CNRS Nantes University UFIP UFIP
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***  mono  ***

elNémo ID: 20092409274177960

Job options:

ID        	=	 20092409274177960
JOBID     	=	 mono
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER mono

ATOM      1  N   PRO A   6       2.368   7.020  25.056  1.00 20.05           N  
ANISOU    1  N   PRO A   6     2604   2552   2459    -14     13    -20       N  
ATOM      2  CA  PRO A   6       3.731   6.644  25.515  1.00 19.12           C  
ANISOU    2  CA  PRO A   6     2459   2455   2349    -40    103    -16       C  
ATOM      3  C   PRO A   6       4.861   7.167  24.643  1.00 18.49           C  
ANISOU    3  C   PRO A   6     2420   2437   2166     71    120     -7       C  
ATOM      4  O   PRO A   6       4.654   7.328  23.470  1.00 21.84           O  
ANISOU    4  O   PRO A   6     2742   3189   2367    165    255    147       O  
ATOM      5  CB  PRO A   6       3.725   5.091  25.418  1.00 19.71           C  
ANISOU    5  CB  PRO A   6     2557   2437   2493      2    128    -44       C  
ATOM      6  CG  PRO A   6       2.214   4.690  25.618  1.00 20.73           C  
ANISOU    6  CG  PRO A   6     2689   2523   2665    -78     42     25       C  
ATOM      7  CD  PRO A   6       1.468   5.839  24.936  1.00 20.84           C  
ANISOU    7  CD  PRO A   6     2673   2677   2568     60      2    -34       C  
ATOM      8  N   GLN A   7       5.983   7.478  25.230  1.00 16.34           N  
ANISOU    8  N   GLN A   7     2191   2069   1946     69    279     18       N  
ATOM      9  CA  GLN A   7       7.185   7.845  24.515  1.00 14.61           C  
ANISOU    9  CA  GLN A   7     2003   1716   1831     20    187     39       C  
ATOM     10  C   GLN A   7       7.601   6.740  23.523  1.00 11.49           C  
ANISOU   10  C   GLN A   7     1650   1327   1388      4    267     75       C  
ATOM     11  O   GLN A   7       7.529   5.527  23.802  1.00 11.70           O  
ANISOU   11  O   GLN A   7     1675   1402   1366    -11    247    328       O  
ATOM     12  CB  GLN A   7       8.291   8.078  25.530  1.00 17.96           C  
ANISOU   12  CB  GLN A   7     2396   2217   2210      5     93     89       C  
ATOM     13  CG  GLN A   7       7.849   9.073  26.583  1.00 24.21           C  
ANISOU   13  CG  GLN A   7     3182   3065   2949     87     99    -86       C  
ATOM     14  CD  GLN A   7       8.752  10.241  26.694  1.00 31.07           C  
ANISOU   14  CD  GLN A   7     3928   3716   4158   -185     22    -42       C  
ATOM     15  NE2 GLN A   7       8.230  11.434  26.360  1.00 34.94           N  
ANISOU   15  NE2 GLN A   7     4412   4214   4649    133    -46    141       N  
ATOM     16  OE1 GLN A   7       9.931  10.088  27.078  1.00 35.92           O  
ANISOU   16  OE1 GLN A   7     4320   4584   4744     37   -151     55       O  
ATOM     17  N   VAL A   8       7.972   7.181  22.344  1.00  8.66           N  
ANISOU   17  N   VAL A   8     1176    976   1137    -46    299    130       N  
ATOM     18  CA  VAL A   8       8.351   6.291  21.271  1.00  8.23           C  
ANISOU   18  CA  VAL A   8     1139   1001    986    -94    130    134       C  
ATOM     19  C   VAL A   8       9.724   6.673  20.735  1.00  7.24           C  
ANISOU   19  C   VAL A   8     1039    867    844    -31    144    143       C  
ATOM     20  O   VAL A   8       9.930   7.816  20.305  1.00  7.96           O  
ANISOU   20  O   VAL A   8     1140    882   1003      0    221    391       O  
ATOM     21  CB  VAL A   8       7.319   6.317  20.119  1.00  9.11           C  
ANISOU   21  CB  VAL A   8     1162   1144   1156    -37     56    143       C  
ATOM     22  CG1 VAL A   8       7.728   5.321  19.026  1.00 11.60           C  
ANISOU   22  CG1 VAL A   8     1462   1541   1402    -41   -107     -8       C  
ATOM     23  CG2 VAL A   8       5.957   6.014  20.640  1.00 10.62           C  
ANISOU   23  CG2 VAL A   8     1349   1202   1485   -104     62     65       C  
ATOM     24  N   GLU A   9      10.673   5.733  20.777  1.00  6.58           N  
ANISOU   24  N   GLU A   9      903    725    868      7    223    167       N  
ATOM     25  CA  GLU A   9      12.027   5.991  20.311  1.00  8.43           C  
ANISOU   25  CA  GLU A   9     1108   1068   1027    -57    144    183       C  
ATOM     26  C   GLU A   9      12.548   4.847  19.490  1.00  7.45           C  
ANISOU   26  C   GLU A   9      813   1080    935    -21     94    147       C  
ATOM     27  O   GLU A   9      12.578   3.713  19.945  1.00  7.68           O  
