CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 20052517281968454

Job options:

ID        	=	 20052517281968454
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   HIS A   7      64.963  63.045  42.182  1.00 49.03           N  
ANISOU    1  N   HIS A   7     5681   6478   6469   -570   -676   -126       N  
ATOM      2  CA  HIS A   7      65.462  62.358  40.999  1.00 43.80           C  
ANISOU    2  CA  HIS A   7     5025   5818   5801   -561   -634    -19       C  
ATOM      3  C   HIS A   7      65.669  60.880  41.295  1.00 38.58           C  
ANISOU    3  C   HIS A   7     4357   5241   5059   -507   -579     26       C  
ATOM      4  O   HIS A   7      66.768  60.454  41.653  1.00 50.64           O  
ANISOU    4  O   HIS A   7     5841   6846   6556   -510   -577     66       O  
ATOM      5  CB  HIS A   7      66.796  62.952  40.548  1.00 35.23           C  
ANISOU    5  CB  HIS A   7     3894   4745   4747   -616   -664     37       C  
ATOM      6  CG  HIS A   7      66.964  64.393  40.904  1.00 28.43           C  
ANISOU    6  CG  HIS A   7     3013   3827   3964   -676   -738    -20       C  
ATOM      7  CD2 HIS A   7      67.996  65.051  41.478  1.00 32.21           C  
ANISOU    7  CD2 HIS A   7     3444   4336   4457   -721   -782    -35       C  
ATOM      8  ND1 HIS A   7      65.994  65.340  40.657  1.00 35.02           N  
ANISOU    8  ND1 HIS A   7     3875   4550   4881   -691   -775    -73       N  
ATOM      9  CE1 HIS A   7      66.419  66.520  41.072  1.00 34.41           C  
ANISOU    9  CE1 HIS A   7     3782   4435   4857   -718   -810   -125       C  
ATOM     10  NE2 HIS A   7      67.633  66.372  41.571  1.00 41.84           N  
ANISOU   10  NE2 HIS A   7     4678   5460   5759   -740   -817   -106       N  
ATOM     11  N   HIS A   8      64.608  60.097  41.154  1.00 21.19           N  
ANISOU   11  N   HIS A   8     2197   3021   2834   -459   -540     22       N  
ATOM     12  CA  HIS A   8      64.719  58.662  41.343  1.00 21.07           C  
ANISOU   12  CA  HIS A   8     2175   3065   2766   -408   -495     72       C  
ATOM     13  C   HIS A   8      64.746  57.892  40.033  1.00 16.36           C  
ANISOU   13  C   HIS A   8     1591   2438   2185   -380   -447    130       C  
ATOM     14  O   HIS A   8      64.913  56.666  40.070  1.00 18.93           O  
ANISOU   14  O   HIS A   8     1904   2797   2490   -334   -413    169       O  
ATOM     15  CB  HIS A   8      63.553  58.127  42.194  1.00 31.95           C  
ANISOU   15  CB  HIS A   8     3578   4460   4103   -373   -487     33       C  
ATOM     16  CG  HIS A   8      63.501  58.689  43.580  1.00 33.12           C  
ANISOU   16  CG  HIS A   8     3698   4673   4214   -397   -528    -35       C  
ATOM     17  CD2 HIS A   8      62.710  58.376  44.634  1.00 27.90           C  
ANISOU   17  CD2 HIS A   8     3032   4072   3495   -383   -532    -75       C  
ATOM     18  ND1 HIS A   8      64.329  59.702  44.011  1.00 32.80           N  
ANISOU   18  ND1 HIS A   8     3620   4654   4191   -445   -572    -73       N  
ATOM     19  CE1 HIS A   8      64.051  59.990  45.270  1.00 30.70           C  
ANISOU   19  CE1 HIS A   8     3326   4461   3879   -458   -600   -146       C  
ATOM     20  NE2 HIS A   8      63.070  59.202  45.670  1.00 41.08           N  
ANISOU   20  NE2 HIS A   8     4657   5808   5142   -422   -575   -147       N  
ATOM     21  N   HIS A   9      64.577  58.555  38.884  1.00 14.79           N  
ANISOU   21  N   HIS A   9     1411   2182   2026   -408   -446    138       N  
ATOM     22  CA  HIS A   9      64.423  57.806  37.649  1.00 12.58           C  
ANISOU   22  CA  HIS A   9     1139   1892   1748   -383   -396    177       C  
ATOM     23  C   HIS A   9      65.712  57.074  37.300  1.00 12.85           C  
ANISOU   23  C   HIS A   9     1116   1995   1770   -371   -372    225       C  
ATOM     24  O   HIS A   9      66.801  57.420  37.750  1.00 14.09           O  
ANISOU   24  O   HIS A   9     1228   2199   1925   -397   -399    242       O  
ATOM     25  CB  HIS A   9      64.018  58.712  36.488  1.00 14.81           C  
ANISOU   25  CB  HIS A   9     1439   2121   2066   -427   -405    188       C  
ATOM     26  CG  HIS A   9      62.741  59.459  36.710  1.00 15.95           C  
ANISOU   26  CG  HIS A   9     1634   2187   2239   -436   -431    140       C  
ATOM     27  CD2 HIS A   9      61.842  59.420  37.724  1.00 16.71           C  
ANISOU   27  CD2 HIS A   9     1762   2263   2324   -408   -441     79       C  
ATOM     28  ND1 HIS A   9      62.273  60.397  35.814  1.00 19.05           N  
ANISOU   28  ND1 HIS A   9     2040   2519   2680   -479   -454    155       N  
ATOM     29  CE1 HIS A   9      61.132  60.896  36.262  1.00 20.10           C  
ANISOU   29  CE1 HIS A   9     2212   2584   2840   -471   -477    100       C  
ATOM     30  NE2 HIS A   9      60.853  60.324  37.419  1.00 19.22           N  
ANISOU   30  NE2 HIS A   9     2112   2502   2689   -428   -467     47       N  
ATOM     31  N   HIS A  10      65.557  56.032  36.483  1.00 12.61           N  
ANISOU   31  N   HIS A  10     1084   1970   1737   -329   -322    239       N  
ATOM     32  CA  HIS A  10      66.688  55.203  36.101  1.00 12.93           C  
ANISOU   32  CA  HIS A  10     1063   2074   1777   -304   -295    268       C  
ATOM     33  C   HIS A  10      66.547  54.779  34.647  1.00 12.85           C  
ANISOU   33  C   HIS A  10     1042   2073   1769   -295   -248    266       C  
ATOM     34  O   HIS A  10      65.480  54.875  34.052  1.00 12.53           O  
ANISOU   34  O   HIS A  10     1046   1987   1727   -298   -232    249       O  
ATOM     35  CB  HIS A  10      66.787  53.967  37.001  1.00 13.90           C  
ANISOU   35  CB  HIS A  10     1170   2207   1903   -242   -285    274       C  
ATOM     36  CG  HIS A  10      65.629  53.034  36.868  1.00 13.99           C  
ANISOU   36  CG  HIS A  10     1224   2167   1926   -192   -255    257       C  
ATOM     37  CD2 HIS A  10      64.525  52.865  37.634  1.00 14.90           C  
ANISOU   37  CD2 HIS A  10     1388   2244   2031   -177   -266    245       C  
ATOM     38  ND1 HIS A  10      65.504  52.147  35.822  1.00 14.57           N  
ANISOU   38  ND1 HIS A  10     1286   2230   2022   -154   -210    245       N  
ATOM     39  CE1 HIS A  10      64.388  51.455  35.960  1.00 16.12           C  
ANISOU   39  CE1 HIS A  10     1525   2372   2228   -118   -196    231       C  
ATOM     40  NE2 HIS A  10      63.773  51.873  37.052  1.00 15.02           N  
ANISOU   40  NE2 HIS A  10     1424   2219   2066   -132   -229    237       N  
ATOM     41  N   HIS A  11      67.650  54.304  34.080  1.00 13.30           N  
ANISOU   41  N   HIS A  11     1030   2199   1824   -286   -225    278       N  
ATOM     42  CA  HIS A  11      67.619  53.894  32.682  1.00 13.55           C  
ANISOU   42  CA  HIS A  11     1032   2268   1847   -282   -179    263       C  
ATOM     43  C   HIS A  11      66.796  52.627  32.497  1.00 13.09           C  
ANISOU   43  C   HIS A  11      996   2168   1810   -211   -137    220       C  
ATOM     44  O   HIS A  11      66.613  51.813  33.419  1.00 13.39           O  
ANISOU   44  O   HIS A  11     1047   2163   1878   -157   -143    217       O  
ATOM     45  CB  HIS A  11      69.022  53.700  32.109  1.00 14.06           C  
ANISOU   45  CB  HIS A  11     1006   2435   1902   -289   -163    273       C  
ATOM     46  CG  HIS A  11      69.818  52.603  32.743  1.00 14.38           C  
ANISOU   46  CG  HIS A  11      998   2492   1974   -222   -154    262       C  
ATOM     47  CD2 HIS A  11      69.656  51.887  33.887  1.00 14.25           C  
ANISOU   47  CD2 HIS A  11     1000   2422   1993   -169   -169    266       C  
ATOM     48  ND1 HIS A  11      70.981  52.151  32.169  1.00 15.03           N  
ANISOU   48  ND1 HIS A  11      989   2663   2057   -207   -131    251       N  
ATOM     49  CE1 HIS A  11      71.524  51.220  32.938  1.00 15.29           C  
ANISOU   49  CE1 HIS A  11      988   2683   2136   -145   -134    250       C  
ATOM     50  NE2 HIS A  11      70.723  51.022  33.974  1.00 14.83           N  
ANISOU   50  NE2 HIS A  11      995   2540   2100   -123   -159    265       N  
ATOM     51  N   GLU A  12      66.263  52.465  31.294  1.00 14.69           N  
ANISOU   51  N   GLU A  12     1198   2386   1997   -217    -99    193       N  
ATOM     52  CA  GLU A  12      65.448  51.306  30.955  1.00 15.88           C  
ANISOU   52  CA  GLU A  12     1365   2497   2171   -156    -59    145       C  
ATOM     53  C   GLU A  12      66.313  50.434  30.053  1.00 16.34           C  
ANISOU   53  C   GLU A  12     1335   2633   2240   -124    -17     99       C  
ATOM     54  O   GLU A  12      66.168  50.423  28.832  1.00 30.36           O  
ANISOU   54  O   GLU A  12     3081   4471   3984   -144     19     65       O  
ATOM     55  CB  GLU A  12      64.128  51.725  30.315  1.00 19.08           C  
ANISOU   55  CB  GLU A  12     1832   2866   2551   -185    -48    136       C  
ATOM     56  CG  GLU A  12      63.149  52.377  31.302  1.00 25.79           C  
ANISOU   56  CG  GLU A  12     2765   3630   3404   -198    -88    160       C  
ATOM     57  CD  GLU A  12      62.854  51.514  32.521  1.00 43.16           C  
ANISOU   57  CD  GLU A  12     4989   5774   5635   -139    -98    155       C  
ATOM     58  OE1 GLU A  12      63.021  50.278  32.438  1.00 45.89           O  
ANISOU   58  OE1 GLU A  12     5305   6114   6016    -82    -73    133       O  
ATOM     59  OE2 GLU A  12      62.463  52.076  33.567  1.00 49.73           O1-
ANISOU   59  OE2 GLU A  12     5863   6571   6461   -152   -136    172       O1-
ATOM     60  N   ASN A  13      67.246  49.714  30.673  1.00 24.33           N  
ANISOU   60  N   ASN A  13     2296   3652   3298    -75    -24     96       N  
ATOM     61  CA  ASN A  13      68.209  48.881  29.950  1.00 25.80           C  
ANISOU   61  CA  ASN A  13     2384   3911   3509    -36     11     42       C  
ATOM     62  C   ASN A  13      67.609  47.498  29.671  1.00 35.17           C  
ANISOU   62  C   ASN A  13     3562   5037   4764     41     42    -30       C  
ATOM     63  O   ASN A  13      68.141  46.454  30.052  1.00 31.19           O  
ANISOU   63  O   ASN A  13     3008   4502   4342    110     40    -54       O  
ATOM     64  CB  ASN A  13      69.540  48.815  30.700  1.00 18.82           C  
ANISOU   64  CB  ASN A  13     1439   3061   2650    -21    -15     75       C  
ATOM     65  CG  ASN A  13      69.396  48.320  32.127  1.00 31.67           C  
ANISOU   65  CG  ASN A  13     3101   4598   4336     21    -54    119       C  
ATOM     66  ND2 ASN A  13      70.485  47.778  32.675  1.00 23.90           N  
ANISOU   66  ND2 ASN A  13     2048   3635   3400     59    -70    135       N  
ATOM     67  OD1 ASN A  13      68.333  48.431  32.737  1.00 42.87           O  
ANISOU   67  OD1 ASN A  13     4599   5939   5751     17    -72    142       O  
ATOM     68  N   LEU A  14      66.461  47.530  28.987  1.00 28.78           N  
ANISOU   68  N   LEU A  14     2803   4206   3928     27     67    -61       N  
ATOM     69  CA  LEU A  14      65.752  46.347  28.501  1.00 37.24           C  
ANISOU   69  CA  LEU A  14     3868   5226   5055     86     99   -139       C  
ATOM     70  C   LEU A  14      65.572  46.490  26.991  1.00 46.02           C  
ANISOU   70  C   LEU A  14     4941   6440   6106     53    149   -210       C  
ATOM     71  O   LEU A  14      66.246  47.322  26.372  1.00 38.32           O  
ANISOU   71  O   LEU A  14     3919   5583   5057     -6    157   -193       O  
ATOM     72  CB  LEU A  14      64.417  46.198  29.229  1.00 26.22           C  
ANISOU   72  CB  LEU A  14     2572   3711   3679     96     78   -104       C  
ATOM     73  CG  LEU A  14      63.604  47.476  29.462  1.00 39.01           C  
ANISOU   73  CG  LEU A  14     4279   5323   5221     26     58    -42       C  
ATOM     74  CD1 LEU A  14      63.101  48.043  28.138  1.00 44.24           C  
ANISOU   74  CD1 LEU A  14     4942   6051   5815    -25     93    -72       C  
ATOM     75  CD2 LEU A  14      62.443  47.234  30.427  1.00 29.01           C  
ANISOU   75  CD2 LEU A  14     3095   3949   3978     46     33    -10       C  
ATOM     76  N   TYR A  15      64.681  45.701  26.379  1.00 19.64           N  
ANISOU   76  N   TYR A  15     1608   3065   2789     84    181   -283       N  
ATOM     77  CA  TYR A  15      64.534  45.759  24.926  1.00 17.17           C  
ANISOU   77  CA  TYR A  15     1243   2871   2410     51    230   -359       C  
ATOM     78  C   TYR A  15      63.083  45.764  24.455  1.00 19.05           C  
ANISOU   78  C   TYR A  15     1550   3068   2618     31    247   -372       C  
ATOM     79  O   TYR A  15      62.674  46.661  23.716  1.00 19.31           O  
ANISOU   79  O   TYR A  15     1597   3182   2559    -43    258   -341       O  
ATOM     80  CB  TYR A  15      65.305  44.606  24.257  1.00 18.15           C  
ANISOU   80  CB  TYR A  15     1250   3053   2592    114    268   -488       C  
ATOM     81  CG  TYR A  15      65.200  44.594  22.747  1.00 17.09           C  
ANISOU   81  CG  TYR A  15     1043   3070   2379     79    323   -583       C  
ATOM     82  CD1 TYR A  15      65.882  45.529  21.977  1.00 19.92           C  
ANISOU   82  CD1 TYR A  15     1339   3605   2624      1    337   -557       C  
ATOM     83  CD2 TYR A  15      64.431  43.641  22.087  1.00 19.09           C  
ANISOU   83  CD2 TYR A  15     1282   3303   2669    117    358   -697       C  
ATOM     84  CE1 TYR A  15      65.788  45.526  20.592  1.00 21.38           C  
ANISOU   84  CE1 TYR A  15     1503   3904   2718    -41    366   -613       C  
ATOM     85  CE2 TYR A  15      64.337  43.626  20.702  1.00 19.47           C  
ANISOU   85  CE2 TYR A  15     1306   3468   2623     74    389   -762       C  
ATOM     86  CZ  TYR A  15      65.013  44.573  19.965  1.00 21.14           C  
ANISOU   86  CZ  TYR A  15     1485   3836   2711     -4    392   -717       C  
ATOM     87  OH  TYR A  15      64.924  44.566  18.589  1.00 26.07           O  
ANISOU   87  OH  TYR A  15     2088   4581   3237    -50    411   -772       O  
ATOM     88  N   PHE A  16      62.293  44.771  24.848  1.00 17.40           N  
ANISOU   88  N   PHE A  16     1382   2739   2491     92    246   -409       N  
ATOM     89  CA  PHE A  16      60.921  44.682  24.368  1.00 17.71           C  
ANISOU   89  CA  PHE A  16     1481   2744   2504     76    264   -428       C  
ATOM     90  C   PHE A  16      60.017  45.656  25.119  1.00 15.70           C  
ANISOU   90  C   PHE A  16     1337   2419   2208     31    228   -318       C  
ATOM     91  O   PHE A  16      60.288  46.020  26.268  1.00 18.10           O  
ANISOU   91  O   PHE A  16     1680   2663   2536     37    185   -243       O  
ATOM     92  CB  PHE A  16      60.396  43.262  24.548  1.00 18.48           C  
ANISOU   92  CB  PHE A  16     1578   2732   2711    153    270   -504       C  
ATOM     93  CG  PHE A  16      61.151  42.246  23.754  1.00 20.71           C  
ANISOU   93  CG  PHE A  16     1746   3070   3054    204    305   -639       C  
ATOM     94  CD1 PHE A  16      60.924  42.105  22.396  1.00 23.38           C  
ANISOU   94  CD1 PHE A  16     2026   3524   3334    181    357   -746       C  
ATOM     95  CD2 PHE A  16      62.096  41.439  24.360  1.00 22.97           C  
ANISOU   95  CD2 PHE A  16     1972   3301   3456    274    283   -664       C  
ATOM     96  CE1 PHE A  16      61.626  41.171  21.659  1.00 29.68           C  
ANISOU   96  CE1 PHE A  16     2731   4369   4176    223    379   -874       C  
ATOM     97  CE2 PHE A  16      62.796  40.504  23.628  1.00 24.74           C  
ANISOU   97  CE2 PHE A  16     2081   3571   3749    327    313   -803       C  
ATOM     98  CZ  PHE A  16      62.557  40.373  22.277  1.00 25.88           C  
ANISOU   98  CZ  PHE A  16     2207   3813   3812    293    352   -896       C  
ATOM     99  N   GLN A  17      58.934  46.074  24.457  1.00 15.88           N  
ANISOU   99  N   GLN A  17     1404   2458   2170    -13    244   -314       N  
ATOM    100  CA  GLN A  17      57.940  46.942  25.080  1.00 14.39           C  
ANISOU  100  CA  GLN A  17     1315   2200   1953    -48    212   -227       C  
ATOM    101  C   GLN A  17      57.506  46.362  26.420  1.00 12.04           C  
ANISOU  101  C   GLN A  17     1077   1770   1727      7    179   -201       C  
ATOM    102  O   GLN A  17      57.303  45.152  26.539  1.00 13.32           O  
ANISOU  102  O   GLN A  17     1227   1873   1959     65    189   -251       O  
ATOM    103  CB  GLN A  17      56.719  47.035  24.161  1.00 16.51           C  
ANISOU  103  CB  GLN A  17     1613   2487   2172    -81    239   -247       C  
ATOM    104  CG  GLN A  17      55.562  47.803  24.753  1.00 17.83           C  
ANISOU  104  CG  GLN A  17     1878   2575   2322   -108    208   -174       C  
ATOM    105  CD  GLN A  17      55.936  49.237  25.047  1.00 17.21           C  
ANISOU  105  CD  GLN A  17     1813   2518   2208   -167    169    -88       C  
ATOM    106  NE2 GLN A  17      55.533  49.727  26.205  1.00 18.34           N  
ANISOU  106  NE2 GLN A  17     2023   2572   2375   -159    127    -40       N  
ATOM    107  OE1 GLN A  17      56.608  49.892  24.242  1.00 22.13           O  
ANISOU  107  OE1 GLN A  17     2379   3244   2786   -221    174    -69       O  
ATOM    108  N   SER A  18      57.362  47.237  27.416  1.00 12.59           N  
ANISOU  108  N   SER A  18     1204   1799   1782    -16    137   -121       N  
ATOM    109  CA  SER A  18      56.968  46.802  28.751  1.00 12.07           C  
ANISOU  109  CA  SER A  18     1185   1638   1764     23    102    -86       C  
ATOM    110  C   SER A  18      56.443  47.975  29.560  1.00 11.91           C  
ANISOU  110  C   SER A  18     1229   1595   1701    -18     64    -23       C  
ATOM    111  O   SER A  18      56.826  49.129  29.331  1.00 13.88           O  
ANISOU  111  O   SER A  18     1474   1890   1910    -68     52      3       O  
ATOM    112  CB  SER A  18      58.193  46.210  29.469  1.00 13.77           C  
ANISOU  112  CB  SER A  18     1343   1850   2038     64     83    -78       C  
ATOM    113  OG  SER A  18      57.863  45.640  30.727  1.00 13.77           O  
ANISOU  113  OG  SER A  18     1372   1774   2086     98     47    -35       O  
ATOM    114  N   VAL A  19      55.589  47.679  30.540  1.00 10.39           N  
ANISOU  114  N   VAL A  19     1089   1336   1523      4     42      0       N  
ATOM    115  CA  VAL A  19      55.377  48.601  31.650  1.00 10.43           C  
ANISOU  115  CA  VAL A  19     1134   1329   1501    -20     -1     45       C  
ATOM    116  C   VAL A  19      56.670  48.645  32.458  1.00 11.11           C  
ANISOU  116  C   VAL A  19     1173   1443   1606    -13    -28     72       C  
ATOM    117  O   VAL A  19      57.379  47.631  32.573  1.00 11.79           O  
ANISOU  117  O   VAL A  19     1211   1528   1741     28    -23     69       O  
ATOM    118  CB  VAL A  19      54.170  48.157  32.493  1.00  9.70           C  
ANISOU  118  CB  VAL A  19     1092   1184   1409      1    -15     59       C  
ATOM    119  CG1 VAL A  19      53.910  49.132  33.623  1.00 10.98           C  
ANISOU  119  CG1 VAL A  19     1284   1352   1535    -24    -56     84       C  
ATOM    120  CG2 VAL A  19      52.949  48.002  31.613  1.00 10.51           C  
ANISOU  120  CG2 VAL A  19     1235   1261   1496     -4     15     32       C  
ATOM    121  N   SER A  20      57.004  49.815  32.994  1.00 11.14           N  
ANISOU  121  N   SER A  20     1184   1469   1580    -52    -60     94       N  
ATOM    122  CA  SER A  20      58.263  49.964  33.719  1.00 11.29           C  
ANISOU  122  CA  SER A  20     1157   1525   1609    -53    -86    118       C  
ATOM    123  C   SER A  20      58.193  51.174  34.635  1.00 11.79           C  
ANISOU  123  C   SER A  20     1243   1595   1641    -93   -129    132       C  
ATOM    124  O   SER A  20      57.317  52.027  34.499  1.00 12.93           O  
ANISOU  124  O   SER A  20     1431   1715   1765   -121   -138    117       O  
ATOM    125  CB  SER A  20      59.446  50.122  32.756  1.00 14.41           C  
ANISOU  125  CB  SER A  20     1493   1974   2010    -68    -67    110       C  
ATOM    126  OG  SER A  20      59.317  51.316  32.007  1.00 17.94           O  
ANISOU  126  OG  SER A  20     1952   2442   2423   -125    -69    111       O  
ATOM    127  N   GLY A  21      59.146  51.244  35.566  1.00 11.95           N  
ANISOU  127  N   GLY A  21     1226   1650   1663    -94   -159    155       N  
ATOM    128  CA  GLY A  21      59.245  52.342  36.504  1.00 13.15           C  
ANISOU  128  CA  GLY A  21     1386   1820   1790   -131   -202    153       C  
ATOM    129  C   GLY A  21      58.928  51.912  37.924  1.00 11.50           C  
ANISOU  129  C   GLY A  21     1176   1632   1560   -114   -228    166       C  
ATOM    130  O   GLY A  21      58.196  50.946  38.173  1.00 11.62           O  
ANISOU  130  O   GLY A  21     1205   1631   1577    -81   -217    181       O  
ATOM    131  N   GLU A  22      59.475  52.680  38.877  1.00 11.76           N  
ANISOU  131  N   GLU A  22     1187   1710   1570   -144   -266    162       N  
ATOM    132  CA  GLU A  22      59.183  52.497  40.287  1.00 11.92           C  
ANISOU  132  CA  GLU A  22     1196   1781   1552   -143   -296    168       C  
ATOM    133  C   GLU A  22      58.278  53.582  40.839  1.00 13.74           C  
ANISOU  133  C   GLU A  22     1457   2015   1749   -172   -320    104       C  
ATOM    134  O   GLU A  22      57.589  53.345  41.835  1.00 17.71           O  
ANISOU  134  O   GLU A  22     1958   2565   2208   -169   -334     97       O  
ATOM    135  CB  GLU A  22      60.469  52.493  41.130  1.00 12.81           C  
ANISOU  135  CB  GLU A  22     1246   1965   1655   -156   -324    201       C  
ATOM    136  CG  GLU A  22      61.467  51.433  40.738  1.00 13.09           C  
ANISOU  136  CG  GLU A  22     1237   2002   1734   -124   -308    260       C  
ATOM    137  CD  GLU A  22      60.881  50.040  40.805  1.00 16.63           C  
ANISOU  137  CD  GLU A  22     1685   2424   2208    -79   -295    303       C  
ATOM    138  OE1 GLU A  22      60.402  49.613  41.899  1.00 16.85           O  
ANISOU  138  OE1 GLU A  22     1702   2493   2206    -80   -320    339       O  
ATOM    139  OE2 GLU A  22      60.894  49.373  39.760  1.00 13.86           O1-
ANISOU  139  OE2 GLU A  22     1339   2017   1909    -46   -261    301       O1-
ATOM    140  N   THR A  23      58.260  54.778  40.221  1.00 14.00           N  
ANISOU  140  N   THR A  23     1509   2004   1806   -202   -329     59       N  
ATOM    141  CA  THR A  23      57.470  55.894  40.709  1.00 14.51           C  
ANISOU  141  CA  THR A  23     1593   2058   1863   -226   -358    -14       C  
ATOM    142  C   THR A  23      56.180  56.006  39.908  1.00 12.92           C  
ANISOU  142  C   THR A  23     1445   1784   1679   -213   -338    -36       C  
ATOM    143  O   THR A  23      56.122  55.590  38.745  1.00 13.44           O  
ANISOU  143  O   THR A  23     1532   1805   1769   -203   -305      1       O  
ATOM    144  CB  THR A  23      58.246  57.213  40.576  1.00 16.15           C  
ANISOU  144  CB  THR A  23     1780   2246   2110   -270   -395    -46       C  
ATOM    145  CG2 THR A  23      59.585  57.140  41.305  1.00 17.32           C  
ANISOU  145  CG2 THR A  23     1873   2468   2240   -286   -415    -23       C  
ATOM    146  OG1 THR A  23      58.449  57.495  39.190  1.00 18.28           O  
ANISOU  146  OG1 THR A  23     2066   2451   2429   -283   -380    -13       O  
ATOM    147  N   PRO A  24      55.131  56.571  40.506  1.00 13.09           N  
ANISOU  147  N   PRO A  24     1484   1804   1686   -215   -356   -102       N  
ATOM    148  CA  PRO A  24      53.864  56.692  39.773  1.00 13.02           C  
ANISOU  148  CA  PRO A  24     1523   1728   1694   -203   -339   -120       C  
ATOM    149  C   PRO A  24      53.984  57.376  38.434  1.00 13.15           C  
ANISOU  149  C   PRO A  24     1558   1664   1774   -225   -337   -102       C  
ATOM    150  O   PRO A  24      53.364  56.933  37.466  1.00 13.27           O  
ANISOU  150  O   PRO A  24     1605   1642   1794   -213   -304    -72       O  
ATOM    151  CB  PRO A  24      52.974  57.474  40.747  1.00 14.57           C  
ANISOU  151  CB  PRO A  24     1716   1944   1874   -207   -371   -212       C  
ATOM    152  CG  PRO A  24      53.469  57.044  42.087  1.00 15.08           C  
ANISOU  152  CG  PRO A  24     1736   2121   1875   -208   -385   -219       C  
ATOM    153  CD  PRO A  24      54.971  56.934  41.928  1.00 14.61           C  
ANISOU  153  CD  PRO A  24     1645   2074   1833   -224   -390   -164       C  
ATOM    154  N   LEU A  25      54.740  58.463  38.344  1.00 13.86           N  
ANISOU  154  N   LEU A  25     1622   1730   1911   -263   -375   -116       N  
ATOM    155  CA  LEU A  25      54.810  59.197  37.087  1.00 14.11           C  
ANISOU  155  CA  LEU A  25     1662   1694   2005   -295   -384    -83       C  
ATOM    156  C   LEU A  25      55.563  58.407  36.024  1.00 14.37           C  
ANISOU  156  C   LEU A  25     1685   1752   2022   -297   -342     -4       C  
ATOM    157  O   LEU A  25      55.195  58.449  34.844  1.00 14.09           O  
ANISOU  157  O   LEU A  25     1664   1688   2003   -311   -324     32       O  
ATOM    158  CB  LEU A  25      55.414  60.577  37.305  1.00 15.43           C  
ANISOU  158  CB  LEU A  25     1798   1825   2241   -341   -445   -110       C  
ATOM    159  CG  LEU A  25      54.533  61.503  38.147  1.00 26.70           C  
ANISOU  159  CG  LEU A  25     3227   3210   3707   -338   -490   -209       C  
ATOM    160  CD1 LEU A  25      55.233  62.824  38.429  1.00 31.77           C  
ANISOU  160  CD1 LEU A  25     3830   3809   4432   -382   -558   -247       C  
ATOM    161  CD2 LEU A  25      53.195  61.749  37.463  1.00 27.18           C  
ANISOU  161  CD2 LEU A  25     3325   3198   3803   -327   -486   -217       C  
ATOM    162  N   GLU A  26      56.602  57.660  36.417  1.00 14.34           N  
ANISOU  162  N   GLU A  26     1650   1811   1986   -284   -327     19       N  
ATOM    163  CA  GLU A  26      57.333  56.847  35.453  1.00 13.98           C  
ANISOU  163  CA  GLU A  26     1585   1797   1930   -278   -286     74       C  
ATOM    164  C   GLU A  26      56.505  55.666  34.960  1.00 12.91           C  
ANISOU  164  C   GLU A  26     1478   1656   1770   -235   -236     79       C  
ATOM    165  O   GLU A  26      56.549  55.306  33.776  1.00 13.27           O  
ANISOU  165  O   GLU A  26     1519   1707   1817   -239   -202    103       O  
ATOM    166  CB  GLU A  26      58.631  56.347  36.081  1.00 15.42           C  
ANISOU  166  CB  GLU A  26     1721   2041   2096   -269   -288     92       C  
ATOM    167  CG  GLU A  26      59.719  57.402  36.200  1.00 24.57           C  
ANISOU  167  CG  GLU A  26     2840   3215   3279   -318   -330    102       C  
ATOM    168  CD  GLU A  26      60.167  57.912  34.845  1.00 46.25           C  
ANISOU  168  CD  GLU A  26     5566   5956   6049   -362   -327    145       C  
ATOM    169  OE1 GLU A  26      59.536  58.858  34.327  1.00 27.60           O  
ANISOU  169  OE1 GLU A  26     3223   3541   3722   -398   -352    147       O  
ATOM    170  OE2 GLU A  26      61.137  57.353  34.290  1.00 55.74           O1-
ANISOU  170  OE2 GLU A  26     6727   7216   7235   -360   -300    180       O1-
ATOM    171  N   ILE A  27      55.762  55.039  35.859  1.00 12.11           N  
ANISOU  171  N   ILE A  27     1400   1555   1645   -199   -232     57       N  
ATOM    172  CA  ILE A  27      54.862  53.970  35.453  1.00 11.48           C  
ANISOU  172  CA  ILE A  27     1350   1460   1551   -163   -192     62       C  
ATOM    173  C   ILE A  27      53.822  54.512  34.485  1.00 11.64           C  
ANISOU  173  C   ILE A  27     1408   1434   1581   -180   -182     51       C  
ATOM    174  O   ILE A  27      53.515  53.889  33.458  1.00 11.71           O  
ANISOU  174  O   ILE A  27     1424   1437   1586   -172   -143     64       O  
ATOM    175  CB  ILE A  27      54.262  53.299  36.704  1.00 10.87           C  
ANISOU  175  CB  ILE A  27     1282   1401   1445   -132   -201     54       C  
ATOM    176  CG1 ILE A  27      55.376  52.597  37.487  1.00 12.49           C  
ANISOU  176  CG1 ILE A  27     1440   1658   1647   -117   -210     87       C  
ATOM    177  CG2 ILE A  27      53.148  52.339  36.318  1.00 11.96           C  
ANISOU  177  CG2 ILE A  27     1456   1513   1575   -102   -168     60       C  
ATOM    178  CD1 ILE A  27      54.987  52.201  38.883  1.00 12.63           C  
ANISOU  178  CD1 ILE A  27     1449   1722   1627   -107   -234     93       C  
ATOM    179  N   ALA A  28      53.297  55.701  34.771  1.00 11.42           N  
ANISOU  179  N   ALA A  28     1395   1373   1569   -207   -219     25       N  
ATOM    180  CA  ALA A  28      52.319  56.314  33.882  1.00 11.43           C  
ANISOU  180  CA  ALA A  28     1426   1326   1592   -226   -218     24       C  
ATOM    181  C   ALA A  28      52.900  56.584  32.499  1.00 11.68           C  
ANISOU  181  C   ALA A  28     1434   1366   1640   -265   -206     73       C  
ATOM    182  O   ALA A  28      52.218  56.362  31.493  1.00 12.27           O  
ANISOU  182  O   ALA A  28     1523   1434   1706   -271   -179     91       O  
ATOM    183  CB  ALA A  28      51.762  57.601  34.491  1.00 13.21           C  
ANISOU  183  CB  ALA A  28     1659   1504   1855   -245   -271    -19       C  
ATOM    184  N   VAL A  29      54.144  57.074  32.422  1.00 12.49           N  
ANISOU  184  N   VAL A  29     1493   1495   1760   -297   -228     98       N  
ATOM    185  CA  VAL A  29      54.766  57.283  31.116  1.00 12.78           C  
ANISOU  185  CA  VAL A  29     1492   1566   1797   -341   -216    151       C  
ATOM    186  C   VAL A  29      54.800  55.986  30.329  1.00 12.90           C  
ANISOU  186  C   VAL A  29     1499   1635   1769   -312   -153    152       C  
ATOM    187  O   VAL A  29      54.518  55.967  29.126  1.00 13.51           O  
ANISOU  187  O   VAL A  29     1564   1740   1829   -340   -129    176       O  
ATOM    188  CB  VAL A  29      56.183  57.875  31.276  1.00 14.67           C  
ANISOU  188  CB  VAL A  29     1681   1839   2055   -377   -248    178       C  
ATOM    189  CG1 VAL A  29      56.993  57.754  29.971  1.00 14.89           C  
ANISOU  189  CG1 VAL A  29     1656   1942   2061   -417   -224    231       C  
ATOM    190  CG2 VAL A  29      56.108  59.326  31.719  1.00 16.79           C  
ANISOU  190  CG2 VAL A  29     1948   2044   2386   -420   -318    179       C  
ATOM    191  N   SER A  30      55.152  54.879  30.984  1.00 12.43           N  
ANISOU  191  N   SER A  30     1436   1593   1693   -260   -128    124       N  
ATOM    192  CA  SER A  30      55.286  53.623  30.260  1.00 11.69           C  
ANISOU  192  CA  SER A  30     1322   1538   1580   -228    -74    112       C  
ATOM    193  C   SER A  30      53.945  53.141  29.725  1.00 10.89           C  
ANISOU  193  C   SER A  30     1264   1409   1465   -213    -44     94       C  
ATOM    194  O   SER A  30      53.905  52.430  28.719  1.00 12.06           O  
ANISOU  194  O   SER A  30     1390   1595   1597   -208     -2     79       O  
ATOM    195  CB  SER A  30      55.939  52.553  31.138  1.00 11.39           C  
ANISOU  195  CB  SER A  30     1267   1508   1553   -175    -66     95       C  
ATOM    196  OG  SER A  30      55.036  51.978  32.072  1.00 11.90           O  
ANISOU  196  OG  SER A  30     1375   1527   1620   -135    -71     82       O  
ATOM    197  N   LEU A  31      52.837  53.491  30.392  1.00 10.70           N  
ANISOU  197  N   LEU A  31     1294   1328   1446   -205    -66     86       N  
ATOM    198  CA  LEU A  31      51.501  53.086  29.961  1.00 10.50           C  
ANISOU  198  CA  LEU A  31     1309   1274   1405   -193    -41     72       C  
ATOM    199  C   LEU A  31      50.896  54.032  28.928  1.00  9.78           C  
ANISOU  199  C   LEU A  31     1223   1182   1311   -244    -48     98       C  
ATOM    200  O   LEU A  31      49.997  53.616  28.186  1.00 10.16           O  
ANISOU  200  O   LEU A  31     1289   1232   1338   -243    -17     93       O  
ATOM    201  CB  LEU A  31      50.579  52.932  31.172  1.00 10.14           C  
ANISOU  201  CB  LEU A  31     1310   1184   1359   -160    -60     52       C  
ATOM    202  CG  LEU A  31      50.832  51.646  31.964  1.00 10.72           C  
ANISOU  202  CG  LEU A  31     1377   1264   1431   -111    -47     45       C  
ATOM    203  CD1 LEU A  31      50.399  51.784  33.410  1.00 11.65           C  
ANISOU  203  CD1 LEU A  31     1514   1373   1538    -96    -81     39       C  
ATOM    204  CD2 LEU A  31      50.154  50.456  31.300  1.00 10.80           C  
ANISOU  204  CD2 LEU A  31     1400   1264   1441    -84     -6     33       C  
ATOM    205  N   GLY A  32      51.353  55.276  28.865  1.00 10.82           N  
ANISOU  205  N   GLY A  32     1335   1308   1468   -291    -90    132       N  
ATOM    206  CA  GLY A  32      50.961  56.175  27.783  1.00 10.63           C  
ANISOU  206  CA  GLY A  32     1298   1289   1452   -350   -105    180       C  
ATOM    207  C   GLY A  32      49.467  56.405  27.672  1.00 10.36           C  
ANISOU  207  C   GLY A  32     1310   1201   1425   -346   -109    176       C  
ATOM    208  O   GLY A  32      48.786  56.740  28.651  1.00 11.02           O  
ANISOU  208  O   GLY A  32     1432   1220   1536   -319   -137    144       O  
ATOM    209  N   LEU A  33      48.962  56.270  26.444  1.00 10.21           N  
ANISOU  209  N   LEU A  33     1280   1222   1378   -377    -83    207       N  
ATOM    210  CA  LEU A  33      47.543  56.438  26.133  1.00  9.77           C  
ANISOU  210  CA  LEU A  33     1261   1129   1323   -379    -83    213       C  
ATOM    211  C   LEU A  33      46.947  55.066  25.885  1.00  9.27           C  
ANISOU  211  C   LEU A  33     1222   1096   1206   -338    -21    169       C  
ATOM    212  O   LEU A  33      47.480  54.289  25.079  1.00 10.06           O  
ANISOU  212  O   LEU A  33     1286   1271   1265   -344     22    160       O  
ATOM    213  CB  LEU A  33      47.360  57.307  24.885  1.00 10.77           C  
ANISOU  213  CB  LEU A  33     1350   1286   1456   -453   -103    293       C  
ATOM    214  CG  LEU A  33      45.922  57.494  24.405  1.00 10.79           C  
ANISOU  214  CG  LEU A  33     1380   1260   1460   -461   -104    312       C  
ATOM    215  CD1 LEU A  33      45.074  58.227  25.443  1.00 12.37           C  
ANISOU  215  CD1 LEU A  33     1624   1347   1728   -430   -152    286       C  
ATOM    216  CD2 LEU A  33      45.883  58.238  23.085  1.00 12.62           C  
ANISOU  216  CD2 LEU A  33     1560   1548   1688   -533   -122    401       C  
ATOM    217  N   GLY A  34      45.845  54.757  26.566  1.00  9.29           N  
ANISOU  217  N   GLY A  34     1278   1043   1210   -296    -19    135       N  
ATOM    218  CA  GLY A  34      45.233  53.452  26.470  1.00  8.61           C  
ANISOU  218  CA  GLY A  34     1215    969   1085   -258     30     96       C  
ATOM    219  C   GLY A  34      43.910  53.433  25.717  1.00  8.27           C  
ANISOU  219  C   GLY A  34     1196    926   1019   -274     46    108       C  
ATOM    220  O   GLY A  34      43.256  54.443  25.499  1.00  8.91           O  
ANISOU  220  O   GLY A  34     1284    980   1120   -304     14    144       O  
ATOM    221  N   TRP A  35      43.498  52.211  25.384  1.00  8.61           N  
ANISOU  221  N   TRP A  35     1250    992   1029   -249     93     73       N  
ATOM    222  CA  TRP A  35      42.271  51.939  24.649  1.00  8.78           C  
ANISOU  222  CA  TRP A  35     1292   1024   1020   -262    117     75       C  
ATOM    223  C   TRP A  35      41.716  50.613  25.138  1.00  8.56           C  
ANISOU  223  C   TRP A  35     1296    972    983   -211    145     26       C  
ATOM    224  O   TRP A  35      42.471  49.659  25.324  1.00  9.20           O  
ANISOU  224  O   TRP A  35     1359   1060   1076   -182    164     -9       O  
ATOM    225  CB  TRP A  35      42.591  51.885  23.164  1.00 10.10           C  
ANISOU  225  CB  TRP A  35     1407   1282   1148   -313    147     90       C  
ATOM    226  CG  TRP A  35      41.453  51.704  22.201  1.00  9.52           C  
ANISOU  226  CG  TRP A  35     1340   1246   1034   -341    172     99       C  
ATOM    227  CD1 TRP A  35      40.744  52.695  21.582  1.00  9.79           C  
ANISOU  227  CD1 TRP A  35     1368   1292   1061   -392    149    165       C  
ATOM    228  CD2 TRP A  35      40.963  50.468  21.668  1.00  9.05           C  
ANISOU  228  CD2 TRP A  35     1281   1219    938   -326    222     42       C  
ATOM    229  CE2 TRP A  35      39.953  50.784  20.724  1.00  9.39           C  
ANISOU  229  CE2 TRP A  35     1321   1307    940   -372    231     75       C  
ATOM    230  CE3 TRP A  35      41.296  49.129  21.874  1.00  9.51           C  
ANISOU  230  CE3 TRP A  35     1337   1272   1006   -280    255    -33       C  
ATOM    231  NE1 TRP A  35      39.844  52.153  20.686  1.00  9.75           N  
ANISOU  231  NE1 TRP A  35     1358   1336   1011   -400    179    152       N  
ATOM    232  CZ2 TRP A  35      39.260  49.795  20.008  1.00  9.93           C  
ANISOU  232  CZ2 TRP A  35     1383   1413    977   -361    266     25       C  
ATOM    233  CZ3 TRP A  35      40.605  48.154  21.176  1.00 10.20           C  
ANISOU  233  CZ3 TRP A  35     1422   1388   1067   -278    296    -83       C  
ATOM    234  CH2 TRP A  35      39.609  48.495  20.242  1.00  9.70           C  
ANISOU  234  CH2 TRP A  35     1357   1376    951   -326    308    -57       C  
ATOM    235  N   ASN A  36      40.393  50.555  25.323  1.00  8.18           N  
ANISOU  235  N   ASN A  36     1292    894    923   -203    144     28       N  
ATOM    236  CA  ASN A  36      39.712  49.334  25.728  1.00  8.27           C  
ANISOU  236  CA  ASN A  36     1332    883    927   -165    166     -4       C  
ATOM    237  C   ASN A  36      39.084  48.611  24.548  1.00  8.48           C  
ANISOU  237  C   ASN A  36     1352    946    923   -184    208    -24       C  
ATOM    238  O   ASN A  36      38.343  49.218  23.766  1.00  8.51           O  
ANISOU  238  O   ASN A  36     1359    977    897   -221    212      1       O  
ATOM    239  CB  ASN A  36      38.529  49.626  26.673  1.00  8.23           C  
ANISOU  239  CB  ASN A  36     1374    837    917   -147    140      7       C  
ATOM    240  CG  ASN A  36      38.934  49.869  28.103  1.00  8.33           C  
ANISOU  240  CG  ASN A  36     1392    824    948   -118    105      4       C  
ATOM    241  ND2 ASN A  36      39.170  51.122  28.443  1.00  8.66           N  
ANISOU  241  ND2 ASN A  36     1426    856   1007   -130     70     12       N  
ATOM    242  OD1 ASN A  36      38.993  48.933  28.905  1.00  8.46           O  
ANISOU  242  OD1 ASN A  36     1414    834    968    -88    104     -3       O  
ATOM    243  N   LEU A  37      39.331  47.309  24.472  1.00  8.27           N  
ANISOU  243  N   LEU A  37     1315    916    912   -157    234    -69       N  
ATOM    244  CA  LEU A  37      38.662  46.406  23.529  1.00  8.57           C  
ANISOU  244  CA  LEU A  37     1347    979    931   -167    272   -109       C  
ATOM    245  C   LEU A  37      37.305  46.020  24.123  1.00  8.26           C  
ANISOU  245  C   LEU A  37     1362    891    887   -151    263    -95       C  
ATOM    246  O   LEU A  37      37.123  44.965  24.727  1.00  8.75           O  
ANISOU  246  O   LEU A  37     1436    906    983   -118    260   -111       O  
ATOM    247  CB  LEU A  37      39.544  45.185  23.309  1.00  8.69           C  
ANISOU  247  CB  LEU A  37     1319    993    989   -139    295   -174       C  
ATOM    248  CG  LEU A  37      39.044  44.171  22.285  1.00  8.53           C  
ANISOU  248  CG  LEU A  37     1279   1000    964   -146    334   -241       C  
ATOM    249  CD1 LEU A  37      39.058  44.744  20.893  1.00 10.76           C  
ANISOU  249  CD1 LEU A  37     1518   1392   1177   -202    366   -255       C  
ATOM    250  CD2 LEU A  37      39.862  42.904  22.368  1.00 10.51           C  
ANISOU  250  CD2 LEU A  37     1488   1217   1290   -104    343   -313       C  
ATOM    251  N   GLY A  38      36.334  46.938  24.008  1.00  7.80           N  
ANISOU  251  N   GLY A  38     1010   1000    953    -59     -1    -33       N  
ATOM    252  CA  GLY A  38      35.067  46.787  24.699  1.00  8.20           C  
ANISOU  252  CA  GLY A  38     1040   1067   1010    -50    -14    -35       C  
ATOM    253  C   GLY A  38      34.006  46.066  23.878  1.00  8.07           C  
ANISOU  253  C   GLY A  38     1019   1070    978    -64    -27    -36       C  
ATOM    254  O   GLY A  38      34.056  45.992  22.656  1.00  8.57           O  
ANISOU  254  O   GLY A  38     1100   1134   1022    -76    -34    -34       O  
ATOM    255  N   ASN A  39      32.991  45.566  24.589  1.00  8.65           N  
ANISOU  255  N   ASN A  39     1066   1161   1059    -64    -33    -39       N  
ATOM    256  CA  ASN A  39      31.934  44.749  23.978  1.00  9.36           C  
ANISOU  256  CA  ASN A  39     1146   1273   1138    -86    -48    -41       C  
ATOM    257  C   ASN A  39      32.529  43.637  23.121  1.00  8.78           C  
ANISOU  257  C   ASN A  39     1101   1185   1048   -115    -39    -52       C  
ATOM    258  O   ASN A  39      32.051  43.337  22.030  1.00  9.61           O  
ANISOU  258  O   ASN A  39     1219   1301   1132   -135    -56    -54       O  
ATOM    259  CB  ASN A  39      30.924  45.584  23.200  1.00 10.35           C  
ANISOU  259  CB  ASN A  39     1259   1422   1253    -77    -76    -28       C  
ATOM    260  CG  ASN A  39      29.944  46.316  24.096  1.00 11.00           C  
ANISOU  260  CG  ASN A  39     1305   1524   1352    -48    -83    -18       C  
ATOM    261  ND2 ASN A  39      28.908  46.891  23.489  1.00 12.90           N  
ANISOU  261  ND2 ASN A  39     1525   1790   1584    -36   -109     -4       N  
ATOM    262  OD1 ASN A  39      30.106  46.365  25.296  1.00 12.11           O  
ANISOU  262  OD1 ASN A  39     1436   1658   1508    -35    -65    -21       O  
ATOM    263  N   GLN A  40      33.566  42.997  23.648  1.00  8.46           N  
ANISOU  263  N   GLN A  40     1076   1124   1016   -116    -13    -60       N  
ATOM    264  CA  GLN A  40      34.375  42.020  22.921  1.00  8.24           C  
ANISOU  264  CA  GLN A  40     1081   1076    975   -132      4    -71       C  
ATOM    265  C   GLN A  40      34.483  40.775  23.802  1.00  8.29           C  
ANISOU  265  C   GLN A  40     1088   1070    992   -140     21    -79       C  
ATOM    266  O   GLN A  40      33.481  40.072  23.980  1.00  8.56           O  
ANISOU  266  O   GLN A  40     1115   1114   1024   -162     12    -83       O  
ATOM    267  CB  GLN A  40      35.694  42.657  22.499  1.00  8.58           C  
ANISOU  267  CB  GLN A  40     1140   1104   1015   -117     20    -67       C  
ATOM    268  CG  GLN A  40      36.392  41.927  21.365  1.00  8.51           C  
ANISOU  268  CG  GLN A  40     1167   1081    985   -128     38    -75       C  
ATOM    269  CD  GLN A  40      35.793  42.231  20.008  1.00  8.10           C  
ANISOU  269  CD  GLN A  40     1136   1039    903   -143     19    -75       C  
ATOM    270  NE2 GLN A  40      35.698  41.212  19.169  1.00  9.43           N  
ANISOU  270  NE2 GLN A  40     1338   1199   1046   -164     24    -89       N  
ATOM    271  OE1 GLN A  40      35.447  43.365  19.699  1.00  9.07           O  
ANISOU  271  OE1 GLN A  40     1251   1174   1022   -135      0    -62       O  
ATOM    272  N   LEU A  41      35.649  40.487  24.397  1.00  8.24           N  
ANISOU  272  N   LEU A  41     1089   1045    997   -124     46    -79       N  
ATOM    273  CA  LEU A  41      35.725  39.325  25.288  1.00  8.43           C  
ANISOU  273  CA  LEU A  41     1117   1056   1030   -127     61    -83       C  
ATOM    274  C   LEU A  41      34.924  39.527  26.568  1.00  7.99           C  
ANISOU  274  C   LEU A  41     1033   1016    990   -124     53    -77       C  
ATOM    275  O   LEU A  41      34.694  38.553  27.304  1.00  8.82           O  
ANISOU  275  O   LEU A  41     1141   1111   1098   -132     64    -78       O  
ATOM    276  CB  LEU A  41      37.167  38.936  25.587  1.00  8.49           C  
ANISOU  276  CB  LEU A  41     1138   1044   1046   -105     87    -82       C  
ATOM    277  CG  LEU A  41      37.978  38.485  24.381  1.00  9.67           C  
ANISOU  277  CG  LEU A  41     1318   1177   1180   -105    105    -89       C  
ATOM    278  CD1 LEU A  41      39.418  38.179  24.757  1.00 11.03           C  
ANISOU  278  CD1 LEU A  41     1490   1337   1364    -78    132    -83       C  
ATOM    279  CD2 LEU A  41      37.364  37.275  23.708  1.00 14.99           C  
ANISOU  279  CD2 LEU A  41     2029   1834   1834   -130    109   -103       C  
ATOM    280  N   ASP A  42      34.496  40.761  26.839  1.00  8.27           N  
ANISOU  280  N   ASP A  42     1042   1070   1030   -110     38    -69       N  
ATOM    281  CA  ASP A  42      33.569  41.045  27.922  1.00  8.00           C  
ANISOU  281  CA  ASP A  42      980   1053   1006   -105     32    -64       C  
ATOM    282  C   ASP A  42      32.126  40.664  27.598  1.00  8.00           C  
ANISOU  282  C   ASP A  42      963   1075   1001   -129     19    -63       C  
ATOM    283  O   ASP A  42      31.316  40.505  28.530  1.00  8.43           O  
ANISOU  283  O   ASP A  42      994   1145   1063   -130     23    -58       O  
ATOM    284  CB  ASP A  42      33.631  42.525  28.355  1.00  8.51           C  
ANISOU  284  CB  ASP A  42     1031   1127   1077    -77     24    -57       C  
ATOM    285  CG  ASP A  42      33.672  43.521  27.191  1.00  8.76           C  
ANISOU  285  CG  ASP A  42     1067   1160   1100    -73      8    -55       C  
ATOM    286  OD1 ASP A  42      34.448  43.317  26.227  1.00  8.96           O  
ANISOU  286  OD1 ASP A  42     1114   1174   1117    -82     12    -57       O  
ATOM    287  OD2 ASP A  42      32.924  44.537  27.268  1.00 10.74           O1-
ANISOU  287  OD2 ASP A  42     1302   1425   1352    -57     -5    -48       O1-
ATOM    288  N   ALA A  43      31.784  40.535  26.322  1.00  8.76           N  
ANISOU  288  N   ALA A  43     1069   1177   1083   -149      4    -67       N  
ATOM    289  CA  ALA A  43      30.405  40.284  25.931  1.00  9.19           C  
ANISOU  289  CA  ALA A  43     1101   1260   1133   -175    -16    -65       C  
ATOM    290  C   ALA A  43      29.983  38.881  26.352  1.00  9.21           C  
ANISOU  290  C   ALA A  43     1109   1255   1136   -210     -6    -70       C  
ATOM    291  O   ALA A  43      30.772  37.928  26.314  1.00 10.06           O  
ANISOU  291  O   ALA A  43     1254   1329   1238   -221     12    -80       O  
ATOM    292  CB  ALA A  43      30.248  40.434  24.421  1.00  9.30           C  
ANISOU  292  CB  ALA A  43     1130   1279   1125   -191    -39    -68       C  
ATOM    293  N   HIS A  44      28.720  38.755  26.735  1.00  9.92           N  
ANISOU  293  N   HIS A  44     1161   1376   1232   -229    -15    -63       N  
ATOM    294  CA  HIS A  44      28.181  37.469  27.146  1.00 10.62           C  
ANISOU  294  CA  HIS A  44     1253   1460   1322   -270     -6    -65       C  
ATOM    295  C   HIS A  44      26.696  37.453  26.812  1.00 11.49           C  
ANISOU  295  C   HIS A  44     1319   1614   1432   -303    -30    -58       C  
ATOM    296  O   HIS A  44      26.027  38.489  26.853  1.00 12.66           O  
ANISOU  296  O   HIS A  44     1423   1800   1588   -279    -44    -46       O  
ATOM    297  CB  HIS A  44      28.423  37.187  28.631  1.00 11.84           C  
ANISOU  297  CB  HIS A  44     1405   1604   1491   -253     24    -59       C  
ATOM    298  CG  HIS A  44      27.860  38.226  29.544  1.00 11.91           C  
ANISOU  298  CG  HIS A  44     1369   1645   1512   -221     26    -46       C  
ATOM    299  CD2 HIS A  44      28.310  39.454  29.881  1.00 11.76           C  
ANISOU  299  CD2 HIS A  44     1342   1628   1497   -174     27    -42       C  
ATOM    300  ND1 HIS A  44      26.681  38.038  30.241  1.00 15.47           N  
ANISOU  300  ND1 HIS A  44     1778   2127   1971   -236     32    -34       N  
ATOM    301  CE1 HIS A  44      26.435  39.116  30.966  1.00 15.61           C  
ANISOU  301  CE1 HIS A  44     1767   2166   1997   -194     39    -26       C  
ATOM    302  NE2 HIS A  44      27.407  39.990  30.766  1.00 12.39           N  
ANISOU  302  NE2 HIS A  44     1383   1740   1587   -157     34    -31       N  
ATOM    303  N   ASN A  45      26.186  36.265  26.510  1.00 11.84           N  
ANISOU  303  N   ASN A  45     1376   1652   1469   -358    -34    -64       N  
ATOM    304  CA  ASN A  45      24.805  36.104  26.099  1.00 14.82           C  
ANISOU  304  CA  ASN A  45     1710   2074   1846   -401    -62    -58       C  
ATOM    305  C   ASN A  45      24.388  34.703  26.491  1.00 14.17           C  
ANISOU  305  C   ASN A  45     1643   1977   1765   -459    -49    -61       C  
ATOM    306  O   ASN A  45      25.152  33.749  26.326  1.00 15.31           O  
ANISOU  306  O   ASN A  45     1849   2070   1897   -478    -35    -76       O  
ATOM    307  CB  ASN A  45      24.666  36.303  24.585  1.00 15.51           C  
ANISOU  307  CB  ASN A  45     1811   2173   1911   -420   -100    -66       C  
ATOM    308  CG  ASN A  45      23.219  36.487  24.150  1.00 22.41           C  
ANISOU  308  CG  ASN A  45     2624   3106   2785   -452   -138    -54       C  
ATOM    309  ND2 ASN A  45      22.929  36.128  22.905  1.00 26.69           N  
ANISOU  309  ND2 ASN A  45     3185   3653   3301   -495   -174    -64       N  
ATOM    310  OD1 ASN A  45      22.377  36.951  24.920  1.00 19.56           O  
ANISOU  310  OD1 ASN A  45     2200   2787   2446   -438   -134    -35       O  
ATOM    311  N   ASN A  46      23.175  34.593  27.035  1.00 19.45           N  
ANISOU  311  N   ASN A  46     2254   2690   2448   -487    -53    -46       N  
ATOM    312  CA  ASN A  46      22.620  33.303  27.445  1.00 25.05           C  
ANISOU  312  CA  ASN A  46     2971   3388   3159   -551    -41    -45       C  
ATOM    313  C   ASN A  46      23.541  32.586  28.432  1.00 29.72           C  
ANISOU  313  C   ASN A  46     3615   3924   3753   -537      2    -48       C  
ATOM    314  O   ASN A  46      23.691  31.364  28.394  1.00 28.70           O  
ANISOU  314  O   ASN A  46     3536   3754   3615   -583     12    -57       O  
ATOM    315  CB  ASN A  46      22.305  32.433  26.226  1.00 26.84           C  
ANISOU  315  CB  ASN A  46     3230   3604   3364   -620    -72    -62       C  
ATOM    316  CG  ASN A  46      21.286  33.080  25.300  1.00 25.77           C  
ANISOU  316  CG  ASN A  46     3037   3530   3223   -638   -120    -55       C  
ATOM    317  ND2 ASN A  46      21.444  32.864  23.999  1.00 33.87           N  
ANISOU  317  ND2 ASN A  46     4104   4544   4223   -666   -153    -73       N  
ATOM    318  OD1 ASN A  46      20.374  33.771  25.753  1.00 27.91           O  
ANISOU  318  OD1 ASN A  46     3230   3860   3514   -624   -126    -34       O  
ATOM    319  N   GLY A  47      24.168  33.360  29.318  1.00 27.95           N  
ANISOU  319  N   GLY A  47     3383   3698   3538   -473     25    -40       N  
ATOM    320  CA  GLY A  47      24.960  32.821  30.403  1.00 26.44           C  
ANISOU  320  CA  GLY A  47     3230   3465   3350   -454     61    -37       C  
ATOM    321  C   GLY A  47      26.405  32.506  30.077  1.00 23.49           C  
ANISOU  321  C   GLY A  47     2925   3036   2966   -427     70    -52       C  
ATOM    322  O   GLY A  47      27.140  32.056  30.969  1.00 23.10           O  
ANISOU  322  O   GLY A  47     2906   2953   2918   -406     97    -47       O  
ATOM    323  N   VAL A  48      26.850  32.735  28.844  1.00 15.51           N  
ANISOU  323  N   VAL A  48     1935   2015   1942   -425     48    -67       N  
ATOM    324  CA  VAL A  48      28.176  32.327  28.418  1.00 13.23           C  
ANISOU  324  CA  VAL A  48     1709   1676   1643   -403     60    -81       C  
ATOM    325  C   VAL A  48      28.830  33.490  27.705  1.00 12.40           C  
ANISOU  325  C   VAL A  48     1594   1582   1534   -360     46    -86       C  
ATOM    326  O   VAL A  48      28.203  34.172  26.884  1.00 12.72           O  
ANISOU  326  O   VAL A  48     1608   1657   1570   -370     18    -88       O  
ATOM    327  CB  VAL A  48      28.122  31.086  27.500  1.00 17.28           C  
ANISOU  327  CB  VAL A  48     2278   2151   2138   -455     57    -98       C  
ATOM    328  CG1 VAL A  48      29.523  30.592  27.183  1.00 17.83           C  
ANISOU  328  CG1 VAL A  48     2413   2166   2197   -423     78   -111       C  
ATOM    329  CG2 VAL A  48      27.287  29.993  28.146  1.00 24.38           C  
ANISOU  329  CG2 VAL A  48     3184   3040   3041   -509     68    -92       C  
ATOM    330  N   ALA A  49      30.095  33.718  28.011  1.00 11.18           N  
ANISOU  330  N   ALA A  49     1462   1402   1382   -315     64    -87       N  
ATOM    331  CA  ALA A  49      30.901  34.653  27.245  1.00 10.48           C  
ANISOU  331  CA  ALA A  49     1377   1317   1289   -281     56    -92       C  
ATOM    332  C   ALA A  49      30.775  34.341  25.765  1.00 10.94           C  
ANISOU  332  C   ALA A  49     1464   1368   1325   -310     39   -107       C  
ATOM    333  O   ALA A  49      30.803  33.182  25.361  1.00 14.05           O  
ANISOU  333  O   ALA A  49     1902   1730   1705   -342     47   -119       O  
ATOM    334  CB  ALA A  49      32.362  34.550  27.697  1.00 14.57           C  
ANISOU  334  CB  ALA A  49     1921   1803   1811   -239     80    -91       C  
ATOM    335  N   ASP A  50      30.597  35.385  24.957  1.00 10.96           N  
ANISOU  335  N   ASP A  50     1446   1397   1320   -301     16   -107       N  
ATOM    336  CA  ASP A  50      30.232  35.231  23.545  1.00 11.46           C  
ANISOU  336  CA  ASP A  50     1532   1465   1358   -332     -7   -119       C  
ATOM    337  C   ASP A  50      30.730  36.505  22.839  1.00 10.97           C  
ANISOU  337  C   ASP A  50     1461   1417   1288   -298    -17   -114       C  
ATOM    338  O   ASP A  50      30.023  37.508  22.777  1.00 11.17           O  
ANISOU  338  O   ASP A  50     1446   1480   1319   -289    -41   -102       O  
ATOM    339  CB  ASP A  50      28.738  35.019  23.412  1.00 12.89           C  
ANISOU  339  CB  ASP A  50     1681   1681   1537   -379    -36   -116       C  
ATOM    340  CG  ASP A  50      28.313  34.634  22.016  1.00 17.47           C  
ANISOU  340  CG  ASP A  50     2290   2262   2085   -422    -64   -130       C  
ATOM    341  OD1 ASP A  50      29.053  34.920  21.064  1.00 16.25           O  
ANISOU  341  OD1 ASP A  50     2172   2093   1909   -406    -64   -139       O  
ATOM    342  OD2 ASP A  50      27.198  34.064  21.885  1.00 18.22           O1-
ANISOU  342  OD2 ASP A  50     2370   2376   2175   -474    -87   -131       O1-
ATOM    343  N   GLU A  51      31.962  36.436  22.351  1.00 10.43           N  
ANISOU  343  N   GLU A  51     1433   1320   1211   -277      4   -122       N  
ATOM    344  CA  GLU A  51      32.702  37.602  21.878  1.00 10.61           C  
ANISOU  344  CA  GLU A  51     1451   1349   1230   -242      4   -115       C  
ATOM    345  C   GLU A  51      31.981  38.378  20.785  1.00 10.31           C  
ANISOU  345  C   GLU A  51     1406   1339   1171   -254    -29   -111       C  
ATOM    346  O   GLU A  51      32.148  39.604  20.692  1.00 11.47           O  
ANISOU  346  O   GLU A  51     1534   1501   1324   -226    -37    -98       O  
ATOM    347  CB  GLU A  51      34.051  37.104  21.353  1.00 11.70           C  
ANISOU  347  CB  GLU A  51     1636   1453   1357   -228     36   -125       C  
ATOM    348  CG  GLU A  51      34.940  38.199  20.836  1.00 12.76           C  
ANISOU  348  CG  GLU A  51     1768   1592   1489   -199     42   -116       C  
ATOM    349  CD  GLU A  51      36.250  37.711  20.212  1.00 10.85           C  
ANISOU  349  CD  GLU A  51     1566   1322   1235   -184     77   -124       C  
ATOM    350  OE1 GLU A  51      36.600  36.502  20.311  1.00 11.60           O  
ANISOU  350  OE1 GLU A  51     1692   1389   1326   -187    100   -136       O  
ATOM    351  OE2 GLU A  51      36.938  38.567  19.633  1.00 10.89           O1-
ANISOU  351  OE2 GLU A  51     1571   1333   1233   -167     84   -117       O1-
ATOM    352  N   THR A  52      31.227  37.706  19.933  1.00 10.38           N  
ANISOU  352  N   THR A  52     1436   1354   1156   -295    -51   -122       N  
ATOM    353  CA  THR A  52      30.625  38.359  18.782  1.00 10.59           C  
ANISOU  353  CA  THR A  52     1462   1406   1156   -306    -86   -118       C  
ATOM    354  C   THR A  52      29.154  38.694  19.002  1.00 10.60           C  
ANISOU  354  C   THR A  52     1410   1453   1166   -323   -125   -106       C  
ATOM    355  O   THR A  52      28.463  39.038  18.033  1.00 12.68           O  
ANISOU  355  O   THR A  52     1671   1743   1405   -339   -161   -101       O  
ATOM    356  CB  THR A  52      30.799  37.503  17.525  1.00 12.71           C  
ANISOU  356  CB  THR A  52     1792   1655   1383   -339    -88   -139       C  
ATOM    357  CG2 THR A  52      32.269  37.317  17.202  1.00 14.29           C  
ANISOU  357  CG2 THR A  52     2040   1816   1574   -313    -46   -148       C  
ATOM    358  OG1 THR A  52      30.203  36.222  17.721  1.00 14.98           O  
ANISOU  358  OG1 THR A  52     2095   1931   1667   -384    -92   -154       O  
ATOM    359  N   SER A  53      28.663  38.634  20.243  1.00 10.70           N  
ANISOU  359  N   SER A  53     1379   1478   1210   -318   -118    -97       N  
ATOM    360  CA  SER A  53      27.239  38.790  20.488  1.00 11.47           C  
ANISOU  360  CA  SER A  53     1420   1621   1317   -336   -149    -85       C  
ATOM    361  C   SER A  53      26.803  40.210  20.819  1.00 10.82           C  
ANISOU  361  C   SER A  53     1288   1572   1251   -291   -162    -62       C  
ATOM    362  O   SER A  53      25.587  40.448  20.907  1.00 11.59           O  
ANISOU  362  O   SER A  53     1334   1714   1356   -299   -188    -49       O  
ATOM    363  CB  SER A  53      26.794  37.852  21.617  1.00 13.21           C  
ANISOU  363  CB  SER A  53     1620   1838   1559   -361   -131    -87       C  
ATOM    364  OG  SER A  53      27.302  38.243  22.873  1.00 13.07           O  
ANISOU  364  OG  SER A  53     1587   1811   1570   -320   -100    -79       O  
ATOM    365  N   TRP A  54      27.740  41.137  21.027  1.00 10.01           N  
ANISOU  365  N   TRP A  54     1199   1449   1156   -245   -143    -57       N  
ATOM    366  CA  TRP A  54      27.403  42.515  21.373  1.00 10.17           C  
ANISOU  366  CA  TRP A  54     1184   1491   1191   -199   -151    -37       C  
ATOM    367  C   TRP A  54      27.920  43.477  20.305  1.00 10.22           C  
ANISOU  367  C   TRP A  54     1219   1489   1175   -178   -164    -30       C  
ATOM    368  O   TRP A  54      28.537  44.503  20.615  1.00 11.24           O  
ANISOU  368  O   TRP A  54     1354   1602   1314   -139   -151    -22       O  
ATOM    369  CB  TRP A  54      27.941  42.917  22.747  1.00  9.90           C  
ANISOU  369  CB  TRP A  54     1139   1440   1184   -165   -119    -35       C  
ATOM    370  CG  TRP A  54      27.261  42.279  23.926  1.00  9.86           C  
ANISOU  370  CG  TRP A  54     1098   1449   1199   -175   -106    -35       C  
ATOM    371  CD1 TRP A  54      26.262  41.341  23.925  1.00 10.83           C  
ANISOU  371  CD1 TRP A  54     1196   1597   1322   -216   -117    -36       C  
ATOM    372  CD2 TRP A  54      27.552  42.546  25.301  1.00  9.96           C  
ANISOU  372  CD2 TRP A  54     1099   1451   1233   -147    -78    -33       C  
ATOM    373  CE2 TRP A  54      26.703  41.742  26.080  1.00  9.72           C  
ANISOU  373  CE2 TRP A  54     1037   1441   1213   -169    -70    -31       C  
ATOM    374  CE3 TRP A  54      28.454  43.394  25.945  1.00 10.08           C  
ANISOU  374  CE3 TRP A  54     1130   1443   1256   -108    -60    -33       C  
ATOM    375  NE1 TRP A  54      25.914  41.029  25.212  1.00 11.38           N  
ANISOU  375  NE1 TRP A  54     1237   1673   1412   -213    -94    -32       N  
ATOM    376  CZ2 TRP A  54      26.724  41.766  27.475  1.00 11.07           C  
ANISOU  376  CZ2 TRP A  54     1195   1610   1401   -150    -43    -28       C  
ATOM    377  CZ3 TRP A  54      28.472  43.429  27.321  1.00 11.34           C  
ANISOU  377  CZ3 TRP A  54     1277   1600   1431    -91    -37    -32       C  
ATOM    378  CH2 TRP A  54      27.612  42.619  28.075  1.00 11.57           C  
ANISOU  378  CH2 TRP A  54     1277   1650   1469   -109    -28    -30       C  
ATOM    379  N   GLY A  55      27.693  43.149  19.044  1.00 10.51           N  
ANISOU  379  N   GLY A  55     1279   1534   1180   -206   -190    -33       N  
ATOM    380  CA  GLY A  55      27.877  44.110  17.987  1.00 11.59           C  
ANISOU  380  CA  GLY A  55     1438   1673   1293   -187   -208    -21       C  
ATOM    381  C   GLY A  55      29.233  44.150  17.322  1.00 10.69           C  
ANISOU  381  C   GLY A  55     1383   1521   1160   -185   -183    -30       C  
ATOM    382  O   GLY A  55      29.416  44.968  16.404  1.00 12.89           O  
ANISOU  382  O   GLY A  55     1684   1798   1414   -172   -196    -17       O  
ATOM    383  N   ASN A  56      30.175  43.308  17.729  1.00  9.72           N  
ANISOU  383  N   ASN A  56     1284   1367   1044   -197   -147    -48       N  
ATOM    384  CA  ASN A  56      31.499  43.273  17.122  1.00  9.94           C  
ANISOU  384  CA  ASN A  56     1360   1362   1055   -194   -118    -55       C  
ATOM    385  C   ASN A  56      31.783  41.915  16.503  1.00  9.87           C  
ANISOU  385  C   ASN A  56     1392   1336   1021   -229   -107    -78       C  
ATOM    386  O   ASN A  56      31.389  40.883  17.043  1.00 11.27           O  
