3459   4190   4675    879    -49   -608       C  
ATOM   1805  CD  GLN A 237       6.031   3.301  16.514  1.00 61.76           C  
ANISOU 1805  CD  GLN A 237     7224   7926   8314   1020    -24   -600       C  
ATOM   1807  NE2 GLN A 237       5.671   3.079  15.255  1.00 39.68           N  
ANISOU 1807  NE2 GLN A 237     4393   5219   5465   1114    -50   -607       N  
ATOM   1806  OE1 GLN A 237       5.725   4.329  17.120  1.00 41.27           O  
ANISOU 1806  OE1 GLN A 237     4731   5251   5698   1048     15   -581       O  
ATOM   1808  N   TYR A 238       8.913   1.068  19.832  1.00 41.49           N  
ANISOU 1808  N   TYR A 238     4632   5151   5981    523   -206   -506       N  
ATOM   1809  CA  TYR A 238       9.786   1.902  20.640  1.00 45.55           C  
ANISOU 1809  CA  TYR A 238     5251   5552   6503    383   -299   -414       C  
ATOM   1810  C   TYR A 238      10.229   3.096  19.810  1.00 38.53           C  
ANISOU 1810  C   TYR A 238     4379   4642   5618    415   -251   -356       C  
ATOM   1811  O   TYR A 238      10.764   2.933  18.710  1.00 50.63           O  
ANISOU 1811  O   TYR A 238     5777   6230   7232    487   -187   -309       O  
ATOM   1812  CB  TYR A 238      11.015   1.108  21.090  1.00 33.99           C  
ANISOU 1812  CB  TYR A 238     3673   4061   5182    270   -431   -302       C  
ATOM   1813  CG  TYR A 238      10.739   0.063  22.146  1.00 47.86           C  
ANISOU 1813  CG  TYR A 238     5484   5789   6910    204   -512   -330       C  
ATOM   1814  CD1 TYR A 238       9.846  -0.976  21.913  1.00 37.67           C  
ANISOU 1814  CD1 TYR A 238     4157   4562   5595    296   -417   -433       C  
ATOM   1815  CD2 TYR A 238      11.389   0.104  23.373  1.00 58.50           C  
ANISOU 1815  CD2 TYR A 238     6947   7035   8247     25   -701   -242       C  
ATOM   1816  CE1 TYR A 238       9.600  -1.934  22.876  1.00 49.89           C  
ANISOU 1816  CE1 TYR A 238     5781   6065   7111    224   -469   -451       C  
ATOM   1817  CE2 TYR A 238      11.151  -0.851  24.340  1.00 57.38           C  
ANISOU 1817  CE2 TYR A 238     6901   6847   8052    -37   -775   -254       C  
ATOM   1818  CZ  TYR A 238      10.256  -1.867  24.087  1.00 62.50           C  
ANISOU 1818  CZ  TYR A 238     7512   7553   8682     69   -640   -360       C  
ATOM   1819  OH  TYR A 238      10.016  -2.818  25.050  1.00 74.31           O  
ANISOU 1819  OH  TYR A 238     9130   8986  10120     -3   -692   -366       O  
ATOM   1820  N   ALA A 239      10.002   4.295  20.336  1.00 41.10           N  
ANISOU 1820  N   ALA A 239     4913   4863   5842    360   -252   -359       N  
ATOM   1821  CA  ALA A 239      10.402   5.516  19.653  1.00 36.69           C  
ANISOU 1821  CA  ALA A 239     4424   4246   5269    371   -202   -299       C  
ATOM   1822  C   ALA A 239      11.281   6.369  20.552  1.00 34.89           C  
ANISOU 1822  C   ALA A 239     4363   3863   5030    140   -321   -220       C  
ATOM   1823  O   ALA A 239      10.878   6.750  21.650  1.00 56.46           O  
ANISOU 1823  O   ALA A 239     7343   6477   7632     48   -363   -268       O  
ATOM   1824  CB  ALA A 239       9.180   6.304  19.205  1.00 36.46           C  
ANISOU 1824  CB  ALA A 239     4526   4212   5117    552    -75   -371       C  
ATOM   1825  N   ASP A 240      12.488   6.659  20.079  1.00 54.47           N  
ANISOU 1825  N   ASP A 240     6721   6331   7643     32   -367    -94       N  
ATOM   1826  CA  ASP A 240      13.392   7.549  20.783  1.00 42.07           C  
ANISOU 1826  CA  ASP A 240     5288   4616   6082   -229   -512      0       C  
ATOM   1827  C   ASP A 240      13.443   8.872  20.041  1.00 44.16           C  
ANISOU 1827  C   ASP A 240     5702   4787   6289   -216   -387     25       C  
ATOM   1828  O   ASP A 240      13.854   8.927  18.887  1.00 52.29           O  
ANISOU 1828  O   ASP A 240     6563   5883   7422   -131   -268     88       O  
ATOM   1829  CB  ASP A 240      14.791   6.937  20.875  1.00 65.35           C  
ANISOU 1829  CB  ASP A 240     7940   7613   9275   -395   -673    160       C  
ATOM   1830  CG  ASP A 240      14.776   5.524  21.426  1.00 86.93           C  
ANISOU 1830  CG  ASP A 240    10510  10434  12084   -359   -776    156       C  
ATOM   1831  OD1 ASP A 240      15.610   4.704  20.988  1.00110.48           O  
ANISOU 1831  OD1 ASP A 240    13170  13504  15302   -326   -784    268       O  
ATOM   1832  OD2 ASP A 240      13.927   5.230  22.292  1.00 92.01           O1-
ANISOU 1832  OD2 ASP A 240    11360  11043  12557   -353   -819     48       O1-
ATOM   1833  N   ILE A 241      13.013   9.936  20.704  1.00 40.21           N  
ANISOU 1833  N   ILE A 241     5562   4108   5608   -296   -390    -25       N  
ATOM   1834  CA  ILE A 241      12.949  11.248  20.080  1.00 50.71           C  
ANISOU 1834  CA  ILE A 241     7101   5308   6857   -269   -260     -5       C  
ATOM   1835  C   ILE A 241      13.901  12.201  20.784  1.00 66.84           C  
ANISOU 1835  C   ILE A 241     9366   7151   8878   -611   -407     74       C  
ATOM   1836  O   ILE A 241      13.715  12.517  21.959  1.00 74.71           O  
ANISOU 1836  O   ILE A 241    10675   7991   9720   -770   -515     19       O  
ATOM   1837  CB  ILE A 241      11.519  11.797  20.134  1.00 48.87           C  
ANISOU 1837  CB  ILE A 241     7138   4999   6433    -27    -92   -126       C  
ATOM   1838  CG1 ILE A 241      10.550  10.741  19.607  1.00 49.02           C  
ANISOU 1838  CG1 ILE A 241     6909   5227   6488    250    -14   -198       C  
ATOM   1839  CG2 ILE A 241      11.409  13.097  19.355  1.00 42.94           C  
ANISOU 1839  CG2 ILE A 241     6600   4109   5606     55     51    -88       C  
ATOM   1840  CD1 ILE A 241       9.163  11.246  19.374  1.00 61.15           C  
ANISOU 1840  CD1 ILE A 241     8583   6735   7916    522    147   -270       C  
ATOM   1841  N   CYS A 242      15.117  12.379  20.033  1.00 81.83           N  
ANISOU 1841  N   CYS A 242    11023   9088  10981   -757   -432    226       N  
ATOM   1842  CA  CYS A 242      16.224  13.186  20.529  1.00102.74           C  
ANISOU 1842  CA  CYS A 242    13770  11581  13684  -1134   -604    342       C  
ATOM   1843  C   CYS A 242      16.291  14.514  19.784  1.00104.09           C  
ANISOU 1843  C   CYS A 242    14178  11588  13782  -1155   -431    374       C  
ATOM   1844  O   CYS A 242      16.829  14.590  18.676  1.00130.46           O  
ANISOU 1844  O   CYS A 242    17293  14999  17275  -1108   -288    473       O  
ATOM   1845  CB  CYS A 242      17.535  12.422  20.356  1.00126.26           C  
ANISOU 1845  CB  CYS A 242    16272  14711  16991  -1300   -749    516       C  
ATOM   1846  SG  CYS A 242      17.369  10.632  20.604  1.00162.64           S  
ANISOU 1846  SG  CYS A 242    20513  19550  21732  -1111   -824    496       S  
ATOM   1847  N   LEU A 243      15.731  15.557  20.389  1.00 94.46           N  
ANISOU 1847  N   LEU A 243    13452  10124  12315  -1216   -413    290       N  
ATOM   1848  CA  LEU A 243      15.654  16.868  19.750  1.00106.28           C  
ANISOU 1848  CA  LEU A 243    15254  11419  13707  -1208   -234    311       C  
ATOM   1849  C   LEU A 243      16.061  18.169  20.430  1.00109.46           C  
ANISOU 1849  C   LEU A 243    16131  11498  13960  -1545   -312    324       C  
ATOM   1850  O   LEU A 243      17.149  18.694  20.192  1.00119.94           O  
ANISOU 1850  O   LEU A 243    17401  12756  15415  -1860   -390    456       O  
ATOM   1851  CB  LEU A 243      14.222  17.163  19.298  1.00107.65           C  
ANISOU 1851  CB  LEU A 243    15651  11557  13694   -790     13    195       C  
ATOM   1852  CG  LEU A 243      13.783  16.743  17.895  1.00135.44           C  
ANISOU 1852  CG  LEU A 243    18901  15274  17286   -444    195    220       C  
ATOM   1853  CD1 LEU A 243      14.665  17.400  16.857  1.00151.54           C  
ANISOU 1853  CD1 LEU A 243    20914  17259  19407   -553    296    356       C  
ATOM   1854  CD2 LEU A 243      13.792  15.235  17.719  1.00143.62           C  
ANISOU 1854  CD2 LEU A 243    19486  16606  18477   -334    129    204       C  
ATOM   1855  N   PHE A 244      15.167  18.690  21.265  1.00 90.51           N  
ANISOU 1855  N   PHE A 244    14215   8883  11292  -1483   -265    189       N  
ATOM   1856  CA  PHE A 244      15.454  19.867  22.071  1.00104.75           C  
ANISOU 1856  CA  PHE A 244    16577  10330  12893  -1811   -336    170       C  
ATOM   1857  C   PHE A 244      15.907  19.178  23.349  1.00 97.18           C  
ANISOU 1857  C   PHE A 244    15611   9400  11913  -2118   -662    153       C  
ATOM   1858  O   PHE A 244      17.064  19.279  23.755  1.00 86.14           O  
ANISOU 1858  O   PHE A 244    14153   7968  10610  -2558   -959    264       O  
ATOM   1859  CB  PHE A 244      14.244  20.781  22.273  1.00107.92           C  
ANISOU 1859  CB  PHE A 244    17539  10452  13014  -1545    -61     40       C  
ATOM   1860  N   ASN A 245      14.971  18.477  23.976  1.00 83.37           N  
ANISOU 1860  N   ASN A 245    13922   7712  10044  -1889   -612     28       N  
ATOM   1861  CA  ASN A 245      15.284  17.523  25.024  1.00 65.33           C  
ANISOU 1861  CA  ASN A 245    11545   5520   7756  -2088   -899     23       C  
ATOM   1862  C   ASN A 245      15.013  16.137  24.458  1.00 75.95           C  
ANISOU 1862  C   ASN A 245    12299   7228   9329  -1781   -859     40       C  
ATOM   1863  O   ASN A 245      14.727  16.003  23.269  1.00 81.44           O  
ANISOU 1863  O   ASN A 245    12689   8085  10171  -1484   -648     61       O  
ATOM   1864  CB  ASN A 245      14.430  17.790  26.262  1.00 73.54           C  
ANISOU 1864  CB  ASN A 245    13191   6303   8447  -2095   -837   -136       C  
ATOM   1865  CG  ASN A 245      14.667  19.172  26.840  1.00 85.54           C  
ANISOU 1865  CG  ASN A 245    15391   7413   9698  -2403   -851   -171       C  
ATOM   1867  ND2 ASN A 245      13.588  19.908  27.080  1.00107.14           N  
ANISOU 1867  ND2 ASN A 245    18643   9884  12181  -2163   -511   -310       N  
ATOM   1866  OD1 ASN A 245      15.808  19.580  27.056  1.00 73.86           O  
ANISOU 1866  OD1 ASN A 245    13967   5844   8251  -2853  -1158    -65       O  
ATOM   1868  N   THR A 246      15.099  15.105  25.287  1.00 67.84           N  
ANISOU 1868  N   THR A 246    11154   6311   8311  -1860  -1064     32       N  
ATOM   1869  CA  THR A 246      14.852  13.755  24.796  1.00 59.34           C  
ANISOU 1869  CA  THR A 246     9563   5546   7437  -1588  -1024     42       C  
ATOM   1870  C   THR A 246      13.579  13.156  25.381  1.00 72.53           C  
ANISOU 1870  C   THR A 246    11396   7228   8935  -1337   -868   -112       C  
ATOM   1871  O   THR A 246      13.328  13.248  26.582  1.00 93.49           O  