ANISOU   27  O   GLU A   9     1099   1001    819   -111    199     26       O  
ATOM     28  CB  GLU A   9      12.976   6.184  21.495  1.00  9.72           C  
ANISOU   28  CB  GLU A   9     1237   1322   1134    -29    254     48       C  
ATOM     29  CG AGLU A   9      14.293   6.848  21.154  0.50 12.18           C  
ANISOU   29  CG AGLU A   9     1428   1560   1638    -12    123     74       C  
ATOM     30  CG BGLU A   9      12.667   7.396  22.353  0.50 13.35           C  
ANISOU   30  CG BGLU A   9     1702   1537   1831    -25     85      0       C  
ATOM     31  CD AGLU A   9      14.908   7.610  22.282  0.50 16.91           C  
ANISOU   31  CD AGLU A   9     1997   2321   2107   -190    -90    -97       C  
ATOM     32  CD BGLU A   9      13.566   7.617  23.548  0.50 17.57           C  
ANISOU   32  CD BGLU A   9     2251   2255   2167     -1    -79    -32       C  
ATOM     33  OE1AGLU A   9      14.806   7.149  23.451  0.50 20.25           O  
ANISOU   33  OE1AGLU A   9     2567   2735   2392   -198    -82     -4       O  
ATOM     34  OE2AGLU A   9      15.495   8.650  21.966  0.50 18.29           O1-
ANISOU   34  OE2AGLU A   9     2448   2039   2462      6   -125    -39       O1-
ATOM     35  OE1BGLU A   9      14.545   6.858  23.754  0.50 19.49           O  
ANISOU   35  OE1BGLU A   9     2464   2469   2471    -54    -79     44       O  
ATOM     36  OE2BGLU A   9      13.260   8.573  24.305  0.50 21.32           O1-
ANISOU   36  OE2BGLU A   9     2889   2678   2531     84      3   -150       O1-
ATOM     37  N   LEU A  10      12.925   5.163  18.256  1.00  5.80           N  
ANISOU   37  N   LEU A  10      612    836    755   -134     30    121       N  
ATOM     38  CA  LEU A  10      13.496   4.211  17.288  1.00  6.04           C  
ANISOU   38  CA  LEU A  10      697    846    750    -34     -4    102       C  
ATOM     39  C   LEU A  10      15.003   4.388  17.258  1.00  5.71           C  
ANISOU   39  C   LEU A  10      696    696    775     -8    -19    216       C  
ATOM     40  O   LEU A  10      15.467   5.511  17.010  1.00  7.98           O  
ANISOU   40  O   LEU A  10      750   1009   1272    -80     30    348       O  
ATOM     41  CB  LEU A  10      12.892   4.453  15.903  1.00  6.81           C  
ANISOU   41  CB  LEU A  10      780    984    825   -130    -10     66       C  
ATOM     42  CG  LEU A  10      13.392   3.543  14.805  1.00  7.71           C  
ANISOU   42  CG  LEU A  10      971   1181    776    -60    -17    -91       C  
ATOM     43  CD1 LEU A  10      12.952   2.107  15.006  1.00  8.83           C  
ANISOU   43  CD1 LEU A  10     1316   1136    901    -27     34   -164       C  
ATOM     44  CD2 LEU A  10      12.983   4.045  13.417  1.00  8.21           C  
ANISOU   44  CD2 LEU A  10      961   1245    912   -196     24    -96       C  
ATOM     45  N   PHE A  11      15.731   3.301  17.518  1.00  5.40           N  
ANISOU   45  N   PHE A  11      515    941    594     19     60     53       N  
ATOM     46  CA  PHE A  11      17.191   3.296  17.489  1.00  5.94           C  
ANISOU   46  CA  PHE A  11      731    843    683    -11     54     79       C  
ATOM     47  C   PHE A  11      17.606   2.532  16.236  1.00  6.52           C  
ANISOU   47  C   PHE A  11      782    909    785     -5      4     54       C  
ATOM     48  O   PHE A  11      17.170   1.391  15.993  1.00  7.28           O  
ANISOU   48  O   PHE A  11      943    892    929     71    120    114       O  
ATOM     49  CB  PHE A  11      17.695   2.577  18.766  1.00  6.57           C  
ANISOU   49  CB  PHE A  11      763    987    745    -40     43    113       C  
ATOM     50  CG  PHE A  11      17.474   3.331  20.016  1.00  8.56           C  
ANISOU   50  CG  PHE A  11      929   1357    964    -32     16    162       C  
ATOM     51  CD1 PHE A  11      18.496   4.111  20.540  1.00 10.36           C  
ANISOU   51  CD1 PHE A  11     1221   1601   1111    -10   -121    -12       C  
ATOM     52  CD2 PHE A  11      16.252   3.303  20.675  1.00  9.45           C  
ANISOU   52  CD2 PHE A  11      967   1497   1124      7     -6     38       C  
ATOM     53  CE1 PHE A  11      18.323   4.774  21.697  1.00 12.16           C  
ANISOU   53  CE1 PHE A  11     1323   1855   1440     98   -224   -113       C  
ATOM     54  CE2 PHE A  11      16.092   3.994  21.838  1.00 10.87           C  
ANISOU   54  CE2 PHE A  11     1054   1784   1292     27    104     -7       C  
ATOM     55  CZ  PHE A  11      17.112   4.729  22.336  1.00 12.37           C  