ANISOU  386  O   ASN A  56     1562   1511   1208   -252   -105    -92       O  
ATOM    387  CB  ASN A  56      32.577  43.574  18.161  1.00  9.99           C  
ANISOU  387  CB  ASN A  56     1359   1344   1093   -167    -81    -54       C  
ATOM    388  CG  ASN A  56      32.533  44.998  18.612  1.00 10.19           C  
ANISOU  388  CG  ASN A  56     1362   1374   1136   -134    -88    -35       C  
ATOM    389  ND2 ASN A  56      32.341  45.220  19.898  1.00 10.02           N  
ANISOU  389  ND2 ASN A  56     1307   1355   1146   -117    -83    -33       N  
ATOM    390  OD1 ASN A  56      32.635  45.906  17.785  1.00 11.59           O  
ANISOU  390  OD1 ASN A  56     1557   1552   1296   -124    -99    -21       O  
ATOM    391  N   ALA A  57      32.466  41.922  15.365  1.00  9.81           N  
ANISOU  391  N   ALA A  57     1433   1315    979   -233    -97    -83       N  
ATOM    392  CA  ALA A  57      33.098  40.719  14.846  1.00 10.01           C  
ANISOU  392  CA  ALA A  57     1508   1313    981   -254    -71   -106       C  
ATOM    393  C   ALA A  57      34.375  40.451  15.638  1.00  9.29           C  
ANISOU  393  C   ALA A  57     1418   1193    918   -229    -22   -110       C  
ATOM    394  O   ALA A  57      34.843  41.288  16.411  1.00  9.90           O  
ANISOU  394  O   ALA A  57     1463   1273   1027   -201    -11    -95       O  
ATOM    395  CB  ALA A  57      33.376  40.858  13.353  1.00 12.22           C  
ANISOU  395  CB  ALA A  57     1841   1590   1210   -263    -74   -109       C  
ATOM    396  N   ALA A  58      34.940  39.263  15.442  1.00 10.57           N  
ANISOU  396  N   ALA A  58     1620   1329   1069   -239      7   -130       N  
ATOM    397  CA  ALA A  58      36.087  38.834  16.228  1.00 10.83           C  
ANISOU  397  CA  ALA A  58     1649   1336   1128   -214     51   -133       C  
ATOM    398  C   ALA A  58      37.282  39.754  16.033  1.00 10.27           C  
ANISOU  398  C   ALA A  58     1573   1265   1064   -184     79   -118       C  
ATOM    399  O   ALA A  58      37.603  40.172  14.919  1.00 11.32           O  
ANISOU  399  O   ALA A  58     1735   1399   1166   -184     84   -115       O  
ATOM    400  CB  ALA A  58      36.464  37.405  15.846  1.00 12.78           C  
ANISOU  400  CB  ALA A  58     1950   1552   1356   -226     79   -156       C  
ATOM    401  N   ALA A  59      37.969  40.048  17.135  1.00  9.87           N  
ANISOU  401  N   ALA A  59     1485   1212   1052   -160     96   -108       N  
ATOM    402  CA  ALA A  59      39.156  40.898  17.101  1.00 10.23           C  
ANISOU  402  CA  ALA A  59     1519   1259   1109   -137    121    -92       C  
ATOM    403  C   ALA A  59      40.297  40.196  16.378  1.00 10.25           C  
ANISOU  403  C   ALA A  59     1555   1244   1095   -126    166   -100       C  
ATOM    404  O   ALA A  59      40.395  38.964  16.380  1.00 10.79           O  
ANISOU  404  O   ALA A  59     1650   1294   1157   -125    184   -117       O  
ATOM    405  CB  ALA A  59      39.579  41.270  18.521  1.00 10.99           C  
ANISOU  405  CB  ALA A  59     1569   1358   1248   -119    123    -82       C  
ATOM    406  N   THR A  60      41.190  40.999  15.783  1.00 10.77           N  
ANISOU  406  N   THR A  60     1621   1317   1155   -116    187    -86       N  
ATOM    407  CA  THR A  60      42.243  40.498  14.914  1.00 11.70           C  
ANISOU  407  CA  THR A  60     1770   1425   1252   -104    235    -90       C  
ATOM    408  C   THR A  60      43.560  41.220  15.178  1.00 10.29           C  
ANISOU  408  C   THR A  60     1554   1256   1098    -86    265    -70       C  
ATOM    409  O   THR A  60      43.599  42.300  15.770  1.00 10.98           O  
ANISOU  409  O   THR A  60     1605   1356   1211    -90    246    -53       O  
ATOM    410  CB  THR A  60      41.887  40.783  13.453  1.00 12.77           C  
ANISOU  410  CB  THR A  60     1954   1562   1337   -121    231    -93       C  
ATOM    411  CG2 THR A  60      40.601  40.090  13.045  1.00 13.65           C  
ANISOU  411  CG2 THR A  60     2102   1668   1418   -146    196   -113       C  
ATOM    412  OG1 THR A  60      41.761  42.215  13.321  1.00 12.99           O  
ANISOU  412  OG1 THR A  60     1961   1606   1368   -127    210    -70       O  
ATOM    413  N   GLN A  61      44.641  40.627  14.660  1.00 11.42           N  
ANISOU  413  N   GLN A  61     1711   1393   1233    -67    316    -71       N  
ATOM    414  CA  GLN A  61      45.922  41.323  14.642  1.00 11.18           C  
ANISOU  414  CA  GLN A  61     1646   1379   1222    -55    349    -50       C  
ATOM    415  C   GLN A  61      45.812  42.660  13.926  1.00 11.07           C  
ANISOU  415  C   GLN A  61     1638   1377   1191    -77    337    -32       C  
ATOM    416  O   GLN A  61      46.447  43.641  14.324  1.00 12.15           O  
ANISOU  416  O   GLN A  61     1736   1526   1354    -82    338    -11       O  
ATOM    417  CB  GLN A  61      46.985  40.454  13.969  1.00 12.48           C  
ANISOU  417  CB  GLN A  61     1830   1540   1373    -29    409    -54       C  
ATOM    418  CG  GLN A  61      48.373  41.057  14.010  1.00 12.53           C  
ANISOU  418  CG  GLN A  61     1790   1569   1403    -16    447    -29       C  
ATOM    419  CD  GLN A  61      48.907  41.108  15.420  1.00 11.74           C  
ANISOU  419  CD  GLN A  61     1624   1481   1355     -4    435    -17       C  
ATOM    420  NE2 GLN A  61      49.067  42.305  15.949  1.00 12.43           N  
ANISOU  420  NE2 GLN A  61     1671   1586   1467    -25    410      2       N  
ATOM    421  OE1 GLN A  61      49.113  40.077  16.052  1.00 13.37           O  
ANISOU  421  OE1 GLN A  61     1824   1680   1577     24    445    -25       O  
ATOM    422  N   ALA A  62      45.018  42.720  12.856  1.00 11.68           N  
ANISOU  422  N   ALA A  62     1767   1448   1223    -92    324    -40       N  
ATOM    423  CA  ALA A  62      44.891  43.955  12.096  1.00 12.29           C  
ANISOU  423  CA  ALA A  62     1857   1532   1279   -110    314    -20       C  
ATOM    424  C   ALA A  62      44.410  45.103  12.974  1.00 11.29           C  
ANISOU  424  C   ALA A  62     1695   1411   1184   -120    271     -5       C  
ATOM    425  O   ALA A  62      44.852  46.246  12.812  1.00 12.01           O  
ANISOU  425  O   ALA A  62     1776   1506   1280   -129    275     18       O  
ATOM    426  CB  ALA A  62      43.955  43.764  10.905  1.00 13.02           C  
ANISOU  426  CB  ALA A  62     2011   1620   1316   -123    296    -31       C  
ATOM    427  N   LEU A  63      43.495  44.833  13.903  1.00 10.83           N  
ANISOU  427  N   LEU A  63     1619   1351   1146   -119    232    -17       N  
ATOM    428  CA  LEU A  63      43.055  45.876  14.829  1.00 10.64           C  
ANISOU  428  CA  LEU A  63     1563   1329   1151   -122    196     -4       C  
ATOM    429  C   LEU A  63      44.223  46.385  15.662  1.00  9.94           C  
ANISOU  429  C   LEU A  63     1432   1243   1101   -120    216      9       C  
ATOM    430  O   LEU A  63      44.423  47.593  15.802  1.00 10.58           O  
ANISOU  430  O   LEU A  63     1504   1322   1193   -130    206     27       O  
ATOM    431  CB  LEU A  63      41.948  45.356  15.749  1.00 10.40           C  
ANISOU  431  CB  LEU A  63     1518   1299   1136   -119    160    -19       C  
ATOM    432  CG  LEU A  63      41.623  46.291  16.920  1.00 10.24           C  
ANISOU  432  CG  LEU A  63     1463   1280   1149   -116    132    -10       C  
ATOM    433  CD1 LEU A  63      41.015  47.613  16.454  1.00 10.32           C  
ANISOU  433  CD1 LEU A  63     1488   1288   1147   -120    106      7       C  
ATOM    434  CD2 LEU A  63      40.749  45.587  17.931  1.00 11.16           C  
ANISOU  434  CD2 LEU A  63     1560   1398   1282   -110    109    -25       C  
ATOM    435  N   PHE A  64      44.988  45.474  16.257  1.00 10.24           N  
ANISOU  435  N   PHE A  64     1445   1285   1161   -106    241      1       N  
ATOM    436  CA  PHE A  64      46.068  45.885  17.150  1.00 10.58           C  
ANISOU  436  CA  PHE A  64     1441   1337   1241   -105    252     14       C  
ATOM    437  C   PHE A  64      47.169  46.607  16.399  1.00 10.93           C  
ANISOU  437  C   PHE A  64     1480   1390   1282   -117    285     35       C  
ATOM    438  O   PHE A  64      47.740  47.572  16.918  1.00 10.63           O  
ANISOU  438  O   PHE A  64     1414   1357   1268   -133    279     51       O  
ATOM    439  CB  PHE A  64      46.541  44.684  17.967  1.00 10.10           C  
ANISOU  439  CB  PHE A  64     1354   1280   1202    -83    267      4       C  
ATOM    440  CG  PHE A  64      45.577  44.324  19.061  1.00  9.58           C  
ANISOU  440  CG  PHE A  64     1283   1208   1151    -78    230     -9       C  
ATOM    441  CD1 PHE A  64      44.434  43.593  18.797  1.00 10.60           C  
ANISOU  441  CD1 PHE A  64     1444   1326   1259    -77    216    -27       C  
ATOM    442  CD2 PHE A  64      45.798  44.760  20.355  1.00 11.41           C  
ANISOU  442  CD2 PHE A  64     1477   1445   1413    -78    210     -4       C  
ATOM    443  CE1 PHE A  64      43.534  43.305  19.811  1.00 10.87           C  
ANISOU  443  CE1 PHE A  64     1468   1357   1306    -76    186    -36       C  
ATOM    444  CE2 PHE A  64      44.925  44.464  21.369  1.00 12.43           C  
ANISOU  444  CE2 PHE A  64     1602   1569   1552    -73    181    -14       C  
ATOM    445  CZ  PHE A  64      43.786  43.740  21.099  1.00 12.11           C  
ANISOU  445  CZ  PHE A  64     1588   1519   1492    -72    171    -29       C  
ATOM    446  N   ASP A  65      47.450  46.193  15.164  1.00 10.90           N  
ANISOU  446  N   ASP A  65     1509   1388   1246   -114    321     35       N  
ATOM    447  CA  ASP A  65      48.398  46.931  14.347  1.00 11.40           C  
ANISOU  447  CA  ASP A  65     1572   1460   1301   -128    356     57       C  
ATOM    448  C   ASP A  65      47.909  48.353  14.117  1.00 11.43           C  
ANISOU  448  C   ASP A  65     1594   1453   1296   -155    327     73       C  
ATOM    449  O   ASP A  65      48.692  49.311  14.160  1.00 12.26           O  
ANISOU  449  O   ASP A  65     1680   1562   1417   -176    339     95       O  
ATOM    450  CB  ASP A  65      48.568  46.227  13.004  1.00 12.34           C  
ANISOU  450  CB  ASP A  65     1733   1579   1376   -117    398     51       C  
ATOM    451  CG  ASP A  65      49.313  44.912  13.092  1.00 13.68           C  
ANISOU  451  CG  ASP A  65     1888   1755   1553    -87    440     39       C  
ATOM    452  OD1 ASP A  65      49.892  44.582  14.143  1.00 14.39           O  
ANISOU  452  OD1 ASP A  65     1928   1856   1684    -73    441     41       O  
ATOM    453  OD2 ASP A  65      49.329  44.192  12.065  1.00 17.81           O1-
ANISOU  453  OD2 ASP A  65     2456   2273   2038    -74    474     28       O1-
ATOM    454  N   ALA A  66      46.601  48.506  13.874  1.00 11.05           N  
ANISOU  454  N   ALA A  66     1583   1390   1224   -154    289     64       N  
ATOM    455  CA  ALA A  66      46.026  49.824  13.659  1.00 11.94           C  
ANISOU  455  CA  ALA A  66     1718   1490   1327   -170    260     81       C  
ATOM    456  C   ALA A  66      46.105  50.671  14.923  1.00 10.44           C  
ANISOU  456  C   ALA A  66     1495   1294   1179   -178    233     87       C  
ATOM    457  O   ALA A  66      46.378  51.877  14.843  1.00 11.59           O  
ANISOU  457  O   ALA A  66     1650   1427   1328   -198    230    106       O  
ATOM    458  CB  ALA A  66      44.582  49.700  13.171  1.00 12.05           C  
ANISOU  458  CB  ALA A  66     1772   1498   1309   -161    223     71       C  
ATOM    459  N   LEU A  67      45.868  50.074  16.095  1.00 10.38           N  
ANISOU  459  N   LEU A  67     1456   1290   1199   -165    215     69       N  
ATOM    460  CA  LEU A  67      45.968  50.832  17.344  1.00 10.83           C  
ANISOU  460  CA  LEU A  67     1485   1339   1290   -173    190     72       C  
ATOM    461  C   LEU A  67      47.383  51.369  17.535  1.00 10.70           C  
ANISOU  461  C   LEU A  67     1439   1330   1295   -197    215     88       C  
ATOM    462  O   LEU A  67      47.580  52.527  17.919  1.00 11.10           O  
ANISOU  462  O   LEU A  67     1493   1367   1359   -220    200    100       O  
ATOM    463  CB  LEU A  67      45.589  49.939  18.520  1.00 10.33           C  
ANISOU  463  CB  LEU A  67     1394   1283   1248   -154    173     51       C  
ATOM    464  CG  LEU A  67      44.127  49.510  18.569  1.00 10.87           C  
ANISOU  464  CG  LEU A  67     1482   1347   1301   -136    144     36       C  
ATOM    465  CD1 LEU A  67      43.919  48.437  19.611  1.00 12.00           C  
ANISOU  465  CD1 LEU A  67     1599   1498   1463   -121    138     19       C  
ATOM    466  CD2 LEU A  67      43.215  50.686  18.848  1.00 15.47           C  
ANISOU  466  CD2 LEU A  67     2081   1914   1883   -136    110     42       C  
ATOM    467  N   ALA A  68      48.387  50.519  17.301  1.00 11.31           N  
ANISOU  467  N   ALA A  68     1489   1430   1380   -193    252     90       N  
ATOM    468  CA  ALA A  68      49.773  50.946  17.438  1.00 12.10           C  
ANISOU  468  CA  ALA A  68     1550   1546   1503   -216    278    108       C  
ATOM    469  C   ALA A  68      50.112  52.011  16.406  1.00 11.37           C  
ANISOU  469  C   ALA A  68     1485   1444   1392   -247    297    132       C  
ATOM    470  O   ALA A  68      50.754  53.021  16.730  1.00 12.85           O  
ANISOU  470  O   ALA A  68     1657   1627   1597   -281    293    148       O  
ATOM    471  CB  ALA A  68      50.705  49.742  17.310  1.00 12.98           C  
ANISOU  471  CB  ALA A  68     1623   1685   1622   -196    318    107       C  
ATOM    472  N   ASN A  69      49.670  51.826  15.167  1.00 12.04           N  
ANISOU  472  N   ASN A  69     1614   1524   1438   -237    315    134       N  
ATOM    473  CA  ASN A  69      49.952  52.831  14.146  1.00 13.23           C  
ANISOU  473  CA  ASN A  69     1797   1663   1565   -265    335    159       C  
ATOM    474  C   ASN A  69      49.314  54.170  14.481  1.00 12.58           C  
ANISOU  474  C   ASN A  69     1745   1549   1486   -284    295    168       C  
ATOM    475  O   ASN A  69      49.861  55.220  14.134  1.00 14.03           O  
ANISOU  475  O   ASN A  69     1942   1721   1669   -319    307    192       O  
ATOM    476  CB  ASN A  69      49.464  52.352  12.777  1.00 14.19           C  
ANISOU  476  CB  ASN A  69     1968   1784   1637   -248    356    158       C  
ATOM    477  CG  ASN A  69      50.306  51.226  12.220  1.00 29.52           C  
ANISOU  477  CG  ASN A  69     3892   3753   3571   -232    409    154       C  
ATOM    478  ND2 ASN A  69      49.757  50.502  11.251  1.00 35.64           N  
ANISOU  478  ND2 ASN A  69     4713   4527   4303   -212    421    142       N  
ATOM    479  OD1 ASN A  69      51.442  51.014  12.645  1.00 31.95           O  
ANISOU  479  OD1 ASN A  69     4147   4084   3911   -237    438    161       O  
ATOM    480  N   ALA A  70      48.158  54.148  15.136  1.00 11.98           N  
ANISOU  480  N   ALA A  70     1683   1458   1412   -263    250    150       N  
ATOM    481  CA  ALA A  70      47.462  55.366  15.527  1.00 12.14           C  
ANISOU  481  CA  ALA A  70     1734   1445   1434   -270    214    157       C  
ATOM    482  C   ALA A  70      48.103  56.059  16.722  1.00 12.20           C  
ANISOU  482  C   ALA A  70     1714   1443   1479   -297    200    157       C  
ATOM    483  O   ALA A  70      47.738  57.203  17.019  1.00 13.68           O  
ANISOU  483  O   ALA A  70     1933   1597   1668   -309    177    164       O  
ATOM    484  CB  ALA A  70      45.996  55.058  15.854  1.00 13.02           C  
ANISOU  484  CB  ALA A  70     1862   1548   1535   -234    174    138       C  
ATOM    485  N   GLY A  71      49.029  55.407  17.415  1.00 11.99           N  
ANISOU  485  N   GLY A  71     1632   1444   1481   -305    213    150       N  
ATOM    486  CA  GLY A  71      49.738  56.014  18.512  1.00 12.33           C  
ANISOU  486  CA  GLY A  71     1647   1484   1556   -335    198    151       C  
ATOM    487  C   GLY A  71      49.270  55.641  19.897  1.00 11.16           C  
ANISOU  487  C   GLY A  71     1478   1336   1427   -315    163    127       C  
ATOM    488  O   GLY A  71      49.729  56.261  20.870  1.00 12.11           O  
ANISOU  488  O   GLY A  71     1585   1449   1568   -342    143    125       O  
ATOM    489  N   PHE A  72      48.393  54.658  20.030  1.00 10.96           N  
ANISOU  489  N   PHE A  72     1451   1319   1393   -274    154    108       N  
ATOM    490  CA  PHE A  72      48.090  54.142  21.357  1.00 10.04           C  
ANISOU  490  CA  PHE A  72     1310   1209   1294   -256    129     88       C  
ATOM    491  C   PHE A  72      49.281  53.355  21.892  1.00 10.40           C  
ANISOU  491  C   PHE A  72     1299   1290   1364   -263    143     89       C  
ATOM    492  O   PHE A  72      50.069  52.787  21.134  1.00 11.93           O  
ANISOU  492  O   PHE A  72     1469   1507   1557   -264    178    100       O  
ATOM    493  CB  PHE A  72      46.837  53.263  21.302  1.00 10.82           C  
ANISOU  493  CB  PHE A  72     1423   1310   1378   -215    119     71       C  
ATOM    494  CG  PHE A  72      45.575  54.052  21.149  1.00  9.60           C  
ANISOU  494  CG  PHE A  72     1313   1128   1206   -202     95     70       C  
ATOM    495  CD1 PHE A  72      44.942  54.600  22.261  1.00  9.92           C  
ANISOU  495  CD1 PHE A  72     1362   1152   1257   -193     65     58       C  
ATOM    496  CD2 PHE A  72      45.036  54.302  19.893  1.00 10.98           C  
ANISOU  496  CD2 PHE A  72     1523   1295   1355   -196    102     81       C  
ATOM    497  CE1 PHE A  72      43.797  55.347  22.135  1.00 10.08           C  
ANISOU  497  CE1 PHE A  72     1420   1148   1263   -174     46     59       C  
ATOM    498  CE2 PHE A  72      43.880  55.061  19.765  1.00 11.75           C  
ANISOU  498  CE2 PHE A  72     1657   1369   1437   -180     77     83       C  
ATOM    499  CZ  PHE A  72      43.262  55.591  20.885  1.00 10.59           C  
ANISOU  499  CZ  PHE A  72     1514   1206   1304   -166     51     73       C  
ATOM    500  N   THR A  73      49.403  53.332  23.221  1.00  9.84           N  
ANISOU  500  N   THR A  73     1206   1223   1311   -264    116     78       N  
ATOM    501  CA  THR A  73      50.497  52.675  23.930  1.00 10.56           C  
ANISOU  501  CA  THR A  73     1240   1347   1425   -269    120     81       C  
ATOM    502  C   THR A  73      50.093  51.336  24.525  1.00  9.46           C  
ANISOU  502  C   THR A  73     1083   1223   1288   -226    117     66       C  
ATOM    503  O   THR A  73      50.912  50.397  24.589  1.00 10.12           O  
ANISOU  503  O   THR A  73     1125   1336   1384   -213    136     72       O  
ATOM    504  CB  THR A  73      50.967  53.570  25.093  1.00 10.86           C  
ANISOU  504  CB  THR A  73     1268   1379   1479   -303     86     79       C  
ATOM    505  CG2 THR A  73      52.313  53.102  25.646  1.00 11.98           C  
ANISOU  505  CG2 THR A  73     1345   1563   1645   -318     88     90       C  
ATOM    506  OG1 THR A  73      51.045  54.931  24.665  1.00 11.88           O  
ANISOU  506  OG1 THR A  73     1431   1479   1603   -343     83     89       O  
ATOM    507  N   SER A  74      48.850  51.263  25.013  1.00  9.20           N  
ANISOU  507  N   SER A  74     1082   1170   1243   -205     95     49       N  
ATOM    508  CA  SER A  74      48.400  50.163  25.846  1.00  9.07           C  
ANISOU  508  CA  SER A  74     1054   1163   1229   -173     86     35       C  
ATOM    509  C   SER A  74      46.948  49.832  25.525  1.00  9.11           C  
ANISOU  509  C   SER A  74     1096   1151   1215   -149     83     22       C  
ATOM    510  O   SER A  74      46.163  50.723  25.198  1.00  9.50           O  
ANISOU  510  O   SER A  74     1178   1179   1252   -154     71     20       O  
ATOM    511  CB  SER A  74      48.485  50.558  27.329  1.00  9.37           C  
ANISOU  511  CB  SER A  74     1083   1200   1277   -181     53     28       C  
ATOM    512  OG  SER A  74      49.799  50.969  27.677  1.00 10.03           O  
ANISOU  512  OG  SER A  74     1132   1302   1378   -211     48     40       O  
ATOM    513  N   VAL A  75      46.580  48.559  25.672  1.00  8.68           N  
ANISOU  513  N   VAL A  75     1034   1105   1158   -122     91     13       N  
ATOM    514  CA  VAL A  75      45.203  48.121  25.457  1.00  8.33           C  
ANISOU  514  CA  VAL A  75     1017   1049   1097   -105     86      1       C  
ATOM    515  C   VAL A  75      44.710  47.367  26.675  1.00  8.65           C  
ANISOU  515  C   VAL A  75     1049   1094   1144    -87     72     -9       C  
ATOM    516  O   VAL A  75      45.348  46.401  27.117  1.00 10.61           O  
ANISOU  516  O   VAL A  75     1277   1354   1402    -76     83     -8       O  
ATOM    517  CB  VAL A  75      45.089  47.229  24.209  1.00  8.95           C  
ANISOU  517  CB  VAL A  75     1108   1131   1161    -96    112      1       C  
ATOM    518  CG1 VAL A  75      43.673  46.748  24.021  1.00 10.51           C  
ANISOU  518  CG1 VAL A  75     1329   1321   1342    -86    101    -12       C  
ATOM    519  CG2 VAL A  75      45.546  47.990  22.988  1.00 11.62           C  
ANISOU  519  CG2 VAL A  75     1460   1467   1489   -113    127     13       C  
ATOM    520  N   ARG A  76      43.536  47.751  27.175  1.00  7.71           N  
ANISOU  520  N   ARG A  76      946    965   1018    -82     53    -18       N  
ATOM    521  CA  ARG A  76      42.836  46.966  28.178  1.00  7.85           C  
ANISOU  521  CA  ARG A  76      960    986   1036    -66     46    -27       C  
ATOM    522  C   ARG A  76      41.885  46.031  27.460  1.00  7.60           C  
ANISOU  522  C   ARG A  76      940    955    993    -58     55    -33       C  
ATOM    523  O   ARG A  76      41.122  46.449  26.577  1.00  8.22           O  
ANISOU  523  O   ARG A  76     1033   1029   1059    -62     52    -33       O  
ATOM    524  CB  ARG A  76      42.106  47.885  29.152  1.00  7.77           C  
ANISOU  524  CB  ARG A  76      960    968   1024    -63     24    -33       C  
ATOM    525  CG  ARG A  76      41.337  47.176  30.265  1.00  8.23           C  
ANISOU  525  CG  ARG A  76     1015   1031   1080    -47     20    -41       C  
ATOM    526  CD  ARG A  76      40.989  48.151  31.362  1.00  7.64           C  
ANISOU  526  CD  ARG A  76      951    950   1003    -43      3    -47       C  
ATOM    527  NE  ARG A  76      40.164  47.649  32.452  1.00  7.93           N  
ANISOU  527  NE  ARG A  76      988    992   1033    -27      3    -53       N  
ATOM    528  CZ  ARG A  76      38.842  47.724  32.514  1.00  7.13           C  
ANISOU  528  CZ  ARG A  76      891    893    926    -14      5    -57       C  
ATOM    529  NH1 ARG A  76      38.123  48.149  31.487  1.00  7.86           N1+
ANISOU  529  NH1 ARG A  76      987    983   1016    -12      5    -55       N1+
ATOM    530  NH2 ARG A  76      38.244  47.356  33.640  1.00  8.22           N  
ANISOU  530  NH2 ARG A  76     1029   1037   1058     -2      8    -61       N  
ATOM    531  N   ILE A  77      41.968  44.758  27.825  1.00  7.66           N  
ANISOU  531  N   ILE A  77      942    966   1003    -49     67    -36       N  
ATOM    532  CA  ILE A  77      41.218  43.661  27.232  1.00  8.22           C  
ANISOU  532  CA  ILE A  77     1026   1033   1063    -48     77    -43       C  
ATOM    533  C   ILE A  77      40.307  43.130  28.336  1.00  7.61           C  
ANISOU  533  C   ILE A  77      946    957    987    -43     68    -47       C  
ATOM    534  O   ILE A  77      40.682  42.208  29.084  1.00  8.49           O  
ANISOU  534  O   ILE A  77     1055   1067   1104    -34     77    -46       O  
ATOM    535  CB  ILE A  77      42.172  42.559  26.731  1.00  8.56           C  
ANISOU  535  CB  ILE A  77     1073   1073   1107    -41    103    -41       C  
ATOM    536  CG1 ILE A  77      43.176  43.099  25.706  1.00  9.57           C  
ANISOU  536  CG1 ILE A  77     1198   1203   1233    -46    118    -34       C  
ATOM    537  CG2 ILE A  77      41.374  41.397  26.146  1.00  8.87           C  
ANISOU  537  CG2 ILE A  77     1137   1102   1132    -45    112    -51       C  
ATOM    538  CD1 ILE A  77      44.391  42.216  25.509  1.00 11.33           C  
ANISOU  538  CD1 ILE A  77     1413   1428   1463    -30    146    -29       C  
ATOM    539  N   PRO A  78      39.106  43.674  28.488  1.00  7.85           N  
ANISOU  539  N   PRO A  78      978    993   1013    -46     53    -51       N  
ATOM    540  CA  PRO A  78      38.163  43.110  29.459  1.00  8.17           C  
ANISOU  540  CA  PRO A  78     1013   1038   1054    -43     51    -54       C  
ATOM    541  C   PRO A  78      37.804  41.694  29.043  1.00  7.56           C  
ANISOU  541  C   PRO A  78      946    955    970    -53     63    -57       C  
ATOM    542  O   PRO A  78      37.552  41.429  27.863  1.00  8.71           O  
ANISOU  542  O   PRO A  78     1104   1099   1106    -66     65    -62       O  
ATOM    543  CB  PRO A  78      36.962  44.052  29.388  1.00 10.15           C  
ANISOU  543  CB  PRO A  78     1259   1299   1300    -41     36    -54       C  
ATOM    544  CG  PRO A  78      37.146  44.902  28.234  1.00 13.13           C  
ANISOU  544  CG  PRO A  78     1644   1674   1673    -44     29    -51       C  
ATOM    545  CD  PRO A  78      38.568  44.854  27.799  1.00  7.97           C  
ANISOU  545  CD  PRO A  78      997   1010   1022    -48     40    -49       C  
ATOM    546  N   VAL A  79      37.748  40.781  30.021  1.00  7.43           N  
ANISOU  546  N   VAL A  79      930    935    957    -50     72    -56       N  
ATOM    547  CA  VAL A  79      37.412  39.387  29.739  1.00  7.71           C  
ANISOU  547  CA  VAL A  79      983    958    987    -63     85    -60       C  
ATOM    548  C   VAL A  79      36.335  38.942  30.723  1.00  7.59           C  
ANISOU  548  C   VAL A  79      962    949    972    -71     84    -58       C  
ATOM    549  O   VAL A  79      36.562  38.943  31.938  1.00  7.66           O  
ANISOU  549  O   VAL A  79      966    960    985    -57     87    -51       O  
ATOM    550  CB  VAL A  79      38.617  38.437  29.849  1.00  8.01           C  
ANISOU  550  CB  VAL A  79     1037    978   1029    -49    104    -56       C  
ATOM    551  CG1 VAL A  79      38.168  37.014  29.500  1.00  8.51           C  
ANISOU  551  CG1 VAL A  79     1130   1020   1084    -63    118    -62       C  
ATOM    552  CG2 VAL A  79      39.754  38.876  28.950  1.00  9.04           C  
ANISOU  552  CG2 VAL A  79     1167   1107   1161    -39    110    -56       C  
ATOM    553  N   THR A  80      35.185  38.541  30.189  1.00  7.88           N  
ANISOU  553  N   THR A  80      999    991   1002    -96     81    -62       N  
ATOM    554  CA  THR A  80      34.151  37.864  30.956  1.00  7.88           C  
ANISOU  554  CA  THR A  80      994    998   1003   -112     85    -58       C  
ATOM    555  C   THR A  80      34.357  36.364  30.812  1.00  7.79           C  
ANISOU  555  C   THR A  80     1015    959    987   -130    101    -61       C  
ATOM    556  O   THR A  80      34.567  35.865  29.701  1.00  8.76           O  
ANISOU  556  O   THR A  80     1161   1066   1103   -144    103    -70       O  
ATOM    557  CB  THR A  80      32.779  38.288  30.448  1.00  8.22           C  
ANISOU  557  CB  THR A  80     1012   1067   1043   -133     70    -60       C  
ATOM    558  CG2 THR A  80      31.654  37.480  31.077  1.00  9.35           C  
ANISOU  558  CG2 THR A  80     1145   1221   1188   -158     77    -55       C  
ATOM    559  OG1 THR A  80      32.614  39.673  30.763  1.00  7.99           O  
ANISOU  559  OG1 THR A  80      959   1059   1020   -107     60    -56       O  
ATOM    560  N   TRP A  81      34.300  35.637  31.939  1.00  8.03           N  
ANISOU  560  N   TRP A  81     1052    979   1019   -128    115    -52       N  
ATOM    561  CA  TRP A  81      34.635  34.223  31.974  1.00  8.35           C  
ANISOU  561  CA  TRP A  81     1132    985   1055   -138    133    -51       C  
ATOM    562  C   TRP A  81      33.402  33.363  32.222  1.00  8.94           C  
ANISOU  562  C   TRP A  81     1213   1058   1127   -178    139    -49       C  
ATOM    563  O   TRP A  81      33.517  32.131  32.331  1.00  9.54           O  
ANISOU  563  O   TRP A  81     1328   1100   1198   -192    155    -47       O  
ATOM    564  CB  TRP A  81      35.704  33.948  33.041  1.00  8.40           C  
ANISOU  564  CB  TRP A  81     1150    977   1065   -103    145    -39       C  
ATOM    565  CG  TRP A  81      36.967  34.755  32.866  1.00  8.38           C  
ANISOU  565  CG  TRP A  81     1134    980   1068    -68    138    -38       C  
ATOM    566  CD1 TRP A  81      37.180  36.023  33.298  1.00  8.49           C  
ANISOU  566  CD1 TRP A  81     1119   1020   1086    -53    123    -36       C  
ATOM    567  CD2 TRP A  81      38.183  34.354  32.214  1.00  8.46           C  
ANISOU  567  CD2 TRP A  81     1162    972   1081    -47    149    -39       C  
ATOM    568  CE2 TRP A  81      39.082  35.436  32.311  1.00  8.51           C  
ANISOU  568  CE2 TRP A  81     1141    999   1095    -24    137    -36       C  
ATOM    569  CE3 TRP A  81      38.603  33.194  31.560  1.00  9.44           C  
ANISOU  569  CE3 TRP A  81     1323   1062   1200    -45    168    -43       C  
ATOM    570  NE1 TRP A  81      38.448  36.444  32.975  1.00  8.79           N  
ANISOU  570  NE1 TRP A  81     1151   1057   1129    -30    121    -35       N  
ATOM    571  CZ2 TRP A  81      40.364  35.390  31.775  1.00  9.36           C  
ANISOU  571  CZ2 TRP A  81     1248   1100   1207      0    146    -33       C  
ATOM    572  CZ3 TRP A  81      39.878  33.159  31.028  1.00 10.04           C  
ANISOU  572  CZ3 TRP A  81     1403   1132   1281    -14    179    -42       C  
ATOM    573  CH2 TRP A  81      40.743  34.243  31.148  1.00  9.92           C  
ANISOU  573  CH2 TRP A  81     1351   1143   1275      7    168    -36       C  
ATOM    574  N   LEU A  82      32.234  33.991  32.337  1.00  9.06           N  
ANISOU  574  N   LEU A  82     1190   1107   1144   -197    127    -47       N  
ATOM    575  CA  LEU A  82      30.986  33.296  32.594  1.00  9.69           C  
ANISOU  575  CA  LEU A  82     1263   1195   1223   -240    132    -42       C  
ATOM    576  C   LEU A  82      30.770  32.188  31.575  1.00  9.52           C  
ANISOU  576  C   LEU A  82     1278   1145   1193   -283    131    -54       C  
ATOM    577  O   LEU A  82      30.978  32.360  30.374  1.00 10.26           O  
ANISOU  577  O   LEU A  82     1381   1236   1280   -289    117    -68       O  
ATOM    578  CB  LEU A  82      29.827  34.298  32.523  1.00  9.70           C  
ANISOU  578  CB  LEU A  82     1210   1245   1229   -248    116    -40       C  
ATOM    579  CG  LEU A  82      29.804  35.361  33.623  1.00 10.50           C  
ANISOU  579  CG  LEU A  82     1282   1373   1336   -209    121    -30       C  
ATOM    580  CD1 LEU A  82      28.737  36.409  33.302  1.00 11.67           C  
ANISOU  580  CD1 LEU A  82     1380   1565   1490   -207    106    -29       C  
ATOM    581  CD2 LEU A  82      29.568  34.742  34.970  1.00 11.42           C  
ANISOU  581  CD2 LEU A  82     1404   1485   1450   -211    146    -17       C  
ATOM    582  N   GLY A  83      30.346  31.033  32.070  1.00 10.37           N  
ANISOU  582  N   GLY A  83     1412   1231   1299   -316    147    -48       N  
ATOM    583  CA  GLY A  83      30.096  29.890  31.228  1.00 12.28           C  
ANISOU  583  CA  GLY A  83     1697   1439   1531   -363    148    -59       C  
ATOM    584  C   GLY A  83      31.323  29.135  30.787  1.00 11.51           C  
ANISOU  584  C   GLY A  83     1663   1287   1424   -340    163    -69       C  
ATOM    585  O   GLY A  83      31.188  28.135  30.070  1.00 13.82           O  
ANISOU  585  O   GLY A  83     2004   1543   1705   -376    166    -82       O  
ATOM    586  N   HIS A  84      32.511  29.546  31.208  1.00 10.70           N  
ANISOU  586  N   HIS A  84     1562   1178   1327   -282    172    -63       N  
ATOM    587  CA  HIS A  84      33.762  28.901  30.836  1.00 11.07           C  
ANISOU  587  CA  HIS A  84     1658   1179   1368   -249    189    -68       C  
ATOM    588  C   HIS A  84      34.582  28.472  32.044  1.00 12.04           C  
ANISOU  588  C   HIS A  84     1796   1282   1497   -208    209    -48       C  
ATOM    589  O   HIS A  84      35.792  28.226  31.911  1.00 12.75           O  
ANISOU  589  O   HIS A  84     1909   1348   1587   -164    221    -47       O  
ATOM    590  CB  HIS A  84      34.589  29.816  29.940  1.00 11.76           C  
ANISOU  590  CB  HIS A  84     1730   1284   1456   -216    180    -79       C  
ATOM    591  CG  HIS A  84      33.999  30.001  28.592  1.00 11.50           C  
ANISOU  591  CG  HIS A  84     1702   1259   1410   -252    163    -98       C  
ATOM    592  CD2 HIS A  84      33.780  31.109  27.857  1.00 14.38           C  
ANISOU  592  CD2 HIS A  84     2032   1661   1773   -253    141   -104       C  
ATOM    593  ND1 HIS A  84      33.604  28.938  27.805  1.00 18.32           N  
ANISOU  593  ND1 HIS A  84     2617   2088   2257   -293    167   -114       N  
ATOM    594  CE1 HIS A  84      33.150  29.391  26.649  1.00 19.06           C  
ANISOU  594  CE1 HIS A  84     2705   2201   2337   -319    146   -129       C  
ATOM    595  NE2 HIS A  84      33.247  30.703  26.654  1.00 16.35           N  
ANISOU  595  NE2 HIS A  84     2308   1900   2002   -293    130   -122       N  
ATOM    596  N   VAL A  85      33.963  28.375  33.215  1.00 11.80           N  
ANISOU  596  N   VAL A  85     1752   1263   1470   -219    213    -31       N  
ATOM    597  CA  VAL A  85      34.655  27.981  34.438  1.00 11.40           C  
ANISOU  597  CA  VAL A  85     1717   1196   1420   -181    228    -10       C  
ATOM    598  C   VAL A  85      33.904  26.821  35.077  1.00 11.89           C  
ANISOU  598  C   VAL A  85     1817   1227   1475   -218    246      3       C  
ATOM    599  O   VAL A  85      32.679  26.883  35.255  1.00 13.23           O  
ANISOU  599  O   VAL A  85     1965   1418   1645   -267    243      4       O  
ATOM    600  CB  VAL A  85      34.783  29.155  35.427  1.00 11.35           C  
ANISOU  600  CB  VAL A  85     1659   1235   1418   -152    216      2       C  
ATOM    601  CG1 VAL A  85      35.514  28.709  36.672  1.00 11.86           C  
ANISOU  601  CG1 VAL A  85     1744   1284   1477   -115    227     25       C  
ATOM    602  CG2 VAL A  85      35.521  30.312  34.778  1.00 13.10           C  
ANISOU  602  CG2 VAL A  85     1847   1483   1646   -122    198     -9       C  
ATOM    603  N   GLY A  86      34.627  25.759  35.409  1.00 11.49           N  
ANISOU  603  N   GLY A  86     1822   1126   1419   -196    266     14       N  
ATOM    604  CA  GLY A  86      34.041  24.580  36.000  1.00 13.04           C  
ANISOU  604  CA  GLY A  86     2065   1282   1607   -229    286     28       C  
ATOM    605  C   GLY A  86      33.681  24.781  37.464  1.00 13.24           C  
ANISOU  605  C   GLY A  86     2070   1331   1629   -224    291     55       C  
ATOM    606  O   GLY A  86      33.792  25.861  38.041  1.00 13.31           O  
ANISOU  606  O   GLY A  86     2028   1388   1640   -198    278     59       O  
ATOM    607  N   GLU A  87      33.251  23.682  38.072  1.00 14.79           N  
ANISOU  607  N   GLU A  87     2314   1488   1817   -252    313     72       N  
ATOM    608  CA  GLU A  87      32.767  23.692  39.441  1.00 15.41           C  
ANISOU  608  CA  GLU A  87     2383   1584   1886   -256    325     99       C  
ATOM    609  C   GLU A  87      33.924  23.644  40.438  1.00 13.75           C  
ANISOU  609  C   GLU A  87     2192   1364   1667   -188    327    122       C  
ATOM    610  O   GLU A  87      35.074  23.329  40.104  1.00 14.16           O  
ANISOU  610  O   GLU A  87     2271   1386   1721   -140    324    122       O  
ATOM    611  CB  GLU A  87      31.844  22.492  39.686  1.00 21.70           C  
ANISOU  611  CB  GLU A  87     3228   2341   2677   -318    349    112       C  
ATOM    612  CG  GLU A  87      30.585  22.491  38.834  1.00 34.96           C  
ANISOU  612  CG  GLU A  87     4883   4038   4364   -395    343     93       C  
ATOM    613  CD  GLU A  87      29.695  23.685  39.116  1.00 44.15           C  
ANISOU  613  CD  GLU A  87     5963   5278   5535   -409    332     92       C  
ATOM    614  OE1 GLU A  87      29.703  24.180  40.263  1.00 58.83           O  
ANISOU  614  OE1 GLU A  87     7798   7166   7387   -380    341    111       O  
ATOM    615  OE2 GLU A  87      28.992  24.133  38.185  1.00 61.08           O1-
ANISOU  615  OE2 GLU A  87     8067   7452   7688   -447    314     71       O1-
ATOM    616  N   ALA A  88      33.596  23.955  41.692  1.00 15.13           N  
ANISOU  616  N   ALA A  88     2352   1567   1831   -183    332    144       N  
ATOM    617  CA  ALA A  88      34.550  23.822  42.777  1.00 14.66           C  
ANISOU  617  CA  ALA A  88     2314   1499   1756   -126    332    170       C  
ATOM    618  C   ALA A  88      34.968  22.358  42.921  1.00 14.51           C  
ANISOU  618  C   ALA A  88     2373   1410   1729   -118    352    191       C  
ATOM    619  O   ALA A  88      34.197  21.449  42.593  1.00 16.81           O  
ANISOU  619  O   ALA A  88     2705   1662   2020   -170    373    191       O  
ATOM    620  CB  ALA A  88      33.907  24.288  44.085  1.00 16.50           C  
ANISOU  620  CB  ALA A  88     2528   1769   1971   -134    338    189       C  
ATOM    621  N   PRO A  89      36.176  22.089  43.437  1.00 14.99           N  
ANISOU  621  N   PRO A  89     2460   1454   1783    -53    347    211       N  
ATOM    622  CA  PRO A  89      37.149  23.055  43.947  1.00 15.44           C  
ANISOU  622  CA  PRO A  89     2473   1555   1836      5    319    216       C  
ATOM    623  C   PRO A  89      38.136  23.576  42.903  1.00 13.99           C  
ANISOU  623  C   PRO A  89     2259   1383   1674     41    300    194       C  
ATOM    624  O   PRO A  89      38.903  24.490  43.191  1.00 16.07           O  
ANISOU  624  O   PRO A  89     2479   1688   1939     79    275    194       O  
ATOM    625  CB  PRO A  89      37.914  22.241  44.996  1.00 17.54           C  
ANISOU  625  CB  PRO A  89     2789   1792   2083     53    324    254       C  
ATOM    626  CG  PRO A  89      37.913  20.862  44.421  1.00 19.77           C  
ANISOU  626  CG  PRO A  89     3142   2001   2371     45    350    260       C  
ATOM    627  CD  PRO A  89      36.562  20.699  43.766  1.00 16.72           C  
ANISOU  627  CD  PRO A  89     2758   1605   1991    -35    368    238       C  
ATOM    628  N   ASP A  90      38.144  22.985  41.711  1.00 13.83           N  
ANISOU  628  N   ASP A  90     2262   1324   1667     28    313    176       N  
ATOM    629  CA  ASP A  90      39.183  23.330  40.751  1.00 15.15           C  
ANISOU  629  CA  ASP A  90     2409   1498   1851     68    302    160       C  
ATOM    630  C   ASP A  90      38.858  24.579  39.947  1.00 12.09           C  
ANISOU  630  C   ASP A  90     1960   1159   1476     42    284    129       C  
ATOM    631  O   ASP A  90      39.778  25.278  39.524  1.00 13.10           O  
ANISOU  631  O   ASP A  90     2051   1313   1615     78    268    122       O  
ATOM    632  CB  ASP A  90      39.427  22.153  39.808  1.00 15.61           C  
ANISOU  632  CB  ASP A  90     2528   1490   1914     72    327    153       C  
ATOM    633  CG  ASP A  90      39.918  20.919  40.541  1.00 33.33           C  
ANISOU  633  CG  ASP A  90     4838   3680   4147    109    346    186       C  
ATOM    634  OD1 ASP A  90      40.896  21.036  41.311  1.00 25.63           O  
ANISOU  634  OD1 ASP A  90     3850   2722   3169    170    334    212       O  
ATOM    635  OD2 ASP A  90      39.315  19.842  40.360  1.00 38.51           O1-
ANISOU  635  OD2 ASP A  90     5561   4276   4795     76    371    187       O1-
ATOM    636  N   TYR A  91      37.583  24.873  39.725  1.00 11.68           N  
ANISOU  636  N   TYR A  91     1894   1122   1424    -18    285    114       N  
ATOM    637  CA  TYR A  91      37.180  26.018  38.919  1.00 10.81           C  
ANISOU  637  CA  TYR A  91     1729   1053   1323    -41    268     87       C  
ATOM    638  C   TYR A  91      37.987  26.075  37.622  1.00 10.28           C  
ANISOU  638  C   TYR A  91     1663    975   1268    -20    266     68       C  
ATOM    639  O   TYR A  91      38.554  27.100  37.257  1.00 10.55           O  
ANISOU  639  O   TYR A  91     1652   1045   1311      1    249     58       O  
ATOM    640  CB  TYR A  91      37.314  27.313  39.715  1.00 11.13           C  
ANISOU  640  CB  TYR A  91     1716   1150   1363    -22    246     91       C  
ATOM    641  CG  TYR A  91      36.503  27.341  40.990  1.00 10.98           C  
ANISOU  641  CG  TYR A  91     1698   1146   1328    -39    252    108       C  
ATOM    642  CD1 TYR A  91      35.143  27.564  40.949  1.00 11.05           C  
ANISOU  642  CD1 TYR A  91     1690   1174   1337    -89    260    100       C  
ATOM    643  CD2 TYR A  91      37.105  27.165  42.229  1.00 11.83           C  
ANISOU  643  CD2 TYR A  91     1821   1253   1420     -3    250    133       C  
ATOM    644  CE1 TYR A  91      34.386  27.623  42.114  1.00 13.20           C  
ANISOU  644  CE1 TYR A  91     1959   1463   1593   -103    272    116       C  
ATOM    645  CE2 TYR A  91      36.365  27.232  43.400  1.00 12.91           C  
ANISOU  645  CE2 TYR A  91     1962   1405   1537    -18    259    149       C  
ATOM    646  CZ  TYR A  91      35.007  27.458  43.332  1.00 12.09           C  
ANISOU  646  CZ  TYR A  91     1840   1319   1434    -67    272    140       C  
ATOM    647  OH  TYR A  91      34.271  27.522  44.499  1.00 14.93           O  
ANISOU  647  OH  TYR A  91     2203   1697   1774    -79    287    156       O  
ATOM    648  N   THR A  92      38.014  24.954  36.909  1.00 10.60           N  
ANISOU  648  N   THR A  92     1759    963   1307    -29    286     62       N  
ATOM    649  CA  THR A  92      38.872  24.837  35.737  1.00 11.07           C  
ANISOU  649  CA  THR A  92     1830   1005   1372     -2    292     46       C  
ATOM    650  C   THR A  92      38.350  25.715  34.613  1.00 10.69           C  
ANISOU  650  C   THR A  92     1747    987   1327    -38    278     17       C  
ATOM    651  O   THR A  92      37.162  25.662  34.259  1.00 11.51           O  
ANISOU  651  O   THR A  92     1855   1093   1427    -96    274      4       O  
ATOM    652  CB  THR A  92      38.924  23.379  35.276  1.00 11.85           C  
ANISOU  652  CB  THR A  92     2007   1032   1462     -5    320     44       C  
ATOM    653  CG2 THR A  92      39.778  23.236  34.030  1.00 12.49           C  
ANISOU  653  CG2 THR A  92     2106   1094   1546     25    332     25       C  
ATOM    654  OG1 THR A  92      39.458  22.597  36.341  1.00 13.01           O  
ANISOU  654  OG1 THR A  92     2187   1149   1605     35    333     75       O  
ATOM    655  N   ILE A  93      39.239  26.508  34.031  1.00 10.55           N  
ANISOU  655  N   ILE A  93     1696    995   1318     -4    270     10       N  
ATOM    656  CA  ILE A  93      38.870  27.370  32.911  1.00 11.17           C  
ANISOU  656  CA  ILE A  93     1746   1100   1397    -31    257    -14       C  
ATOM    657  C   ILE A  93      38.954  26.583  31.609  1.00 11.20           C  
ANISOU  657  C   ILE A  93     1801   1064   1392    -42    275    -35       C  
ATOM    658  O   ILE A  93      39.950  25.898  31.342  1.00 11.93           O  
ANISOU  658  O   ILE A  93     1928   1123   1483      1    298    -32       O  
ATOM    659  CB  ILE A  93      39.773  28.614  32.841  1.00 10.80           C  
ANISOU  659  CB  ILE A  93     1645   1099   1362      5    242    -12       C  
ATOM    660  CG1 ILE A  93      39.664  29.439  34.119  1.00 12.35           C  
ANISOU  660  CG1 ILE A  93     1798   1332   1563     12    222      4       C  
ATOM    661  CG2 ILE A  93      39.411  29.463  31.624  1.00 11.58           C  
ANISOU  661  CG2 ILE A  93     1723   1220   1459    -22    231    -34       C  
ATOM    662  CD1 ILE A  93      40.635  30.587  34.210  1.00 12.92           C  
ANISOU  662  CD1 ILE A  93     1822   1442   1645     43    205      8       C  
ATOM    663  N  AASP A  94      37.908  26.672  30.779  0.61 11.09           N  
ANISOU  663  N  AASP A  94     1793   1052   1368    -97    265    -56       N  
ATOM    664  N  BASP A  94      37.892  26.687  30.809  0.39 11.97           N  
ANISOU  664  N  BASP A  94     1904   1164   1479    -97    265    -55       N  
ATOM    665  CA AASP A  94      37.917  26.001  29.480  0.61 11.92           C  
ANISOU  665  CA AASP A  94     1952   1120   1458   -114    278    -79       C  
ATOM    666  CA BASP A  94      37.862  26.229  29.431  0.39 10.51           C  
ANISOU  666  CA BASP A  94     1762    951   1279   -116    274    -80       C  
ATOM    667  C  AASP A  94      39.162  26.390  28.685  0.61 12.28           C  
ANISOU  667  C  AASP A  94     1992   1171   1504    -63    291    -85       C  
ATOM    668  C  BASP A  94      39.153  26.603  28.722  0.39 11.09           C  
ANISOU  668  C  BASP A  94     1830   1029   1355    -63    287    -84       C  
ATOM    669  O  AASP A  94      39.446  27.575  28.498  0.61 10.60           O  
ANISOU  669  O  AASP A  94     1724   1004   1299    -52    275    -84       O  
ATOM    670  O  BASP A  94      39.515  27.786  28.640  0.39 12.70           O  
ANISOU  670  O  BASP A  94     1979   1280   1569    -47    272    -80       O  
ATOM    671  CB AASP A  94      36.667  26.404  28.697  0.61 12.92           C  
ANISOU  671  CB AASP A  94     2067   1269   1574   -179    254    -99       C  
ATOM    672  CB BASP A  94      36.667  26.890  28.743  0.39 10.03           C  
ANISOU  672  CB BASP A  94     1676    923   1211   -175    246    -97       C  
ATOM    673  CG AASP A  94      36.703  25.912  27.269  0.61 19.38           C  
ANISOU  673  CG AASP A  94     2938   2056   2370   -198    262   -126       C  
ATOM    674  CG BASP A  94      36.446  26.379  27.339  0.39  9.27           C  
ANISOU  674  CG BASP A  94     1630    798   1092   -205    250   -124       C  
ATOM    675  OD1AASP A  94      36.457  24.704  27.074  0.61 16.18           O  
ANISOU  675  OD1AASP A  94     2600   1596   1950   -222    277   -136       O  
ATOM    676  OD2AASP A  94      36.990  26.731  26.355  0.61 16.05           O1-
ANISOU  676  OD2AASP A  94     2495   1662   1942   -189    253   -137       O1-
ATOM    677  OD1BASP A  94      37.398  26.424  26.523  0.39 14.08           O  
ANISOU  677  OD1BASP A  94     2259   1396   1694   -170    265   -134       O  
ATOM    678  OD2BASP A  94      35.312  25.946  27.041  0.39 14.62           O1-
ANISOU  678  OD2BASP A  94     2328   1469   1760   -267    236   -135       O1-
ATOM    679  N  AGLU A  95      39.889  25.390  28.177  0.61 12.51           N  
ANISOU  679  N  AGLU A  95     2081   1150   1524    -34    322    -91       N  
ATOM    680  N  BGLU A  95      39.849  25.590  28.209  0.39 11.36           N  
ANISOU  680  N  BGLU A  95     1923   1013   1379    -36    318    -90       N  
ATOM    681  CA AGLU A  95      41.214  25.687  27.636  0.61 10.66           C  
ANISOU  681  CA AGLU A  95     1834    923   1294     24    342    -89       C  
ATOM    682  CA BGLU A  95      41.193  25.799  27.684  0.39 13.26           C  
ANISOU  682  CA BGLU A  95     2156   1257   1624     23    339    -88       C  
ATOM    683  C  AGLU A  95      41.129  26.502  26.350  0.61 10.04           C  
ANISOU  683  C  AGLU A  95     1741    871   1203      5    334   -110       C  
ATOM    684  C  BGLU A  95      41.170  26.466  26.316  0.39 12.48           C  
ANISOU  684  C  BGLU A  95     2053   1178   1512      6    336   -111       C  
ATOM    685  O  AGLU A  95      41.987  27.360  26.093  0.61 12.06           O  
ANISOU  685  O  AGLU A  95     1953   1161   1468     38    337   -104       O  
ATOM    686  O  BGLU A  95      42.110  27.201  25.978  0.39 10.05           O  
ANISOU  686  O  BGLU A  95     1708    900   1212     43    343   -105       O  
ATOM    687  CB AGLU A  95      42.018  24.408  27.418  0.61 11.26           C  
ANISOU  687  CB AGLU A  95     1977    939   1363     69    382    -89       C  
ATOM    688  CB BGLU A  95      41.959  24.474  27.673  0.39 13.84           C  
ANISOU  688  CB BGLU A  95     2295   1271   1693     68    377    -84       C  
ATOM    689  CG AGLU A  95      43.510  24.669  27.425  0.61 11.88           C  
ANISOU  689  CG AGLU A  95     2023   1036   1457    144    403    -72       C  
ATOM    690  CG BGLU A  95      42.138  23.853  29.067  0.39 14.77           C  
ANISOU  690  CG BGLU A  95     2417   1371   1823     95    380    -56       C  
ATOM    691  CD AGLU A  95      43.992  25.137  28.783  0.61 11.32           C  
ANISOU  691  CD AGLU A  95     1891   1001   1409    175    385    -40       C  
ATOM    692  CD BGLU A  95      40.840  23.314  29.654  0.39 14.96           C  
ANISOU  692  CD BGLU A  95     2473   1373   1841     34    367    -57       C  
ATOM    693  OE1AGLU A  95      43.647  24.491  29.794  0.61 11.45           O  
ANISOU  693  OE1AGLU A  95     1929    995   1428    174    381    -25       O  
ATOM    694  OE2AGLU A  95      44.699  26.169  28.839  0.61 13.46           O1-
ANISOU  694  OE2AGLU A  95     2096   1324   1696    197    374    -30       O1-
ATOM    695  OE1BGLU A  95      39.791  23.412  28.990  0.39 25.31           O  
ANISOU  695  OE1BGLU A  95     3795   2683   3138    -29    353    -80       O  
ATOM    696  OE2BGLU A  95      40.855  22.814  30.777  0.39 11.94           O1-
ANISOU  696  OE2BGLU A  95     2098    974   1463     49    370    -33       O1-
ATOM    697  N   THR A  96      40.134  26.227  25.506  1.00 10.92           N  
ANISOU  697  N   THR A  96     1892    965   1291    -51    325   -135       N  
ATOM    698  CA  THR A  96      39.998  26.974  24.262  1.00 10.54           C  
ANISOU  698  CA  THR A  96     1836    941   1226    -70    315   -153       C  
ATOM    699  C   THR A  96      39.686  28.441  24.527  1.00 10.01           C  
ANISOU  699  C   THR A  96     1692    937   1174    -81    282   -142       C  
ATOM    700  O   THR A  96      40.197  29.320  23.826  1.00 10.26           O  
ANISOU  700  O   THR A  96     1699    996   1203    -67    281   -144       O  
ATOM    701  CB  THR A  96      38.942  26.339  23.373  1.00 11.60           C  
ANISOU  701  CB  THR A  96     2030   1048   1331   -131    306   -181       C  
ATOM    702  CG2 THR A  96      38.628  27.196  22.163  1.00 14.40           C  
ANISOU  702  CG2 THR A  96     2374   1434   1664   -157    286   -197       C  
ATOM    703  OG1 THR A  96      39.438  25.067  22.923  1.00 14.06           O  
ANISOU  703  OG1 THR A  96     2424   1294   1624   -114    342   -195       O  
ATOM    704  N   TYR A  97      38.856  28.738  25.528  1.00 10.02           N  
ANISOU  704  N   TYR A  97     1658    960   1190   -106    256   -130       N  
ATOM    705  CA  TYR A  97      38.599  30.145  25.833  1.00 10.04           C  
ANISOU  705  CA  TYR A  97     1592   1017   1206   -109    228   -120       C  
ATOM    706  C   TYR A  97      39.864  30.830  26.333  1.00  9.47           C  
ANISOU  706  C   TYR A  97     1480    964   1152    -56    237   -103       C  
ATOM    707  O   TYR A  97      40.167  31.965  25.946  1.00  9.62           O  
ANISOU  707  O   TYR A  97     1463   1017   1176    -50    226   -101       O  
ATOM    708  CB  TYR A  97      37.461  30.273  26.833  1.00 10.96           C  
ANISOU  708  CB  TYR A  97     1681   1151   1332   -141    205   -112       C  
ATOM    709  CG  TYR A  97      36.999  31.706  26.974  1.00 10.44           C  
ANISOU  709  CG  TYR A  97     1556   1137   1276   -146    177   -106       C  
ATOM    710  CD1 TYR A  97      36.454  32.385  25.889  1.00 11.60           C  
ANISOU  710  CD1 TYR A  97     1695   1304   1409   -170    158   -117       C  
ATOM    711  CD2 TYR A  97      37.122  32.395  28.172  1.00  9.39           C  
ANISOU  711  CD2 TYR A  97     1380   1028   1160   -125    169    -88       C  
ATOM    712  CE1 TYR A  97      36.034  33.697  25.993  1.00 11.12           C  
ANISOU  712  CE1 TYR A  97     1585   1284   1355   -170    133   -110       C  
ATOM    713  CE2 TYR A  97      36.692  33.710  28.286  1.00  9.22           C  
ANISOU  713  CE2 TYR A  97     1312   1046   1145   -128    146    -85       C  
ATOM    714  CZ  TYR A  97      36.147  34.353  27.201  1.00  9.30           C  
ANISOU  714  CZ  TYR A  97     1315   1073   1144   -148    129    -95       C  
ATOM    715  OH  TYR A  97      35.700  35.656  27.251  1.00  9.68           O  
ANISOU  715  OH  TYR A  97     1324   1157   1198   -146    107    -90       O  
ATOM    716  N   LEU A  98      40.608  30.166  27.215  1.00  9.78           N  
ANISOU  716  N   LEU A  98     1526    986   1205    -20    255    -88       N  
ATOM    717  CA  LEU A  98      41.878  30.719  27.669  1.00 10.23           C  
ANISOU  717  CA  LEU A  98     1544   1064   1279     29    262    -70       C  
ATOM    718  C   LEU A  98      42.831  30.930  26.502  1.00 10.12           C  
ANISOU  718  C   LEU A  98     1533   1052   1260     52    284    -77       C  
ATOM    719  O   LEU A  98      43.552  31.937  26.452  1.00 10.52           O  
ANISOU  719  O   LEU A  98     1537   1138   1322     67    279    -67       O  
ATOM    720  CB  LEU A  98      42.456  29.800  28.740  1.00 11.60           C  
ANISOU  720  CB  LEU A  98     1729   1215   1463     65    276    -52       C  
ATOM    721  CG  LEU A  98      43.694  30.252  29.495  1.00 12.55           C  
ANISOU  721  CG  LEU A  98     1804   1363   1603    112    275    -29       C  
ATOM    722  CD1 LEU A  98      43.512  31.627  30.114  1.00 12.50           C  
ANISOU  722  CD1 LEU A  98     1741   1403   1606     96    241    -23       C  
ATOM    723  CD2 LEU A  98      44.036  29.232  30.567  1.00 15.08           C  
ANISOU  723  CD2 LEU A  98     2144   1658   1927    145    284     -9       C  
ATOM    724  N   ASN A  99      42.837  30.004  25.538  1.00 10.12           N  
ANISOU  724  N   ASN A  99     1590   1014   1240     51    310    -93       N  
ATOM    725  CA  ASN A  99      43.639  30.201  24.343  1.00 10.56           C  
ANISOU  725  CA  ASN A  99     1655   1072   1285     71    335   -101       C  
ATOM    726  C   ASN A  99      43.211  31.453  23.588  1.00  9.83           C  
ANISOU  726  C   ASN A  99     1536   1016   1184     38    313   -108       C  
ATOM    727  O   ASN A  99      44.061  32.188  23.067  1.00 10.92           O  
ANISOU  727  O   ASN A  99     1646   1177   1325     57    325   -102       O  
ATOM    728  CB  ASN A  99      43.536  28.979  23.438  1.00 10.77           C  
ANISOU  728  CB  ASN A  99     1760   1048   1285     71    366   -123       C  
ATOM    729  CG  ASN A  99      44.409  29.116  22.216  1.00 11.98           C  
ANISOU  729  CG  ASN A  99     1927   1202   1422     96    399   -131       C  
ATOM    730  ND2 ASN A  99      43.829  29.570  21.120  1.00 12.66           N  
ANISOU  730  ND2 ASN A  99     2034   1296   1482     59    390   -150       N  
ATOM    731  OD1 ASN A  99      45.605  28.818  22.258  1.00 13.12           O  
ANISOU  731  OD1 ASN A  99     2063   1344   1578    151    435   -119       O  
ATOM    732  N   ARG A 100      41.904  31.703  23.478  1.00 10.15           N  
ANISOU  732  N   ARG A 100     1583   1061   1212    -11    281   -120       N  
ATOM    733  CA  ARG A 100      41.446  32.906  22.785  1.00  9.72           C  
ANISOU  733  CA  ARG A 100     1504   1039   1149    -37    257   -123       C  
ATOM    734  C   ARG A 100      41.951  34.166  23.488  1.00  9.65           C  
ANISOU  734  C   ARG A 100     1432   1069   1166    -21    243   -103       C  
ATOM    735  O   ARG A 100      42.383  35.126  22.838  1.00  9.79           O  
ANISOU  735  O   ARG A 100     1432   1108   1181    -19    243    -99       O  
ATOM    736  CB  ARG A 100      39.923  32.930  22.680  1.00 10.10           C  
ANISOU  736  CB  ARG A 100     1562   1091   1184    -87    223   -134       C  
ATOM    737  CG  ARG A 100      39.361  34.197  22.053  1.00 10.19           C  
ANISOU  737  CG  ARG A 100     1546   1137   1187   -109    195   -134       C  
ATOM    738  CD  ARG A 100      39.905  34.428  20.650  1.00 10.92           C  
ANISOU  738  CD  ARG A 100     1667   1227   1253   -105    211   -142       C  
ATOM    739  NE  ARG A 100      39.384  35.650  20.053  1.00 10.30           N  
ANISOU  739  NE  ARG A 100     1567   1180   1165   -123    182   -138       N  
ATOM    740  CZ  ARG A 100      39.969  36.297  19.057  1.00 10.52           C  
ANISOU  740  CZ  ARG A 100     1604   1217   1177   -115    194   -136       C  
ATOM    741  NH1 ARG A 100      41.110  35.864  18.541  1.00 11.39           N1+
ANISOU  741  NH1 ARG A 100     1738   1312   1280    -90    235   -138       N1+
ATOM    742  NH2 ARG A 100      39.413  37.411  18.601  1.00 11.04           N  
ANISOU  742  NH2 ARG A 100     1654   1308   1234   -131    165   -129       N  
ATOM    743  N   VAL A 101      41.883  34.192  24.819  1.00  9.24           N  
ANISOU  743  N   VAL A 101     1351   1023   1135    -13    230    -90       N  
ATOM    744  CA  VAL A 101      42.438  35.331  25.549  1.00  9.68           C  
ANISOU  744  CA  VAL A 101     1354   1112   1213      1    215    -73       C  
ATOM    745  C   VAL A 101      43.918  35.487  25.199  1.00  8.92           C  
ANISOU  745  C   VAL A 101     1241   1022   1125     34    241    -63       C  
ATOM    746  O   VAL A 101      44.412  36.603  24.958  1.00  9.30           O  
ANISOU  746  O   VAL A 101     1257   1096   1180     32    234    -55       O  
ATOM    747  CB  VAL A 101      42.212  35.155  27.065  1.00  9.92           C  
ANISOU  747  CB  VAL A 101     1365   1145   1259      8    200    -62       C  
ATOM    748  CG1 VAL A 101      42.871  36.278  27.839  1.00 10.32           C  
ANISOU  748  CG1 VAL A 101     1369   1225   1328     20    184    -48       C  
ATOM    749  CG2 VAL A 101      40.723  35.106  27.380  1.00  9.65           C  
ANISOU  749  CG2 VAL A 101     1340   1110   1217    -27    179    -70       C  
ATOM    750  N   ALA A 102      44.650  34.367  25.158  1.00  9.72           N  
ANISOU  750  N   ALA A 102     1364   1102   1227     65    272    -61       N  
ATOM    751  CA  ALA A 102      46.061  34.413  24.790  1.00 10.58           C  
ANISOU  751  CA  ALA A 102     1452   1222   1346    101    301    -49       C  
ATOM    752  C   ALA A 102      46.274  34.896  23.361  1.00 10.30           C  
ANISOU  752  C   ALA A 102     1429   1192   1292     91    320    -58       C  
ATOM    753  O   ALA A 102      47.294  35.552  23.080  1.00 10.62           O  
ANISOU  753  O   ALA A 102     1433   1258   1343    106    335    -45       O  
ATOM    754  CB  ALA A 102      46.701  33.037  25.007  1.00 11.11           C  
ANISOU  754  CB  ALA A 102     1545   1262   1416    144    334    -45       C  
ATOM    755  N   GLU A 103      45.355  34.592  22.443  1.00 10.01           N  
ANISOU  755  N   GLU A 103     1442   1135   1227     65    320    -79       N  
ATOM    756  CA  GLU A 103      45.472  35.122  21.086  1.00 10.23           C  
ANISOU  756  CA  GLU A 103     1487   1170   1231     53    334    -86       C  
ATOM    757  C   GLU A 103      45.415  36.645  21.096  1.00  9.88           C  
ANISOU  757  C   GLU A 103     1399   1159   1195     31    308    -74       C  
ATOM    758  O   GLU A 103      46.209  37.316  20.431  1.00 10.38           O  
ANISOU  758  O   GLU A 103     1447   1240   1257     36    326    -65       O  
ATOM    759  CB  GLU A 103      44.361  34.571  20.192  1.00 11.17           C  
ANISOU  759  CB  GLU A 103     1667   1262   1314     22    328   -111       C  
ATOM    760  CG  GLU A 103      44.531  33.117  19.834  1.00 13.16           C  
ANISOU  760  CG  GLU A 103     1977   1473   1549     40    362   -127       C  
ATOM    761  CD  GLU A 103      43.408  32.552  18.989  1.00 13.28           C  
ANISOU  761  CD  GLU A 103     2056   1462   1526      1    350   -153       C  
ATOM    762  OE1 GLU A 103      42.408  33.251  18.712  1.00 15.16           O  
ANISOU  762  OE1 GLU A 103     2288   1718   1753    -40    311   -157       O  
ATOM    763  OE2 GLU A 103      43.520  31.360  18.598  1.00 16.93           O1-
ANISOU  763  OE2 GLU A 103     2580   1884   1970     11    378   -170       O1-
ATOM    764  N   VAL A 104      44.464  37.202  21.831  1.00  9.66           N  
ANISOU  764  N   VAL A 104     1356   1140   1176      7    267    -74       N  
ATOM    765  CA  VAL A 104      44.278  38.646  21.850  1.00  9.39           C  
ANISOU  765  CA  VAL A 104     1291   1130   1148    -12    241    -64       C  
ATOM    766  C   VAL A 104      45.442  39.324  22.566  1.00  9.74           C  
ANISOU  766  C   VAL A 104     1287   1195   1221      4    245    -45       C  
ATOM    767  O   VAL A 104      45.957  40.340  22.086  1.00 10.04           O  
ANISOU  767  O   VAL A 104     1307   1248   1259     -5    247    -35       O  
ATOM    768  CB  VAL A 104      42.900  38.994  22.442  1.00  9.60           C  
ANISOU  768  CB  VAL A 104     1316   1158   1174    -36    201    -70       C  
ATOM    769  CG1 VAL A 104      42.707  40.501  22.492  1.00 10.36           C  
ANISOU  769  CG1 VAL A 104     1387   1273   1275    -49    176    -60       C  
ATOM    770  CG2 VAL A 104      41.798  38.359  21.605  1.00 10.50           C  
ANISOU  770  CG2 VAL A 104     1473   1258   1259    -58    194    -87       C  
ATOM    771  N   VAL A 105      45.899  38.762  23.688  1.00 10.04           N  
ANISOU  771  N   VAL A 105     1302   1233   1279     25    245    -38       N  
ATOM    772  CA  VAL A 105      47.132  39.239  24.318  1.00 10.30           C  
ANISOU  772  CA  VAL A 105     1286   1289   1337     40    248    -19       C  