ANISOU 1871  O   THR A 246    14459   9704  11358  -1492   -945   -183       O  
ATOM   1872  CB  THR A 246      16.042  12.815  25.067  1.00 72.62           C  
ANISOU 1872  CB  THR A 246    10841   7392   9358  -1825  -1361    197       C  
ATOM   1874  CG2 THR A 246      17.285  13.316  24.349  1.00 64.91           C  
ANISOU 1874  CG2 THR A 246     9585   6442   8634  -2038  -1459    375       C  
ATOM   1873  OG1 THR A 246      16.299  12.751  26.475  1.00 91.49           O  
ANISOU 1873  OG1 THR A 246    13559   9635  11569  -2136  -1662    196       O  
ATOM   1875  N   ALA A 247      12.774  12.551  24.515  1.00 61.63           N  
ANISOU 1875  N   ALA A 247     9709   6046   7661   -968   -644   -160       N  
ATOM   1876  CA  ALA A 247      11.569  11.857  24.941  1.00 52.05           C  
ANISOU 1876  CA  ALA A 247     8537   4887   6354   -732   -489   -284       C  
ATOM   1877  C   ALA A 247      11.578  10.438  24.393  1.00 49.39           C  
ANISOU 1877  C   ALA A 247     7699   4840   6227   -584   -529   -258       C  
ATOM   1878  O   ALA A 247      12.293  10.139  23.436  1.00 59.78           O  
ANISOU 1878  O   ALA A 247     8658   6307   7748   -565   -579   -162       O  
ATOM   1879  CB  ALA A 247      10.333  12.597  24.470  1.00 58.45           C  
ANISOU 1879  CB  ALA A 247     9512   5622   7073   -416   -162   -375       C  
ATOM   1880  N   GLN A 248      10.832   9.579  24.987  1.00 54.10           N  
ANISOU 1880  N   GLN A 248     8297   5491   6768   -493   -485   -339       N  
ATOM   1881  CA  GLN A 248      10.729   8.187  24.568  1.00 46.72           C  
ANISOU 1881  CA  GLN A 248     6959   4793   6000   -363   -508   -332       C  
ATOM   1882  C   GLN A 248       9.361   7.613  24.899  1.00 51.03           C  
ANISOU 1882  C   GLN A 248     7545   5379   6466   -165   -315   -457       C  
ATOM   1883  O   GLN A 248       8.723   8.027  25.867  1.00 57.77           O  
ANISOU 1883  O   GLN A 248     8753   6063   7133   -197   -210   -532       O  
ATOM   1884  CB  GLN A 248      11.817   7.346  25.239  1.00 39.42           C  
ANISOU 1884  CB  GLN A 248     5925   3897   5157   -603   -800   -231       C  
ATOM   1885  N   TYR A 249       8.904   6.665  24.087  1.00 45.81           N  
ANISOU 1885  N   TYR A 249     6535   4926   5945     26   -249   -477       N  
ATOM   1886  CA  TYR A 249       7.685   5.934  24.410  1.00 40.15           C  
ANISOU 1886  CA  TYR A 249     5785   4270   5199    164    -99   -576       C  
ATOM   1887  C   TYR A 249       7.699   4.511  23.867  1.00 35.23           C  
ANISOU 1887  C   TYR A 249     4819   3845   4721    221   -156   -574       C  
ATOM   1888  O   TYR A 249       8.419   4.203  22.916  1.00 52.82           O  
ANISOU 1888  O   TYR A 249     6812   6178   7077    245   -236   -512       O  
ATOM   1889  CB  TYR A 249       6.421   6.693  23.958  1.00 46.26           C  
ANISOU 1889  CB  TYR A 249     6590   5037   5949    408    147   -639       C  
ATOM   1890  CG  TYR A 249       6.221   6.831  22.457  1.00 52.13           C  
ANISOU 1890  CG  TYR A 249     7056   5939   6813    605    169   -608       C  
ATOM   1891  CD1 TYR A 249       5.820   5.748  21.682  1.00 54.41           C  
ANISOU 1891  CD1 TYR A 249     7027   6433   7213    705    146   -628       C  
ATOM   1892  CD2 TYR A 249       6.392   8.057  21.824  1.00 61.91           C  
ANISOU 1892  CD2 TYR A 249     8405   7094   8023    680    214   -561       C  
ATOM   1893  CE1 TYR A 249       5.627   5.874  20.319  1.00 57.78           C  
ANISOU 1893  CE1 TYR A 249     7273   6983   7698    863    144   -601       C  
ATOM   1894  CE2 TYR A 249       6.195   8.194  20.459  1.00 47.51           C  
ANISOU 1894  CE2 TYR A 249     6386   5396   6269    856    225   -523       C  
ATOM   1895  CZ  TYR A 249       5.810   7.099  19.713  1.00 55.49           C  
ANISOU 1895  CZ  TYR A 249     7101   6614   7368    943    181   -544       C  
ATOM   1896  OH  TYR A 249       5.615   7.221  18.355  1.00 48.41           O  
ANISOU 1896  OH  TYR A 249     6076   5825   6493   1094    169   -508       O  
ATOM   1897  N   LYS A 250       6.906   3.652  24.498  1.00 50.97           N  
ANISOU 1897  N   LYS A 250     6820   5861   6684    233    -85   -644       N  
ATOM   1898  CA  LYS A 250       6.675   2.295  24.026  1.00 48.85           C  
ANISOU 1898  CA  LYS A 250     6281   5750   6528    288   -101   -665       C  
ATOM   1899  C   LYS A 250       5.185   2.156  23.762  1.00 63.31           C  
ANISOU 1899  C   LYS A 250     8015   7665   8376    445     92   -755       C  
ATOM   1900  O   LYS A 250       4.382   2.171  24.696  1.00 73.31           O  
ANISOU 1900  O   LYS A 250     9429   8854   9570    429    234   -807       O  
ATOM   1901  CB  LYS A 250       7.088   1.272  25.086  1.00 57.30           C  
ANISOU 1901  CB  LYS A 250     7445   6761   7565    125   -211   -646       C  
ATOM   1902  CG  LYS A 250       8.471   1.477  25.680  1.00 70.55           C  
ANISOU 1902  CG  LYS A 250     9245   8334   9227    -63   -445   -531       C  
ATOM   1903  CD  LYS A 250       8.738   0.452  26.773  1.00 73.41           C  
ANISOU 1903  CD  LYS A 250     9729   8628   9535   -205   -573   -497       C  
ATOM   1904  CE  LYS A 250      10.123   0.618  27.372  1.00 84.02           C  
ANISOU 1904  CE  LYS A 250    11154   9881  10888   -401   -872   -349       C  
ATOM   1905  NZ  LYS A 250      10.408  -0.433  28.389  1.00 80.07           N1+
ANISOU 1905  NZ  LYS A 250    10775   9313  10336   -521  -1035   -289       N1+
ATOM   1906  N   CYS A 251       4.809   2.027  22.497  1.00 57.00           N  
ANISOU 1906  N   CYS A 251     6971   7017   7671    589    100   -763       N  
ATOM   1907  CA  CYS A 251       3.396   1.924  22.155  1.00 54.55           C  
ANISOU 1907  CA  CYS A 251     6507   6807   7411    725    227   -820       C  
ATOM   1908  C   CYS A 251       3.070   0.594  21.495  1.00 46.48           C  
ANISOU 1908  C   CYS A 251     5257   5935   6469    709    162   -858       C  
ATOM   1909  O   CYS A 251       3.613   0.272  20.440  1.00 49.80           O  
ANISOU 1909  O   CYS A 251     5582   6429   6910    732     57   -841       O  
ATOM   1910  CB  CYS A 251       2.972   3.077  21.243  1.00 46.16           C  
ANISOU 1910  CB  CYS A 251     5396   5777   6365    909    265   -786       C  
ATOM   1911  SG  CYS A 251       1.211   3.095  20.877  1.00 69.14           S  
ANISOU 1911  SG  CYS A 251     8063   8816   9389   1092    380   -807       S  
ATOM   1912  N   PRO A 252       2.178  -0.185  22.122  1.00 56.03           N  
ANISOU 1912  N   PRO A 252     6411   7167   7710    657    248   -913       N  
ATOM   1913  CA  PRO A 252       1.732  -1.458  21.548  1.00 54.97           C  
ANISOU 1913  CA  PRO A 252     6090   7152   7643    609    191   -959       C  
ATOM   1914  C   PRO A 252       0.956  -1.231  20.257  1.00 48.66           C  
ANISOU 1914  C   PRO A 252     5074   6508   6906    726    130   -960       C  
ATOM   1915  O   PRO A 252      -0.062  -0.545  20.268  1.00 48.14           O  
ANISOU 1915  O   PRO A 252     4892   6490   6908    833    208   -943       O  
ATOM   1916  CB  PRO A 252       0.812  -2.032  22.631  1.00 36.22           C  
ANISOU 1916  CB  PRO A 252     3720   4745   5295    521    341  -1002       C  
ATOM   1917  CG  PRO A 252       0.381  -0.862  23.431  1.00 38.64           C  
ANISOU 1917  CG  PRO A 252     4149   4957   5574    601    519   -983       C  
ATOM   1918  CD  PRO A 252       1.526   0.104  23.409  1.00 45.76           C  
ANISOU 1918  CD  PRO A 252     5257   5757   6374    627    433   -934       C  
ATOM   1919  N   VAL A 253       1.448  -1.786  19.156  1.00 55.79           N  
ANISOU 1919  N   VAL A 253     5944   7472   7782    715     -5   -968       N  
ATOM   1920  CA  VAL A 253       0.773  -1.641  17.875  1.00 44.06           C  
ANISOU 1920  CA  VAL A 253     4318   6119   6304    795   -113   -965       C  
ATOM   1921  C   VAL A 253       0.019  -2.916  17.518  1.00 46.26           C  
ANISOU 1921  C   VAL A 253     4475   6486   6616    668   -193  -1032       C  
ATOM   1922  O   VAL A 253      -0.820  -2.923  16.614  1.00 42.84           O  
ANISOU 1922  O   VAL A 253     3902   6176   6200    685   -321  -1029       O  
ATOM   1923  CB  VAL A 253       1.750  -1.260  16.748  1.00 50.71           C  
ANISOU 1923  CB  VAL A 253     5273   6947   7048    864   -192   -929       C  
ATOM   1924  CG1 VAL A 253       2.329   0.122  17.003  1.00 32.71           C  
ANISOU 1924  CG1 VAL A 253     3097   4583   4747    969   -126   -854       C  
ATOM   1925  CG2 VAL A 253       2.852  -2.295  16.628  1.00 32.18           C  
ANISOU 1925  CG2 VAL A 253     3036   4528   4663    767   -191   -957       C  
ATOM   1926  N   ALA A 254       0.317  -3.998  18.228  1.00 43.37           N  
ANISOU 1926  N   ALA A 254     4179   6047   6253    524   -138  -1084       N  
ATOM   1927  CA  ALA A 254      -0.518  -5.196  18.115  1.00 51.08           C  
ANISOU 1927  CA  ALA A 254     5059   7078   7270    368   -182  -1150       C  
ATOM   1928  C   ALA A 254      -0.527  -5.945  19.436  1.00 47.39           C  
ANISOU 1928  C   ALA A 254     4656   6510   6839    242    -43  -1177       C  
ATOM   1929  O   ALA A 254       0.381  -5.781  20.239  1.00 45.23           O  
ANISOU 1929  O   ALA A 254     4550   6114   6521    262     30  -1148       O  
ATOM   1930  CB  ALA A 254      -0.033  -6.099  16.986  1.00 40.58           C  
ANISOU 1930  CB  ALA A 254     3847   5736   5834    302   -306  -1203       C  
ATOM   1931  N   MET A 255      -1.559  -6.749  19.672  1.00 43.98           N  
ANISOU 1931  N   MET A 255     4098   6125   6487     96    -18  -1220       N  
ATOM   1932  CA  MET A 255      -1.616  -7.542  20.896  1.00 49.97           C  
ANISOU 1932  CA  MET A 255     4957   6770   7259    -41    131  -1242       C  
ATOM   1933  C   MET A 255      -2.662  -8.646  20.872  1.00 55.74           C  
ANISOU 1933  C   MET A 255     5562   7544   8072   -248    137  -1296       C  
ATOM   1934  O   MET A 255      -3.654  -8.575  20.149  1.00 61.87           O  
ANISOU 1934  O   MET A 255     6087   8471   8949   -288     39  -1298       O  
ATOM   1935  CB  MET A 255      -1.834  -6.647  22.120  1.00 53.28           C  
ANISOU 1935  CB  MET A 255     5403   7135   7706     29    327  -1196       C  
ATOM   1936  CG  MET A 255      -3.011  -5.704  22.006  1.00 78.67           C  
ANISOU 1936  CG  MET A 255     8353  10476  11064    134    410  -1160       C  
ATOM   1937  SD  MET A 255      -3.046  -4.505  23.354  1.00125.09           S  
ANISOU 1937  SD  MET A 255    14384  16224  16919    258    686  -1114       S  
ATOM   1938  CE  MET A 255      -4.594  -3.669  23.017  1.00180.97           C  