ANISOU   55  CZ  PHE A  11     1633   1909   1158     47    -34   -225       C  
ATOM     56  N   VAL A  12      18.469   3.157  15.453  1.00  6.08           N  
ANISOU   56  N   VAL A  12      748    762    799    -82     99     -8       N  
ATOM     57  CA  VAL A  12      18.912   2.662  14.179  1.00  6.51           C  
ANISOU   57  CA  VAL A  12      846    893    732   -119     51    -32       C  
ATOM     58  C   VAL A  12      20.419   2.722  14.049  1.00  6.57           C  
ANISOU   58  C   VAL A  12      847    951    697   -100    101    -17       C  
ATOM     59  O   VAL A  12      21.091   3.535  14.678  1.00  6.30           O  
ANISOU   59  O   VAL A  12      877    829    686    -91    -13    -56       O  
ATOM     60  CB  VAL A  12      18.229   3.404  13.003  1.00  6.52           C  
ANISOU   60  CB  VAL A  12      820   1076    580   -141     75     13       C  
ATOM     61  CG1 VAL A  12      16.752   3.283  13.133  1.00  9.45           C  
ANISOU   61  CG1 VAL A  12      999   1706    883     31    -33     63       C  
ATOM     62  CG2 VAL A  12      18.664   4.860  12.911  1.00  7.71           C  
ANISOU   62  CG2 VAL A  12     1031   1230    667    -34    -33    114       C  
ATOM     63  N   LYS A  13      20.966   1.835  13.239  1.00  7.31           N  
ANISOU   63  N   LYS A  13      856    968    951   -194     64   -125       N  
ATOM     64  CA  LYS A  13      22.414   1.820  13.015  1.00  7.83           C  
ANISOU   64  CA  LYS A  13      917   1074    982   -108     91   -143       C  
ATOM     65  C   LYS A  13      22.893   3.131  12.359  1.00  7.74           C  
ANISOU   65  C   LYS A  13      968   1084    888    -74    119   -176       C  
ATOM     66  O   LYS A  13      22.335   3.585  11.385  1.00  7.93           O  
ANISOU   66  O   LYS A  13      960   1215    836   -100    128   -197       O  
ATOM     67  CB  LYS A  13      22.780   0.611  12.148  1.00  9.67           C  
ANISOU   67  CB  LYS A  13     1148   1191   1333   -168    109   -185       C  
ATOM     68  CG  LYS A  13      24.272   0.450  11.957  1.00 11.20           C  
ANISOU   68  CG  LYS A  13     1370   1199   1684   -147    142   -178       C  
ATOM     69  CD  LYS A  13      24.706  -0.871  11.276  1.00 15.49           C  
ANISOU   69  CD  LYS A  13     1933   1650   2301     86    231   -285       C  
ATOM     70  CE  LYS A  13      26.235  -0.885  10.909  1.00 16.79           C  
ANISOU   70  CE  LYS A  13     2040   2095   2240     73    115   -223       C  
ATOM     71  NZ  LYS A  13      27.264  -0.882  12.027  1.00 20.33           N1+
ANISOU   71  NZ  LYS A  13     2653   2453   2617    208   -131   -210       N1+
ATOM     72  N   ALA A  14      23.952   3.714  12.913  1.00  7.03           N  
ANISOU   72  N   ALA A  14      953    848    869   -173    177   -156       N  
ATOM     73  CA  ALA A  14      24.582   4.895  12.325  1.00  7.07           C  
ANISOU   73  CA  ALA A  14      974    782    931    -57     21     21       C  
ATOM     74  C   ALA A  14      25.419   4.521  11.083  1.00  7.73           C  
ANISOU   74  C   ALA A  14     1015    888   1031    -77    117     11       C  
ATOM     75  O   ALA A  14      25.925   3.402  10.944  1.00  8.99           O  
ANISOU   75  O   ALA A  14     1290    912   1213   -122    190    151       O  
ATOM     76  CB  ALA A  14      25.481   5.540  13.380  1.00  6.63           C  
ANISOU   76  CB  ALA A  14      740    872    905     -9     35    -27       C  
ATOM     77  N   GLY A  15      25.634   5.505  10.237  1.00  6.84           N  
ANISOU   77  N   GLY A  15     1016    789    791   -123    131   -145       N  
ATOM     78  CA  GLY A  15      26.416   5.390   9.041  1.00  8.18           C  
ANISOU   78  CA  GLY A  15     1139    996    970   -138     92    -47       C  
ATOM     79  C   GLY A  15      27.890   5.630   9.304  1.00  7.43           C  
ANISOU   79  C   GLY A  15     1113    829    879   -156      2     10       C  
ATOM     80  O   GLY A  15      28.356   5.525  10.413  1.00  6.27           O  
ANISOU   80  O   GLY A  15      953    587    839   -168     27     48       O  
ATOM     81  N   SER A  16      28.604   5.933   8.244  1.00  8.03           N  
ANISOU   81  N   SER A  16     1179   1024    847    -79     38     13       N  
ATOM     82  CA  SER A  16      30.046   5.984   8.194  1.00  8.82           C  
ANISOU   82  CA  SER A  16     1215   1164    972     -2     59     22       C  
ATOM     83  C   SER A  16      30.676   6.906   9.204  1.00  8.36           C  
ANISOU   83  C   SER A  16     1092   1086    996     23    143    -80       C  