ATOM    773  C   VAL A 105      48.281  39.226  23.323  1.00  9.81           C  
ANISOU  773  C   VAL A 105     1215   1238   1274     55    287    -10       C  
ATOM    774  O   VAL A 105      49.085  40.164  23.259  1.00 10.74           O  
ANISOU  774  O   VAL A 105     1295   1380   1404     46    288      5       O  
ATOM    775  CB  VAL A 105      47.451  38.392  25.565  1.00 10.28           C  
ANISOU  775  CB  VAL A 105     1269   1286   1352     67    244    -12       C  
ATOM    776  CG1 VAL A 105      48.862  38.662  26.054  1.00 11.85           C  
ANISOU  776  CG1 VAL A 105     1415   1512   1574     86    250     10       C  
ATOM    777  CG2 VAL A 105      46.446  38.666  26.667  1.00 10.75           C  
ANISOU  777  CG2 VAL A 105     1329   1342   1413     50    207    -16       C  
ATOM    778  N   GLY A 106      48.379  38.160  22.531  1.00 10.61           N  
ANISOU  778  N   GLY A 106     1352   1321   1359     76    323    -19       N  
ATOM    779  CA  GLY A 106      49.443  38.055  21.548  1.00 10.99           C  
ANISOU  779  CA  GLY A 106     1395   1378   1403     95    368    -12       C  
ATOM    780  C   GLY A 106      49.360  39.080  20.447  1.00 10.82           C  
ANISOU  780  C   GLY A 106     1382   1366   1362     66    373    -12       C  
ATOM    781  O   GLY A 106      50.394  39.528  19.941  1.00 11.16           O  
ANISOU  781  O   GLY A 106     1397   1431   1412     71    401      4       O  
ATOM    782  N   TYR A 107      48.145  39.485  20.065  1.00 10.82           N  
ANISOU  782  N   TYR A 107     1419   1352   1340     34    345    -26       N  
ATOM    783  CA  TYR A 107      48.020  40.559  19.088  1.00 10.91           C  
ANISOU  783  CA  TYR A 107     1441   1372   1333      8    344    -22       C  
ATOM    784  C   TYR A 107      48.634  41.837  19.642  1.00 10.22           C  
ANISOU  784  C   TYR A 107     1302   1309   1272     -8    328     -1       C  
ATOM    785  O   TYR A 107      49.342  42.560  18.938  1.00 11.12           O  
ANISOU  785  O   TYR A 107     1405   1436   1382    -19    349     13       O  
ATOM    786  CB  TYR A 107      46.553  40.854  18.772  1.00 11.40           C  
ANISOU  786  CB  TYR A 107     1541   1420   1370    -20    307    -36       C  
ATOM    787  CG  TYR A 107      45.714  39.755  18.177  1.00 11.48           C  
ANISOU  787  CG  TYR A 107     1605   1407   1350    -20    311    -59       C  
ATOM    788  CD1 TYR A 107      46.256  38.712  17.440  1.00 12.29           C  
ANISOU  788  CD1 TYR A 107     1742   1495   1434      1    354    -69       C  
ATOM    789  CD2 TYR A 107      44.342  39.771  18.365  1.00 11.30           C  
ANISOU  789  CD2 TYR A 107     1600   1377   1318    -42    270    -70       C  
ATOM    790  CE1 TYR A 107      45.438  37.714  16.905  1.00 12.58           C  
ANISOU  790  CE1 TYR A 107     1837   1505   1440     -6    353    -92       C  
ATOM    791  CE2 TYR A 107      43.531  38.802  17.839  1.00 12.57           C  
ANISOU  791  CE2 TYR A 107     1808   1517   1450    -52    268    -91       C  
ATOM    792  CZ  TYR A 107      44.071  37.770  17.121  1.00 12.64           C  
ANISOU  792  CZ  TYR A 107     1857   1507   1438    -37    308   -103       C  
ATOM    793  OH  TYR A 107      43.224  36.794  16.614  1.00 13.78           O  
ANISOU  793  OH  TYR A 107     2055   1627   1552    -53    302   -126       O  
ATOM    794  N   ALA A 108      48.345  42.145  20.907  1.00 10.96           N  
ANISOU  794  N   ALA A 108     1369   1406   1389    -14    291      1       N  
ATOM    795  CA  ALA A 108      48.914  43.337  21.524  1.00 11.24           C  
ANISOU  795  CA  ALA A 108     1364   1460   1448    -33    272     18       C  
ATOM    796  C   ALA A 108      50.428  43.232  21.597  1.00 11.59           C  
ANISOU  796  C   ALA A 108     1359   1530   1514    -20    302     37       C  
ATOM    797  O   ALA A 108      51.145  44.181  21.259  1.00 11.65           O  
ANISOU  797  O   ALA A 108     1343   1554   1529    -43    310     53       O  
ATOM    798  CB  ALA A 108      48.326  43.527  22.920  1.00 12.04           C  
ANISOU  798  CB  ALA A 108     1451   1558   1564    -37    230     13       C  
ATOM    799  N   GLU A 109      50.933  42.074  22.010  1.00 11.77           N  
ANISOU  799  N   GLU A 109     1368   1558   1548     15    320     37       N  
ATOM    800  CA  GLU A 109      52.363  41.883  22.134  1.00 12.68           C  
ANISOU  800  CA  GLU A 109     1430   1703   1686     35    348     58       C  
ATOM    801  C   GLU A 109      53.045  42.100  20.791  1.00 12.22           C  
ANISOU  801  C   GLU A 109     1373   1656   1616     33    396     67       C  
ATOM    802  O   GLU A 109      54.043  42.820  20.697  1.00 13.23           O  
ANISOU  802  O   GLU A 109     1453   1814   1761     18    408     88       O  
ATOM    803  CB  GLU A 109      52.647  40.473  22.640  1.00 12.68           C  
ANISOU  803  CB  GLU A 109     1426   1699   1694     84    364     56       C  
ATOM    804  CG  GLU A 109      54.096  40.265  23.030  1.00 14.21           C  
ANISOU  804  CG  GLU A 109     1553   1929   1917    110    384     81       C  
ATOM    805  CD  GLU A 109      54.381  38.871  23.545  1.00 15.09           C  
ANISOU  805  CD  GLU A 109     1665   2034   2036    166    399     83       C  
ATOM    806  OE1 GLU A 109      53.517  37.987  23.388  1.00 17.95           O  
ANISOU  806  OE1 GLU A 109     2086   2357   2377    181    405     63       O  
ATOM    807  OE2 GLU A 109      55.470  38.665  24.109  1.00 17.63           O1-
ANISOU  807  OE2 GLU A 109     1926   2388   2383    193    404    106       O1-
ATOM    808  N  ASER A 110      52.510  41.473  19.739  0.50 11.52           N  
ANISOU  808  N  ASER A 110     1339   1542   1494     46    424     51       N  
ATOM    809  N  BSER A 110      52.525  41.485  19.729  0.20 10.86           N  
ANISOU  809  N  BSER A 110     1256   1460   1412     46    425     51       N  
ATOM    810  N  CSER A 110      52.505  41.489  19.733  0.30 11.28           N  
ANISOU  810  N  CSER A 110     1310   1513   1464     45    424     51       N  
ATOM    811  CA ASER A 110      53.082  41.564  18.400  0.50 11.48           C  
ANISOU  811  CA ASER A 110     1348   1546   1469     48    475     57       C  
ATOM    812  CA BSER A 110      53.188  41.585  18.433  0.20 11.92           C  
ANISOU  812  CA BSER A 110     1398   1604   1528     49    476     59       C  
ATOM    813  CA CSER A 110      53.117  41.564  18.411  0.30 12.61           C  
ANISOU  813  CA CSER A 110     1489   1689   1613     49    475     58       C  
ATOM    814  C  ASER A 110      53.138  43.005  17.922  0.50 12.12           C  
ANISOU  814  C  ASER A 110     1422   1638   1546      2    465     71       C  
ATOM    815  C  BSER A 110      53.102  42.988  17.842  0.20 12.81           C  
ANISOU  815  C  BSER A 110     1513   1723   1630      2    466     70       C  
ATOM    816  C  CSER A 110      53.102  42.984  17.860  0.30 13.20           C  
ANISOU  816  C  CSER A 110     1562   1773   1681      2    466     70       C  
ATOM    817  O  ASER A 110      54.093  43.411  17.252  0.50 13.35           O  
ANISOU  817  O  ASER A 110     1552   1816   1703     -4    503     90       O  
ATOM    818  O  BSER A 110      53.932  43.339  17.002  0.20 13.96           O  
ANISOU  818  O  BSER A 110     1645   1888   1771     -3    508     86       O  
ATOM    819  O  CSER A 110      53.976  43.347  17.069  0.30 14.12           O  
ANISOU  819  O  CSER A 110     1662   1910   1794     -3    507     87       O  
ATOM    820  CB ASER A 110      52.234  40.719  17.443  0.50 12.27           C  
ANISOU  820  CB ASER A 110     1523   1611   1527     61    493     32       C  
ATOM    821  CB BSER A 110      52.625  40.549  17.461  0.20 14.82           C  
ANISOU  821  CB BSER A 110     1834   1942   1857     72    507     37       C  
ATOM    822  CB CSER A 110      52.391  40.610  17.459  0.30 15.92           C  
ANISOU  822  CB CSER A 110     1981   2076   1992     67    499     33       C  
ATOM    823  OG ASER A 110      52.647  40.915  16.098  0.50 13.49           O  
ANISOU  823  OG ASER A 110     1701   1771   1653     59    539     36       O  
ATOM    824  OG BSER A 110      51.311  40.879  17.065  0.20 16.27           O  
ANISOU  824  OG BSER A 110     2072   2099   2010     42    474     18       O  
ATOM    825  OG CSER A 110      52.495  39.262  17.896  0.30 17.66           O  
ANISOU  825  OG CSER A 110     2210   2282   2218    111    514     23       O  
ATOM    826  N   ALA A 111      52.106  43.782  18.226  1.00 11.62           N  
ANISOU  826  N   ALA A 111     1383   1557   1476    -30    417     62       N  
ATOM    827  CA  ALA A 111      52.018  45.174  17.813  1.00 11.94           C  
ANISOU  827  CA  ALA A 111     1428   1598   1510    -72    403     75       C  
ATOM    828  C   ALA A 111      52.810  46.122  18.691  1.00 12.56           C  
ANISOU  828  C   ALA A 111     1449   1698   1624    -99    384     95       C  
ATOM    829  O   ALA A 111      52.796  47.332  18.426  1.00 13.95           O  
ANISOU  829  O   ALA A 111     1633   1871   1798   -137    373    106       O  
ATOM    830  CB  ALA A 111      50.552  45.604  17.750  1.00 12.51           C  
ANISOU  830  CB  ALA A 111     1551   1641   1559    -88    361     59       C  
ATOM    831  N   GLY A 112      53.504  45.626  19.711  1.00 11.74           N  
ANISOU  831  N   GLY A 112     1293   1615   1552    -82    378    100       N  
ATOM    832  CA  GLY A 112      54.308  46.492  20.547  1.00 13.31           C  
ANISOU  832  CA  GLY A 112     1436   1837   1782   -112    356    118       C  
ATOM    833  C   GLY A 112      53.514  47.294  21.546  1.00 11.60           C  
ANISOU  833  C   GLY A 112     1235   1601   1571   -138    299    107       C  
ATOM    834  O   GLY A 112      53.937  48.388  21.929  1.00 12.13           O  
ANISOU  834  O   GLY A 112     1282   1675   1653   -178    278    119       O  
ATOM    835  N   LEU A 113      52.370  46.783  21.976  1.00 10.50           N  
ANISOU  835  N   LEU A 113     1132   1438   1419   -118    274     86       N  
ATOM    836  CA  LEU A 113      51.504  47.440  22.939  1.00 10.19           C  
ANISOU  836  CA  LEU A 113     1111   1380   1382   -134    225     75       C  
ATOM    837  C   LEU A 113      51.599  46.745  24.289  1.00 10.11           C  
ANISOU  837  C   LEU A 113     1073   1380   1389   -113    201     69       C  
ATOM    838  O   LEU A 113      51.832  45.533  24.371  1.00 11.72           O  
ANISOU  838  O   LEU A 113     1265   1592   1596    -77    220     68       O  
ATOM    839  CB  LEU A 113      50.059  47.386  22.443  1.00 10.24           C  
ANISOU  839  CB  LEU A 113     1175   1355   1360   -126    215     57       C  
ATOM    840  CG  LEU A 113      49.798  48.082  21.109  1.00 10.96           C  
ANISOU  840  CG  LEU A 113     1303   1435   1428   -144    232     63       C  
ATOM    841  CD1 LEU A 113      48.503  47.612  20.485  1.00 12.62           C  
ANISOU  841  CD1 LEU A 113     1562   1626   1609   -128    226     47       C  
ATOM    842  CD2 LEU A 113      49.773  49.592  21.308  1.00 13.23           C  
ANISOU  842  CD2 LEU A 113     1598   1710   1720   -180    207     73       C  
ATOM    843  N   ASN A 114      51.393  47.512  25.359  1.00  9.66           N  
ANISOU  843  N   ASN A 114     1012   1318   1340   -134    160     66       N  
ATOM    844  CA  ASN A 114      51.123  46.903  26.652  1.00  9.37           C  
ANISOU  844  CA  ASN A 114      967   1284   1310   -114    134     57       C  
ATOM    845  C   ASN A 114      49.685  46.383  26.654  1.00  9.62           C  
ANISOU  845  C   ASN A 114     1044   1288   1321    -94    128     38       C  
ATOM    846  O   ASN A 114      48.858  46.826  25.854  1.00  9.57           O  
ANISOU  846  O   ASN A 114     1075   1263   1299   -102    132     31       O  
ATOM    847  CB  ASN A 114      51.285  47.902  27.786  1.00 10.57           C  
ANISOU  847  CB  ASN A 114     1110   1438   1470   -144     93     56       C  
ATOM    848  CG  ASN A 114      52.649  48.532  27.819  1.00 11.93           C  
ANISOU  848  CG  ASN A 114     1235   1637   1662   -176     91     76       C  
ATOM    849  ND2 ASN A 114      52.664  49.852  27.966  1.00 13.72           N  
ANISOU  849  ND2 ASN A 114     1475   1850   1887   -220     69     75       N  
ATOM    850  OD1 ASN A 114      53.673  47.859  27.731  1.00 11.93           O  
ANISOU  850  OD1 ASN A 114     1186   1670   1678   -162    110     92       O  
ATOM    851  N   ALA A 115      49.379  45.449  27.553  1.00  9.51           N  
ANISOU  851  N   ALA A 115     1029   1275   1310    -68    119     31       N  
ATOM    852  CA  ALA A 115      48.060  44.832  27.611  1.00  9.44           C  
ANISOU  852  CA  ALA A 115     1058   1245   1285    -52    116     15       C  
ATOM    853  C   ALA A 115      47.642  44.610  29.049  1.00  8.88           C  
ANISOU  853  C   ALA A 115      986   1174   1216    -44     89     10       C  
ATOM    854  O   ALA A 115      48.468  44.222  29.880  1.00  9.99           O  
ANISOU  854  O   ALA A 115     1098   1331   1368    -33     82     19       O  
ATOM    855  CB  ALA A 115      48.061  43.488  26.875  1.00 10.97           C  
ANISOU  855  CB  ALA A 115     1262   1434   1471    -26    149     13       C  
ATOM    856  N   ILE A 116      46.354  44.810  29.329  1.00  8.31           N  
ANISOU  856  N   ILE A 116      943   1084   1131    -46     75     -4       N  
ATOM    857  CA  ILE A 116      45.764  44.485  30.624  1.00  8.07           C  
ANISOU  857  CA  ILE A 116      918   1052   1097    -36     56    -10       C  
ATOM    858  C   ILE A 116      44.674  43.452  30.370  1.00  8.16           C  
ANISOU  858  C   ILE A 116      953   1051   1098    -22     69    -18       C  
ATOM    859  O   ILE A 116      43.848  43.657  29.482  1.00  9.42           O  
ANISOU  859  O   ILE A 116     1131   1201   1248    -30     74    -25       O  
ATOM    860  CB  ILE A 116      45.130  45.721  31.292  1.00  8.40           C  
ANISOU  860  CB  ILE A 116      974   1086   1133    -51     30    -18       C  
ATOM    861  CG1 ILE A 116      46.139  46.862  31.451  1.00  9.83           C  
ANISOU  861  CG1 ILE A 116     1141   1273   1321    -74     15    -12       C  
ATOM    862  CG2 ILE A 116      44.521  45.331  32.643  1.00  9.70           C  
ANISOU  862  CG2 ILE A 116     1145   1250   1289    -38     16    -24       C  
ATOM    863  CD1 ILE A 116      45.535  48.132  32.023  1.00 10.81           C  
ANISOU  863  CD1 ILE A 116     1290   1382   1437    -88     -8    -22       C  
ATOM    864  N   ILE A 117      44.637  42.366  31.151  1.00  7.92           N  
ANISOU  864  N   ILE A 117      922   1019   1067     -4     73    -16       N  
ATOM    865  CA  ILE A 117      43.503  41.437  31.135  1.00  8.26           C  
ANISOU  865  CA  ILE A 117      990   1049   1101      1     82    -24       C  
ATOM    866  C   ILE A 117      42.906  41.406  32.541  1.00  7.38           C  
ANISOU  866  C   ILE A 117      881    939    984      5     66    -24       C  
ATOM    867  O   ILE A 117      43.597  41.659  33.530  1.00  8.49           O  
ANISOU  867  O   ILE A 117     1008   1089   1127     11     52    -17       O  
ATOM    868  CB  ILE A 117      43.878  40.020  30.660  1.00  8.52           C  
ANISOU  868  CB  ILE A 117     1032   1070   1133     17    108    -21       C  
ATOM    869  CG1 ILE A 117      44.993  39.400  31.500  1.00  9.42           C  
ANISOU  869  CG1 ILE A 117     1129   1192   1258     42    110     -6       C  
ATOM    870  CG2 ILE A 117      44.247  40.050  29.176  1.00  9.93           C  
ANISOU  870  CG2 ILE A 117     1217   1247   1310     13    128    -24       C  
ATOM    871  CD1 ILE A 117      45.308  37.960  31.149  1.00 10.53           C  
ANISOU  871  CD1 ILE A 117     1288   1316   1399     65    138     -2       C  
ATOM    872  N   ASN A 118      41.620  41.055  32.633  1.00  7.58           N  
ANISOU  872  N   ASN A 118      922    957   1000     -1     69    -32       N  
ATOM    873  CA  ASN A 118      40.933  41.109  33.921  1.00  7.63           C  
ANISOU  873  CA  ASN A 118      933    967   1000      2     60    -32       C  
ATOM    874  C   ASN A 118      39.889  39.991  34.022  1.00  7.64           C  
ANISOU  874  C   ASN A 118      948    959    994     -1     74    -33       C  
ATOM    875  O   ASN A 118      39.814  39.081  33.192  1.00  8.24           O  
ANISOU  875  O   ASN A 118     1037   1024   1071     -7     89    -34       O  
ATOM    876  CB  ASN A 118      40.322  42.504  34.164  1.00  8.19           C  
ANISOU  876  CB  ASN A 118     1001   1044   1066     -4     44    -40       C  
ATOM    877  CG  ASN A 118      39.059  42.746  33.353  1.00  7.94           C  
ANISOU  877  CG  ASN A 118      973   1012   1031    -13     47    -46       C  
ATOM    878  ND2 ASN A 118      38.454  43.903  33.542  1.00  8.25           N  
ANISOU  878  ND2 ASN A 118     1013   1056   1068    -11     37    -51       N  
ATOM    879  OD1 ASN A 118      38.647  41.893  32.559  1.00  8.04           O  
ANISOU  879  OD1 ASN A 118      990   1021   1043    -21     59    -47       O  
ATOM    880  N   ILE A 119      39.119  40.051  35.109  1.00  7.60           N  
ANISOU  880  N   ILE A 119      947    960    981      0     71    -32       N  
ATOM    881  CA  ILE A 119      37.822  39.390  35.255  1.00  7.74           C  
ANISOU  881  CA  ILE A 119      972    977    993    -12     83    -33       C  
ATOM    882  C   ILE A 119      36.771  40.493  35.191  1.00  7.89           C  
ANISOU  882  C   ILE A 119      978   1011   1010    -17     75    -40       C  
ATOM    883  O   ILE A 119      36.789  41.412  36.021  1.00  8.72           O  
ANISOU  883  O   ILE A 119     1080   1123   1109     -5     66    -42       O  
ATOM    884  CB  ILE A 119      37.741  38.602  36.571  1.00  8.29           C  
ANISOU  884  CB  ILE A 119     1054   1043   1054     -5     91    -23       C  
ATOM    885  CG1 ILE A 119      38.727  37.434  36.571  1.00  9.03           C  
ANISOU  885  CG1 ILE A 119     1163   1119   1150      6     99    -12       C  
ATOM    886  CG2 ILE A 119      36.311  38.139  36.817  1.00  9.47           C  
ANISOU  886  CG2 ILE A 119     1205   1197   1198    -22    104    -22       C  
ATOM    887  CD1 ILE A 119      38.770  36.656  37.879  1.00  9.94           C  
ANISOU  887  CD1 ILE A 119     1295   1229   1254     17    105      2       C  
ATOM    888  N   HIS A 120      35.864  40.422  34.206  1.00  7.88           N  
ANISOU  888  N   HIS A 120      969   1014   1010    -33     76    -45       N  
ATOM    889  CA  HIS A 120      35.021  41.574  33.891  1.00  7.52           C  
ANISOU  889  CA  HIS A 120      909    984    965    -30     66    -49       C  
ATOM    890  C   HIS A 120      33.593  41.328  34.351  1.00  7.99           C  
ANISOU  890  C   HIS A 120      953   1060   1021    -36     74    -46       C  
ATOM    891  O   HIS A 120      33.291  41.527  35.544  1.00  8.26           O  
ANISOU  891  O   HIS A 120      986   1102   1051    -23     82    -43       O  
ATOM    892  CB  HIS A 120      35.186  41.981  32.420  1.00  7.84           C  
ANISOU  892  CB  HIS A 120      948   1021   1008    -38     56    -53       C  
ATOM    893  CG  HIS A 120      34.826  43.397  32.141  1.00  7.36           C  
ANISOU  893  CG  HIS A 120      880    969    947    -26     43    -54       C  
ATOM    894  CD2 HIS A 120      33.700  43.929  31.609  1.00  8.29           C  
ANISOU  894  CD2 HIS A 120      984   1102   1064    -25     35    -53       C  
ATOM    895  ND1 HIS A 120      35.695  44.444  32.390  1.00  7.95           N  
ANISOU  895  ND1 HIS A 120      963   1034   1023    -14     36    -55       N  
ATOM    896  CE1 HIS A 120      35.106  45.560  31.988  1.00  7.85           C  
ANISOU  896  CE1 HIS A 120      948   1025   1009     -4     26    -55       C  
ATOM    897  NE2 HIS A 120      33.894  45.282  31.521  1.00  8.06           N  
ANISOU  897  NE2 HIS A 120      960   1068   1035     -7     25    -53       N  
ATOM    898  N   HIS A 121      32.658  40.942  33.465  1.00  7.87           N  
ANISOU  898  N   HIS A 121      925   1056   1009    -57     72    -46       N  
ATOM    899  CA  HIS A 121      31.240  40.905  33.866  1.00  8.04           C  
ANISOU  899  CA  HIS A 121      921   1104   1031    -63     78    -41       C  
ATOM    900  C   HIS A 121      30.883  39.740  34.782  1.00  8.19           C  
ANISOU  900  C   HIS A 121      944   1122   1048    -80     99    -34       C  
ATOM    901  O   HIS A 121      29.749  39.693  35.266  1.00  8.61           O  
ANISOU  901  O   HIS A 121      971   1199   1101    -86    109    -27       O  
ATOM    902  CB  HIS A 121      30.319  40.999  32.664  1.00  8.41           C  
ANISOU  902  CB  HIS A 121      946   1169   1080    -81     64    -41       C  
ATOM    903  CG  HIS A 121      30.307  42.351  32.036  1.00  8.25           C  
ANISOU  903  CG  HIS A 121      917   1156   1060    -57     47    -42       C  
ATOM    904  CD2 HIS A 121      30.310  42.719  30.728  1.00  8.37           C  
ANISOU  904  CD2 HIS A 121      934   1174   1074    -63     28    -43       C  
ATOM    905  ND1 HIS A 121      30.289  43.515  32.776  1.00  9.14           N  
ANISOU  905  ND1 HIS A 121     1027   1272   1174    -23     49    -41       N  
ATOM    906  CE1 HIS A 121      30.270  44.540  31.938  1.00  9.04           C  
ANISOU  906  CE1 HIS A 121     1014   1260   1162     -8     33    -40       C  
ATOM    907  NE2 HIS A 121      30.278  44.089  30.689  1.00  8.70           N  
ANISOU  907  NE2 HIS A 121      972   1217   1116    -32     19    -40       N  
ATOM    908  N   ASP A 122      31.822  38.853  35.096  1.00  8.25           N  
ANISOU  908  N   ASP A 122      981   1104   1052    -84    106    -33       N  
ATOM    909  CA  ASP A 122      31.595  37.939  36.212  1.00  8.44           C  
ANISOU  909  CA  ASP A 122     1015   1122   1069    -91    127    -23       C  
ATOM    910  C   ASP A 122      31.172  38.689  37.462  1.00  8.16           C  
ANISOU  910  C   ASP A 122      967   1106   1026    -68    136    -18       C  
ATOM    911  O   ASP A 122      30.441  38.149  38.292  1.00  9.09           O  
ANISOU  911  O   ASP A 122     1082   1234   1139    -78    156     -9       O  
ATOM    912  CB  ASP A 122      32.875  37.167  36.535  1.00  8.63           C  
ANISOU  912  CB  ASP A 122     1074   1115   1089    -83    131    -20       C  
ATOM    913  CG  ASP A 122      33.376  36.334  35.376  1.00  8.49           C  
ANISOU  913  CG  ASP A 122     1076   1074   1077   -100    129    -26       C  
ATOM    914  OD1 ASP A 122      33.697  36.940  34.324  1.00  9.40           O  
ANISOU  914  OD1 ASP A 122     1185   1192   1197    -97    115    -35       O  
ATOM    915  OD2 ASP A 122      33.476  35.086  35.526  1.00  9.75           O1-
ANISOU  915  OD2 ASP A 122     1262   1209   1233   -114    143    -20       O1-
ATOM    916  N   GLY A 123      31.650  39.920  37.629  1.00  8.35           N  
ANISOU  916  N   GLY A 123      990   1133   1048    -38    125    -26       N  
ATOM    917  CA  GLY A 123      31.307  40.744  38.757  1.00  9.02           C  
ANISOU  917  CA  GLY A 123     1074   1231   1122    -13    133    -25       C  
ATOM    918  C   GLY A 123      30.165  41.700  38.529  1.00  9.13           C  
ANISOU  918  C   GLY A 123     1058   1271   1141      0    136    -27       C  
ATOM    919  O   GLY A 123      29.912  42.539  39.407  1.00 11.61           O  
ANISOU  919  O   GLY A 123     1374   1593   1443     28    146    -30       O  
ATOM    920  N   ALA A 124      29.458  41.633  37.405  1.00  8.70           N  
ANISOU  920  N   ALA A 124      975   1230   1099    -17    128    -26       N  
ATOM    921  CA  ALA A 124      28.438  42.637  37.124  1.00  9.66           C  
ANISOU  921  CA  ALA A 124     1065   1379   1226      3    126    -25       C  
ATOM    922  C   ALA A 124      27.316  42.572  38.149  1.00  9.59           C  
ANISOU  922  C   ALA A 124     1033   1399   1213     13    155    -15       C  
ATOM    923  O   ALA A 124      26.637  41.549  38.284  1.00 10.11           O  
ANISOU  923  O   ALA A 124     1078   1480   1282    -17    169     -5       O  
ATOM    924  CB  ALA A 124      27.884  42.453  35.718  1.00 10.74           C  
ANISOU  924  CB  ALA A 124     1176   1530   1375    -19    108    -22       C  
ATOM    925  N   ASN A 125      27.128  43.677  38.874  1.00 10.26           N  
ANISOU  925  N   ASN A 125     1122   1488   1289     55    166    -19       N  
ATOM    926  CA  ASN A 125      25.969  43.907  39.732  1.00 10.31           C  
ANISOU  926  CA  ASN A 125     1101   1526   1291     76    197    -11       C  
ATOM    927  C   ASN A 125      25.827  42.895  40.860  1.00  9.99           C  
ANISOU  927  C   ASN A 125     1068   1490   1237     58    226     -2       C  
ATOM    928  O   ASN A 125      24.758  42.791  41.457  1.00 11.43           O  
ANISOU  928  O   ASN A 125     1220   1704   1418     63    257      9       O  
ATOM    929  CB  ASN A 125      24.680  43.944  38.917  1.00 12.07           C  
ANISOU  929  CB  ASN A 125     1264   1789   1532     71    195      2       C  
ATOM    930  CG  ASN A 125      24.779  44.859  37.727  1.00 14.20           C  
ANISOU  930  CG  ASN A 125     1528   2055   1812     88    164     -3       C  
ATOM    931  ND2 ASN A 125      24.163  44.456  36.620  1.00 16.75           N  
ANISOU  931  ND2 ASN A 125     1812   2401   2149     61    145      6       N  
ATOM    932  OD1 ASN A 125      25.437  45.908  37.784  1.00 14.63           O  
ANISOU  932  OD1 ASN A 125     1616   2082   1859    121    156    -14       O  
ATOM    933  N  ASER A 126      26.886  42.166  41.181  0.73  9.07           N  
ANISOU  933  N  ASER A 126      992   1343   1111     38    219     -5       N  
ATOM    934  N  BSER A 126      26.893  42.165  41.184  0.27 10.57           N  
ANISOU  934  N  BSER A 126     1182   1533   1301     38    219     -5       N  
ATOM    935  CA ASER A 126      26.823  41.141  42.212  0.73  9.56           C  
ANISOU  935  CA ASER A 126     1069   1406   1159     21    245      6       C  
ATOM    936  CA BSER A 126      26.863  41.108  42.193  0.27 12.34           C  
ANISOU  936  CA BSER A 126     1421   1756   1510     19    244      6       C  
ATOM    937  C  ASER A 126      25.831  40.038  41.867  0.73  9.33           C  
ANISOU  937  C  ASER A 126     1004   1399   1143    -22    260     22       C  
ATOM    938  C  BSER A 126      25.864  40.006  41.857  0.27 12.41           C  
ANISOU  938  C  BSER A 126     1394   1787   1533    -23    259     22       C  
ATOM    939  O  ASER A 126      25.378  39.315  42.755  0.73 11.64           O  
ANISOU  939  O  ASER A 126     1298   1700   1425    -36    290     36       O  
ATOM    940  O  BSER A 126      25.435  39.265  42.744  0.27 11.03           O  
ANISOU  940  O  BSER A 126     1223   1621   1348    -38    289     36       O  
ATOM    941  CB ASER A 126      26.472  41.753  43.575  0.73 11.91           C  
ANISOU  941  CB ASER A 126     1379   1714   1431     56    275      6       C  
ATOM    942  CB BSER A 126      26.578  41.653  43.598  0.27 10.32           C  
ANISOU  942  CB BSER A 126     1182   1510   1230     53    274      6       C  
ATOM    943  OG ASER A 126      27.040  41.030  44.649  0.73 10.66           O  
ANISOU  943  OG ASER A 126     1261   1541   1249     48    288     12       O  
ATOM    944  OG BSER A 126      27.740  42.221  44.174  0.27 12.36           O  
ANISOU  944  OG BSER A 126     1490   1740   1467     76    258     -7       O  
ATOM    945  N   GLN A 127      25.505  39.856  40.585  1.00 10.30           N  
ANISOU  945  N   GLN A 127     1097   1530   1288    -47    238     22       N  
ATOM    946  CA  GLN A 127      24.451  38.916  40.208  1.00 11.63           C  
ANISOU  946  CA  GLN A 127     1227   1722   1468    -93    248     36       C  
ATOM    947  C   GLN A 127      24.973  37.552  39.781  1.00 11.56           C  
ANISOU  947  C   GLN A 127     1248   1682   1461   -142    239     37       C  
ATOM    948  O   GLN A 127      24.153  36.644  39.562  1.00 13.38           O  
ANISOU  948  O   GLN A 127     1457   1926   1699   -189    248     48       O  
ATOM    949  CB  GLN A 127      23.513  39.528  39.156  1.00 14.01           C  
ANISOU  949  CB  GLN A 127     1473   2061   1789    -93    230     37       C  
ATOM    950  CG  GLN A 127      24.084  39.615  37.760  1.00 14.78           C  
ANISOU  950  CG  GLN A 127     1580   2140   1894   -105    190     25       C  
ATOM    951  CD  GLN A 127      23.141  40.343  36.796  1.00 21.78           C  
ANISOU  951  CD  GLN A 127     2414   3067   2796    -98    170     28       C  
ATOM    952  NE2 GLN A 127      22.194  39.610  36.232  1.00 16.63           N  
ANISOU  952  NE2 GLN A 127     1721   2445   2154   -145    163     39       N  
ATOM    953  OE1 GLN A 127      23.269  41.548  36.570  1.00 31.29           O  
ANISOU  953  OE1 GLN A 127     3616   4273   4000    -53    159     23       O  
ATOM    954  N   TYR A 128      26.288  37.363  39.705  1.00 11.18           N  
ANISOU  954  N   TYR A 128     1250   1592   1405   -132    225     27       N  
ATOM    955  CA  TYR A 128      26.886  36.074  39.359  1.00 11.05           C  
ANISOU  955  CA  TYR A 128     1270   1540   1389   -168    221     29       C  
ATOM    956  C   TYR A 128      27.770  35.596  40.514  1.00 11.93           C  
ANISOU  956  C   TYR A 128     1428   1622   1483   -151    236     36       C  
ATOM    957  O   TYR A 128      27.555  35.987  41.667  1.00 12.73           O  
ANISOU  957  O   TYR A 128     1529   1737   1569   -128    256     43       O  
ATOM    958  CB  TYR A 128      27.648  36.173  38.031  1.00 11.91           C  
ANISOU  958  CB  TYR A 128     1391   1627   1506   -170    190     13       C  
ATOM    959  CG  TYR A 128      26.824  36.758  36.902  1.00 10.92           C  
ANISOU  959  CG  TYR A 128     1223   1531   1393   -182    170      8       C  
ATOM    960  CD1 TYR A 128      25.752  36.061  36.364  1.00 14.08           C  
ANISOU  960  CD1 TYR A 128     1597   1952   1802   -230    169     14       C  
ATOM    961  CD2 TYR A 128      27.120  37.996  36.370  1.00 11.65           C  
ANISOU  961  CD2 TYR A 128     1305   1633   1489   -147    150     -2       C  
ATOM    962  CE1 TYR A 128      24.998  36.596  35.327  1.00 14.77           C  
ANISOU  962  CE1 TYR A 128     1643   2072   1898   -240    145     11       C  
ATOM    963  CE2 TYR A 128      26.381  38.530  35.336  1.00 13.32           C  
ANISOU  963  CE2 TYR A 128     1481   1872   1709   -154    129     -4       C  
ATOM    964  CZ  TYR A 128      25.324  37.827  34.826  1.00 12.95           C  
ANISOU  964  CZ  TYR A 128     1403   1848   1668   -199    126      3       C  
ATOM    965  OH  TYR A 128      24.580  38.371  33.796  1.00 17.15           O  
ANISOU  965  OH  TYR A 128     1897   2412   2207   -204    100      3       O  
ATOM    966  N   TRP A 129      28.770  34.752  40.244  1.00 12.21           N  
ANISOU  966  N   TRP A 129     1505   1617   1516   -159    228     35       N  
ATOM    967  CA  TRP A 129      29.520  34.134  41.338  1.00 12.76           C  
ANISOU  967  CA  TRP A 129     1618   1662   1569   -144    242     47       C  
ATOM    968  C   TRP A 129      30.291  35.159  42.164  1.00 10.80           C  
ANISOU  968  C   TRP A 129     1378   1420   1306    -96    233     43       C  
ATOM    969  O   TRP A 129      30.501  34.955  43.366  1.00 11.90           O  
ANISOU  969  O   TRP A 129     1541   1556   1424    -82    247     55       O  
ATOM    970  CB  TRP A 129      30.494  33.066  40.813  1.00 12.90           C  
ANISOU  970  CB  TRP A 129     1677   1634   1589   -152    234     48       C  
ATOM    971  CG  TRP A 129      31.617  33.593  39.960  1.00 11.83           C  
ANISOU  971  CG  TRP A 129     1546   1487   1462   -127    208     32       C  
ATOM    972  CD1 TRP A 129      31.616  33.736  38.604  1.00 11.61           C  
ANISOU  972  CD1 TRP A 129     1506   1457   1448   -141    192     17       C  
ATOM    973  CD2 TRP A 129      32.909  34.039  40.406  1.00 11.10           C  
ANISOU  973  CD2 TRP A 129     1468   1386   1363    -86    194     32       C  
ATOM    974  CE2 TRP A 129      33.632  34.434  39.258  1.00 10.85           C  
ANISOU  974  CE2 TRP A 129     1430   1348   1345    -78    174     18       C  
ATOM    975  CE3 TRP A 129      33.535  34.129  41.655  1.00 11.14           C  
ANISOU  975  CE3 TRP A 129     1491   1390   1350    -58    195     43       C  
ATOM    976  NE1 TRP A 129      32.812  34.246  38.180  1.00 12.38           N  
ANISOU  976  NE1 TRP A 129     1611   1545   1549   -110    175      9       N  
ATOM    977  CZ2 TRP A 129      34.926  34.924  39.326  1.00 10.99           C  
ANISOU  977  CZ2 TRP A 129     1453   1361   1363    -46    158     16       C  
ATOM    978  CZ3 TRP A 129      34.825  34.607  41.721  1.00 11.35           C  
ANISOU  978  CZ3 TRP A 129     1525   1413   1377    -26    173     40       C  
ATOM    979  CH2 TRP A 129      35.511  35.007  40.558  1.00 11.47           C  
ANISOU  979  CH2 TRP A 129     1526   1424   1409    -21    156     27       C  
ATOM    980  N   LEU A 130      30.761  36.228  41.543  1.00 10.64           N  
ANISOU  980  N   LEU A 130     1342   1406   1293    -74    209     26       N  
ATOM    981  CA  LEU A 130      31.603  37.227  42.197  1.00 10.61           C  
ANISOU  981  CA  LEU A 130     1350   1404   1277    -37    195     19       C  
ATOM    982  C   LEU A 130      30.636  38.189  42.870  1.00 10.68           C  
ANISOU  982  C   LEU A 130     1339   1442   1276    -22    210     17       C  
ATOM    983  O   LEU A 130      30.216  39.181  42.276  1.00 11.36           O  
ANISOU  983  O   LEU A 130     1400   1544   1373    -12    202      5       O  
ATOM    984  CB  LEU A 130      32.498  37.846  41.135  1.00 10.96           C  
ANISOU  984  CB  LEU A 130     1389   1439   1337    -28    167      5       C  
ATOM    985  CG  LEU A 130      33.568  38.832  41.569  1.00 11.10           C  
ANISOU  985  CG  LEU A 130     1419   1454   1346      1    146     -3       C  
ATOM    986  CD1 LEU A 130      34.469  38.309  42.659  1.00 10.92           C  
ANISOU  986  CD1 LEU A 130     1426   1420   1304     14    143      8       C  
ATOM    987  CD2 LEU A 130      34.381  39.201  40.337  1.00 11.38           C  
ANISOU  987  CD2 LEU A 130     1446   1479   1400      0    124    -13       C  
ATOM    988  N   ASP A 131      30.252  37.869  44.117  1.00 10.54           N  
ANISOU  988  N   ASP A 131     1336   1431   1236    -18    235     29       N  
ATOM    989  CA  ASP A 131      29.047  38.395  44.776  1.00 11.15           C  
ANISOU  989  CA  ASP A 131     1393   1540   1303     -9    264     31       C  
ATOM    990  C   ASP A 131      29.389  39.068  46.102  1.00 10.04           C  
ANISOU  990  C   ASP A 131     1284   1401   1130     24    272     28       C  
ATOM    991  O   ASP A 131      29.390  38.435  47.160  1.00 11.17           O  
ANISOU  991  O   ASP A 131     1454   1541   1247     23    291     42       O  
ATOM    992  CB  ASP A 131      28.102  37.192  44.980  1.00 13.16           C  
ANISOU  992  CB  ASP A 131     1637   1803   1561    -45    295     52       C  
ATOM    993  CG  ASP A 131      26.837  37.536  45.728  1.00 12.67           C  
ANISOU  993  CG  ASP A 131     1548   1778   1489    -39    333     60       C  
ATOM    994  OD1 ASP A 131      26.548  38.711  46.018  1.00 13.34           O  
ANISOU  994  OD1 ASP A 131     1621   1882   1567     -4    338     49       O  
ATOM    995  OD2 ASP A 131      26.105  36.558  46.082  1.00 16.22           O1-
ANISOU  995  OD2 ASP A 131     1990   2235   1936    -72    362     80       O1-
ATOM    996  N  AILE A 132      29.663  40.374  46.035  0.64  9.93           N  
ANISOU  996  N  AILE A 132     1271   1388   1112     53    255      9       N  
ATOM    997  N  BILE A 132      29.638  40.374  46.050  0.36  9.94           N  
ANISOU  997  N  BILE A 132     1273   1390   1114     54    256      9       N  
ATOM    998  CA AILE A 132      30.077  41.135  47.215  0.64  9.44           C  
ANISOU  998  CA AILE A 132     1248   1324   1016     83    256      0       C  
ATOM    999  CA BILE A 132      30.086  41.065  47.251  0.36 10.77           C  
ANISOU  999  CA BILE A 132     1418   1492   1184     82    257      1       C  
ATOM   1000  C  AILE A 132      28.948  41.248  48.229  0.64 10.02           C  
ANISOU 1000  C  AILE A 132     1320   1420   1065     97    301      7       C  
ATOM   1001  C  BILE A 132      28.946  41.259  48.244  0.36 10.19           C  
ANISOU 1001  C  BILE A 132     1343   1442   1087     98    301      7       C  
ATOM   1002  O  AILE A 132      29.194  41.270  49.441  0.64 11.34           O  
ANISOU 1002  O  AILE A 132     1528   1585   1195    111    312      8       O  
ATOM   1003  O  BILE A 132      29.182  41.347  49.456  0.36 10.19           O  
ANISOU 1003  O  BILE A 132     1383   1439   1048    113    312      7       O  
ATOM   1004  CB AILE A 132      30.617  42.516  46.794  0.64  9.97           C  
ANISOU 1004  CB AILE A 132     1321   1381   1087    105    228    -23       C  
ATOM   1005  CB BILE A 132      30.781  42.392  46.902  0.36  8.69           C  
ANISOU 1005  CB BILE A 132     1164   1216    922    103    226    -22       C  
ATOM   1006  CG1AILE A 132      31.235  43.281  47.969  0.64 14.20           C  
ANISOU 1006  CG1AILE A 132     1905   1907   1584    128    220    -36       C  
ATOM   1007  CG2AILE A 132      29.512  43.364  46.158  0.64 12.03           C  
ANISOU 1007  CG2AILE A 132     1546   1658   1365    120    243    -30       C  
ATOM   1008  CG1BILE A 132      31.509  42.922  48.134  0.36  7.82           C  
ANISOU 1008  CG1BILE A 132     1104   1096    772    122    217    -31       C  
ATOM   1009  CG2BILE A 132      29.775  43.421  46.376  0.36  8.36           C  
ANISOU 1009  CG2BILE A 132     1094   1189    894    122    239    -32       C  
ATOM   1010  CD1AILE A 132      32.570  42.737  48.425  0.64 13.41           C  
ANISOU 1010  CD1AILE A 132     1836   1790   1469    117    190    -31       C  
ATOM   1011  CD1BILE A 132      32.519  43.980  47.823  0.36  7.13           C  
ANISOU 1011  CD1BILE A 132     1034    990    685    129    178    -51       C  
ATOM   1012  N   LYS A 133      27.703  41.351  47.770  1.00 11.06           N  
ANISOU 1012  N   LYS A 133     1407   1579   1217     95    327     12       N  
ATOM   1013  CA  LYS A 133      26.607  41.566  48.703  1.00 12.04           C  
ANISOU 1013  CA  LYS A 133     1523   1731   1320    114    374     18       C  
ATOM   1014  C   LYS A 133      26.514  40.420  49.697  1.00 11.81           C  
ANISOU 1014  C   LYS A 133     1517   1704   1266     93    402     40       C  
ATOM   1015  O   LYS A 133      26.476  40.633  50.914  1.00 12.52           O  
ANISOU 1015  O   LYS A 133     1643   1797   1317    115    426     41       O  
ATOM   1016  CB  LYS A 133      25.285  41.734  47.959  1.00 13.41           C  
ANISOU 1016  CB  LYS A 133     1631   1939   1524    112    395     25       C  
ATOM   1017  CG  LYS A 133      24.162  42.193  48.898  1.00 16.68           C  
ANISOU 1017  CG  LYS A 133     2032   2387   1919    143    448     31       C  
ATOM   1018  CD  LYS A 133      22.849  42.517  48.182  1.00 17.29           C  
ANISOU 1018  CD  LYS A 133     2036   2506   2028    150    467     40       C  
ATOM   1019  CE  LYS A 133      22.213  41.270  47.583  1.00 42.97           C  
ANISOU 1019  CE  LYS A 133     5238   5780   5307     94    471     63       C  
ATOM   1020  NZ  LYS A 133      20.939  41.558  46.856  1.00 39.55           N1+
ANISOU 1020  NZ  LYS A 133     4726   5395   4906     96    483     73       N1+
ATOM   1021  N  AASP A 134      26.485  39.183  49.192  0.38 12.03           N  
ANISOU 1021  N  AASP A 134     1530   1726   1315     51    399     58       N  
ATOM   1022  N  BASP A 134      26.498  39.186  49.188  0.62 11.69           N  
ANISOU 1022  N  BASP A 134     1487   1683   1272     51    399     58       N  
ATOM   1023  CA AASP A 134      26.362  38.031  50.078  0.38 13.28           C  
ANISOU 1023  CA AASP A 134     1714   1881   1451     28    427     82       C  
ATOM   1024  CA BASP A 134      26.374  38.023  50.058  0.62  9.80           C  
ANISOU 1024  CA BASP A 134     1273   1441   1011     28    427     82       C  
ATOM   1025  C  AASP A 134      27.694  37.630  50.699  0.38 11.70           C  
ANISOU 1025  C  AASP A 134     1574   1647   1223     35    401     84       C  
ATOM   1026  C  BASP A 134      27.698  37.631  50.690  0.62 10.39           C  
ANISOU 1026  C  BASP A 134     1408   1481   1057     35    401     84       C  
ATOM   1027  O  AASP A 134      27.703  37.075  51.802  0.38 12.56           O  
ANISOU 1027  O  AASP A 134     1721   1755   1298     35    424    101       O  
ATOM   1028  O  BASP A 134      27.701  37.093  51.798  0.62 10.98           O  
ANISOU 1028  O  BASP A 134     1520   1554   1097     35    424    101       O  
ATOM   1029  CB AASP A 134      25.725  36.853  49.340  0.38 13.96           C  
ANISOU 1029  CB AASP A 134     1766   1971   1567    -22    438    101       C  
ATOM   1030  CB BASP A 134      25.761  36.862  49.283  0.62 12.81           C  
ANISOU 1030  CB BASP A 134     1619   1824   1422    -22    435    101       C  
ATOM   1031  CG AASP A 134      24.233  37.048  49.098  0.38 17.70           C  
ANISOU 1031  CG AASP A 134     2177   2490   2060    -34    473    109       C  
ATOM   1032  CG BASP A 134      24.355  37.166  48.805  0.62 14.13           C  
ANISOU 1032  CG BASP A 134     1720   2034   1614    -33    462    104       C  
ATOM   1033  OD1AASP A 134      23.712  38.151  49.371  0.38 16.40           O  
ANISOU 1033  OD1AASP A 134     1991   2352   1889      5    488     99       O  
ATOM   1034  OD2AASP A 134      23.579  36.089  48.633  0.38 25.70           O1-
ANISOU 1034  OD2AASP A 134     3161   3511   3094    -82    484    126       O1-
ATOM   1035  OD1BASP A 134      23.516  37.577  49.636  0.62 17.36           O  
ANISOU 1035  OD1BASP A 134     2116   2475   2006    -13    503    111       O  
ATOM   1036  OD2BASP A 134      24.102  37.013  47.589  0.62 15.62           O1-
ANISOU 1036  OD2BASP A 134     1869   2227   1838    -58    440    101       O1-
ATOM   1037  N   ALA A 135      28.825  37.901  50.035  1.00 10.81           N  
ANISOU 1037  N   ALA A 135     1472   1511   1124     41    354     70       N  
ATOM   1038  CA  ALA A 135      30.103  37.610  50.668  1.00 11.13           C  
ANISOU 1038  CA  ALA A 135     1562   1527   1139     52    326     73       C  
ATOM   1039  C   ALA A 135      30.277  38.420  51.938  1.00 10.53           C  
ANISOU 1039  C   ALA A 135     1525   1459   1016     83    331     65       C  
ATOM   1040  O   ALA A 135      30.902  37.946  52.897  1.00 11.74           O  
ANISOU 1040  O   ALA A 135     1724   1603   1134     88    325     78       O  
ATOM   1041  CB  ALA A 135      31.255  37.921  49.720  1.00 11.00           C  
ANISOU 1041  CB  ALA A 135     1542   1492   1147     55    278     58       C  
ATOM   1042  N   ALA A 136      29.712  39.625  51.994  1.00 10.82           N  
ANISOU 1042  N   ALA A 136     1551   1513   1049    105    342     44       N  
ATOM   1043  CA  ALA A 136      29.857  40.473  53.163  1.00 11.24           C  
ANISOU 1043  CA  ALA A 136     1648   1569   1054    135    348     31       C  
ATOM   1044  C   ALA A 136      28.954  40.051  54.312  1.00 11.63           C  
ANISOU 1044  C   ALA A 136     1716   1636   1065    139    401     48       C  
ATOM   1045  O   ALA A 136      29.153  40.527  55.433  1.00 14.07           O  
ANISOU 1045  O   ALA A 136     2076   1946   1324    162    407     41       O  
ATOM   1046  CB  ALA A 136      29.561  41.932  52.785  1.00 11.91           C  
ANISOU 1046  CB  ALA A 136     1721   1657   1146    160    344      2       C  
ATOM   1047  N   THR A 137      27.951  39.194  54.077  1.00 11.38           N  
ANISOU 1047  N   THR A 137     1649   1622   1054    116    441     71       N  
ATOM   1048  CA  THR A 137      27.091  38.713  55.142  1.00 12.23           C  
ANISOU 1048  CA  THR A 137     1771   1748   1127    115    496     92       C  
ATOM   1049  C   THR A 137      27.267  37.231  55.444  1.00 11.71           C  
ANISOU 1049  C   THR A 137     1725   1670   1055     82    504    125       C  
ATOM   1050  O   THR A 137      26.796  36.781  56.477  1.00 14.41           O  
ANISOU 1050  O   THR A 137     2094   2021   1359     80    545    145       O  
ATOM   1051  CB  THR A 137      25.608  38.995  54.848  1.00 12.69           C  
ANISOU 1051  CB  THR A 137     1770   1843   1207    116    547     95       C  
ATOM   1052  CG2 THR A 137      25.329  40.481  54.707  1.00 15.08           C  
ANISOU 1052  CG2 THR A 137     2062   2156   1510    160    547     65       C  
ATOM   1053  OG1 THR A 137      25.212  38.318  53.656  1.00 14.79           O  
ANISOU 1053  OG1 THR A 137     1979   2112   1526     78    539    106       O  
ATOM   1054  N   ASP A 138      27.919  36.463  54.596  1.00 12.00           N  
ANISOU 1054  N   ASP A 138     1752   1682   1124     57    469    132       N  
ATOM   1055  CA  ASP A 138      27.982  35.010  54.741  1.00 12.13           C  
ANISOU 1055  CA  ASP A 138     1788   1680   1140     24    480    164       C  
ATOM   1056  C   ASP A 138      29.414  34.567  54.488  1.00 11.37           C  
ANISOU 1056  C   ASP A 138     1725   1549   1047     29    428    166       C  
ATOM   1057  O   ASP A 138      29.889  34.593  53.354  1.00 12.06           O  
ANISOU 1057  O   ASP A 138     1785   1623   1175     22    395    153       O  
ATOM   1058  CB  ASP A 138      27.013  34.341  53.763  1.00 14.14           C  
ANISOU 1058  CB  ASP A 138     1989   1941   1441    -19    503    175       C  
ATOM   1059  CG  ASP A 138      26.912  32.845  53.960  1.00 18.02           C  
ANISOU 1059  CG  ASP A 138     2506   2410   1930    -58    523    208       C  
ATOM   1060  OD1 ASP A 138      27.822  32.253  54.564  1.00 19.83           O  
ANISOU 1060  OD1 ASP A 138     2793   2611   2133    -48    507    223       O  
ATOM   1061  OD2 ASP A 138      25.900  32.261  53.516  1.00 21.18           O1-
ANISOU 1061  OD2 ASP A 138     2870   2821   2356   -100    553    221       O1-
ATOM   1062  N   GLU A 139      30.089  34.127  55.544  1.00 11.85           N  
ANISOU 1062  N   GLU A 139     1842   1596   1064     43    421    184       N  
ATOM   1063  CA  GLU A 139      31.481  33.708  55.430  1.00 12.82           C  
ANISOU 1063  CA  GLU A 139     1993   1692   1186     55    371    189       C  
ATOM   1064  C   GLU A 139      31.658  32.547  54.457  1.00 12.40           C  
ANISOU 1064  C   GLU A 139     1928   1610   1174     29    367    205       C  
ATOM   1065  O   GLU A 139      32.721  32.421  53.840  1.00 12.14           O  
ANISOU 1065  O   GLU A 139     1893   1558   1161     41    325    200       O  
ATOM   1066  CB  GLU A 139      32.024  33.317  56.805  1.00 15.77           C  
ANISOU 1066  CB  GLU A 139     2429   2060   1501     73    368    213       C  
ATOM   1067  CG  GLU A 139      31.328  32.128  57.431  1.00 14.47           C  
ANISOU 1067  CG  GLU A 139     2294   1886   1317     52    415    250       C  
ATOM   1068  CD  GLU A 139      31.740  31.920  58.876  1.00 19.13           C  
ANISOU 1068  CD  GLU A 139     2951   2477   1841     74    415    272       C  
ATOM   1069  OE1 GLU A 139      32.636  32.649  59.357  1.00 24.87           O  
ANISOU 1069  OE1 GLU A 139     3699   3212   2538    103    372    258       O  
ATOM   1070  OE2 GLU A 139      31.176  31.027  59.518  1.00 19.60           O1-
ANISOU 1070  OE2 GLU A 139     3042   2529   1876     58    456    304       O1-
ATOM   1071  N   THR A 140      30.648  31.681  54.322  1.00 12.13           N  
ANISOU 1071  N   THR A 140     1887   1570   1152     -6    410    224       N  
ATOM   1072  CA  THR A 140      30.752  30.578  53.370  1.00 13.25           C  
ANISOU 1072  CA  THR A 140     2025   1679   1331    -34    407    235       C  
ATOM   1073  C   THR A 140      30.797  31.096  51.939  1.00 12.11           C  
ANISOU 1073  C   THR A 140     1829   1537   1234    -42    383    206       C  
ATOM   1074  O   THR A 140      31.571  30.591  51.109  1.00 12.99           O  
ANISOU 1074  O   THR A 140     1945   1620   1370    -42    357    204       O  
ATOM   1075  CB  THR A 140      29.572  29.626  53.573  1.00 15.65           C  
ANISOU 1075  CB  THR A 140     2333   1978   1634    -79    459    260       C  
ATOM   1076  CG2 THR A 140      29.701  28.401  52.679  1.00 20.55           C  
ANISOU 1076  CG2 THR A 140     2965   2555   2286   -112    456    271       C  
ATOM   1077  OG1 THR A 140      29.550  29.195  54.938  1.00 16.80           O  
ANISOU 1077  OG1 THR A 140     2531   2121   1730    -70    483    289       O  
ATOM   1078  N   VAL A 141      29.987  32.105  51.627  1.00 12.80           N  
ANISOU 1078  N   VAL A 141     1870   1660   1333    -46    393    184       N  
ATOM   1079  CA  VAL A 141      30.044  32.718  50.309  1.00 13.71           C  
ANISOU 1079  CA  VAL A 141     1939   1780   1489    -49    367    158       C  
ATOM   1080  C   VAL A 141      31.384  33.415  50.113  1.00 11.47           C  
ANISOU 1080  C   VAL A 141     1665   1488   1205    -13    321    141       C  
ATOM   1081  O   VAL A 141      32.010  33.282  49.057  1.00 12.05           O  
ANISOU 1081  O   VAL A 141     1726   1545   1308    -16    295    131       O  
ATOM   1082  CB  VAL A 141      28.855  33.673  50.096  1.00 13.55           C  
ANISOU 1082  CB  VAL A 141     1868   1800   1479    -54    388    143       C  
ATOM   1083  CG1 VAL A 141      28.981  34.407  48.766  1.00 14.48           C  
ANISOU 1083  CG1 VAL A 141     1944   1923   1634    -52    358    117       C  
ATOM   1084  CG2 VAL A 141      27.547  32.904  50.144  1.00 15.79           C  
ANISOU 1084  CG2 VAL A 141     2132   2098   1771    -97    432    162       C  
ATOM   1085  N   ASN A 142      31.838  34.188  51.107  1.00 10.85           N  
ANISOU 1085  N   ASN A 142     1608   1422   1092     18    310    136       N  
ATOM   1086  CA  ASN A 142      33.123  34.865  50.960  1.00 10.86           C  
ANISOU 1086  CA  ASN A 142     1615   1419   1093     45    263    121       C  
ATOM   1087  C   ASN A 142      34.235  33.860  50.677  1.00 10.43           C  
ANISOU 1087  C   ASN A 142     1579   1335   1047     49    239    138       C  
ATOM   1088  O   ASN A 142      35.068  34.073  49.785  1.00 10.63           O  
ANISOU 1088  O   ASN A 142     1586   1353   1100     56    209    126       O  
ATOM   1089  CB  ASN A 142      33.410  35.692  52.211  1.00 10.87           C  
ANISOU 1089  CB  ASN A 142     1646   1436   1049     71    255    115       C  
ATOM   1090  CG  ASN A 142      34.504  36.732  52.006  1.00 10.46           C  
ANISOU 1090  CG  ASN A 142     1590   1386    998     90    207     93       C  
ATOM   1091  ND2 ASN A 142      35.117  37.161  53.096  1.00 12.15           N  
ANISOU 1091  ND2 ASN A 142     1840   1607   1170    108    186     92       N  
ATOM   1092  OD1 ASN A 142      34.764  37.173  50.890  1.00 12.26           O  
ANISOU 1092  OD1 ASN A 142     1784   1611   1263     85    188     77       O  
ATOM   1093  N   SER A 143      34.236  32.735  51.383  1.00 10.75           N  
ANISOU 1093  N   SER A 143     1659   1359   1068     47    256    167       N  
ATOM   1094  CA  SER A 143      35.259  31.724  51.149  1.00 11.40           C  
ANISOU 1094  CA  SER A 143     1763   1411   1159     58    238    186       C  
ATOM   1095  C   SER A 143      35.170  31.155  49.740  1.00 10.98           C  
ANISOU 1095  C   SER A 143     1689   1335   1150     37    243    179       C  
ATOM   1096  O   SER A 143      36.204  30.929  49.095  1.00 11.50           O  
ANISOU 1096  O   SER A 143     1751   1384   1234     55    217    178       O  
ATOM   1097  CB  SER A 143      35.130  30.608  52.186  1.00 12.99           C  
ANISOU 1097  CB  SER A 143     2015   1592   1327     59    260    222       C  
ATOM   1098  OG  SER A 143      35.514  31.078  53.463  1.00 14.89           O  
ANISOU 1098  OG  SER A 143     2283   1852   1521     84    246    230       O  
ATOM   1099  N   ALA A 144      33.952  30.893  49.246  1.00 11.02           N  
ANISOU 1099  N   ALA A 144     1678   1339   1171      0    275    175       N  
ATOM   1100  CA  ALA A 144      33.793  30.348  47.900  1.00 11.66           C  
ANISOU 1100  CA  ALA A 144     1745   1399   1289    -25    277    166       C  
ATOM   1101  C   ALA A 144      34.223  31.345  46.829  1.00 11.04           C  
ANISOU 1101  C   ALA A 144     1624   1335   1236    -16    249    137       C  
ATOM   1102  O   ALA A 144      34.808  30.949  45.816  1.00 11.37           O  
ANISOU 1102  O   ALA A 144     1665   1355   1300    -16    237    131       O  
ATOM   1103  CB  ALA A 144      32.335  29.925  47.683  1.00 13.40           C  
ANISOU 1103  CB  ALA A 144     1953   1623   1517    -74    313    168       C  
ATOM   1104  N   VAL A 145      33.895  32.628  47.008  1.00 10.83           N  
ANISOU 1104  N   VAL A 145     1568   1343   1205     -9    241    119       N  
ATOM   1105  CA  VAL A 145      34.334  33.643  46.059  1.00 10.13           C  
ANISOU 1105  CA  VAL A 145     1446   1267   1138      1    214     94       C  
ATOM   1106  C   VAL A 145      35.850  33.695  46.018  1.00  9.47           C  
ANISOU 1106  C   VAL A 145     1372   1172   1055     30    182     96       C  
ATOM   1107  O   VAL A 145      36.459  33.724  44.944  1.00  9.80           O  
ANISOU 1107  O   VAL A 145     1398   1204   1121     32    168     86       O  
ATOM   1108  CB  VAL A 145      33.742  35.021  46.397  1.00 10.48           C  
ANISOU 1108  CB  VAL A 145     1465   1343   1173      8    213     77       C  
ATOM   1109  CG1 VAL A 145      34.340  36.074  45.475  1.00 12.52           C  
ANISOU 1109  CG1 VAL A 145     1697   1607   1451     18    184     55       C  
ATOM   1110  CG2 VAL A 145      32.232  35.004  46.280  1.00 12.79           C  
ANISOU 1110  CG2 VAL A 145     1735   1654   1472    -18    245     77       C  
ATOM   1111  N   LYS A 146      36.476  33.723  47.193  1.00 10.05           N  
ANISOU 1111  N   LYS A 146     1470   1250   1100     54    171    109       N  
ATOM   1112  CA  LYS A 146      37.930  33.766  47.245  1.00 10.47           C  
ANISOU 1112  CA  LYS A 146     1525   1300   1153     82    137    115       C  
ATOM   1113  C   LYS A 146      38.546  32.524  46.615  1.00 10.26           C  
ANISOU 1113  C   LYS A 146     1510   1242   1145     90    142    131       C  
ATOM   1114  O   LYS A 146      39.562  32.618  45.914  1.00 10.81           O  
ANISOU 1114  O   LYS A 146     1563   1311   1234    106    122    127       O  
ATOM   1115  CB  LYS A 146      38.394  33.924  48.687  1.00 10.35           C  
ANISOU 1115  CB  LYS A 146     1536   1298   1099    103    122    129       C  
ATOM   1116  CG  LYS A 146      38.087  35.298  49.282  1.00 10.32           C  
ANISOU 1116  CG  LYS A 146     1526   1321   1075    102    111    108       C  
ATOM   1117  CD  LYS A 146      38.471  35.337  50.748  1.00 11.45           C  
ANISOU 1117  CD  LYS A 146     1705   1475   1172    119     97    122       C  
ATOM   1118  CE  LYS A 146      38.227  36.688  51.374  1.00 14.17           C  
ANISOU 1118  CE  LYS A 146     2054   1840   1490    119     86     99       C  
ATOM   1119  NZ  LYS A 146      38.556  36.696  52.833  1.00 16.37           N1+
ANISOU 1119  NZ  LYS A 146     2376   2129   1717    133     72    111       N1+
ATOM   1120  N   ALA A 147      37.961  31.355  46.856  1.00 10.30           N  
ANISOU 1120  N   ALA A 147     1549   1222   1144     79    171    149       N  
ATOM   1121  CA  ALA A 147      38.510  30.133  46.280  1.00 11.12           C  
ANISOU 1121  CA  ALA A 147     1675   1288   1262     88    179    164       C  
ATOM   1122  C   ALA A 147      38.462  30.184  44.758  1.00  9.80           C  
ANISOU 1122  C   ALA A 147     1485   1111   1128     73    182    142       C  
ATOM   1123  O   ALA A 147      39.411  29.783  44.079  1.00 10.45           O  
ANISOU 1123  O   ALA A 147     1568   1176   1226     95    176    144       O  
ATOM   1124  CB  ALA A 147      37.739  28.917  46.785  1.00 11.78           C  
ANISOU 1124  CB  ALA A 147     1804   1340   1331     70    212    186       C  
ATOM   1125  N   GLN A 148      37.351  30.671  44.205  1.00  9.86           N  
ANISOU 1125  N   GLN A 148     1472   1131   1145     36    194    122       N  
ATOM   1126  CA  GLN A 148      37.227  30.776  42.753  1.00  9.98           C  
ANISOU 1126  CA  GLN A 148     1467   1138   1185     18    194    101       C  
ATOM   1127  C   GLN A 148      38.185  31.828  42.192  1.00  9.30           C  
ANISOU 1127  C   GLN A 148     1347   1074   1112     41    167     86       C  
ATOM   1128  O   GLN A 148      38.838  31.601  41.162  1.00  9.57           O  
ANISOU 1128  O   GLN A 148     1379   1095   1164     49    165     79       O  
ATOM   1129  CB  GLN A 148      35.777  31.069  42.370  1.00 10.04           C  
ANISOU 1129  CB  GLN A 148     1457   1160   1198    -25    208     87       C  
ATOM   1130  CG  GLN A 148      35.592  31.154  40.871  1.00  9.95           C  
ANISOU 1130  CG  GLN A 148     1430   1144   1208    -46    205     66       C  
ATOM   1131  CD  GLN A 148      34.168  30.991  40.407  1.00  9.96           C  
ANISOU 1131  CD  GLN A 148     1419   1151   1213    -94    218     59       C  
ATOM   1132  NE2 GLN A 148      33.963  31.127  39.107  1.00 10.29           N  
ANISOU 1132  NE2 GLN A 148     1448   1192   1269   -113    211     41       N  
ATOM   1133  OE1 GLN A 148      33.265  30.720  41.189  1.00 10.57           O  
ANISOU 1133  OE1 GLN A 148     1499   1236   1280   -114    236     70       O  
ATOM   1134  N  ALEU A 149      38.263  32.998  42.841  0.42  9.77           N  
ANISOU 1134  N  ALEU A 149     1384   1166   1162     49    148     80       N  
ATOM   1135  N  BLEU A 149      38.282  32.979  42.863  0.58  9.76           N  
ANISOU 1135  N  BLEU A 149     1383   1164   1159     50    148     81       N  
ATOM   1136  CA ALEU A 149      39.214  34.022  42.416  0.42  9.76           C  
ANISOU 1136  CA ALEU A 149     1353   1183   1171     65    122     69       C  
ATOM   1137  CA BLEU A 149      39.199  34.028  42.428  0.58  9.73           C  
ANISOU 1137  CA BLEU A 149     1351   1180   1167     65    122     69       C  
ATOM   1138  C  ALEU A 149      40.628  33.455  42.369  0.42  8.56           C  
ANISOU 1138  C  ALEU A 149     1206   1022   1025     97    110     84       C  
ATOM   1139  C  BLEU A 149      40.638  33.520  42.404  0.58 10.02           C  
ANISOU 1139  C  BLEU A 149     1389   1208   1209     97    109     83       C  
ATOM   1140  O  ALEU A 149      41.338  33.587  41.365  0.42 12.14           O  
ANISOU 1140  O  ALEU A 149     1640   1474   1498    104    106     77       O  
ATOM   1141  O  BLEU A 149      41.381  33.766  41.444  0.58  8.65           O  
ANISOU 1141  O  BLEU A 149     1195   1037   1056    104    102     76       O  
ATOM   1142  CB ALEU A 149      39.168  35.213  43.375  0.42 11.37           C  
ANISOU 1142  CB ALEU A 149     1547   1415   1357     70    103     63       C  
ATOM   1143  CB BLEU A 149      39.050  35.224  43.366  0.58  9.56           C  
ANISOU 1143  CB BLEU A 149     1318   1186   1127     68    105     62       C  
ATOM   1144  CG ALEU A 149      38.092  36.271  43.164  0.42  8.98           C  
ANISOU 1144  CG ALEU A 149     1228   1130   1055     51    107     43       C  
ATOM   1145  CG BLEU A 149      39.748  36.522  42.991  0.58 10.63           C  
ANISOU 1145  CG BLEU A 149     1426   1341   1272     72     78     46       C  
ATOM   1146  CD1ALEU A 149      38.075  37.225  44.351  0.42  9.42           C  
ANISOU 1146  CD1ALEU A 149     1291   1205   1086     61     94     39       C  
ATOM   1147  CD2ALEU A 149      38.312  37.036  41.869  0.42 10.74           C  
ANISOU 1147  CD2ALEU A 149     1424   1356   1302     43     97     25       C  
ATOM   1148  CD1BLEU A 149      39.129  37.151  41.759  0.58  9.87           C  
ANISOU 1148  CD1BLEU A 149     1309   1246   1195     53     84     27       C  
ATOM   1149  CD2BLEU A 149      39.672  37.471  44.176  0.58 12.80           C  
ANISOU 1149  CD2BLEU A 149     1707   1634   1521     77     62     42       C  
ATOM   1150  N   ALA A 150      41.052  32.810  43.451  1.00  9.50           N  
ANISOU 1150  N   ALA A 150     1347   1136   1127    119    107    107       N  
ATOM   1151  CA  ALA A 150      42.418  32.313  43.520  1.00 10.35           C  
ANISOU 1151  CA  ALA A 150     1452   1241   1240    156     93    126       C  
ATOM   1152  C   ALA A 150      42.651  31.234  42.469  1.00  9.63           C  
ANISOU 1152  C   ALA A 150     1376   1115   1168    166    118    129       C  
ATOM   1153  O   ALA A 150      43.707  31.206  41.820  1.00 10.48           O  
ANISOU 1153  O   ALA A 150     1463   1227   1293    191    112    131       O  
ATOM   1154  CB  ALA A 150      42.701  31.770  44.923  1.00 11.97           C  
ANISOU 1154  CB  ALA A 150     1684   1446   1417    179     84    153       C  
ATOM   1155  N   ALA A 151      41.689  30.330  42.282  1.00  9.51           N  
ANISOU 1155  N   ALA A 151     1398   1067   1150    146    147    129       N  
ATOM   1156  CA  ALA A 151      41.875  29.243  41.323  1.00  9.98           C  
ANISOU 1156  CA  ALA A 151     1484   1087   1223    153    171    130       C  
ATOM   1157  C   ALA A 151      41.918  29.782  39.897  1.00  9.65           C  
ANISOU 1157  C   ALA A 151     1416   1050   1200    138    174    103       C  
ATOM   1158  O   ALA A 151      42.745  29.348  39.087  1.00 10.68           O  
ANISOU 1158  O   ALA A 151     1550   1165   1343    163    183    103       O  
ATOM   1159  CB  ALA A 151      40.765  28.207  41.467  1.00 10.77           C  