ANISOU 1938  CE  MET A 255    21069  23455  24238    408    809  -1057       C  
ATOM   1939  N   GLU A 256      -2.416  -9.669  21.682  1.00 56.41           N  
ANISOU 1939  N   GLU A 256     5827   7488   8116   -391    233  -1325       N  
ATOM   1940  CA  GLU A 256      -3.357 -10.752  21.898  1.00 62.03           C  
ANISOU 1940  CA  GLU A 256     6466   8198   8903   -623    285  -1371       C  
ATOM   1941  C   GLU A 256      -3.293 -11.193  23.352  1.00 63.60           C  
ANISOU 1941  C   GLU A 256     6853   8237   9075   -709    507  -1356       C  
ATOM   1942  O   GLU A 256      -2.211 -11.434  23.887  1.00 54.24           O  
ANISOU 1942  O   GLU A 256     5954   6894   7760   -667    510  -1336       O  
ATOM   1943  CB  GLU A 256      -3.033 -11.935  20.992  1.00 63.03           C  
ANISOU 1943  CB  GLU A 256     6731   8270   8948   -757    128  -1443       C  
ATOM   1944  CG  GLU A 256      -3.816 -13.188  21.334  1.00 52.53           C  
ANISOU 1944  CG  GLU A 256     5414   6878   7665  -1035    189  -1495       C  
ATOM   1945  CD  GLU A 256      -3.599 -14.300  20.335  1.00 66.33           C  
ANISOU 1945  CD  GLU A 256     7338   8551   9313  -1180     34  -1579       C  
ATOM   1946  OE1 GLU A 256      -2.959 -14.044  19.292  1.00 81.74           O  
ANISOU 1946  OE1 GLU A 256     9375  10520  11164  -1057   -111  -1598       O  
ATOM   1947  OE2 GLU A 256      -4.071 -15.429  20.594  1.00 65.02           O1-
ANISOU 1947  OE2 GLU A 256     7262   8285   9156  -1425     80  -1628       O1-
ATOM   1948  N   GLU A 257      -4.453 -11.292  23.992  1.00 64.44           N  
ANISOU 1948  N   GLU A 257     6795   8380   9310   -831    692  -1350       N  
ATOM   1949  CA  GLU A 257      -4.520 -11.790  25.360  1.00 57.99           C  
ANISOU 1949  CA  GLU A 257     6198   7394   8441   -944    934  -1338       C  
ATOM   1950  C   GLU A 257      -5.141 -13.178  25.397  1.00 54.82           C  
ANISOU 1950  C   GLU A 257     5801   6939   8089  -1220    975  -1383       C  
ATOM   1951  O   GLU A 257      -6.359 -13.326  25.470  1.00 75.83           O  
ANISOU 1951  O   GLU A 257     8188   9694  10930  -1366   1101  -1381       O  
ATOM   1952  CB  GLU A 257      -5.298 -10.831  26.261  1.00 58.84           C  
ANISOU 1952  CB  GLU A 257     6196   7524   8636   -870   1216  -1290       C  
ATOM   1953  CG  GLU A 257      -4.617  -9.489  26.464  1.00 76.05           C  
ANISOU 1953  CG  GLU A 257     8489   9685  10721   -627   1214  -1251       C  
ATOM   1954  CD  GLU A 257      -5.273  -8.661  27.550  1.00102.76           C  
ANISOU 1954  CD  GLU A 257    11909  13004  14129   -562   1554  -1215       C  
ATOM   1955  OE1 GLU A 257      -4.998  -7.445  27.618  1.00116.05           O  
ANISOU 1955  OE1 GLU A 257    13642  14680  15770   -367   1581  -1187       O  
ATOM   1956  OE2 GLU A 257      -6.058  -9.228  28.339  1.00109.67           O1-
ANISOU 1956  OE2 GLU A 257    12796  13814  15060   -710   1821  -1216       O1-
ATOM   1957  N   ALA A 258      -4.288 -14.193  25.343  1.00 64.78           N  
ANISOU 1957  N   ALA A 258     7367   8038   9207  -1291    875  -1412       N  
ATOM   1958  CA  ALA A 258      -4.733 -15.576  25.411  1.00 73.51           C  
ANISOU 1958  CA  ALA A 258     8572   9036  10322  -1559    917  -1458       C  
ATOM   1959  C   ALA A 258      -5.062 -15.991  26.842  1.00 60.21           C  
ANISOU 1959  C   ALA A 258     7084   7189   8603  -1690   1202  -1420       C  
ATOM   1960  O   ALA A 258      -4.276 -15.760  27.767  1.00 67.59           O  
ANISOU 1960  O   ALA A 258     8319   7978   9385  -1579   1270  -1365       O  
ATOM   1961  CB  ALA A 258      -3.673 -16.494  24.828  1.00 70.72           C  
ANISOU 1961  CB  ALA A 258     8512   8531   9828  -1548    745  -1493       C  
ATOM   1962  N   ASP A 259      -6.223 -16.615  27.017  1.00 72.54           N  
ANISOU 1962  N   ASP A 259     8490   8769  10302  -1946   1358  -1440       N  
ATOM   1963  CA  ASP A 259      -6.597 -17.184  28.307  1.00106.54           C  
ANISOU 1963  CA  ASP A 259    13020  12895  14565  -2112   1663  -1407       C  
ATOM   1964  C   ASP A 259      -5.968 -18.559  28.489  1.00 94.61           C  
ANISOU 1964  C   ASP A 259    11922  11134  12891  -2259   1609  -1426       C  
ATOM   1965  O   ASP A 259      -6.502 -19.411  29.198  1.00107.46           O  
ANISOU 1965  O   ASP A 259    13706  12611  14511  -2495   1819  -1418       O  
ATOM   1966  CB  ASP A 259      -8.119 -17.274  28.449  1.00121.49           C  
ANISOU 1966  CB  ASP A 259    14542  14906  16711  -2336   1897  -1400       C  
ATOM   1967  CG  ASP A 259      -8.736 -15.977  28.933  1.00135.06           C  
ANISOU 1967  CG  ASP A 259    15991  16758  18568  -2163   2133  -1340       C  
ATOM   1968  OD1 ASP A 259      -8.046 -15.218  29.647  1.00137.18           O  
ANISOU 1968  OD1 ASP A 259    16530  16931  18660  -1951   2222  -1310       O  
ATOM   1969  OD2 ASP A 259      -9.913 -15.718  28.607  1.00138.31           O1-
ANISOU 1969  OD2 ASP A 259    15925  17356  19269  -2243   2229  -1314       O1-
ATOM   1970  N   ASP A 260      -4.830 -18.765  27.836  1.00 84.47           N  
ANISOU 1970  N   ASP A 260    10816   9791  11489  -2106   1351  -1440       N  
ATOM   1971  CA  ASP A 260      -4.084 -20.008  27.952  1.00 80.68           C  
ANISOU 1971  CA  ASP A 260    10736   9051  10867  -2169   1299  -1439       C  
ATOM   1972  C   ASP A 260      -3.477 -20.142  29.341  1.00 65.78           C  
ANISOU 1972  C   ASP A 260     9237   6944   8812  -2116   1427  -1338       C  
ATOM   1973  O   ASP A 260      -2.762 -19.259  29.809  1.00 75.75           O  
ANISOU 1973  O   ASP A 260    10564   8226   9992  -1904   1372  -1268       O  
ATOM   1974  CB  ASP A 260      -2.994 -20.075  26.883  1.00 75.23           C  
ANISOU 1974  CB  ASP A 260    10103   8356  10128  -1969   1039  -1461       C  
ATOM   1975  CG  ASP A 260      -3.556 -20.344  25.502  1.00 68.33           C  
ANISOU 1975  CG  ASP A 260     9016   7606   9339  -2091    901  -1571       C  
ATOM   1976  OD1 ASP A 260      -4.442 -21.215  25.384  1.00 81.84           O  
ANISOU 1976  OD1 ASP A 260    10730   9267  11097  -2391    959  -1631       O  
ATOM   1977  OD2 ASP A 260      -3.120 -19.680  24.538  1.00 71.65           O1-
ANISOU 1977  OD2 ASP A 260     9290   8166   9767  -1910    728  -1593       O1-
ATOM   1978  N   THR A 261      -3.768 -21.261  29.989  1.00 59.42           N  
ANISOU 1978  N   THR A 261     8720   5917   7940  -2333   1580  -1325       N  
ATOM   1979  CA  THR A 261      -3.364 -21.486  31.365  1.00 66.27           C  
ANISOU 1979  CA  THR A 261    10004   6555   8620  -2332   1710  -1220       C  
ATOM   1980  C   THR A 261      -2.271 -22.543  31.442  1.00 64.74           C  
ANISOU 1980  C   THR A 261    10211   6093   8294  -2261   1557  -1153       C  
ATOM   1981  O   THR A 261      -2.335 -23.561  30.754  1.00 84.29           O  
ANISOU 1981  O   THR A 261    12745   8467  10813  -2366   1524  -1211       O  
ATOM   1982  CB  THR A 261      -4.575 -21.927  32.219  1.00 78.13           C  
ANISOU 1982  CB  THR A 261    11575   7975  10137  -2630   2060  -1226       C  
ATOM   1984  CG2 THR A 261      -4.140 -22.341  33.615  1.00 87.63           C  
ANISOU 1984  CG2 THR A 261    13315   8890  11091  -2658   2191  -1115       C  
ATOM   1983  OG1 THR A 261      -5.508 -20.843  32.316  1.00 70.10           O  
ANISOU 1983  OG1 THR A 261    10188   7186   9262  -2635   2246  -1251       O  
ATOM   1985  N   VAL A 262      -1.262 -22.291  32.269  1.00 57.44           N  
ANISOU 1985  N   VAL A 262     9570   5042   7213  -2083   1452  -1023       N  
ATOM   1986  CA  VAL A 262      -0.235 -23.288  32.535  1.00 59.30           C  
ANISOU 1986  CA  VAL A 262    10184   5003   7343  -1994   1315   -912       C  
ATOM   1987  C   VAL A 262      -0.320 -23.742  33.987  1.00 74.76           C  
ANISOU 1987  C   VAL A 262    12606   6711   9090  -2123   1448   -799       C  
ATOM   1988  O   VAL A 262       0.050 -23.007  34.903  1.00 92.06           O  
ANISOU 1988  O   VAL A 262    14955   8891  11132  -2052   1399   -703       O  
ATOM   1989  CB  VAL A 262       1.177 -22.751  32.249  1.00 74.39           C  
ANISOU 1989  CB  VAL A 262    12040   6953   9270  -1672   1014   -807       C  
ATOM   1990  CG1 VAL A 262       2.175 -23.897  32.216  1.00 53.75           C  
ANISOU 1990  CG1 VAL A 262     9711   4071   6640  -1544    887   -691       C  
ATOM   1991  CG2 VAL A 262       1.197 -21.990  30.936  1.00 61.50           C  
ANISOU 1991  CG2 VAL A 262     9964   5591   7810  -1546    922   -914       C  
ATOM   1992  N   ALA A 263      -0.819 -24.957  34.183  1.00 88.50           N  
ANISOU 1992  N   ALA A 263    14603   8230  10793  -2334   1617   -812       N  
ATOM   1993  CA  ALA A 263      -0.985 -25.536  35.511  1.00 79.74           C  
ANISOU 1993  CA  ALA A 263    13986   6847   9464  -2487   1779   -706       C  
ATOM   1994  C   ALA A 263       0.367 -25.753  36.189  1.00 72.58           C  
ANISOU 1994  C   ALA A 263    13462   5728   8387  -2264   1503   -503       C  
ATOM   1995  O   ALA A 263       1.400 -25.771  35.521  1.00 80.70           O  
ANISOU 1995  O   ALA A 263    14358   6783   9520  -2008   1227   -447       O  
ATOM   1996  CB  ALA A 263      -1.745 -26.852  35.402  1.00 88.84           C  
ANISOU 1996  CB  ALA A 263    15319   7798  10639  -2764   2002   -763       C  
ATOM   1997  N   PRO A 264       0.370 -25.906  37.524  1.00 70.35           N  
ANISOU 1997  N   PRO A 264    13654   5231   7845  -2362   1576   -378       N  
ATOM   1998  CA  PRO A 264       1.630 -26.214  38.211  1.00 70.78           C  
ANISOU 1998  CA  PRO A 264    14091   5065   7736  -2174   1261   -153       C  
ATOM   1999  C   PRO A 264       2.176 -27.575  37.789  1.00 72.34           C  
ANISOU 1999  C   PRO A 264    14459   5014   8011  -2084   1175    -75       C  
ATOM   2000  O   PRO A 264       1.392 -28.493  37.542  1.00 80.67           O  
ANISOU 2000  O   PRO A 264    15617   5939   9097  -2286   1436   -173       O  
ATOM   2001  CB  PRO A 264       1.223 -26.251  39.688  1.00 87.66           C  
ANISOU 2001  CB  PRO A 264    16773   6991   9542  -2376   1427    -63       C  
ATOM   2002  CG  PRO A 264      -0.019 -25.435  39.765  1.00 68.08           C  
ANISOU 2002  CG  PRO A 264    14083   4705   7078  -2575   1794   -237       C  
ATOM   2003  CD  PRO A 264      -0.734 -25.678  38.474  1.00 73.63           C  
ANISOU 2003  CD  PRO A 264    14269   5604   8103  -2632   1939   -420       C  
ATOM   2004  N   SER A 265       3.500 -27.691  37.712  1.00 74.49           N  
ANISOU 2004  N   SER A 265    14757   5215   8333  -1786    824    107       N  
ATOM   2005  CA  SER A 265       4.167 -28.936  37.325  1.00 79.45           C  