ATOM     84  O   SER A  16      31.807   6.662   9.600  1.00 11.56           O  
ANISOU   84  O   SER A  16     1433   1572   1385    171    -67   -302       O  
ATOM     85  CB  SER A  16      30.528   6.380   6.769  1.00 10.49           C  
ANISOU   85  CB  SER A  16     1529   1417   1039     -6     99    -64       C  
ATOM     86  OG  SER A  16      30.024   7.649   6.310  1.00 14.86           O  
ANISOU   86  OG  SER A  16     2520   1667   1459   -131     -9    166       O  
ATOM     87  N   ASP A  17      30.015   8.002   9.553  1.00  6.32           N  
ANISOU   87  N   ASP A  17      939    726    735    -40     24     -1       N  
ATOM     88  CA  ASP A  17      30.563   8.972  10.509  1.00  6.54           C  
ANISOU   88  CA  ASP A  17      916    620    948     -7     48     46       C  
ATOM     89  C   ASP A  17      30.108   8.774  11.955  1.00  5.57           C  
ANISOU   89  C   ASP A  17      847    484    785     90    -34     22       C  
ATOM     90  O   ASP A  17      30.413   9.560  12.819  1.00  6.86           O  
ANISOU   90  O   ASP A  17     1181    421   1003    -16    -59     62       O  
ATOM     91  CB  ASP A  17      30.267  10.398  10.042  1.00  6.73           C  
ANISOU   91  CB  ASP A  17     1103    631    821    -42    213    116       C  
ATOM     92  CG  ASP A  17      28.826  10.773  10.040  1.00  8.49           C  
ANISOU   92  CG  ASP A  17     1394    609   1220    145     83    -17       C  
ATOM     93  OD1 ASP A  17      27.921   9.977  10.394  1.00  7.53           O  
ANISOU   93  OD1 ASP A  17     1271    707    882    225    -47    161       O  
ATOM     94  OD2 ASP A  17      28.496  11.918   9.607  1.00 13.31           O1-
ANISOU   94  OD2 ASP A  17     1791   1013   2253    256     73    737       O1-
ATOM     95  N   GLY A  18      29.384   7.685  12.223  1.00  5.45           N  
ANISOU   95  N   GLY A  18      769    458    841    -22     17     16       N  
ATOM     96  CA  GLY A  18      28.881   7.403  13.539  1.00  5.82           C  
ANISOU   96  CA  GLY A  18      909    530    769    -34    -42     50       C  
ATOM     97  C   GLY A  18      27.721   8.277  13.997  1.00  6.81           C  
ANISOU   97  C   GLY A  18      949    789    848    -87     30      0       C  
ATOM     98  O   GLY A  18      27.337   8.179  15.131  1.00  7.49           O  
ANISOU   98  O   GLY A  18     1217    745    883    112    257    -83       O  
ATOM     99  N   ALA A  19      27.206   9.138  13.117  1.00  6.18           N  
ANISOU   99  N   ALA A  19      990    547    808     26     37    -44       N  
ATOM    100  CA  ALA A  19      26.178  10.116  13.470  1.00  6.62           C  
ANISOU  100  CA  ALA A  19     1037    570    906     70     31     25       C  
ATOM    101  C   ALA A  19      24.931  10.031  12.603  1.00  6.73           C  
ANISOU  101  C   ALA A  19     1042    567    947     62     80    -20       C  
ATOM    102  O   ALA A  19      23.798   9.965  13.116  1.00  7.80           O  
ANISOU  102  O   ALA A  19     1104    739   1119     89    113   -104       O  
ATOM    103  CB  ALA A  19      26.789  11.554  13.382  1.00  7.27           C  
ANISOU  103  CB  ALA A  19     1033    689   1039      8    135    -37       C  
ATOM    104  N   LYS A  20      25.092  10.048  11.280  1.00  6.85           N  
ANISOU  104  N   LYS A  20      890    766    947     30    -23    -84       N  
ATOM    105  CA  LYS A  20      23.926   9.957  10.393  1.00  8.07           C  
ANISOU  105  CA  LYS A  20     1117    918   1030     89    -88   -117       C  
ATOM    106  C   LYS A  20      23.320   8.552  10.386  1.00  8.26           C  
ANISOU  106  C   LYS A  20     1160    950   1027     75    -44   -186       C  
ATOM    107  O   LYS A  20      23.938   7.614  10.853  1.00  8.09           O  
ANISOU  107  O   LYS A  20     1138    828   1104      6   -121   -244       O  
ATOM    108  CB  LYS A  20      24.362  10.288   8.976  1.00  9.31           C  
ANISOU  108  CB  LYS A  20     1214   1026   1297   -107    -29    -21       C  
ATOM    109  CG  LYS A  20      25.248   9.226   8.400  1.00 12.39           C  
ANISOU  109  CG  LYS A  20     1546   1600   1560      9     34    -78       C  
ATOM    110  CD  LYS A  20      26.055   9.695   7.281  1.00 16.83           C  
ANISOU  110  CD  LYS A  20     2580   1841   1971     39    150     11       C  
ATOM    111  CE  LYS A  20      25.154  10.235   6.215  1.00 20.20           C  
ANISOU  111  CE  LYS A  20     2536   2793   2344     97   -113    -80       C  