ANISOU 1159  CB  ALA A 151     1632   1148   1312    123    199    134       C  
ATOM   1160  N   MET A 152      41.032  30.716  39.562  1.00  9.08           N  
ANISOU 1160  N   MET A 152     1322    999   1129    101    167     82       N  
ATOM   1161  CA  MET A 152      41.045  31.303  38.229  1.00  9.23           C  
ANISOU 1161  CA  MET A 152     1319   1025   1162     87    167     60       C  
ATOM   1162  C   MET A 152      42.336  32.057  37.980  1.00  8.97           C  
ANISOU 1162  C   MET A 152     1251   1017   1142    116    150     61       C  
ATOM   1163  O   MET A 152      42.978  31.876  36.942  1.00  9.58           O  
ANISOU 1163  O   MET A 152     1324   1086   1231    128    161     56       O  
ATOM   1164  CB  MET A 152      39.833  32.214  38.038  1.00  9.38           C  
ANISOU 1164  CB  MET A 152     1320   1066   1180     47    160     42       C  
ATOM   1165  CG  MET A 152      38.510  31.464  37.917  1.00  9.59           C  
ANISOU 1165  CG  MET A 152     1372   1073   1200     10    178     38       C  
ATOM   1166  SD  MET A 152      37.097  32.568  37.812  1.00  9.99           S  
ANISOU 1166  SD  MET A 152     1388   1157   1250    -28    169     23       S  
ATOM   1167  CE  MET A 152      37.379  33.375  36.239  1.00 11.46           C  
ANISOU 1167  CE  MET A 152     1552   1353   1449    -32    157      2       C  
ATOM   1168  N   TRP A 153      42.735  32.918  38.917  1.00  8.86           N  
ANISOU 1168  N   TRP A 153     1210   1034   1122    125    125     69       N  
ATOM   1169  CA  TRP A 153      43.942  33.708  38.716  1.00  9.15           C  
ANISOU 1169  CA  TRP A 153     1208   1097   1171    143    105     71       C  
ATOM   1170  C   TRP A 153      45.188  32.836  38.701  1.00 10.07           C  
ANISOU 1170  C   TRP A 153     1322   1207   1296    186    112     92       C  
ATOM   1171  O   TRP A 153      46.144  33.169  37.993  1.00 10.17           O  
ANISOU 1171  O   TRP A 153     1305   1235   1325    200    111     92       O  
ATOM   1172  CB  TRP A 153      44.034  34.858  39.720  1.00  9.54           C  
ANISOU 1172  CB  TRP A 153     1236   1180   1211    136     74     70       C  
ATOM   1173  CG  TRP A 153      43.277  36.054  39.237  1.00  9.13           C  
ANISOU 1173  CG  TRP A 153     1171   1138   1159    104     68     47       C  
ATOM   1174  CD1 TRP A 153      42.160  36.627  39.786  1.00  9.65           C  
ANISOU 1174  CD1 TRP A 153     1247   1209   1212     84     65     37       C  
ATOM   1175  CD2 TRP A 153      43.576  36.815  38.060  1.00  8.75           C  
ANISOU 1175  CD2 TRP A 153     1101   1098   1128     92     67     34       C  
ATOM   1176  CE2 TRP A 153      42.619  37.844  37.958  1.00  8.58           C  
ANISOU 1176  CE2 TRP A 153     1078   1083   1101     67     61     17       C  
ATOM   1177  CE3 TRP A 153      44.580  36.742  37.092  1.00  8.98           C  
ANISOU 1177  CE3 TRP A 153     1110   1129   1173    104     74     37       C  
ATOM   1178  NE1 TRP A 153      41.756  37.707  39.014  1.00  9.13           N  
ANISOU 1178  NE1 TRP A 153     1164   1150   1153     64     61     19       N  
ATOM   1179  CZ2 TRP A 153      42.618  38.759  36.923  1.00  9.35           C  
ANISOU 1179  CZ2 TRP A 153     1160   1185   1209     52     58      4       C  
ATOM   1180  CZ3 TRP A 153      44.582  37.665  36.064  1.00  9.34           C  
ANISOU 1180  CZ3 TRP A 153     1140   1182   1228     85     74     23       C  
ATOM   1181  CH2 TRP A 153      43.600  38.651  35.981  1.00  9.93           C  
ANISOU 1181  CH2 TRP A 153     1217   1259   1296     59     64      8       C  
ATOM   1182  N   THR A 154      45.211  31.719  39.438  1.00  9.61           N  
ANISOU 1182  N   THR A 154     1297   1126   1227    210    120    112       N  
ATOM   1183  CA  THR A 154      46.343  30.796  39.324  1.00 10.07           C  
ANISOU 1183  CA  THR A 154     1356   1173   1295    258    131    134       C  
ATOM   1184  C   THR A 154      46.466  30.278  37.896  1.00 10.07           C  
ANISOU 1184  C   THR A 154     1370   1148   1310    264    164    120       C  
ATOM   1185  O   THR A 154      47.555  30.263  37.310  1.00 10.13           O  
ANISOU 1185  O   THR A 154     1351   1167   1333    296    171    127       O  
ATOM   1186  CB  THR A 154      46.184  29.634  40.315  1.00 10.38           C  
ANISOU 1186  CB  THR A 154     1441   1185   1319    282    138    158       C  
ATOM   1187  CG2 THR A 154      47.278  28.601  40.139  1.00 11.27           C  
ANISOU 1187  CG2 THR A 154     1562   1280   1441    339    153    182       C  
ATOM   1188  OG1 THR A 154      46.238  30.137  41.654  1.00 11.07           O  
ANISOU 1188  OG1 THR A 154     1516   1301   1388    282    106    172       O  
ATOM   1189  N   GLN A 155      45.341  29.853  37.316  1.00  9.80           N  
ANISOU 1189  N   GLN A 155     1376   1079   1268    231    185    102       N  
ATOM   1190  CA  GLN A 155      45.364  29.342  35.950  1.00  9.90           C  
ANISOU 1190  CA  GLN A 155     1410   1063   1287    231    215     86       C  
ATOM   1191  C   GLN A 155      45.736  30.425  34.945  1.00 10.10           C  
ANISOU 1191  C   GLN A 155     1394   1120   1324    219    210     69       C  
ATOM   1192  O   GLN A 155      46.498  30.166  33.997  1.00 10.30           O  
ANISOU 1192  O   GLN A 155     1417   1138   1357    243    232     67       O  
ATOM   1193  CB  GLN A 155      44.009  28.743  35.597  1.00 10.58           C  
ANISOU 1193  CB  GLN A 155     1546   1112   1361    188    230     68       C  
ATOM   1194  CG  GLN A 155      43.686  27.454  36.302  1.00 10.64           C  
ANISOU 1194  CG  GLN A 155     1609   1076   1358    197    246     84       C  
ATOM   1195  CD  GLN A 155      42.238  27.096  36.113  1.00 10.77           C  
ANISOU 1195  CD  GLN A 155     1661   1067   1363    140    254     68       C  
ATOM   1196  NE2 GLN A 155      41.420  27.414  37.093  1.00 11.13           N  
ANISOU 1196  NE2 GLN A 155     1698   1130   1400    114    240     75       N  
ATOM   1197  OE1 GLN A 155      41.857  26.560  35.071  1.00 12.28           O  
ANISOU 1197  OE1 GLN A 155     1887   1227   1552    119    272     50       O  
ATOM   1198  N   ILE A 156      45.185  31.628  35.096  1.00  9.38           N  
ANISOU 1198  N   ILE A 156     1273   1059   1232    183    185     58       N  
ATOM   1199  CA  ILE A 156      45.508  32.706  34.161  1.00  9.34           C  
ANISOU 1199  CA  ILE A 156     1234   1080   1236    169    180     45       C  
ATOM   1200  C   ILE A 156      46.982  33.066  34.272  1.00  9.98           C  
ANISOU 1200  C   ILE A 156     1270   1191   1332    203    174     62       C  
ATOM   1201  O   ILE A 156      47.700  33.179  33.267  1.00 10.26           O  
ANISOU 1201  O   ILE A 156     1289   1232   1377    215    192     60       O  
ATOM   1202  CB  ILE A 156      44.594  33.917  34.413  1.00  9.32           C  
ANISOU 1202  CB  ILE A 156     1215   1099   1228    129    155     31       C  
ATOM   1203  CG1 ILE A 156      43.130  33.565  34.146  1.00 10.03           C  
ANISOU 1203  CG1 ILE A 156     1338   1167   1305     95    162     16       C  
ATOM   1204  CG2 ILE A 156      45.045  35.092  33.564  1.00  9.89           C  
ANISOU 1204  CG2 ILE A 156     1254   1197   1309    117    148     22       C  
ATOM   1205  CD1 ILE A 156      42.148  34.552  34.787  1.00 10.62           C  
ANISOU 1205  CD1 ILE A 156     1398   1263   1374     67    140      9       C  
ATOM   1206  N   ALA A 157      47.470  33.224  35.504  1.00  9.84           N  
ANISOU 1206  N   ALA A 157     1230   1194   1314    219    149     81       N  
ATOM   1207  CA  ALA A 157      48.878  33.554  35.700  1.00 11.02           C  
ANISOU 1207  CA  ALA A 157     1329   1378   1478    248    137    100       C  
ATOM   1208  C   ALA A 157      49.777  32.475  35.120  1.00 11.43           C  
ANISOU 1208  C   ALA A 157     1384   1417   1542    297    170    115       C  
ATOM   1209  O   ALA A 157      50.795  32.778  34.471  1.00 11.76           O  
ANISOU 1209  O   ALA A 157     1385   1484   1600    314    180    122       O  
ATOM   1210  CB  ALA A 157      49.159  33.742  37.188  1.00 12.10           C  
ANISOU 1210  CB  ALA A 157     1451   1539   1609    256    101    119       C  
ATOM   1211  N   ASN A 158      49.443  31.204  35.333  1.00 11.51           N  
ANISOU 1211  N   ASN A 158     1443   1386   1543    323    190    121       N  
ATOM   1212  CA  ASN A 158      50.282  30.133  34.803  1.00 12.58           C  
ANISOU 1212  CA  ASN A 158     1590   1502   1687    377    225    135       C  
ATOM   1213  C   ASN A 158      50.288  30.148  33.277  1.00 11.68           C  
ANISOU 1213  C   ASN A 158     1488   1374   1576    370    261    113       C  
ATOM   1214  O   ASN A 158      51.310  29.869  32.647  1.00 12.76           O  
ANISOU 1214  O   ASN A 158     1604   1519   1726    412    288    123       O  
ATOM   1215  CB  ASN A 158      49.828  28.784  35.353  1.00 13.60           C  
ANISOU 1215  CB  ASN A 158     1782   1582   1804    402    240    144       C  
ATOM   1216  CG  ASN A 158      50.311  28.538  36.776  1.00 13.36           C  
ANISOU 1216  CG  ASN A 158     1736   1568   1771    433    212    177       C  
ATOM   1217  ND2 ASN A 158      49.592  27.684  37.496  1.00 18.03           N  
ANISOU 1217  ND2 ASN A 158     2384   2120   2345    434    215    184       N  
ATOM   1218  OD1 ASN A 158      51.314  29.085  37.213  1.00 18.57           O  
ANISOU 1218  OD1 ASN A 158     2338   2276   2443    455    188    196       O  
ATOM   1219  N   ARG A 159      49.151  30.461  32.661  1.00 11.19           N  
ANISOU 1219  N   ARG A 159     1458   1293   1502    320    263     85       N  
ATOM   1220  CA  ARG A 159      49.062  30.463  31.201  1.00 11.58           C  
ANISOU 1220  CA  ARG A 159     1527   1328   1547    310    294     63       C  
ATOM   1221  C   ARG A 159      49.914  31.560  30.581  1.00 11.47           C  
ANISOU 1221  C   ARG A 159     1454   1359   1546    307    293     65       C  
ATOM   1222  O   ARG A 159      50.334  31.436  29.423  1.00 13.45           O  
ANISOU 1222  O   ARG A 159     1710   1604   1795    319    327     58       O  
ATOM   1223  CB  ARG A 159      47.602  30.623  30.770  1.00 12.12           C  
ANISOU 1223  CB  ARG A 159     1636   1373   1597    253    287     36       C  
ATOM   1224  CG  ARG A 159      47.357  30.633  29.277  1.00 12.81           C  
ANISOU 1224  CG  ARG A 159     1750   1444   1672    236    313     12       C  
ATOM   1225  CD  ARG A 159      47.767  29.310  28.644  1.00 12.93           C  
ANISOU 1225  CD  ARG A 159     1819   1415   1680    274    356      9       C  
ATOM   1226  NE  ARG A 159      47.472  29.242  27.219  1.00 14.43           N  
ANISOU 1226  NE  ARG A 159     2047   1586   1851    255    380    -17       N  
ATOM   1227  CZ  ARG A 159      48.195  29.846  26.278  1.00 14.90           C  
ANISOU 1227  CZ  ARG A 159     2080   1669   1911    266    398    -19       C  
ATOM   1228  NH1 ARG A 159      49.258  30.558  26.614  1.00 14.58           N1+
ANISOU 1228  NH1 ARG A 159     1973   1674   1894    291    395      3       N1+
ATOM   1229  NH2 ARG A 159      47.863  29.730  25.007  1.00 14.87           N  
ANISOU 1229  NH2 ARG A 159     2119   1646   1884    247    419    -43       N  
ATOM   1230  N   PHE A 160      50.173  32.629  31.322  1.00 11.32           N  
ANISOU 1230  N   PHE A 160     1474   1189   1637    234    439     21       N  
ATOM   1231  CA  PHE A 160      50.938  33.779  30.848  1.00 12.03           C  
ANISOU 1231  CA  PHE A 160     1510   1349   1713    223    411     23       C  
ATOM   1232  C   PHE A 160      52.272  33.917  31.571  1.00 13.24           C  
ANISOU 1232  C   PHE A 160     1595   1547   1890    284    402     81       C  
ATOM   1233  O   PHE A 160      52.884  34.991  31.550  1.00 13.24           O  
ANISOU 1233  O   PHE A 160     1541   1614   1877    269    364     94       O  
ATOM   1234  CB  PHE A 160      50.091  35.047  30.954  1.00 11.59           C  
ANISOU 1234  CB  PHE A 160     1446   1336   1621    159    345      9       C  
ATOM   1235  CG  PHE A 160      48.920  35.032  30.025  1.00 10.49           C  
ANISOU 1235  CG  PHE A 160     1360   1173   1455     99    353    -43       C  
ATOM   1236  CD1 PHE A 160      49.122  35.099  28.651  1.00 12.05           C  
ANISOU 1236  CD1 PHE A 160     1570   1375   1635     76    385    -80       C  
ATOM   1237  CD2 PHE A 160      47.630  34.908  30.500  1.00 11.22           C  
ANISOU 1237  CD2 PHE A 160     1484   1244   1534     65    331    -53       C  
ATOM   1238  CE1 PHE A 160      48.056  35.062  27.775  1.00 12.56           C  
ANISOU 1238  CE1 PHE A 160     1678   1428   1667     18    389   -125       C  
ATOM   1239  CE2 PHE A 160      46.561  34.863  29.629  1.00 11.15           C  
ANISOU 1239  CE2 PHE A 160     1515   1224   1497      7    336    -96       C  
ATOM   1240  CZ  PHE A 160      46.768  34.932  28.270  1.00 11.39           C  
ANISOU 1240  CZ  PHE A 160     1557   1263   1508    -17    363   -132       C  
ATOM   1241  N   ALA A 161      52.754  32.832  32.181  1.00 15.28           N  
ANISOU 1241  N   ALA A 161     1853   1771   2182    351    438    120       N  
ATOM   1242  CA  ALA A 161      53.955  32.912  33.007  1.00 17.58           C  
ANISOU 1242  CA  ALA A 161     2071   2115   2493    410    423    186       C  
ATOM   1243  C   ALA A 161      55.174  33.338  32.205  1.00 17.47           C  
ANISOU 1243  C   ALA A 161     2002   2151   2486    429    443    191       C  
ATOM   1244  O   ALA A 161      56.109  33.915  32.770  1.00 22.33           O  
ANISOU 1244  O   ALA A 161     2542   2840   3102    447    408    238       O  
ATOM   1245  CB  ALA A 161      54.218  31.562  33.670  1.00 21.60           C  
ANISOU 1245  CB  ALA A 161     2594   2572   3042    486    469    232       C  
ATOM   1246  N   ASP A 162      55.192  33.050  30.908  1.00 15.74           N  
ANISOU 1246  N   ASP A 162     1816   1897   2267    422    499    144       N  
ATOM   1247  CA  ASP A 162      56.326  33.394  30.067  1.00 15.66           C  
ANISOU 1247  CA  ASP A 162     1756   1934   2262    440    527    147       C  
ATOM   1248  C   ASP A 162      56.301  34.834  29.572  1.00 15.43           C  
ANISOU 1248  C   ASP A 162     1698   1970   2195    368    476    125       C  
ATOM   1249  O   ASP A 162      57.286  35.278  28.971  1.00 18.30           O  
ANISOU 1249  O   ASP A 162     2010   2384   2560    376    491    135       O  
ATOM   1250  CB  ASP A 162      56.372  32.447  28.860  1.00 18.21           C  
ANISOU 1250  CB  ASP A 162     2132   2192   2596    463    617    102       C  
ATOM   1251  CG  ASP A 162      55.098  32.503  28.027  1.00 37.82           C  
ANISOU 1251  CG  ASP A 162     4696   4630   5043    387    620     29       C  
ATOM   1252  OD1 ASP A 162      54.009  32.692  28.608  1.00 27.11           O  
ANISOU 1252  OD1 ASP A 162     3371   3258   3671    343    572     20       O  
ATOM   1253  OD2 ASP A 162      55.188  32.360  26.790  1.00 43.86           O1-
ANISOU 1253  OD2 ASP A 162     5489   5382   5793    371    670    -19       O1-
ATOM   1254  N   LYS A 163      55.231  35.572  29.804  1.00 11.88           N  
ANISOU 1254  N   LYS A 163     1278   1520   1716    302    421    100       N  
ATOM   1255  CA  LYS A 163      55.117  36.916  29.258  1.00 12.13           C  
ANISOU 1255  CA  LYS A 163     1293   1600   1717    237    380     81       C  
ATOM   1256  C   LYS A 163      55.807  37.935  30.149  1.00 12.86           C  
ANISOU 1256  C   LYS A 163     1316   1762   1808    227    320    123       C  
ATOM   1257  O   LYS A 163      55.737  37.853  31.379  1.00 15.52           O  
ANISOU 1257  O   LYS A 163     1639   2109   2151    242    284    154       O  
ATOM   1258  CB  LYS A 163      53.646  37.302  29.097  1.00 12.40           C  
ANISOU 1258  CB  LYS A 163     1387   1604   1722    175    350     40       C  
ATOM   1259  CG  LYS A 163      52.865  36.385  28.182  1.00 14.10           C  
ANISOU 1259  CG  LYS A 163     1671   1759   1928    166    402     -8       C  
ATOM   1260  CD  LYS A 163      53.458  36.302  26.782  1.00 15.40           C  
ANISOU 1260  CD  LYS A 163     1837   1932   2083    163    454    -35       C  
ATOM   1261  CE  LYS A 163      52.499  35.598  25.834  1.00 19.89           C  
ANISOU 1261  CE  LYS A 163     2480   2450   2628    131    494    -92       C  
ATOM   1262  NZ  LYS A 163      53.061  35.477  24.464  1.00 23.62           N1+
ANISOU 1262  NZ  LYS A 163     2959   2933   3082    126    549   -124       N1+
ATOM   1263  N   GLY A 164      56.468  38.897  29.522  1.00 12.67           N  
ANISOU 1263  N   GLY A 164     1251   1789   1772    195    310    123       N  
ATOM   1264  CA  GLY A 164      57.110  39.981  30.230  1.00 14.63           C  
ANISOU 1264  CA  GLY A 164     1440   2104   2016    168    254    154       C  
ATOM   1265  C   GLY A 164      56.121  41.021  30.725  1.00 11.69           C  
ANISOU 1265  C   GLY A 164     1098   1726   1619    106    195    134       C  
ATOM   1266  O   GLY A 164      54.898  40.858  30.683  1.00 11.82           O  
ANISOU 1266  O   GLY A 164     1174   1692   1624     90    192    105       O  
ATOM   1267  N   ASN A 165      56.689  42.131  31.194  1.00 10.94           N  
ANISOU 1267  N   ASN A 165      958   1684   1516     68    150    151       N  
ATOM   1268  CA  ASN A 165      55.907  43.139  31.891  1.00 10.39           C  
ANISOU 1268  CA  ASN A 165      913   1608   1426     16     96    137       C  
ATOM   1269  C   ASN A 165      55.125  44.060  30.959  1.00  9.88           C  
ANISOU 1269  C   ASN A 165      889   1518   1346    -36     94    104       C  
ATOM   1270  O   ASN A 165      54.470  44.991  31.457  1.00 10.27           O  
ANISOU 1270  O   ASN A 165      961   1557   1383    -76     56     92       O  
ATOM   1271  CB  ASN A 165      56.770  43.922  32.880  1.00 11.39           C  
ANISOU 1271  CB  ASN A 165      983   1796   1547    -10     49    163       C  
ATOM   1272  CG  ASN A 165      56.923  43.196  34.215  1.00 12.17           C  
ANISOU 1272  CG  ASN A 165     1063   1914   1647     29     29    193       C  
ATOM   1273  ND2 ASN A 165      57.680  43.794  35.130  1.00 14.75           N  
ANISOU 1273  ND2 ASN A 165     1338   2304   1961      4    -15    216       N  
ATOM   1274  OD1 ASN A 165      56.335  42.125  34.435  1.00 13.13           O  
ANISOU 1274  OD1 ASN A 165     1217   1996   1778     77     51    196       O  
ATOM   1275  N   PHE A 166      55.069  43.784  29.650  1.00 10.28           N  
ANISOU 1275  N   PHE A 166      957   1554   1396    -33    136     88       N  
ATOM   1276  CA  PHE A 166      54.040  44.419  28.830  1.00 10.18           C  
ANISOU 1276  CA  PHE A 166      992   1514   1364    -74    134     61       C  
ATOM   1277  C   PHE A 166      52.651  44.029  29.318  1.00  9.46           C  
ANISOU 1277  C   PHE A 166      953   1376   1264    -70    121     42       C  
ATOM   1278  O   PHE A 166      51.684  44.762  29.071  1.00 10.10           O  
ANISOU 1278  O   PHE A 166     1065   1441   1330   -103    103     29       O  
ATOM   1279  CB  PHE A 166      54.187  44.075  27.336  1.00 10.41           C  
ANISOU 1279  CB  PHE A 166     1030   1542   1383    -73    182     48       C  
ATOM   1280  CG  PHE A 166      53.586  42.753  26.934  1.00 10.11           C  
ANISOU 1280  CG  PHE A 166     1033   1466   1342    -41    223     23       C  
ATOM   1281  CD1 PHE A 166      54.294  41.573  27.069  1.00 11.24           C  
ANISOU 1281  CD1 PHE A 166     1163   1603   1506     13    264     29       C  
ATOM   1282  CD2 PHE A 166      52.292  42.690  26.428  1.00 10.17           C  
ANISOU 1282  CD2 PHE A 166     1095   1443   1328    -66    221     -5       C  
ATOM   1283  CE1 PHE A 166      53.739  40.362  26.724  1.00 11.63           C  
ANISOU 1283  CE1 PHE A 166     1258   1606   1556     38    306      3       C  
ATOM   1284  CE2 PHE A 166      51.732  41.479  26.092  1.00 11.13           C  
ANISOU 1284  CE2 PHE A 166     1257   1529   1444    -48    258    -31       C  
ATOM   1285  CZ  PHE A 166      52.460  40.306  26.238  1.00 11.53           C  
ANISOU 1285  CZ  PHE A 166     1301   1563   1518      2    302    -30       C  
ATOM   1286  N   LEU A 167      52.525  42.859  29.962  1.00  9.56           N  
ANISOU 1286  N   LEU A 167      974   1369   1288    -27    135     45       N  
ATOM   1287  CA  LEU A 167      51.235  42.289  30.331  1.00  8.88           C  
ANISOU 1287  CA  LEU A 167      938   1242   1197    -23    132     28       C  
ATOM   1288  C   LEU A 167      50.964  42.533  31.806  1.00  8.58           C  
ANISOU 1288  C   LEU A 167      894   1206   1159    -20     92     43       C  
ATOM   1289  O   LEU A 167      51.761  42.152  32.677  1.00  9.55           O  
ANISOU 1289  O   LEU A 167      985   1350   1294     10     85     69       O  
ATOM   1290  CB  LEU A 167      51.214  40.800  30.013  1.00  9.50           C  
ANISOU 1290  CB  LEU A 167     1038   1287   1286     16    181     19       C  
ATOM   1291  CG  LEU A 167      49.915  40.075  30.377  1.00  9.49           C  
ANISOU 1291  CG  LEU A 167     1087   1241   1280     14    183      3       C  
ATOM   1292  CD1 LEU A 167      48.699  40.630  29.641  1.00  9.99           C  
ANISOU 1292  CD1 LEU A 167     1183   1297   1316    -34    171    -25       C  
ATOM   1293  CD2 LEU A 167      50.081  38.579  30.073  1.00 11.03           C  
ANISOU 1293  CD2 LEU A 167     1306   1395   1490     52    238     -6       C  
ATOM   1294  N   VAL A 168      49.814  43.159  32.059  1.00  8.82           N  
ANISOU 1294  N   VAL A 168      956   1220   1175    -48     66     28       N  
ATOM   1295  CA  VAL A 168      49.301  43.495  33.384  1.00  8.41           C  
ANISOU 1295  CA  VAL A 168      910   1167   1117    -51     32     33       C  
ATOM   1296  C   VAL A 168      48.066  42.645  33.657  1.00  8.27           C  
ANISOU 1296  C   VAL A 168      932   1114   1095    -39     43     24       C  
ATOM   1297  O   VAL A 168      47.247  42.427  32.759  1.00  8.72           O  
ANISOU 1297  O   VAL A 168     1017   1151   1147    -53     60      5       O  
ATOM   1298  CB  VAL A 168      48.906  44.988  33.397  1.00  8.33           C  
ANISOU 1298  CB  VAL A 168      907   1162   1096    -92      3     23       C  
ATOM   1299  CG1 VAL A 168      48.204  45.393  34.689  1.00  9.36           C  
ANISOU 1299  CG1 VAL A 168     1054   1287   1216    -96    -26     20       C  
ATOM   1300  CG2 VAL A 168      50.106  45.876  33.136  1.00 10.10           C  
ANISOU 1300  CG2 VAL A 168     1095   1418   1324   -114     -7     32       C  
ATOM   1301  N   PHE A 169      47.920  42.181  34.902  1.00  8.26           N  
ANISOU 1301  N   PHE A 169      932   1113   1094    -18     30     38       N  
ATOM   1302  CA  PHE A 169      46.681  41.541  35.345  1.00  8.51           C  
ANISOU 1302  CA  PHE A 169      999   1115   1120    -15     36     32       C  
ATOM   1303  C   PHE A 169      45.921  42.522  36.243  1.00  7.89           C  
ANISOU 1303  C   PHE A 169      928   1046   1024    -34      3     28       C  
ATOM   1304  O   PHE A 169      46.511  43.062  37.185  1.00  8.82           O  
ANISOU 1304  O   PHE A 169     1027   1190   1134    -34    -22     38       O  
ATOM   1305  CB  PHE A 169      46.957  40.277  36.177  1.00  8.63           C  
ANISOU 1305  CB  PHE A 169     1014   1119   1146     25     51     57       C  
ATOM   1306  CG  PHE A 169      47.779  39.205  35.489  1.00  9.16           C  
ANISOU 1306  CG  PHE A 169     1076   1169   1236     57     92     66       C  
ATOM   1307  CD1 PHE A 169      47.852  39.061  34.112  1.00  9.48           C  
ANISOU 1307  CD1 PHE A 169     1128   1193   1281     45    122     41       C  
ATOM   1308  CD2 PHE A 169      48.477  38.314  36.290  1.00  9.59           C  
ANISOU 1308  CD2 PHE A 169     1115   1224   1305    103    102    102       C  
ATOM   1309  CE1 PHE A 169      48.617  38.048  33.549  1.00 10.71           C  
ANISOU 1309  CE1 PHE A 169     1283   1329   1458     79    167     46       C  
ATOM   1310  CE2 PHE A 169      49.241  37.306  35.734  1.00 11.01           C  
ANISOU 1310  CE2 PHE A 169     1291   1382   1510    142    147    114       C  
ATOM   1311  CZ  PHE A 169      49.310  37.165  34.363  1.00 10.90           C  
ANISOU 1311  CZ  PHE A 169     1292   1346   1502    131    182     82       C  
ATOM   1312  N   GLU A 170      44.622  42.705  35.981  1.00  7.60           N  
ANISOU 1312  N   GLU A 170      918    992    979    -51      5     13       N  
ATOM   1313  CA  GLU A 170      43.724  43.538  36.784  1.00  7.69           C  
ANISOU 1313  CA  GLU A 170      940   1006    976    -62    -16      8       C  
ATOM   1314  C   GLU A 170      42.711  42.614  37.458  1.00  7.60           C  
ANISOU 1314  C   GLU A 170      948    982    959    -52     -5     13       C  
ATOM   1315  O   GLU A 170      42.016  41.860  36.783  1.00  7.97           O  
ANISOU 1315  O   GLU A 170     1009   1011   1010    -58     15      8       O  
ATOM   1316  CB  GLU A 170      43.030  44.544  35.869  1.00  8.06           C  
ANISOU 1316  CB  GLU A 170      993   1048   1020    -85    -18     -5       C  
ATOM   1317  CG  GLU A 170      41.944  45.363  36.524  1.00  8.18           C  
ANISOU 1317  CG  GLU A 170     1021   1060   1025    -89    -28     -9       C  
ATOM   1318  CD  GLU A 170      41.195  46.190  35.502  1.00  7.82           C  
ANISOU 1318  CD  GLU A 170      979   1010    981   -103    -26    -11       C  
ATOM   1319  OE1 GLU A 170      41.783  47.197  34.989  1.00  8.35           O  
ANISOU 1319  OE1 GLU A 170     1041   1076   1054   -114    -32    -11       O  
ATOM   1320  OE2 GLU A 170      40.045  45.837  35.174  1.00  8.63           O1-
ANISOU 1320  OE2 GLU A 170     1086   1113   1078   -105    -18     -8       O1-
ATOM   1321  N   ALA A 171      42.626  42.680  38.789  1.00  7.96           N  
ANISOU 1321  N   ALA A 171      994   1039    992    -41    -19     23       N  
ATOM   1322  CA  ALA A 171      41.972  41.637  39.577  1.00  8.40           C  
ANISOU 1322  CA  ALA A 171     1063   1086   1043    -27     -7     37       C  
ATOM   1323  C   ALA A 171      40.535  41.396  39.153  1.00  7.82           C  
ANISOU 1323  C   ALA A 171     1007    996    967    -43      7     28       C  
ATOM   1324  O   ALA A 171      40.083  40.244  39.098  1.00  8.56           O  
ANISOU 1324  O   ALA A 171     1115   1071   1067    -42     28     36       O  
ATOM   1325  CB  ALA A 171      41.980  42.068  41.038  1.00  9.02           C  
ANISOU 1325  CB  ALA A 171     1140   1190   1098    -20    -27     45       C  
ATOM   1326  N   MET A 172      39.784  42.484  38.962  1.00  7.46           N  
ANISOU 1326  N   MET A 172      961    960    914    -57     -2     15       N  
ATOM   1327  CA  MET A 172      38.352  42.468  38.678  1.00  7.89           C  
ANISOU 1327  CA  MET A 172     1021   1014    963    -70      7     12       C  
ATOM   1328  C   MET A 172      37.991  43.867  38.215  1.00  7.48           C  
ANISOU 1328  C   MET A 172      961    970    909    -76     -4      4       C  
ATOM   1329  O   MET A 172      38.855  44.749  38.122  1.00  8.41           O  
ANISOU 1329  O   MET A 172     1076   1087   1031    -74    -16     -3       O  
ATOM   1330  CB  MET A 172      37.534  41.982  39.865  1.00  9.36           C  
ANISOU 1330  CB  MET A 172     1214   1205   1137    -63     13     24       C  
ATOM   1331  CG  MET A 172      37.659  42.782  41.107  1.00  9.84           C  
ANISOU 1331  CG  MET A 172     1276   1281   1180    -48      1     24       C  
ATOM   1332  SD  MET A 172      37.201  41.822  42.581  1.00 10.85           S  
ANISOU 1332  SD  MET A 172     1414   1420   1290    -36     11     45       S  
ATOM   1333  CE  MET A 172      38.760  40.972  42.850  1.00 12.25           C  
ANISOU 1333  CE  MET A 172     1589   1593   1473    -20      4     63       C  
ATOM   1334  N   ASN A 173      36.705  44.057  37.893  1.00  7.42           N  
ANISOU 1334  N   ASN A 173      949    972    898    -83      2      8       N  
ATOM   1335  CA  ASN A 173      36.233  45.253  37.202  1.00  7.85           C  
ANISOU 1335  CA  ASN A 173      994   1033    955    -83     -3     10       C  
ATOM   1336  C   ASN A 173      35.524  46.213  38.155  1.00  7.30           C  
ANISOU 1336  C   ASN A 173      927    966    882    -62      0     11       C  
ATOM   1337  O   ASN A 173      36.203  46.945  38.888  1.00  8.09           O  
ANISOU 1337  O   ASN A 173     1040   1053    981    -52     -5     -1       O  
ATOM   1338  CB  ASN A 173      35.387  44.849  35.988  1.00  7.55           C  
ANISOU 1338  CB  ASN A 173      942   1012    913   -105      1     18       C  
ATOM   1339  CG  ASN A 173      34.935  46.047  35.205  1.00  7.57           C  
ANISOU 1339  CG  ASN A 173      931   1027    918   -101     -5     31       C  
ATOM   1340  ND2 ASN A 173      33.675  46.061  34.789  1.00  7.69           N  
ANISOU 1340  ND2 ASN A 173      925   1070    926   -107     -4     49       N  
ATOM   1341  OD1 ASN A 173      35.718  46.973  35.001  1.00  7.71           O  
ANISOU 1341  OD1 ASN A 173      954   1029    945    -93    -11     29       O  
ATOM   1342  N   GLU A 174      34.184  46.216  38.161  1.00  7.40           N  
ANISOU 1342  N   GLU A 174      926    996    890    -57     10     25       N  
ATOM   1343  CA  GLU A 174      33.372  47.184  38.899  1.00  7.54           C  
ANISOU 1343  CA  GLU A 174      943   1015    906    -31     21     29       C  
ATOM   1344  C   GLU A 174      32.542  46.419  39.913  1.00  7.73           C  
ANISOU 1344  C   GLU A 174      963   1057    917    -26     34     34       C  
ATOM   1345  O   GLU A 174      31.525  45.815  39.577  1.00  8.81           O  
ANISOU 1345  O   GLU A 174     1078   1219   1050    -37     40     52       O  
ATOM   1346  CB  GLU A 174      32.470  47.968  37.947  1.00  8.07           C  
ANISOU 1346  CB  GLU A 174      988   1096    984    -21     24     51       C  
ATOM   1347  CG  GLU A 174      33.228  48.897  37.043  1.00  8.38           C  
ANISOU 1347  CG  GLU A 174     1033   1114   1036    -22     16     52       C  
ATOM   1348  CD  GLU A 174      32.364  49.722  36.113  1.00  8.91           C  
ANISOU 1348  CD  GLU A 174     1077   1196   1112     -7     19     84       C  
ATOM   1349  OE1 GLU A 174      31.155  49.405  35.953  1.00 10.03           O  
ANISOU 1349  OE1 GLU A 174     1189   1375   1247     -3     24    108       O  
ATOM   1350  OE2 GLU A 174      32.866  50.728  35.537  1.00  9.70           O1-
ANISOU 1350  OE2 GLU A 174     1186   1273   1225      0     18     90       O1-
ATOM   1351  N   ILE A 175      32.990  46.424  41.153  1.00  8.13           N  
ANISOU 1351  N   ILE A 175     1035   1100    955    -16     37     20       N  
ATOM   1352  CA  ILE A 175      32.377  45.630  42.210  1.00  8.13           C  
ANISOU 1352  CA  ILE A 175     1035   1118    937    -13     50     28       C  
ATOM   1353  C   ILE A 175      31.430  46.512  43.018  1.00  8.34           C  
ANISOU 1353  C   ILE A 175     1060   1155    954     15     72     26       C  
ATOM   1354  O   ILE A 175      31.829  47.544  43.581  1.00  8.92           O  
ANISOU 1354  O   ILE A 175     1155   1211   1022     32     76      5       O  
ATOM   1355  CB  ILE A 175      33.461  45.004  43.098  1.00  8.73           C  
ANISOU 1355  CB  ILE A 175     1132   1187    999    -18     40     20       C  
ATOM   1356  CG1 ILE A 175      34.370  44.076  42.264  1.00  9.35           C  
ANISOU 1356  CG1 ILE A 175     1209   1252   1091    -37     27     24       C  
ATOM   1357  CG2 ILE A 175      32.832  44.278  44.279  1.00  9.48           C  
ANISOU 1357  CG2 ILE A 175     1229   1301   1071    -14     56     32       C  
ATOM   1358  CD1 ILE A 175      33.660  42.957  41.514  1.00 10.35           C  
ANISOU 1358  CD1 ILE A 175     1325   1381   1226    -58     37     39       C  
ATOM   1359  N   HIS A 176      30.164  46.094  43.069  1.00  8.94           N  
ANISOU 1359  N   HIS A 176     1111   1258   1027     17     89     48       N  
ATOM   1360  CA  HIS A 176      29.151  46.753  43.878  1.00  9.30           C  
ANISOU 1360  CA  HIS A 176     1149   1320   1064     48    117     51       C  
ATOM   1361  C   HIS A 176      28.039  45.747  44.154  1.00  9.67           C  
ANISOU 1361  C   HIS A 176     1168   1406   1101     35    131     77       C  
ATOM   1362  O   HIS A 176      27.898  44.729  43.454  1.00  9.73           O  
ANISOU 1362  O   HIS A 176     1159   1424   1114      0    119     93       O  
ATOM   1363  CB  HIS A 176      28.588  48.009  43.200  1.00  9.69           C  
ANISOU 1363  CB  HIS A 176     1184   1364   1134     78    128     58       C  
ATOM   1364  CG  HIS A 176      27.835  47.721  41.955  1.00  9.31           C  
ANISOU 1364  CG  HIS A 176     1093   1344   1101     66    119     91       C  
ATOM   1365  CD2 HIS A 176      28.270  47.455  40.701  1.00 10.60           C  
ANISOU 1365  CD2 HIS A 176     1247   1505   1274     38     94     97       C  
ATOM   1366  ND1 HIS A 176      26.461  47.651  41.918  1.00 10.23           N  
ANISOU 1366  ND1 HIS A 176     1166   1504   1217     78    137    122       N  
ATOM   1367  CE1 HIS A 176      26.082  47.363  40.688  1.00  9.97           C  
ANISOU 1367  CE1 HIS A 176     1099   1499   1192     55    119    146       C  
ATOM   1368  NE2 HIS A 176      27.161  47.243  39.925  1.00 10.18           N  
ANISOU 1368  NE2 HIS A 176     1148   1496   1223     30     94    130       N  
ATOM   1369  N   ASP A 177      27.228  46.058  45.161  1.00  9.52           N  
ANISOU 1369  N   ASP A 177     1143   1407   1066     61    161     81       N  
ATOM   1370  CA  ASP A 177      26.231  45.108  45.639  1.00  9.78           C  
ANISOU 1370  CA  ASP A 177     1150   1479   1085     46    178    106       C  
ATOM   1371  C   ASP A 177      24.933  45.114  44.859  1.00  9.34           C  
ANISOU 1371  C   ASP A 177     1041   1464   1045     44    187    138       C  
ATOM   1372  O   ASP A 177      23.995  44.416  45.262  1.00 11.16           O  
ANISOU 1372  O   ASP A 177     1243   1733   1263     29    204    161       O  
ATOM   1373  CB  ASP A 177      25.959  45.335  47.135  1.00 10.10           C  
ANISOU 1373  CB  ASP A 177     1208   1533   1097     71    208     98       C  
ATOM   1374  CG  ASP A 177      25.237  46.635  47.457  1.00 10.09           C  
ANISOU 1374  CG  ASP A 177     1200   1538   1097    121    241     90       C  
ATOM   1375  OD1 ASP A 177      24.861  47.400  46.545  1.00 11.11           O  
ANISOU 1375  OD1 ASP A 177     1306   1662   1254    141    243     99       O  
ATOM   1376  OD2 ASP A 177      25.010  46.840  48.659  1.00 12.16           O1-
ANISOU 1376  OD2 ASP A 177     1479   1811   1331    140    271     78       O1-
ATOM   1377  N   GLY A 178      24.883  45.838  43.739  1.00 10.02           N  
ANISOU 1377  N   GLY A 178     1109   1547   1152     54    174    144       N  
ATOM   1378  CA  GLY A 178      23.682  46.025  42.949  1.00 10.44           C  
ANISOU 1378  CA  GLY A 178     1103   1647   1216     58    178    180       C  
ATOM   1379  C   GLY A 178      23.263  47.479  42.862  1.00 10.28           C  
ANISOU 1379  C   GLY A 178     1070   1624   1212    119    199    190       C  
ATOM   1380  O   GLY A 178      22.667  47.896  41.862  1.00 11.63           O  
ANISOU 1380  O   GLY A 178     1198   1824   1398    129    192    222       O  
ATOM   1381  N   SER A 179      23.594  48.272  43.890  1.00 10.72           N  
ANISOU 1381  N   SER A 179     1164   1644   1263    161    226    163       N  
ATOM   1382  CA  SER A 179      23.177  49.660  43.962  1.00 10.74           C  
ANISOU 1382  CA  SER A 179     1165   1632   1285    224    258    168       C  
ATOM   1383  C   SER A 179      24.234  50.650  43.515  1.00 11.33           C  
ANISOU 1383  C   SER A 179     1285   1643   1377    237    247    143       C  
ATOM   1384  O   SER A 179      24.078  51.856  43.759  1.00 12.12           O  
ANISOU 1384  O   SER A 179     1403   1710   1493    289    279    137       O  
ATOM   1385  CB  SER A 179      22.716  49.987  45.379  1.00 12.82           C  
ANISOU 1385  CB  SER A 179     1445   1896   1531    261    305    151       C  
ATOM   1386  OG  SER A 179      21.497  49.327  45.668  1.00 15.89           O  
ANISOU 1386  OG  SER A 179     1778   2350   1908    260    324    186       O  
ATOM   1387  N   TRP A 180      25.296  50.185  42.863  1.00 10.40           N  
ANISOU 1387  N   TRP A 180     1187   1505   1259    192    206    128       N  
ATOM   1388  CA  TRP A 180      26.190  51.074  42.120  1.00 10.49           C  
ANISOU 1388  CA  TRP A 180     1226   1468   1291    198    192    117       C  
ATOM   1389  C   TRP A 180      26.861  52.114  43.012  1.00 10.99           C  
ANISOU 1389  C   TRP A 180     1347   1473   1355    223    215     75       C  
ATOM   1390  O   TRP A 180      27.165  53.224  42.568  1.00 13.02           O  
ANISOU 1390  O   TRP A 180     1625   1687   1636    246    224     73       O  
ATOM   1391  CB  TRP A 180      25.476  51.693  40.922  1.00 11.51           C  
ANISOU 1391  CB  TRP A 180     1313   1615   1445    223    192    164       C  
ATOM   1392  CG  TRP A 180      25.275  50.727  39.799  1.00 11.00           C  
ANISOU 1392  CG  TRP A 180     1205   1600   1373    177    156    192       C  
ATOM   1393  CD1 TRP A 180      24.192  49.929  39.563  1.00 12.06           C  
ANISOU 1393  CD1 TRP A 180     1284   1801   1496    160    152    225       C  
ATOM   1394  CD2 TRP A 180      26.208  50.450  38.771  1.00 10.79           C  
ANISOU 1394  CD2 TRP A 180     1191   1562   1348    137    120    186       C  
ATOM   1395  CE2 TRP A 180      25.629  49.488  37.927  1.00 11.70           C  
ANISOU 1395  CE2 TRP A 180     1261   1735   1449     96     98    211       C  
ATOM   1396  CE3 TRP A 180      27.471  50.941  38.467  1.00 10.92           C  
ANISOU 1396  CE3 TRP A 180     1250   1527   1373    128    107    160       C  
ATOM   1397  NE1 TRP A 180      24.396  49.181  38.439  1.00 12.86           N  
ANISOU 1397  NE1 TRP A 180     1368   1931   1590    108    116    235       N  
ATOM   1398  CZ2 TRP A 180      26.282  49.003  36.799  1.00 13.52           C  
ANISOU 1398  CZ2 TRP A 180     1495   1970   1673     51     67    208       C  
ATOM   1399  CZ3 TRP A 180      28.115  50.463  37.340  1.00 12.14           C  
ANISOU 1399  CZ3 TRP A 180     1400   1688   1523     87     76    163       C  
ATOM   1400  CH2 TRP A 180      27.523  49.510  36.530  1.00 12.77           C  
ANISOU 1400  CH2 TRP A 180     1441   1823   1587     51     58    184       C  
ATOM   1401  N   GLY A 181      27.142  51.750  44.253  1.00 11.06           N  
ANISOU 1401  N   GLY A 181     1386   1481   1335    213    225     41       N  
ATOM   1402  CA  GLY A 181      27.803  52.626  45.197  1.00 12.20           C  
ANISOU 1402  CA  GLY A 181     1587   1579   1469    224    245     -6       C  
ATOM   1403  C   GLY A 181      26.892  53.296  46.194  1.00 12.05           C  
ANISOU 1403  C   GLY A 181     1580   1558   1441    271    299    -18       C  
ATOM   1404  O   GLY A 181      27.389  53.932  47.133  1.00 12.74           O  
ANISOU 1404  O   GLY A 181     1721   1611   1510    273    319    -65       O  
ATOM   1405  N   TRP A 182      25.585  53.157  46.029  1.00 11.48           N  
ANISOU 1405  N   TRP A 182     1457   1524   1379    307    324     24       N  
ATOM   1406  CA  TRP A 182      24.597  53.800  46.886  1.00 13.06           C  
ANISOU 1406  CA  TRP A 182     1659   1727   1576    362    384     20       C  
ATOM   1407  C   TRP A 182      23.707  52.728  47.490  1.00 13.35           C  
ANISOU 1407  C   TRP A 182     1653   1834   1586    355    392     43       C  
ATOM   1408  O   TRP A 182      22.475  52.837  47.471  1.00 16.74           O  
ANISOU 1408  O   TRP A 182     2034   2300   2027    396    427     80       O  
ATOM   1409  CB  TRP A 182      23.804  54.822  46.074  1.00 14.72           C  
ANISOU 1409  CB  TRP A 182     1843   1920   1832    422    413     58       C  
ATOM   1410  CG  TRP A 182      24.718  55.869  45.567  1.00 16.55           C  
ANISOU 1410  CG  TRP A 182     2125   2076   2089    424    409     36       C  
ATOM   1411  CD1 TRP A 182      25.318  55.915  44.345  1.00 20.98           C  
ANISOU 1411  CD1 TRP A 182     2675   2623   2673    400    367     58       C  
ATOM   1412  CD2 TRP A 182      25.196  56.997  46.295  1.00 22.67           C  
ANISOU 1412  CD2 TRP A 182     2971   2777   2865    443    448    -18       C  
ATOM   1413  CE2 TRP A 182      26.073  57.701  45.449  1.00 24.07           C  
ANISOU 1413  CE2 TRP A 182     3177   2896   3070    428    428    -22       C  
ATOM   1414  CE3 TRP A 182      24.962  57.485  47.583  1.00 24.57           C  
ANISOU 1414  CE3 TRP A 182     3257   2996   3082    468    501    -65       C  
ATOM   1415  NE1 TRP A 182      26.128  57.024  44.260  1.00 25.66           N  
ANISOU 1415  NE1 TRP A 182     3327   3139   3285    404    379     27       N  
ATOM   1416  CZ2 TRP A 182      26.706  58.876  45.844  1.00 36.34           C  
ANISOU 1416  CZ2 TRP A 182     4805   4368   4635    433    458    -71       C  
ATOM   1417  CZ3 TRP A 182      25.592  58.648  47.975  1.00 36.89           C  
ANISOU 1417  CZ3 TRP A 182     4893   4474   4648    473    532   -119       C  
ATOM   1418  CH2 TRP A 182      26.455  59.330  47.109  1.00 34.11           C  
ANISOU 1418  CH2 TRP A 182     4570   4061   4329    453    510   -121       C  
ATOM   1419  N   GLY A 183      24.344  51.673  48.003  1.00 14.45           N  
ANISOU 1419  N   GLY A 183     1807   1993   1692    303    362     27       N  
ATOM   1420  CA  GLY A 183      23.649  50.575  48.639  1.00 14.42           C  
ANISOU 1420  CA  GLY A 183     1771   2049   1661    287    369     48       C  
ATOM   1421  C   GLY A 183      24.112  50.348  50.059  1.00 14.03           C  
ANISOU 1421  C   GLY A 183     1768   2001   1563    274    382     10       C  
ATOM   1422  O   GLY A 183      24.411  51.298  50.801  1.00 13.45           O  
ANISOU 1422  O   GLY A 183     1742   1894   1472    297    411    -34       O  
ATOM   1423  N   ASP A 184      24.179  49.077  50.457  1.00 13.94           N  
ANISOU 1423  N   ASP A 184     1744   2027   1524    234    363     27       N  
ATOM   1424  CA  ASP A 184      24.544  48.752  51.829  1.00 12.82           C  
ANISOU 1424  CA  ASP A 184     1639   1900   1330    222    374      2       C  
ATOM   1425  C   ASP A 184      26.006  49.051  52.108  1.00 13.86           C  
ANISOU 1425  C   ASP A 184     1828   1996   1444    197    341    -41       C  
ATOM   1426  O   ASP A 184      26.390  49.120  53.284  1.00 13.77           O  
ANISOU 1426  O   ASP A 184     1853   1996   1383    190    351    -70       O  
ATOM   1427  CB  ASP A 184      24.211  47.288  52.125  1.00 12.73           C  
ANISOU 1427  CB  ASP A 184     1600   1936   1301    187    363     41       C  
ATOM   1428  CG  ASP A 184      22.727  47.033  52.280  1.00 16.68           C  
ANISOU 1428  CG  ASP A 184     2049   2485   1804    206    404     78       C  
ATOM   1429  OD1 ASP A 184      21.928  47.989  52.240  1.00 17.60           O  
ANISOU 1429  OD1 ASP A 184     2148   2605   1934    253    444     75       O  
ATOM   1430  OD2 ASP A 184      22.360  45.849  52.466  1.00 20.57           O1-
ANISOU 1430  OD2 ASP A 184     2517   3014   2285    172    399    113       O1-
ATOM   1431  N   ASN A 185      26.816  49.286  51.075  1.00 12.82           N  
ANISOU 1431  N   ASN A 185     1700   1825   1345    183    304    -46       N  
ATOM   1432  CA  ASN A 185      28.192  49.702  51.301  1.00 13.26           C  
ANISOU 1432  CA  ASN A 185     1802   1851   1386    159    276    -86       C  
ATOM   1433  C   ASN A 185      28.267  50.993  52.102  1.00 11.93           C  
ANISOU 1433  C   ASN A 185     1681   1656   1194    179    311   -138       C  
ATOM   1434  O   ASN A 185      29.267  51.233  52.789  1.00 12.73           O  
ANISOU 1434  O   ASN A 185     1825   1753   1260    151    294   -177       O  
ATOM   1435  CB  ASN A 185      28.913  49.896  49.965  1.00 12.30           C  
ANISOU 1435  CB  ASN A 185     1673   1693   1309    145    239    -80       C  
ATOM   1436  CG  ASN A 185      28.225  50.898  49.070  1.00 12.13           C  
ANISOU 1436  CG  ASN A 185     1638   1641   1330    181    263    -74       C  
ATOM   1437  ND2 ASN A 185      28.857  52.049  48.857  1.00 12.17           N  
ANISOU 1437  ND2 ASN A 185     1679   1596   1349    186    265   -107       N  
ATOM   1438  OD1 ASN A 185      27.126  50.644  48.577  1.00 13.45           O  
ANISOU 1438  OD1 ASN A 185     1761   1832   1517    202    279    -36       O  
ATOM   1439  N   ARG A 186      27.236  51.841  52.016  1.00 12.38           N  
ANISOU 1439  N   ARG A 186     1734   1697   1273    226    360   -141       N  
ATOM   1440  CA  ARG A 186      27.259  53.116  52.704  1.00 13.83           C  
ANISOU 1440  CA  ARG A 186     1972   1843   1442    248    403   -195       C  
ATOM   1441  C   ARG A 186      26.866  53.001  54.163  1.00 15.08           C  
ANISOU 1441  C   ARG A 186     2154   2038   1539    253    441   -221       C  
ATOM   1442  O   ARG A 186      27.172  53.907  54.949  1.00 16.39           O  
ANISOU 1442  O   ARG A 186     2378   2178   1674    252    470   -280       O  
ATOM   1443  CB  ARG A 186      26.248  54.077  52.067  1.00 16.53           C  
ANISOU 1443  CB  ARG A 186     2298   2149   1832    308    452   -181       C  
ATOM   1444  CG  ARG A 186      26.485  54.352  50.608  1.00 19.32           C  
ANISOU 1444  CG  ARG A 186     2628   2468   2243    311    423   -151       C  
ATOM   1445  CD  ARG A 186      27.136  55.694  50.420  1.00 32.37           C  
ANISOU 1445  CD  ARG A 186     4337   4045   3917    317    437   -194       C  
ATOM   1446  NE  ARG A 186      27.629  55.854  49.059  1.00 29.37           N  
ANISOU 1446  NE  ARG A 186     3939   3637   3583    306    400   -166       N  
ATOM   1447  CZ  ARG A 186      28.579  56.711  48.707  1.00 24.00           C  
ANISOU 1447  CZ  ARG A 186     3303   2896   2919    286    390   -196       C  
ATOM   1448  NH1 ARG A 186      29.145  57.489  49.620  1.00 23.90           N1+
ANISOU 1448  NH1 ARG A 186     3357   2843   2881    269    412   -260       N1+
ATOM   1449  NH2 ARG A 186      28.968  56.778  47.440  1.00 19.91           N  
ANISOU 1449  NH2 ARG A 186     2763   2361   2441    276    357   -164       N  
ATOM   1450  N   THR A 187      26.169  51.935  54.538  1.00 14.73           N  
ANISOU 1450  N   THR A 187     2069   2054   1474    253    445   -180       N  
ATOM   1451  CA  THR A 187      25.542  51.848  55.838  1.00 16.84           C  
ANISOU 1451  CA  THR A 187     2350   2362   1687    267    491   -195       C  
ATOM   1452  C   THR A 187      25.982  50.653  56.666  1.00 14.46           C  
ANISOU 1452  C   THR A 187     2046   2118   1329    223    460   -178       C  
ATOM   1453  O   THR A 187      25.611  50.583  57.836  1.00 18.39           O  
ANISOU 1453  O   THR A 187     2561   2655   1770    227    494   -193       O  
ATOM   1454  CB  THR A 187      24.012  51.802  55.673  1.00 20.01           C  
ANISOU 1454  CB  THR A 187     2700   2790   2115    319    543   -155       C  
ATOM   1455  CG2 THR A 187      23.504  53.080  55.007  1.00 30.06           C  
ANISOU 1455  CG2 THR A 187     3976   4008   3439    374    584   -166       C  
ATOM   1456  OG1 THR A 187      23.648  50.679  54.866  1.00 26.03           O  
ANISOU 1456  OG1 THR A 187     3398   3585   2906    302    509    -91       O  
ATOM   1457  N   ASP A 188      26.784  49.747  56.135  1.00 12.52           N  
ANISOU 1457  N   ASP A 188     1784   1879   1096    185    400   -148       N  
ATOM   1458  CA  ASP A 188      27.062  48.476  56.795  1.00 11.90           C  
ANISOU 1458  CA  ASP A 188     1695   1852    976    154    375   -114       C  
ATOM   1459  C   ASP A 188      28.262  48.528  57.725  1.00 14.85           C  
ANISOU 1459  C   ASP A 188     2112   2242   1288    119    346   -147       C  
ATOM   1460  O   ASP A 188      28.702  47.471  58.203  1.00 21.27           O  
ANISOU 1460  O   ASP A 188     2917   3095   2069     94    317   -112       O  
ATOM   1461  CB  ASP A 188      27.227  47.336  55.778  1.00 11.86           C  
ANISOU 1461  CB  ASP A 188     1647   1843   1016    134    333    -59       C  
ATOM   1462  CG  ASP A 188      28.522  47.429  54.973  1.00 11.62           C  
ANISOU 1462  CG  ASP A 188     1628   1776   1013    111    280    -71       C  
ATOM   1463  OD1 ASP A 188      29.228  48.477  55.055  1.00 11.63           O  
ANISOU 1463  OD1 ASP A 188     1665   1749   1005    108    274   -120       O  
ATOM   1464  OD2 ASP A 188      28.814  46.454  54.260  1.00 12.32           O1-
ANISOU 1464  OD2 ASP A 188     1691   1861   1130     93    248    -32       O1-
ATOM   1465  N   GLY A 189      28.814  49.711  57.981  1.00 12.96           N  
ANISOU 1465  N   GLY A 189     1920   1975   1031    115    352   -210       N  
ATOM   1466  CA  GLY A 189      29.968  49.831  58.840  1.00 14.40           C  
ANISOU 1466  CA  GLY A 189     2141   2182   1151     73    320   -243       C  
ATOM   1467  C   GLY A 189      31.292  49.572  58.169  1.00 14.03           C  
ANISOU 1467  C   GLY A 189     2085   2121   1125     39    255   -233       C  
ATOM   1468  O   GLY A 189      32.330  49.589  58.845  1.00 16.72           O  
ANISOU 1468  O   GLY A 189     2446   2493   1412      1    221   -252       O  
ATOM   1469  N   GLY A 190      31.295  49.336  56.865  1.00 12.43           N  
ANISOU 1469  N   GLY A 190     1849   1878    994     50    237   -203       N  
ATOM   1470  CA  GLY A 190      32.520  49.147  56.118  1.00 13.10           C  
ANISOU 1470  CA  GLY A 190     1924   1947   1105     23    182   -194       C  
ATOM   1471  C   GLY A 190      32.785  47.729  55.682  1.00 11.46           C  
ANISOU 1471  C   GLY A 190     1675   1760    919     19    150   -130       C  
ATOM   1472  O   GLY A 190      33.841  47.480  55.089  1.00 11.61           O  
ANISOU 1472  O   GLY A 190     1683   1770    958      1    108   -119       O  
ATOM   1473  N   ARG A 191      31.872  46.785  55.917  1.00 12.20           N  
ANISOU 1473  N   ARG A 191     1793   1647   1197     89    262     22       N  
ATOM   1474  CA  ARG A 191      32.184  45.386  55.636  1.00 11.49           C  
ANISOU 1474  CA  ARG A 191     1682   1552   1131     71    256     56       C  
ATOM   1475  C   ARG A 191      32.410  45.143  54.148  1.00 10.21           C  
ANISOU 1475  C   ARG A 191     1469   1379   1032     50    221     48       C  
ATOM   1476  O   ARG A 191      33.372  44.468  53.768  1.00 10.52           O  
ANISOU 1476  O   ARG A 191     1506   1411   1078     38    187     60       O  
ATOM   1477  CB  ARG A 191      31.096  44.465  56.174  1.00 12.27           C  
ANISOU 1477  CB  ARG A 191     1771   1650   1242     70    323     88       C  
ATOM   1478  CG  ARG A 191      31.404  42.997  55.982  1.00 13.75           C  
ANISOU 1478  CG  ARG A 191     1948   1821   1454     51    326    125       C  
ATOM   1479  CD  ARG A 191      32.720  42.570  56.620  1.00 14.77           C  
ANISOU 1479  CD  ARG A 191     2126   1954   1533     64    290    146       C  
ATOM   1480  NE  ARG A 191      32.991  41.159  56.380  1.00 16.60           N  
ANISOU 1480  NE  ARG A 191     2351   2161   1794     53    298    184       N  
ATOM   1481  CZ  ARG A 191      34.202  40.644  56.254  1.00 15.56           C  
ANISOU 1481  CZ  ARG A 191     2232   2025   1654     61    255    200       C  
ATOM   1482  NH1 ARG A 191      35.289  41.410  56.349  1.00 17.99           N1+
ANISOU 1482  NH1 ARG A 191     2553   2357   1926     74    195    181       N1+
ATOM   1483  NH2 ARG A 191      34.339  39.344  56.004  1.00 24.22           N  
ANISOU 1483  NH2 ARG A 191     3326   3091   2785     55    273    234       N  
ATOM   1484  N   GLN A 192      31.515  45.627  53.290  1.00  9.83           N  
ANISOU 1484  N   GLN A 192     1378   1330   1028     47    231     31       N  
ATOM   1485  CA  GLN A 192      31.727  45.403  51.869  1.00  9.55           C  
ANISOU 1485  CA  GLN A 192     1301   1287   1040     28    197     23       C  
ATOM   1486  C   GLN A 192      33.067  45.980  51.417  1.00  9.15           C  
ANISOU 1486  C   GLN A 192     1270   1232    974     26    142      7       C  
ATOM   1487  O   GLN A 192      33.775  45.346  50.619  1.00  9.35           O  
ANISOU 1487  O   GLN A 192     1281   1250   1021     10    115     11       O  
ATOM   1488  CB  GLN A 192      30.596  45.987  51.038  1.00  9.90           C  
ANISOU 1488  CB  GLN A 192     1299   1340   1124     31    207      8       C  
ATOM   1489  CG  GLN A 192      29.310  45.196  51.101  1.00  9.91           C  
ANISOU 1489  CG  GLN A 192     1255   1349   1161     20    252     23       C  
ATOM   1490  CD  GLN A 192      28.253  45.791  50.192  1.00  9.65           C  
ANISOU 1490  CD  GLN A 192     1165   1334   1168     26    250     10       C  
ATOM   1491  NE2 GLN A 192      27.003  45.489  50.419  1.00 11.33           N  
ANISOU 1491  NE2 GLN A 192     1332   1563   1410     24    293     19       N  
ATOM   1492  OE1 GLN A 192      28.589  46.547  49.265  1.00 12.66           O  
ANISOU 1492  OE1 GLN A 192     1541   1716   1553     35    209     -6       O  
ATOM   1493  N   TYR A 193      33.441  47.184  51.881  1.00  9.62           N  
ANISOU 1493  N   TYR A 193     1364   1294    999     40    129    -13       N  
ATOM   1494  CA  TYR A 193      34.737  47.724  51.477  1.00  9.26           C  
ANISOU 1494  CA  TYR A 193     1332   1244    944     30     81    -28       C  
ATOM   1495  C   TYR A 193      35.869  46.809  51.925  1.00  9.35           C  
ANISOU 1495  C   TYR A 193     1354   1263    936     22     57    -10       C  
ATOM   1496  O   TYR A 193      36.854  46.600  51.189  1.00  9.75           O  
ANISOU 1496  O   TYR A 193     1388   1311   1005      9     23     -9       O  
ATOM   1497  CB  TYR A 193      34.962  49.123  52.052  1.00 10.31           C  
ANISOU 1497  CB  TYR A 193     1505   1372   1041     38     74    -57       C  
ATOM   1498  CG  TYR A 193      33.940  50.151  51.630  1.00  9.96           C  
ANISOU 1498  CG  TYR A 193     1456   1314   1016     56     99    -73       C  
ATOM   1499  CD1 TYR A 193      33.487  50.232  50.332  1.00 10.87           C  
ANISOU 1499  CD1 TYR A 193     1530   1425   1177     57     94    -69       C  
ATOM   1500  CD2 TYR A 193      33.409  51.038  52.555  1.00  9.89           C  
ANISOU 1500  CD2 TYR A 193     1485   1299    975     78    129    -90       C  
ATOM   1501  CE1 TYR A 193      32.534  51.165  49.963  1.00 11.20           C  
ANISOU 1501  CE1 TYR A 193     1564   1457   1235     83    115    -77       C  
ATOM   1502  CE2 TYR A 193      32.461  51.976  52.206  1.00 10.58           C  
ANISOU 1502  CE2 TYR A 193     1567   1371   1082    104    157   -101       C  
ATOM   1503  CZ  TYR A 193      32.023  52.039  50.896  1.00 10.76           C  
ANISOU 1503  CZ  TYR A 193     1544   1392   1154    109    148    -91       C  
ATOM   1504  OH  TYR A 193      31.065  52.937  50.489  1.00 12.21           O  
ANISOU 1504  OH  TYR A 193     1716   1565   1359    143    171    -94       O  
ATOM   1505  N   ALA A 194      35.753  46.261  53.133  1.00 10.12           N  
ANISOU 1505  N   ALA A 194     1479   1370    996     33     76     10       N  
ATOM   1506  CA  ALA A 194      36.784  45.381  53.656  1.00 10.08           C  
ANISOU 1506  CA  ALA A 194     1486   1375    968     35     53     36       C  
ATOM   1507  C   ALA A 194      36.862  44.094  52.849  1.00 10.15           C  
ANISOU 1507  C   ALA A 194     1463   1368   1025     29     60     61       C  
ATOM   1508  O   ALA A 194      37.956  43.594  52.574  1.00 10.60           O  
ANISOU 1508  O   ALA A 194     1512   1427   1090     30     30     73       O  
ATOM   1509  CB  ALA A 194      36.522  45.068  55.129  1.00 12.45           C  
ANISOU 1509  CB  ALA A 194     1830   1690   1211     54     77     56       C  
ATOM   1510  N   VAL A 195      35.713  43.538  52.467  1.00  9.75           N  
ANISOU 1510  N   VAL A 195     1392   1301   1009     22    102     68       N  
ATOM   1511  CA  VAL A 195      35.711  42.318  51.666  1.00  9.43           C  
ANISOU 1511  CA  VAL A 195     1328   1239   1015     10    113     84       C  
ATOM   1512  C   VAL A 195      36.401  42.540  50.328  1.00  9.56           C  
ANISOU 1512  C   VAL A 195     1318   1250   1063     -2     77     62       C  
ATOM   1513  O   VAL A 195      37.209  41.707  49.897  1.00  9.37           O  
ANISOU 1513  O   VAL A 195     1289   1214   1057     -2     67     75       O  
ATOM   1514  CB  VAL A 195      34.276  41.791  51.500  1.00 10.75           C  
ANISOU 1514  CB  VAL A 195     1475   1394   1216     -6    161     87       C  
ATOM   1515  CG1 VAL A 195      34.232  40.678  50.469  1.00 12.63           C  
ANISOU 1515  CG1 VAL A 195     1689   1606   1505    -29    167     89       C  
ATOM   1516  CG2 VAL A 195      33.736  41.308  52.834  1.00 12.83           C  
ANISOU 1516  CG2 VAL A 195     1767   1658   1450      5    207    118       C  
ATOM   1517  N   LEU A 196      36.112  43.654  49.652  1.00  9.17           N  
ANISOU 1517  N   LEU A 196     1255   1210   1021     -8     63     33       N  
ATOM   1518  CA  LEU A 196      36.785  43.918  48.384  1.00  8.70           C  
ANISOU 1518  CA  LEU A 196     1176   1146    984    -19     34     16       C  
ATOM   1519  C   LEU A 196      38.294  44.022  48.590  1.00  8.83           C  
ANISOU 1519  C   LEU A 196     1201   1169    984    -13      2     21       C  
ATOM   1520  O   LEU A 196      39.087  43.497  47.792  1.00  9.01           O  
ANISOU 1520  O   LEU A 196     1209   1185   1030    -16     -9     24       O  
ATOM   1521  CB  LEU A 196      36.221  45.181  47.739  1.00  9.30           C  
ANISOU 1521  CB  LEU A 196     1243   1228   1064    -21     26     -9       C  
ATOM   1522  CG  LEU A 196      36.881  45.570  46.424  1.00  9.48           C  
ANISOU 1522  CG  LEU A 196     1253   1247   1104    -30      1    -23       C  
ATOM   1523  CD1 LEU A 196      36.863  44.467  45.377  1.00  9.89           C  
ANISOU 1523  CD1 LEU A 196     1285   1289   1185    -43      6    -22       C  
ATOM   1524  CD2 LEU A 196      36.203  46.820  45.853  1.00 10.71           C  
ANISOU 1524  CD2 LEU A 196     1405   1404   1259    -25     -2    -39       C  
ATOM   1525  N   ASN A 197      38.718  44.682  49.660  1.00  8.94           N  
ANISOU 1525  N   ASN A 197     1238   1200    959     -4    -14     21       N  
ATOM   1526  CA  ASN A 197      40.146  44.744  49.941  1.00  9.10           C  
ANISOU 1526  CA  ASN A 197     1257   1236    965     -2    -51     26       C  
ATOM   1527  C   ASN A 197      40.732  43.354  50.178  1.00  9.88           C  
ANISOU 1527  C   ASN A 197     1351   1333   1072     16    -48     61       C  
ATOM   1528  O   ASN A 197      41.861  43.069  49.744  1.00 10.11           O  
ANISOU 1528  O   ASN A 197     1358   1368   1117     20    -69     68       O  
ATOM   1529  CB  ASN A 197      40.421  45.678  51.118  1.00  9.93           C  
ANISOU 1529  CB  ASN A 197     1391   1363   1020     -1    -72     14       C  
ATOM   1530  CG  ASN A 197      40.264  47.150  50.749  1.00  9.72           C  
ANISOU 1530  CG  ASN A 197     1371   1329    992    -18    -80    -23       C  
ATOM   1531  ND2 ASN A 197      39.688  47.933  51.645  1.00 11.19           N  
ANISOU 1531  ND2 ASN A 197     1594   1518   1142    -15    -71    -40       N  
ATOM   1532  OD1 ASN A 197      40.673  47.578  49.668  1.00 10.39           O  
ANISOU 1532  OD1 ASN A 197     1435   1404   1108    -33    -90    -35       O  
ATOM   1533  N   GLU A 198      39.983  42.473  50.851  1.00  9.36           N  
ANISOU 1533  N   GLU A 198     1303   1257    997     28    -16     86       N  
ATOM   1534  CA  GLU A 198      40.423  41.098  51.044  1.00 10.29           C  
ANISOU 1534  CA  GLU A 198     1424   1360   1126     48     -4    124       C  
ATOM   1535  C   GLU A 198      40.549  40.370  49.712  1.00  9.56           C  
ANISOU 1535  C   GLU A 198     1307   1238   1088     40     11    118       C  
ATOM   1536  O   GLU A 198      41.502  39.602  49.500  1.00 10.13           O  
ANISOU 1536  O   GLU A 198     1370   1302   1176     59      6    139       O  
ATOM   1537  CB  GLU A 198      39.430  40.333  51.937  1.00 11.40           C  
ANISOU 1537  CB  GLU A 198     1594   1486   1252     56     39    152       C  
ATOM   1538  CG  GLU A 198      39.360  40.792  53.375  1.00 13.92           C  
ANISOU 1538  CG  GLU A 198     1947   1834   1508     71     33    165       C  
ATOM   1539  CD  GLU A 198      38.226  40.155  54.196  1.00 22.62           C  
ANISOU 1539  CD  GLU A 198     3080   2921   2595     76     88    192       C  
ATOM   1540  OE1 GLU A 198      37.576  39.169  53.747  1.00 14.74           O  
ANISOU 1540  OE1 GLU A 198     2074   1886   1640     66    131    207       O  
ATOM   1541  OE2 GLU A 198      37.982  40.649  55.329  1.00 18.05           O1-
ANISOU 1541  OE2 GLU A 198     2534   2366   1959     87     92    197       O1-
ATOM   1542  N   TRP A 199      39.578  40.564  48.816  1.00  8.81           N  
ANISOU 1542  N   TRP A 199     1201   1127   1018     14     30     91       N  
ATOM   1543  CA  TRP A 199      39.626  39.908  47.516  1.00  8.62           C  
ANISOU 1543  CA  TRP A 199     1162   1076   1036      2     43     79       C  
ATOM   1544  C   TRP A 199      40.845  40.340  46.720  1.00  9.20           C  
ANISOU 1544  C   TRP A 199     1217   1162   1118      7     15     67       C  
ATOM   1545  O   TRP A 199      41.501  39.511  46.068  1.00  9.35           O  
ANISOU 1545  O   TRP A 199     1230   1161   1162     16     25     72       O  