ANISOU 2005  CA  SER A 265    15551   5578   9056  -1624    746    213       C  
ATOM   2006  C   SER A 265       3.705 -29.444  35.963  1.00 82.90           C  
ANISOU 2006  C   SER A 265    15713   6071   9713  -1649    937      7       C  
ATOM   2007  O   SER A 265       3.405 -30.626  35.795  1.00 90.92           O  
ANISOU 2007  O   SER A 265    17003   6823  10717  -1748   1106    -20       O  
ATOM   2008  CB  SER A 265       3.985 -30.016  38.395  1.00 72.27           C  
ANISOU 2008  CB  SER A 265    15266   4287   7907  -1770    844    350       C  
ATOM   2009  OG  SER A 265       4.607 -29.631  39.609  1.00104.59           O  
ANISOU 2009  OG  SER A 265    19677   8291  11770  -1717    590    574       O  
ATOM   2010  N   SER A 266       3.651 -28.537  34.995  1.00 76.74           N  
ANISOU 2010  N   SER A 266    14433   5617   9109  -1573    900   -135       N  
ATOM   2011  CA  SER A 266       3.263 -28.891  33.638  1.00 73.54           C  
ANISOU 2011  CA  SER A 266    13781   5283   8880  -1599   1030   -330       C  
ATOM   2012  C   SER A 266       3.914 -27.946  32.642  1.00 70.20           C  
ANISOU 2012  C   SER A 266    12890   5140   8642  -1345    859   -367       C  
ATOM   2013  O   SER A 266       4.379 -26.867  33.005  1.00 68.40           O  
ANISOU 2013  O   SER A 266    12469   5106   8416  -1225    681   -285       O  
ATOM   2014  CB  SER A 266       1.743 -28.847  33.483  1.00 77.15           C  
ANISOU 2014  CB  SER A 266    14143   5858   9312  -1981   1304   -546       C  
ATOM   2015  OG  SER A 266       1.247 -27.537  33.695  1.00 74.78           O  
ANISOU 2015  OG  SER A 266    13521   5875   9017  -2039   1310   -605       O  
ATOM   2016  N   THR A 267       3.947 -28.360  31.382  1.00 79.42           N  
ANISOU 2016  N   THR A 267    13923   6309   9945  -1282    922   -492       N  
ATOM   2017  CA  THR A 267       4.513 -27.532  30.328  1.00 70.64           C  
ANISOU 2017  CA  THR A 267    12406   5440   8994  -1057    808   -539       C  
ATOM   2018  C   THR A 267       3.420 -27.057  29.383  1.00 63.85           C  
ANISOU 2018  C   THR A 267    11268   4830   8164  -1275    918   -785       C  
ATOM   2019  O   THR A 267       2.326 -27.617  29.349  1.00 60.41           O  
ANISOU 2019  O   THR A 267    10946   4339   7668  -1585   1080   -918       O  
ATOM   2020  CB  THR A 267       5.581 -28.291  29.527  1.00 65.17           C  
ANISOU 2020  CB  THR A 267    11788   4542   8431   -754    794   -466       C  
ATOM   2022  CG2 THR A 267       6.686 -28.781  30.447  1.00 61.91           C  
ANISOU 2022  CG2 THR A 267    11600   3886   8039   -509    653   -183       C  
ATOM   2021  OG1 THR A 267       4.979 -29.413  28.872  1.00 94.27           O  
ANISOU 2021  OG1 THR A 267    15737   8008  12074   -916   1001   -619       O  
ATOM   2023  N   PHE A 268       3.724 -26.017  28.620  1.00 61.27           N  
ANISOU 2023  N   PHE A 268    10567   4773   7938  -1122    814   -828       N  
ATOM   2024  CA  PHE A 268       2.779 -25.461  27.665  1.00 70.70           C  
ANISOU 2024  CA  PHE A 268    11475   6220   9167  -1287    862  -1031       C  
ATOM   2025  C   PHE A 268       3.544 -24.945  26.457  1.00 67.68           C  
ANISOU 2025  C   PHE A 268    10866   5961   8887  -1033    772  -1057       C  
ATOM   2026  O   PHE A 268       4.631 -24.399  26.598  1.00 56.35           O  
ANISOU 2026  O   PHE A 268     9321   4563   7526   -757    657   -913       O  
ATOM   2027  CB  PHE A 268       1.973 -24.334  28.312  1.00 61.12           C  
ANISOU 2027  CB  PHE A 268    10021   5269   7935  -1429    863  -1053       C  
ATOM   2028  CG  PHE A 268       1.014 -23.657  27.377  1.00 59.81           C  
ANISOU 2028  CG  PHE A 268     9507   5380   7839  -1563    879  -1220       C  
ATOM   2029  CD1 PHE A 268       1.302 -22.404  26.856  1.00 54.25           C  
ANISOU 2029  CD1 PHE A 268     8475   4935   7202  -1386    763  -1224       C  
ATOM   2030  CD2 PHE A 268      -0.173 -24.272  27.014  1.00 57.53           C  
ANISOU 2030  CD2 PHE A 268     9215   5086   7556  -1875    990  -1357       C  
ATOM   2031  CE1 PHE A 268       0.420 -21.777  25.993  1.00 65.46           C  
ANISOU 2031  CE1 PHE A 268     9586   6601   8686  -1490    751  -1353       C  
ATOM   2032  CE2 PHE A 268      -1.058 -23.652  26.150  1.00 65.07           C  
ANISOU 2032  CE2 PHE A 268     9824   6305   8595  -1999    951  -1480       C  
ATOM   2033  CZ  PHE A 268      -0.761 -22.404  25.638  1.00 66.61           C  
ANISOU 2033  CZ  PHE A 268     9708   6753   8847  -1790    829  -1475       C  
ATOM   2034  N   CYS A 269       2.985 -25.130  25.269  1.00 62.67           N  
ANISOU 2034  N   CYS A 269    10178   5382   8250  -1146    821  -1232       N  
ATOM   2035  CA  CYS A 269       3.657 -24.688  24.054  1.00 64.37           C  
ANISOU 2035  CA  CYS A 269    10246   5688   8523   -924    776  -1268       C  
ATOM   2036  C   CYS A 269       2.648 -24.264  23.000  1.00 58.84           C  
ANISOU 2036  C   CYS A 269     9371   5200   7786  -1128    747  -1459       C  
ATOM   2037  O   CYS A 269       1.767 -25.038  22.627  1.00 64.76           O  
ANISOU 2037  O   CYS A 269    10281   5861   8462  -1407    794  -1592       O  
ATOM   2038  CB  CYS A 269       4.558 -25.795  23.504  1.00 60.01           C  
ANISOU 2038  CB  CYS A 269    10008   4814   7978   -735    883  -1238       C  
ATOM   2039  SG  CYS A 269       5.533 -25.302  22.067  1.00105.07           S  
ANISOU 2039  SG  CYS A 269    15586  10581  13756   -425    911  -1256       S  
ATOM   2040  N   LYS A 270       2.778 -23.033  22.518  1.00 62.25           N  
ANISOU 2040  N   LYS A 270     9481   5904   8267  -1003    648  -1459       N  
ATOM   2041  CA  LYS A 270       1.836 -22.524  21.530  1.00 47.96           C  
ANISOU 2041  CA  LYS A 270     7485   4312   6425  -1172    575  -1608       C  
ATOM   2042  C   LYS A 270       2.460 -21.463  20.632  1.00 61.63           C  
ANISOU 2042  C   LYS A 270     9013   6221   8181   -935    499  -1595       C  
ATOM   2043  O   LYS A 270       3.348 -20.723  21.051  1.00 64.82           O  
ANISOU 2043  O   LYS A 270     9280   6684   8665   -693    481  -1465       O  
ATOM   2044  CB  LYS A 270       0.594 -21.962  22.226  1.00 59.49           C  
ANISOU 2044  CB  LYS A 270     8691   5983   7929  -1410    544  -1628       C  
ATOM   2045  CG  LYS A 270      -0.596 -21.745  21.305  1.00 60.25           C  
ANISOU 2045  CG  LYS A 270     8597   6271   8024  -1651    447  -1762       C  
ATOM   2046  CD  LYS A 270      -1.746 -21.098  22.050  1.00 67.63           C  
ANISOU 2046  CD  LYS A 270     9211   7419   9067  -1822    460  -1742       C  
ATOM   2047  CE  LYS A 270      -2.935 -20.854  21.141  1.00 85.07           C  
ANISOU 2047  CE  LYS A 270    11158   9838  11328  -2048    324  -1835       C  
ATOM   2048  NZ  LYS A 270      -4.053 -20.197  21.872  1.00 95.58           N1+
ANISOU 2048  NZ  LYS A 270    12121  11375  12822  -2173    381  -1790       N1+
ATOM   2049  N   VAL A 271       1.989 -21.400  19.392  1.00 58.35           N  
ANISOU 2049  N   VAL A 271     8604   5881   7685  -1030    441  -1725       N  
ATOM   2050  CA  VAL A 271       2.430 -20.382  18.451  1.00 51.84           C  
ANISOU 2050  CA  VAL A 271     7621   5223   6852   -841    376  -1723       C  
ATOM   2051  C   VAL A 271       1.353 -19.314  18.311  1.00 48.78           C  
ANISOU 2051  C   VAL A 271     6899   5146   6489   -974    218  -1757       C  
ATOM   2052  O   VAL A 271       0.220 -19.614  17.936  1.00 65.02           O  
ANISOU 2052  O   VAL A 271     8933   7270   8504  -1246    124  -1857       O  
ATOM   2053  CB  VAL A 271       2.712 -20.988  17.059  1.00 61.27           C  
ANISOU 2053  CB  VAL A 271     9120   6262   7897   -831    422  -1834       C  
ATOM   2054  CG1 VAL A 271       3.247 -19.925  16.113  1.00 46.28           C  
ANISOU 2054  CG1 VAL A 271     7096   4513   5973   -625    390  -1815       C  
ATOM   2055  CG2 VAL A 271       3.689 -22.145  17.168  1.00 48.89           C  
ANISOU 2055  CG2 VAL A 271     7903   4348   6323   -685    626  -1800       C  
ATOM   2056  N   TYR A 272       1.707 -18.070  18.619  1.00 53.11           N  
ANISOU 2056  N   TYR A 272     7184   5874   7120   -785    184  -1661       N  
ATOM   2057  CA  TYR A 272       0.777 -16.954  18.474  1.00 47.51           C  
ANISOU 2057  CA  TYR A 272     6159   5439   6452   -844     62  -1671       C  
ATOM   2058  C   TYR A 272       1.140 -16.138  17.242  1.00 54.72           C  
ANISOU 2058  C   TYR A 272     7030   6461   7299   -693    -24  -1682       C  
ATOM   2059  O   TYR A 272       2.307 -15.942  16.960  1.00 65.83           O  
ANISOU 2059  O   TYR A 272     8534   7786   8693   -473     52  -1627       O  
ATOM   2060  CB  TYR A 272       0.818 -16.059  19.713  1.00 53.84           C  
ANISOU 2060  CB  TYR A 272     6756   6338   7365   -753    105  -1563       C  
ATOM   2061  CG  TYR A 272       0.467 -16.774  20.995  1.00 53.67           C  
ANISOU 2061  CG  TYR A 272     6819   6198   7376   -899    210  -1540       C  
ATOM   2062  CD1 TYR A 272       1.461 -17.284  21.821  1.00 51.01           C  
ANISOU 2062  CD1 TYR A 272     6692   5663   7027   -798    283  -1453       C  
ATOM   2063  CD2 TYR A 272      -0.857 -16.938  21.381  1.00 54.56           C  
ANISOU 2063  CD2 TYR A 272     6796   6392   7540  -1138    238  -1586       C  
ATOM   2064  CE1 TYR A 272       1.146 -17.939  22.996  1.00 56.63           C  
ANISOU 2064  CE1 TYR A 272     7538   6247   7732   -936    375  -1422       C  
ATOM   2065  CE2 TYR A 272      -1.183 -17.593  22.555  1.00 66.15           C  
ANISOU 2065  CE2 TYR A 272     8377   7734   9023  -1282    375  -1561       C  
ATOM   2066  CZ  TYR A 272      -0.177 -18.090  23.358  1.00 57.90           C  
ANISOU 2066  CZ  TYR A 272     7603   6479   7920  -1181    440  -1483       C  
ATOM   2067  OH  TYR A 272      -0.492 -18.743  24.524  1.00 57.31           O  
ANISOU 2067  OH  TYR A 272     7693   6258   7823  -1327    571  -1449       O  
ATOM   2068  N   THR A 273       0.147 -15.654  16.508  1.00 55.57           N  
ANISOU 2068  N   THR A 273     6986   6751   7376   -811   -183  -1735       N  
ATOM   2069  CA  THR A 273       0.436 -14.922  15.279  1.00 42.55           C  
ANISOU 2069  CA  THR A 273     5358   5185   5623   -686   -277  -1742       C  
ATOM   2070  C   THR A 273      -0.172 -13.525  15.279  1.00 49.90           C  
ANISOU 2070  C   THR A 273     5954   6368   6637   -612   -396  -1675       C  
ATOM   2071  O   THR A 273      -1.390 -13.368  15.336  1.00 62.58           O  
ANISOU 2071  O   THR A 273     7336   8126   8314   -770   -526  -1684       O  
ATOM   2072  CB  THR A 273      -0.045 -15.695  14.040  1.00 45.02           C  