ATOM    112  NZ  LYS A  20      25.949  10.794   5.056  1.00 25.24           N1+
ANISOU  112  NZ  LYS A  20     3631   3223   2735   -302     51      6       N1+
ATOM    113  N   ILE A  21      22.096   8.419   9.896  1.00  8.89           N  
ANISOU  113  N   ILE A  21     1218    816   1341    182   -122   -284       N  
ATOM    114  CA  ILE A  21      21.508   7.095   9.704  1.00  8.76           C  
ANISOU  114  CA  ILE A  21     1173   1124   1030     58     18   -185       C  
ATOM    115  C   ILE A  21      22.289   6.363   8.598  1.00  9.28           C  
ANISOU  115  C   ILE A  21     1196   1283   1043     18      2   -175       C  
ATOM    116  O   ILE A  21      22.556   6.893   7.550  1.00  9.79           O  
ANISOU  116  O   ILE A  21     1479   1149   1091    145   -190   -329       O  
ATOM    117  CB  ILE A  21      20.015   7.172   9.345  1.00  9.33           C  
ANISOU  117  CB  ILE A  21     1229   1300   1015    120      9   -117       C  
ATOM    118  CG1 ILE A  21      19.180   7.866  10.439  1.00  9.31           C  
ANISOU  118  CG1 ILE A  21     1449   1143    944     22     30     66       C  
ATOM    119  CG2 ILE A  21      19.461   5.775   9.092  1.00 10.82           C  
ANISOU  119  CG2 ILE A  21     1230   1674   1206    -32   -172    -73       C  
ATOM    120  CD1 ILE A  21      17.745   8.037  10.036  1.00 12.36           C  
ANISOU  120  CD1 ILE A  21     1494   1479   1723     37     -9    -31       C  
ATOM    121  N   GLY A  22      22.616   5.138   8.907  1.00  8.69           N  
ANISOU  121  N   GLY A  22     1178   1093   1030    -30     72   -214       N  
ATOM    122  CA  GLY A  22      23.264   4.240   7.970  1.00  7.55           C  
ANISOU  122  CA  GLY A  22      949    969    947      1     82    -45       C  
ATOM    123  C   GLY A  22      22.334   3.614   6.955  1.00  8.05           C  
ANISOU  123  C   GLY A  22     1027    932   1098    -85     68    -96       C  
ATOM    124  O   GLY A  22      21.115   3.556   7.151  1.00  9.41           O  
ANISOU  124  O   GLY A  22     1045   1343   1185     48    -29   -422       O  
ATOM    125  N   ASN A  23      22.901   3.129   5.872  1.00  8.21           N  
ANISOU  125  N   ASN A  23     1072   1098    950   -181    -23    121       N  
ATOM    126  CA  ASN A  23      22.173   2.306   4.947  1.00  8.22           C  
ANISOU  126  CA  ASN A  23     1050   1065   1008    -59    -86      3       C  
ATOM    127  C   ASN A  23      21.595   1.094   5.674  1.00  8.93           C  
ANISOU  127  C   ASN A  23     1295   1196    901    -86     10   -112       C  
ATOM    128  O   ASN A  23      22.315   0.374   6.357  1.00 11.56           O  
ANISOU  128  O   ASN A  23     1638   1309   1445   -160    -72    -57       O  
ATOM    129  CB  ASN A  23      23.123   1.759   3.886  1.00  9.39           C  
ANISOU  129  CB  ASN A  23     1186   1308   1074   -181     17    -77       C  
ATOM    130  CG  ASN A  23      22.414   0.853   2.906  1.00 12.96           C  
ANISOU  130  CG  ASN A  23     1585   1853   1484   -101     30    -61       C  
ATOM    131  ND2 ASN A  23      21.624   1.438   2.084  1.00 12.19           N  
ANISOU  131  ND2 ASN A  23     1420   2407    804   -499    -45    -52       N  
ATOM    132  OD1 ASN A  23      22.555  -0.377   2.970  1.00 15.59           O  
ANISOU  132  OD1 ASN A  23     1810   2040   2072   -184     25   -295       O  
ATOM    133  N   CYS A  24      20.314   0.922   5.589  1.00  9.33           N  
ANISOU  133  N   CYS A  24     1321   1170   1053    -40    -68   -155       N  
ATOM    134  CA  CYS A  24      19.627  -0.214   6.220  1.00 11.04           C  
ANISOU  134  CA  CYS A  24     1477   1407   1310    -18     -9     29       C  
ATOM    135  C   CYS A  24      18.165  -0.124   5.886  1.00  9.94           C  
ANISOU  135  C   CYS A  24     1274   1257   1242    -28     40    -60       C  
ATOM    136  O   CYS A  24      17.465   0.750   6.385  1.00 12.29           O  
ANISOU  136  O   CYS A  24     1470   1732   1468    -11     84   -184       O  
ATOM    137  CB  CYS A  24      19.713  -0.154   7.744  1.00 11.99           C  
ANISOU  137  CB  CYS A  24     1401   1690   1462     69   -112    -58       C  
ATOM    138  SG  CYS A  24      18.956  -1.535   8.622  1.00 18.50           S  
ANISOU  138  SG  CYS A  24     2942   2364   1721    316    541    556       S  
ATOM    139  N   PRO A  25      17.670  -0.989   5.022  1.00  8.49           N  
ANISOU  139  N   PRO A  25     1019   1165   1040     -9    -60     34       N  