ATOM   1546  CB  TRP A 199      38.368  40.238  46.721  1.00  8.89           C  
ANISOU 1546  CB  TRP A 199     1185   1106   1086    -27     55     49       C  
ATOM   1547  CG  TRP A 199      37.102  39.608  47.221  1.00  8.58           C  
ANISOU 1547  CG  TRP A 199     1151   1052   1056    -40     91     58       C  
ATOM   1548  CD1 TRP A 199      36.947  38.738  48.252  1.00  9.30           C  
ANISOU 1548  CD1 TRP A 199     1264   1127   1143    -30    120     91       C  
ATOM   1549  CD2 TRP A 199      35.802  39.822  46.673  1.00  8.47           C  
ANISOU 1549  CD2 TRP A 199     1117   1042   1060    -66    103     35       C  
ATOM   1550  CE2 TRP A 199      34.893  39.054  47.409  1.00  9.13           C  
ANISOU 1550  CE2 TRP A 199     1204   1110   1154    -77    142     53       C  
ATOM   1551  CE3 TRP A 199      35.328  40.600  45.618  1.00  9.39           C  
ANISOU 1551  CE3 TRP A 199     1209   1175   1184    -80     83      5       C  
ATOM   1552  NE1 TRP A 199      35.612  38.386  48.365  1.00  9.41           N  
ANISOU 1552  NE1 TRP A 199     1271   1131   1174    -54    156     88       N  
ATOM   1553  CZ2 TRP A 199      33.524  39.039  47.118  1.00 10.05           C  
ANISOU 1553  CZ2 TRP A 199     1292   1232   1293   -105    161     37       C  
ATOM   1554  CZ3 TRP A 199      33.980  40.590  45.335  1.00 10.76           C  
ANISOU 1554  CZ3 TRP A 199     1357   1356   1376   -101     96     -9       C  
ATOM   1555  CH2 TRP A 199      33.100  39.809  46.072  1.00 11.17           C  
ANISOU 1555  CH2 TRP A 199     1404   1397   1443   -115    134      6       C  
ATOM   1556  N   ASN A 200      41.167  41.637  46.749  1.00  9.10           N  
ANISOU 1556  N   ASN A 200     1196   1176   1085      0    -14     50       N  
ATOM   1557  CA  ASN A 200      42.353  42.090  46.039  1.00  8.79           C  
ANISOU 1557  CA  ASN A 200     1135   1148   1056      0    -35     42       C  
ATOM   1558  C   ASN A 200      43.605  41.431  46.602  1.00  9.45           C  
ANISOU 1558  C   ASN A 200     1207   1243   1142     26    -48     70       C  
ATOM   1559  O   ASN A 200      44.528  41.090  45.845  1.00  9.59           O  
ANISOU 1559  O   ASN A 200     1202   1258   1185     34    -45     72       O  
ATOM   1560  CB  ASN A 200      42.463  43.610  46.085  1.00  9.05           C  
ANISOU 1560  CB  ASN A 200     1166   1201   1070    -17    -61     20       C  
ATOM   1561  CG  ASN A 200      41.527  44.296  45.103  1.00  9.11           C  
ANISOU 1561  CG  ASN A 200     1178   1198   1085    -35    -50     -4       C  
ATOM   1562  ND2 ASN A 200      41.188  45.548  45.396  1.00  9.42           N  
ANISOU 1562  ND2 ASN A 200     1228   1244   1106    -43    -61    -18       N  
ATOM   1563  OD1 ASN A 200      41.138  43.717  44.082  1.00 10.03           O  
ANISOU 1563  OD1 ASN A 200     1290   1300   1221    -39    -33    -10       O  
ATOM   1564  N   GLN A 201      43.659  41.251  47.923  1.00  9.45           N  
ANISOU 1564  N   GLN A 201     1220   1259   1113     43    -61     94       N  
ATOM   1565  CA  GLN A 201      44.802  40.568  48.526  1.00 10.11           C  
ANISOU 1565  CA  GLN A 201     1290   1358   1194     76    -78    129       C  
ATOM   1566  C   GLN A 201      44.887  39.114  48.069  1.00  9.88           C  
ANISOU 1566  C   GLN A 201     1264   1291   1200    103    -41    153       C  
ATOM   1567  O   GLN A 201      45.982  38.600  47.801  1.00 10.68           O  
ANISOU 1567  O   GLN A 201     1339   1395   1322    130    -45    171       O  
ATOM   1568  CB  GLN A 201      44.718  40.634  50.051  1.00 10.76           C  
ANISOU 1568  CB  GLN A 201     1395   1466   1227     92    -99    152       C  
ATOM   1569  CG  GLN A 201      45.957  40.086  50.749  1.00 10.99           C  
ANISOU 1569  CG  GLN A 201     1406   1526   1246    130   -130    190       C  
ATOM   1570  CD  GLN A 201      47.145  40.996  50.551  1.00 11.27           C  
ANISOU 1570  CD  GLN A 201     1395   1603   1284    116   -178    171       C  
ATOM   1571  NE2 GLN A 201      48.100  40.573  49.734  1.00 12.39           N  
ANISOU 1571  NE2 GLN A 201     1494   1744   1469    131   -174    180       N  
ATOM   1572  OE1 GLN A 201      47.191  42.093  51.104  1.00 12.78           O  
ANISOU 1572  OE1 GLN A 201     1590   1824   1440     90   -212    147       O  
ATOM   1573  N   VAL A 202      43.745  38.428  47.989  1.00  9.82           N  
ANISOU 1573  N   VAL A 202     1286   1244   1200     94     -2    154       N  
ATOM   1574  CA  VAL A 202      43.718  37.050  47.496  1.00  9.37           C  
ANISOU 1574  CA  VAL A 202     1242   1139   1179    111     39    170       C  
ATOM   1575  C   VAL A 202      44.273  36.967  46.081  1.00  9.98           C  
ANISOU 1575  C   VAL A 202     1298   1202   1291    105     49    143       C  
ATOM   1576  O   VAL A 202      45.049  36.058  45.756  1.00 10.12           O  
ANISOU 1576  O   VAL A 202     1312   1196   1335    136     69    160       O  
ATOM   1577  CB  VAL A 202      42.286  36.486  47.590  1.00 10.55           C  
ANISOU 1577  CB  VAL A 202     1423   1250   1334     86     78    165       C  
ATOM   1578  CG1 VAL A 202      42.151  35.199  46.787  1.00 11.88           C  
ANISOU 1578  CG1 VAL A 202     1608   1362   1546     86    122    163       C  
ATOM   1579  CG2 VAL A 202      41.889  36.262  49.046  1.00 12.19           C  
ANISOU 1579  CG2 VAL A 202     1658   1466   1509    102     83    203       C  
ATOM   1580  N   PHE A 203      43.858  37.896  45.218  1.00  9.57           N  
ANISOU 1580  N   PHE A 203     1237   1162   1237     69     40    103       N  
ATOM   1581  CA  PHE A 203      44.370  37.968  43.850  1.00  9.41           C  
ANISOU 1581  CA  PHE A 203     1202   1135   1239     62     50     77       C  
ATOM   1582  C   PHE A 203      45.874  38.165  43.829  1.00  9.00           C  
ANISOU 1582  C   PHE A 203     1115   1109   1196     90     35     93       C  
ATOM   1583  O   PHE A 203      46.592  37.415  43.153  1.00  9.68           O  
ANISOU 1583  O   PHE A 203     1194   1175   1310    113     61     97       O  
ATOM   1584  CB  PHE A 203      43.647  39.113  43.122  1.00  9.04           C  
ANISOU 1584  CB  PHE A 203     1153   1104   1178     24     37     40       C  
ATOM   1585  CG  PHE A 203      44.404  39.724  41.973  1.00  8.96           C  
ANISOU 1585  CG  PHE A 203     1125   1106   1174     17     35     21       C  
ATOM   1586  CD1 PHE A 203      44.491  39.093  40.738  1.00  8.83           C  
ANISOU 1586  CD1 PHE A 203     1118   1064   1173     16     65      2       C  
ATOM   1587  CD2 PHE A 203      44.997  40.959  42.120  1.00  9.00           C  
ANISOU 1587  CD2 PHE A 203     1109   1145   1167      9      7     20       C  
ATOM   1588  CE1 PHE A 203      45.167  39.693  39.682  1.00  8.91           C  
ANISOU 1588  CE1 PHE A 203     1116   1088   1183     10     69    -13       C  
ATOM   1589  CE2 PHE A 203      45.672  41.553  41.065  1.00  9.39           C  
ANISOU 1589  CE2 PHE A 203     1144   1202   1223      0     13      6       C  
ATOM   1590  CZ  PHE A 203      45.738  40.919  39.842  1.00  9.02           C  
ANISOU 1590  CZ  PHE A 203     1106   1134   1188      2     45     -8       C  
ATOM   1591  N   VAL A 204      46.378  39.165  44.556  1.00  9.67           N  
ANISOU 1591  N   VAL A 204     1176   1238   1261     86     -5    100       N  
ATOM   1592  CA  VAL A 204      47.821  39.403  44.550  1.00  9.98           C  
ANISOU 1592  CA  VAL A 204     1171   1310   1313    105    -24    114       C  
ATOM   1593  C   VAL A 204      48.559  38.152  45.006  1.00 10.35           C  
ANISOU 1593  C   VAL A 204     1207   1347   1379    158    -13    154       C  
ATOM   1594  O   VAL A 204      49.512  37.693  44.360  1.00 10.66           O  
ANISOU 1594  O   VAL A 204     1217   1383   1450    185      7    162       O  
ATOM   1595  CB  VAL A 204      48.177  40.620  45.421  1.00  9.41           C  
ANISOU 1595  CB  VAL A 204     1078   1285   1212     86    -74    111       C  
ATOM   1596  CG1 VAL A 204      49.691  40.759  45.566  1.00 11.46           C  
ANISOU 1596  CG1 VAL A 204     1280   1585   1489    103   -100    128       C  
ATOM   1597  CG2 VAL A 204      47.588  41.900  44.857  1.00 10.52           C  
ANISOU 1597  CG2 VAL A 204     1229   1426   1341     40    -79     74       C  
ATOM   1598  N   ASP A 205      48.121  37.567  46.122  1.00 10.44           N  
ANISOU 1598  N   ASP A 205     1245   1352   1370    179    -19    184       N  
ATOM   1599  CA  ASP A 205      48.814  36.402  46.659  1.00 11.25           C  
ANISOU 1599  CA  ASP A 205     1342   1444   1487    237     -9    232       C  
ATOM   1600  C   ASP A 205      48.822  35.258  45.655  1.00 10.85           C  
ANISOU 1600  C   ASP A 205     1309   1334   1479    258     50    230       C  
ATOM   1601  O   ASP A 205      49.831  34.559  45.500  1.00 11.57           O  
ANISOU 1601  O   ASP A 205     1376   1420   1600    308     64    257       O  
ATOM   1602  CB  ASP A 205      48.154  35.948  47.963  1.00 12.07           C  
ANISOU 1602  CB  ASP A 205     1486   1543   1557    253    -16    266       C  
ATOM   1603  CG  ASP A 205      48.335  36.939  49.108  1.00 13.34           C  
ANISOU 1603  CG  ASP A 205     1635   1766   1667    243    -75    272       C  
ATOM   1604  OD1 ASP A 205      49.107  37.898  48.978  1.00 15.15           O  
ANISOU 1604  OD1 ASP A 205     1821   2043   1895    226   -114    253       O  
ATOM   1605  OD2 ASP A 205      47.697  36.723  50.171  1.00 17.24           O1-
ANISOU 1605  OD2 ASP A 205     2168   2259   2123    251    -78    295       O1-
ATOM   1606  N   ALA A 206      47.695  35.024  44.988  1.00 10.58           N  
ANISOU 1606  N   ALA A 206     1317   1254   1450    222     84    197       N  
ATOM   1607  CA  ALA A 206      47.608  33.911  44.054  1.00 10.95           C  
ANISOU 1607  CA  ALA A 206     1391   1239   1532    234    140    186       C  
ATOM   1608  C   ALA A 206      48.529  34.119  42.860  1.00 10.98           C  
ANISOU 1608  C   ALA A 206     1363   1250   1558    242    155    163       C  
ATOM   1609  O   ALA A 206      49.184  33.178  42.406  1.00 11.29           O  
ANISOU 1609  O   ALA A 206     1406   1255   1630    283    195    174       O  
ATOM   1610  CB  ALA A 206      46.162  33.712  43.596  1.00 12.04           C  
ANISOU 1610  CB  ALA A 206     1573   1335   1665    184    164    150       C  
ATOM   1611  N   VAL A 207      48.584  35.343  42.329  1.00 10.17           N  
ANISOU 1611  N   VAL A 207     1234   1189   1440    204    129    133       N  
ATOM   1612  CA  VAL A 207      49.473  35.625  41.205  1.00  9.99           C  
ANISOU 1612  CA  VAL A 207     1183   1178   1436    208    148    114       C  
ATOM   1613  C   VAL A 207      50.926  35.450  41.627  1.00 10.60           C  
ANISOU 1613  C   VAL A 207     1203   1285   1538    260    141    153       C  
ATOM   1614  O   VAL A 207      51.714  34.785  40.944  1.00 11.75           O  
ANISOU 1614  O   VAL A 207     1336   1413   1717    297    183    158       O  
ATOM   1615  CB  VAL A 207      49.204  37.035  40.645  1.00 10.12           C  
ANISOU 1615  CB  VAL A 207     1188   1230   1429    156    123     81       C  
ATOM   1616  CG1 VAL A 207      50.266  37.404  39.600  1.00 11.20           C  
ANISOU 1616  CG1 VAL A 207     1289   1382   1583    161    146     71       C  
ATOM   1617  CG2 VAL A 207      47.799  37.124  40.046  1.00 10.65           C  
ANISOU 1617  CG2 VAL A 207     1303   1269   1474    114    131     44       C  
ATOM   1618  N   ARG A 208      51.305  36.050  42.759  1.00 11.13           N  
ANISOU 1618  N   ARG A 208     1234   1404   1590    264     88    181       N  
ATOM   1619  CA  ARG A 208      52.700  35.993  43.180  1.00 11.52           C  
ANISOU 1619  CA  ARG A 208     1217   1497   1662    308     69    217       C  
ATOM   1620  C   ARG A 208      53.141  34.562  43.464  1.00 12.52           C  
ANISOU 1620  C   ARG A 208     1350   1590   1817    382    101    260       C  
ATOM   1621  O   ARG A 208      54.299  34.218  43.222  1.00 13.29           O  
ANISOU 1621  O   ARG A 208     1396   1704   1950    430    116    282       O  
ATOM   1622  CB  ARG A 208      52.943  36.870  44.409  1.00 12.41           C  
ANISOU 1622  CB  ARG A 208     1297   1673   1746    294     -2    233       C  
ATOM   1623  CG  ARG A 208      52.657  38.345  44.220  1.00 11.74           C  
ANISOU 1623  CG  ARG A 208     1204   1618   1637    226    -32    194       C  
ATOM   1624  CD  ARG A 208      53.369  38.962  43.037  1.00 12.47           C  
ANISOU 1624  CD  ARG A 208     1257   1721   1758    203     -9    170       C  
ATOM   1625  NE  ARG A 208      53.165  40.414  43.027  1.00 11.84           N  
ANISOU 1625  NE  ARG A 208     1173   1668   1657    141    -40    140       N  
ATOM   1626  CZ  ARG A 208      53.146  41.172  41.939  1.00 10.73           C  
ANISOU 1626  CZ  ARG A 208     1034   1518   1524    103    -14    111       C  
ATOM   1627  NH1 ARG A 208      53.285  40.633  40.740  1.00 11.14           N1+
ANISOU 1627  NH1 ARG A 208     1094   1541   1597    119     42    104       N1+
ATOM   1628  NH2 ARG A 208      52.960  42.478  42.042  1.00 11.13           N  
ANISOU 1628  NH2 ARG A 208     1086   1585   1556     51    -42     89       N  
ATOM   1629  N   ALA A 209      52.238  33.716  43.969  1.00 11.90           N  
ANISOU 1629  N   ALA A 209     1333   1460   1726    393    117    273       N  
ATOM   1630  CA  ALA A 209      52.602  32.353  44.325  1.00 12.89           C  
ANISOU 1630  CA  ALA A 209     1476   1545   1879    465    151    319       C  
ATOM   1631  C   ALA A 209      53.020  31.536  43.116  1.00 12.62           C  
ANISOU 1631  C   ALA A 209     1451   1455   1888    494    221    303       C  
ATOM   1632  O   ALA A 209      53.724  30.531  43.275  1.00 14.64           O  
ANISOU 1632  O   ALA A 209     1701   1685   2178    567    252    344       O  
ATOM   1633  CB  ALA A 209      51.434  31.664  45.020  1.00 13.34           C  
ANISOU 1633  CB  ALA A 209     1605   1548   1914    458    164    333       C  
ATOM   1634  N   THR A 210      52.624  31.941  41.908  1.00 12.60           N  
ANISOU 1634  N   THR A 210     1465   1436   1885    444    249    246       N  
ATOM   1635  CA  THR A 210      53.029  31.196  40.723  1.00 13.42           C  
ANISOU 1635  CA  THR A 210     1586   1491   2023    471    318    224       C  
ATOM   1636  C   THR A 210      54.483  31.452  40.342  1.00 14.26           C  
ANISOU 1636  C   THR A 210     1614   1643   2160    515    328    241       C  
ATOM   1637  O   THR A 210      55.022  30.725  39.508  1.00 15.80           O  
ANISOU 1637  O   THR A 210     1817   1799   2388    556    392    234       O  
ATOM   1638  CB  THR A 210      52.112  31.479  39.526  1.00 12.65           C  
ANISOU 1638  CB  THR A 210     1538   1363   1906    405    344    157       C  
ATOM   1639  CG2 THR A 210      50.655  31.201  39.864  1.00 13.53           C  
ANISOU 1639  CG2 THR A 210     1714   1433   1993    359    336    139       C  
ATOM   1640  OG1 THR A 210      52.280  32.830  39.074  1.00 12.93           O  
ANISOU 1640  OG1 THR A 210     1533   1460   1919    359    312    133       O  
ATOM   1641  N   GLY A 211      55.123  32.462  40.925  1.00 14.40           N  
ANISOU 1641  N   GLY A 211     1558   1741   2170    505    269    261       N  
ATOM   1642  CA  GLY A 211      56.551  32.636  40.752  1.00 16.49           C  
ANISOU 1642  CA  GLY A 211     1736   2057   2473    548    273    285       C  
ATOM   1643  C   GLY A 211      56.936  33.185  39.390  1.00 14.76           C  
ANISOU 1643  C   GLY A 211     1499   1843   2265    519    318    243       C  
ATOM   1644  O   GLY A 211      56.117  33.674  38.604  1.00 15.16           O  
ANISOU 1644  O   GLY A 211     1600   1873   2286    458    331    195       O  
ATOM   1645  N   GLY A 212      58.239  33.137  39.134  1.00 17.09           N  
ANISOU 1645  N   GLY A 212     1715   2175   2603    565    340    267       N  
ATOM   1646  CA  GLY A 212      58.764  33.544  37.846  1.00 16.53           C  
ANISOU 1646  CA  GLY A 212     1624   2110   2548    549    396    235       C  
ATOM   1647  C   GLY A 212      58.458  34.992  37.566  1.00 15.71           C  
ANISOU 1647  C   GLY A 212     1509   2047   2411    462    360    203       C  
ATOM   1648  O   GLY A 212      58.484  35.852  38.465  1.00 16.23           O  
ANISOU 1648  O   GLY A 212     1535   2167   2466    427    287    216       O  
ATOM   1649  N  AASN A 213      58.135  35.273  36.298  0.59 16.77           N  
ANISOU 1649  N  AASN A 213     1688   2156   2529    427    411    161       N  
ATOM   1650  N  BASN A 213      58.144  35.285  36.302  0.41 15.73           N  
ANISOU 1650  N  BASN A 213     1555   2024   2397    427    411    161       N  
ATOM   1651  CA AASN A 213      57.791  36.626  35.890  0.59 15.54           C  
ANISOU 1651  CA AASN A 213     1535   2028   2342    349    387    133       C  
ATOM   1652  CA BASN A 213      57.825  36.656  35.927  0.41 14.52           C  
ANISOU 1652  CA BASN A 213     1402   1902   2213    349    385    135       C  
ATOM   1653  C  AASN A 213      56.602  37.160  36.673  0.59 13.97           C  
ANISOU 1653  C  AASN A 213     1381   1827   2099    300    318    123       C  
ATOM   1654  C  BASN A 213      56.600  37.173  36.672  0.41 14.66           C  
ANISOU 1654  C  BASN A 213     1469   1915   2187    299    318    123       C  
ATOM   1655  O  AASN A 213      56.483  38.374  36.871  0.59 14.34           O  
ANISOU 1655  O  AASN A 213     1410   1909   2129    245    276    115       O  
ATOM   1656  O  BASN A 213      56.448  38.386  36.847  0.41 14.75           O  
ANISOU 1656  O  BASN A 213     1465   1960   2180    243    277    114       O  
ATOM   1657  CB AASN A 213      57.464  36.650  34.394  0.59 17.06           C  
ANISOU 1657  CB AASN A 213     1786   2184   2510    330    454     93       C  
ATOM   1658  CB BASN A 213      57.604  36.758  34.419  0.41 15.79           C  
ANISOU 1658  CB BASN A 213     1614   2031   2353    329    453     96       C  
ATOM   1659  CG AASN A 213      58.688  36.444  33.526  0.59 19.71           C  
ANISOU 1659  CG AASN A 213     2074   2533   2883    367    529    100       C  
ATOM   1660  CG BASN A 213      58.906  36.754  33.631  0.41 16.66           C  
ANISOU 1660  CG BASN A 213     1662   2164   2502    359    519    106       C  
ATOM   1661  ND2AASN A 213      58.584  35.535  32.562  0.59 17.37           N  
ANISOU 1661  ND2AASN A 213     1836   2185   2580    401    602     76       N  
ATOM   1662  OD1AASN A 213      59.719  37.089  33.726  0.59 28.32           O  
ANISOU 1662  OD1AASN A 213     3074   3678   4008    364    523    125       O  
ATOM   1663  ND2BASN A 213      58.794  36.908  32.319  0.41 19.83           N  
ANISOU 1663  ND2BASN A 213     2110   2545   2878    342    582     75       N  
ATOM   1664  OD1BASN A 213      59.999  36.614  34.194  0.41 14.32           O  
ANISOU 1664  OD1BASN A 213     1277   1908   2256    399    515    143       O  
ATOM   1665  N   ASN A 214      55.702  36.281  37.112  1.00 13.32           N  
ANISOU 1665  N   ASN A 214     1360   1699   2002    318    311    121       N  
ATOM   1666  CA  ASN A 214      54.526  36.736  37.851  1.00 12.40           C  
ANISOU 1666  CA  ASN A 214     1284   1580   1846    274    255    112       C  
ATOM   1667  C   ASN A 214      54.874  37.323  39.208  1.00 12.49           C  
ANISOU 1667  C   ASN A 214     1243   1644   1858    270    186    143       C  
ATOM   1668  O   ASN A 214      54.039  38.024  39.784  1.00 13.10           O  
ANISOU 1668  O   ASN A 214     1346   1730   1900    227    140    132       O  
ATOM   1669  CB  ASN A 214      53.519  35.595  37.965  1.00 12.44           C  
ANISOU 1669  CB  ASN A 214     1363   1523   1841    290    273    104       C  
ATOM   1670  CG  ASN A 214      52.906  35.242  36.631  1.00 12.05           C  
ANISOU 1670  CG  ASN A 214     1375   1426   1775    272    325     59       C  
ATOM   1671  ND2 ASN A 214      52.631  33.970  36.422  1.00 13.04           N  
ANISOU 1671  ND2 ASN A 214     1548   1491   1913    303    368     52       N  
ATOM   1672  OD1 ASN A 214      52.701  36.112  35.779  1.00 14.88           O  
ANISOU 1672  OD1 ASN A 214     1742   1801   2109    230    328     31       O  
ATOM   1673  N   GLN A 215      56.086  37.088  39.719  1.00 13.16           N  
ANISOU 1673  N   GLN A 215     1254   1768   1978    314    176    180       N  
ATOM   1674  CA  GLN A 215      56.489  37.677  40.992  1.00 12.77           C  
ANISOU 1674  CA  GLN A 215     1153   1778   1923    307    103    205       C  
ATOM   1675  C   GLN A 215      56.682  39.179  40.894  1.00 12.93           C  
ANISOU 1675  C   GLN A 215     1140   1841   1932    237     70    181       C  
ATOM   1676  O   GLN A 215      56.550  39.890  41.901  1.00 15.69           O  
ANISOU 1676  O   GLN A 215     1478   2225   2257    207      6    183       O  
ATOM   1677  CB  GLN A 215      57.803  37.063  41.478  1.00 19.59           C  
ANISOU 1677  CB  GLN A 215     1935   2680   2828    372     97    251       C  
ATOM   1678  CG  GLN A 215      57.708  35.603  41.785  1.00 37.64           C  
ANISOU 1678  CG  GLN A 215     4252   4923   5126    449    125    285       C  
ATOM   1679  CD  GLN A 215      58.613  35.188  42.925  1.00 40.20           C  
ANISOU 1679  CD  GLN A 215     4509   5298   5466    510     79    342       C  
ATOM   1680  NE2 GLN A 215      58.223  34.137  43.632  1.00 49.77           N  
ANISOU 1680  NE2 GLN A 215     5767   6474   6669    565     80    378       N  
ATOM   1681  OE1 GLN A 215      59.652  35.805  43.169  1.00 47.79           O  
ANISOU 1681  OE1 GLN A 215     5379   6332   6448    507     42    355       O  
ATOM   1682  N   THR A 216      57.013  39.684  39.704  1.00 12.39           N  
ANISOU 1682  N   THR A 216     1060   1768   1879    211    116    159       N  
ATOM   1683  CA  THR A 216      57.363  41.087  39.519  1.00 12.08           C  
ANISOU 1683  CA  THR A 216      986   1763   1839    147     96    142       C  
ATOM   1684  C   THR A 216      56.475  41.788  38.495  1.00 11.54           C  
ANISOU 1684  C   THR A 216      986   1657   1742     99    127    107       C  
ATOM   1685  O   THR A 216      56.790  42.912  38.087  1.00 11.94           O  
ANISOU 1685  O   THR A 216     1018   1724   1796     49    130     95       O  
ATOM   1686  CB  THR A 216      58.845  41.231  39.129  1.00 15.14           C  
ANISOU 1686  CB  THR A 216     1278   2194   2280    157    121    159       C  
ATOM   1687  CG2 THR A 216      59.749  40.897  40.309  1.00 16.71           C  
ANISOU 1687  CG2 THR A 216     1395   2451   2504    192     66    194       C  
ATOM   1688  OG1 THR A 216      59.156  40.340  38.053  1.00 16.05           O  
ANISOU 1688  OG1 THR A 216     1400   2280   2419    204    199    162       O  
ATOM   1689  N   ARG A 217      55.387  41.155  38.078  1.00 10.94           N  
ANISOU 1689  N   ARG A 217      987   1532   1637    112    150     92       N  
ATOM   1690  CA  ARG A 217      54.454  41.738  37.120  1.00 10.52           C  
ANISOU 1690  CA  ARG A 217      998   1449   1550     74    171     62       C  
ATOM   1691  C   ARG A 217      53.676  42.882  37.763  1.00 10.05           C  
ANISOU 1691  C   ARG A 217      961   1397   1460     25    119     50       C  
ATOM   1692  O   ARG A 217      53.334  42.834  38.942  1.00 10.19           O  
ANISOU 1692  O   ARG A 217      979   1425   1468     28     71     58       O  
ATOM   1693  CB  ARG A 217      53.469  40.651  36.674  1.00 11.32           C  
ANISOU 1693  CB  ARG A 217     1167   1503   1631     99    198     47       C  
ATOM   1694  CG  ARG A 217      52.552  41.065  35.532  1.00 10.44           C  
ANISOU 1694  CG  ARG A 217     1118   1366   1482     68    220     16       C  
ATOM   1695  CD  ARG A 217      51.661  39.939  35.039  1.00 10.28           C  
ANISOU 1695  CD  ARG A 217     1159   1303   1445     86    245     -5       C  
ATOM   1696  NE  ARG A 217      52.398  38.736  34.704  1.00 11.46           N  
ANISOU 1696  NE  ARG A 217     1301   1431   1623    133    295      0       N  
ATOM   1697  CZ  ARG A 217      53.194  38.602  33.649  1.00 12.25           C  
ANISOU 1697  CZ  ARG A 217     1393   1529   1731    149    351     -6       C  
ATOM   1698  NH1 ARG A 217      53.342  39.596  32.785  1.00 11.74           N1+
ANISOU 1698  NH1 ARG A 217     1331   1484   1646    117    366    -16       N1+
ATOM   1699  NH2 ARG A 217      53.853  37.461  33.464  1.00 14.10           N  
ANISOU 1699  NH2 ARG A 217     1621   1741   1996    200    400     -1       N  
ATOM   1700  N   TYR A 218      53.375  43.927  36.971  1.00  9.87           N  
ANISOU 1700  N   TYR A 218      964   1367   1420    -16    132     33       N  
ATOM   1701  CA  TYR A 218      52.481  44.982  37.444  1.00  9.29           C  
ANISOU 1701  CA  TYR A 218      925   1289   1317    -55     92     21       C  
ATOM   1702  C   TYR A 218      51.048  44.463  37.458  1.00  9.13           C  
ANISOU 1702  C   TYR A 218      967   1240   1263    -42     84      8       C  
ATOM   1703  O   TYR A 218      50.597  43.800  36.513  1.00  9.40           O  
ANISOU 1703  O   TYR A 218     1035   1252   1286    -28    118     -2       O  
ATOM   1704  CB  TYR A 218      52.566  46.230  36.557  1.00  9.86           C  
ANISOU 1704  CB  TYR A 218     1011   1355   1382    -95    113     13       C  
ATOM   1705  CG  TYR A 218      53.907  46.930  36.592  1.00  9.69           C  
ANISOU 1705  CG  TYR A 218      926   1360   1397   -123    121     23       C  
ATOM   1706  CD1 TYR A 218      54.973  46.448  35.868  1.00 10.82           C  
ANISOU 1706  CD1 TYR A 218     1024   1516   1572   -106    169     35       C  
ATOM   1707  CD2 TYR A 218      54.106  48.070  37.368  1.00 10.76           C  
ANISOU 1707  CD2 TYR A 218     1045   1506   1538   -168     84     17       C  
ATOM   1708  CE1 TYR A 218      56.204  47.081  35.897  1.00 11.06           C  
ANISOU 1708  CE1 TYR A 218      986   1575   1643   -136    179     44       C  
ATOM   1709  CE2 TYR A 218      55.335  48.699  37.413  1.00 11.65           C  
ANISOU 1709  CE2 TYR A 218     1094   1643   1689   -202     89     23       C  
ATOM   1710  CZ  TYR A 218      56.379  48.211  36.668  1.00 11.04           C  
ANISOU 1710  CZ  TYR A 218      964   1584   1647   -188    137     38       C  
ATOM   1711  OH  TYR A 218      57.614  48.816  36.688  1.00 12.53           O  
ANISOU 1711  OH  TYR A 218     1079   1802   1881   -225    146     44       O  
ATOM   1712  N   LEU A 219      50.342  44.758  38.545  1.00  8.73           N  
ANISOU 1712  N   LEU A 219      930   1192   1196    -51     41      7       N  
ATOM   1713  CA  LEU A 219      48.971  44.323  38.739  1.00  8.94           C  
ANISOU 1713  CA  LEU A 219     1004   1197   1196    -43     32     -3       C  
ATOM   1714  C   LEU A 219      48.088  45.527  39.035  1.00  8.38           C  
ANISOU 1714  C   LEU A 219      960   1123   1100    -72      7    -14       C  
ATOM   1715  O   LEU A 219      48.524  46.488  39.685  1.00 10.52           O  
ANISOU 1715  O   LEU A 219     1217   1409   1373    -93    -16    -14       O  
ATOM   1716  CB  LEU A 219      48.858  43.343  39.908  1.00  9.25           C  
ANISOU 1716  CB  LEU A 219     1036   1238   1240    -16     14     12       C  
ATOM   1717  CG  LEU A 219      49.861  42.191  39.918  1.00  9.41           C  
ANISOU 1717  CG  LEU A 219     1024   1261   1290     22     34     32       C  
ATOM   1718  CD1 LEU A 219      49.665  41.345  41.171  1.00 10.14           C  
ANISOU 1718  CD1 LEU A 219     1119   1354   1381     51     13     54       C  
ATOM   1719  CD2 LEU A 219      49.760  41.331  38.673  1.00 10.10           C  
ANISOU 1719  CD2 LEU A 219     1134   1318   1386     38     84     21       C  
ATOM   1720  N   GLY A 220      46.836  45.463  38.573  1.00  8.18           N  
ANISOU 1720  N   GLY A 220      975   1081   1053    -72     12    -26       N  
ATOM   1721  CA  GLY A 220      45.834  46.475  38.878  1.00  8.39           C  
ANISOU 1721  CA  GLY A 220     1027   1102   1057    -86     -8    -34       C  
ATOM   1722  C   GLY A 220      44.831  45.947  39.893  1.00  7.90           C  
ANISOU 1722  C   GLY A 220      977   1039    986    -75    -25    -35       C  
ATOM   1723  O   GLY A 220      44.398  44.801  39.802  1.00  8.50           O  
ANISOU 1723  O   GLY A 220     1057   1107   1065    -61    -14    -34       O  
ATOM   1724  N   VAL A 221      44.465  46.801  40.843  1.00  8.11           N  
ANISOU 1724  N   VAL A 221     1012   1070   1000    -83    -47    -37       N  
ATOM   1725  CA  VAL A 221      43.510  46.464  41.897  1.00  8.51           C  
ANISOU 1725  CA  VAL A 221     1075   1121   1037    -73    -57    -36       C  
ATOM   1726  C   VAL A 221      42.524  47.613  42.060  1.00  7.87           C  
ANISOU 1726  C   VAL A 221     1017   1034    939    -79    -62    -46       C  
ATOM   1727  O   VAL A 221      42.949  48.765  42.221  1.00  8.96           O  
ANISOU 1727  O   VAL A 221     1163   1169   1073    -92    -71    -53       O  
ATOM   1728  CB  VAL A 221      44.221  46.113  43.220  1.00  9.48           C  
ANISOU 1728  CB  VAL A 221     1185   1260   1157    -66    -75    -24       C  
ATOM   1729  CG1 VAL A 221      44.798  44.706  43.142  1.00  9.94           C  
ANISOU 1729  CG1 VAL A 221     1225   1319   1234    -45    -64     -6       C  
ATOM   1730  CG2 VAL A 221      45.317  47.121  43.555  1.00 10.26           C  
ANISOU 1730  CG2 VAL A 221     1269   1374   1256    -85    -97    -29       C  
ATOM   1731  N   PRO A 222      41.208  47.345  42.031  1.00  8.21           N  
ANISOU 1731  N   PRO A 222     1070   1073    976    -69    -55    -49       N  
ATOM   1732  CA  PRO A 222      40.240  48.439  42.085  1.00  8.07           C  
ANISOU 1732  CA  PRO A 222     1070   1050    946    -65    -56    -55       C  
ATOM   1733  C   PRO A 222      39.694  48.722  43.474  1.00  8.19           C  
ANISOU 1733  C   PRO A 222     1097   1068    948    -57    -58    -57       C  
ATOM   1734  O   PRO A 222      39.723  47.886  44.382  1.00  9.09           O  
ANISOU 1734  O   PRO A 222     1207   1190   1057    -53    -57    -50       O  
ATOM   1735  CB  PRO A 222      39.110  47.930  41.178  1.00  9.06           C  
ANISOU 1735  CB  PRO A 222     1189   1180   1076    -58    -49    -57       C  
ATOM   1736  CG  PRO A 222      39.096  46.441  41.458  1.00  8.69           C  
ANISOU 1736  CG  PRO A 222     1128   1134   1040    -60    -41    -54       C  
ATOM   1737  CD  PRO A 222      40.580  46.082  41.590  1.00  8.42           C  
ANISOU 1737  CD  PRO A 222     1090   1098   1012    -63    -43    -47       C  
ATOM   1738  N   GLY A 223      39.130  49.924  43.614  1.00  9.22           N  
ANISOU 1738  N   GLY A 223     1247   1188   1068    -51    -55    -65       N  
ATOM   1739  CA  GLY A 223      38.256  50.252  44.712  1.00  9.62           C  
ANISOU 1739  CA  GLY A 223     1312   1238   1104    -36    -46    -70       C  
ATOM   1740  C   GLY A 223      36.805  50.008  44.348  1.00  8.31           C  
ANISOU 1740  C   GLY A 223     1132   1079    948    -17    -31    -64       C  
ATOM   1741  O   GLY A 223      36.461  49.585  43.241  1.00  8.87           O  
ANISOU 1741  O   GLY A 223     1182   1156   1032    -18    -34    -60       O  
ATOM   1742  N   TYR A 224      35.932  50.302  45.307  1.00  8.74           N  
ANISOU 1742  N   TYR A 224     1195   1135    992      0    -13    -67       N  
ATOM   1743  CA  TYR A 224      34.521  49.970  45.173  1.00  9.03           C  
ANISOU 1743  CA  TYR A 224     1205   1185   1042     17      4    -60       C  
ATOM   1744  C   TYR A 224      33.899  50.703  43.994  1.00  8.17           C  
ANISOU 1744  C   TYR A 224     1083   1076    945     33     -3    -58       C  
ATOM   1745  O   TYR A 224      34.046  51.925  43.861  1.00  8.60           O  
ANISOU 1745  O   TYR A 224     1165   1111    993     49     -2    -60       O  
ATOM   1746  CB  TYR A 224      33.793  50.285  46.485  1.00  9.64           C  
ANISOU 1746  CB  TYR A 224     1296   1262   1104     36     32    -62       C  
ATOM   1747  CG  TYR A 224      32.441  49.616  46.604  1.00  9.11           C  
ANISOU 1747  CG  TYR A 224     1192   1215   1056     46     57    -52       C  
ATOM   1748  CD1 TYR A 224      31.298  50.194  46.090  1.00 10.15           C  
ANISOU 1748  CD1 TYR A 224     1295   1356   1205     71     66    -50       C  
ATOM   1749  CD2 TYR A 224      32.305  48.402  47.276  1.00  9.54           C  
ANISOU 1749  CD2 TYR A 224     1236   1277   1111     31     74    -42       C  
ATOM   1750  CE1 TYR A 224      30.068  49.588  46.208  1.00  9.76           C  
ANISOU 1750  CE1 TYR A 224     1201   1330   1178     75     88    -42       C  
ATOM   1751  CE2 TYR A 224      31.072  47.798  47.412  1.00 10.03           C  
ANISOU 1751  CE2 TYR A 224     1260   1355   1195     32    102    -34       C  
ATOM   1752  CZ  TYR A 224      29.950  48.400  46.901  1.00  9.66           C  
ANISOU 1752  CZ  TYR A 224     1178   1323   1168     52    109    -35       C  
ATOM   1753  OH  TYR A 224      28.699  47.833  47.021  1.00 10.53           O  
ANISOU 1753  OH  TYR A 224     1239   1454   1306     50    136    -28       O  
ATOM   1754  N   VAL A 225      33.238  49.922  43.129  1.00  8.67           N  
ANISOU 1754  N   VAL A 225     1110   1160   1025     29    -10    -53       N  
ATOM   1755  CA  VAL A 225      32.587  50.350  41.889  1.00  8.53           C  
ANISOU 1755  CA  VAL A 225     1073   1156   1014     43    -26    -47       C  
ATOM   1756  C   VAL A 225      33.469  51.261  41.046  1.00  8.08           C  
ANISOU 1756  C   VAL A 225     1048   1079    943     47    -40    -44       C  
ATOM   1757  O   VAL A 225      32.972  52.031  40.224  1.00  9.64           O  
ANISOU 1757  O   VAL A 225     1245   1280   1138     72    -48    -33       O  
ATOM   1758  CB  VAL A 225      31.138  50.850  42.135  1.00  9.92           C  
ANISOU 1758  CB  VAL A 225     1219   1348   1200     77    -14    -40       C  
ATOM   1759  CG1 VAL A 225      31.074  52.273  42.679  1.00 10.76           C  
ANISOU 1759  CG1 VAL A 225     1360   1429   1299    114      4    -37       C  
ATOM   1760  CG2 VAL A 225      30.277  50.699  40.881  1.00 10.71           C  
ANISOU 1760  CG2 VAL A 225     1278   1482   1310     85    -39    -34       C  
ATOM   1761  N   THR A 226      34.790  51.106  41.162  1.00  7.94           N  
ANISOU 1761  N   THR A 226     1054   1044    919     22    -42    -50       N  
ATOM   1762  CA  THR A 226      35.786  51.942  40.477  1.00  8.47           C  
ANISOU 1762  CA  THR A 226     1150   1089    978     16    -47    -46       C  
ATOM   1763  C   THR A 226      35.514  53.438  40.644  1.00  8.10           C  
ANISOU 1763  C   THR A 226     1134   1016    927     41    -36    -41       C  
ATOM   1764  O   THR A 226      35.887  54.251  39.788  1.00  9.11           O  
ANISOU 1764  O   THR A 226     1285   1126   1051     46    -36    -30       O  
ATOM   1765  CB  THR A 226      36.019  51.553  39.013  1.00  8.61           C  
ANISOU 1765  CB  THR A 226     1161   1120    991      9    -59    -40       C  
ATOM   1766  CG2 THR A 226      36.546  50.148  38.898  1.00  8.83           C  
ANISOU 1766  CG2 THR A 226     1171   1160   1024    -17    -62    -50       C  
ATOM   1767  OG1 THR A 226      34.820  51.673  38.240  1.00  9.78           O  
ANISOU 1767  OG1 THR A 226     1292   1290   1134     33    -71    -31       O  
ATOM   1768  N   ASN A 227      34.915  53.819  41.759  1.00  8.51           N  
ANISOU 1768  N   ASN A 227     1193   1060    980     58    -21    -48       N  
ATOM   1769  CA  ASN A 227      34.560  55.212  42.008  1.00  8.57           C  
ANISOU 1769  CA  ASN A 227     1235   1035    986     87     -4    -46       C  
ATOM   1770  C   ASN A 227      35.696  55.927  42.730  1.00  8.28           C  
ANISOU 1770  C   ASN A 227     1243    962    942     60      3    -65       C  
ATOM   1771  O   ASN A 227      36.203  55.435  43.735  1.00  9.10           O  
ANISOU 1771  O   ASN A 227     1348   1074   1038     36      0    -83       O  
ATOM   1772  CB  ASN A 227      33.300  55.249  42.865  1.00  9.77           C  
ANISOU 1772  CB  ASN A 227     1373   1198   1142    122     16    -48       C  
ATOM   1773  CG  ASN A 227      32.902  56.650  43.225  1.00  9.98           C  
ANISOU 1773  CG  ASN A 227     1439   1185   1168    158     41    -49       C  
ATOM   1774  ND2 ASN A 227      32.192  57.307  42.330  1.00 13.11           N  
ANISOU 1774  ND2 ASN A 227     1830   1577   1573    200     42    -26       N  
ATOM   1775  OD1 ASN A 227      33.246  57.163  44.299  1.00 10.85           O  
ANISOU 1775  OD1 ASN A 227     1588   1267   1267    151     60    -71       O  
ATOM   1776  N   ILE A 228      36.106  57.088  42.221  1.00  8.58           N  
ANISOU 1776  N   ILE A 228     1319    959    982     61     12    -61       N  
ATOM   1777  CA  ILE A 228      37.249  57.777  42.825  1.00  8.88           C  
ANISOU 1777  CA  ILE A 228     1395    961   1017     23     16    -84       C  
ATOM   1778  C   ILE A 228      37.032  58.051  44.315  1.00  9.18           C  
ANISOU 1778  C   ILE A 228     1458    988   1042     24     27   -113       C  
ATOM   1779  O   ILE A 228      37.922  57.797  45.140  1.00  9.93           O  
ANISOU 1779  O   ILE A 228     1559   1091   1125    -14     12   -136       O  
ATOM   1780  CB  ILE A 228      37.615  59.049  42.041  1.00  9.49           C  
ANISOU 1780  CB  ILE A 228     1515    987   1105     22     32    -73       C  
ATOM   1781  CG1 ILE A 228      38.338  58.656  40.745  1.00 10.17           C  
ANISOU 1781  CG1 ILE A 228     1581   1087   1195      2     22    -51       C  
ATOM   1782  CG2 ILE A 228      38.477  59.984  42.894  1.00 10.27           C  
ANISOU 1782  CG2 ILE A 228     1659   1039   1203    -16     43   -105       C  
ATOM   1783  CD1 ILE A 228      38.611  59.797  39.797  1.00 11.08           C  
ANISOU 1783  CD1 ILE A 228     1737   1155   1317      5     43    -29       C  
ATOM   1784  N  AASP A 229      35.871  58.583  44.694  0.58  9.61           N  
ANISOU 1784  N  AASP A 229     1529   1029   1095     70     52   -112       N  
ATOM   1785  N  BASP A 229      35.870  58.601  44.680  0.42  9.95           N  
ANISOU 1785  N  BASP A 229     1572   1072   1138     71     52   -112       N  
ATOM   1786  CA AASP A 229      35.676  58.933  46.098  0.58  9.39           C  
ANISOU 1786  CA AASP A 229     1534    986   1046     73     70   -143       C  
ATOM   1787  CA BASP A 229      35.623  58.945  46.076  0.42 11.14           C  
ANISOU 1787  CA BASP A 229     1756   1208   1269     76     71   -142       C  
ATOM   1788  C  AASP A 229      35.694  57.697  46.990  0.58  9.77           C  
ANISOU 1788  C  AASP A 229     1552   1084   1075     60     56   -150       C  
ATOM   1789  C  BASP A 229      35.695  57.710  46.969  0.42  9.54           C  
ANISOU 1789  C  BASP A 229     1524   1054   1047     60     56   -149       C  
ATOM   1790  O  AASP A 229      36.325  57.691  48.058  0.58  9.69           O  
ANISOU 1790  O  AASP A 229     1568   1074   1038     32     49   -177       O  
ATOM   1791  O  BASP A 229      36.369  57.713  48.008  0.42 13.14           O  
ANISOU 1791  O  BASP A 229     2005   1510   1477     31     48   -176       O  
ATOM   1792  CB AASP A 229      34.387  59.727  46.275  0.58  9.80           C  
ANISOU 1792  CB AASP A 229     1606   1014   1104    134    108   -138       C  
ATOM   1793  CB BASP A 229      34.262  59.631  46.220  0.42 12.06           C  
ANISOU 1793  CB BASP A 229     1886   1305   1391    138    108   -134       C  
ATOM   1794  CG AASP A 229      34.543  61.147  45.813  0.58 10.97           C  
ANISOU 1794  CG AASP A 229     1809   1096   1264    146    129   -139       C  
ATOM   1795  CG BASP A 229      34.246  61.031  45.635  0.42 13.47           C  
ANISOU 1795  CG BASP A 229     2113   1421   1585    159    130   -129       C  
ATOM   1796  OD1AASP A 229      35.301  61.895  46.465  0.58 13.55           O  
ANISOU 1796  OD1AASP A 229     2191   1377   1579    112    136   -174       O  
ATOM   1797  OD2AASP A 229      33.953  61.489  44.766  0.58 12.88           O1-
ANISOU 1797  OD2AASP A 229     2039   1329   1525    186    135   -104       O1-
ATOM   1798  OD1BASP A 229      35.321  61.575  45.293  0.42 11.95           O  
ANISOU 1798  OD1BASP A 229     1953   1193   1396    117    121   -138       O  
ATOM   1799  OD2BASP A 229      33.139  61.611  45.511  0.42 13.59           O1-
ANISOU 1799  OD2BASP A 229     2133   1420   1611    221    159   -113       O1-
ATOM   1800  N   LEU A 230      34.985  56.645  46.596  1.00  9.63           N  
ANISOU 1800  N   LEU A 230     1482   1107   1068     77     53   -125       N  
ATOM   1801  CA  LEU A 230      34.962  55.449  47.432  1.00  9.11           C  
ANISOU 1801  CA  LEU A 230     1394   1080    988     66     48   -126       C  
ATOM   1802  C   LEU A 230      36.317  54.761  47.481  1.00  9.13           C  
ANISOU 1802  C   LEU A 230     1389   1097    982     21     14   -129       C  
ATOM   1803  O   LEU A 230      36.624  54.063  48.460  1.00 10.09           O  
ANISOU 1803  O   LEU A 230     1513   1241   1081     10      8   -134       O  
ATOM   1804  CB  LEU A 230      33.879  54.477  46.987  1.00  9.74           C  
ANISOU 1804  CB  LEU A 230     1420   1194   1087     87     56   -101       C  
ATOM   1805  CG  LEU A 230      32.455  55.016  47.082  1.00 10.43           C  
ANISOU 1805  CG  LEU A 230     1498   1280   1186    136     89    -95       C  
ATOM   1806  CD1 LEU A 230      31.466  53.939  46.650  1.00 11.54           C  
ANISOU 1806  CD1 LEU A 230     1574   1461   1349    144     91    -74       C  
ATOM   1807  CD2 LEU A 230      32.124  55.481  48.490  1.00 13.13           C  
ANISOU 1807  CD2 LEU A 230     1879   1609   1501    152    125   -114       C  
ATOM   1808  N   THR A 231      37.120  54.929  46.430  1.00  9.33           N  
ANISOU 1808  N   THR A 231     1406   1114   1026      0     -5   -123       N  
ATOM   1809  CA  THR A 231      38.472  54.377  46.397  1.00 10.06           C  
ANISOU 1809  CA  THR A 231     1485   1221   1118    -38    -33   -125       C  
ATOM   1810  C   THR A 231      39.390  55.153  47.342  1.00  9.38           C  
ANISOU 1810  C   THR A 231     1433   1119   1010    -68    -45   -154       C  
ATOM   1811  O   THR A 231      40.031  54.571  48.229  1.00 10.54           O  
ANISOU 1811  O   THR A 231     1575   1293   1136    -85    -67   -161       O  
ATOM   1812  CB  THR A 231      39.000  54.394  44.959  1.00  9.20           C  
ANISOU 1812  CB  THR A 231     1356   1106   1034    -50    -40   -110       C  
ATOM   1813  CG2 THR A 231      40.414  53.832  44.861  1.00 10.26           C  
ANISOU 1813  CG2 THR A 231     1469   1257   1175    -85    -62   -111       C  
ATOM   1814  OG1 THR A 231      38.145  53.586  44.139  1.00  9.57           O  
ANISOU 1814  OG1 THR A 231     1372   1172   1093    -27    -35    -90       O  
ATOM   1815  N  AVAL A 232      39.460  56.478  47.203  0.58 10.52           N  
ANISOU 1815  N  AVAL A 232     1617   1221   1159    -76    -34   -172       N  
ATOM   1816  N  BVAL A 232      39.464  56.473  47.174  0.42 10.61           N  
ANISOU 1816  N  BVAL A 232     1627   1232   1171    -76    -34   -172       N  
ATOM   1817  CA AVAL A 232      40.359  57.207  48.096  0.58 11.58           C  
ANISOU 1817  CA AVAL A 232     1785   1341   1274   -114    -49   -207       C  
ATOM   1818  CA BVAL A 232      40.281  57.290  48.067  0.42 10.54           C  
ANISOU 1818  CA BVAL A 232     1656   1205   1142   -112    -46   -208       C  
ATOM   1819  C  AVAL A 232      39.944  57.038  49.555  0.58 13.10           C  
ANISOU 1819  C  AVAL A 232     2006   1550   1423   -103    -48   -228       C  
ATOM   1820  C  BVAL A 232      39.934  57.011  49.522  0.42  9.00           C  
ANISOU 1820  C  BVAL A 232     1484   1030    904   -102    -48   -227       C  
ATOM   1821  O  AVAL A 232      40.798  57.036  50.452  0.58 15.25           O  
ANISOU 1821  O  AVAL A 232     2289   1839   1666   -135    -77   -253       O  
ATOM   1822  O  BVAL A 232      40.822  56.878  50.375  0.42  9.98           O  
ANISOU 1822  O  BVAL A 232     1614   1176   1001   -134    -79   -248       O  
ATOM   1823  CB AVAL A 232      40.525  58.692  47.708  0.58 13.27           C  
ANISOU 1823  CB AVAL A 232     2046   1495   1503   -130    -30   -226       C  
ATOM   1824  CB BVAL A 232      40.123  58.780  47.701  0.42 12.49           C  
ANISOU 1824  CB BVAL A 232     1953   1389   1402   -115    -20   -224       C  
ATOM   1825  CG1AVAL A 232      40.993  58.820  46.261  0.58 13.60           C  
ANISOU 1825  CG1AVAL A 232     2063   1523   1581   -142    -27   -200       C  
ATOM   1826  CG2AVAL A 232      39.252  59.472  47.950  0.58 11.53           C  
ANISOU 1826  CG2AVAL A 232     1869   1236   1275    -84      9   -232       C  
ATOM   1827  CG1BVAL A 232      40.477  59.677  48.872  0.42 12.42           C  
ANISOU 1827  CG1BVAL A 232     2000   1354   1366   -143    -21   -271       C  
ATOM   1828  CG2BVAL A 232      40.982  59.104  46.481  0.42 11.24           C  
ANISOU 1828  CG2BVAL A 232     1779   1214   1279   -145    -24   -209       C  
ATOM   1829  N   GLU A 233      38.644  56.904  49.829  1.00 11.36           N  
ANISOU 1829  N   GLU A 233     1795   1329   1194    -56    -15   -219       N  
ATOM   1830  CA  GLU A 233      38.193  56.795  51.212  1.00 11.70           C  
ANISOU 1830  CA  GLU A 233     1870   1384   1191    -43     -4   -238       C  
ATOM   1831  C   GLU A 233      38.385  55.405  51.802  1.00 11.18           C  
ANISOU 1831  C   GLU A 233     1773   1371   1104    -42    -23   -217       C  
ATOM   1832  O   GLU A 233      38.640  55.292  53.011  1.00 13.41           O  
ANISOU 1832  O   GLU A 233     2085   1672   1336    -49    -33   -234       O  
ATOM   1833  CB  GLU A 233      36.716  57.199  51.300  1.00 13.03           C  
ANISOU 1833  CB  GLU A 233     2055   1532   1363      9     47   -234       C  
ATOM   1834  CG  GLU A 233      36.477  58.668  50.934  1.00 18.05           C  
ANISOU 1834  CG  GLU A 233     2736   2108   2015     20     73   -254       C  
ATOM   1835  CD  GLU A 233      35.041  58.991  50.545  1.00 36.24           C  
ANISOU 1835  CD  GLU A 233     5033   4396   4341     81    119   -234       C  
ATOM   1836  OE1 GLU A 233      34.178  58.089  50.578  1.00 31.40           O  
ANISOU 1836  OE1 GLU A 233     4376   3822   3734    109    132   -208       O  
ATOM   1837  OE2 GLU A 233      34.781  60.166  50.196  1.00 31.90           O1-
ANISOU 1837  OE2 GLU A 233     4521   3794   3807    100    144   -243       O1-
ATOM   1838  N   ASN A 234      38.271  54.347  51.013  1.00 10.33           N  
ANISOU 1838  N   ASN A 234     1612   1285   1026    -34    -27   -181       N  
ATOM   1839  CA  ASN A 234      38.152  53.004  51.568  1.00 10.46           C  
ANISOU 1839  CA  ASN A 234     1607   1340   1028    -24    -30   -156       C  
ATOM   1840  C   ASN A 234      39.129  51.980  51.023  1.00 10.47           C  
ANISOU 1840  C   ASN A 234     1565   1364   1049    -42    -62   -133       C  
ATOM   1841  O   ASN A 234      39.268  50.909  51.638  1.00 11.73           O  
ANISOU 1841  O   ASN A 234     1715   1550   1191    -34    -68   -112       O  
ATOM   1842  CB  ASN A 234      36.723  52.461  51.400  1.00 11.18           C  
ANISOU 1842  CB  ASN A 234     1679   1433   1135     10     13   -134       C  
ATOM   1843  CG  ASN A 234      35.686  53.422  51.918  1.00 11.92           C  
ANISOU 1843  CG  ASN A 234     1808   1507   1216     38     53   -152       C  
ATOM   1844  ND2 ASN A 234      35.603  53.536  53.205  1.00 11.07           N  
ANISOU 1844  ND2 ASN A 234     1742   1406   1059     44     66   -167       N  
ATOM   1845  OD1 ASN A 234      34.968  54.074  51.132  1.00 13.62           O  
ANISOU 1845  OD1 ASN A 234     2012   1700   1461     57     72   -152       O  
ATOM   1846  N   PHE A 235      39.788  52.226  49.900  1.00 10.45           N  
ANISOU 1846  N   PHE A 235     1538   1351   1082    -60    -78   -133       N  
ATOM   1847  CA  PHE A 235      40.741  51.265  49.351  1.00 10.33           C  
ANISOU 1847  CA  PHE A 235     1482   1356   1087    -72   -102   -112       C  
ATOM   1848  C   PHE A 235      41.942  51.124  50.277  1.00 10.37           C  
ANISOU 1848  C   PHE A 235     1486   1388   1064    -90   -140   -118       C  
ATOM   1849  O   PHE A 235      42.439  52.110  50.826  1.00 11.64           O  
ANISOU 1849  O   PHE A 235     1673   1546   1204   -114   -159   -147       O  
ATOM   1850  CB  PHE A 235      41.186  51.758  47.968  1.00 11.61           C  
ANISOU 1850  CB  PHE A 235     1624   1499   1287    -88   -103   -113       C  
ATOM   1851  CG  PHE A 235      42.299  50.961  47.346  1.00 10.40           C  
ANISOU 1851  CG  PHE A 235     1430   1363   1157   -101   -121    -97       C  
ATOM   1852  CD1 PHE A 235      43.606  51.285  47.612  1.00 10.99           C  
ANISOU 1852  CD1 PHE A 235     1492   1451   1231   -129   -150   -107       C  
ATOM   1853  CD2 PHE A 235      42.040  49.937  46.444  1.00 10.85           C  
ANISOU 1853  CD2 PHE A 235     1461   1423   1238    -86   -107    -76       C  
ATOM   1854  CE1 PHE A 235      44.648  50.584  47.039  1.00 11.76           C  
ANISOU 1854  CE1 PHE A 235     1546   1567   1355   -135   -161    -91       C  
ATOM   1855  CE2 PHE A 235      43.071  49.237  45.858  1.00 11.53           C  
ANISOU 1855  CE2 PHE A 235     1514   1520   1345    -93   -115    -63       C  
ATOM   1856  CZ  PHE A 235      44.380  49.554  46.159  1.00 11.90           C  
ANISOU 1856  CZ  PHE A 235     1543   1583   1395   -113   -140    -68       C  
ATOM   1857  N   VAL A 236      42.423  49.892  50.419  1.00 10.46           N  
ANISOU 1857  N   VAL A 236     1469   1425   1078    -79   -153    -89       N  
ATOM   1858  CA  VAL A 236      43.646  49.587  51.150  1.00 11.34           C  
ANISOU 1858  CA  VAL A 236     1568   1573   1170    -89   -195    -85       C  
ATOM   1859  C   VAL A 236      44.581  48.853  50.198  1.00 10.91           C  
ANISOU 1859  C   VAL A 236     1460   1527   1159    -89   -205    -62       C  
ATOM   1860  O   VAL A 236      44.207  47.831  49.623  1.00 11.40           O  
ANISOU 1860  O   VAL A 236     1508   1580   1245    -67   -180    -37       O  
ATOM   1861  CB  VAL A 236      43.368  48.734  52.404  1.00 12.23           C  
ANISOU 1861  CB  VAL A 236     1700   1710   1235    -61   -199    -63       C  
ATOM   1862  CG1 VAL A 236      44.690  48.330  53.068  1.00 13.91           C  
ANISOU 1862  CG1 VAL A 236     1891   1967   1427    -63   -250    -50       C  
ATOM   1863  CG2 VAL A 236      42.469  49.482  53.380  1.00 13.49           C  
ANISOU 1863  CG2 VAL A 236     1917   1863   1347    -59   -182    -87       C  
ATOM   1864  N   LEU A 237      45.784  49.361  50.034  1.00 11.09           N  
ANISOU 1864  N   LEU A 237     1455   1566   1194   -117   -236    -75       N  
ATOM   1865  CA  LEU A 237      46.740  48.720  49.136  1.00 11.73           C  
ANISOU 1865  CA  LEU A 237     1482   1657   1318   -115   -239    -54       C  
ATOM   1866  C   LEU A 237      47.115  47.351  49.685  1.00 11.69           C  
ANISOU 1866  C   LEU A 237     1456   1680   1307    -78   -251    -17       C  
ATOM   1867  O   LEU A 237      47.503  47.252  50.847  1.00 12.04           O  
ANISOU 1867  O   LEU A 237     1504   1758   1312    -72   -287    -11       O  
ATOM   1868  CB  LEU A 237      47.988  49.586  49.026  1.00 14.01           C  
ANISOU 1868  CB  LEU A 237     1737   1963   1621   -156   -270    -74       C  
ATOM   1869  CG  LEU A 237      48.950  49.227  47.897  1.00 15.99           C  
ANISOU 1869  CG  LEU A 237     1931   2219   1923   -160   -260    -58       C  
ATOM   1870  CD1 LEU A 237      48.341  49.494  46.536  1.00 15.53           C  
ANISOU 1870  CD1 LEU A 237     1889   2119   1894   -163   -213    -61       C  
ATOM   1871  CD2 LEU A 237      50.263  50.002  48.062  1.00 17.94           C  
ANISOU 1871  CD2 LEU A 237     2137   2496   2186   -205   -296    -76       C  
ATOM   1872  N   PRO A 238      47.022  46.285  48.889  1.00 10.62           N  
ANISOU 1872  N   PRO A 238     1303   1530   1204    -51   -221      9       N  
ATOM   1873  CA  PRO A 238      47.424  44.967  49.385  1.00 10.69           C  
ANISOU 1873  CA  PRO A 238     1296   1555   1211    -11   -226     49       C  
ATOM   1874  C   PRO A 238      48.895  44.938  49.749  1.00 11.68           C  
ANISOU 1874  C   PRO A 238     1370   1726   1341     -8   -270     61       C  
ATOM   1875  O   PRO A 238      49.710  45.696  49.197  1.00 12.62           O  
ANISOU 1875  O   PRO A 238     1452   1857   1485    -40   -284     41       O  
ATOM   1876  CB  PRO A 238      47.160  44.037  48.196  1.00 10.97           C  
ANISOU 1876  CB  PRO A 238     1322   1556   1290      6   -181     62       C  
ATOM   1877  CG  PRO A 238      46.068  44.725  47.437  1.00 11.08           C  
ANISOU 1877  CG  PRO A 238     1363   1538   1308    -18   -153     33       C  
ATOM   1878  CD  PRO A 238      46.381  46.197  47.559  1.00 11.11           C  
ANISOU 1878  CD  PRO A 238     1368   1554   1300    -54   -178      4       C  
ATOM   1879  N   GLN A 239      49.235  44.026  50.658  1.00 11.42           N  
ANISOU 1879  N   GLN A 239     1333   1719   1287     31   -291     97       N  
ATOM   1880  CA  GLN A 239      50.629  43.674  50.891  1.00 12.94           C  
ANISOU 1880  CA  GLN A 239     1465   1958   1492     50   -331    121       C  
ATOM   1881  C   GLN A 239      51.172  42.912  49.690  1.00 12.45           C  
ANISOU 1881  C   GLN A 239     1360   1876   1492     73   -293    139       C  
ATOM   1882  O   GLN A 239      50.448  42.186  49.008  1.00 14.01           O  
ANISOU 1882  O   GLN A 239     1587   2026   1711     91   -242    147       O  
ATOM   1883  CB  GLN A 239      50.727  42.783  52.122  1.00 14.64           C  
ANISOU 1883  CB  GLN A 239     1695   2202   1665     98   -357    165       C  
ATOM   1884  CG  GLN A 239      50.195  43.419  53.390  1.00 20.77           C  
ANISOU 1884  CG  GLN A 239     2522   3001   2368     82   -389    149       C  
ATOM   1885  CD  GLN A 239      50.920  44.696  53.747  1.00 26.14           C  
ANISOU 1885  CD  GLN A 239     3178   3726   3029     32   -447    107       C  
ATOM   1886  NE2 GLN A 239      50.189  45.803  53.765  1.00 33.53           N  
ANISOU 1886  NE2 GLN A 239     4157   4638   3945    -14   -437     58       N  
ATOM   1887  OE1 GLN A 239      52.126  44.692  54.001  1.00 39.70           O  
ANISOU 1887  OE1 GLN A 239     4836   5497   4750     34   -499    116       O  
ATOM   1888  N   ASP A 240      52.459  43.083  49.418  1.00 12.95           N  
ANISOU 1888  N   ASP A 240     1355   1977   1587     71   -318    143       N  
ATOM   1889  CA  ASP A 240      53.083  42.466  48.257  1.00 12.95           C  
ANISOU 1889  CA  ASP A 240     1313   1962   1647     93   -277    157       C  
ATOM   1890  C   ASP A 240      54.501  42.053  48.615  1.00 16.91           C  
ANISOU 1890  C   ASP A 240     1735   2520   2170    126   -313    190       C  
ATOM   1891  O   ASP A 240      55.079  42.520  49.597  1.00 19.56           O  
ANISOU 1891  O   ASP A 240     2041   2913   2478    115   -377    191       O  
ATOM   1892  CB  ASP A 240      53.046  43.438  47.066  1.00 13.20           C  
ANISOU 1892  CB  ASP A 240     1337   1971   1706     41   -248    118       C  
ATOM   1893  CG  ASP A 240      53.107  42.748  45.712  1.00 12.25           C  
ANISOU 1893  CG  ASP A 240     1211   1814   1631     62   -186    123       C  
ATOM   1894  OD1 ASP A 240      53.293  41.505  45.655  1.00 13.28           O  
ANISOU 1894  OD1 ASP A 240     1336   1932   1778    117   -163    155       O  
ATOM   1895  OD2 ASP A 240      52.966  43.479  44.708  1.00 12.33           O1-
ANISOU 1895  OD2 ASP A 240     1226   1804   1654     25   -159     96       O1-
ATOM   1896  N   VAL A 241      55.035  41.125  47.817  1.00 16.25           N  
ANISOU 1896  N   VAL A 241     1619   2421   2136    171   -271    216       N  
ATOM   1897  CA  VAL A 241      56.390  40.612  48.007  1.00 19.01           C  
ANISOU 1897  CA  VAL A 241     1884   2820   2517    215   -294    252       C  
ATOM   1898  C   VAL A 241      57.445  41.432  47.276  1.00 19.78           C  
ANISOU 1898  C   VAL A 241     1902   2954   2661    176   -296    231       C  
ATOM   1899  O   VAL A 241      58.647  41.167  47.433  1.00 25.91           O  
ANISOU 1899  O   VAL A 241     2592   3784   3470    205   -319    258       O  
ATOM   1900  CB  VAL A 241      56.492  39.154  47.509  1.00 23.97           C  
ANISOU 1900  CB  VAL A 241     2518   3409   3182    291   -237    293       C  
ATOM   1901  CG1 VAL A 241      55.531  38.263  48.281  1.00 28.50           C  
ANISOU 1901  CG1 VAL A 241     3168   3945   3717    329   -231    321       C  
ATOM   1902  CG2 VAL A 241      56.203  39.072  46.010  1.00 28.27           C  
ANISOU 1902  CG2 VAL A 241     3082   3896   3765    276   -162    265       C  
ATOM   1903  N   VAL A 242      57.034  42.390  46.460  1.00 16.19           N  
ANISOU 1903  N   VAL A 242     1470   2469   2211    113   -268    187       N  
ATOM   1904  CA  VAL A 242      57.889  43.286  45.703  1.00 14.26           C  
ANISOU 1904  CA  VAL A 242     1163   2247   2008     64   -259    165       C  
ATOM   1905  C   VAL A 242      57.280  44.666  45.880  1.00 14.01           C  
ANISOU 1905  C   VAL A 242     1174   2205   1944    -14   -282    119       C  
ATOM   1906  O   VAL A 242      56.098  44.803  46.192  1.00 14.71           O  
ANISOU 1906  O   VAL A 242     1344   2257   1989    -21   -282    105       O  
ATOM   1907  CB  VAL A 242      57.910  42.863  44.217  1.00 16.19           C  
ANISOU 1907  CB  VAL A 242     1413   2446   2294     81   -175    165       C  
ATOM   1908  CG1 VAL A 242      56.486  42.817  43.652  1.00 17.76           C  
ANISOU 1908  CG1 VAL A 242     1710   2575   2461     71   -135    142       C  
ATOM   1909  CG2 VAL A 242      58.798  43.781  43.399  1.00 31.63           C  
ANISOU 1909  CG2 VAL A 242     3306   4422   4291     31   -155    147       C  
ATOM   1910  N   ASP A 243      58.094  45.698  45.714  1.00 13.86           N  
ANISOU 1910  N   ASP A 243     1100   2216   1949    -72   -299     98       N  
ATOM   1911  CA  ASP A 243      57.587  47.057  45.836  1.00 13.94           C  
ANISOU 1911  CA  ASP A 243     1155   2206   1935   -147   -314     54       C  
ATOM   1912  C   ASP A 243      57.150  47.606  44.481  1.00 12.10           C  
ANISOU 1912  C   ASP A 243      958   1916   1722   -175   -244     37       C  
ATOM   1913  O   ASP A 243      57.672  47.231  43.429  1.00 13.15           O  
ANISOU 1913  O   ASP A 243     1057   2044   1898   -159   -192     52       O  
ATOM   1914  CB  ASP A 243      58.624  47.986  46.465  1.00 17.42           C  
ANISOU 1914  CB  ASP A 243     1527   2703   2388   -207   -372     33       C  
ATOM   1915  CG  ASP A 243      58.952  47.612  47.908  1.00 19.73           C  
ANISOU 1915  CG  ASP A 243     1795   3059   2643   -186   -453     45       C  
ATOM   1916  OD1 ASP A 243      58.105  46.983  48.571  1.00 28.28           O  
ANISOU 1916  OD1 ASP A 243     2940   4128   3675   -140   -465     59       O  
ATOM   1917  OD2 ASP A 243      60.058  47.959  48.368  1.00 40.57           O1-
ANISOU 1917  OD2 ASP A 243     4351   5764   5301   -216   -506     40       O1-
ATOM   1918  N   ASN A 244      56.191  48.523  44.522  1.00 12.59           N  
ANISOU 1918  N   ASN A 244     1093   1937   1752   -215   -243      6       N  
ATOM   1919  CA  ASN A 244      55.850  49.362  43.369  1.00 12.83           C  
ANISOU 1919  CA  ASN A 244     1159   1920   1796   -252   -190    -10       C  
ATOM   1920  C   ASN A 244      55.321  48.580  42.176  1.00 11.47           C  
ANISOU 1920  C   ASN A 244     1016   1711   1630   -208   -127      7       C  
ATOM   1921  O   ASN A 244      55.556  48.978  41.030  1.00 12.17           O  
ANISOU 1921  O   ASN A 244     1104   1780   1741   -226    -77      6       O  
ATOM   1922  CB  ASN A 244      57.057  50.207  42.940  1.00 14.90           C  
ANISOU 1922  CB  ASN A 244     1355   2202   2106   -309   -182    -18       C  
ATOM   1923  CG  ASN A 244      57.655  50.947  44.078  1.00 15.69           C  
ANISOU 1923  CG  ASN A 244     1420   2340   2201   -361   -248    -42       C  
ATOM   1924  ND2 ASN A 244      58.979  50.924  44.195  1.00 15.47           N  
ANISOU 1924  ND2 ASN A 244     1293   2368   2217   -382   -268    -35       N  
ATOM   1925  OD1 ASN A 244      56.910  51.521  44.874  1.00 15.71           O  
ANISOU 1925  OD1 ASN A 244     1482   2325   2160   -381   -281    -68       O  
ATOM   1926  N   ARG A 245      54.576  47.503  42.427  1.00 10.95           N  
ANISOU 1926  N   ARG A 245      983   1635   1541   -154   -127     21       N  
ATOM   1927  CA  ARG A 245      54.011  46.714  41.342  1.00 10.53           C  
ANISOU 1927  CA  ARG A 245      964   1547   1490   -118    -72     29       C  
ATOM   1928  C   ARG A 245      52.504  46.562  41.466  1.00 10.08           C  
ANISOU 1928  C   ARG A 245      984   1454   1392   -106    -73     19       C  
ATOM   1929  O   ARG A 245      51.925  45.717  40.769  1.00 11.69           O  
ANISOU 1929  O   ARG A 245     1216   1632   1592    -76    -38     24       O  
ATOM   1930  CB  ARG A 245      54.678  45.343  41.224  1.00 10.96           C  
ANISOU 1930  CB  ARG A 245      977   1618   1571    -61    -54     57       C  
ATOM   1931  CG  ARG A 245      56.143  45.391  40.793  1.00 11.38           C  
ANISOU 1931  CG  ARG A 245      946   1705   1672    -64    -36     70       C  
ATOM   1932  CD  ARG A 245      56.299  45.868  39.364  1.00 10.90           C  