ANISOU 2072  CB  THR A 273     5923   5433   5748   -882   -402  -1864       C  
ATOM   2074  CG2 THR A 273       0.307 -14.940  12.773  1.00 45.35           C  
ANISOU 2074  CG2 THR A 273     6059   5534   5637   -749   -484  -1864       C  
ATOM   2073  OG1 THR A 273       0.588 -16.978  14.011  1.00 53.84           O  
ANISOU 2073  OG1 THR A 273     7408   6271   6777   -920   -246  -1929       O  
ATOM   2075  N   LEU A 274       0.685 -12.512  15.207  1.00 55.05           N  
ANISOU 2075  N   LEU A 274     6564   7054   7300   -368   -342  -1594       N  
ATOM   2076  CA  LEU A 274       0.225 -11.128  15.279  1.00 53.54           C  
ANISOU 2076  CA  LEU A 274     6102   7058   7183   -264   -420  -1521       C  
ATOM   2077  C   LEU A 274       0.648 -10.330  14.058  1.00 57.22           C  
ANISOU 2077  C   LEU A 274     6643   7571   7526   -122   -495  -1499       C  
ATOM   2078  O   LEU A 274       1.759 -10.483  13.566  1.00 54.86           O  
ANISOU 2078  O   LEU A 274     6560   7145   7140    -11   -388  -1496       O  
ATOM   2079  CB  LEU A 274       0.773 -10.448  16.535  1.00 64.38           C  
ANISOU 2079  CB  LEU A 274     7368   8415   8677   -130   -283  -1430       C  
ATOM   2080  CG  LEU A 274       0.482 -11.101  17.884  1.00 51.06           C  
ANISOU 2080  CG  LEU A 274     5664   6657   7080   -249   -180  -1431       C  
ATOM   2081  CD1 LEU A 274       0.868 -10.154  19.001  1.00 52.48           C  
ANISOU 2081  CD1 LEU A 274     5774   6838   7328   -130    -91  -1341       C  
ATOM   2082  CD2 LEU A 274      -0.983 -11.494  17.991  1.00100.89           C  
ANISOU 2082  CD2 LEU A 274    11809  13067  13458   -455   -231  -1482       C  
ATOM   2083  N   THR A 275      -0.235  -9.465  13.575  1.00 62.35           N  
ANISOU 2083  N   THR A 275     7753   7932   8005  -1263    430  -1335       N  
ATOM   2084  CA  THR A 275       0.110  -8.607  12.452  1.00 37.14           C  
ANISOU 2084  CA  THR A 275     4445   4759   4908  -1124    401  -1319       C  
ATOM   2085  C   THR A 275      -0.148  -7.145  12.784  1.00 47.26           C  
ANISOU 2085  C   THR A 275     5278   6299   6379   -839    298  -1262       C  
ATOM   2086  O   THR A 275      -1.290  -6.741  13.001  1.00 67.41           O  
ANISOU 2086  O   THR A 275     7544   9227   8841   -918    210  -1187       O  
ATOM   2087  CB  THR A 275      -0.667  -8.989  11.181  1.00 44.82           C  
ANISOU 2087  CB  THR A 275     5534   5882   5614  -1522    354  -1291       C  
ATOM   2089  CG2 THR A 275      -0.042  -8.328   9.959  1.00 37.79           C  
ANISOU 2089  CG2 THR A 275     4649   4896   4813  -1372    362  -1293       C  
ATOM   2088  OG1 THR A 275      -0.649 -10.412  11.018  1.00 57.87           O  
ANISOU 2088  OG1 THR A 275     7698   7286   7005  -1859    448  -1342       O  
ATOM   2090  N   PRO A 276       0.924  -6.346  12.840  1.00 53.59           N  
ANISOU 2090  N   PRO A 276     6041   6910   7410   -501    318  -1279       N  
ATOM   2091  CA  PRO A 276       0.808  -4.908  13.089  1.00 39.59           C  
ANISOU 2091  CA  PRO A 276     3979   5285   5778   -233    233  -1235       C  
ATOM   2092  C   PRO A 276       0.284  -4.186  11.855  1.00 52.49           C  
ANISOU 2092  C   PRO A 276     5483   7111   7350   -263    163  -1179       C  
ATOM   2093  O   PRO A 276       0.863  -4.316  10.777  1.00 56.78           O  
ANISOU 2093  O   PRO A 276     6173   7512   7890   -326    188  -1198       O  
ATOM   2094  CB  PRO A 276       2.256  -4.479  13.364  1.00 37.05           C  
ANISOU 2094  CB  PRO A 276     3745   4676   5658     14    270  -1258       C  
ATOM   2095  CG  PRO A 276       3.016  -5.752  13.614  1.00 41.42           C  
ANISOU 2095  CG  PRO A 276     4552   4994   6193    -52    385  -1292       C  
ATOM   2096  CD  PRO A 276       2.325  -6.789  12.797  1.00 32.39           C  
ANISOU 2096  CD  PRO A 276     3602   3872   4830   -353    430  -1317       C  
ATOM   2097  N   PHE A 277      -0.805  -3.444  12.010  1.00 50.21           N  
ANISOU 2097  N   PHE A 277     4922   7160   6996   -190     89  -1094       N  
ATOM   2098  CA  PHE A 277      -1.324  -2.618  10.927  1.00 50.26           C  
ANISOU 2098  CA  PHE A 277     4775   7378   6941   -148     17  -1008       C  
ATOM   2099  C   PHE A 277      -1.916  -1.327  11.483  1.00 45.58           C  
ANISOU 2099  C   PHE A 277     3958   6985   6376    208    -16   -919       C  
ATOM   2100  O   PHE A 277      -2.090  -1.195  12.693  1.00 51.85           O  
ANISOU 2100  O   PHE A 277     4708   7792   7201    366     20   -925       O  
ATOM   2101  CB  PHE A 277      -2.333  -3.388  10.065  1.00 37.46           C  
ANISOU 2101  CB  PHE A 277     3085   6073   5074   -532    -33   -935       C  
ATOM   2102  CG  PHE A 277      -3.547  -3.868  10.813  1.00 46.45           C  
ANISOU 2102  CG  PHE A 277     4003   7609   6036   -699    -59   -842       C  
ATOM   2103  CD1 PHE A 277      -3.522  -5.064  11.514  1.00 47.76           C  
ANISOU 2103  CD1 PHE A 277     4348   7672   6126   -968     -9   -909       C  
ATOM   2104  CD2 PHE A 277      -4.726  -3.139  10.788  1.00 51.23           C  
ANISOU 2104  CD2 PHE A 277     4222   8720   6524   -581   -124   -663       C  
ATOM   2105  CE1 PHE A 277      -4.640  -5.512  12.190  1.00 44.95           C  
ANISOU 2105  CE1 PHE A 277     3783   7713   5585  -1169    -38   -811       C  
ATOM   2106  CE2 PHE A 277      -5.847  -3.584  11.462  1.00 58.49           C  
ANISOU 2106  CE2 PHE A 277     4883  10085   7258   -740   -139   -541       C  
ATOM   2107  CZ  PHE A 277      -5.803  -4.773  12.163  1.00 43.04           C  
ANISOU 2107  CZ  PHE A 277     3101   8023   5228  -1065   -104   -621       C  
ATOM   2108  N   LEU A 278      -2.216  -0.376  10.603  1.00 45.69           N  
ANISOU 2108  N   LEU A 278     3876   7129   6357    355    -68   -834       N  
ATOM   2109  CA  LEU A 278      -2.597   0.965  11.044  1.00 44.69           C  
ANISOU 2109  CA  LEU A 278     3661   7084   6237    775    -67   -751       C  
ATOM   2110  C   LEU A 278      -4.077   1.123  11.379  1.00 50.12           C  
ANISOU 2110  C   LEU A 278     4015   8287   6740    905    -62   -576       C  
ATOM   2111  O   LEU A 278      -4.435   1.930  12.234  1.00 51.13           O  
ANISOU 2111  O   LEU A 278     4111   8464   6851   1283     -2   -521       O  
ATOM   2112  CB  LEU A 278      -2.188   2.012  10.004  1.00 41.56           C  
ANISOU 2112  CB  LEU A 278     3365   6555   5870    932   -112   -723       C  
ATOM   2113  CG  LEU A 278      -2.311   3.459  10.490  1.00 45.54           C  
ANISOU 2113  CG  LEU A 278     3957   6981   6366   1385    -89   -664       C  
ATOM   2114  CD1 LEU A 278      -1.405   3.689  11.691  1.00 39.39           C  
ANISOU 2114  CD1 LEU A 278     3437   5826   5705   1476    -45   -784       C  
ATOM   2115  CD2 LEU A 278      -2.006   4.455   9.387  1.00 51.66           C  
ANISOU 2115  CD2 LEU A 278     4863   7637   7128   1507   -139   -622       C  
ATOM   2116  N   ALA A 279      -4.929   0.352  10.707  1.00 50.56           N  
ANISOU 2116  N   ALA A 279     3838   8748   6625    583   -118   -471       N  
ATOM   2117  CA  ALA A 279      -6.381   0.522  10.810  1.00 53.95           C  
ANISOU 2117  CA  ALA A 279     3858   9805   6837    673   -131   -238       C  
ATOM   2118  C   ALA A 279      -6.910   0.481  12.244  1.00 48.98           C  
ANISOU 2118  C   ALA A 279     3095   9341   6175    870    -39   -200       C  
ATOM   2119  O   ALA A 279      -7.864   1.180  12.582  1.00 69.87           O  
ANISOU 2119  O   ALA A 279     5470  12386   8691   1229     12     -5       O  
ATOM   2120  CB  ALA A 279      -7.100  -0.508   9.946  1.00 46.40           C  
ANISOU 2120  CB  ALA A 279     2708   9257   5665    138   -233   -134       C  
ATOM   2121  N   ASN A 280      -6.287  -0.338  13.082  1.00 51.76           N  
ANISOU 2121  N   ASN A 280     3655   9384   6629    663     -3   -372       N  
ATOM   2122  CA  ASN A 280      -6.697  -0.446  14.480  1.00 67.70           C  
ANISOU 2122  CA  ASN A 280     5590  11513   8621    813     85   -358       C  
ATOM   2123  C   ASN A 280      -5.777   0.315  15.439  1.00 51.69           C  
ANISOU 2123  C   ASN A 280     3877   8984   6778   1182    164   -503       C  
ATOM   2124  O   ASN A 280      -5.688  -0.012  16.622  1.00 53.31           O  
ANISOU 2124  O   ASN A 280     4152   9095   7009   1198    226   -567       O  
ATOM   2125  CB  ASN A 280      -6.865  -1.916  14.897  1.00 43.80           C  
ANISOU 2125  CB  ASN A 280     2558   8573   5512    306     67   -408       C  
ATOM   2126  CG  ASN A 280      -5.559  -2.697  14.880  1.00 40.88           C  
ANISOU 2126  CG  ASN A 280     2604   7617   5310     57     63   -637       C  
ATOM   2128  ND2 ASN A 280      -4.514  -2.114  14.302  1.00 40.58           N  
ANISOU 2128  ND2 ASN A 280     2794   7176   5449    218     53   -736       N  
ATOM   2127  OD1 ASN A 280      -5.494  -3.815  15.392  1.00 60.93           O  
ANISOU 2127  OD1 ASN A 280     5262  10089   7802   -265     77   -703       O  
ATOM   2129  N   ASN A 281      -5.103   1.333  14.909  1.00 46.99           N  
ANISOU 2129  N   ASN A 281     3493   8079   6282   1435    151   -542       N  
ATOM   2130  CA  ASN A 281      -4.193   2.167  15.688  1.00 39.48           C  
ANISOU 2130  CA  ASN A 281     2892   6655   5453   1713    197   -658       C  
ATOM   2131  C   ASN A 281      -4.338   3.648  15.356  1.00 51.49           C  
ANISOU 2131  C   ASN A 281     4545   8108   6911   2160    228   -575       C  
ATOM   2132  O   ASN A 281      -3.437   4.439  15.636  1.00 63.61           O  
ANISOU 2132  O   ASN A 281     6455   9198   8517   2296    230   -670       O  
ATOM   2133  CB  ASN A 281      -2.742   1.745  15.454  1.00 36.60           C  
ANISOU 2133  CB  ASN A 281     2803   5824   5278   1437    135   -830       C  
ATOM   2134  CG  ASN A 281      -2.360   0.501  16.230  1.00 48.55           C  
ANISOU 2134  CG  ASN A 281     4343   7249   6854   1146    148   -928       C  
ATOM   2136  ND2 ASN A 281      -1.728  -0.446  15.548  1.00 40.07           N  
ANISOU 2136  ND2 ASN A 281     3328   6053   5844    823    113   -994       N  
ATOM   2135  OD1 ASN A 281      -2.628   0.391  17.427  1.00 60.75           O  
ANISOU 2135  OD1 ASN A 281     5891   8820   8372   1233    203   -937       O  
ATOM   2137  N   ARG A 282      -5.466   4.021  14.757  1.00 47.63           N  
ANISOU 2137  N   ARG A 282     3768   8070   6257   2374    249   -377       N  
ATOM   2138  CA  ARG A 282      -5.660   5.393  14.293  1.00 45.45           C  
ANISOU 2138  CA  ARG A 282     3708   7669   5891   2742    280   -263       C  
ATOM   2139  C   ARG A 282      -5.914   6.384  15.430  1.00 59.34           C  