ATOM    140  CA  PRO A  25      16.289  -0.867   4.619  1.00  9.36           C  
ANISOU  140  CA  PRO A  25     1062   1425   1066     61      0     40       C  
ATOM    141  C   PRO A  25      15.295  -1.103   5.738  1.00  9.12           C  
ANISOU  141  C   PRO A  25     1014   1374   1075     49     26    109       C  
ATOM    142  O   PRO A  25      14.175  -0.625   5.621  1.00  9.53           O  
ANISOU  142  O   PRO A  25     1025   1709    886    209    111     14       O  
ATOM    143  CB  PRO A  25      16.158  -1.854   3.478  1.00 10.80           C  
ANISOU  143  CB  PRO A  25     1292   1587   1221    101     80      2       C  
ATOM    144  CG  PRO A  25      17.226  -2.744   3.641  1.00  9.75           C  
ANISOU  144  CG  PRO A  25     1404   1193   1104    192   -144      8       C  
ATOM    145  CD  PRO A  25      18.334  -2.081   4.324  1.00  8.49           C  
ANISOU  145  CD  PRO A  25     1160   1218    845     20      0    110       C  
ATOM    146  N   PHE A  26      15.696  -1.800   6.792  1.00  8.44           N  
ANISOU  146  N   PHE A  26      889   1320    997     84     32    137       N  
ATOM    147  CA  PHE A  26      14.816  -2.014   7.951  1.00  8.98           C  
ANISOU  147  CA  PHE A  26     1016   1380   1012     83    -38    168       C  
ATOM    148  C   PHE A  26      14.646  -0.735   8.761  1.00  8.40           C  
ANISOU  148  C   PHE A  26      941   1446    803    139    -69    132       C  
ATOM    149  O   PHE A  26      13.514  -0.398   9.209  1.00  9.04           O  
ANISOU  149  O   PHE A  26      982   1758    692    207      1     91       O  
ATOM    150  CB  PHE A  26      15.425  -3.131   8.804  1.00 11.44           C  
ANISOU  150  CB  PHE A  26     1338   1566   1439     -4    -24    281       C  
ATOM    151  CG  PHE A  26      15.681  -4.380   7.992  1.00 16.69           C  
ANISOU  151  CG  PHE A  26     2145   1974   2222     -1    -13    131       C  
ATOM    152  CD1 PHE A  26      14.642  -5.218   7.716  1.00 22.34           C  
ANISOU  152  CD1 PHE A  26     2759   2681   3045   -170    -65   -217       C  
ATOM    153  CD2 PHE A  26      16.914  -4.608   7.324  1.00 21.40           C  
ANISOU  153  CD2 PHE A  26     2691   2449   2991    188     24    -62       C  
ATOM    154  CE1 PHE A  26      14.838  -6.340   6.904  1.00 26.03           C  
ANISOU  154  CE1 PHE A  26     3354   3053   3483     93     46   -294       C  
ATOM    155  CE2 PHE A  26      17.109  -5.701   6.505  1.00 24.34           C  
ANISOU  155  CE2 PHE A  26     3108   2928   3211     72     39    -74       C  
ATOM    156  CZ  PHE A  26      16.076  -6.565   6.298  1.00 26.28           C  
ANISOU  156  CZ  PHE A  26     3259   3257   3469    -90     -3   -244       C  
ATOM    157  N   SER A  27      15.727   0.016   8.905  1.00  9.27           N  
ANISOU  157  N   SER A  27     1239   1438    845    190   -119   -176       N  
ATOM    158  CA  SER A  27      15.652   1.281   9.610  1.00  9.75           C  
ANISOU  158  CA  SER A  27     1274   1374   1057    118    -24   -138       C  
ATOM    159  C   SER A  27      14.717   2.249   8.898  1.00  9.23           C  
ANISOU  159  C   SER A  27     1097   1495    916     84    -41   -215       C  
ATOM    160  O   SER A  27      13.849   2.878   9.523  1.00  9.57           O  
ANISOU  160  O   SER A  27     1193   1564    878    250   -109   -293       O  
ATOM    161  CB  SER A  27      17.025   1.920   9.537  1.00  9.44           C  
ANISOU  161  CB  SER A  27     1235   1230   1119    102   -217    -89       C  
ATOM    162  OG  SER A  27      17.964   1.199  10.250  1.00 10.28           O  
ANISOU  162  OG  SER A  27     1491   1125   1288      4   -177    144       O  
ATOM    163  N   GLN A  28      14.833   2.351   7.576  1.00  8.42           N  
ANISOU  163  N   GLN A  28      977   1349    874     59    -66   -137       N  
ATOM    164  CA  GLN A  28      14.003   3.267   6.842  1.00  7.78           C  
ANISOU  164  CA  GLN A  28     1036   1174    744    -68    -21   -131       C  
ATOM    165  C   GLN A  28      12.552   2.830   6.877  1.00  6.98           C  
ANISOU  165  C   GLN A  28      975   1065    610     61     13    -42       C  
ATOM    166  O   GLN A  28      11.665   3.665   7.026  1.00  7.30           O  
ANISOU  166  O   GLN A  28     1037   1125    608    152     81     14       O  
ATOM    167  CB  GLN A  28      14.540   3.440   5.416  1.00  7.69           C  
ANISOU  167  CB  GLN A  28     1034   1134    751   -148     24   -106       C  
ATOM    168  CG  GLN A  28      13.742   4.445   4.666  1.00  8.10           C  