ANISOU 1932  CD  ARG A 245      894   1620   1627    -87     26     60       C  
ATOM   1933  NE  ARG A 245      57.696  45.943  38.958  1.00 11.96           N  
ANISOU 1933  NE  ARG A 245      943   1789   1811    -92     51     74       N  
ATOM   1934  CZ  ARG A 245      58.486  46.987  39.189  1.00 12.28           C  
ANISOU 1934  CZ  ARG A 245      930   1859   1876   -147     32     68       C  
ATOM   1935  NH1 ARG A 245      58.022  48.061  39.833  1.00 13.54           N1+
ANISOU 1935  NH1 ARG A 245     1121   2013   2012   -202    -12     46       N1+
ATOM   1936  NH2 ARG A 245      59.747  46.970  38.782  1.00 14.06           N  
ANISOU 1936  NH2 ARG A 245     1070   2119   2153   -151     61     82       N  
ATOM   1937  N   LEU A 246      51.852  47.357  42.312  1.00 10.37           N  
ANISOU 1937  N   LEU A 246     1009   1367   1563     37   -383     60       N  
ATOM   1938  CA  LEU A 246      50.402  47.381  42.424  1.00 10.14           C  
ANISOU 1938  CA  LEU A 246     1069   1344   1440     36   -337     43       C  
ATOM   1939  C   LEU A 246      49.903  48.769  42.059  1.00  9.84           C  
ANISOU 1939  C   LEU A 246     1043   1307   1388     -3   -329     14       C  
ATOM   1940  O   LEU A 246      50.374  49.771  42.608  1.00 11.51           O  
ANISOU 1940  O   LEU A 246     1253   1513   1608    -23   -399     -1       O  
ATOM   1941  CB  LEU A 246      49.926  47.034  43.831  1.00 10.14           C  
ANISOU 1941  CB  LEU A 246     1153   1341   1357     64   -386     45       C  
ATOM   1942  CG  LEU A 246      50.340  45.667  44.347  1.00 10.59           C  
ANISOU 1942  CG  LEU A 246     1213   1393   1416    107   -400     77       C  
ATOM   1943  CD1 LEU A 246      49.762  45.461  45.742  1.00 12.01           C  
ANISOU 1943  CD1 LEU A 246     1497   1567   1499    133   -441     80       C  
ATOM   1944  CD2 LEU A 246      49.943  44.534  43.422  1.00 10.58           C  
ANISOU 1944  CD2 LEU A 246     1196   1390   1435    121   -304     92       C  
ATOM   1945  N   MET A 247      48.934  48.820  41.143  1.00  9.07           N  
ANISOU 1945  N   MET A 247      963   1214   1270    -14   -250      5       N  
ATOM   1946  CA  MET A 247      48.385  50.074  40.637  1.00  9.21           C  
ANISOU 1946  CA  MET A 247      992   1230   1278    -46   -233    -17       C  
ATOM   1947  C   MET A 247      46.899  50.140  40.961  1.00  8.98           C  
ANISOU 1947  C   MET A 247     1035   1203   1173    -39   -202    -28       C  
ATOM   1948  O   MET A 247      46.176  49.162  40.736  1.00  9.75           O  
ANISOU 1948  O   MET A 247     1150   1304   1250    -23   -154    -17       O  
ATOM   1949  CB  MET A 247      48.578  50.189  39.112  1.00  9.81           C  
ANISOU 1949  CB  MET A 247     1020   1304   1405    -65   -168    -13       C  
ATOM   1950  CG  MET A 247      49.981  49.849  38.624  1.00 10.98           C  
ANISOU 1950  CG  MET A 247     1089   1444   1638    -64   -166      6       C  
ATOM   1951  SD  MET A 247      50.239  50.095  36.873  1.00 11.86           S  
ANISOU 1951  SD  MET A 247     1165   1544   1796    -83    -76     12       S  
ATOM   1952  CE  MET A 247      49.151  48.850  36.195  1.00 12.18           C  
ANISOU 1952  CE  MET A 247     1261   1588   1778    -63     -8     14       C  
ATOM   1953  N   VAL A 248      46.448  51.272  41.488  1.00  8.83           N  
ANISOU 1953  N   VAL A 248     1056   1178   1121    -51   -227    -48       N  
ATOM   1954  CA  VAL A 248      45.036  51.459  41.819  1.00  9.00           C  
ANISOU 1954  CA  VAL A 248     1138   1197   1083    -42   -190    -55       C  
ATOM   1955  C   VAL A 248      44.262  51.776  40.549  1.00  8.95           C  
ANISOU 1955  C   VAL A 248     1110   1194   1097    -60   -132    -56       C  
ATOM   1956  O   VAL A 248      44.577  52.733  39.836  1.00  9.99           O  
ANISOU 1956  O   VAL A 248     1216   1321   1257    -84   -135    -65       O  
ATOM   1957  CB  VAL A 248      44.866  52.588  42.838  1.00 10.16           C  
ANISOU 1957  CB  VAL A 248     1342   1328   1188    -44   -230    -77       C  
ATOM   1958  CG1 VAL A 248      43.414  52.728  43.262  1.00 11.92           C  
ANISOU 1958  CG1 VAL A 248     1627   1544   1358    -26   -179    -80       C  
ATOM   1959  CG2 VAL A 248      45.764  52.360  44.057  1.00 11.22           C  
ANISOU 1959  CG2 VAL A 248     1508   1457   1300    -30   -307    -78       C  
ATOM   1960  N   ALA A 249      43.226  50.994  40.276  1.00  8.85           N  
ANISOU 1960  N   ALA A 249     1110   1184   1068    -49    -84    -46       N  
ATOM   1961  CA  ALA A 249      42.384  51.181  39.103  1.00  8.95           C  
ANISOU 1961  CA  ALA A 249     1109   1198   1095    -64    -43    -45       C  
ATOM   1962  C   ALA A 249      41.126  51.952  39.473  1.00  8.32           C  
ANISOU 1962  C   ALA A 249     1059   1110    991    -60    -27    -50       C  
ATOM   1963  O   ALA A 249      40.420  51.559  40.398  1.00  9.74           O  
ANISOU 1963  O   ALA A 249     1272   1285   1144    -39    -10    -45       O  
ATOM   1964  CB  ALA A 249      41.978  49.817  38.536  1.00  9.92           C  
ANISOU 1964  CB  ALA A 249     1222   1323   1224    -59     -8    -31       C  
ATOM   1965  N   VAL A 250      40.830  53.035  38.728  1.00  8.73           N  
ANISOU 1965  N   VAL A 250     1102   1158   1058    -77    -24    -57       N  
ATOM   1966  CA  VAL A 250      39.563  53.751  38.840  1.00  8.45           C  
ANISOU 1966  CA  VAL A 250     1084   1112   1015    -70     -2    -57       C  
ATOM   1967  C   VAL A 250      38.978  53.921  37.443  1.00  7.61           C  
ANISOU 1967  C   VAL A 250      950   1006    934    -86     10    -48       C  
ATOM   1968  O   VAL A 250      39.680  53.840  36.439  1.00  8.14           O  
ANISOU 1968  O   VAL A 250     1000   1077   1014   -104      3    -48       O  
ATOM   1969  CB  VAL A 250      39.694  55.116  39.544  1.00  8.65           C  
ANISOU 1969  CB  VAL A 250     1142   1121   1025    -67    -18    -73       C  
ATOM   1970  CG1 VAL A 250      40.140  54.935  40.985  1.00 10.10           C  
ANISOU 1970  CG1 VAL A 250     1371   1298   1169    -50    -39    -83       C  
ATOM   1971  CG2 VAL A 250      40.619  56.042  38.793  1.00 10.32           C  
ANISOU 1971  CG2 VAL A 250     1334   1329   1261    -94    -45    -83       C  
ATOM   1972  N   HIS A 251      37.677  54.193  37.388  1.00  7.71           N  
ANISOU 1972  N   HIS A 251      962   1011    955    -78     29    -40       N  
ATOM   1973  CA  HIS A 251      37.007  54.551  36.139  1.00  7.64           C  
ANISOU 1973  CA  HIS A 251      934    999    968    -91     26    -30       C  
ATOM   1974  C   HIS A 251      36.453  55.960  36.280  1.00  7.75           C  
ANISOU 1974  C   HIS A 251      958    998    991    -81     28    -30       C  
ATOM   1975  O   HIS A 251      36.092  56.388  37.383  1.00  8.99           O  
ANISOU 1975  O   HIS A 251     1134   1143   1139    -61     47    -35       O  
ATOM   1976  CB  HIS A 251      35.877  53.568  35.790  1.00  7.92           C  
ANISOU 1976  CB  HIS A 251      949   1036   1025    -91     36    -14       C  
ATOM   1977  CG  HIS A 251      36.362  52.175  35.518  1.00  7.85           C  
ANISOU 1977  CG  HIS A 251      939   1035   1010   -101     36    -15       C  
ATOM   1978  CD2 HIS A 251      37.615  51.680  35.414  1.00  7.47           C  
ANISOU 1978  CD2 HIS A 251      899    995    945   -106     32    -24       C  
ATOM   1979  ND1 HIS A 251      35.520  51.108  35.298  1.00  7.51           N  
ANISOU 1979  ND1 HIS A 251      880    987    986   -107     42     -5       N  
ATOM   1980  CE1 HIS A 251      36.234  50.013  35.075  1.00  7.99           C  
ANISOU 1980  CE1 HIS A 251      951   1051   1035   -114     44     -9       C  
ATOM   1981  NE2 HIS A 251      37.513  50.328  35.141  1.00  8.11           N  
ANISOU 1981  NE2 HIS A 251      978   1075   1029   -111     40    -20       N  
ATOM   1982  N   PHE A 252      36.384  56.689  35.162  1.00  7.96           N  
ANISOU 1982  N   PHE A 252      978   1018   1028    -94     13    -24       N  
ATOM   1983  CA  PHE A 252      35.982  58.089  35.210  1.00  8.30           C  
ANISOU 1983  CA  PHE A 252     1032   1041   1080    -84     15    -23       C  
ATOM   1984  C   PHE A 252      35.192  58.450  33.964  1.00  7.92           C  
ANISOU 1984  C   PHE A 252      970    986   1052    -88     -1     -3       C  
ATOM   1985  O   PHE A 252      35.777  58.608  32.888  1.00  8.63           O  
ANISOU 1985  O   PHE A 252     1072   1077   1131   -106    -18      0       O  
ATOM   1986  CB  PHE A 252      37.187  59.023  35.342  1.00  8.94           C  
ANISOU 1986  CB  PHE A 252     1136   1111   1148    -97      6    -40       C  
ATOM   1987  CG  PHE A 252      36.808  60.472  35.444  1.00  8.72           C  
ANISOU 1987  CG  PHE A 252     1128   1056   1129    -88     10    -41       C  
ATOM   1988  CD1 PHE A 252      36.381  61.006  36.653  1.00  9.06           C  
ANISOU 1988  CD1 PHE A 252     1197   1081   1166    -65     29    -52       C  
ATOM   1989  CD2 PHE A 252      36.859  61.306  34.336  1.00  9.70           C  
ANISOU 1989  CD2 PHE A 252     1255   1167   1265    -98      2    -29       C  
ATOM   1990  CE1 PHE A 252      36.034  62.338  36.753  1.00 10.27           C  
ANISOU 1990  CE1 PHE A 252     1374   1201   1328    -53     39    -54       C  
ATOM   1991  CE2 PHE A 252      36.509  62.635  34.435  1.00 10.64           C  
ANISOU 1991  CE2 PHE A 252     1394   1254   1394    -87      9    -28       C  
ATOM   1992  CZ  PHE A 252      36.096  63.147  35.641  1.00 10.27           C  
ANISOU 1992  CZ  PHE A 252     1368   1188   1345    -65     27    -41       C  
ATOM   1993  N   TYR A 253      33.890  58.634  34.135  1.00  8.26           N  
ANISOU 1993  N   TYR A 253      992   1019   1127    -67      6     14       N  
ATOM   1994  CA  TYR A 253      32.992  59.035  33.062  1.00  8.74           C  
ANISOU 1994  CA  TYR A 253     1035   1070   1214    -66    -22     38       C  
ATOM   1995  C   TYR A 253      32.249  60.325  33.401  1.00  8.91           C  
ANISOU 1995  C   TYR A 253     1053   1066   1265    -37     -7     50       C  
ATOM   1996  O   TYR A 253      31.303  60.704  32.690  1.00  9.77           O  
ANISOU 1996  O   TYR A 253     1138   1163   1410    -27    -31     76       O  
ATOM   1997  CB  TYR A 253      31.978  57.941  32.778  1.00  9.97           C  
ANISOU 1997  CB  TYR A 253     1151   1234   1403    -69    -38     54       C  
ATOM   1998  CG  TYR A 253      32.517  56.671  32.157  1.00  9.16           C  
ANISOU 1998  CG  TYR A 253     1058   1149   1274    -97    -59     45       C  
ATOM   1999  CD1 TYR A 253      32.821  56.636  30.804  1.00  9.76           C  
ANISOU 1999  CD1 TYR A 253     1161   1224   1325   -117    -98     47       C  
ATOM   2000  CD2 TYR A 253      32.668  55.506  32.901  1.00  8.68           C  
ANISOU 2000  CD2 TYR A 253      987   1099   1212   -100    -36     35       C  
ATOM   2001  CE1 TYR A 253      33.246  55.471  30.200  1.00  9.99           C  
ANISOU 2001  CE1 TYR A 253     1208   1261   1327   -139   -111     37       C  
ATOM   2002  CE2 TYR A 253      33.114  54.339  32.304  1.00  9.03           C  
ANISOU 2002  CE2 TYR A 253     1042   1152   1236   -123    -51     27       C  
ATOM   2003  CZ  TYR A 253      33.393  54.322  30.950  1.00  8.40           C  
ANISOU 2003  CZ  TYR A 253      991   1069   1131   -142    -87     27       C  
ATOM   2004  OH  TYR A 253      33.753  53.180  30.277  1.00  9.38           O  
ANISOU 2004  OH  TYR A 253     1138   1195   1232   -163    -99     18       O  
ATOM   2005  N   ASP A 254      32.643  61.024  34.459  1.00  9.18           N  
ANISOU 2005  N   ASP A 254     1114   1086   1287    -23     28     33       N  
ATOM   2006  CA  ASP A 254      31.828  62.135  34.928  1.00  9.01           C  
ANISOU 2006  CA  ASP A 254     1095   1034   1296     11     56     43       C  
ATOM   2007  C   ASP A 254      31.760  63.237  33.872  1.00  9.50           C  
ANISOU 2007  C   ASP A 254     1164   1076   1368     11     28     59       C  
ATOM   2008  O   ASP A 254      32.801  63.631  33.337  1.00  9.63           O  
ANISOU 2008  O   ASP A 254     1216   1093   1352    -13     11     47       O  
ATOM   2009  CB  ASP A 254      32.423  62.767  36.188  1.00  9.49           C  
ANISOU 2009  CB  ASP A 254     1206   1075   1326     22     92     14       C  
ATOM   2010  CG  ASP A 254      32.415  61.863  37.398  1.00  9.72           C  
ANISOU 2010  CG  ASP A 254     1245   1114   1335     32    125      1       C  
ATOM   2011  OD1 ASP A 254      31.830  60.753  37.358  1.00 11.15           O  
ANISOU 2011  OD1 ASP A 254     1387   1314   1537     32    131     17       O  
ATOM   2012  OD2 ASP A 254      32.996  62.313  38.441  1.00 10.38           O1-
ANISOU 2012  OD2 ASP A 254     1385   1181   1380     39    143    -25       O1-
ATOM   2013  N   PRO A 255      30.579  63.809  33.596  1.00 10.17           N  
ANISOU 2013  N   PRO A 255     1220   1140   1503     41     28     89       N  
ATOM   2014  CA  PRO A 255      29.243  63.407  34.061  1.00 10.76           C  
ANISOU 2014  CA  PRO A 255     1239   1210   1640     70     50    112       C  
ATOM   2015  C   PRO A 255      28.660  62.395  33.076  1.00 10.29           C  
ANISOU 2015  C   PRO A 255     1128   1173   1608     51     -5    135       C  
ATOM   2016  O   PRO A 255      28.571  62.702  31.871  1.00 11.02           O  
ANISOU 2016  O   PRO A 255     1223   1263   1700     42    -63    152       O  
ATOM   2017  CB  PRO A 255      28.464  64.722  34.057  1.00 10.46           C  
ANISOU 2017  CB  PRO A 255     1195   1132   1647    110     69    135       C  
ATOM   2018  CG  PRO A 255      29.109  65.539  32.965  1.00 11.92           C  
ANISOU 2018  CG  PRO A 255     1418   1310   1802     94     23    138       C  
ATOM   2019  CD  PRO A 255      30.510  65.016  32.750  1.00 10.64           C  
ANISOU 2019  CD  PRO A 255     1298   1173   1570     49      6    107       C  
ATOM   2020  N   ILE A 256      28.267  61.211  33.553  1.00 10.39           N  
ANISOU 2020  N   ILE A 256     1104   1202   1642     44      9    135       N  
ATOM   2021  CA  ILE A 256      27.839  60.147  32.652  1.00 10.60           C  
ANISOU 2021  CA  ILE A 256     1092   1246   1690     17    -49    148       C  
ATOM   2022  C   ILE A 256      26.652  60.557  31.795  1.00 12.60           C  
ANISOU 2022  C   ILE A 256     1293   1483   2013     30   -102    187       C  
ATOM   2023  O   ILE A 256      26.515  60.087  30.658  1.00 12.42           O  
ANISOU 2023  O   ILE A 256     1266   1467   1984      4   -179    196       O  
ATOM   2024  CB  ILE A 256      27.586  58.846  33.441  1.00 11.62           C  
ANISOU 2024  CB  ILE A 256     1190   1387   1838      9    -15    143       C  
ATOM   2025  CG1 ILE A 256      27.316  57.667  32.505  1.00 11.83           C  
ANISOU 2025  CG1 ILE A 256     1189   1427   1877    -27    -79    149       C  
ATOM   2026  CG2 ILE A 256      26.449  59.016  34.425  1.00 12.83           C  
ANISOU 2026  CG2 ILE A 256     1290   1518   2068     45     47    166       C  
ATOM   2027  CD1 ILE A 256      28.497  57.243  31.671  1.00 11.88           C  
ANISOU 2027  CD1 ILE A 256     1258   1452   1803    -61   -118    123       C  
ATOM   2028  N   ASP A 257      25.762  61.414  32.299  1.00 12.10           N  
ANISOU 2028  N   ASP A 257     1189   1392   2016     72    -67    212       N  
ATOM   2029  CA  ASP A 257      24.650  61.833  31.455  1.00 14.85           C  
ANISOU 2029  CA  ASP A 257     1479   1722   2439     87   -127    254       C  
ATOM   2030  C   ASP A 257      25.145  62.483  30.169  1.00 13.26           C  
ANISOU 2030  C   ASP A 257     1333   1521   2184     75   -202    257       C  
ATOM   2031  O   ASP A 257      24.499  62.347  29.123  1.00 16.33           O  
ANISOU 2031  O   ASP A 257     1696   1906   2602     68   -289    284       O  
ATOM   2032  CB  ASP A 257      23.733  62.799  32.213  1.00 21.12           C  
ANISOU 2032  CB  ASP A 257     2227   2481   3314    142    -65    281       C  
ATOM   2033  CG  ASP A 257      22.861  62.096  33.241  1.00 18.06           C  
ANISOU 2033  CG  ASP A 257     1767   2086   3008    158      4    294       C  
ATOM   2034  OD1 ASP A 257      22.896  60.846  33.321  1.00 21.23           O  
ANISOU 2034  OD1 ASP A 257     2148   2508   3408    124     -6    285       O  
ATOM   2035  OD2 ASP A 257      22.141  62.802  33.981  1.00 22.87           O1-
ANISOU 2035  OD2 ASP A 257     2344   2663   3683    206     76    316       O1-
ATOM   2036  N   TYR A 258      26.269  63.194  30.231  1.00 12.36           N  
ANISOU 2036  N   TYR A 258     1298   1406   1994     73   -173    233       N  
ATOM   2037  CA  TYR A 258      26.870  63.791  29.038  1.00 12.79           C  
ANISOU 2037  CA  TYR A 258     1415   1456   1990     60   -227    237       C  
ATOM   2038  C   TYR A 258      27.703  62.768  28.257  1.00 11.67           C  
ANISOU 2038  C   TYR A 258     1319   1341   1775     14   -266    215       C  
ATOM   2039  O   TYR A 258      27.554  62.620  27.034  1.00 12.48           O  
ANISOU 2039  O   TYR A 258     1447   1441   1853      0   -339    231       O  
ATOM   2040  CB  TYR A 258      27.733  65.012  29.416  1.00 12.47           C  
ANISOU 2040  CB  TYR A 258     1433   1394   1909     74   -173    222       C  
ATOM   2041  CG  TYR A 258      28.531  65.507  28.225  1.00 12.19           C  
ANISOU 2041  CG  TYR A 258     1470   1354   1809     55   -211    226       C  
ATOM   2042  CD1 TYR A 258      27.891  66.068  27.132  1.00 12.49           C  
ANISOU 2042  CD1 TYR A 258     1515   1371   1858     71   -275    265       C  
ATOM   2043  CD2 TYR A 258      29.911  65.370  28.170  1.00 11.43           C  
ANISOU 2043  CD2 TYR A 258     1431   1268   1643     23   -184    194       C  
ATOM   2044  CE1 TYR A 258      28.598  66.469  26.021  1.00 12.88           C  
ANISOU 2044  CE1 TYR A 258     1642   1411   1840     55   -303    272       C  
ATOM   2045  CE2 TYR A 258      30.632  65.787  27.063  1.00 12.26           C  
ANISOU 2045  CE2 TYR A 258     1601   1362   1693      6   -204    202       C  
ATOM   2046  CZ  TYR A 258      29.966  66.327  25.984  1.00 11.99           C  
ANISOU 2046  CZ  TYR A 258     1587   1308   1661     23   -261    241       C  
ATOM   2047  OH  TYR A 258      30.681  66.719  24.876  1.00 13.17           O  
ANISOU 2047  OH  TYR A 258     1814   1442   1748      9   -273    251       O  
ATOM   2048  N   THR A 259      28.581  62.038  28.941  1.00 10.80           N  
ANISOU 2048  N   THR A 259     1224   1252   1627     -7   -218    180       N  
ATOM   2049  CA  THR A 259      29.544  61.224  28.209  1.00 10.24           C  
ANISOU 2049  CA  THR A 259     1204   1199   1486    -44   -239    159       C  
ATOM   2050  C   THR A 259      28.895  60.036  27.516  1.00 11.59           C  
ANISOU 2050  C   THR A 259     1357   1380   1668    -66   -302    166       C  
ATOM   2051  O   THR A 259      29.380  59.626  26.458  1.00 11.65           O  
ANISOU 2051  O   THR A 259     1421   1389   1616    -90   -341    160       O  
ATOM   2052  CB  THR A 259      30.692  60.782  29.117  1.00 10.20           C  
ANISOU 2052  CB  THR A 259     1218   1211   1446    -58   -176    124       C  
ATOM   2053  CG2 THR A 259      31.505  61.970  29.601  1.00 11.52           C  
ANISOU 2053  CG2 THR A 259     1418   1365   1596    -48   -132    113       C  
ATOM   2054  OG1 THR A 259      30.145  60.064  30.226  1.00 10.04           O  
ANISOU 2054  OG1 THR A 259     1146   1201   1468    -50   -146    118       O  
ATOM   2055  N   GLU A 260      27.826  59.464  28.071  1.00 11.35           N  
ANISOU 2055  N   GLU A 260     1251   1350   1711    -60   -309    178       N  
ATOM   2056  CA  GLU A 260      27.120  58.386  27.397  1.00 12.11           C  
ANISOU 2056  CA  GLU A 260     1323   1449   1830    -86   -380    185       C  
ATOM   2057  C   GLU A 260      25.841  58.858  26.706  1.00 13.75           C  
ANISOU 2057  C   GLU A 260     1485   1636   2104    -73   -462    224       C  
ATOM   2058  O   GLU A 260      25.273  58.109  25.907  1.00 15.93           O  
ANISOU 2058  O   GLU A 260     1753   1907   2392    -99   -546    231       O  
ATOM   2059  CB  GLU A 260      26.809  57.236  28.363  1.00 12.85           C  
ANISOU 2059  CB  GLU A 260     1360   1553   1970    -97   -341    174       C  
ATOM   2060  CG  GLU A 260      26.274  56.004  27.651  1.00 15.16           C  
ANISOU 2060  CG  GLU A 260     1638   1842   2278   -133   -412    173       C  
ATOM   2061  CD  GLU A 260      26.447  54.728  28.439  1.00 41.36           C  
ANISOU 2061  CD  GLU A 260     4936   5169   5608   -153   -365    153       C  
ATOM   2062  OE1 GLU A 260      26.227  54.760  29.654  1.00 19.50           O  
ANISOU 2062  OE1 GLU A 260     2121   2403   2886   -132   -291    158       O  
ATOM   2063  OE2 GLU A 260      26.808  53.695  27.837  1.00 32.71           O1-
ANISOU 2063  OE2 GLU A 260     3881   4075   4472   -186   -398    133       O1-
ATOM   2064  N   ASN A 261      25.374  60.066  26.992  1.00 16.30           N  
ANISOU 2064  N   ASN A 261     1779   1943   2472    -34   -444    250       N  
ATOM   2065  CA  ASN A 261      24.286  60.690  26.230  1.00 16.58           C  
ANISOU 2065  CA  ASN A 261     1777   1956   2566    -14   -528    293       C  
ATOM   2066  C   ASN A 261      22.987  59.887  26.303  1.00 23.22           C  
ANISOU 2066  C   ASN A 261     2516   2791   3516    -24   -582    316       C  
ATOM   2067  O   ASN A 261      22.275  59.748  25.307  1.00 22.90           O  
ANISOU 2067  O   ASN A 261     2462   2739   3502    -35   -694    340       O  
ATOM   2068  CB  ASN A 261      24.697  60.918  24.771  1.00 16.31           C  
ANISOU 2068  CB  ASN A 261     1836   1915   2446    -30   -614    297       C  
ATOM   2069  CG  ASN A 261      23.753  61.849  24.030  1.00 18.69           C  
ANISOU 2069  CG  ASN A 261     2118   2190   2794      0   -697    344       C  
ATOM   2070  ND2 ASN A 261      23.530  61.571  22.745  1.00 25.83           N  
ANISOU 2070  ND2 ASN A 261     3073   3085   3655    -20   -811    356       N  
ATOM   2071  OD1 ASN A 261      23.231  62.803  24.602  1.00 18.63           O  
ANISOU 2071  OD1 ASN A 261     2055   2167   2857     42   -660    371       O  
ATOM   2072  N   ALA A 262      22.652  59.379  27.492  1.00 30.37           N  
ANISOU 2072  N   ALA A 262     3349   3701   4490    -18   -503    312       N  
ATOM   2073  CA  ALA A 262      21.531  58.448  27.620  1.00 31.27           C  
ANISOU 2073  CA  ALA A 262     3362   3806   4712    -36   -540    331       C  
ATOM   2074  C   ALA A 262      20.237  59.026  27.053  1.00 31.33           C  
ANISOU 2074  C   ALA A 262     3286   3788   4829    -15   -625    383       C  
ATOM   2075  O   ALA A 262      19.620  58.436  26.159  1.00 46.64           O  
ANISOU 2075  O   ALA A 262     5231   5718   6773    -48   -714    383       O  
ATOM   2076  CB  ALA A 262      21.345  58.040  29.086  1.00 40.65           C  
ANISOU 2076  CB  ALA A 262     4491   4995   5959    -22   -420    327       C  
ATOM   2077  N   ASP A 263      19.796  60.167  27.575  1.00 23.67           N  
ANISOU 2077  N   ASP A 263     2273   2801   3920     39   -571    412       N  
ATOM   2078  CA  ASP A 263      18.510  60.738  27.185  1.00 24.14           C  
ANISOU 2078  CA  ASP A 263     2276   2832   4063     59   -609    450       C  
ATOM   2079  C   ASP A 263      18.618  61.714  26.016  1.00 22.39           C  
ANISOU 2079  C   ASP A 263     2115   2601   3789     74   -701    467       C  
ATOM   2080  O   ASP A 263      17.645  62.415  25.721  1.00 22.87           O  
ANISOU 2080  O   ASP A 263     2133   2639   3918    100   -729    500       O  
ATOM   2081  CB  ASP A 263      17.833  61.412  28.380  1.00 33.94           C  
ANISOU 2081  CB  ASP A 263     3443   4051   5402    110   -491    474       C  
ATOM   2082  CG  ASP A 263      16.312  61.392  28.278  1.00 41.97           C  
ANISOU 2082  CG  ASP A 263     4371   5039   6535    114   -511    509       C  
ATOM   2083  OD1 ASP A 263      15.765  60.482  27.614  1.00 33.76           O  
ANISOU 2083  OD1 ASP A 263     3311   3997   5518     69   -595    508       O  
ATOM   2084  OD2 ASP A 263      15.664  62.291  28.854  1.00 33.48           O1-
ANISOU 2084  OD2 ASP A 263     3249   3940   5533    161   -442    538       O1-
ATOM   2085  N   ASN A 264      19.770  61.761  25.347  1.00 22.34           N  
ANISOU 2085  N   ASN A 264     2213   2611   3664     58   -746    446       N  
ATOM   2086  CA  ASN A 264      19.982  62.574  24.148  1.00 21.12           C  
ANISOU 2086  CA  ASN A 264     2143   2446   3438     67   -829    461       C  
ATOM   2087  C   ASN A 264      19.518  64.018  24.341  1.00 20.99           C  
ANISOU 2087  C   ASN A 264     2099   2402   3474    128   -798    499       C  
ATOM   2088  O   ASN A 264      18.857  64.604  23.480  1.00 23.12           O  
ANISOU 2088  O   ASN A 264     2376   2654   3754    140   -870    525       O  
ATOM   2089  CB  ASN A 264      19.327  61.937  22.916  1.00 30.13           C  
ANISOU 2089  CB  ASN A 264     3308   3579   4559     28   -947    459       C  
ATOM   2090  CG  ASN A 264      19.916  62.447  21.615  1.00 25.09           C  
ANISOU 2090  CG  ASN A 264     2796   2935   3801     26  -1025    459       C  
ATOM   2091  ND2 ASN A 264      19.071  62.573  20.595  1.00 38.16           N  
ANISOU 2091  ND2 ASN A 264     4461   4571   5465     21  -1120    477       N  
ATOM   2092  OD1 ASN A 264      21.108  62.735  21.525  1.00 38.29           O  
ANISOU 2092  OD1 ASN A 264     4560   4615   5375     28   -996    446       O  
ATOM   2093  N   ILE A 265      19.887  64.604  25.476  1.00 22.23           N  
ANISOU 2093  N   ILE A 265     2232   2553   3661    167   -686    500       N  
ATOM   2094  CA  ILE A 265      19.530  65.980  25.774  1.00 24.18           C  
ANISOU 2094  CA  ILE A 265     2463   2768   3956    227   -638    532       C  
ATOM   2095  C   ILE A 265      20.734  66.865  26.102  1.00 18.85           C  
ANISOU 2095  C   ILE A 265     1895   2088   3179    239   -551    502       C  
ATOM   2096  O   ILE A 265      20.618  68.092  25.988  1.00 21.03           O  
ANISOU 2096  O   ILE A 265     2191   2331   3468    283   -537    529       O  
ATOM   2097  CB  ILE A 265      18.487  66.069  26.906  1.00 30.43           C  
ANISOU 2097  CB  ILE A 265     3146   3545   4871    257   -544    544       C  
ATOM   2098  CG1 ILE A 265      19.012  65.325  28.134  1.00 29.24           C  
ANISOU 2098  CG1 ILE A 265     2977   3409   4724    249   -440    513       C  
ATOM   2099  CG2 ILE A 265      17.148  65.507  26.445  1.00 34.65           C  
ANISOU 2099  CG2 ILE A 265     3599   4078   5489    235   -612    564       C  
ATOM   2100  CD1 ILE A 265      18.112  65.397  29.337  1.00 45.10           C  
ANISOU 2100  CD1 ILE A 265     4906   5399   6832    280   -326    522       C  
ATOM   2101  N   TYR A 266      21.863  66.303  26.517  1.00 17.33           N  
ANISOU 2101  N   TYR A 266     1769   1923   2893    200   -491    449       N  
ATOM   2102  CA  TYR A 266      23.026  67.102  26.915  1.00 15.43           C  
ANISOU 2102  CA  TYR A 266     1619   1675   2568    204   -408    418       C  
ATOM   2103  C   TYR A 266      24.071  66.978  25.816  1.00 15.08           C  
ANISOU 2103  C   TYR A 266     1680   1645   2406    165   -460    401       C  
ATOM   2104  O   TYR A 266      24.764  65.964  25.720  1.00 16.90           O  
ANISOU 2104  O   TYR A 266     1941   1905   2574    121   -461    367       O  
ATOM   2105  CB  TYR A 266      23.589  66.611  28.240  1.00 15.64           C  
ANISOU 2105  CB  TYR A 266     1644   1719   2581    192   -303    373       C  
ATOM   2106  CG  TYR A 266      22.592  66.615  29.367  1.00 17.24           C  
ANISOU 2106  CG  TYR A 266     1756   1906   2890    231   -234    389       C  
ATOM   2107  CD1 TYR A 266      21.828  67.737  29.646  1.00 19.27           C  
ANISOU 2107  CD1 TYR A 266     1978   2120   3222    289   -201    424       C  
ATOM   2108  CD2 TYR A 266      22.415  65.488  30.155  1.00 23.06           C  
ANISOU 2108  CD2 TYR A 266     2446   2664   3653    213   -194    371       C  
ATOM   2109  CE1 TYR A 266      20.914  67.738  30.683  1.00 21.71           C  
ANISOU 2109  CE1 TYR A 266     2209   2409   3632    329   -122    440       C  
ATOM   2110  CE2 TYR A 266      21.505  65.477  31.192  1.00 30.45           C  
ANISOU 2110  CE2 TYR A 266     3305   3580   4685    250   -117    389       C  
ATOM   2111  CZ  TYR A 266      20.758  66.605  31.452  1.00 25.34           C  
ANISOU 2111  CZ  TYR A 266     2625   2890   4114    309    -78    423       C  
ATOM   2112  OH  TYR A 266      19.853  66.592  32.488  1.00 30.39           O  
ANISOU 2112  OH  TYR A 266     3192   3504   4852    351     14    443       O  
ATOM   2113  N   SER A 267      24.205  68.030  25.010  1.00 15.28           N  
ANISOU 2113  N   SER A 267     1765   1642   2400    185   -491    428       N  
ATOM   2114  CA  SER A 267      25.088  68.015  23.855  1.00 15.61           C  
ANISOU 2114  CA  SER A 267     1912   1686   2333    155   -535    422       C  
ATOM   2115  C   SER A 267      26.321  68.894  24.019  1.00 13.99           C  
ANISOU 2115  C   SER A 267     1791   1465   2061    151   -453    401       C  
ATOM   2116  O   SER A 267      27.167  68.911  23.121  1.00 15.08           O  
ANISOU 2116  O   SER A 267     2017   1601   2111    126   -467    397       O  
ATOM   2117  CB  SER A 267      24.321  68.455  22.602  1.00 17.60           C  
ANISOU 2117  CB  SER A 267     2185   1914   2588    177   -646    474       C  
ATOM   2118  OG  SER A 267      23.772  69.756  22.777  1.00 17.08           O  
ANISOU 2118  OG  SER A 267     2098   1808   2583    230   -631    513       O  
ATOM   2119  N   GLN A 268      26.447  69.620  25.127  1.00 13.62           N  
ANISOU 2119  N   GLN A 268     1721   1402   2054    173   -368    388       N  
ATOM   2120  CA  GLN A 268      27.578  70.519  25.357  1.00 13.57           C  
ANISOU 2120  CA  GLN A 268     1786   1372   1998    165   -298    367       C  
ATOM   2121  C   GLN A 268      28.128  70.311  26.762  1.00 11.96           C  
ANISOU 2121  C   GLN A 268     1560   1180   1805    153   -213    319       C  
ATOM   2122  O   GLN A 268      27.475  69.716  27.626  1.00 13.91           O  
ANISOU 2122  O   GLN A 268     1739   1443   2103    165   -196    311       O  
ATOM   2123  CB  GLN A 268      27.172  71.984  25.128  1.00 14.04           C  
ANISOU 2123  CB  GLN A 268     1867   1378   2088    210   -292    405       C  
ATOM   2124  CG  GLN A 268      26.528  72.183  23.769  1.00 14.91           C  
ANISOU 2124  CG  GLN A 268     2002   1474   2189    228   -388    458       C  
ATOM   2125  CD  GLN A 268      26.317  73.643  23.391  1.00 15.48           C  
ANISOU 2125  CD  GLN A 268     2115   1490   2276    271   -383    500       C  
ATOM   2126  NE2 GLN A 268      25.871  73.860  22.168  1.00 15.08           N  
ANISOU 2126  NE2 GLN A 268     2102   1423   2203    287   -469    548       N  
ATOM   2127  OE1 GLN A 268      26.546  74.559  24.191  1.00 16.60           O  
ANISOU 2127  OE1 GLN A 268     2262   1598   2447    289   -306    488       O  
ATOM   2128  N   TRP A 269      29.358  70.782  26.976  1.00 11.61           N  
ANISOU 2128  N   TRP A 269     1576   1125   1711    127   -162    290       N  
ATOM   2129  CA  TRP A 269      30.081  70.545  28.214  1.00 11.20           C  
ANISOU 2129  CA  TRP A 269     1519   1084   1653    108    -99    242       C  
ATOM   2130  C   TRP A 269      31.082  71.665  28.451  1.00 10.66           C  
ANISOU 2130  C   TRP A 269     1511    977   1563     96    -53    224       C  
ATOM   2131  O   TRP A 269      31.639  72.226  27.507  1.00 11.91           O  
ANISOU 2131  O   TRP A 269     1720   1114   1692     82    -63    241       O  
ATOM   2132  CB  TRP A 269      30.843  69.206  28.145  1.00 10.75           C  
ANISOU 2132  CB  TRP A 269     1458   1075   1551     63   -109    213       C  
ATOM   2133  CG  TRP A 269      31.565  68.856  29.392  1.00 10.69           C  
ANISOU 2133  CG  TRP A 269     1444   1081   1535     46    -59    168       C  
ATOM   2134  CD1 TRP A 269      31.035  68.219  30.477  1.00  9.58           C  
ANISOU 2134  CD1 TRP A 269     1260    957   1422     59    -38    152       C  
ATOM   2135  CD2 TRP A 269      32.947  69.111  29.703  1.00 10.25           C  
ANISOU 2135  CD2 TRP A 269     1429   1020   1446     11    -28    135       C  
ATOM   2136  CE2 TRP A 269      33.173  68.618  31.006  1.00 10.28           C  
ANISOU 2136  CE2 TRP A 269     1415   1039   1452      7      0    100       C  
ATOM   2137  CE3 TRP A 269      34.014  69.695  29.011  1.00 10.55           C  
ANISOU 2137  CE3 TRP A 269     1514   1038   1456    -17    -21    136       C  
ATOM   2138  NE1 TRP A 269      31.997  68.076  31.447  1.00 10.27           N  
ANISOU 2138  NE1 TRP A 269     1369   1051   1483     38     -1    111       N  
ATOM   2139  CZ2 TRP A 269      34.420  68.682  31.626  1.00 10.40           C  
ANISOU 2139  CZ2 TRP A 269     1455   1052   1444    -25     19     64       C  
ATOM   2140  CZ3 TRP A 269      35.244  69.759  29.635  1.00 11.52           C  
ANISOU 2140  CZ3 TRP A 269     1650   1159   1568    -51      7    101       C  
ATOM   2141  CH2 TRP A 269      35.438  69.248  30.925  1.00 11.14           C  
ANISOU 2141  CH2 TRP A 269     1580   1128   1524    -55     20     65       C  
ATOM   2142  N   GLY A 270      31.311  71.982  29.718  1.00 11.84           N  
ANISOU 2142  N   GLY A 270     1659   1111   1726    100     -3    190       N  
ATOM   2143  CA  GLY A 270      32.367  72.897  30.093  1.00 11.21           C  
ANISOU 2143  CA  GLY A 270     1635    996   1630     77     34    163       C  
ATOM   2144  C   GLY A 270      31.936  74.347  30.152  1.00 12.09           C  
ANISOU 2144  C   GLY A 270     1779   1043   1771    111     58    180       C  
ATOM   2145  O   GLY A 270      30.763  74.694  30.026  1.00 12.74           O  
ANISOU 2145  O   GLY A 270     1838   1107   1894    161     53    214       O  
ATOM   2146  N   HIS A 271      32.935  75.217  30.315  1.00 11.55           N  
ANISOU 2146  N   HIS A 271     1763    934   1689     83     84    158       N  
ATOM   2147  CA  HIS A 271      32.670  76.620  30.618  1.00 14.40           C  
ANISOU 2147  CA  HIS A 271     2167   1225   2078    111    117    163       C  
ATOM   2148  C   HIS A 271      31.845  77.308  29.541  1.00 11.74           C  
ANISOU 2148  C   HIS A 271     1837    860   1765    152     99    222       C  
ATOM   2149  O   HIS A 271      31.101  78.249  29.847  1.00 15.07           O  
ANISOU 2149  O   HIS A 271     2271   1230   2225    199    124    237       O  
ATOM   2150  CB  HIS A 271      33.966  77.444  30.712  1.00 21.22           C  
ANISOU 2150  CB  HIS A 271     3087   2045   2928     63    137    135       C  
ATOM   2151  CG  HIS A 271      34.941  76.981  31.744  1.00 28.02           C  
ANISOU 2151  CG  HIS A 271     3951   2924   3772     18    142     78       C  
ATOM   2152  CD2 HIS A 271      36.288  76.846  31.686  1.00 29.65           C  
ANISOU 2152  CD2 HIS A 271     4165   3135   3967    -43    134     54       C  
ATOM   2153  ND1 HIS A 271      34.576  76.644  33.028  1.00 28.46           N  
ANISOU 2153  ND1 HIS A 271     4003   2987   3823     36    154     42       N  
ATOM   2154  CE1 HIS A 271      35.654  76.298  33.710  1.00 24.74           C  
ANISOU 2154  CE1 HIS A 271     3542   2527   3331    -12    143     -3       C  
ATOM   2155  NE2 HIS A 271      36.705  76.409  32.919  1.00 34.25           N  
ANISOU 2155  NE2 HIS A 271     4745   3731   4537    -61    129      4       N  
ATOM   2156  N   THR A 272      32.019  76.930  28.280  1.00 12.48           N  
ANISOU 2156  N   THR A 272     1933    977   1832    136     59    256       N  
ATOM   2157  CA  THR A 272      31.355  77.645  27.196  1.00 12.56           C  
ANISOU 2157  CA  THR A 272     1966    954   1853    173     33    314       C  
ATOM   2158  C   THR A 272      29.993  77.061  26.846  1.00 13.77           C  
ANISOU 2158  C   THR A 272     2060   1136   2035    220    -20    353       C  
ATOM   2159  O   THR A 272      29.298  77.618  25.991  1.00 16.09           O  
ANISOU 2159  O   THR A 272     2366   1403   2344    257    -56    405       O  
ATOM   2160  CB  THR A 272      32.222  77.707  25.924  1.00 13.09           C  
ANISOU 2160  CB  THR A 272     2087   1017   1868    137     19    337       C  
ATOM   2161  CG2 THR A 272      33.662  78.029  26.262  1.00 15.67           C  
ANISOU 2161  CG2 THR A 272     2450   1325   2180     80     69    299       C  
ATOM   2162  OG1 THR A 272      32.137  76.468  25.213  1.00 13.56           O  
ANISOU 2162  OG1 THR A 272     2125   1136   1890    123    -30    346       O  
ATOM   2163  N   ALA A 273      29.589  75.979  27.499  1.00 13.41           N  
ANISOU 2163  N   ALA A 273     1951   1141   2005    218    -28    330       N  
ATOM   2164  CA  ALA A 273      28.349  75.309  27.144  1.00 14.46           C  
ANISOU 2164  CA  ALA A 273     2017   1302   2176    252    -84    366       C  
ATOM   2165  C   ALA A 273      27.133  76.167  27.447  1.00 16.52           C  
ANISOU 2165  C   ALA A 273     2243   1518   2517    320    -73    403       C  
ATOM   2166  O   ALA A 273      27.091  76.888  28.444  1.00 17.59           O  
ANISOU 2166  O   ALA A 273     2387   1614   2682    343     -3    383       O  
ATOM   2167  CB  ALA A 273      28.246  74.003  27.926  1.00 15.84           C  
ANISOU 2167  CB  ALA A 273     2132   1530   2356    233    -78    332       C  
ATOM   2168  N   ASP A 274      26.135  76.060  26.589  1.00 16.23           N  
ANISOU 2168  N   ASP A 274     2167   1484   2516    352   -144    457       N  
ATOM   2169  CA  ASP A 274      24.838  76.670  26.860  1.00 17.81           C  
ANISOU 2169  CA  ASP A 274     2306   1647   2812    421   -140    499       C  
ATOM   2170  C   ASP A 274      24.214  75.965  28.055  1.00 17.92           C  
ANISOU 2170  C   ASP A 274     2238   1683   2888    435    -92    476       C  
ATOM   2171  O   ASP A 274      24.146  74.729  28.067  1.00 17.00           O  
ANISOU 2171  O   ASP A 274     2075   1620   2764    404   -125    462       O  
ATOM   2172  CB  ASP A 274      23.950  76.498  25.625  1.00 21.27           C  
ANISOU 2172  CB  ASP A 274     2712   2093   3278    445   -249    561       C  
ATOM   2173  CG  ASP A 274      22.594  77.166  25.768  1.00 30.26           C  
ANISOU 2173  CG  ASP A 274     3776   3189   4531    520   -257    616       C  
ATOM   2174  OD1 ASP A 274      22.049  77.207  26.891  1.00 34.07           O  
ANISOU 2174  OD1 ASP A 274     4197   3660   5088    552   -182    604       O  
ATOM   2175  OD2 ASP A 274      22.068  77.651  24.746  1.00 41.35           O1-
ANISOU 2175  OD2 ASP A 274     5189   4572   5953    551   -336    673       O1-
ATOM   2176  N   PRO A 275      23.759  76.698  29.081  1.00 20.55           N  
ANISOU 2176  N   PRO A 275     2559   1970   3279    483     -8    472       N  
ATOM   2177  CA  PRO A 275      23.224  76.015  30.271  1.00 23.73           C  
ANISOU 2177  CA  PRO A 275     2898   2389   3730    497     54    450       C  
ATOM   2178  C   PRO A 275      22.054  75.098  29.975  1.00 20.06           C  
ANISOU 2178  C   PRO A 275     2317   1956   3350    515      1    492       C  
ATOM   2179  O   PRO A 275      21.819  74.147  30.727  1.00 25.81           O  
ANISOU 2179  O   PRO A 275     2994   2713   4099    504     35    472       O  
ATOM   2180  CB  PRO A 275      22.812  77.171  31.196  1.00 27.94           C  
ANISOU 2180  CB  PRO A 275     3452   2852   4314    558    152    451       C  
ATOM   2181  CG  PRO A 275      23.626  78.327  30.742  1.00 32.38           C  
ANISOU 2181  CG  PRO A 275     4112   3369   4821    549    151    444       C  
ATOM   2182  CD  PRO A 275      23.785  78.163  29.252  1.00 23.09           C  
ANISOU 2182  CD  PRO A 275     2938   2220   3617    525     44    483       C  
ATOM   2183  N   SER A 276      21.311  75.357  28.901  1.00 21.81           N  
ANISOU 2183  N   SER A 276     2497   2168   3623    541    -86    551       N  
ATOM   2184  CA  SER A 276      20.157  74.534  28.560  1.00 22.20           C  
ANISOU 2184  CA  SER A 276     2428   2241   3766    554   -153    594       C  
ATOM   2185  C   SER A 276      20.534  73.265  27.805  1.00 19.07           C  
ANISOU 2185  C   SER A 276     2031   1906   3309    487   -249    579       C  
ATOM   2186  O   SER A 276      19.640  72.464  27.501  1.00 22.51           O  
ANISOU 2186  O   SER A 276     2372   2362   3817    485   -315    608       O  
ATOM   2187  CB  SER A 276      19.156  75.343  27.729  1.00 24.39           C  
ANISOU 2187  CB  SER A 276     2675   2500   4094    591   -215    644       C  
ATOM   2188  OG  SER A 276      19.658  75.604  26.433  1.00 24.65           O  
ANISOU 2188  OG  SER A 276     2778   2532   4057    574   -316    665       O  
ATOM   2189  N   LEU A 277      21.821  73.066  27.498  1.00 17.76           N  
ANISOU 2189  N   LEU A 277     1965   1764   3018    432   -254    535       N  
ATOM   2190  CA  LEU A 277      22.270  71.927  26.706  1.00 16.99           C  
ANISOU 2190  CA  LEU A 277     1885   1717   2853    373   -336    520       C  
ATOM   2191  C   LEU A 277      23.332  71.102  27.420  1.00 15.92           C  
ANISOU 2191  C   LEU A 277     1786   1619   2644    321   -275    456       C  
ATOM   2192  O   LEU A 277      24.006  70.286  26.783  1.00 16.31           O  
ANISOU 2192  O   LEU A 277     1876   1704   2619    271   -323    436       O  
ATOM   2193  CB  LEU A 277      22.811  72.391  25.353  1.00 16.10           C  
ANISOU 2193  CB  LEU A 277     1863   1596   2659    358   -413    539       C  
ATOM   2194  CG  LEU A 277      21.836  73.169  24.479  1.00 19.32           C  
ANISOU 2194  CG  LEU A 277     2250   1967   3125    408   -495    606       C  
ATOM   2195  CD1 LEU A 277      22.529  73.656  23.212  1.00 19.72           C  
ANISOU 2195  CD1 LEU A 277     2416   2005   3073    393   -555    622       C  
ATOM   2196  CD2 LEU A 277      20.604  72.336  24.130  1.00 22.84           C  
ANISOU 2196  CD2 LEU A 277     2588   2431   3660    415   -594    642       C  
ATOM   2197  N   LYS A 278      23.496  71.293  28.723  1.00 16.30           N  
ANISOU 2197  N   LYS A 278     1828   1656   2708    335   -172    426       N  
ATOM   2198  CA  LYS A 278      24.547  70.613  29.471  1.00 17.01           C  
ANISOU 2198  CA  LYS A 278     1959   1776   2726    291   -119    368       C  
ATOM   2199  C   LYS A 278      23.986  70.009  30.750  1.00 15.72           C  
ANISOU 2199  C   LYS A 278     1736   1620   2619    308    -47    354       C  
ATOM   2200  O   LYS A 278      22.946  70.434  31.257  1.00 16.74           O  
ANISOU 2200  O   LYS A 278     1806   1716   2837    360     -6    384       O  
ATOM   2201  CB  LYS A 278      25.671  71.592  29.842  1.00 18.20           C  
ANISOU 2201  CB  LYS A 278     2203   1900   2812    284    -61    335       C  
ATOM   2202  CG  LYS A 278      25.204  72.708  30.760  1.00 17.21           C  
ANISOU 2202  CG  LYS A 278     2082   1720   2736    337     17    338       C  
ATOM   2203  CD  LYS A 278      26.294  73.744  30.991  1.00 21.20           C  
ANISOU 2203  CD  LYS A 278     2683   2190   3181    323     57    306       C  
ATOM   2204  CE  LYS A 278      27.532  73.120  31.618  1.00 15.80           C  
ANISOU 2204  CE  LYS A 278     2043   1536   2423    269     80    248       C  
ATOM   2205  NZ  LYS A 278      27.244  72.473  32.941  1.00 20.56           N1+
ANISOU 2205  NZ  LYS A 278     2622   2151   3038    280    137    220       N1+
ATOM   2206  N   ALA A 279      24.694  69.007  31.269  1.00 15.28           N  
ANISOU 2206  N   ALA A 279     1697   1601   2510    267    -27    313       N  
ATOM   2207  CA  ALA A 279      24.380  68.470  32.586  1.00 15.25           C  
ANISOU 2207  CA  ALA A 279     1661   1598   2534    280     53    295       C  
ATOM   2208  C   ALA A 279      24.617  69.542  33.645  1.00 15.72           C  
ANISOU 2208  C   ALA A 279     1778   1613   2580    315    144    273       C  
ATOM   2209  O   ALA A 279      25.347  70.513  33.426  1.00 16.44           O  
ANISOU 2209  O   ALA A 279     1941   1682   2625    311    142    259       O  
ATOM   2210  CB  ALA A 279      25.256  67.252  32.877  1.00 18.26           C  
ANISOU 2210  CB  ALA A 279     2066   2025   2847    229     50    254       C  
ATOM   2211  N   ASP A 280      23.999  69.363  34.812  1.00 17.54           N  
ANISOU 2211  N   ASP A 280     1986   1827   2853    349    229    271       N  
ATOM   2212  CA  ASP A 280      24.058  70.390  35.846  1.00 17.42           C  
ANISOU 2212  CA  ASP A 280     2034   1760   2826    390    321    252       C  
ATOM   2213  C   ASP A 280      25.269  70.250  36.760  1.00 17.15           C  
ANISOU 2213  C   ASP A 280     2096   1731   2688    358    353    191       C  
ATOM   2214  O   ASP A 280      25.337  70.938  37.786  1.00 19.62           O  
ANISOU 2214  O   ASP A 280     2475   2000   2979    388    428    167       O  
ATOM   2215  CB  ASP A 280      22.761  70.449  36.660  1.00 21.04           C  
ANISOU 2215  CB  ASP A 280     2433   2182   3380    452    411    283       C  
ATOM   2216  CG  ASP A 280      22.484  69.175  37.435  1.00 31.07           C  
ANISOU 2216  CG  ASP A 280     3667   3479   4658    443    455    277       C  
ATOM   2217  OD1 ASP A 280      23.372  68.306  37.527  1.00 25.22           O  
ANISOU 2217  OD1 ASP A 280     2961   2781   3839    392    423    242       O  
ATOM   2218  OD2 ASP A 280      21.359  69.044  37.961  1.00 46.58           O1-
ANISOU 2218  OD2 ASP A 280     5565   5417   6715    489    528    311       O1-
ATOM   2219  N   TRP A 281      26.231  69.402  36.402  1.00 15.34           N  
ANISOU 2219  N   TRP A 281     1881   1553   2396    300    294    167       N  
ATOM   2220  CA  TRP A 281      27.439  69.226  37.195  1.00 13.66           C  
ANISOU 2220  CA  TRP A 281     1749   1348   2094    268    307    113       C  
ATOM   2221  C   TRP A 281      28.514  68.661  36.279  1.00 13.07           C  
ANISOU 2221  C   TRP A 281     1676   1318   1970    208    226    100       C  
ATOM   2222  O   TRP A 281      28.278  68.393  35.098  1.00 12.77           O  
ANISOU 2222  O   TRP A 281     1591   1302   1957    194    169    130       O  
ATOM   2223  CB  TRP A 281      27.175  68.287  38.378  1.00 15.08           C  
ANISOU 2223  CB  TRP A 281     1930   1538   2262    279    365    100       C  
ATOM   2224  CG  TRP A 281      27.034  66.864  37.948  1.00 14.17           C  
ANISOU 2224  CG  TRP A 281     1747   1476   2163    251    327    115       C  
ATOM   2225  CD1 TRP A 281      25.964  66.304  37.302  1.00 15.29           C  
ANISOU 2225  CD1 TRP A 281     1793   1631   2386    260    310    159       C  
ATOM   2226  CD2 TRP A 281      27.995  65.817  38.121  1.00 12.45           C  
ANISOU 2226  CD2 TRP A 281     1550   1299   1880    206    297     86       C  
ATOM   2227  CE2 TRP A 281      27.446  64.653  37.551  1.00 12.92           C  
ANISOU 2227  CE2 TRP A 281     1532   1394   1983    191    268    113       C  
ATOM   2228  CE3 TRP A 281      29.267  65.746  38.699  1.00 13.24           C  
ANISOU 2228  CE3 TRP A 281     1724   1407   1897    178    286     42       C  
ATOM   2229  NE1 TRP A 281      26.207  64.980  37.061  1.00 15.56           N  
ANISOU 2229  NE1 TRP A 281     1797   1710   2407    222    273    156       N  
ATOM   2230  CZ2 TRP A 281      28.116  63.431  37.551  1.00 14.00           C  
ANISOU 2230  CZ2 TRP A 281     1671   1572   2079    153    240     96       C  
ATOM   2231  CZ3 TRP A 281      29.929  64.536  38.690  1.00 13.61           C  
ANISOU 2231  CZ3 TRP A 281     1763   1498   1910    143    254     30       C  
ATOM   2232  CH2 TRP A 281      29.348  63.393  38.127  1.00 13.01           C  
ANISOU 2232  CH2 TRP A 281     1616   1454   1874    133    237     57       C  
ATOM   2233  N   GLY A 282      29.711  68.489  36.827  1.00 12.56           N  
ANISOU 2233  N   GLY A 282     1671   1264   1837    174    222     57       N  
ATOM   2234  CA  GLY A 282      30.720  67.677  36.173  1.00 12.21           C  
ANISOU 2234  CA  GLY A 282     1620   1265   1755    122    164     45       C  
ATOM   2235  C   GLY A 282      31.580  68.370  35.141  1.00 10.89           C  
ANISOU 2235  C   GLY A 282     1476   1092   1571     90    121     45       C  
ATOM   2236  O   GLY A 282      32.094  67.704  34.236  1.00 10.81           O  
ANISOU 2236  O   GLY A 282     1447   1116   1545     57     79     52       O  
ATOM   2237  N   ASP A 283      31.752  69.684  35.253  1.00 11.47           N  
ANISOU 2237  N   ASP A 283     1595   1117   1645    101    138     39       N  
ATOM   2238  CA  ASP A 283      32.583  70.442  34.316  1.00 11.48           C  
ANISOU 2238  CA  ASP A 283     1623   1104   1636     71    109     42       C  
ATOM   2239  C   ASP A 283      34.054  70.380  34.701  1.00 10.29           C  
ANISOU 2239  C   ASP A 283     1508    957   1445     22     97      1       C  
ATOM   2240  O   ASP A 283      34.470  69.453  35.408  1.00 10.49           O  
ANISOU 2240  O   ASP A 283     1526   1013   1445      8     93    -23       O  
ATOM   2241  CB  ASP A 283      32.003  71.853  34.175  1.00 13.15           C  
ANISOU 2241  CB  ASP A 283     1862   1257   1878    105    131     60       C  
ATOM   2242  CG  ASP A 283      30.625  71.823  33.528  1.00 12.95           C  
ANISOU 2242  CG  ASP A 283     1784   1232   1905    150    125    109       C  
ATOM   2243  OD1 ASP A 283      30.489  71.223  32.444  1.00 13.04           O  
ANISOU 2243  OD1 ASP A 283     1761   1276   1919    136     77    137       O  
ATOM   2244  OD2 ASP A 283      29.682  72.401  34.118  1.00 18.46           O1-
ANISOU 2244  OD2 ASP A 283     2477   1893   2643    199    168    121       O1-
ATOM   2245  N   GLU A 284      34.852  71.324  34.207  1.00 10.96           N  
ANISOU 2245  N   GLU A 284     1625   1009   1529     -4     89     -2       N  
ATOM   2246  CA  GLU A 284      36.302  71.222  34.320  1.00 10.91           C  
ANISOU 2246  CA  GLU A 284     1633   1008   1505    -56     71    -31       C  
ATOM   2247  C   GLU A 284      36.768  71.061  35.758  1.00 11.15           C  
ANISOU 2247  C   GLU A 284     1690   1033   1512    -64     70    -77       C  
ATOM   2248  O   GLU A 284      37.721  70.313  36.024  1.00 11.88           O  
ANISOU 2248  O   GLU A 284     1769   1155   1591    -97     44    -96       O  
ATOM   2249  CB  GLU A 284      36.951  72.480  33.725  1.00 11.47           C  
ANISOU 2249  CB  GLU A 284     1737   1029   1592    -79     75    -26       C  
ATOM   2250  CG  GLU A 284      36.810  72.641  32.211  1.00 12.23           C  
ANISOU 2250  CG  GLU A 284     1823   1126   1697    -79     72     19       C  
ATOM   2251  CD  GLU A 284      35.534  73.332  31.751  1.00 11.75           C  
ANISOU 2251  CD  GLU A 284     1772   1039   1653    -30     81     56       C  
ATOM   2252  OE1 GLU A 284      34.542  73.406  32.519  1.00 11.96           O  
ANISOU 2252  OE1 GLU A 284     1793   1059   1694     12     95     52       O  
ATOM   2253  OE2 GLU A 284      35.532  73.829  30.585  1.00 12.35           O1-
ANISOU 2253  OE2 GLU A 284     1862   1097   1732    -30     77     92       O1-
ATOM   2254  N  AASP A 285      36.140  71.775  36.693  0.30 11.39           N  
ANISOU 2254  N  AASP A 285     1768   1023   1539    -32     97    -93       N  
ATOM   2255  N  BASP A 285      36.132  71.783  36.690  0.70 11.61           N  
ANISOU 2255  N  BASP A 285     1794   1049   1566    -31     98    -93       N  
ATOM   2256  CA AASP A 285      36.576  71.723  38.080  0.30 12.06           C  
ANISOU 2256  CA AASP A 285     1902   1093   1588    -37     93   -138       C  
ATOM   2257  CA BASP A 285      36.545  71.737  38.087  0.70 12.68           C  
ANISOU 2257  CA BASP A 285     1981   1171   1666    -36     94   -138       C  
ATOM   2258  C  AASP A 285      36.266  70.384  38.737  0.30 11.71           C  
ANISOU 2258  C  AASP A 285     1837   1096   1516    -21     96   -141       C  
ATOM   2259  C  BASP A 285      36.295  70.369  38.707  0.70 11.33           C  
ANISOU 2259  C  BASP A 285     1787   1049   1468    -23     94   -141       C  
ATOM   2260  O  AASP A 285      36.881  70.057  39.759  0.30 11.18           O  
ANISOU 2260  O  AASP A 285     1808   1030   1411    -34     76   -176       O  
ATOM   2261  O  BASP A 285      36.973  69.997  39.677  0.70 12.64           O  
ANISOU 2261  O  BASP A 285     1986   1219   1597    -39     72   -175       O  
ATOM   2262  CB AASP A 285      35.953  72.874  38.869  0.30 12.98           C  
ANISOU 2262  CB AASP A 285     2090   1143   1698     -3    132   -156       C  
ATOM   2263  CB BASP A 285      35.828  72.825  38.886  0.70 14.27           C  
ANISOU 2263  CB BASP A 285     2251   1308   1862      2    136   -154       C  
ATOM   2264  CG AASP A 285      36.530  74.231  38.485  0.30 18.18           C  
ANISOU 2264  CG AASP A 285     2786   1742   2377    -29    123   -165       C  
ATOM   2265  CG BASP A 285      34.317  72.726  38.790  0.70 16.69           C  
ANISOU 2265  CG BASP A 285     2534   1615   2192     65    191   -118       C  
ATOM   2266  OD1AASP A 285      37.514  74.283  37.718  0.30 15.23           O  
ANISOU 2266  OD1AASP A 285     2384   1378   2023    -78     88   -160       O  
ATOM   2267  OD2AASP A 285      35.996  75.252  38.959  0.30 20.65           O1-
ANISOU 2267  OD2AASP A 285     3160   1995   2691      1    159   -176       O1-
ATOM   2268  OD1BASP A 285      33.796  72.607  37.662  0.70 19.64           O  
ANISOU 2268  OD1BASP A 285     2847   2010   2605     74    187    -75       O  
ATOM   2269  OD2BASP A 285      33.649  72.775  39.846  0.70 26.33           O1-
ANISOU 2269  OD2BASP A 285     3797   2812   3395    105    237   -132       O1-
ATOM   2270  N   ASN A 286      35.320  69.611  38.196  1.00 10.95           N  
ANISOU 2270  N   ASN A 286     1685   1036   1439      6    115   -105       N  
ATOM   2271  CA  ASN A 286      35.136  68.246  38.670  1.00 11.36           C  
ANISOU 2271  CA  ASN A 286     1711   1134   1472     13    117   -104       C  
ATOM   2272  C   ASN A 286      36.264  67.339  38.190  1.00 10.65           C  
ANISOU 2272  C   ASN A 286     1587   1088   1373    -32     69   -109       C  
ATOM   2273  O   ASN A 286      36.722  66.461  38.934  1.00 10.89           O  
ANISOU 2273  O   ASN A 286     1623   1141   1374    -39     56   -126       O  
ATOM   2274  CB  ASN A 286      33.784  67.684  38.242  1.00 10.72           C  
ANISOU 2274  CB  ASN A 286     1576   1071   1425     51    148    -65       C  
ATOM   2275  CG  ASN A 286      33.535  66.308  38.821  1.00 10.25           C  
ANISOU 2275  CG  ASN A 286     1493   1049   1351     57    158    -64       C  
ATOM   2276  ND2 ASN A 286      33.546  65.290  37.977  1.00 10.85           N  
ANISOU 2276  ND2 ASN A 286     1511   1168   1442     39    131    -44       N  
ATOM   2277  OD1 ASN A 286      33.354  66.169  40.040  1.00 11.73           O  
ANISOU 2277  OD1 ASN A 286     1726   1221   1508     80    193    -82       O  
ATOM   2278  N   VAL A 287      36.712  67.514  36.946  1.00 10.15           N  
ANISOU 2278  N   VAL A 287     1491   1033   1333    -58     49    -90       N  
ATOM   2279  CA  VAL A 287      37.819  66.707  36.449  1.00 10.54           C  
ANISOU 2279  CA  VAL A 287     1509   1116   1380    -97     18    -93       C  
ATOM   2280  C   VAL A 287      39.052  66.910  37.318  1.00 11.14           C  
ANISOU 2280  C   VAL A 287     1610   1179   1444   -127    -11   -128       C  
ATOM   2281  O   VAL A 287      39.656  65.954  37.826  1.00 11.50           O  
ANISOU 2281  O   VAL A 287     1643   1253   1475   -137    -34   -140       O  
ATOM   2282  CB  VAL A 287      38.123  67.049  34.980  1.00 10.74           C  
ANISOU 2282  CB  VAL A 287     1513   1140   1429   -117     14    -67       C  
ATOM   2283  CG1 VAL A 287      39.298  66.203  34.490  1.00 12.00           C  
ANISOU 2283  CG1 VAL A 287     1642   1329   1590   -152     -2    -68       C  
ATOM   2284  CG2 VAL A 287      36.917  66.853  34.092  1.00 10.66           C  
ANISOU 2284  CG2 VAL A 287     1483   1140   1426    -89     24    -31       C  
ATOM   2285  N   THR A 288      39.462  68.163  37.488  1.00 11.85           N  
ANISOU 2285  N   THR A 288     1737   1222   1544   -143    -18   -145       N  
ATOM   2286  CA  THR A 288      40.669  68.416  38.270  1.00 12.58           C  
ANISOU 2286  CA  THR A 288     1850   1296   1634   -179    -61   -179       C  
ATOM   2287  C   THR A 288      40.446  68.124  39.748  1.00 11.94           C  
ANISOU 2287  C   THR A 288     1823   1210   1504   -157    -74   -210       C  
ATOM   2288  O   THR A 288      41.357  67.628  40.428  1.00 13.20           O  
ANISOU 2288  O   THR A 288     1985   1379   1650   -179   -123   -231       O  
ATOM   2289  CB  THR A 288      41.177  69.843  38.061  1.00 15.06           C  
ANISOU 2289  CB  THR A 288     2192   1554   1978   -207    -67   -191       C  
ATOM   2290  CG2 THR A 288      41.608  70.056  36.621  1.00 16.33           C  
ANISOU 2290  CG2 THR A 288     2305   1717   2183   -232    -51   -159       C  
ATOM   2291  OG1 THR A 288      40.140  70.760  38.382  1.00 14.25           O  
ANISOU 2291  OG1 THR A 288     2145   1410   1859   -172    -34   -195       O  
ATOM   2292  N   GLY A 289      39.247  68.395  40.267  1.00 11.68           N  
ANISOU 2292  N   GLY A 289     1835   1158   1443   -112    -31   -210       N  
ATOM   2293  CA  GLY A 289      38.987  68.101  41.663  1.00 12.35           C  
ANISOU 2293  CA  GLY A 289     1986   1233   1473    -87    -29   -236       C  
ATOM   2294  C   GLY A 289      39.050  66.621  41.977  1.00 11.43           C  
ANISOU 2294  C   GLY A 289     1841   1168   1334    -78    -37   -226       C  
ATOM   2295  O   GLY A 289      39.601  66.205  43.003  1.00 12.40           O  
ANISOU 2295  O   GLY A 289     2007   1290   1412    -81    -73   -249       O  
ATOM   2296  N   GLN A 290      38.466  65.797  41.110  1.00 10.71           N  
ANISOU 2296  N   GLN A 290     1681   1117   1270    -66     -9   -190       N  
ATOM   2297  CA  GLN A 290      38.497  64.356  41.323  1.00 10.62           C  
ANISOU 2297  CA  GLN A 290     1642   1151   1244    -59    -12   -178       C  
ATOM   2298  C   GLN A 290      39.898  63.808  41.122  1.00 10.69           C  
ANISOU 2298  C   GLN A 290     1616   1183   1262    -99    -72   -186       C  
ATOM   2299  O   GLN A 290      40.351  62.952  41.894  1.00 11.12           O  
ANISOU 2299  O   GLN A 290     1684   1254   1287    -96    -98   -194       O  
ATOM   2300  CB  GLN A 290      37.498  63.675  40.394  1.00 10.88           C  
ANISOU 2300  CB  GLN A 290     1612   1212   1308    -42     28   -141       C  
ATOM   2301  CG  GLN A 290      36.054  64.004  40.709  1.00 10.90           C  
ANISOU 2301  CG  GLN A 290     1631   1193   1317      2     88   -127       C  
ATOM   2302  CD  GLN A 290      35.696  63.632  42.131  1.00 11.19           C  
ANISOU 2302  CD  GLN A 290     1729   1216   1306     33    120   -140       C  
ATOM   2303  NE2 GLN A 290      35.338  62.372  42.340  1.00 11.95           N  
ANISOU 2303  NE2 GLN A 290     1800   1342   1399     45    139   -122       N  
ATOM   2304  OE1 GLN A 290      35.749  64.467  43.030  1.00 12.91           O  
ANISOU 2304  OE1 GLN A 290     2025   1393   1489     47    131   -165       O  
ATOM   2305  N   PHE A 291      40.593  64.253  40.075  1.00 10.81           N  
ANISOU 2305  N   PHE A 291     1587   1199   1323   -133    -89   -179       N  
ATOM   2306  CA  PHE A 291      41.938  63.732  39.855  1.00 10.86           C  
ANISOU 2306  CA  PHE A 291     1550   1223   1353   -167   -134   -181       C  
ATOM   2307  C   PHE A 291      42.891  64.205  40.958  1.00 11.87           C  
ANISOU 2307  C   PHE A 291     1718   1324   1468   -188   -197   -215       C  
ATOM   2308  O   PHE A 291      43.845  63.484  41.300  1.00 12.10           O  
ANISOU 2308  O   PHE A 291     1720   1371   1505   -202   -244   -218       O  
ATOM   2309  CB  PHE A 291      42.459  64.095  38.463  1.00 11.35           C  
ANISOU 2309  CB  PHE A 291     1558   1285   1468   -197   -123   -162       C  
ATOM   2310  CG  PHE A 291      41.741  63.415  37.322  1.00 10.96           C  
ANISOU 2310  CG  PHE A 291     1475   1264   1424   -182    -81   -130       C  
ATOM   2311  CD1 PHE A 291      40.668  62.570  37.515  1.00 11.24           C  
ANISOU 2311  CD1 PHE A 291     1514   1323   1433   -149    -59   -120       C  
ATOM   2312  CD2 PHE A 291      42.169  63.639  36.025  1.00 10.67           C  
ANISOU 2312  CD2 PHE A 291     1408   1226   1421   -203    -65   -111       C  
ATOM   2313  CE1 PHE A 291      40.025  61.976  36.432  1.00 11.13           C  
ANISOU 2313  CE1 PHE A 291     1472   1330   1428   -142    -34    -93       C  
ATOM   2314  CE2 PHE A 291      41.533  63.059  34.944  1.00 11.86           C  
ANISOU 2314  CE2 PHE A 291     1543   1396   1566   -191    -36    -85       C  
ATOM   2315  CZ  PHE A 291      40.465  62.232  35.145  1.00 11.03           C  
ANISOU 2315  CZ  PHE A 291     1439   1314   1437   -162    -28    -78       C  
ATOM   2316  N   ALA A 292      42.639  65.392  41.540  1.00 11.99           N  
ANISOU 2316  N   ALA A 292     1799   1293   1464   -188   -202   -240       N  
ATOM   2317  CA  ALA A 292      43.448  65.863  42.662  1.00 12.46           C  
ANISOU 2317  CA  ALA A 292     1914   1321   1501   -209   -271   -277       C  
ATOM   2318  C   ALA A 292      43.333  64.928  43.856  1.00 12.28           C  
ANISOU 2318  C   ALA A 292     1941   1312   1411   -180   -295   -287       C  
ATOM   2319  O   ALA A 292      44.305  64.760  44.609  1.00 13.21           O  