ANISOU 2139  C   ARG A 282     5800   9206   7542   3104    412   -223       C  
ATOM   2140  O   ARG A 282      -5.727   7.589  15.264  1.00 58.34           O  
ANISOU 2140  O   ARG A 282     6028   8798   7339   3383    446   -195       O  
ATOM   2141  CB  ARG A 282      -6.794   5.463  13.264  1.00 51.82           C  
ANISOU 2141  CB  ARG A 282     4177   8976   6534   2761    248    -28       C  
ATOM   2142  CG  ARG A 282      -6.676   4.445  12.140  1.00 59.11           C  
ANISOU 2142  CG  ARG A 282     4788  10166   7504   2332    112    -48       C  
ATOM   2143  CD  ARG A 282      -7.159   5.018  10.819  1.00 70.40           C  
ANISOU 2143  CD  ARG A 282     6103  11826   8822   2409     46    125       C  
ATOM   2144  NE  ARG A 282      -6.122   5.793  10.144  1.00 77.09           N  
ANISOU 2144  NE  ARG A 282     7262  12242   9786   2548      7      6       N  
ATOM   2145  CZ  ARG A 282      -5.603   5.481   8.959  1.00 66.50           C  
ANISOU 2145  CZ  ARG A 282     5956  10804   8505   2202   -106    -50       C  
ATOM   2146  NH1 ARG A 282      -6.030   4.411   8.301  1.00 52.84           N1+
ANISOU 2146  NH1 ARG A 282     3941   9423   6712   1762   -190     -3       N1+
ATOM   2147  NH2 ARG A 282      -4.661   6.246   8.426  1.00 68.58           N  
ANISOU 2147  NH2 ARG A 282     6576  10621   8859   2271   -132   -145       N  
ATOM   2148  N   GLU A 283      -6.333   5.874  16.583  1.00 50.01           N  
ANISOU 2148  N   GLU A 283     4535   8143   6324   3083    486   -222       N  
ATOM   2149  CA  GLU A 283      -6.640   6.725  17.730  1.00 61.58           C  
ANISOU 2149  CA  GLU A 283     6311   9433   7655   3410    621   -185       C  
ATOM   2150  C   GLU A 283      -5.380   7.102  18.510  1.00 67.59           C  
ANISOU 2150  C   GLU A 283     7560   9605   8517   3378    617   -392       C  
ATOM   2151  O   GLU A 283      -5.419   7.959  19.392  1.00 59.04           O  
ANISOU 2151  O   GLU A 283     6856   8275   7300   3612    713   -386       O  
ATOM   2152  CB  GLU A 283      -7.630   6.021  18.664  1.00 51.57           C  
ANISOU 2152  CB  GLU A 283     4748   8561   6285   3397    702    -88       C  
ATOM   2153  CG  GLU A 283      -6.991   5.034  19.645  1.00 65.09           C  
ANISOU 2153  CG  GLU A 283     6465  10127   8139   3128    690   -270       C  
ATOM   2154  CD  GLU A 283      -6.475   3.758  18.986  1.00 85.91           C  
ANISOU 2154  CD  GLU A 283     8818  12883  10940   2694    563   -377       C  
ATOM   2155  OE1 GLU A 283      -6.639   3.590  17.755  1.00 65.95           O  
ANISOU 2155  OE1 GLU A 283     6077  10565   8415   2563    478   -312       O  
ATOM   2156  OE2 GLU A 283      -5.906   2.915  19.711  1.00 77.12           O1-
ANISOU 2156  OE2 GLU A 283     7716  11655   9930   2480    551   -530       O1-
ATOM   2157  N   LYS A 284      -4.267   6.456  18.184  1.00 50.00           N  
ANISOU 2157  N   LYS A 284     5335   7172   6490   3074    502   -564       N  
ATOM   2158  CA  LYS A 284      -3.027   6.658  18.922  1.00 47.94           C  
ANISOU 2158  CA  LYS A 284     5485   6418   6312   2971    466   -743       C  
ATOM   2159  C   LYS A 284      -2.192   7.806  18.364  1.00 45.30           C  
ANISOU 2159  C   LYS A 284     5595   5671   5946   3029    409   -778       C  
ATOM   2160  O   LYS A 284      -1.238   7.587  17.620  1.00 43.76           O  
ANISOU 2160  O   LYS A 284     5412   5324   5890   2798    284   -870       O  
ATOM   2161  CB  LYS A 284      -2.215   5.360  18.953  1.00 39.54           C  
ANISOU 2161  CB  LYS A 284     4222   5346   5455   2567    361   -887       C  
ATOM   2162  CG  LYS A 284      -2.955   4.223  19.636  1.00 39.56           C  
ANISOU 2162  CG  LYS A 284     3882   5695   5455   2459    414   -868       C  
ATOM   2163  CD  LYS A 284      -2.148   2.941  19.675  1.00 38.01           C  
ANISOU 2163  CD  LYS A 284     3598   5414   5431   1996    323   -975       C  
ATOM   2164  CE  LYS A 284      -2.868   1.893  20.505  1.00 43.03           C  
ANISOU 2164  CE  LYS A 284     3998   6330   6022   1880    380   -961       C  
ATOM   2165  NZ  LYS A 284      -2.079   0.643  20.644  1.00 53.99           N1+
ANISOU 2165  NZ  LYS A 284     5391   7580   7544   1482    315  -1060       N1+
ATOM   2166  N   ARG A 285      -2.552   9.030  18.738  1.00 45.69           N  
ANISOU 2166  N   ARG A 285     6032   5542   5787   3298    498   -695       N  
ATOM   2167  CA  ARG A 285      -1.833  10.209  18.270  1.00 53.36           C  
ANISOU 2167  CA  ARG A 285     7501   6109   6664   3330    449   -714       C  
ATOM   2168  C   ARG A 285      -0.370  10.176  18.713  1.00 54.69           C  
ANISOU 2168  C   ARG A 285     8015   5853   6912   3003    328   -880       C  
ATOM   2169  O   ARG A 285      -0.062   9.791  19.839  1.00 65.01           O  
ANISOU 2169  O   ARG A 285     9407   7062   8231   2882    335   -954       O  
ATOM   2170  CB  ARG A 285      -2.511  11.490  18.767  1.00 50.56           C  
ANISOU 2170  CB  ARG A 285     7568   5631   6013   3673    582   -597       C  
ATOM   2171  CG  ARG A 285      -1.942  12.758  18.152  1.00 83.56           C  
ANISOU 2171  CG  ARG A 285    12282   9431  10035   3712    543   -586       C  
ATOM   2172  CD  ARG A 285      -1.447  13.724  19.213  1.00 84.62           C  
ANISOU 2172  CD  ARG A 285    13100   9123   9929   3692    579   -624       C  
ATOM   2173  NE  ARG A 285      -2.518  14.558  19.746  1.00 78.81           N  
ANISOU 2173  NE  ARG A 285    12606   8443   8895   4118    764   -480       N  
ATOM   2174  CZ  ARG A 285      -2.829  15.760  19.272  1.00104.22           C  
ANISOU 2174  CZ  ARG A 285    16238  11517  11843   4389    836   -369       C  
ATOM   2175  NH1 ARG A 285      -2.148  16.266  18.253  1.00105.32           N1+
ANISOU 2175  NH1 ARG A 285    16588  11443  11985   4244    725   -394       N1+
ATOM   2176  NH2 ARG A 285      -3.820  16.457  19.814  1.00124.71           N  
ANISOU 2176  NH2 ARG A 285    19059  14183  14143   4818   1027   -223       N  
ATOM   2177  N   GLY A 286       0.526  10.574  17.817  1.00 53.27           N  
ANISOU 2177  N   GLY A 286     8029   5443   6770   2844    206   -923       N  
ATOM   2178  CA  GLY A 286       1.944  10.611  18.121  1.00 42.47           C  
ANISOU 2178  CA  GLY A 286     6941   3747   5447   2425     59  -1019       C  
ATOM   2179  C   GLY A 286       2.682   9.368  17.661  1.00 44.46           C  
ANISOU 2179  C   GLY A 286     6695   4223   5976   2014    -55  -1049       C  
ATOM   2180  O   GLY A 286       3.912   9.330  17.664  1.00 48.79           O  
ANISOU 2180  O   GLY A 286     7336   4623   6578   1636   -181  -1068       O  
ATOM   2181  N   LEU A 287       1.925   8.348  17.269  1.00 38.06           N  
ANISOU 2181  N   LEU A 287     5373   3784   5305   2087     -1  -1033       N  
ATOM   2182  CA  LEU A 287       2.496   7.095  16.793  1.00 35.53           C  
ANISOU 2182  CA  LEU A 287     4652   3645   5204   1756    -66  -1060       C  
ATOM   2183  C   LEU A 287       3.376   7.335  15.565  1.00 57.27           C  
ANISOU 2183  C   LEU A 287     7420   6321   8019   1546   -161  -1042       C  
ATOM   2184  O   LEU A 287       3.039   8.134  14.691  1.00 48.49           O  
ANISOU 2184  O   LEU A 287     6423   5181   6821   1694   -162   -997       O  
ATOM   2185  CB  LEU A 287       1.378   6.104  16.466  1.00 38.76           C  
ANISOU 2185  CB  LEU A 287     4620   4439   5667   1849      9  -1035       C  
ATOM   2186  CG  LEU A 287       1.754   4.684  16.037  1.00 55.69           C  
ANISOU 2186  CG  LEU A 287     6439   6743   7977   1539    -20  -1069       C  
ATOM   2187  CD1 LEU A 287       2.497   3.959  17.149  1.00 35.26           C  
ANISOU 2187  CD1 LEU A 287     3883   4044   5471   1360    -29  -1126       C  
ATOM   2188  CD2 LEU A 287       0.507   3.911  15.618  1.00 41.75           C  
ANISOU 2188  CD2 LEU A 287     4331   5354   6177   1580     36  -1023       C  
ATOM   2189  N   ALA A 288       4.510   6.647  15.512  1.00 45.55           N  
ANISOU 2189  N   ALA A 288     5818   4821   6668   1226   -228  -1057       N  
ATOM   2190  CA  ALA A 288       5.478   6.855  14.443  1.00 47.66           C  
ANISOU 2190  CA  ALA A 288     6086   5042   6980   1017   -303  -1021       C  
ATOM   2191  C   ALA A 288       5.058   6.176  13.147  1.00 48.65           C  
ANISOU 2191  C   ALA A 288     5915   5377   7194   1029   -262  -1016       C  
ATOM   2192  O   ALA A 288       4.764   4.982  13.121  1.00 49.76           O  
ANISOU 2192  O   ALA A 288     5787   5693   7427    989   -204  -1042       O  
ATOM   2193  CB  ALA A 288       6.860   6.378  14.874  1.00 43.17           C  
ANISOU 2193  CB  ALA A 288     5463   4448   6490    718   -368   -992       C  
ATOM   2194  N   LEU A 289       5.042   6.956  12.072  1.00 47.07           N  
ANISOU 2194  N   LEU A 289     5817   5133   6933   1058   -295   -980       N  
ATOM   2195  CA  LEU A 289       4.690   6.473  10.744  1.00 52.96           C  
ANISOU 2195  CA  LEU A 289     6342   6056   7725   1037   -273   -965       C  
ATOM   2196  C   LEU A 289       5.792   6.872   9.780  1.00 43.91           C  
ANISOU 2196  C   LEU A 289     5281   4810   6594    840   -330   -932       C  
ATOM   2197  O   LEU A 289       6.529   7.822  10.039  1.00 45.79           O  
ANISOU 2197  O   LEU A 289     5784   4857   6756    756   -402   -901       O  
ATOM   2198  CB  LEU A 289       3.375   7.100  10.284  1.00 49.57           C  
ANISOU 2198  CB  LEU A 289     5920   5740   7175   1313   -254   -920       C  
ATOM   2199  CG  LEU A 289       2.167   6.963  11.207  1.00 43.77           C  
ANISOU 2199  CG  LEU A 289     5090   5167   6373   1569   -185   -905       C  
ATOM   2200  CD1 LEU A 289       1.042   7.851  10.722  1.00 42.73           C  
ANISOU 2200  CD1 LEU A 289     4989   5163   6083   1909   -160   -803       C  
ATOM   2201  CD2 LEU A 289       1.718   5.517  11.271  1.00 53.84           C  
ANISOU 2201  CD2 LEU A 289     6015   6712   7729   1421   -145   -930       C  
ATOM   2202  N   ASP A 290       5.911   6.153   8.670  1.00 40.17           N  
ANISOU 2202  N   ASP A 290     4614   4466   6183    737   -297   -930       N  
ATOM   2203  CA  ASP A 290       6.879   6.531   7.648  1.00 37.29           C  
ANISOU 2203  CA  ASP A 290     4308   4044   5816    573   -330   -885       C  
ATOM   2204  C   ASP A 290       6.514   7.891   7.070  1.00 43.30           C  
ANISOU 2204  C   ASP A 290     5317   4691   6444    664   -402   -847       C  
ATOM   2205  O   ASP A 290       5.335   8.233   6.974  1.00 46.15           O  
ANISOU 2205  O   ASP A 290     5701   5103   6729    895   -394   -842       O  
ATOM   2206  CB  ASP A 290       6.984   5.466   6.557  1.00 34.17           C  