ANISOU  168  CG  GLN A  28     1116   1027    933   -110      0   -196       C  
ATOM    169  CD  GLN A  28      14.234   4.772   3.274  1.00  9.21           C  
ANISOU  169  CD  GLN A  28     1431   1221    846      1    -29   -197       C  
ATOM    170  NE2 GLN A  28      13.576   5.715   2.624  1.00  8.06           N  
ANISOU  170  NE2 GLN A  28     1118   1228    713   -255    -32    -10       N  
ATOM    171  OE1 GLN A  28      15.176   4.151   2.779  1.00 10.09           O  
ANISOU  171  OE1 GLN A  28     1743   1072   1017    -72    262    -19       O  
ATOM    172  N   ARG A  29      12.306   1.514   6.751  1.00  5.72           N  
ANISOU  172  N   ARG A  29      758    842    570    124    -92    -38       N  
ATOM    173  CA  ARG A  29      10.958   1.013   6.849  1.00  6.79           C  
ANISOU  173  CA  ARG A  29      956    974    649     69    -44     -1       C  
ATOM    174  C   ARG A  29      10.251   1.484   8.104  1.00  6.69           C  
ANISOU  174  C   ARG A  29      864   1010    668    102     -7    -40       C  
ATOM    175  O   ARG A  29       9.122   1.972   8.070  1.00  6.70           O  
ANISOU  175  O   ARG A  29      928   1085    532    190    -42     44       O  
ATOM    176  CB  ARG A  29      11.001  -0.530   6.808  1.00  6.94           C  
ANISOU  176  CB  ARG A  29     1027   1016    592     56      0    -76       C  
ATOM    177  CG  ARG A  29       9.720  -1.265   6.982  1.00  7.74           C  
ANISOU  177  CG  ARG A  29     1235   1181    525     56     34     91       C  
ATOM    178  CD  ARG A  29      10.068  -2.785   6.942  1.00 10.00           C  
ANISOU  178  CD  ARG A  29     1407   1357   1033   -143   -402    444       C  
ATOM    179  NE  ARG A  29       8.963  -3.574   7.347  1.00 13.39           N  
ANISOU  179  NE  ARG A  29     1803   1835   1447     31     21    311       N  
ATOM    180  CZ  ARG A  29       9.033  -4.894   7.492  1.00 13.90           C  
ANISOU  180  CZ  ARG A  29     1937   1711   1633    -94     67    117       C  
ATOM    181  NH1 ARG A  29      10.159  -5.495   7.283  1.00 13.29           N1+
ANISOU  181  NH1 ARG A  29     2155   1523   1369      7   -219     11       N1+
ATOM    182  NH2 ARG A  29       7.985  -5.572   7.915  1.00 15.05           N  
ANISOU  182  NH2 ARG A  29     2008   1866   1845   -161     62    285       N  
ATOM    183  N   LEU A  30      10.868   1.307   9.262  1.00  6.89           N  
ANISOU  183  N   LEU A  30      904   1058    655    207    -16     43       N  
ATOM    184  CA  LEU A  30      10.258   1.653  10.528  1.00  7.13           C  
ANISOU  184  CA  LEU A  30      924   1131    651     45    -26     29       C  
ATOM    185  C   LEU A  30      10.104   3.171  10.696  1.00  7.22           C  
ANISOU  185  C   LEU A  30     1017   1110    616     43    -44    -80       C  
ATOM    186  O   LEU A  30       9.127   3.640  11.252  1.00  7.35           O  
ANISOU  186  O   LEU A  30      970   1052    769     93     -6    -41       O  
ATOM    187  CB  LEU A  30      11.027   1.052  11.688  1.00  7.00           C  
ANISOU  187  CB  LEU A  30      853   1187    620     60     85     45       C  
ATOM    188  CG  LEU A  30      10.993  -0.477  11.751  1.00  8.67           C  
ANISOU  188  CG  LEU A  30      986   1458    850     17   -171     -7       C  
ATOM    189  CD1 LEU A  30      11.835  -0.957  12.942  1.00  9.94           C  
ANISOU  189  CD1 LEU A  30     1269   1383   1122     85   -137    155       C  
ATOM    190  CD2 LEU A  30       9.607  -1.041  11.814  1.00  8.47           C  
ANISOU  190  CD2 LEU A  30     1155   1227    837    -81    -54     43       C  
ATOM    191  N   PHE A  31      11.082   3.946  10.212  1.00  6.89           N  
ANISOU  191  N   PHE A  31      827   1032    758    175     71    -56       N  
ATOM    192  CA  PHE A  31      10.978   5.414  10.203  1.00  7.45           C  
ANISOU  192  CA  PHE A  31      958   1072    798     21     28      1       C  
ATOM    193  C   PHE A  31       9.726   5.799   9.418  1.00  7.23           C  
ANISOU  193  C   PHE A  31      981   1076    690    -46     -5    -65       C  
ATOM    194  O   PHE A  31       8.928   6.665   9.880  1.00  7.43           O  
ANISOU  194  O   PHE A  31     1105   1024    691    -33    -48    -97       O  
ATOM    195  CB  PHE A  31      12.320   5.959   9.657  1.00  8.16           C  
ANISOU  195  CB  PHE A  31      969   1188    942    -25     -1    -93       C  
ATOM    196  CG  PHE A  31      12.583   7.440   9.856  1.00  7.55           C  