ANISOU 2319  O   ALA A 292     2078   1424   1518   -200   -374   -307       O  
ATOM   2320  CB  ALA A 292      43.038  67.282  43.047  1.00 13.53           C  
ANISOU 2320  CB  ALA A 292     2126   1397   1619   -209   -262   -305       C  
ATOM   2321  N   LYS A 293      42.162  64.317  44.064  1.00 11.99           N  
ANISOU 2321  N   LYS A 293     1930   1293   1334   -133   -230   -271       N  
ATOM   2322  CA  LYS A 293      42.025  63.360  45.164  1.00 12.10           C  
ANISOU 2322  CA  LYS A 293     1996   1318   1283   -104   -240   -274       C  
ATOM   2323  C   LYS A 293      42.918  62.155  44.931  1.00 11.77           C  
ANISOU 2323  C   LYS A 293     1886   1320   1267   -117   -284   -256       C  
ATOM   2324  O   LYS A 293      43.582  61.668  45.857  1.00 12.59           O  
ANISOU 2324  O   LYS A 293     2025   1423   1334   -116   -346   -267       O  
ATOM   2325  CB  LYS A 293      40.564  62.927  45.308  1.00 13.17           C  
ANISOU 2325  CB  LYS A 293     2156   1460   1390    -54   -148   -253       C  
ATOM   2326  CG  LYS A 293      39.616  64.044  45.690  1.00 12.72           C  
ANISOU 2326  CG  LYS A 293     2171   1355   1308    -28    -93   -268       C  
ATOM   2327  CD  LYS A 293      38.161  63.611  45.684  1.00 13.36           C  
ANISOU 2327  CD  LYS A 293     2248   1442   1388     20      4   -239       C  
ATOM   2328  CE  LYS A 293      37.242  64.754  46.048  1.00 15.15           C  
ANISOU 2328  CE  LYS A 293     2539   1615   1601     51     66   -250       C  
ATOM   2329  NZ  LYS A 293      35.802  64.415  45.842  1.00 14.27           N1+
ANISOU 2329  NZ  LYS A 293     2394   1508   1520     95    162   -214       N1+
ATOM   2330  N   MET A 294      42.948  61.659  43.693  1.00 11.34           N  
ANISOU 2330  N   MET A 294     1737   1298   1273   -128   -254   -227       N  
ATOM   2331  CA  MET A 294      43.810  60.530  43.369  1.00 11.18           C  
ANISOU 2331  CA  MET A 294     1649   1314   1284   -138   -284   -208       C  
ATOM   2332  C   MET A 294      45.280  60.896  43.529  1.00 11.62           C  
ANISOU 2332  C   MET A 294     1677   1358   1381   -177   -369   -223       C  
ATOM   2333  O   MET A 294      46.086  60.083  44.007  1.00 12.16           O  
ANISOU 2333  O   MET A 294     1727   1440   1452   -177   -422   -218       O  
ATOM   2334  CB  MET A 294      43.555  60.070  41.932  1.00 11.15           C  
ANISOU 2334  CB  MET A 294     1566   1338   1333   -144   -230   -179       C  
ATOM   2335  CG  MET A 294      42.198  59.420  41.722  1.00 10.91           C  
ANISOU 2335  CG  MET A 294     1545   1324   1278   -110   -162   -160       C  
ATOM   2336  SD  MET A 294      41.941  57.888  42.683  1.00 11.15           S  
ANISOU 2336  SD  MET A 294     1599   1374   1261    -76   -156   -148       S  
ATOM   2337  CE  MET A 294      43.114  56.808  41.868  1.00 11.48           C  
ANISOU 2337  CE  MET A 294     1560   1447   1354    -95   -182   -130       C  
ATOM   2338  N   LYS A 295      45.650  62.122  43.140  1.00 11.86           N  
ANISOU 2338  N   LYS A 295     1698   1357   1450   -212   -383   -238       N  
ATOM   2339  CA  LYS A 295      47.042  62.541  43.262  1.00 12.46           C  
ANISOU 2339  CA  LYS A 295     1735   1415   1582   -256   -464   -251       C  
ATOM   2340  C   LYS A 295      47.448  62.664  44.726  1.00 13.78           C  
ANISOU 2340  C   LYS A 295     1979   1558   1696   -255   -556   -281       C  
ATOM   2341  O   LYS A 295      48.542  62.241  45.108  1.00 14.05           O  
ANISOU 2341  O   LYS A 295     1977   1597   1764   -273   -638   -281       O  
ATOM   2342  CB  LYS A 295      47.252  63.863  42.527  1.00 13.72           C  
ANISOU 2342  CB  LYS A 295     1875   1540   1796   -294   -451   -259       C  
ATOM   2343  CG  LYS A 295      48.670  64.393  42.626  1.00 15.72           C  
ANISOU 2343  CG  LYS A 295     2080   1767   2125   -346   -531   -270       C  
ATOM   2344  CD  LYS A 295      48.845  65.676  41.822  1.00 20.25           C  
ANISOU 2344  CD  LYS A 295     2633   2302   2758   -385   -505   -273       C  
ATOM   2345  CE  LYS A 295      50.064  66.464  42.285  1.00 30.07           C  
ANISOU 2345  CE  LYS A 295     3857   3504   4066   -440   -594   -295       C  
ATOM   2346  NZ  LYS A 295      51.318  65.706  42.067  1.00 31.27           N1+
ANISOU 2346  NZ  LYS A 295     3901   3684   4295   -452   -619   -267       N1+
ATOM   2347  N  AGLU A 296      46.574  63.229  45.561  0.54 14.09           N  
ANISOU 2347  N  AGLU A 296     2131   1570   1653   -233   -543   -307       N  
ATOM   2348  N  BGLU A 296      46.593  63.248  45.563  0.46 13.59           N  
ANISOU 2348  N  BGLU A 296     2068   1506   1591   -234   -545   -308       N  
ATOM   2349  CA AGLU A 296      46.900  63.429  46.971  0.54 15.49           C  
ANISOU 2349  CA AGLU A 296     2408   1715   1761   -231   -629   -341       C  
ATOM   2350  CA BGLU A 296      46.942  63.410  46.972  0.46 14.00           C  
ANISOU 2350  CA BGLU A 296     2218   1527   1574   -232   -632   -341       C  
ATOM   2351  C  AGLU A 296      46.972  62.106  47.723  0.54 15.41           C  
ANISOU 2351  C  AGLU A 296     2422   1735   1699   -195   -656   -325       C  
ATOM   2352  C  BGLU A 296      47.029  62.059  47.672  0.46 12.97           C  
ANISOU 2352  C  BGLU A 296     2104   1428   1395   -197   -657   -323       C  
ATOM   2353  O  AGLU A 296      47.854  61.914  48.571  0.54 14.70           O  
ANISOU 2353  O  AGLU A 296     2345   1641   1600   -200   -739   -328       O  
ATOM   2354  O  BGLU A 296      47.990  61.785  48.403  0.46 16.19           O  
ANISOU 2354  O  BGLU A 296     2511   1835   1805   -204   -743   -323       O  
ATOM   2355  CB AGLU A 296      45.855  64.349  47.612  0.54 18.47           C  
ANISOU 2355  CB AGLU A 296     2911   2049   2059   -208   -586   -371       C  
ATOM   2356  CB BGLU A 296      45.921  64.314  47.665  0.46 14.91           C  
ANISOU 2356  CB BGLU A 296     2461   1597   1606   -209   -593   -371       C  
ATOM   2357  CG AGLU A 296      45.872  64.371  49.138  0.54 29.72           C  
ANISOU 2357  CG AGLU A 296     4447   3451   3392   -181   -622   -387       C  
ATOM   2358  CG BGLU A 296      46.141  64.477  49.166  0.46 23.26           C  
ANISOU 2358  CG BGLU A 296     3620   2632   2586   -190   -641   -388       C  
ATOM   2359  CD AGLU A 296      44.869  65.358  49.718  0.54 30.45           C  
ANISOU 2359  CD AGLU A 296     4654   3498   3419   -155   -560   -410       C  
ATOM   2360  CD BGLU A 296      47.444  65.172  49.496  0.46 20.71           C  
ANISOU 2360  CD BGLU A 296     3267   2289   2312   -234   -737   -401       C  
ATOM   2361  OE1AGLU A 296      44.743  66.470  49.165  0.54 34.98           O  
ANISOU 2361  OE1AGLU A 296     5219   4041   4032   -178   -539   -425       O  
ATOM   2362  OE2AGLU A 296      44.203  65.015  50.718  0.54 37.66           O1-
ANISOU 2362  OE2AGLU A 296     5663   4401   4244   -108   -525   -408       O1-
ATOM   2363  OE1BGLU A 296      47.965  65.902  48.627  0.46 27.36           O  
ANISOU 2363  OE1BGLU A 296     4032   3122   3241   -279   -744   -404       O  
ATOM   2364  OE2BGLU A 296      47.945  64.987  50.627  0.46 31.46           O1-
ANISOU 2364  OE2BGLU A 296     4684   3641   3628   -225   -802   -406       O1-
ATOM   2365  N   THR A 297      46.050  61.182  47.436  1.00 13.05           N  
ANISOU 2365  N   THR A 297     2113   1471   1376   -154   -565   -296       N  
ATOM   2366  CA  THR A 297      45.963  59.952  48.203  1.00 13.45           C  
ANISOU 2366  CA  THR A 297     2200   1541   1368   -116   -576   -279       C  
ATOM   2367  C   THR A 297      46.944  58.898  47.714  1.00 13.15           C  
ANISOU 2367  C   THR A 297     2056   1540   1399   -125   -616   -249       C  
ATOM   2368  O   THR A 297      47.497  58.148  48.528  1.00 14.64           O  
ANISOU 2368  O   THR A 297     2272   1734   1557   -109   -683   -243       O  
ATOM   2369  CB  THR A 297      44.530  59.414  48.159  1.00 13.79           C  
ANISOU 2369  CB  THR A 297     2278   1597   1365    -70   -459   -259       C  
ATOM   2370  CG2 THR A 297      44.413  58.112  48.931  1.00 15.52           C  
ANISOU 2370  CG2 THR A 297     2538   1832   1528    -31   -458   -238       C  
ATOM   2371  OG1 THR A 297      43.641  60.393  48.720  1.00 16.31           O  
ANISOU 2371  OG1 THR A 297     2698   1876   1625    -54   -416   -284       O  
ATOM   2372  N   PHE A 298      47.160  58.808  46.399  1.00 12.59           N  
ANISOU 2372  N   PHE A 298     1872   1493   1418   -146   -573   -229       N  
ATOM   2373  CA  PHE A 298      47.967  57.738  45.816  1.00 12.16           C  
ANISOU 2373  CA  PHE A 298     1718   1471   1431   -148   -584   -198       C  
ATOM   2374  C   PHE A 298      49.254  58.256  45.188  1.00 12.30           C  
ANISOU 2374  C   PHE A 298     1640   1482   1554   -194   -637   -197       C  
ATOM   2375  O   PHE A 298      50.346  57.934  45.674  1.00 13.51           O  
ANISOU 2375  O   PHE A 298     1758   1632   1743   -203   -727   -193       O  
ATOM   2376  CB  PHE A 298      47.106  56.934  44.829  1.00 12.18           C  
ANISOU 2376  CB  PHE A 298     1680   1503   1443   -126   -476   -170       C  
ATOM   2377  CG  PHE A 298      45.916  56.298  45.478  1.00 12.22           C  
ANISOU 2377  CG  PHE A 298     1764   1512   1365    -84   -424   -164       C  
ATOM   2378  CD1 PHE A 298      46.088  55.360  46.478  1.00 12.56           C  
ANISOU 2378  CD1 PHE A 298     1854   1559   1359    -54   -459   -154       C  
ATOM   2379  CD2 PHE A 298      44.635  56.668  45.131  1.00 12.21           C  
ANISOU 2379  CD2 PHE A 298     1790   1508   1341    -73   -342   -165       C  
ATOM   2380  CE1 PHE A 298      44.996  54.776  47.099  1.00 13.22           C  
ANISOU 2380  CE1 PHE A 298     2012   1641   1370    -15   -400   -145       C  
ATOM   2381  CE2 PHE A 298      43.527  56.084  45.749  1.00 13.02           C  
ANISOU 2381  CE2 PHE A 298     1955   1610   1382    -34   -286   -156       C  
ATOM   2382  CZ  PHE A 298      43.723  55.140  46.738  1.00 13.62           C  
ANISOU 2382  CZ  PHE A 298     2080   1687   1408     -7   -311   -146       C  
ATOM   2383  N   ILE A 299      49.157  59.069  44.137  1.00 12.26           N  
ANISOU 2383  N   ILE A 299     1588   1469   1602   -222   -585   -199       N  
ATOM   2384  CA  ILE A 299      50.332  59.432  43.347  1.00 12.89           C  
ANISOU 2384  CA  ILE A 299     1565   1541   1793   -264   -606   -188       C  
ATOM   2385  C   ILE A 299      51.412  60.052  44.223  1.00 13.65           C  
ANISOU 2385  C   ILE A 299     1657   1605   1922   -298   -728   -209       C  
ATOM   2386  O   ILE A 299      52.583  59.652  44.172  1.00 14.41           O  
ANISOU 2386  O   ILE A 299     1669   1708   2099   -308   -770   -189       O  
ATOM   2387  CB  ILE A 299      49.919  60.389  42.213  1.00 13.36           C  
ANISOU 2387  CB  ILE A 299     1606   1587   1884   -287   -530   -189       C  
ATOM   2388  CG1 ILE A 299      48.813  59.790  41.333  1.00 13.38           C  
ANISOU 2388  CG1 ILE A 299     1615   1617   1851   -256   -427   -169       C  
ATOM   2389  CG2 ILE A 299      51.118  60.771  41.368  1.00 16.14           C  
ANISOU 2389  CG2 ILE A 299     1855   1926   2353   -329   -535   -174       C  
ATOM   2390  CD1 ILE A 299      49.165  58.464  40.680  1.00 13.34           C  
ANISOU 2390  CD1 ILE A 299     1545   1644   1880   -237   -390   -137       C  
ATOM   2391  N   ASP A 300      51.034  61.050  45.022  1.00 15.02           N  
ANISOU 2391  N   ASP A 300     1926   1747   2034   -307   -764   -245       N  
ATOM   2392  CA  ASP A 300      51.994  61.764  45.855  1.00 16.11           C  
ANISOU 2392  CA  ASP A 300     2073   1859   2189   -328   -841   -258       C  
ATOM   2393  C   ASP A 300      52.517  60.911  46.996  1.00 15.18           C  
ANISOU 2393  C   ASP A 300     1983   1751   2034   -300   -918   -250       C  
ATOM   2394  O   ASP A 300      53.497  61.300  47.635  1.00 18.18           O  
ANISOU 2394  O   ASP A 300     2352   2112   2444   -318   -995   -254       O  
ATOM   2395  CB  ASP A 300      51.360  63.025  46.444  1.00 17.13           C  
ANISOU 2395  CB  ASP A 300     2310   1948   2251   -337   -843   -296       C  
ATOM   2396  CG  ASP A 300      51.170  64.122  45.417  1.00 17.11           C  
ANISOU 2396  CG  ASP A 300     2275   1922   2303   -373   -787   -303       C  
ATOM   2397  OD1 ASP A 300      51.636  63.982  44.269  1.00 19.41           O  
ANISOU 2397  OD1 ASP A 300     2462   2226   2687   -394   -748   -277       O  
ATOM   2398  OD2 ASP A 300      50.550  65.155  45.768  1.00 23.10           O1-
ANISOU 2398  OD2 ASP A 300     3119   2645   3011   -377   -776   -333       O1-
ATOM   2399  N   GLN A 301      51.870  59.788  47.288  1.00 15.63           N  
ANISOU 2399  N   GLN A 301     2081   1835   2025   -257   -902   -238       N  
ATOM   2400  CA  GLN A 301      52.333  58.844  48.294  1.00 16.86           C  
ANISOU 2400  CA  GLN A 301     2263   1999   2144   -225   -967   -224       C  
ATOM   2401  C   GLN A 301      53.097  57.681  47.676  1.00 16.97           C  
ANISOU 2401  C   GLN A 301     2160   2044   2244   -215   -969   -184       C  
ATOM   2402  O   GLN A 301      53.375  56.694  48.362  1.00 19.88           O  
ANISOU 2402  O   GLN A 301     2545   2424   2586   -182  -1011   -165       O  
ATOM   2403  CB  GLN A 301      51.154  58.331  49.118  1.00 19.71           C  
ANISOU 2403  CB  GLN A 301     2754   2362   2372   -179   -941   -232       C  
ATOM   2404  CG  GLN A 301      50.435  59.425  49.873  1.00 25.98           C  
ANISOU 2404  CG  GLN A 301     3673   3120   3080   -179   -931   -269       C  
ATOM   2405  CD  GLN A 301      51.343  60.113  50.877  1.00 36.67           C  
ANISOU 2405  CD  GLN A 301     5062   4439   4431   -198  -1025   -284       C  
ATOM   2406  NE2 GLN A 301      51.926  59.329  51.774  1.00 42.72           N  
ANISOU 2406  NE2 GLN A 301     5851   5208   5171   -175  -1093   -269       N  
ATOM   2407  OE1 GLN A 301      51.523  61.329  50.841  1.00 56.26           O  
ANISOU 2407  OE1 GLN A 301     7551   6890   6933   -232  -1038   -309       O  
ATOM   2408  N   GLY A 302      53.435  57.775  46.399  1.00 15.07           N  
ANISOU 2408  N   GLY A 302     1807   1813   2105   -240   -916   -168       N  
ATOM   2409  CA  GLY A 302      54.233  56.761  45.744  1.00 16.34           C  
ANISOU 2409  CA  GLY A 302     1853   1995   2359   -230   -902   -129       C  
ATOM   2410  C   GLY A 302      53.453  55.590  45.203  1.00 14.28           C  
ANISOU 2410  C   GLY A 302     1588   1766   2074   -194   -839   -110       C  
ATOM   2411  O   GLY A 302      54.068  54.585  44.807  1.00 15.81           O  
ANISOU 2411  O   GLY A 302     1701   1975   2332   -174   -824    -75       O  
ATOM   2412  N   ILE A 303      52.133  55.674  45.181  1.00 13.38           N  
ANISOU 2412  N   ILE A 303     1563   1658   1861   -176   -763   -124       N  
ATOM   2413  CA  ILE A 303      51.285  54.574  44.734  1.00 12.79           C  
ANISOU 2413  CA  ILE A 303     1503   1612   1747   -136   -666   -102       C  
ATOM   2414  C   ILE A 303      50.780  54.903  43.331  1.00 11.99           C  
ANISOU 2414  C   ILE A 303     1358   1517   1681   -153   -558    -98       C  
ATOM   2415  O   ILE A 303      50.077  55.912  43.164  1.00 11.78           O  
ANISOU 2415  O   ILE A 303     1375   1478   1623   -170   -532   -121       O  
ATOM   2416  CB  ILE A 303      50.104  54.351  45.695  1.00 12.40           C  
ANISOU 2416  CB  ILE A 303     1578   1561   1572   -103   -653   -115       C  
ATOM   2417  CG1 ILE A 303      50.608  54.090  47.115  1.00 16.30           C  
ANISOU 2417  CG1 ILE A 303     2137   2043   2014    -85   -763   -118       C  
ATOM   2418  CG2 ILE A 303      49.236  53.199  45.195  1.00 13.32           C  
ANISOU 2418  CG2 ILE A 303     1697   1702   1664    -68   -554    -90       C  
ATOM   2419  CD1 ILE A 303      49.506  54.100  48.151  1.00 18.24           C  
ANISOU 2419  CD1 ILE A 303     2523   2276   2131    -54   -746   -134       C  
ATOM   2420  N   PRO A 304      51.094  54.094  42.325  1.00 11.12           N  
ANISOU 2420  N   PRO A 304     1174   1421   1629   -144   -496    -71       N  
ATOM   2421  CA  PRO A 304      50.591  54.368  40.971  1.00 11.16           C  
ANISOU 2421  CA  PRO A 304     1157   1430   1653   -157   -398    -67       C  
ATOM   2422  C   PRO A 304      49.101  54.101  40.868  1.00 10.49           C  
ANISOU 2422  C   PRO A 304     1147   1357   1483   -136   -337    -73       C  
ATOM   2423  O   PRO A 304      48.527  53.334  41.641  1.00 10.58           O  
ANISOU 2423  O   PRO A 304     1208   1377   1434   -106   -343    -71       O  
ATOM   2424  CB  PRO A 304      51.395  53.409  40.080  1.00 11.83           C  
ANISOU 2424  CB  PRO A 304     1159   1521   1813   -147   -353    -37       C  
ATOM   2425  CG  PRO A 304      51.819  52.308  40.983  1.00 15.74           C  
ANISOU 2425  CG  PRO A 304     1652   2025   2304   -114   -404    -21       C  
ATOM   2426  CD  PRO A 304      51.899  52.859  42.379  1.00 12.03           C  
ANISOU 2426  CD  PRO A 304     1233   1547   1791   -118   -510    -41       C  
ATOM   2427  N   ALA A 305      48.485  54.737  39.872  1.00 10.16           N  
ANISOU 2427  N   ALA A 305     1106   1312   1442   -153   -276    -78       N  
ATOM   2428  CA  ALA A 305      47.060  54.582  39.626  1.00  9.87           C  
ANISOU 2428  CA  ALA A 305     1123   1283   1343   -137   -222    -80       C  
ATOM   2429  C   ALA A 305      46.788  54.814  38.153  1.00  9.49           C  
ANISOU 2429  C   ALA A 305     1051   1235   1320   -152   -157    -72       C  
ATOM   2430  O   ALA A 305      47.508  55.559  37.486  1.00 10.96           O  
ANISOU 2430  O   ALA A 305     1200   1407   1556   -178   -152    -70       O  
ATOM   2431  CB  ALA A 305      46.248  55.571  40.469  1.00 10.82           C  
ANISOU 2431  CB  ALA A 305     1311   1391   1410   -138   -243   -103       C  
ATOM   2432  N   TYR A 306      45.709  54.203  37.652  1.00  9.18           N  
ANISOU 2432  N   TYR A 306     1037   1205   1245   -137   -110    -65       N  
ATOM   2433  CA  TYR A 306      45.340  54.374  36.257  1.00  8.51           C  
ANISOU 2433  CA  TYR A 306      947   1117   1169   -149    -60    -58       C  
ATOM   2434  C   TYR A 306      43.834  54.493  36.125  1.00  8.57           C  
ANISOU 2434  C   TYR A 306      995   1128   1133   -141    -42    -60       C  
ATOM   2435  O   TYR A 306      43.069  54.033  36.967  1.00  9.25           O  
ANISOU 2435  O   TYR A 306     1106   1221   1189   -122    -48    -62       O  
ATOM   2436  CB  TYR A 306      45.869  53.259  35.350  1.00  9.63           C  
ANISOU 2436  CB  TYR A 306     1063   1263   1334   -144    -20    -42       C  
ATOM   2437  CG  TYR A 306      45.321  51.862  35.605  1.00  9.08           C  
ANISOU 2437  CG  TYR A 306     1010   1205   1236   -120     -9    -37       C  
ATOM   2438  CD1 TYR A 306      45.796  51.092  36.651  1.00  9.99           C  
ANISOU 2438  CD1 TYR A 306     1115   1326   1354   -101    -37    -32       C  
ATOM   2439  CD2 TYR A 306      44.355  51.302  34.776  1.00  9.28           C  
ANISOU 2439  CD2 TYR A 306     1062   1230   1235   -119     25    -34       C  
ATOM   2440  CE1 TYR A 306      45.324  49.809  36.876  1.00 10.79           C  
ANISOU 2440  CE1 TYR A 306     1234   1432   1434    -80    -20    -25       C  
ATOM   2441  CE2 TYR A 306      43.876  50.022  34.989  1.00  9.33           C  
ANISOU 2441  CE2 TYR A 306     1082   1240   1224   -103     36    -30       C  
ATOM   2442  CZ  TYR A 306      44.366  49.265  36.042  1.00  8.87           C  
ANISOU 2442  CZ  TYR A 306     1014   1186   1171    -83     19    -24       C  
ATOM   2443  OH  TYR A 306      43.941  47.981  36.282  1.00  9.75           O  
ANISOU 2443  OH  TYR A 306     1141   1295   1268    -66     35    -17       O  
ATOM   2444  N   ILE A 307      43.419  55.142  35.043  1.00  8.64           N  
ANISOU 2444  N   ILE A 307     1011   1129   1144   -154    -19    -56       N  
ATOM   2445  CA  ILE A 307      42.007  55.338  34.717  1.00  8.33           C  
ANISOU 2445  CA  ILE A 307      999   1089   1079   -147     -8    -53       C  
ATOM   2446  C   ILE A 307      41.684  54.268  33.679  1.00  8.10           C  
ANISOU 2446  C   ILE A 307      971   1065   1042   -147     15    -43       C  
ATOM   2447  O   ILE A 307      41.920  54.429  32.476  1.00  8.61           O  
ANISOU 2447  O   ILE A 307     1044   1121   1107   -159     33    -36       O  
ATOM   2448  CB  ILE A 307      41.738  56.758  34.226  1.00  8.93           C  
ANISOU 2448  CB  ILE A 307     1086   1147   1158   -159     -8    -54       C  
ATOM   2449  CG1 ILE A 307      42.066  57.788  35.315  1.00 10.02           C  
ANISOU 2449  CG1 ILE A 307     1233   1272   1301   -161    -33    -69       C  
ATOM   2450  CG2 ILE A 307      40.296  56.896  33.777  1.00 10.21           C  
ANISOU 2450  CG2 ILE A 307     1266   1308   1305   -149     -3    -45       C  
ATOM   2451  CD1 ILE A 307      42.318  59.162  34.788  1.00 12.36           C  
ANISOU 2451  CD1 ILE A 307     1536   1545   1616   -179    -32    -70       C  
ATOM   2452  N   GLY A 308      41.175  53.136  34.155  1.00  8.01           N  
ANISOU 2452  N   GLY A 308      961   1063   1020   -134     17    -41       N  
ATOM   2453  CA  GLY A 308      40.958  51.980  33.310  1.00  7.97           C  
ANISOU 2453  CA  GLY A 308      963   1057   1008   -136     35    -36       C  
ATOM   2454  C   GLY A 308      39.861  52.152  32.282  1.00  7.57           C  
ANISOU 2454  C   GLY A 308      932    998    945   -147     30    -31       C  
ATOM   2455  O   GLY A 308      39.845  51.412  31.292  1.00  8.15           O  
ANISOU 2455  O   GLY A 308     1026   1065   1007   -155     39    -30       O  
ATOM   2456  N   GLU A 309      38.929  53.086  32.514  1.00  7.71           N  
ANISOU 2456  N   GLU A 309      949   1016    967   -145     13    -28       N  
ATOM   2457  CA  GLU A 309      37.904  53.435  31.543  1.00  7.69           C  
ANISOU 2457  CA  GLU A 309      958   1003    960   -152     -4    -19       C  
ATOM   2458  C   GLU A 309      37.587  54.922  31.681  1.00  7.42           C  
ANISOU 2458  C   GLU A 309      922    962    934   -147    -13    -15       C  
ATOM   2459  O   GLU A 309      37.433  55.425  32.802  1.00  8.08           O  
ANISOU 2459  O   GLU A 309      994   1047   1029   -134     -8    -19       O  
ATOM   2460  CB  GLU A 309      36.605  52.653  31.743  1.00  7.96           C  
ANISOU 2460  CB  GLU A 309      978   1037   1009   -151    -17    -13       C  
ATOM   2461  CG  GLU A 309      36.736  51.160  31.621  1.00  8.04           C  
ANISOU 2461  CG  GLU A 309      993   1047   1013   -158    -10    -18       C  
ATOM   2462  CD  GLU A 309      35.429  50.400  31.822  1.00  7.90           C  
ANISOU 2462  CD  GLU A 309      956   1023   1024   -162    -23    -10       C  
ATOM   2463  OE1 GLU A 309      34.339  51.026  31.746  1.00  8.49           O  
ANISOU 2463  OE1 GLU A 309     1008   1092   1124   -162    -44      2       O  
ATOM   2464  OE2 GLU A 309      35.507  49.155  32.043  1.00  8.28           O1-
ANISOU 2464  OE2 GLU A 309     1006   1067   1074   -166    -10    -13       O1-
ATOM   2465  N   MET A 310      37.439  55.590  30.534  1.00  8.29           N  
ANISOU 2465  N   MET A 310     1055   1060   1034   -155    -25     -6       N  
ATOM   2466  CA  MET A 310      36.993  56.977  30.404  1.00  7.94           C  
ANISOU 2466  CA  MET A 310     1016   1003    998   -149    -35      4       C  
ATOM   2467  C   MET A 310      36.502  57.109  28.961  1.00  8.08           C  
ANISOU 2467  C   MET A 310     1065   1007    996   -157    -61     20       C  
ATOM   2468  O   MET A 310      36.685  56.193  28.151  1.00  8.40           O  
ANISOU 2468  O   MET A 310     1131   1048   1011   -168    -66     17       O  
ATOM   2469  CB  MET A 310      38.107  57.977  30.755  1.00  8.17           C  
ANISOU 2469  CB  MET A 310     1050   1023   1030   -153    -15     -4       C  
ATOM   2470  CG  MET A 310      39.433  57.745  30.062  1.00  9.80           C  
ANISOU 2470  CG  MET A 310     1271   1227   1227   -170      8     -6       C  
ATOM   2471  SD  MET A 310      39.524  58.242  28.328  1.00 10.26           S  
ANISOU 2471  SD  MET A 310     1380   1263   1258   -180     17     13       S  
ATOM   2472  CE  MET A 310      39.347  60.030  28.445  1.00 11.88           C  
ANISOU 2472  CE  MET A 310     1591   1444   1479   -177     13     23       C  
ATOM   2473  N   GLY A 311      35.864  58.228  28.622  1.00  8.68           N  
ANISOU 2473  N   GLY A 311     1149   1069   1080   -148    -80     35       N  
ATOM   2474  CA  GLY A 311      35.502  58.464  27.239  1.00  9.61           C  
ANISOU 2474  CA  GLY A 311     1311   1171   1171   -152   -111     53       C  
ATOM   2475  C   GLY A 311      34.258  59.320  27.110  1.00  9.22           C  
ANISOU 2475  C   GLY A 311     1247   1109   1148   -135   -151     76       C  
ATOM   2476  O   GLY A 311      33.733  59.849  28.088  1.00 10.05           O  
ANISOU 2476  O   GLY A 311     1310   1214   1294   -117   -141     78       O  
ATOM   2477  N   CYS A 312      33.787  59.444  25.863  1.00  9.07           N  
ANISOU 2477  N   CYS A 312     1270   1076   1102   -137   -197     94       N  
ATOM   2478  CA  CYS A 312      32.628  60.268  25.550  1.00 10.01           C  
ANISOU 2478  CA  CYS A 312     1376   1178   1248   -118   -246    123       C  
ATOM   2479  C   CYS A 312      32.149  59.855  24.169  1.00 10.43           C  
ANISOU 2479  C   CYS A 312     1481   1220   1261   -128   -315    137       C  
ATOM   2480  O   CYS A 312      32.970  59.720  23.256  1.00 10.26           O  
ANISOU 2480  O   CYS A 312     1536   1188   1172   -141   -303    133       O  
ATOM   2481  CB  CYS A 312      33.013  61.758  25.544  1.00 10.90           C  
ANISOU 2481  CB  CYS A 312     1512   1270   1361   -102   -219    136       C  
ATOM   2482  SG  CYS A 312      31.646  62.893  25.363  1.00 12.08           S  
ANISOU 2482  SG  CYS A 312     1638   1395   1556    -69   -267    174       S  
ATOM   2483  N   VAL A 313      30.831  59.684  24.008  1.00 10.58           N  
ANISOU 2483  N   VAL A 313     1461   1235   1321   -121   -386    156       N  
ATOM   2484  CA  VAL A 313      30.286  59.208  22.743  1.00 11.63           C  
ANISOU 2484  CA  VAL A 313     1646   1355   1418   -134   -471    167       C  
ATOM   2485  C   VAL A 313      30.289  60.310  21.681  1.00 10.92           C  
ANISOU 2485  C   VAL A 313     1629   1239   1281   -119   -505    196       C  
ATOM   2486  O   VAL A 313      30.277  61.512  21.958  1.00 12.02           O  
ANISOU 2486  O   VAL A 313     1755   1368   1445    -94   -480    216       O  
ATOM   2487  CB  VAL A 313      28.883  58.590  22.895  1.00 12.15           C  
ANISOU 2487  CB  VAL A 313     1638   1423   1556   -138   -548    179       C  
ATOM   2488  CG1 VAL A 313      28.930  57.384  23.814  1.00 12.67           C  
ANISOU 2488  CG1 VAL A 313     1648   1508   1656   -156   -511    152       C  
ATOM   2489  CG2 VAL A 313      27.861  59.624  23.368  1.00 13.23           C  
ANISOU 2489  CG2 VAL A 313     1699   1551   1777   -105   -567    213       C  
ATOM   2490  N   HIS A 314      30.285  59.866  20.432  1.00 11.57           N  
ANISOU 2490  N   HIS A 314     1800   1305   1291   -133   -563    198       N  
ATOM   2491  CA  HIS A 314      30.273  60.703  19.239  1.00 12.26           C  
ANISOU 2491  CA  HIS A 314     1983   1363   1314   -120   -605    227       C  
ATOM   2492  C   HIS A 314      28.948  61.425  19.065  1.00 12.97           C  
ANISOU 2492  C   HIS A 314     2029   1439   1460    -96   -700    267       C  
ATOM   2493  O   HIS A 314      27.873  60.894  19.359  1.00 14.38           O  
ANISOU 2493  O   HIS A 314     2128   1626   1710   -100   -770    271       O  
ATOM   2494  CB  HIS A 314      30.535  59.794  18.033  1.00 14.08           C  
ANISOU 2494  CB  HIS A 314     2328   1576   1445   -143   -647    214       C  
ATOM   2495  CG  HIS A 314      30.424  60.444  16.691  1.00 13.58           C  
ANISOU 2495  CG  HIS A 314     2386   1478   1297   -130   -704    243       C  
ATOM   2496  CD2 HIS A 314      29.596  60.179  15.655  1.00 15.56           C  
ANISOU 2496  CD2 HIS A 314     2705   1706   1501   -134   -826    258       C  
ATOM   2497  ND1 HIS A 314      31.279  61.434  16.251  1.00 14.28           N  
ANISOU 2497  ND1 HIS A 314     2552   1545   1330   -113   -633    262       N  
ATOM   2498  CE1 HIS A 314      30.960  61.768  15.012  1.00 15.86           C  
ANISOU 2498  CE1 HIS A 314     2867   1711   1448   -103   -704    289       C  
ATOM   2499  NE2 HIS A 314      29.943  61.019  14.625  1.00 14.93           N  
ANISOU 2499  NE2 HIS A 314     2733   1594   1346   -115   -810    278       N  
ATOM   2500  N   ARG A 315      29.042  62.647  18.553  1.00 13.21           N  
ANISOU 2500  N   ARG A 315     2111   1445   1464    -70   -700    299       N  
ATOM   2501  CA  ARG A 315      27.891  63.416  18.099  1.00 15.18           C  
ANISOU 2501  CA  ARG A 315     2345   1673   1750    -41   -798    344       C  
ATOM   2502  C   ARG A 315      28.036  63.694  16.605  1.00 16.09           C  
ANISOU 2502  C   ARG A 315     2603   1754   1754    -38   -861    368       C  
ATOM   2503  O   ARG A 315      29.096  64.136  16.152  1.00 17.38           O  
ANISOU 2503  O   ARG A 315     2865   1902   1836    -37   -785    366       O  
ATOM   2504  CB  ARG A 315      27.766  64.739  18.859  1.00 14.53           C  
ANISOU 2504  CB  ARG A 315     2201   1581   1737     -4   -743    369       C  
ATOM   2505  CG  ARG A 315      26.970  64.637  20.163  1.00 15.14           C  
ANISOU 2505  CG  ARG A 315     2135   1678   1939      8   -727    365       C  
ATOM   2506  CD  ARG A 315      27.695  63.932  21.300  1.00 13.88           C  
ANISOU 2506  CD  ARG A 315     1931   1549   1795    -14   -630    319       C  
ATOM   2507  NE  ARG A 315      26.927  64.106  22.528  1.00 14.22           N  
ANISOU 2507  NE  ARG A 315     1857   1599   1946      8   -601    323       N  
ATOM   2508  CZ  ARG A 315      27.322  63.714  23.734  1.00 13.00           C  
ANISOU 2508  CZ  ARG A 315     1653   1465   1820      0   -518    292       C  
ATOM   2509  NH1 ARG A 315      28.475  63.072  23.900  1.00 13.55           N1+
ANISOU 2509  NH1 ARG A 315     1767   1554   1828    -30   -464    254       N1+
ATOM   2510  NH2 ARG A 315      26.540  63.948  24.780  1.00 14.09           N  
ANISOU 2510  NH2 ARG A 315     1700   1601   2050     27   -488    301       N  
ATOM   2511  N   ALA A 316      26.974  63.435  15.844  1.00 19.93           N  
ANISOU 2511  N   ALA A 316     3094   2231   2249    -37   -978    380       N  
ATOM   2512  CA  ALA A 316      27.016  63.686  14.409  1.00 19.43           C  
ANISOU 2512  CA  ALA A 316     3153   2138   2091    -34  -1011    385       C  
ATOM   2513  C   ALA A 316      26.962  65.173  14.082  1.00 24.53           C  
ANISOU 2513  C   ALA A 316     3830   2760   2733      7  -1000    429       C  
ATOM   2514  O   ALA A 316      27.435  65.577  13.014  1.00 25.92           O  
ANISOU 2514  O   ALA A 316     4126   2908   2812     13   -985    435       O  
ATOM   2515  CB  ALA A 316      25.860  62.954  13.717  1.00 24.25           C  
ANISOU 2515  CB  ALA A 316     3746   2743   2726    -50  -1126    375       C  
ATOM   2516  N   ASP A 317      26.418  65.984  14.985  1.00 22.88           N  
ANISOU 2516  N   ASP A 317     3515   2553   2625     37  -1000    460       N  
ATOM   2517  CA  ASP A 317      26.340  67.425  14.793  1.00 27.06           C  
ANISOU 2517  CA  ASP A 317     4066   3054   3162     79   -982    503       C  
ATOM   2518  C   ASP A 317      27.703  68.076  15.015  1.00 20.67           C  
ANISOU 2518  C   ASP A 317     3332   2227   2294     80   -864    506       C  
ATOM   2519  O   ASP A 317      28.361  67.828  16.029  1.00 20.44           O  
ANISOU 2519  O   ASP A 317     3254   2215   2297     64   -782    482       O  
ATOM   2520  CB  ASP A 317      25.328  67.978  15.799  1.00 32.02           C  
ANISOU 2520  CB  ASP A 317     4550   3687   3930    112  -1005    531       C  
ATOM   2521  CG  ASP A 317      25.214  69.484  15.752  1.00 36.31           C  
ANISOU 2521  CG  ASP A 317     5105   4196   4494    159   -978    575       C  
ATOM   2522  OD1 ASP A 317      24.582  70.001  14.809  1.00 41.69           O  
ANISOU 2522  OD1 ASP A 317     5821   4861   5159    180  -1042    601       O  
ATOM   2523  OD2 ASP A 317      25.747  70.149  16.662  1.00 34.89           O1-
ANISOU 2523  OD2 ASP A 317     4904   4001   4351    175   -895    583       O1-
ATOM   2524  N   ASP A 318      28.105  68.946  14.080  1.00 24.94           N  
ANISOU 2524  N   ASP A 318     3977   2736   2763     96   -837    528       N  
ATOM   2525  CA  ASP A 318      29.428  69.564  14.121  1.00 22.26           C  
ANISOU 2525  CA  ASP A 318     3714   2372   2371     91   -716    530       C  
ATOM   2526  C   ASP A 318      29.655  70.330  15.422  1.00 22.53           C  
ANISOU 2526  C   ASP A 318     3664   2399   2496    103   -645    537       C  
ATOM   2527  O   ASP A 318      30.717  70.226  16.046  1.00 20.65           O  
ANISOU 2527  O   ASP A 318     3411   2173   2264     76   -534    501       O  
ATOM   2528  CB  ASP A 318      29.579  70.537  12.944  1.00 30.07           C  
ANISOU 2528  CB  ASP A 318     4807   3324   3294    113   -704    560       C  
ATOM   2529  CG  ASP A 318      30.251  69.914  11.733  1.00 39.42           C  
ANISOU 2529  CG  ASP A 318     6115   4503   4361     91   -682    538       C  
ATOM   2530  OD1 ASP A 318      30.805  68.802  11.849  1.00 48.85           O  
ANISOU 2530  OD1 ASP A 318     7320   5717   5525     58   -653    498       O  
ATOM   2531  OD2 ASP A 318      30.227  70.550  10.655  1.00 46.70           O1-
ANISOU 2531  OD2 ASP A 318     7127   5395   5223    109   -689    561       O1-
ATOM   2532  N   LEU A 319      28.691  71.155  15.822  1.00 19.95           N  
ANISOU 2532  N   LEU A 319     3268   2059   2254    142   -689    570       N  
ATOM   2533  CA  LEU A 319      28.884  71.976  17.011  1.00 18.39           C  
ANISOU 2533  CA  LEU A 319     2987   1855   2145    154   -600    559       C  
ATOM   2534  C   LEU A 319      29.012  71.108  18.250  1.00 17.09           C  
ANISOU 2534  C   LEU A 319     2713   1738   2042    127   -555    505       C  
ATOM   2535  O   LEU A 319      29.916  71.302  19.071  1.00 17.16           O  
ANISOU 2535  O   LEU A 319     2702   1751   2066    108   -455    472       O  
ATOM   2536  CB  LEU A 319      27.713  72.943  17.154  1.00 17.71           C  
ANISOU 2536  CB  LEU A 319     2849   1741   2139    208   -657    607       C  
ATOM   2537  CG  LEU A 319      27.735  73.800  18.414  1.00 16.97           C  
ANISOU 2537  CG  LEU A 319     2675   1634   2138    227   -570    595       C  
ATOM   2538  CD1 LEU A 319      29.000  74.644  18.486  1.00 17.42           C  
ANISOU 2538  CD1 LEU A 319     2805   1658   2155    210   -460    584       C  
ATOM   2539  CD2 LEU A 319      26.501  74.682  18.444  1.00 19.38           C  
ANISOU 2539  CD2 LEU A 319     2932   1907   2525    287   -627    647       C  
ATOM   2540  N   SER A 320      28.108  70.143  18.405  1.00 17.04           N  
ANISOU 2540  N   SER A 320     2636   1764   2074    125   -633    498       N  
ATOM   2541  CA  SER A 320      28.175  69.253  19.559  1.00 16.20           C  
ANISOU 2541  CA  SER A 320     2434   1700   2023    102   -591    452       C  
ATOM   2542  C   SER A 320      29.485  68.469  19.588  1.00 14.31           C  
ANISOU 2542  C   SER A 320     2242   1482   1713     56   -520    406       C  
ATOM   2543  O   SER A 320      30.075  68.273  20.660  1.00 14.45           O  
ANISOU 2543  O   SER A 320     2207   1520   1764     41   -442    369       O  
ATOM   2544  CB  SER A 320      26.982  68.299  19.540  1.00 17.17           C  
ANISOU 2544  CB  SER A 320     2481   1845   2196    103   -690    458       C  
ATOM   2545  OG  SER A 320      25.759  69.020  19.546  1.00 18.02           O  
ANISOU 2545  OG  SER A 320     2529   1931   2387    148   -753    504       O  
ATOM   2546  N   GLU A 321      29.959  68.007  18.421  1.00 14.65           N  
ANISOU 2546  N   GLU A 321     2388   1519   1660     37   -546    410       N  
ATOM   2547  CA  GLU A 321      31.180  67.202  18.401  1.00 13.83           C  
ANISOU 2547  CA  GLU A 321     2325   1433   1498     -1   -473    371       C  
ATOM   2548  C   GLU A 321      32.382  68.005  18.893  1.00 13.43           C  
ANISOU 2548  C   GLU A 321     2284   1367   1453     -9   -359    360       C  
ATOM   2549  O   GLU A 321      33.298  67.445  19.503  1.00 12.38           O  
ANISOU 2549  O   GLU A 321     2123   1255   1326    -36   -290    323       O  
ATOM   2550  CB  GLU A 321      31.403  66.624  17.005  1.00 14.56           C  
ANISOU 2550  CB  GLU A 321     2539   1511   1482    -13   -515    379       C  
ATOM   2551  CG  GLU A 321      32.531  65.596  16.915  1.00 15.14           C  
ANISOU 2551  CG  GLU A 321     2651   1600   1501    -48   -444    340       C  
ATOM   2552  CD  GLU A 321      32.246  64.277  17.628  1.00 12.94           C  
ANISOU 2552  CD  GLU A 321     2291   1362   1261    -69   -466    301       C  
ATOM   2553  OE1 GLU A 321      31.303  64.187  18.450  1.00 13.68           O  
ANISOU 2553  OE1 GLU A 321     2282   1477   1440    -61   -512    299       O  
ATOM   2554  OE2 GLU A 321      33.008  63.304  17.387  1.00 13.12           O1-
ANISOU 2554  OE2 GLU A 321     2356   1394   1234    -93   -426    272       O1-
ATOM   2555  N  ASER A 322      32.398  69.315  18.647  0.44 13.39           N  
ANISOU 2555  N  ASER A 322     2315   1321   1453     14   -341    393       N  
ATOM   2556  N  BSER A 322      32.402  69.315  18.635  0.56 13.36           N  
ANISOU 2556  N  BSER A 322     2311   1317   1447     14   -341    394       N  
ATOM   2557  CA ASER A 322      33.493  70.136  19.148  0.44 13.23           C  
ANISOU 2557  CA ASER A 322     2297   1279   1450      1   -239    383       C  
ATOM   2558  CA BSER A 322      33.480  70.148  19.151  0.56 13.28           C  
ANISOU 2558  CA BSER A 322     2303   1285   1457      1   -240    383       C  
ATOM   2559  C  ASER A 322      33.610  70.022  20.665  0.44 12.33           C  
ANISOU 2559  C  ASER A 322     2078   1191   1415     -8   -201    343       C  
ATOM   2560  C  BSER A 322      33.606  69.995  20.662  0.56 12.43           C  
ANISOU 2560  C  BSER A 322     2090   1205   1427     -9   -202    343       C  
ATOM   2561  O  ASER A 322      34.717  69.961  21.206  0.44 12.72           O  
ANISOU 2561  O  ASER A 322     2115   1246   1473    -37   -129    313       O  
ATOM   2562  O  BSER A 322      34.713  69.888  21.197  0.56 12.72           O  
ANISOU 2562  O  BSER A 322     2115   1248   1472    -38   -130    312       O  
ATOM   2563  CB ASER A 322      33.289  71.591  18.725  0.44 15.21           C  
ANISOU 2563  CB ASER A 322     2597   1476   1704     30   -234    427       C  
ATOM   2564  CB BSER A 322      33.220  71.615  18.805  0.56 15.06           C  
ANISOU 2564  CB BSER A 322     2572   1459   1693     31   -237    427       C  
ATOM   2565  OG ASER A 322      34.470  72.349  18.923  0.44 18.58           O  
ANISOU 2565  OG ASER A 322     3050   1873   2138      9   -137    421       O  
ATOM   2566  OG BSER A 322      32.947  71.778  17.427  0.56 13.81           O  
ANISOU 2566  OG BSER A 322     2518   1273   1457     48   -285    470       O  
ATOM   2567  N   PHE A 323      32.473  69.993  21.366  1.00 12.55           N  
ANISOU 2567  N   PHE A 323     2032   1234   1504     17   -249    344       N  
ATOM   2568  CA  PHE A 323      32.489  69.850  22.815  1.00 12.20           C  
ANISOU 2568  CA  PHE A 323     1903   1211   1523     14   -211    308       C  
ATOM   2569  C   PHE A 323      33.005  68.487  23.247  1.00 10.41           C  
ANISOU 2569  C   PHE A 323     1644   1029   1282    -18   -198    268       C  
ATOM   2570  O   PHE A 323      33.678  68.382  24.278  1.00 11.12           O  
ANISOU 2570  O   PHE A 323     1698   1131   1396    -35   -146    234       O  
ATOM   2571  CB  PHE A 323      31.089  70.099  23.373  1.00 12.06           C  
ANISOU 2571  CB  PHE A 323     1818   1191   1574     54   -254    325       C  
ATOM   2572  CG  PHE A 323      30.672  71.537  23.334  1.00 11.97           C  
ANISOU 2572  CG  PHE A 323     1823   1131   1595     91   -246    358       C  
ATOM   2573  CD1 PHE A 323      31.011  72.399  24.369  1.00 12.41           C  
ANISOU 2573  CD1 PHE A 323     1864   1161   1689     97   -179    338       C  
ATOM   2574  CD2 PHE A 323      29.961  72.029  22.262  1.00 15.11           C  
ANISOU 2574  CD2 PHE A 323     2258   1502   1980    120   -310    408       C  
ATOM   2575  CE1 PHE A 323      30.634  73.714  24.342  1.00 15.40           C  
ANISOU 2575  CE1 PHE A 323     2264   1488   2098    132   -167    366       C  
ATOM   2576  CE2 PHE A 323      29.583  73.356  22.227  1.00 15.87           C  
ANISOU 2576  CE2 PHE A 323     2371   1549   2109    158   -300    441       C  
ATOM   2577  CZ  PHE A 323      29.924  74.193  23.273  1.00 16.43           C  
ANISOU 2577  CZ  PHE A 323     2426   1594   2223    164   -224    420       C  
ATOM   2578  N   ARG A 324      32.674  67.431  22.494  1.00 10.68           N  
ANISOU 2578  N   ARG A 324     1693   1085   1279    -27   -250    272       N  
ATOM   2579  CA  ARG A 324      33.178  66.101  22.813  1.00 10.33           C  
ANISOU 2579  CA  ARG A 324     1627   1078   1220    -55   -235    237       C  
ATOM   2580  C   ARG A 324      34.699  66.054  22.719  1.00 10.74           C  
ANISOU 2580  C   ARG A 324     1718   1126   1236    -84   -161    217       C  
ATOM   2581  O   ARG A 324      35.377  65.488  23.586  1.00 10.86           O  
ANISOU 2581  O   ARG A 324     1690   1164   1272   -102   -121    185       O  
ATOM   2582  CB  ARG A 324      32.574  65.067  21.863  1.00 11.34           C  
ANISOU 2582  CB  ARG A 324     1783   1218   1307    -61   -307    245       C  
ATOM   2583  CG  ARG A 324      33.116  63.671  22.089  1.00 11.06           C  
ANISOU 2583  CG  ARG A 324     1736   1213   1252    -90   -288    209       C  
ATOM   2584  CD  ARG A 324      33.219  62.875  20.824  1.00 12.00           C  
ANISOU 2584  CD  ARG A 324     1938   1327   1295   -104   -324    212       C  
ATOM   2585  NE  ARG A 324      33.575  61.484  21.074  1.00 10.65           N  
ANISOU 2585  NE  ARG A 324     1752   1181   1114   -127   -311    179       N  
ATOM   2586  CZ  ARG A 324      33.778  60.590  20.110  1.00 10.75           C  
ANISOU 2586  CZ  ARG A 324     1840   1186   1058   -142   -330    171       C  
ATOM   2587  NH1 ARG A 324      33.691  60.939  18.840  1.00 11.92           N1+
ANISOU 2587  NH1 ARG A 324     2090   1305   1135   -137   -364    193       N1+
ATOM   2588  NH2 ARG A 324      34.077  59.341  20.433  1.00 11.03           N  
ANISOU 2588  NH2 ARG A 324     1857   1241   1093   -161   -313    141       N  
ATOM   2589  N   LEU A 325      35.260  66.629  21.653  1.00 10.92           N  
ANISOU 2589  N   LEU A 325     1823   1118   1211    -87   -140    240       N  
ATOM   2590  CA  LEU A 325      36.710  66.629  21.505  1.00 11.16           C  
ANISOU 2590  CA  LEU A 325     1881   1137   1222   -114    -60    228       C  
ATOM   2591  C   LEU A 325      37.361  67.456  22.597  1.00 11.17           C  
ANISOU 2591  C   LEU A 325     1830   1129   1285   -123    -10    212       C  
ATOM   2592  O   LEU A 325      38.407  67.081  23.128  1.00 12.13           O  
ANISOU 2592  O   LEU A 325     1921   1261   1426   -148     37    187       O  
ATOM   2593  CB  LEU A 325      37.123  67.100  20.116  1.00 11.13           C  
ANISOU 2593  CB  LEU A 325     1981   1094   1153   -113    -37    262       C  
ATOM   2594  CG  LEU A 325      37.037  66.014  19.052  1.00 13.29           C  
ANISOU 2594  CG  LEU A 325     2326   1375   1349   -115    -62    264       C  
ATOM   2595  CD1 LEU A 325      35.614  65.596  18.743  1.00 18.07           C  
ANISOU 2595  CD1 LEU A 325     2936   1994   1937    -97   -170    273       C  
ATOM   2596  CD2 LEU A 325      37.747  66.453  17.778  1.00 19.27           C  
ANISOU 2596  CD2 LEU A 325     3199   2088   2035   -115     -9    293       C  
ATOM   2597  N   TYR A 326      36.755  68.598  22.945  1.00 11.01           N  
ANISOU 2597  N   TYR A 326     1802   1083   1297   -103    -24    227       N  
ATOM   2598  CA  TYR A 326      37.258  69.395  24.060  1.00 11.08           C  
ANISOU 2598  CA  TYR A 326     1772   1077   1361   -113     13    205       C  
ATOM   2599  C   TYR A 326      37.247  68.593  25.359  1.00 10.18           C  
ANISOU 2599  C   TYR A 326     1588   1003   1279   -119      7    165       C  
ATOM   2600  O   TYR A 326      38.246  68.570  26.083  1.00 10.73           O  
ANISOU 2600  O   TYR A 326     1633   1074   1371   -145     40    138       O  
ATOM   2601  CB  TYR A 326      36.459  70.700  24.185  1.00 11.11           C  
ANISOU 2601  CB  TYR A 326     1789   1042   1392    -83     -1    228       C  
ATOM   2602  CG  TYR A 326      36.753  71.450  25.465  1.00 11.18           C  
ANISOU 2602  CG  TYR A 326     1763   1032   1452    -89     27    199       C  
ATOM   2603  CD1 TYR A 326      38.047  71.833  25.792  1.00 11.16           C  
ANISOU 2603  CD1 TYR A 326     1763   1009   1467   -127     74    179       C  
ATOM   2604  CD2 TYR A 326      35.742  71.751  26.360  1.00 11.59           C  
ANISOU 2604  CD2 TYR A 326     1783   1083   1538    -57      8    192       C  
ATOM   2605  CE1 TYR A 326      38.323  72.491  26.969  1.00 12.18           C  
ANISOU 2605  CE1 TYR A 326     1872   1118   1638   -136     87    148       C  
ATOM   2606  CE2 TYR A 326      36.003  72.405  27.546  1.00 11.27           C  
ANISOU 2606  CE2 TYR A 326     1729   1020   1531    -60     34    162       C  
ATOM   2607  CZ  TYR A 326      37.301  72.774  27.845  1.00 11.37           C  
ANISOU 2607  CZ  TYR A 326     1754   1013   1552   -102     67    138       C  
ATOM   2608  OH  TYR A 326      37.591  73.436  29.020  1.00 12.68           O  
ANISOU 2608  OH  TYR A 326     1918   1151   1747   -110     82    104       O  
ATOM   2609  N   TYR A 327      36.130  67.934  25.663  1.00 10.59           N  
ANISOU 2609  N   TYR A 327     1606   1082   1334    -96    -38    164       N  
ATOM   2610  CA  TYR A 327      36.050  67.101  26.858  1.00 10.10           C  
ANISOU 2610  CA  TYR A 327     1487   1054   1295    -99    -38    131       C  
ATOM   2611  C   TYR A 327      37.171  66.067  26.885  1.00  9.51           C  
ANISOU 2611  C   TYR A 327     1405   1006   1203   -130    -16    109       C  
ATOM   2612  O   TYR A 327      37.878  65.918  27.892  1.00 10.11           O  
ANISOU 2612  O   TYR A 327     1451   1091   1300   -144      5     80       O  
ATOM   2613  CB  TYR A 327      34.675  66.405  26.914  1.00 10.04           C  
ANISOU 2613  CB  TYR A 327     1447   1070   1300    -73    -85    142       C  
ATOM   2614  CG  TYR A 327      34.560  65.422  28.058  1.00  9.40           C  
ANISOU 2614  CG  TYR A 327     1314   1021   1237    -75    -78    114       C  
ATOM   2615  CD1 TYR A 327      34.144  65.840  29.317  1.00 10.58           C  
ANISOU 2615  CD1 TYR A 327     1434   1163   1422    -56    -58    100       C  
ATOM   2616  CD2 TYR A 327      34.897  64.093  27.892  1.00  9.12           C  
ANISOU 2616  CD2 TYR A 327     1269   1018   1180    -95    -84    101       C  
ATOM   2617  CE1 TYR A 327      34.064  64.956  30.379  1.00  9.77           C  
ANISOU 2617  CE1 TYR A 327     1299   1086   1328    -55    -45     77       C  
ATOM   2618  CE2 TYR A 327      34.815  63.202  28.949  1.00  9.46           C  
ANISOU 2618  CE2 TYR A 327     1271   1086   1238    -95    -75     78       C  
ATOM   2619  CZ  TYR A 327      34.407  63.634  30.179  1.00  8.42           C  
ANISOU 2619  CZ  TYR A 327     1115    948   1137    -75    -56     68       C  
ATOM   2620  OH  TYR A 327      34.355  62.716  31.213  1.00  9.32           O  
ANISOU 2620  OH  TYR A 327     1200   1083   1256    -74    -42     49       O  
ATOM   2621  N   LEU A 328      37.345  65.317  25.794  1.00  9.99           N  
ANISOU 2621  N   LEU A 328     1496   1076   1224   -138    -21    121       N  
ATOM   2622  CA  LEU A 328      38.349  64.260  25.779  1.00  9.84           C  
ANISOU 2622  CA  LEU A 328     1469   1078   1192   -161      6    102       C  
ATOM   2623  C   LEU A 328      39.750  64.821  25.897  1.00 10.94           C  
ANISOU 2623  C   LEU A 328     1608   1198   1353   -185     60     96       C  
ATOM   2624  O   LEU A 328      40.594  64.255  26.603  1.00 11.35           O  
ANISOU 2624  O   LEU A 328     1619   1266   1428   -201     78     74       O  
ATOM   2625  CB  LEU A 328      38.189  63.417  24.515  1.00 10.29           C  
ANISOU 2625  CB  LEU A 328     1575   1138   1195   -162     -6    116       C  
ATOM   2626  CG  LEU A 328      36.928  62.552  24.466  1.00  9.74           C  
ANISOU 2626  CG  LEU A 328     1494   1092   1116   -149    -67    116       C  
ATOM   2627  CD1 LEU A 328      36.790  61.912  23.109  1.00 11.73           C  
ANISOU 2627  CD1 LEU A 328     1816   1336   1306   -153    -89    129       C  
ATOM   2628  CD2 LEU A 328      36.960  61.471  25.541  1.00 10.78           C  
ANISOU 2628  CD2 LEU A 328     1565   1256   1274   -154    -65     88       C  
ATOM   2629  N   GLU A 329      40.020  65.936  25.218  1.00 11.05           N  
ANISOU 2629  N   GLU A 329     1662   1172   1364   -189     84    119       N  
ATOM   2630  CA  GLU A 329      41.327  66.574  25.326  1.00 12.66           C  
ANISOU 2630  CA  GLU A 329     1857   1349   1604   -216    136    116       C  
ATOM   2631  C   GLU A 329      41.561  67.060  26.749  1.00 13.29           C  
ANISOU 2631  C   GLU A 329     1885   1428   1735   -226    121     87       C  
ATOM   2632  O   GLU A 329      42.647  66.862  27.317  1.00 14.54           O  
ANISOU 2632  O   GLU A 329     2005   1589   1932   -252    138     69       O  
ATOM   2633  CB  GLU A 329      41.438  67.724  24.315  1.00 13.44           C  
ANISOU 2633  CB  GLU A 329     2017   1399   1691   -217    167    150       C  
ATOM   2634  CG  GLU A 329      42.860  68.208  24.080  1.00 14.86           C  
ANISOU 2634  CG  GLU A 329     2192   1545   1910   -250    235    157       C  
ATOM   2635  CD  GLU A 329      42.998  69.229  22.955  1.00 11.85           C  
ANISOU 2635  CD  GLU A 329     1882   1111   1511   -250    279    197       C  
ATOM   2636  OE1 GLU A 329      42.022  69.616  22.291  1.00 16.43           O  
ANISOU 2636  OE1 GLU A 329     2523   1680   2041   -222    252    221       O  
ATOM   2637  OE2 GLU A 329      44.146  69.713  22.765  1.00 18.97           O1-
ANISOU 2637  OE2 GLU A 329     2774   1978   2456   -279    344    206       O1-
ATOM   2638  N   TYR A 330      40.542  67.672  27.356  1.00 12.14           N  
ANISOU 2638  N   TYR A 330     1743   1277   1593   -204     88     83       N  
ATOM   2639  CA  TYR A 330      40.682  68.190  28.712  1.00 12.41           C  
ANISOU 2639  CA  TYR A 330     1751   1303   1663   -210     76     52       C  
ATOM   2640  C   TYR A 330      40.943  67.068  29.711  1.00 12.25           C  
ANISOU 2640  C   TYR A 330     1688   1323   1645   -214     58     23       C  
ATOM   2641  O   TYR A 330      41.813  67.188  30.596  1.00 12.71           O  
ANISOU 2641  O   TYR A 330     1723   1375   1730   -236     53     -2       O  
ATOM   2642  CB  TYR A 330      39.426  68.967  29.114  1.00 12.11           C  
ANISOU 2642  CB  TYR A 330     1731   1247   1622   -177     56     57       C  
ATOM   2643  CG  TYR A 330      39.648  69.770  30.362  1.00 11.76           C  
ANISOU 2643  CG  TYR A 330     1687   1177   1606   -183     55     26       C  
ATOM   2644  CD1 TYR A 330      39.435  69.228  31.615  1.00 11.91           C  
ANISOU 2644  CD1 TYR A 330     1687   1218   1622   -174     38     -5       C  
ATOM   2645  CD2 TYR A 330      40.118  71.065  30.287  1.00 11.90           C  
ANISOU 2645  CD2 TYR A 330     1732   1141   1648   -200     72     27       C  
ATOM   2646  CE1 TYR A 330      39.672  69.961  32.756  1.00 13.75           C  
ANISOU 2646  CE1 TYR A 330     1937   1420   1866   -179     33    -36       C  
ATOM   2647  CE2 TYR A 330      40.358  71.805  31.423  1.00 13.56           C  
ANISOU 2647  CE2 TYR A 330     1954   1320   1879   -209     65     -6       C  
ATOM   2648  CZ  TYR A 330      40.139  71.245  32.653  1.00 12.44           C  
ANISOU 2648  CZ  TYR A 330     1801   1200   1724   -199     43    -39       C  
ATOM   2649  OH  TYR A 330      40.380  71.964  33.799  1.00 15.20           O  
ANISOU 2649  OH  TYR A 330     2180   1514   2082   -207     32    -75       O  
ATOM   2650  N   VAL A 331      40.200  65.970  29.599  1.00 11.84           N  
ANISOU 2650  N   VAL A 331     1625   1308   1565   -193     42     26       N  
ATOM   2651  CA  VAL A 331      40.349  64.869  30.537  1.00 11.14           C  
ANISOU 2651  CA  VAL A 331     1503   1255   1476   -192     29      3       C  
ATOM   2652  C   VAL A 331      41.694  64.180  30.353  1.00 11.00           C  
ANISOU 2652  C   VAL A 331     1461   1248   1471   -219     45     -3       C  
ATOM   2653  O   VAL A 331      42.337  63.798  31.334  1.00 11.37           O  
ANISOU 2653  O   VAL A 331     1478   1306   1536   -228     32    -24       O  
ATOM   2654  CB  VAL A 331      39.167  63.888  30.403  1.00 12.19           C  
ANISOU 2654  CB  VAL A 331     1629   1417   1584   -167     11     11       C  
ATOM   2655  CG1 VAL A 331      39.405  62.643  31.235  1.00 12.44           C  
ANISOU 2655  CG1 VAL A 331     1631   1481   1613   -167      6     -8       C  
ATOM   2656  CG2 VAL A 331      37.872  64.559  30.830  1.00 12.28           C  
ANISOU 2656  CG2 VAL A 331     1647   1417   1604   -138     -1     18       C  
ATOM   2657  N   CYS A 332      42.140  63.992  29.106  1.00 10.86           N  
ANISOU 2657  N   CYS A 332     1457   1223   1445   -228     76     19       N  
ATOM   2658  CA  CYS A 332      43.434  63.339  28.901  1.00 10.94           C  
ANISOU 2658  CA  CYS A 332     1439   1238   1479   -249    105     18       C  
ATOM   2659  C   CYS A 332      44.586  64.200  29.411  1.00 11.52           C  
ANISOU 2659  C   CYS A 332     1482   1285   1612   -278    113     10       C  
ATOM   2660  O   CYS A 332      45.538  63.677  30.008  1.00 12.39           O  
ANISOU 2660  O   CYS A 332     1543   1405   1759   -292    108     -2       O  
ATOM   2661  CB  CYS A 332      43.633  62.951  27.442  1.00 11.39           C  
ANISOU 2661  CB  CYS A 332     1532   1288   1510   -248    149     43       C  
ATOM   2662  SG  CYS A 332      42.646  61.527  26.925  1.00 11.19           S  
ANISOU 2662  SG  CYS A 332     1533   1293   1424   -224    130     44       S  
ATOM   2663  N  ALYS A 333      44.519  65.513  29.190  0.65 11.40           N  
ANISOU 2663  N  ALYS A 333     1491   1231   1609   -288    121     18       N  
ATOM   2664  N  BLYS A 333      44.532  65.514  29.173  0.35 11.21           N  
ANISOU 2664  N  BLYS A 333     1467   1207   1585   -289    122     18       N  
ATOM   2665  CA ALYS A 333      45.559  66.398  29.705  0.65 12.36           C  
ANISOU 2665  CA ALYS A 333     1584   1320   1793   -323    121      8       C  
ATOM   2666  CA BLYS A 333      45.568  66.389  29.714  0.35 11.84           C  
ANISOU 2666  CA BLYS A 333     1517   1253   1727   -323    121      8       C  
ATOM   2667  C  ALYS A 333      45.565  66.406  31.230  0.65 12.83           C  
ANISOU 2667  C  ALYS A 333     1622   1388   1864   -326     62    -28       C  
ATOM   2668  C  BLYS A 333      45.568  66.348  31.238  0.35 11.37           C  
ANISOU 2668  C  BLYS A 333     1436   1206   1679   -325     62    -28       C  
ATOM   2669  O  ALYS A 333      46.637  66.395  31.852  0.65 15.11           O  
ANISOU 2669  O  ALYS A 333     1866   1670   2204   -354     41    -42       O  
ATOM   2670  O  BLYS A 333      46.631  66.249  31.869  0.35  9.62           O  
ANISOU 2670  O  BLYS A 333     1169    979   1506   -352     41    -42       O  
ATOM   2671  CB ALYS A 333      45.361  67.798  29.130  0.65 12.39           C  
ANISOU 2671  CB ALYS A 333     1630   1275   1805   -332    144     25       C  
ATOM   2672  CB BLYS A 333      45.379  67.822  29.213  0.35 13.60           C  
ANISOU 2672  CB BLYS A 333     1780   1427   1959   -333    141     22       C  
ATOM   2673  CG ALYS A 333      46.350  68.839  29.637  0.65 16.74           C  
ANISOU 2673  CG ALYS A 333     2155   1780   2425   -373    141     13       C  
ATOM   2674  CG BLYS A 333      46.427  68.798  29.762  0.35 13.04           C  
ANISOU 2674  CG BLYS A 333     1681   1313   1960   -375    137     10       C  
ATOM   2675  CD ALYS A 333      47.792  68.427  29.384  0.65 17.54           C  
ANISOU 2675  CD ALYS A 333     2194   1876   2594   -406    172     23       C  
ATOM   2676  CD BLYS A 333      46.171  70.244  29.337  0.35 16.69           C  
ANISOU 2676  CD BLYS A 333     2190   1720   2432   -384    158     24       C  
ATOM   2677  CE ALYS A 333      48.754  69.551  29.750  0.65 21.96           C  
ANISOU 2677  CE ALYS A 333     2724   2382   3237   -454    168     16       C  
ATOM   2678  CE BLYS A 333      47.207  71.197  29.932  0.35 21.43           C  
ANISOU 2678  CE BLYS A 333     2761   2272   3110   -433    147      7       C  
ATOM   2679  NZ ALYS A 333      50.146  69.056  29.928  0.65 31.37           N1+
ANISOU 2679  NZ ALYS A 333     3830   3573   4515   -487    173     18       N1+
ATOM   2680  NZ BLYS A 333      47.099  71.319  31.417  0.35 23.38           N1+
ANISOU 2680  NZ BLYS A 333     3003   2522   3358   -438     74    -39       N1+
ATOM   2681  N   ALA A 334      44.385  66.400  31.855  1.00 11.64           N  
ANISOU 2681  N   ALA A 334     1504   1252   1668   -296     34    -42       N  
ATOM   2682  CA  ALA A 334      44.316  66.337  33.306  1.00 12.16           C  
ANISOU 2682  CA  ALA A 334     1569   1323   1727   -293    -14    -75       C  
ATOM   2683  C   ALA A 334      44.848  65.008  33.815  1.00 12.04           C  
ANISOU 2683  C   ALA A 334     1514   1347   1712   -290    -34    -83       C  
ATOM   2684  O   ALA A 334      45.561  64.965  34.830  1.00 12.55           O  
ANISOU 2684  O   ALA A 334     1564   1409   1797   -305    -77   -105       O  
ATOM   2685  CB  ALA A 334      42.889  66.581  33.777  1.00 12.44           C  
ANISOU 2685  CB  ALA A 334     1649   1361   1718   -255    -19    -81       C  
ATOM   2686  N   ALA A 335      44.525  63.908  33.135  1.00 11.42           N  
ANISOU 2686  N   ALA A 335     1425   1303   1612   -272     -9    -65       N  
ATOM   2687  CA  ALA A 335      45.068  62.618  33.539  1.00 11.28           C  
ANISOU 2687  CA  ALA A 335     1372   1317   1598   -267    -22    -68       C  
ATOM   2688  C   ALA A 335      46.594  62.663  33.557  1.00 11.21           C  
ANISOU 2688  C   ALA A 335     1310   1295   1655   -298    -27    -67       C  
ATOM   2689  O   ALA A 335      47.235  62.240  34.531  1.00 11.93           O  
ANISOU 2689  O   ALA A 335     1372   1394   1765   -303    -71    -82       O  
ATOM   2690  CB  ALA A 335      44.559  61.528  32.595  1.00 11.59           C  
ANISOU 2690  CB  ALA A 335     1413   1382   1608   -248     12    -49       C  
ATOM   2691  N   LYS A 336      47.197  63.185  32.492  1.00 11.56           N  
ANISOU 2691  N   LYS A 336     1340   1314   1738   -319     19    -47       N  
ATOM   2692  CA  LYS A 336      48.650  63.323  32.453  1.00 12.02           C  
ANISOU 2692  CA  LYS A 336     1335   1352   1878   -351     24    -40       C  
ATOM   2693  C   LYS A 336      49.145  64.184  33.608  1.00 12.59           C  
ANISOU 2693  C   LYS A 336     1394   1401   1989   -379    -44    -66       C  
ATOM   2694  O   LYS A 336      50.114  63.832  34.298  1.00 13.51           O  
ANISOU 2694  O   LYS A 336     1456   1519   2158   -395    -88    -74       O  
ATOM   2695  CB  LYS A 336      49.065  63.918  31.107  1.00 13.82           C  
ANISOU 2695  CB  LYS A 336     1564   1548   2137   -368     98    -11       C  
ATOM   2696  CG  LYS A 336      50.551  64.175  30.956  1.00 15.85           C  
ANISOU 2696  CG  LYS A 336     1748   1776   2497   -403    120      3       C  
ATOM   2697  CD  LYS A 336      51.355  62.901  31.007  1.00 16.80           C  
ANISOU 2697  CD  LYS A 336     1806   1921   2657   -392    131     12       C  
ATOM   2698  CE  LYS A 336      52.817  63.153  30.672  1.00 19.74           C  
ANISOU 2698  CE  LYS A 336     2093   2259   3147   -424    169     35       C  
ATOM   2699  NZ  LYS A 336      53.615  61.919  30.878  1.00 37.70           N1+
ANISOU 2699  NZ  LYS A 336     4299   4556   5471   -407    172     46       N1+
ATOM   2700  N   ASP A 337      48.504  65.335  33.822  1.00 11.74           N  
ANISOU 2700  N   ASP A 337     1338   1266   1857   -386    -56    -80       N  
ATOM   2701  CA  ASP A 337      48.954  66.259  34.859  1.00 12.78           C  
ANISOU 2701  CA  ASP A 337     1473   1364   2020   -417   -120   -110       C  
ATOM   2702  C   ASP A 337      48.848  65.674  36.262  1.00 12.95           C  
ANISOU 2702  C   ASP A 337     1510   1408   2004   -402   -195   -139       C  
ATOM   2703  O   ASP A 337      49.599  66.084  37.159  1.00 14.94           O  
ANISOU 2703  O   ASP A 337     1751   1636   2290   -431   -265   -163       O  
ATOM   2704  CB  ASP A 337      48.139  67.548  34.798  1.00 13.93           C  
ANISOU 2704  CB  ASP A 337     1686   1472   2136   -418   -109   -119       C  
ATOM   2705  CG  ASP A 337      48.457  68.402  33.587  1.00 17.20           C  
ANISOU 2705  CG  ASP A 337     2092   1847   2595   -441    -48    -91       C  