ANISOU 2206  CB  ASP A 290     3715   3786   5480    480   -250   -896       C  
ATOM   2207  CG  ASP A 290       7.956   4.354   6.924  1.00 53.10           C  
ANISOU 2207  CG  ASP A 290     5984   6216   7974    379   -163   -893       C  
ATOM   2208  OD1 ASP A 290       8.775   4.564   7.844  1.00 45.96           O  
ANISOU 2208  OD1 ASP A 290     5097   5268   7097    333   -196   -850       O  
ATOM   2209  OD2 ASP A 290       7.910   3.277   6.293  1.00 50.23           O1-
ANISOU 2209  OD2 ASP A 290     5535   5921   7629    348    -58   -918       O1-
ATOM   2210  N   GLY A 291       7.535   8.663   6.708  1.00 40.61           N  
ANISOU 2210  N   GLY A 291     5162   4218   6050    485   -469   -797       N  
ATOM   2211  CA  GLY A 291       7.365  10.051   6.313  1.00 35.42           C  
ANISOU 2211  CA  GLY A 291     4858   3374   5227    538   -544   -758       C  
ATOM   2212  C   GLY A 291       6.346  10.278   5.217  1.00 44.44           C  
ANISOU 2212  C   GLY A 291     5972   4594   6319    737   -527   -741       C  
ATOM   2213  O   GLY A 291       6.270   9.508   4.260  1.00 42.05           O  
ANISOU 2213  O   GLY A 291     5411   4471   6093    664   -492   -745       O  
ATOM   2214  N   LYS A 292       5.556  11.337   5.366  1.00 47.91           N  
ANISOU 2214  N   LYS A 292     6706   4899   6600   1002   -545   -707       N  
ATOM   2215  CA  LYS A 292       4.525  11.675   4.394  1.00 49.16           C  
ANISOU 2215  CA  LYS A 292     6831   5170   6676   1243   -537   -646       C  
ATOM   2216  C   LYS A 292       4.981  12.795   3.472  1.00 60.26           C  
ANISOU 2216  C   LYS A 292     8586   6368   7942   1177   -606   -591       C  
ATOM   2217  O   LYS A 292       5.690  13.709   3.894  1.00 63.73           O  
ANISOU 2217  O   LYS A 292     9448   6508   8260   1068   -655   -587       O  
ATOM   2218  CB  LYS A 292       3.242  12.110   5.102  1.00 50.37           C  
ANISOU 2218  CB  LYS A 292     7058   5367   6714   1682   -479   -598       C  
ATOM   2219  CG  LYS A 292       2.634  11.065   6.014  1.00 53.21           C  
ANISOU 2219  CG  LYS A 292     7074   5966   7177   1755   -411   -636       C  
ATOM   2220  CD  LYS A 292       1.309  11.546   6.586  1.00 47.11           C  
ANISOU 2220  CD  LYS A 292     6325   5314   6260   2225   -335   -547       C  
ATOM   2221  CE  LYS A 292       0.689  10.483   7.473  1.00 47.52           C  
ANISOU 2221  CE  LYS A 292     6014   5644   6398   2253   -271   -571       C  
ATOM   2222  NZ  LYS A 292       0.678   9.162   6.782  1.00 52.03           N1+
ANISOU 2222  NZ  LYS A 292     6157   6505   7107   1934   -301   -599       N1+
ATOM   2223  N   LEU A 293       4.565  12.722   2.213  1.00 50.27           N  
ANISOU 2223  N   LEU A 293     7175   5259   6666   1203   -619   -541       N  
ATOM   2224  CA  LEU A 293       4.776  13.818   1.278  1.00 54.98           C  
ANISOU 2224  CA  LEU A 293     8110   5672   7106   1196   -680   -474       C  
ATOM   2225  C   LEU A 293       3.818  14.950   1.623  1.00 50.83           C  
ANISOU 2225  C   LEU A 293     7952   4992   6368   1644   -660   -391       C  
ATOM   2226  O   LEU A 293       4.225  16.100   1.778  1.00 65.56           O  
ANISOU 2226  O   LEU A 293    10363   6498   8047   1659   -691   -370       O  
ATOM   2227  CB  LEU A 293       4.553  13.359  -0.166  1.00 53.46           C  
ANISOU 2227  CB  LEU A 293     7651   5710   6951   1101   -697   -437       C  
ATOM   2228  CG  LEU A 293       5.634  12.501  -0.833  1.00 65.66           C  
ANISOU 2228  CG  LEU A 293     8985   7332   8632    693   -689   -495       C  
ATOM   2229  CD1 LEU A 293       5.579  11.063  -0.346  1.00101.43           C  
ANISOU 2229  CD1 LEU A 293    13132  12076  13332    619   -611   -569       C  
ATOM   2230  CD2 LEU A 293       5.476  12.546  -2.342  1.00 91.68           C  
ANISOU 2230  CD2 LEU A 293    12234  10729  11870    614   -716   -445       C  
ATOM   2231  N   LYS A 294       2.539  14.610   1.743  1.00 66.87           N  
ANISOU 2231  N   LYS A 294     9702   7310   8396   2010   -600   -325       N  
ATOM   2232  CA  LYS A 294       1.521  15.563   2.165  1.00 71.45           C  
ANISOU 2232  CA  LYS A 294    10560   7823   8765   2547   -534   -210       C  
ATOM   2233  C   LYS A 294       0.620  15.233   3.346  1.00 66.92           C  
ANISOU 2233  C   LYS A 294     9815   7425   8188   2895   -426   -188       C  
ATOM   2234  O   LYS A 294       0.844  15.711   4.458  1.00 85.39           O  
ANISOU 2234  O   LYS A 294    12530   9470  10446   3009   -369   -240       O  
ATOM   2235  CB  LYS A 294       0.564  15.878   1.016  1.00 57.82           C  
ANISOU 2235  CB  LYS A 294     8692   6352   6925   2831   -547    -43       C  
ATOM   2236  CG  LYS A 294       1.178  16.721  -0.079  1.00 59.45           C  
ANISOU 2236  CG  LYS A 294     9270   6298   7023   2685   -627    -16       C  
ATOM   2237  CD  LYS A 294       0.163  17.047  -1.155  1.00 77.50           C  
ANISOU 2237  CD  LYS A 294    11411   8859   9178   3004   -644    174       C  
ATOM   2238  CE  LYS A 294       0.675  18.138  -2.080  1.00 76.73           C  
ANISOU 2238  CE  LYS A 294    11821   8422   8912   2962   -706    218       C  
ATOM   2239  NZ  LYS A 294       1.990  17.780  -2.674  1.00 82.30           N1+
ANISOU 2239  NZ  LYS A 294    12538   8981   9753   2341   -796     77       N1+
ATOM   2240  N   HIS A 295      -0.401  14.418   3.103  1.00 68.71           N  
ANISOU 2240  N   HIS A 295     9490   8146   8473   3028   -403   -101       N  
ATOM   2241  CA  HIS A 295      -1.282  13.970   4.178  1.00 68.16           C  
ANISOU 2241  CA  HIS A 295     9167   8333   8399   3307   -302    -62       C  
ATOM   2242  C   HIS A 295      -1.759  12.576   3.788  1.00 69.22           C  
ANISOU 2242  C   HIS A 295     8653   8972   8677   3036   -344    -51       C  
ATOM   2243  O   HIS A 295      -2.675  12.033   4.404  1.00 71.20           O  
ANISOU 2243  O   HIS A 295     8560   9584   8907   3201   -284     24       O  
ATOM   2244  CB  HIS A 295      -2.471  14.852   4.561  1.00 55.66           C  
ANISOU 2244  CB  HIS A 295     7710   6865   6575   3982   -178    133       C  
ATOM   2245  CG  HIS A 295      -2.083  16.101   5.286  1.00 71.88           C  
ANISOU 2245  CG  HIS A 295    10508   8363   8440   4272    -93    100       C  
ATOM   2247  CD2 HIS A 295      -1.530  16.287   6.508  1.00 63.46           C  
ANISOU 2247  CD2 HIS A 295     9808   6947   7356   4164    -37    -34       C  
ATOM   2246  ND1 HIS A 295      -2.241  17.358   4.742  1.00 77.91           N  
ANISOU 2246  ND1 HIS A 295    11740   8902   8962   4514    -58    210       N  
ATOM   2248  CE1 HIS A 295      -1.808  18.265   5.600  1.00 81.87           C  
ANISOU 2248  CE1 HIS A 295    12875   8947   9284   4510     19    139       C  
ATOM   2249  NE2 HIS A 295      -1.373  17.641   6.680  1.00 82.05           N  
ANISOU 2249  NE2 HIS A 295    12840   8897   9438   4290     25     -2       N  
ATOM   2250  N   GLU A 296      -1.131  12.000   2.768  1.00 56.81           N  
ANISOU 2250  N   GLU A 296     6955   7416   7216   2601   -439   -119       N  
ATOM   2251  CA  GLU A 296      -1.487  10.659   2.325  1.00 44.78           C  
ANISOU 2251  CA  GLU A 296     4949   6285   5778   2279   -476   -124       C  
ATOM   2252  C   GLU A 296      -1.115   9.635   3.388  1.00 65.77           C  
ANISOU 2252  C   GLU A 296     7489   8912   8587   2061   -428   -269       C  
ATOM   2253  O   GLU A 296      -0.188   9.848   4.173  1.00 57.72           O  
ANISOU 2253  O   GLU A 296     6744   7532   7656   2013   -399   -394       O  
ATOM   2254  CB  GLU A 296      -0.794  10.317   1.002  1.00 43.52           C  
ANISOU 2254  CB  GLU A 296     4795   6068   5672   1886   -556   -178       C  
ATOM   2255  CG  GLU A 296       0.676   9.916   1.129  1.00 42.99           C  
ANISOU 2255  CG  GLU A 296     4918   5643   5773   1531   -546   -367       C  
ATOM   2256  CD  GLU A 296       1.595  11.090   1.428  1.00 65.65           C  
ANISOU 2256  CD  GLU A 296     8234   8087   8624   1614   -553   -403       C  
ATOM   2257  OE1 GLU A 296       2.809  10.858   1.599  1.00 49.86           O  
ANISOU 2257  OE1 GLU A 296     6347   5863   6733   1330   -552   -511       O  
ATOM   2258  OE2 GLU A 296       1.111  12.242   1.488  1.00 62.84           O1-
ANISOU 2258  OE2 GLU A 296     8133   7631   8113   1957   -555   -305       O1-
ATOM   2259  N   ASP A 297      -1.847   8.527   3.411  1.00 48.73           N  
ANISOU 2259  N   ASP A 297     4939   7147   6429   1901   -429   -235       N  
ATOM   2260  CA  ASP A 297      -1.593   7.461   4.367  1.00 43.39           C  
ANISOU 2260  CA  ASP A 297     4157   6459   5870   1689   -382   -358       C  
ATOM   2261  C   ASP A 297      -0.213   6.841   4.191  1.00 38.13           C  
ANISOU 2261  C   ASP A 297     3660   5460   5367   1328   -381   -535       C  
ATOM   2262  O   ASP A 297       0.244   6.627   3.070  1.00 58.01           O  
ANISOU 2262  O   ASP A 297     6211   7938   7893   1099   -417   -555       O  
ATOM   2263  CB  ASP A 297      -2.664   6.377   4.255  1.00 47.45           C  
ANISOU 2263  CB  ASP A 297     4268   7464   6297   1510   -398   -271       C  
ATOM   2264  CG  ASP A 297      -3.729   6.500   5.323  1.00 66.94           C  
ANISOU 2264  CG  ASP A 297     6519  10242   8671   1819   -339   -151       C  
ATOM   2265  OD1 ASP A 297      -3.426   7.048   6.404  1.00 76.32           O  
ANISOU 2265  OD1 ASP A 297     7914  11173   9912   2091   -261   -211       O  
ATOM   2266  OD2 ASP A 297      -4.865   6.044   5.085  1.00 65.74           O1-
ANISOU 2266  OD2 ASP A 297     5995  10616   8369   1768   -371     17       O1-
ATOM   2267  N   THR A 298       0.450   6.568   5.310  1.00 51.99           N  
ANISOU 2267  N   THR A 298     5516   7001   7235   1302   -330   -643       N  
ATOM   2268  CA  THR A 298       1.709   5.832   5.300  1.00 42.22           C  
ANISOU 2268  CA  THR A 298     4365   5539   6139   1009   -307   -767       C  
ATOM   2269  C   THR A 298       1.705   4.803   6.422  1.00 45.31           C  
ANISOU 2269  C   THR A 298     4653   5962   6601    930   -248   -836       C  
ATOM   2270  O   THR A 298       1.022   4.973   7.431  1.00 69.62           O  
ANISOU 2270  O   THR A 298     7676   9132   9645   1118   -229   -812       O  
ATOM   2271  CB  THR A 298       2.929   6.756   5.463  1.00 49.16           C  
ANISOU 2271  CB  THR A 298     5532   6077   7070   1022   -329   -800       C  
ATOM   2273  CG2 THR A 298       3.067   7.698   4.266  1.00 35.09           C  
ANISOU 2273  CG2 THR A 298     3896   4229   5209   1041   -387   -739       C  
ATOM   2272  OG1 THR A 298       2.797   7.521   6.667  1.00 54.62           O  
ANISOU 2272  OG1 THR A 298     6391   6637   7726   1244   -326   -795       O  
ATOM   2274  N   ASN A 299       2.469   3.734   6.238  1.00 45.91           N  
ANISOU 2274  N   ASN A 299     4730   5958   6756    681   -201   -912       N  
ATOM   2275  CA  ASN A 299       2.493   2.632   7.189  1.00 42.58           C  
ANISOU 2275  CA  ASN A 299     4248   5548   6382    592   -137   -972       C  
ATOM   2276  C   ASN A 299       3.125   3.000   8.527  1.00 47.74           C  
ANISOU 2276  C   ASN A 299     4989   6023   7126    716   -128  -1003       C  
ATOM   2277  O   ASN A 299       3.658   4.099   8.695  1.00 44.01           O  
ANISOU 2277  O   ASN A 299     4665   5392   6666    825   -174   -983       O  
ATOM   2278  CB  ASN A 299       3.232   1.439   6.581  1.00 44.57           C  
ANISOU 2278  CB  ASN A 299     4563   5711   6660    355    -59  -1029       C  
ATOM   2279  CG  ASN A 299       4.561   1.834   5.964  1.00 49.04           C  
ANISOU 2279  CG  ASN A 299     5249   6082   7303    346    -38  -1027       C  
ATOM   2281  ND2 ASN A 299       5.591   1.947   6.794  1.00 46.26           N  
ANISOU 2281  ND2 ASN A 299     4933   5591   7053    399    -16  -1028       N  
ATOM   2280  OD1 ASN A 299       4.656   2.042   4.755  1.00 50.10           O  
ANISOU 2280  OD1 ASN A 299     5425   6225   7386    273    -46  -1007       O  
ATOM   2282  N   LEU A 300       3.045   2.074   9.479  1.00 41.05           N  
ANISOU 2282  N   LEU A 300     4088   5198   6311    666    -77  -1046       N  
ATOM   2283  CA  LEU A 300       3.763   2.203  10.739  1.00 41.09           C  
ANISOU 2283  CA  LEU A 300     4175   5042   6397    726    -71  -1071       C  
ATOM   2284  C   LEU A 300       5.240   2.386  10.417  1.00 46.18           C  
ANISOU 2284  C   LEU A 300     4915   5508   7121    640    -78  -1057       C  
ATOM   2285  O   LEU A 300       5.778   1.681   9.563  1.00 31.89           O  
ANISOU 2285  O   LEU A 300     3083   3699   5336    529    -20  -1056       O  
ATOM   2286  CB  LEU A 300       3.562   0.947  11.584  1.00 40.15           C  
ANISOU 2286  CB  LEU A 300     3989   4971   6294    643     -6  -1114       C  
ATOM   2287  CG  LEU A 300       2.117   0.600  11.950  1.00 38.84           C  
ANISOU 2287  CG  LEU A 300     3684   5052   6022    659      4  -1104       C  
ATOM   2288  CD1 LEU A 300       2.014  -0.835  12.431  1.00 46.98           C  
ANISOU 2288  CD1 LEU A 300     4705   6108   7036    475     68  -1148       C  
ATOM   2289  CD2 LEU A 300       1.594   1.551  13.013  1.00 32.76           C  
ANISOU 2289  CD2 LEU A 300     2917   4310   5222    901    -14  -1078       C  
ATOM   2290  N   ALA A 301       5.886   3.341  11.081  1.00 33.71           N  
ANISOU 2290  N   ALA A 301     3462   3797   5550    678   -144  -1030       N  
ATOM   2291  CA  ALA A 301       7.266   3.703  10.752  1.00 37.40           C  
ANISOU 2291  CA  ALA A 301     3984   4176   6050    552   -178   -970       C  
ATOM   2292  C   ALA A 301       8.194   2.500  10.724  1.00 42.07           C  
ANISOU 2292  C   ALA A 301     4441   4820   6725    471    -89   -940       C  
ATOM   2293  O   ALA A 301       8.152   1.650  11.611  1.00 46.85           O  
ANISOU 2293  O   ALA A 301     4995   5440   7367    498    -40   -960       O  
ATOM   2294  CB  ALA A 301       7.796   4.749  11.719  1.00 30.19           C  
ANISOU 2294  CB  ALA A 301     3257   3130   5083    519   -277   -933       C  
ATOM   2295  N   SER A 302       9.023   2.436   9.690  1.00 43.30           N  
ANISOU 2295  N   SER A 302     4558   5004   6889    403    -52   -881       N  
ATOM   2296  CA  SER A 302      10.002   1.370   9.561  1.00 40.72           C  
ANISOU 2296  CA  SER A 302     4126   4737   6608    405     71   -816       C  
ATOM   2297  C   SER A 302      11.095   1.515  10.612  1.00 36.48           C  
ANISOU 2297  C   SER A 302     3505   4257   6097    368     23   -697       C  
ATOM   2298  O   SER A 302      11.382   2.623  11.070  1.00 56.05           O  
ANISOU 2298  O   SER A 302     6043   6718   8534    252   -121   -651       O  
ATOM   2299  CB  SER A 302      10.624   1.381   8.163  1.00 47.55           C  
ANISOU 2299  CB  SER A 302     4974   5645   7449    372    141   -760       C  
ATOM   2300  OG  SER A 302       9.650   1.123   7.168  1.00 59.14           O  
ANISOU 2300  OG  SER A 302     6526   7075   8868    369    182   -857       O  
ATOM   2301  N   SER A 303      11.698   0.391  10.989  1.00 32.43           N  
ANISOU 2301  N   SER A 303     2891   3810   5621    458    143   -634       N  
ATOM   2302  CA  SER A 303      12.829   0.394  11.910  1.00 38.33           C  
ANISOU 2302  CA  SER A 303     3496   4691   6376    431    103   -470       C  
ATOM   2303  C   SER A 303      13.958   1.269  11.380  1.00 36.18           C  
ANISOU 2303  C   SER A 303     3107   4585   6054    282     28   -298       C  
ATOM   2304  O   SER A 303      14.240   1.272  10.185  1.00 45.40           O  
ANISOU 2304  O   SER A 303     4242   5801   7206    302    111   -267       O  
ATOM   2305  CB  SER A 303      13.355  -1.028  12.118  1.00 31.93           C  
ANISOU 2305  CB  SER A 303     2598   3945   5588    627    287   -392       C  
ATOM   2306  OG  SER A 303      12.318  -1.918  12.492  1.00 46.83           O  
ANISOU 2306  OG  SER A 303     4640   5669   7486    712    362   -548       O  
ATOM   2307  N   THR A 304      14.595   2.016  12.273  1.00 55.73           N  
ANISOU 2307  N   THR A 304     5541   7158   8478     92   -134   -179       N  
ATOM   2308  CA  THR A 304      15.764   2.804  11.915  1.00 35.48           C  
ANISOU 2308  CA  THR A 304     2846   4814   5821   -134   -228     28       C  
ATOM   2309  C   THR A 304      17.020   1.943  11.977  1.00 47.55           C  
ANISOU 2309  C   THR A 304     4026   6691   7351    -30   -115    284       C  
ATOM   2310  O   THR A 304      17.277   1.281  12.980  1.00 39.89           O  
ANISOU 2310  O   THR A 304     2943   5812   6401     63    -99    363       O  
ATOM   2311  CB  THR A 304      15.951   3.993  12.869  1.00 63.57           C  
ANISOU 2311  CB  THR A 304     6562   8337   9255   -459   -468     73       C  
ATOM   2313  CG2 THR A 304      17.106   4.878  12.404  1.00 38.79           C  
ANISOU 2313  CG2 THR A 304     3331   5436   5971   -790   -590    294       C  
ATOM   2312  OG1 THR A 304      14.745   4.763  12.918  1.00 49.86           O  
ANISOU 2312  OG1 THR A 304     5187   6265   7493   -459   -534   -148       O  
ATOM   2314  N   LEU A 305      17.799   1.949  10.903  1.00 42.17           N  
ANISOU 2314  N   LEU A 305     3169   6223   6632    -13    -22    433       N  
ATOM   2315  CA  LEU A 305      19.064   1.226  10.890  1.00 41.08           C  
ANISOU 2315  CA  LEU A 305     2663   6487   6459    138    110    732       C  
ATOM   2316  C   LEU A 305      20.209   2.170  11.229  1.00 70.36           C  
ANISOU 2316  C   LEU A 305     6122  10586  10023   -235    -91   1023       C  
ATOM   2317  O   LEU A 305      20.451   3.142  10.515  1.00 66.08           O  
ANISOU 2317  O   LEU A 305     5619  10097   9390   -517   -194   1058       O  
ATOM   2318  CB  LEU A 305      19.302   0.577   9.528  1.00 50.16           C  
ANISOU 2318  CB  LEU A 305     3756   7686   7615    414    371    760       C  
ATOM   2319  CG  LEU A 305      18.261  -0.449   9.077  1.00 47.27           C  
ANISOU 2319  CG  LEU A 305     3677   6956   7328    720    577    504       C  
ATOM   2320  CD1 LEU A 305      18.627  -1.013   7.717  1.00 41.02           C  
ANISOU 2320  CD1 LEU A 305     2890   6210   6487    951    836    553       C  
ATOM   2321  CD2 LEU A 305      18.119  -1.563  10.100  1.00 39.74           C  
ANISOU 2321  CD2 LEU A 305     2745   5941   6414    968    676    501       C  
ATOM   2322  N   LEU A 306      20.907   1.887  12.325  1.00 58.63           N  
ANISOU 2322  N   LEU A 306     4398   9388   8491   -274   -161   1244       N  
ATOM   2323  CA  LEU A 306      22.030   2.718  12.746  1.00 66.12           C  
ANISOU 2323  CA  LEU A 306     5087  10779   9256   -701   -379   1563       C  
ATOM   2324  C   LEU A 306      23.364   2.099  12.343  1.00 77.81           C  
ANISOU 2324  C   LEU A 306     6028  12871  10665   -514   -223   1969       C  
ATOM   2325  O   LEU A 306      23.415   0.968  11.859  1.00 77.36           O  
ANISOU 2325  O   LEU A 306     5911  12797  10684      5     76   1966       O  
ATOM   2326  CB  LEU A 306      22.001   2.959  14.258  1.00 68.94           C  
ANISOU 2326  CB  LEU A 306     5515  11127   9550   -951   -599   1594       C  
ATOM   2327  CG  LEU A 306      20.866   3.815  14.827  1.00 67.34           C  
ANISOU 2327  CG  LEU A 306     5845  10399   9340  -1193   -778   1266       C  
ATOM   2328  CD1 LEU A 306      20.589   5.003  13.922  1.00 56.95           C  
ANISOU 2328  CD1 LEU A 306     4822   8881   7935  -1475   -874   1149       C  
ATOM   2329  CD2 LEU A 306      19.601   2.997  15.030  1.00 71.98           C  
ANISOU 2329  CD2 LEU A 306     6665  10559  10125   -781   -615    945       C  
ATOM   2330  N   ARG A 307      24.441   2.850  12.550  1.00 98.12           N  
ANISOU 2330  N   ARG A 307     8472  15814  12996   -907   -403   2235       N  
ATOM   2331  CA  ARG A 307      25.779   2.395  12.187  1.00112.59           C  
ANISOU 2331  CA  ARG A 307    10008  18118  14653   -723   -264   2569       C  
ATOM   2332  C   ARG A 307      26.646   2.131  13.415  1.00129.72           C  
ANISOU 2332  C   ARG A 307    12010  20625  16654   -788   -368   2847       C  
ATOM   2333  O   ARG A 307      26.512   2.808  14.436  1.00135.76           O  
ANISOU 2333  O   ARG A 307    12899  21347  17337  -1214   -632   2838       O  
ATOM   2334  CB  ARG A 307      26.461   3.423  11.283  1.00 61.69           C  
ANISOU 2334  CB  ARG A 307     3505  11920   8013  -1105   -366   2720       C  
ATOM   2335  N   GLU A 308      27.531   1.142  13.300  1.00132.01           N  
ANISOU 2335  N   GLU A 308    12052  21238  16868   -362   -152   3104       N  
ATOM   2336  CA  GLU A 308      28.505   0.818  14.344  1.00116.52           C  
ANISOU 2336  CA  GLU A 308     9871  19691  14712   -380   -221   3442       C  
ATOM   2337  C   GLU A 308      27.866   0.599  15.715  1.00116.08           C  
ANISOU 2337  C   GLU A 308     9955  19398  14751   -444   -347   3306       C  
ATOM   2338  O   GLU A 308      28.069   1.391  16.637  1.00104.04           O  
ANISOU 2338  O   GLU A 308     8463  17992  13076   -943   -627   3398       O  
ATOM   2339  CB  GLU A 308      29.583   1.903  14.431  1.00 87.37           C  
ANISOU 2339  CB  GLU A 308     6008  16491  10698   -938   -464   3774       C  
TER   
END



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