ATOM   2706  OD1 ASP A 337      49.506  68.192  32.943  1.00 18.30           O  
ANISOU 2706  OD1 ASP A 337     2170   1980   2802   -467    -17    -68       O  
ATOM   2707  OD2 ASP A 337      47.646  69.308  33.297  1.00 18.88           O1-
ANISOU 2707  OD2 ASP A 337     2362   2034   2777   -431    -27    -88       O1-
ATOM   2708  N   TYR A 338      47.898  64.771  36.496  1.00 12.80           N  
ANISOU 2708  N   TYR A 338     1522   1426   1913   -359   -186   -139       N  
ATOM   2709  CA  TYR A 338      47.638  64.218  37.823  1.00 13.04           C  
ANISOU 2709  CA  TYR A 338     1585   1474   1895   -338   -243   -164       C  
ATOM   2710  C   TYR A 338      48.169  62.799  37.976  1.00 14.45           C  
ANISOU 2710  C   TYR A 338     1716   1692   2083   -323   -257   -151       C  
ATOM   2711  O   TYR A 338      47.869  62.138  38.981  1.00 18.81           O  
ANISOU 2711  O   TYR A 338     2300   2261   2586   -299   -294   -163       O  
ATOM   2712  CB  TYR A 338      46.148  64.301  38.164  1.00 13.11           C  
ANISOU 2712  CB  TYR A 338     1668   1490   1825   -299   -219   -172       C  
ATOM   2713  CG  TYR A 338      45.703  65.709  38.481  1.00 12.53           C  
ANISOU 2713  CG  TYR A 338     1653   1370   1739   -307   -223   -193       C  
ATOM   2714  CD1 TYR A 338      45.771  66.201  39.773  1.00 13.20           C  
ANISOU 2714  CD1 TYR A 338     1796   1428   1793   -310   -278   -229       C  
ATOM   2715  CD2 TYR A 338      45.242  66.570  37.479  1.00 13.65           C  
ANISOU 2715  CD2 TYR A 338     1800   1490   1896   -311   -173   -177       C  
ATOM   2716  CE1 TYR A 338      45.383  67.502  40.073  1.00 14.61           C  
ANISOU 2716  CE1 TYR A 338     2037   1557   1959   -316   -277   -251       C  
ATOM   2717  CE2 TYR A 338      44.851  67.864  37.771  1.00 14.22           C  
ANISOU 2717  CE2 TYR A 338     1927   1514   1961   -315   -174   -194       C  
ATOM   2718  CZ  TYR A 338      44.923  68.327  39.069  1.00 14.18           C  
ANISOU 2718  CZ  TYR A 338     1978   1480   1928   -318   -223   -232       C  
ATOM   2719  OH  TYR A 338      44.531  69.621  39.351  1.00 16.95           O  
ANISOU 2719  OH  TYR A 338     2393   1777   2271   -321   -218   -252       O  
ATOM   2720  N   GLY A 339      48.917  62.293  36.996  1.00 13.25           N  
ANISOU 2720  N   GLY A 339     1496   1549   1990   -334   -219   -123       N  
ATOM   2721  CA  GLY A 339      49.709  61.091  37.189  1.00 13.39           C  
ANISOU 2721  CA  GLY A 339     1458   1592   2039   -324   -236   -111       C  
ATOM   2722  C   GLY A 339      49.092  59.771  36.806  1.00 12.42           C  
ANISOU 2722  C   GLY A 339     1343   1505   1872   -285   -191    -94       C  
ATOM   2723  O   GLY A 339      49.601  58.728  37.233  1.00 13.53           O  
ANISOU 2723  O   GLY A 339     1452   1664   2024   -270   -213    -87       O  
ATOM   2724  N   MET A 340      48.038  59.758  35.987  1.00 11.44           N  
ANISOU 2724  N   MET A 340     1257   1389   1702   -270   -132    -87       N  
ATOM   2725  CA  MET A 340      47.312  58.525  35.683  1.00 10.64           C  
ANISOU 2725  CA  MET A 340     1170   1317   1556   -238    -99    -76       C  
ATOM   2726  C   MET A 340      47.174  58.315  34.180  1.00 10.55           C  
ANISOU 2726  C   MET A 340     1155   1304   1549   -239    -30    -54       C  
ATOM   2727  O   MET A 340      46.743  59.236  33.470  1.00 12.10           O  
ANISOU 2727  O   MET A 340     1378   1483   1738   -250     -5    -51       O  
ATOM   2728  CB  MET A 340      45.909  58.598  36.299  1.00 11.24           C  
ANISOU 2728  CB  MET A 340     1307   1400   1562   -216   -108    -89       C  
ATOM   2729  CG  MET A 340      45.922  58.636  37.816  1.00 11.89           C  
ANISOU 2729  CG  MET A 340     1417   1483   1619   -206   -165   -109       C  
ATOM   2730  SD  MET A 340      44.279  58.877  38.520  1.00 12.52           S  
ANISOU 2730  SD  MET A 340     1570   1561   1627   -177   -152   -120       S  
ATOM   2731  CE  MET A 340      44.093  60.648  38.276  1.00 13.42           C  
ANISOU 2731  CE  MET A 340     1708   1638   1752   -198   -151   -134       C  
ATOM   2732  N   PRO A 341      47.513  57.142  33.652  1.00 10.39           N  
ANISOU 2732  N   PRO A 341     1114   1296   1536   -225      4    -40       N  
ATOM   2733  CA  PRO A 341      47.240  56.871  32.230  1.00  9.65           C  
ANISOU 2733  CA  PRO A 341     1043   1197   1427   -222     68    -24       C  
ATOM   2734  C   PRO A 341      45.759  56.625  32.013  1.00  9.74           C  
ANISOU 2734  C   PRO A 341     1110   1222   1370   -207     65    -29       C  
ATOM   2735  O   PRO A 341      45.149  55.853  32.755  1.00 10.48           O  
ANISOU 2735  O   PRO A 341     1211   1335   1438   -189     41    -37       O  
ATOM   2736  CB  PRO A 341      48.046  55.599  31.939  1.00 10.97           C  
ANISOU 2736  CB  PRO A 341     1178   1370   1621   -208    101    -12       C  
ATOM   2737  CG  PRO A 341      48.265  54.955  33.262  1.00 15.78           C  
ANISOU 2737  CG  PRO A 341     1759   1997   2239   -195     46    -20       C  
ATOM   2738  CD  PRO A 341      48.271  56.047  34.299  1.00 10.20           C  
ANISOU 2738  CD  PRO A 341     1050   1286   1539   -211    -16    -36       C  
ATOM   2739  N   PRO A 342      45.152  57.269  30.998  1.00  9.70           N  
ANISOU 2739  N   PRO A 342     1143   1203   1340   -213     88    -21       N  
ATOM   2740  CA  PRO A 342      43.735  57.035  30.700  1.00  9.52           C  
ANISOU 2740  CA  PRO A 342     1162   1189   1265   -200     77    -21       C  
ATOM   2741  C   PRO A 342      43.546  56.013  29.594  1.00  9.56           C  
ANISOU 2741  C   PRO A 342     1196   1194   1241   -194    106    -12       C  
ATOM   2742  O   PRO A 342      44.296  56.004  28.608  1.00  9.79           O  
ANISOU 2742  O   PRO A 342     1240   1206   1275   -200    151     -1       O  
ATOM   2743  CB  PRO A 342      43.268  58.418  30.239  1.00 10.95           C  
ANISOU 2743  CB  PRO A 342     1369   1349   1440   -208     74    -15       C  
ATOM   2744  CG  PRO A 342      44.483  58.969  29.500  1.00 11.25           C  
ANISOU 2744  CG  PRO A 342     1400   1363   1510   -227    116     -3       C  
ATOM   2745  CD  PRO A 342      45.701  58.409  30.229  1.00 10.25           C  
ANISOU 2745  CD  PRO A 342     1217   1243   1433   -232    117     -9       C  
ATOM   2746  N   PHE A 343      42.514  55.168  29.741  1.00  8.78           N  
ANISOU 2746  N   PHE A 343     1112   1109   1114   -183     84    -17       N  
ATOM   2747  CA  PHE A 343      42.148  54.151  28.757  1.00  8.17           C  
ANISOU 2747  CA  PHE A 343     1073   1027   1003   -181     98    -15       C  
ATOM   2748  C   PHE A 343      40.751  54.462  28.230  1.00  8.21           C  
ANISOU 2748  C   PHE A 343     1112   1029    978   -183     62    -11       C  
ATOM   2749  O   PHE A 343      39.763  54.354  28.965  1.00  8.99           O  
ANISOU 2749  O   PHE A 343     1190   1141   1085   -177     29    -13       O  
ATOM   2750  CB  PHE A 343      42.168  52.750  29.378  1.00  8.70           C  
ANISOU 2750  CB  PHE A 343     1122   1107   1074   -171     98    -23       C  
ATOM   2751  CG  PHE A 343      43.558  52.203  29.627  1.00  8.08           C  
ANISOU 2751  CG  PHE A 343     1014   1027   1028   -164    133    -21       C  
ATOM   2752  CD1 PHE A 343      44.372  52.739  30.623  1.00  9.62           C  
ANISOU 2752  CD1 PHE A 343     1161   1230   1265   -163    122    -22       C  
ATOM   2753  CD2 PHE A 343      44.034  51.149  28.881  1.00  8.33           C  
ANISOU 2753  CD2 PHE A 343     1069   1046   1051   -158    174    -20       C  
ATOM   2754  CE1 PHE A 343      45.654  52.233  30.838  1.00  9.71           C  
ANISOU 2754  CE1 PHE A 343     1132   1238   1318   -156    145    -16       C  
ATOM   2755  CE2 PHE A 343      45.304  50.634  29.096  1.00  9.69           C  
ANISOU 2755  CE2 PHE A 343     1205   1214   1264   -147    211    -14       C  
ATOM   2756  CZ  PHE A 343      46.110  51.176  30.079  1.00  9.84           C  
ANISOU 2756  CZ  PHE A 343     1162   1243   1335   -146    193    -10       C  
ATOM   2757  N   TYR A 344      40.673  54.839  26.960  1.00  8.23           N  
ANISOU 2757  N   TYR A 344     1166   1012    948   -189     69     -1       N  
ATOM   2758  CA  TYR A 344      39.408  55.187  26.322  1.00  7.99           C  
ANISOU 2758  CA  TYR A 344     1170    976    891   -190     23      8       C  
ATOM   2759  C   TYR A 344      38.532  53.948  26.155  1.00  7.78           C  
ANISOU 2759  C   TYR A 344     1154    952    849   -193    -10      0       C  
ATOM   2760  O   TYR A 344      39.015  52.883  25.767  1.00  8.83           O  
ANISOU 2760  O   TYR A 344     1314   1079    962   -196     13    -10       O  
ATOM   2761  CB  TYR A 344      39.731  55.831  24.954  1.00  8.99           C  
ANISOU 2761  CB  TYR A 344     1366   1075    976   -194     41     22       C  
ATOM   2762  CG  TYR A 344      38.495  56.162  24.153  1.00  8.73           C  
ANISOU 2762  CG  TYR A 344     1376   1030    909   -193    -18     34       C  
ATOM   2763  CD1 TYR A 344      37.848  57.385  24.291  1.00  9.13           C  
ANISOU 2763  CD1 TYR A 344     1414   1078    977   -186    -49     50       C  
ATOM   2764  CD2 TYR A 344      37.926  55.214  23.303  1.00  8.97           C  
ANISOU 2764  CD2 TYR A 344     1461   1052    896   -200    -52     29       C  
ATOM   2765  CE1 TYR A 344      36.683  57.651  23.601  1.00  9.42           C  
ANISOU 2765  CE1 TYR A 344     1481   1104    993   -182   -112     65       C  
ATOM   2766  CE2 TYR A 344      36.758  55.473  22.627  1.00  9.18           C  
ANISOU 2766  CE2 TYR A 344     1521   1068    900   -201   -124     41       C  
ATOM   2767  CZ  TYR A 344      36.143  56.695  22.780  1.00  9.27           C  
ANISOU 2767  CZ  TYR A 344     1509   1079    936   -190   -155     62       C  
ATOM   2768  OH  TYR A 344      34.959  56.979  22.134  1.00 10.78           O  
ANISOU 2768  OH  TYR A 344     1723   1258   1115   -188   -235     79       O  
ATOM   2769  N   TRP A 345      37.232  54.089  26.435  1.00  7.98           N  
ANISOU 2769  N   TRP A 345     1158    984    892   -192    -63      5       N  
ATOM   2770  CA  TRP A 345      36.285  52.979  26.318  1.00  8.13           C  
ANISOU 2770  CA  TRP A 345     1175   1002    913   -201   -102      0       C  
ATOM   2771  C   TRP A 345      35.735  52.883  24.897  1.00  8.03           C  
ANISOU 2771  C   TRP A 345     1230    966    855   -213   -149      4       C  
ATOM   2772  O   TRP A 345      34.926  53.719  24.480  1.00  9.34           O  
ANISOU 2772  O   TRP A 345     1401   1126   1023   -211   -198     21       O  
ATOM   2773  CB  TRP A 345      35.122  53.153  27.305  1.00  8.89           C  
ANISOU 2773  CB  TRP A 345     1206   1110   1063   -194   -130      8       C  
ATOM   2774  CG  TRP A 345      34.116  52.044  27.175  1.00  8.89           C  
ANISOU 2774  CG  TRP A 345     1193   1103   1080   -208   -170      6       C  
ATOM   2775  CD1 TRP A 345      32.877  52.127  26.645  1.00  9.37           C  
ANISOU 2775  CD1 TRP A 345     1244   1152   1163   -217   -234     19       C  
ATOM   2776  CD2 TRP A 345      34.315  50.669  27.513  1.00  8.40           C  
ANISOU 2776  CD2 TRP A 345     1129   1041   1022   -217   -151     -8       C  
ATOM   2777  CE2 TRP A 345      33.142  49.973  27.166  1.00  9.19           C  
ANISOU 2777  CE2 TRP A 345     1219   1127   1147   -237   -205     -5       C  
ATOM   2778  CE3 TRP A 345      35.364  49.960  28.109  1.00  8.77           C  
ANISOU 2778  CE3 TRP A 345     1178   1096   1060   -210    -97    -20       C  
ATOM   2779  NE1 TRP A 345      32.273  50.891  26.636  1.00  9.61           N  
ANISOU 2779  NE1 TRP A 345     1263   1174   1213   -237   -259     12       N  
ATOM   2780  CZ2 TRP A 345      33.001  48.601  27.376  1.00 10.16           C  
ANISOU 2780  CZ2 TRP A 345     1339   1240   1282   -252   -200    -17       C  
ATOM   2781  CZ3 TRP A 345      35.226  48.602  28.302  1.00  9.48           C  
ANISOU 2781  CZ3 TRP A 345     1268   1176   1157   -220    -92    -29       C  
ATOM   2782  CH2 TRP A 345      34.054  47.940  27.943  1.00 10.45           C  
ANISOU 2782  CH2 TRP A 345     1386   1282   1301   -242   -140    -28       C  
ATOM   2783  N   ASP A 346      36.126  51.838  24.171  1.00  8.84           N  
ANISOU 2783  N   ASP A 346     1390   1053    915   -224   -140    -10       N  
ATOM   2784  CA  ASP A 346      35.691  51.638  22.782  1.00  9.12           C  
ANISOU 2784  CA  ASP A 346     1514   1060    891   -237   -188    -11       C  
ATOM   2785  C   ASP A 346      34.838  50.369  22.707  1.00  8.92           C  
ANISOU 2785  C   ASP A 346     1490   1024    874   -258   -241    -26       C  
ATOM   2786  O   ASP A 346      35.347  49.248  22.589  1.00  9.21           O  
ANISOU 2786  O   ASP A 346     1562   1049    890   -265   -210    -46       O  
ATOM   2787  CB  ASP A 346      36.886  51.581  21.829  1.00  9.50           C  
ANISOU 2787  CB  ASP A 346     1653   1086    872   -232   -127    -16       C  
ATOM   2788  CG  ASP A 346      36.483  51.621  20.376  1.00 10.11           C  
ANISOU 2788  CG  ASP A 346     1843   1129    870   -240   -174    -15       C  
ATOM   2789  OD1 ASP A 346      35.513  50.924  20.008  1.00 10.50           O  
ANISOU 2789  OD1 ASP A 346     1917   1166    908   -259   -252    -25       O  
ATOM   2790  OD2 ASP A 346      37.145  52.348  19.593  1.00 10.67           O1-
ANISOU 2790  OD2 ASP A 346     1983   1182    890   -230   -133     -2       O1-
ATOM   2791  N   ALA A 347      33.512  50.547  22.729  1.00  9.58           N  
ANISOU 2791  N   ALA A 347     1537   1108    996   -269   -324    -15       N  
ATOM   2792  CA  ALA A 347      32.583  49.430  22.658  1.00 10.18           C  
ANISOU 2792  CA  ALA A 347     1601   1169   1096   -295   -384    -26       C  
ATOM   2793  C   ALA A 347      32.383  48.939  21.234  1.00 10.34           C  
ANISOU 2793  C   ALA A 347     1734   1153   1043   -317   -448    -40       C  
ATOM   2794  O   ALA A 347      31.647  47.984  21.029  1.00 11.16           O  
ANISOU 2794  O   ALA A 347     1841   1236   1162   -345   -509    -53       O  
ATOM   2795  CB  ALA A 347      31.224  49.839  23.253  1.00 11.49           C  
ANISOU 2795  CB  ALA A 347     1671   1346   1349   -298   -445     -3       C  
ATOM   2796  N   GLY A 348      33.002  49.575  20.240  1.00 11.09           N  
ANISOU 2796  N   GLY A 348     1924   1233   1056   -305   -437    -37       N  
ATOM   2797  CA  GLY A 348      32.863  49.095  18.877  1.00 12.52           C  
ANISOU 2797  CA  GLY A 348     2234   1373   1149   -323   -494    -52       C  
ATOM   2798  C   GLY A 348      31.442  49.252  18.384  1.00 13.24           C  
ANISOU 2798  C   GLY A 348     2319   1451   1260   -345   -632    -41       C  
ATOM   2799  O   GLY A 348      30.774  50.269  18.619  1.00 13.29           O  
ANISOU 2799  O   GLY A 348     2259   1475   1316   -333   -676    -10       O  
ATOM   2800  N   GLY A 349      30.971  48.230  17.683  1.00 13.76           N  
ANISOU 2800  N   GLY A 349     2438   1484   1308   -366   -684    -59       N  
ATOM   2801  CA  GLY A 349      29.725  48.370  16.960  1.00 15.10           C  
ANISOU 2801  CA  GLY A 349     2600   1634   1502   -373   -793    -41       C  
ATOM   2802  C   GLY A 349      29.957  48.989  15.593  1.00 24.42           C  
ANISOU 2802  C   GLY A 349     3908   2785   2587   -356   -812    -31       C  
ATOM   2803  O   GLY A 349      31.075  49.009  15.070  1.00 35.09           O  
ANISOU 2803  O   GLY A 349     5362   4120   3848   -341   -733    -43       O  
ATOM   2804  N   ASP A 350      28.878  49.521  15.016  1.00 17.60           N  
ANISOU 2804  N   ASP A 350     3031   1909   1748   -355   -913     -8       N  
ATOM   2805  CA  ASP A 350      28.907  50.028  13.644  1.00 23.31           C  
ANISOU 2805  CA  ASP A 350     3878   2594   2383   -342   -948      2       C  
ATOM   2806  C   ASP A 350      29.083  51.537  13.555  1.00 32.67           C  
ANISOU 2806  C   ASP A 350     5067   3794   3554   -312   -938     34       C  
ATOM   2807  O   ASP A 350      29.045  52.087  12.449  1.00 47.11           O  
ANISOU 2807  O   ASP A 350     6993   5590   5315   -299   -968     46       O  
ATOM   2808  CB  ASP A 350      27.652  49.589  12.868  1.00 25.81           C  
ANISOU 2808  CB  ASP A 350     4205   2877   2724   -362  -1073      5       C  
ATOM   2809  CG  ASP A 350      26.372  50.227  13.390  1.00 20.23           C  
ANISOU 2809  CG  ASP A 350     3364   2191   2131   -362  -1159     37       C  
ATOM   2810  OD1 ASP A 350      26.427  51.116  14.259  1.00 20.79           O  
ANISOU 2810  OD1 ASP A 350     3344   2298   2256   -344  -1125     58       O  
ATOM   2811  OD2 ASP A 350      25.282  49.821  12.916  1.00 22.79           O1-
ANISOU 2811  OD2 ASP A 350     3671   2490   2496   -381  -1262     42       O1-
ATOM   2812  N   GLY A 351      29.273  52.220  14.678  1.00 26.59           N  
ANISOU 2812  N   GLY A 351     4196   3065   2841   -301   -896     49       N  
ATOM   2813  CA  GLY A 351      29.494  53.648  14.649  1.00 33.98           C  
ANISOU 2813  CA  GLY A 351     5136   4011   3763   -272   -880     80       C  
ATOM   2814  C   GLY A 351      28.302  54.475  14.235  1.00 34.88           C  
ANISOU 2814  C   GLY A 351     5216   4116   3922   -261   -983    114       C  
ATOM   2815  O   GLY A 351      28.481  55.612  13.794  1.00 45.42           O  
ANISOU 2815  O   GLY A 351     6595   5443   5220   -235   -978    140       O  
ATOM   2816  N   THR A 352      27.091  53.939  14.350  1.00 24.35           N  
ANISOU 2816  N   THR A 352     3802   2778   2670   -278  -1073    116       N  
ATOM   2817  CA  THR A 352      25.879  54.695  14.078  1.00 25.00           C  
ANISOU 2817  CA  THR A 352     3830   2852   2817   -267  -1170    150       C  
ATOM   2818  C   THR A 352      25.168  55.020  15.383  1.00 20.50           C  
ANISOU 2818  C   THR A 352     3092   2316   2382   -260  -1171    171       C  
ATOM   2819  O   THR A 352      25.498  54.494  16.448  1.00 21.82           O  
ANISOU 2819  O   THR A 352     3188   2510   2594   -271  -1110    156       O  
ATOM   2820  CB  THR A 352      24.919  53.907  13.176  1.00 23.73           C  
ANISOU 2820  CB  THR A 352     3700   2655   2663   -291  -1275    142       C  
ATOM   2821  CG2 THR A 352      25.623  53.451  11.909  1.00 27.23           C  
ANISOU 2821  CG2 THR A 352     4316   3058   2971   -297  -1268    118       C  
ATOM   2822  OG1 THR A 352      24.416  52.766  13.891  1.00 22.74           O  
ANISOU 2822  OG1 THR A 352     3483   2539   2620   -320  -1285    125       O  
ATOM   2823  N   GLY A 353      24.189  55.905  15.296  1.00 22.91           N  
ANISOU 2823  N   GLY A 353     3335   2616   2755   -240  -1235    208       N  
ATOM   2824  CA  GLY A 353      23.368  56.225  16.438  1.00 20.82           C  
ANISOU 2824  CA  GLY A 353     2910   2373   2628   -229  -1233    233       C  
ATOM   2825  C   GLY A 353      23.966  57.316  17.295  1.00 19.45           C  
ANISOU 2825  C   GLY A 353     2698   2225   2467   -195  -1158    253       C  
ATOM   2826  O   GLY A 353      24.971  57.954  16.956  1.00 23.07           O  
ANISOU 2826  O   GLY A 353     3252   2683   2829   -180  -1114    253       O  
ATOM   2827  N   THR A 354      23.323  57.526  18.439  1.00 19.99           N  
ANISOU 2827  N   THR A 354     2626   2311   2660   -182  -1135    272       N  
ATOM   2828  CA  THR A 354      23.624  58.649  19.313  1.00 19.46           C  
ANISOU 2828  CA  THR A 354     2505   2259   2629   -144  -1074    298       C  
ATOM   2829  C   THR A 354      24.433  58.255  20.538  1.00 17.05           C  
ANISOU 2829  C   THR A 354     2159   1983   2337   -150   -973    276       C  
ATOM   2830  O   THR A 354      24.654  59.097  21.416  1.00 18.29           O  
ANISOU 2830  O   THR A 354     2269   2150   2531   -117   -883    285       O  
ATOM   2831  CB  THR A 354      22.325  59.339  19.747  1.00 20.33           C  
ANISOU 2831  CB  THR A 354     2491   2361   2873   -114  -1099    338       C  
ATOM   2832  CG2 THR A 354      21.552  59.849  18.538  1.00 21.90           C  
ANISOU 2832  CG2 THR A 354     2731   2532   3059   -105  -1195    361       C  
ATOM   2833  OG1 THR A 354      21.513  58.415  20.484  1.00 23.96           O  
ANISOU 2833  OG1 THR A 354     2839   2825   3440   -134  -1090    332       O  
ATOM   2834  N   GLN A 355      24.874  57.000  20.628  1.00 17.68           N  
ANISOU 2834  N   GLN A 355     2262   2072   2384   -187   -953    237       N  
ATOM   2835  CA  GLN A 355      25.627  56.545  21.791  1.00 17.75           C  
ANISOU 2835  CA  GLN A 355     2236   2105   2403   -190   -828    208       C  
ATOM   2836  C   GLN A 355      26.803  55.683  21.362  1.00 15.52           C  
ANISOU 2836  C   GLN A 355     2059   1826   2013   -216   -790    167       C  
ATOM   2837  O   GLN A 355      27.087  54.646  21.977  1.00 17.66           O  
ANISOU 2837  O   GLN A 355     2305   2108   2297   -236   -743    141       O  
ATOM   2838  CB  GLN A 355      24.732  55.786  22.771  1.00 18.97           C  
ANISOU 2838  CB  GLN A 355     2267   2266   2676   -200   -821    211       C  
ATOM   2839  CG  GLN A 355      23.607  56.615  23.368  1.00 21.00           C  
ANISOU 2839  CG  GLN A 355     2407   2516   3055   -167   -830    253       C  
ATOM   2840  CD  GLN A 355      22.894  55.887  24.493  1.00 24.68           C  
ANISOU 2840  CD  GLN A 355     2755   2986   3636   -174   -785    256       C  
ATOM   2841  NE2 GLN A 355      21.987  54.987  24.133  1.00 23.67           N  
ANISOU 2841  NE2 GLN A 355     2590   2841   3562   -203   -847    259       N  
ATOM   2842  OE1 GLN A 355      23.162  56.125  25.672  1.00 27.54           O  
ANISOU 2842  OE1 GLN A 355     3079   3360   4024   -149   -673    253       O  
ATOM   2843  N   SER A 356      27.496  56.080  20.297  1.00 16.38           N  
ANISOU 2843  N   SER A 356     2287   1921   2016   -214   -803    165       N  
ATOM   2844  CA  SER A 356      28.589  55.285  19.759  1.00 16.75           C  
ANISOU 2844  CA  SER A 356     2441   1963   1962   -235   -762    131       C  
ATOM   2845  C   SER A 356      29.922  55.723  20.354  1.00 12.82           C  
ANISOU 2845  C   SER A 356     1956   1482   1434   -217   -632    119       C  
ATOM   2846  O   SER A 356      30.325  56.889  20.222  1.00 12.57           O  
ANISOU 2846  O   SER A 356     1948   1447   1383   -194   -599    138       O  
ATOM   2847  CB  SER A 356      28.668  55.371  18.240  1.00 19.64           C  
ANISOU 2847  CB  SER A 356     2945   2297   2221   -241   -835    134       C  
ATOM   2848  OG  SER A 356      29.801  54.638  17.791  1.00 18.04           O  
ANISOU 2848  OG  SER A 356     2846   2085   1924   -255   -770    102       O  
ATOM   2849  N   TRP A 357      30.611  54.771  20.980  1.00 11.04           N  
ANISOU 2849  N   TRP A 357     1423   1326   1448   -130   -128     59       N  
ATOM   2850  CA  TRP A 357      31.952  54.960  21.497  1.00 10.56           C  
ANISOU 2850  CA  TRP A 357     1420   1279   1314   -145   -121     58       C  
ATOM   2851  C   TRP A 357      33.022  54.576  20.486  1.00 10.67           C  
ANISOU 2851  C   TRP A 357     1435   1345   1273   -154   -168     64       C  
ATOM   2852  O   TRP A 357      34.208  54.765  20.750  1.00 11.46           O  
ANISOU 2852  O   TRP A 357     1563   1459   1333   -166   -169     67       O  
ATOM   2853  CB  TRP A 357      32.172  54.060  22.725  1.00 11.38           C  
ANISOU 2853  CB  TRP A 357     1564   1364   1397   -153    -78     36       C  
ATOM   2854  CG  TRP A 357      31.193  54.200  23.838  1.00 10.64           C  
ANISOU 2854  CG  TRP A 357     1490   1207   1344   -149     -6     24       C  
ATOM   2855  CD1 TRP A 357      30.004  53.548  23.972  1.00 13.10           C  
ANISOU 2855  CD1 TRP A 357     1764   1487   1725   -141     38     11       C  
ATOM   2856  CD2 TRP A 357      31.330  55.019  25.010  1.00 10.39           C  
ANISOU 2856  CD2 TRP A 357     1532   1126   1290   -157     44     21       C  
ATOM   2857  CE2 TRP A 357      30.181  54.814  25.801  1.00 11.59           C  
ANISOU 2857  CE2 TRP A 357     1694   1212   1496   -151    130      6       C  
ATOM   2858  CE3 TRP A 357      32.308  55.898  25.469  1.00 12.14           C  
ANISOU 2858  CE3 TRP A 357     1816   1345   1452   -175     26     26       C  
ATOM   2859  NE1 TRP A 357      29.389  53.918  25.139  1.00 12.84           N  
ANISOU 2859  NE1 TRP A 357     1774   1385   1720   -140    125      1       N  
ATOM   2860  CZ2 TRP A 357      29.978  55.457  27.010  1.00 12.54           C  
ANISOU 2860  CZ2 TRP A 357     1900   1263   1601   -159    209     -3       C  
ATOM   2861  CZ3 TRP A 357      32.106  56.527  26.687  1.00 12.65           C  
ANISOU 2861  CZ3 TRP A 357     1966   1344   1497   -187     88     15       C  
ATOM   2862  CH2 TRP A 357      30.947  56.311  27.435  1.00 12.91           C  
ANISOU 2862  CH2 TRP A 357     2023   1310   1574   -178    183      0       C  
ATOM   2863  N   ALA A 358      32.642  54.017  19.338  1.00 10.60           N  
ANISOU 2863  N   ALA A 358     1400   1360   1267   -152   -204     65       N  
ATOM   2864  CA  ALA A 358      33.615  53.358  18.477  1.00 11.32           C  
ANISOU 2864  CA  ALA A 358     1507   1489   1306   -162   -222     62       C  
ATOM   2865  C   ALA A 358      34.550  54.351  17.798  1.00  9.96           C  
ANISOU 2865  C   ALA A 358     1358   1328   1097   -169   -230     85       C  
ATOM   2866  O   ALA A 358      34.101  55.337  17.194  1.00 11.76           O  
ANISOU 2866  O   ALA A 358     1593   1546   1329   -164   -253    106       O  
ATOM   2867  CB  ALA A 358      32.875  52.566  17.395  1.00 13.19           C  
ANISOU 2867  CB  ALA A 358     1731   1737   1543   -166   -257     53       C  
ATOM   2868  N   LEU A 359      35.835  54.049  17.839  1.00 10.35           N  
ANISOU 2868  N   LEU A 359     1418   1393   1120   -180   -211     82       N  
ATOM   2869  CA  LEU A 359      36.855  54.714  17.034  1.00 10.53           C  
ANISOU 2869  CA  LEU A 359     1459   1425   1118   -192   -201     98       C  
ATOM   2870  C   LEU A 359      37.372  53.823  15.919  1.00 10.12           C  
ANISOU 2870  C   LEU A 359     1423   1388   1033   -197   -186     91       C  
ATOM   2871  O   LEU A 359      37.750  54.338  14.858  1.00 10.46           O  
ANISOU 2871  O   LEU A 359     1503   1429   1044   -207   -174    105       O  
ATOM   2872  CB  LEU A 359      38.033  55.151  17.907  1.00 11.09           C  
ANISOU 2872  CB  LEU A 359     1517   1492   1204   -205   -184     99       C  
ATOM   2873  CG  LEU A 359      37.687  56.061  19.083  1.00 11.87           C  
ANISOU 2873  CG  LEU A 359     1624   1566   1320   -209   -192    100       C  
ATOM   2874  CD1 LEU A 359      38.950  56.374  19.896  1.00 13.18           C  
ANISOU 2874  CD1 LEU A 359     1784   1730   1496   -231   -195     98       C  
ATOM   2875  CD2 LEU A 359      37.006  57.339  18.648  1.00 14.59           C  
ANISOU 2875  CD2 LEU A 359     1988   1889   1667   -206   -192    119       C  
ATOM   2876  N   PHE A 360      37.391  52.504  16.136  1.00 10.68           N  
ANISOU 2876  N   PHE A 360     1482   1466   1109   -192   -176     69       N  
ATOM   2877  CA  PHE A 360      37.853  51.549  15.147  1.00 10.69           C  
ANISOU 2877  CA  PHE A 360     1509   1472   1082   -197   -147     57       C  
ATOM   2878  C   PHE A 360      36.827  50.434  14.989  1.00  9.92           C  
ANISOU 2878  C   PHE A 360     1420   1374    976   -196   -167     33       C  
ATOM   2879  O   PHE A 360      36.169  50.035  15.964  1.00 10.97           O  
ANISOU 2879  O   PHE A 360     1523   1503   1144   -187   -179     23       O  
ATOM   2880  CB  PHE A 360      39.150  50.841  15.591  1.00 11.18           C  
ANISOU 2880  CB  PHE A 360     1540   1533   1174   -190   -100     52       C  
ATOM   2881  CG  PHE A 360      40.305  51.762  15.832  1.00 10.72           C  
ANISOU 2881  CG  PHE A 360     1454   1473   1147   -198    -82     71       C  
ATOM   2882  CD1 PHE A 360      40.473  52.363  17.064  1.00 11.46           C  
ANISOU 2882  CD1 PHE A 360     1515   1567   1272   -198   -116     79       C  
ATOM   2883  CD2 PHE A 360      41.224  52.017  14.840  1.00 11.92           C  
ANISOU 2883  CD2 PHE A 360     1619   1615   1295   -210    -27     78       C  
ATOM   2884  CE1 PHE A 360      41.531  53.219  17.297  1.00 12.14           C  
ANISOU 2884  CE1 PHE A 360     1572   1649   1393   -213   -110     92       C  
ATOM   2885  CE2 PHE A 360      42.292  52.868  15.067  1.00 11.99           C  
ANISOU 2885  CE2 PHE A 360     1590   1617   1350   -222     -7     92       C  
ATOM   2886  CZ  PHE A 360      42.443  53.464  16.303  1.00 12.15           C  
ANISOU 2886  CZ  PHE A 360     1567   1642   1408   -226    -56     99       C  
ATOM   2887  N   ASN A 361      36.728  49.891  13.780  1.00 10.10           N  
ANISOU 2887  N   ASN A 361     1493   1395    951   -210   -163     21       N  
ATOM   2888  CA  ASN A 361      36.107  48.582  13.615  1.00  9.85           C  
ANISOU 2888  CA  ASN A 361     1472   1356    913   -218   -166    -10       C  
ATOM   2889  C   ASN A 361      37.019  47.550  14.282  1.00 10.00           C  
ANISOU 2889  C   ASN A 361     1470   1369    962   -203   -104    -21       C  
ATOM   2890  O   ASN A 361      38.218  47.485  13.986  1.00 10.19           O  
ANISOU 2890  O   ASN A 361     1500   1387    985   -197    -49    -14       O  
ATOM   2891  CB  ASN A 361      35.912  48.282  12.128  1.00 11.22           C  
ANISOU 2891  CB  ASN A 361     1727   1522   1014   -244   -178    -23       C  
ATOM   2892  CG  ASN A 361      35.191  46.976  11.893  1.00 10.92           C  
ANISOU 2892  CG  ASN A 361     1707   1473    968   -262   -190    -60       C  
ATOM   2893  ND2 ASN A 361      33.979  47.044  11.377  1.00 14.62           N  
ANISOU 2893  ND2 ASN A 361     2189   1943   1424   -284   -274    -68       N  
ATOM   2894  OD1 ASN A 361      35.732  45.907  12.182  1.00 12.35           O  
ANISOU 2894  OD1 ASN A 361     1888   1642   1163   -257   -128    -80       O  
ATOM   2895  N   HIS A 362      36.466  46.757  15.219  1.00  9.54           N  
ANISOU 2895  N   HIS A 362     1382   1302    939   -194   -107    -35       N  
ATOM   2896  CA  HIS A 362      37.283  45.878  16.037  1.00  9.64           C  
ANISOU 2896  CA  HIS A 362     1375   1304    983   -172    -61    -36       C  
ATOM   2897  C   HIS A 362      37.845  44.688  15.270  1.00  9.66           C  
ANISOU 2897  C   HIS A 362     1412   1288    972   -173     -4    -55       C  
ATOM   2898  O   HIS A 362      38.732  44.003  15.790  1.00 10.22           O  
ANISOU 2898  O   HIS A 362     1463   1344   1077   -147     38    -48       O  
ATOM   2899  CB  HIS A 362      36.489  45.371  17.243  1.00  9.35           C  
ANISOU 2899  CB  HIS A 362     1321   1253    977   -163    -71    -42       C  
ATOM   2900  CG  HIS A 362      36.214  46.411  18.283  1.00  8.56           C  
ANISOU 2900  CG  HIS A 362     1199   1158    897   -157   -100    -23       C  
ATOM   2901  CD2 HIS A 362      36.294  47.766  18.279  1.00  9.48           C  
ANISOU 2901  CD2 HIS A 362     1305   1287   1010   -161   -128     -4       C  
ATOM   2902  ND1 HIS A 362      35.790  46.056  19.548  1.00  9.02           N  
ANISOU 2902  ND1 HIS A 362     1259   1193    976   -146    -91    -24       N  
ATOM   2903  CE1 HIS A 362      35.611  47.143  20.277  1.00  9.48           C  
ANISOU 2903  CE1 HIS A 362     1314   1250   1039   -146   -109     -9       C  
ATOM   2904  NE2 HIS A 362      35.910  48.195  19.531  1.00  9.15           N  
ANISOU 2904  NE2 HIS A 362     1260   1230    987   -154   -134      3       N  
ATOM   2905  N   ALA A 363      37.357  44.430  14.062  1.00 10.32           N  
ANISOU 2905  N   ALA A 363     1551   1366   1005   -201     -4    -79       N  
ATOM   2906  CA  ALA A 363      37.858  43.333  13.253  1.00 11.92           C  
ANISOU 2906  CA  ALA A 363     1806   1540   1183   -208     63   -103       C  
ATOM   2907  C   ALA A 363      38.749  43.787  12.108  1.00 12.41           C  
ANISOU 2907  C   ALA A 363     1919   1593   1203   -218    113    -98       C  
ATOM   2908  O   ALA A 363      39.756  43.130  11.815  1.00 14.22           O  
ANISOU 2908  O   ALA A 363     2161   1793   1449   -204    203   -102       O  
ATOM   2909  CB  ALA A 363      36.689  42.522  12.682  1.00 13.11           C  
ANISOU 2909  CB  ALA A 363     2009   1677   1297   -244     35   -143       C  
ATOM   2910  N   THR A 364      38.418  44.885  11.425  1.00 11.70           N  
ANISOU 2910  N   THR A 364     1864   1519   1064   -239     68    -86       N  
ATOM   2911  CA  THR A 364      39.261  45.337  10.319  1.00 12.06           C  
ANISOU 2911  CA  THR A 364     1976   1545   1062   -251    131    -80       C  
ATOM   2912  C   THR A 364      40.333  46.319  10.763  1.00 12.21           C  
ANISOU 2912  C   THR A 364     1931   1573   1137   -230    165    -45       C  
ATOM   2913  O   THR A 364      41.318  46.506  10.045  1.00 13.14           O  
ANISOU 2913  O   THR A 364     2081   1664   1250   -234    252    -40       O  
ATOM   2914  CB  THR A 364      38.426  46.033   9.236  1.00 12.43           C  
ANISOU 2914  CB  THR A 364     2116   1595   1014   -286     66    -80       C  
ATOM   2915  CG2 THR A 364      37.309  45.138   8.735  1.00 15.17           C  
ANISOU 2915  CG2 THR A 364     2523   1932   1307   -318      9   -117       C  
ATOM   2916  OG1 THR A 364      37.886  47.235   9.790  1.00 12.41           O  
ANISOU 2916  OG1 THR A 364     2056   1623   1035   -276    -17    -49       O  
ATOM   2917  N   GLY A 365      40.156  46.970  11.900  1.00 11.00           N  
ANISOU 2917  N   GLY A 365     1694   1448   1038   -212    104    -23       N  
ATOM   2918  CA  GLY A 365      41.071  47.997  12.335  1.00 12.05           C  
ANISOU 2918  CA  GLY A 365     1771   1588   1221   -203    118      6       C  
ATOM   2919  C   GLY A 365      40.901  49.342  11.665  1.00 10.76           C  
ANISOU 2919  C   GLY A 365     1650   1427   1010   -224     99     25       C  
ATOM   2920  O   GLY A 365      41.660  50.271  11.970  1.00 12.46           O  
ANISOU 2920  O   GLY A 365     1824   1644   1268   -224    116     46       O  
ATOM   2921  N   GLU A 366      39.918  49.489  10.777  1.00 11.18           N  
ANISOU 2921  N   GLU A 366     1787   1479    981   -243     58     19       N  
ATOM   2922  CA  GLU A 366      39.707  50.766  10.125  1.00 11.25           C  
ANISOU 2922  CA  GLU A 366     1849   1484    941   -257     32     44       C  
ATOM   2923  C   GLU A 366      39.155  51.785  11.104  1.00 10.51           C  
ANISOU 2923  C   GLU A 366     1689   1413    893   -244    -40     66       C  
ATOM   2924  O   GLU A 366      38.295  51.479  11.936  1.00 11.05           O  
ANISOU 2924  O   GLU A 366     1709   1498    992   -232    -99     58       O  
ATOM   2925  CB  GLU A 366      38.729  50.616   8.966  1.00 12.41           C  
ANISOU 2925  CB  GLU A 366     2106   1621    988   -278    -19     36       C  
ATOM   2926  CG  GLU A 366      39.278  49.797   7.818  1.00 14.34           C  
ANISOU 2926  CG  GLU A 366     2458   1830   1162   -300     63     13       C  
ATOM   2927  CD  GLU A 366      40.350  50.523   7.024  1.00 16.85           C  
ANISOU 2927  CD  GLU A 366     2843   2112   1448   -311    163     31       C  
ATOM   2928  OE1 GLU A 366      40.453  51.763   7.126  1.00 19.68           O  
ANISOU 2928  OE1 GLU A 366     3188   2473   1816   -308    146     64       O  
ATOM   2929  OE2 GLU A 366      41.093  49.848   6.278  1.00 23.84           O1-
ANISOU 2929  OE2 GLU A 366     3799   2957   2302   -325    272     11       O1-
ATOM   2930  N   MET A 367      39.639  53.019  10.994  1.00 11.20           N  
ANISOU 2930  N   MET A 367     1781   1490    982   -249    -23     93       N  
ATOM   2931  CA  MET A 367      39.068  54.119  11.754  1.00 11.46           C  
ANISOU 2931  CA  MET A 367     1775   1532   1046   -239    -82    114       C  
ATOM   2932  C   MET A 367      37.675  54.444  11.232  1.00 11.31           C  
ANISOU 2932  C   MET A 367     1801   1513    983   -234   -165    126       C  
ATOM   2933  O   MET A 367      37.422  54.402  10.028  1.00 12.72           O  
ANISOU 2933  O   MET A 367     2068   1678   1086   -246   -179    132       O  
ATOM   2934  CB  MET A 367      39.954  55.358  11.644  1.00 11.98           C  
ANISOU 2934  CB  MET A 367     1847   1580   1125   -252    -36    138       C  
ATOM   2935  CG  MET A 367      41.203  55.286  12.487  1.00 12.51           C  
ANISOU 2935  CG  MET A 367     1835   1648   1269   -257     14    130       C  
ATOM   2936  SD  MET A 367      42.157  56.796  12.326  1.00 14.28           S  
ANISOU 2936  SD  MET A 367     2060   1844   1520   -283     65    153       S  
ATOM   2937  CE  MET A 367      43.654  56.316  13.169  1.00 15.83           C  
ANISOU 2937  CE  MET A 367     2148   2043   1823   -292    109    139       C  
ATOM   2938  N   LEU A 368      36.782  54.787  12.152  1.00 11.05           N  
ANISOU 2938  N   LEU A 368     1710   1488   1000   -218   -221    130       N  
ATOM   2939  CA  LEU A 368      35.408  55.130  11.826  1.00 11.01           C  
ANISOU 2939  CA  LEU A 368     1715   1479    990   -206   -304    145       C  
ATOM   2940  C   LEU A 368      35.169  56.625  11.990  1.00 10.53           C  
ANISOU 2940  C   LEU A 368     1654   1398    950   -192   -320    182       C  
ATOM   2941  O   LEU A 368      35.624  57.232  12.964  1.00 10.60           O  
ANISOU 2941  O   LEU A 368     1622   1401   1004   -189   -281    184       O  
ATOM   2942  CB  LEU A 368      34.434  54.366  12.717  1.00 12.04           C  
ANISOU 2942  CB  LEU A 368     1774   1618   1182   -196   -338    122       C  
ATOM   2943  CG  LEU A 368      34.554  52.843  12.647  1.00 12.20           C  
ANISOU 2943  CG  LEU A 368     1794   1651   1191   -209   -320     85       C  
ATOM   2944  CD1 LEU A 368      33.543  52.178  13.581  1.00 14.54           C  
ANISOU 2944  CD1 LEU A 368     2023   1947   1555   -201   -342     64       C  
ATOM   2945  CD2 LEU A 368      34.376  52.348  11.233  1.00 14.07           C  
ANISOU 2945  CD2 LEU A 368     2112   1885   1350   -230   -352     78       C  
ATOM   2946  N   ASN A 369      34.427  57.213  11.055  1.00 11.19           N  
ANISOU 2946  N   ASN A 369     1789   1465    998   -184   -384    213       N  
ATOM   2947  CA  ASN A 369      33.986  58.609  11.150  1.00 11.47           C  
ANISOU 2947  CA  ASN A 369     1825   1473   1061   -161   -407    254       C  
ATOM   2948  C   ASN A 369      35.201  59.493  11.416  1.00 11.55           C  
ANISOU 2948  C   ASN A 369     1857   1468   1064   -174   -322    263       C  
ATOM   2949  O   ASN A 369      36.206  59.371  10.697  1.00 13.18           O  
ANISOU 2949  O   ASN A 369     2123   1672   1211   -198   -270    261       O  
ATOM   2950  CB  ASN A 369      32.859  58.691  12.173  1.00 11.89           C  
ANISOU 2950  CB  ASN A 369     1785   1520   1212   -135   -442    251       C  
ATOM   2951  CG  ASN A 369      31.701  57.780  11.822  1.00 11.39           C  
ANISOU 2951  CG  ASN A 369     1689   1468   1171   -130   -524    240       C  
ATOM   2952  ND2 ASN A 369      31.052  57.231  12.830  1.00 13.87           N  
ANISOU 2952  ND2 ASN A 369     1918   1784   1569   -123   -514    214       N  
ATOM   2953  OD1 ASN A 369      31.415  57.564  10.650  1.00 12.64           O  
ANISOU 2953  OD1 ASN A 369     1907   1629   1269   -138   -594    253       O  
ATOM   2954  N   ASN A 370      35.141  60.400  12.389  1.00 11.52           N  
ANISOU 2954  N   ASN A 370     1810   1446   1122   -164   -301    270       N  
ATOM   2955  CA  ASN A 370      36.206  61.349  12.685  1.00 11.93           C  
ANISOU 2955  CA  ASN A 370     1879   1477   1176   -184   -232    277       C  
ATOM   2956  C   ASN A 370      37.154  60.838  13.759  1.00 11.43           C  
ANISOU 2956  C   ASN A 370     1760   1434   1149   -208   -183    238       C  
ATOM   2957  O   ASN A 370      37.726  61.640  14.515  1.00 12.15           O  
ANISOU 2957  O   ASN A 370     1838   1507   1272   -224   -149    236       O  
ATOM   2958  CB  ASN A 370      35.606  62.692  13.110  1.00 12.55           C  
ANISOU 2958  CB  ASN A 370     1958   1514   1296   -163   -238    306       C  
ATOM   2959  CG  ASN A 370      34.804  62.585  14.390  1.00 11.25           C  
ANISOU 2959  CG  ASN A 370     1724   1346   1206   -145   -247    287       C  
ATOM   2960  ND2 ASN A 370      34.852  63.616  15.223  1.00 12.48           N  
ANISOU 2960  ND2 ASN A 370     1878   1463   1400   -146   -209    290       N  
ATOM   2961  OD1 ASN A 370      34.160  61.560  14.639  1.00 12.36           O  
ANISOU 2961  OD1 ASN A 370     1820   1511   1367   -135   -279    267       O  
ATOM   2962  N   ALA A 371      37.353  59.528  13.844  1.00 11.17           N  
ANISOU 2962  N   ALA A 371     1699   1434   1112   -212   -186    210       N  
ATOM   2963  CA  ALA A 371      38.204  58.982  14.887  1.00 11.20           C  
ANISOU 2963  CA  ALA A 371     1650   1454   1152   -228   -157    181       C  
ATOM   2964  C   ALA A 371      39.595  59.596  14.879  1.00 10.55           C  
ANISOU 2964  C   ALA A 371     1566   1360   1084   -259   -104    183       C  
ATOM   2965  O   ALA A 371      40.186  59.781  15.942  1.00 10.67           O  
ANISOU 2965  O   ALA A 371     1541   1374   1141   -275   -102    169       O  
ATOM   2966  CB  ALA A 371      38.324  57.464  14.745  1.00 12.03           C  
ANISOU 2966  CB  ALA A 371     1736   1588   1248   -224   -158    157       C  
ATOM   2967  N   GLN A 372      40.150  59.897  13.702  1.00 10.93           N  
ANISOU 2967  N   GLN A 372     1660   1393   1099   -271    -62    199       N  
ATOM   2968  CA  GLN A 372      41.499  60.454  13.662  1.00 11.35           C  
ANISOU 2968  CA  GLN A 372     1699   1428   1186   -305      3    199       C  
ATOM   2969  C   GLN A 372      41.587  61.728  14.493  1.00 10.71           C  
ANISOU 2969  C   GLN A 372     1607   1322   1140   -323     -4    204       C  
ATOM   2970  O   GLN A 372      42.560  61.945  15.231  1.00 11.59           O  
ANISOU 2970  O   GLN A 372     1667   1430   1306   -355      9    189       O  
ATOM   2971  CB  GLN A 372      41.920  60.741  12.223  1.00 13.02           C  
ANISOU 2971  CB  GLN A 372     1985   1613   1350   -317     68    218       C  
ATOM   2972  CG  GLN A 372      43.343  61.274  12.108  1.00 14.36           C  
ANISOU 2972  CG  GLN A 372     2130   1754   1573   -356    154    216       C  
ATOM   2973  CD  GLN A 372      44.371  60.220  12.455  1.00 13.73           C  
ANISOU 2973  CD  GLN A 372     1963   1693   1560   -365    186    190       C  
ATOM   2974  NE2 GLN A 372      45.043  60.380  13.582  1.00 15.35           N  
ANISOU 2974  NE2 GLN A 372     2077   1905   1849   -383    161    176       N  
ATOM   2975  OE1 GLN A 372      44.544  59.247  11.710  1.00 17.46           O  
ANISOU 2975  OE1 GLN A 372     2457   2168   2009   -354    228    183       O  
ATOM   2976  N   GLU A 373      40.577  62.591  14.383  1.00 11.06           N  
ANISOU 2976  N   GLU A 373     1700   1344   1158   -305    -28    227       N  
ATOM   2977  CA  GLU A 373      40.594  63.854  15.110  1.00 11.77           C  
ANISOU 2977  CA  GLU A 373     1797   1398   1278   -321    -21    231       C  
ATOM   2978  C   GLU A 373      40.464  63.623  16.609  1.00 11.90           C  
ANISOU 2978  C   GLU A 373     1768   1425   1330   -327    -56    201       C  
ATOM   2979  O   GLU A 373      41.085  64.341  17.410  1.00 12.11           O  
ANISOU 2979  O   GLU A 373     1788   1429   1386   -364    -47    187       O  
ATOM   2980  CB  GLU A 373      39.468  64.745  14.591  1.00 13.99           C  
ANISOU 2980  CB  GLU A 373     2139   1645   1531   -289    -35    267       C  
ATOM   2981  CG  GLU A 373      39.730  65.360  13.213  1.00 15.01           C  
ANISOU 2981  CG  GLU A 373     2344   1744   1614   -291      3    303       C  
ATOM   2982  CD  GLU A 373      39.741  64.371  12.049  1.00 34.45           C  
ANISOU 2982  CD  GLU A 373     4841   4230   4017   -281     -2    309       C  
ATOM   2983  OE1 GLU A 373      38.996  63.371  12.091  1.00 24.60           O  
ANISOU 2983  OE1 GLU A 373     3571   3019   2758   -256    -60    298       O  
ATOM   2984  OE2 GLU A 373      40.492  64.602  11.075  1.00 46.71           O1-
ANISOU 2984  OE2 GLU A 373     6455   5759   5533   -303     61    323       O1-
ATOM   2985  N   VAL A 374      39.659  62.637  17.000  1.00 11.62           N  
ANISOU 2985  N   VAL A 374     1711   1416   1287   -296    -95    190       N  
ATOM   2986  CA  VAL A 374      39.511  62.295  18.407  1.00 11.66           C  
ANISOU 2986  CA  VAL A 374     1695   1424   1311   -301   -120    164       C  
ATOM   2987  C   VAL A 374      40.825  61.766  18.972  1.00 11.34           C  
ANISOU 2987  C   VAL A 374     1613   1404   1292   -335   -130    143       C  
ATOM   2988  O   VAL A 374      41.274  62.171  20.054  1.00 11.65           O  
ANISOU 2988  O   VAL A 374     1655   1426   1345   -366   -149    126       O  
ATOM   2989  CB  VAL A 374      38.378  61.271  18.576  1.00 12.41           C  
ANISOU 2989  CB  VAL A 374     1778   1538   1400   -262   -146    158       C  
ATOM   2990  CG1 VAL A 374      38.297  60.811  20.028  1.00 14.27           C  
ANISOU 2990  CG1 VAL A 374     2009   1768   1643   -269   -158    132       C  
ATOM   2991  CG2 VAL A 374      37.048  61.864  18.137  1.00 15.87           C  
ANISOU 2991  CG2 VAL A 374     2236   1950   1843   -228   -149    181       C  
ATOM   2992  N   ILE A 375      41.448  60.829  18.258  1.00 10.87           N  
ANISOU 2992  N   ILE A 375     1517   1374   1238   -330   -121    144       N  
ATOM   2993  CA  ILE A 375      42.723  60.267  18.679  1.00 11.22           C  
ANISOU 2993  CA  ILE A 375     1503   1433   1325   -354   -131    130       C  
ATOM   2994  C   ILE A 375      43.771  61.360  18.803  1.00 10.93           C  
ANISOU 2994  C   ILE A 375     1450   1371   1332   -403   -117    130       C  
ATOM   2995  O   ILE A 375      44.540  61.394  19.769  1.00 11.61           O  
ANISOU 2995  O   ILE A 375     1500   1455   1456   -433   -160    115       O  
ATOM   2996  CB  ILE A 375      43.137  59.154  17.698  1.00 11.74           C  
ANISOU 2996  CB  ILE A 375     1540   1524   1398   -335    -99    134       C  
ATOM   2997  CG1 ILE A 375      42.150  57.986  17.785  1.00 11.64           C  
ANISOU 2997  CG1 ILE A 375     1540   1534   1350   -296   -123    127       C  
ATOM   2998  CG2 ILE A 375      44.551  58.705  17.971  1.00 12.81           C  
ANISOU 2998  CG2 ILE A 375     1599   1664   1605   -354    -96    127       C  
ATOM   2999  CD1 ILE A 375      42.193  57.032  16.611  1.00 13.09           C  
ANISOU 2999  CD1 ILE A 375     1728   1730   1515   -278    -84    128       C  
ATOM   3000  N   ASP A 376      43.791  62.289  17.845  1.00 11.09           N  
ANISOU 3000  N   ASP A 376     1502   1365   1345   -414    -61    146       N  
ATOM   3001  CA  ASP A 376      44.791  63.350  17.878  1.00 11.10           C  
ANISOU 3001  CA  ASP A 376     1487   1334   1395   -466    -33    144       C  
ATOM   3002  C   ASP A 376      44.674  64.208  19.125  1.00 10.93           C  
ANISOU 3002  C   ASP A 376     1489   1289   1377   -498    -79    126       C  
ATOM   3003  O   ASP A 376      45.688  64.592  19.699  1.00 12.02           O  
ANISOU 3003  O   ASP A 376     1587   1413   1568   -550   -101    110       O  
ATOM   3004  CB  ASP A 376      44.675  64.211  16.619  1.00 11.93           C  
ANISOU 3004  CB  ASP A 376     1648   1406   1477   -468     43    168       C  
ATOM   3005  CG  ASP A 376      45.204  63.510  15.380  1.00 12.88           C  
ANISOU 3005  CG  ASP A 376     1759   1535   1600   -458    108    179       C  
ATOM   3006  OD1 ASP A 376      45.867  62.455  15.516  1.00 16.71           O  
ANISOU 3006  OD1 ASP A 376     2175   2047   2129   -455    104    166       O  
ATOM   3007  OD2 ASP A 376      44.958  64.021  14.266  1.00 14.61           O1-
ANISOU 3007  OD2 ASP A 376     2050   1726   1773   -452    166    203       O1-
ATOM   3008  N   VAL A 377      43.452  64.535  19.562  1.00 10.31           N  
ANISOU 3008  N   VAL A 377     1476   1196   1245   -472    -93    128       N  
ATOM   3009  CA  VAL A 377      43.341  65.389  20.748  1.00 11.61           C  
ANISOU 3009  CA  VAL A 377     1683   1323   1404   -507   -118    108       C  
ATOM   3010  C   VAL A 377      43.718  64.634  22.021  1.00 10.92           C  
ANISOU 3010  C   VAL A 377     1578   1254   1316   -524   -193     82       C  
ATOM   3011  O   VAL A 377      44.264  65.222  22.953  1.00 12.14           O  
ANISOU 3011  O   VAL A 377     1753   1381   1477   -576   -231     60       O  
ATOM   3012  CB  VAL A 377      41.976  66.100  20.879  1.00 12.73           C  
ANISOU 3012  CB  VAL A 377     1901   1427   1508   -475    -90    118       C  
ATOM   3013  CG1 VAL A 377      41.669  66.929  19.639  1.00 17.48           C  
ANISOU 3013  CG1 VAL A 377     2529   2004   2110   -457    -32    151       C  
ATOM   3014  CG2 VAL A 377      40.863  65.123  21.183  1.00 16.71           C  
ANISOU 3014  CG2 VAL A 377     2410   1955   1985   -422   -109    118       C  
ATOM   3015  N   MET A 378      43.429  63.330  22.074  1.00 11.00           N  
ANISOU 3015  N   MET A 378     1561   1304   1313   -482   -219     85       N  
ATOM   3016  CA  MET A 378      43.825  62.544  23.242  1.00 11.77           C  
ANISOU 3016  CA  MET A 378     1653   1415   1406   -493   -293     68       C  
ATOM   3017  C   MET A 378      45.338  62.397  23.301  1.00 10.92           C  
ANISOU 3017  C   MET A 378     1462   1320   1366   -533   -341     65       C  
ATOM   3018  O   MET A 378      45.942  62.539  24.369  1.00 12.66           O  
ANISOU 3018  O   MET A 378     1692   1528   1591   -575   -419     50       O  
ATOM   3019  CB  MET A 378      43.126  61.174  23.234  1.00 10.60           C  
ANISOU 3019  CB  MET A 378     1498   1299   1232   -437   -298     75       C  
ATOM   3020  CG  MET A 378      41.617  61.284  23.369  1.00 11.93           C  
ANISOU 3020  CG  MET A 378     1732   1447   1353   -402   -258     75       C  
ATOM   3021  SD  MET A 378      40.768  59.772  23.841  1.00 11.85           S  
ANISOU 3021  SD  MET A 378     1731   1455   1314   -356   -267     71       S  
ATOM   3022  CE  MET A 378      41.121  58.730  22.423  1.00 12.37           C  
ANISOU 3022  CE  MET A 378     1715   1572   1412   -324   -254     88       C  
ATOM   3023  N   LYS A 379      45.972  62.159  22.149  1.00 12.12           N  
ANISOU 3023  N   LYS A 379     1537   1491   1577   -525   -295     80       N  
ATOM   3024  CA  LYS A 379      47.426  62.055  22.115  1.00 12.99           C  
ANISOU 3024  CA  LYS A 379     1548   1605   1783   -561   -323     79       C  
ATOM   3025  C   LYS A 379      48.082  63.363  22.531  1.00 13.22           C  
ANISOU 3025  C   LYS A 379     1579   1595   1848   -634   -343     63       C  
ATOM   3026  O   LYS A 379      49.122  63.364  23.196  1.00 14.87           O  
ANISOU 3026  O   LYS A 379     1726   1801   2124   -679   -422     53       O  
ATOM   3027  CB  LYS A 379      47.901  61.689  20.710  1.00 13.54           C  
ANISOU 3027  CB  LYS A 379     1551   1684   1908   -541   -233     96       C  
ATOM   3028  CG  LYS A 379      47.572  60.263  20.325  1.00 14.98           C  
ANISOU 3028  CG  LYS A 379     1717   1900   2074   -481   -221    107       C  
ATOM   3029  CD  LYS A 379      48.415  59.764  19.164  1.00 17.41           C  
ANISOU 3029  CD  LYS A 379     1952   2208   2456   -471   -138    117       C  
ATOM   3030  CE  LYS A 379      48.212  60.562  17.901  1.00 25.52           C  
ANISOU 3030  CE  LYS A 379     3028   3211   3458   -482    -33    125       C  
ATOM   3031  NZ  LYS A 379      49.065  60.007  16.807  1.00 24.14           N1+
ANISOU 3031  NZ  LYS A 379     2799   3024   3349   -475     65    133       N1+
ATOM   3032  N  AARG A 380      47.485  64.493  22.153  0.68 12.91           N  
ANISOU 3032  N  AARG A 380     1613   1523   1770   -649   -278     62       N  
ATOM   3033  N  BARG A 380      47.507  64.495  22.119  0.32 13.57           N  
ANISOU 3033  N  BARG A 380     1694   1606   1855   -649   -276     62       N  
ATOM   3034  CA AARG A 380      48.051  65.781  22.538  0.68 14.88           C  
ANISOU 3034  CA AARG A 380     1877   1726   2049   -723   -286     43       C  
ATOM   3035  CA BARG A 380      48.039  65.783  22.547  0.32 14.79           C  
ANISOU 3035  CA BARG A 380     1867   1716   2038   -722   -286     43       C  
ATOM   3036  C  AARG A 380      48.063  65.942  24.052  0.68 15.56           C  
ANISOU 3036  C  AARG A 380     2017   1797   2097   -763   -393     15       C  
ATOM   3037  C  BARG A 380      48.109  65.856  24.065  0.32 14.88           C  
ANISOU 3037  C  BARG A 380     1925   1715   2015   -761   -398     16       C  
ATOM   3038  O  AARG A 380      49.001  66.521  24.611  0.68 17.72           O  
ANISOU 3038  O  AARG A 380     2264   2048   2423   -835   -453     -6       O  
ATOM   3039  O  BARG A 380      49.124  66.267  24.637  0.32 18.99           O  
ANISOU 3039  O  BARG A 380     2405   2217   2592   -830   -468     -3       O  
ATOM   3040  CB AARG A 380      47.256  66.901  21.872  0.68 15.75           C  
ANISOU 3040  CB AARG A 380     2071   1797   2116   -718   -192     52       C  
ATOM   3041  CB BARG A 380      47.168  66.918  22.013  0.32 18.68           C  
ANISOU 3041  CB BARG A 380     2452   2168   2480   -718   -199     50       C  
ATOM   3042  CG AARG A 380      47.888  68.272  21.951  0.68 15.83           C  
ANISOU 3042  CG AARG A 380     2096   1752   2168   -793   -168     36       C  
ATOM   3043  CG BARG A 380      47.676  67.542  20.737  0.32 18.38           C  
ANISOU 3043  CG BARG A 380     2384   2108   2493   -733   -102     67       C  
ATOM   3044  CD AARG A 380      47.311  69.143  20.847  0.68 28.37           C  
ANISOU 3044  CD AARG A 380     3742   3304   3733   -773    -55     61       C  
ATOM   3045  CD BARG A 380      47.279  69.007  20.667  0.32 22.06           C  
ANISOU 3045  CD BARG A 380     2936   2511   2933   -763    -48     66       C  
ATOM   3046  NE AARG A 380      47.630  68.571  19.541  0.68 31.70           N  
ANISOU 3046  NE AARG A 380     4110   3750   4185   -740     11     89       N  
ATOM   3047  NE BARG A 380      45.836  69.211  20.769  0.32 16.40           N  
ANISOU 3047  NE BARG A 380     2318   1783   2131   -708    -32     79       N  
ATOM   3048  CZ AARG A 380      46.783  68.478  18.520  0.68 26.95           C  
ANISOU 3048  CZ AARG A 380     3563   3151   3526   -681     73    121       C  
ATOM   3049  CZ BARG A 380      44.991  69.113  19.747  0.32 16.52           C  
ANISOU 3049  CZ BARG A 380     2364   1803   2109   -645     23    114       C  
ATOM   3050  NH1AARG A 380      45.535  68.917  18.630  0.68 22.48           N1+
ANISOU 3050  NH1AARG A 380     3085   2568   2889   -642     73    134       N1+
ATOM   3051  NH2AARG A 380      47.191  67.929  17.384  0.68 29.22           N  
ANISOU 3051  NH2AARG A 380     3817   3452   3831   -662    133    141       N  
ATOM   3052  NH1BARG A 380      45.435  68.790  18.542  0.32 18.36           N1+
ANISOU 3052  NH1BARG A 380     2563   2052   2362   -632     73    138       N1+
ATOM   3053  NH2BARG A 380      43.698  69.333  19.937  0.32 13.93           N  
ANISOU 3053  NH2BARG A 380     2105   1459   1728   -597     27    126       N  
ATOM   3054  N   GLY A 381      47.046  65.420  24.740  1.00 15.48           N  
ANISOU 3054  N   GLY A 381     2090   1795   1998   -721   -417     13       N  
ATOM   3055  CA  GLY A 381      47.011  65.540  26.188  1.00 18.16           C  
ANISOU 3055  CA  GLY A 381     2512   2109   2280   -760   -507    -13       C  
ATOM   3056  C   GLY A 381      48.078  64.700  26.870  1.00 18.23           C  
ANISOU 3056  C   GLY A 381     2453   2144   2331   -781   -635    -14       C  
ATOM   3057  O   GLY A 381      48.611  65.089  27.907  1.00 19.34           O  
ANISOU 3057  O   GLY A 381     2633   2261   2455   -827   -719    -36       O  
ATOM   3058  N   ILE A 382      48.389  63.528  26.310  1.00 16.18           N  
ANISOU 3058  N   ILE A 382     2093   1931   2123   -728   -638     11       N  
ATOM   3059  CA  ILE A 382      49.323  62.608  26.957  1.00 17.08           C  
ANISOU 3059  CA  ILE A 382     2139   2067   2285   -732   -761     19       C  
ATOM   3060  C   ILE A 382      50.763  62.875  26.544  1.00 19.56           C  
ANISOU 3060  C   ILE A 382     2307   2384   2739   -763   -780     21       C  
ATOM   3061  O   ILE A 382      51.665  62.834  27.382  1.00 21.91           O  
ANISOU 3061  O   ILE A 382     2574   2680   3069   -773   -871     13       O  
ATOM   3062  CB  ILE A 382      48.929  61.148  26.651  1.00 16.50           C  
ANISOU 3062  CB  ILE A 382     2035   2033   2202   -649   -742     46       C  
ATOM   3063  CG1 ILE A 382      47.520  60.858  27.156  1.00 16.14           C  
ANISOU 3063  CG1 ILE A 382     2125   1979   2028   -610   -708     41       C  
ATOM   3064  CG2 ILE A 382      49.927  60.176  27.264  1.00 20.86           C  
ANISOU 3064  CG2 ILE A 382     2512   2602   2813   -632   -852     61       C  
ATOM   3065  CD1 ILE A 382      47.330  61.146  28.613  1.00 17.44           C  
ANISOU 3065  CD1 ILE A 382     2418   2107   2103   -645   -790     22       C  
ATOM   3066  N   PHE A 383      51.007  63.140  25.258  1.00 18.60           N  
ANISOU 3066  N   PHE A 383     2101   2264   2700   -770   -678     31       N  
ATOM   3067  CA  PHE A 383      52.357  63.150  24.720  1.00 20.85           C  
ANISOU 3067  CA  PHE A 383     2229   2548   3143   -796   -675     37       C  
ATOM   3068  C   PHE A 383      52.911  64.550  24.460  1.00 23.49           C  
ANISOU 3068  C   PHE A 383     2550   2843   3532   -868   -628     13       C  
ATOM   3069  O   PHE A 383      54.099  64.670  24.135  1.00 28.04           O  
ANISOU 3069  O   PHE A 383     3001   3414   4240   -889   -614      8       O  
ATOM   3070  CB  PHE A 383      52.409  62.325  23.424  1.00 19.32           C  
ANISOU 3070  CB  PHE A 383     1957   2377   3009   -735   -557     63       C  
ATOM   3071  CG  PHE A 383      51.924  60.894  23.579  1.00 18.23           C  
ANISOU 3071  CG  PHE A 383     1829   2275   2824   -657   -582     82       C  
ATOM   3072  CD1 PHE A 383      52.547  60.020  24.459  1.00 20.82           C  
ANISOU 3072  CD1 PHE A 383     2096   2615   3200   -644   -709     94       C  
ATOM   3073  CD2 PHE A 383      50.857  60.423  22.834  1.00 20.34           C  
ANISOU 3073  CD2 PHE A 383     2166   2559   3003   -597   -483     91       C  
ATOM   3074  CE1 PHE A 383      52.107  58.710  24.595  1.00 25.12           C  
ANISOU 3074  CE1 PHE A 383     2658   3184   3702   -572   -722    113       C  
ATOM   3075  CE2 PHE A 383      50.417  59.111  22.972  1.00 20.76           C  
ANISOU 3075  CE2 PHE A 383     2230   2639   3019   -532   -500    105       C  
ATOM   3076  CZ  PHE A 383      51.047  58.262  23.856  1.00 22.77           C  
ANISOU 3076  CZ  PHE A 383     2430   2902   3320   -519   -612    116       C  
ATOM   3077  N   THR A 384      52.107  65.603  24.610  1.00 20.70           N  
ANISOU 3077  N   THR A 384     2322   2456   3086   -906   -596     -4       N  
ATOM   3078  CA  THR A 384      52.531  66.971  24.315  1.00 33.07           C  
ANISOU 3078  CA  THR A 384     3891   3976   4698   -974   -537    -25       C  
ATOM   3079  C   THR A 384      52.515  67.810  25.585  1.00 35.40           C  
ANISOU 3079  C   THR A 384     4282   4244   4925  -1013   -617    -66       C  
ATOM   3080  O   THR A 384      51.556  67.756  26.361  1.00 43.79           O  
ANISOU 3080  O   THR A 384     5476   5303   5861   -992   -650    -71       O  
ATOM   3081  CB  THR A 384      51.591  67.612  23.272  1.00 23.61           C  
ANISOU 3081  CB  THR A 384     2777   2756   3439   -953   -390    -10       C  
ATOM   3082  CG2 THR A 384      51.958  69.071  23.019  1.00 44.56           C  
ANISOU 3082  CG2 THR A 384     5453   5348   6131  -1030   -328    -29       C  
ATOM   3083  OG1 THR A 384      51.667  66.879  22.040  1.00 37.60           O  
ANISOU 3083  OG1 THR A 384     4481   4554   5252   -894   -291     20       O  
ATOM   3084  N   VAL A 385      53.572  68.595  25.790  1.00 36.39           N  
ANISOU 3084  N   VAL A 385     4346   4345   5136  -1072   -635    -95       N  
ATOM   3085  CA  VAL A 385      53.657  69.457  26.967  1.00 45.00           C  
ANISOU 3085  CA  VAL A 385     5526   5404   6167  -1119   -709   -136       C  
ATOM   3086  C   VAL A 385      52.797  70.709  26.803  1.00 50.54           C  
ANISOU 3086  C   VAL A 385     6359   6046   6797  -1151   -616   -150       C  
ATOM   3087  O   VAL A 385      52.739  71.311  25.729  1.00 46.16           O  
ANISOU 3087  O   VAL A 385     5784   5463   6293  -1168   -500   -138       O  
ATOM   3088  CB  VAL A 385      55.113  69.852  27.293  1.00 45.99           C  
ANISOU 3088  CB  VAL A 385     5537   5525   6410  -1178   -771   -166       C  
ATOM   3089  CG1 VAL A 385      55.144  70.823  28.471  1.00 47.59           C  
ANISOU 3089  CG1 VAL A 385     5849   5689   6544  -1235   -843   -209       C  
ATOM   3090  CG2 VAL A 385      55.951  68.621  27.583  1.00 45.28           C  
ANISOU 3090  CG2 VAL A 385     5328   5488   6387  -1138   -871   -144       C  
ATOM   3091  OXT VAL A 385      52.152  71.157  27.753  1.00 53.09           O1-
ANISOU 3091  OXT VAL A 385     6820   6344   7010  -1157   -648   -169       O1-
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.