ANISOU  196  CG  PHE A  31      847   1178    843    -31    -55   -126       C  
ATOM    197  CD1 PHE A  31      13.873   7.902   9.535  1.00  8.00           C  
ANISOU  197  CD1 PHE A  31     1046   1186    807      0    100    -82       C  
ATOM    198  CD2 PHE A  31      11.629   8.350  10.289  1.00  7.78           C  
ANISOU  198  CD2 PHE A  31     1355   1243    356    -76     59   -108       C  
ATOM    199  CE1 PHE A  31      14.186   9.252   9.647  1.00  8.71           C  
ANISOU  199  CE1 PHE A  31      780   1326   1203    -54   -138     10       C  
ATOM    200  CE2 PHE A  31      11.985   9.717  10.423  1.00  7.72           C  
ANISOU  200  CE2 PHE A  31     1115   1189    628     52    121   -225       C  
ATOM    201  CZ  PHE A  31      13.265  10.152  10.083  1.00  7.73           C  
ANISOU  201  CZ  PHE A  31     1113   1061    763      9   -118    -45       C  
ATOM    202  N   MET A  32       9.558   5.204   8.224  1.00  6.40           N  
ANISOU  202  N   MET A  32      926    868    636     70    -24    -70       N  
ATOM    203  CA  MET A  32       8.382   5.486   7.419  1.00  7.08           C  
ANISOU  203  CA  MET A  32      933    981    774     63    -93    -22       C  
ATOM    204  C   MET A  32       7.064   5.120   8.134  1.00  6.64           C  
ANISOU  204  C   MET A  32      954    989    579     31    -67    -53       C  
ATOM    205  O   MET A  32       6.118   5.916   8.092  1.00  6.67           O  
ANISOU  205  O   MET A  32     1032    966    534     18    -55      3       O  
ATOM    206  CB  MET A  32       8.440   4.797   6.075  1.00  6.88           C  
ANISOU  206  CB  MET A  32      775   1045    794     87    -54   -137       C  
ATOM    207  CG  MET A  32       9.497   5.361   5.149  1.00  7.11           C  
ANISOU  207  CG  MET A  32      963   1039    697     96     22    -23       C  
ATOM    208  SD  MET A  32       9.539   4.552   3.521  1.00  7.94           S  
ANISOU  208  SD  MET A  32     1156   1177    684     69    140    -52       S  
ATOM    209  CE  MET A  32       7.933   5.033   2.854  1.00  9.17           C  
ANISOU  209  CE  MET A  32     1275   1402    805     90     49   -170       C  
ATOM    210  N   VAL A  33       7.017   3.953   8.788  1.00  5.95           N  
ANISOU  210  N   VAL A  33      723    877    660     17     38     -9       N  
ATOM    211  CA  VAL A  33       5.805   3.553   9.473  1.00  6.04           C  
ANISOU  211  CA  VAL A  33      804    932    557     20    -50     57       C  
ATOM    212  C   VAL A  33       5.441   4.595  10.559  1.00  5.96           C  
ANISOU  212  C   VAL A  33      738    999    526     24     15     13       C  
ATOM    213  O   VAL A  33       4.294   5.024  10.660  1.00  6.43           O  
ANISOU  213  O   VAL A  33      781   1093    568      9     87    -57       O  
ATOM    214  CB  VAL A  33       5.971   2.168  10.117  1.00  7.09           C  
ANISOU  214  CB  VAL A  33     1029    982    681    -32    -31    -10       C  
ATOM    215  CG1 VAL A  33       4.804   1.846  11.017  1.00  8.16           C  
ANISOU  215  CG1 VAL A  33     1024   1086    990     95     73     70       C  
ATOM    216  CG2 VAL A  33       6.124   1.064   9.016  1.00  7.43           C  
ANISOU  216  CG2 VAL A  33     1135   1049    638    -83    -53     33       C  
ATOM    217  N   LEU A  34       6.409   4.990  11.394  1.00  6.11           N  
ANISOU  217  N   LEU A  34      831    910    579     47     37    -46       N  
ATOM    218  CA  LEU A  34       6.184   5.955  12.463  1.00  6.34           C  
ANISOU  218  CA  LEU A  34      854    884    671    -45     47     64       C  
ATOM    219  C   LEU A  34       5.715   7.282  11.899  1.00  6.54           C  
ANISOU  219  C   LEU A  34      844    964    677    -57    -65     74       C  
ATOM    220  O   LEU A  34       4.782   7.895  12.448  1.00  7.03           O  
ANISOU  220  O   LEU A  34     1058   1054    557     71    -61     47       O  
ATOM    221  CB  LEU A  34       7.432   6.088  13.305  1.00  7.53           C  
ANISOU  221  CB  LEU A  34     1117    978    764    -67    -59    112       C  
ATOM    222  CG  LEU A  34       7.706   4.856  14.171  1.00  7.60           C  
ANISOU  222  CG  LEU A  34     1027   1130    730     36    101    120       C  
ATOM    223  CD1 LEU A  34       9.151   4.897  14.719  1.00  8.95           C  
ANISOU  223  CD1 LEU A  34     1125   1356    918     15     61     12       C  
ATOM    224  CD2 LEU A  34       6.710   4.759  15.328  1.00  8.26           C  
ANISOU  224  CD2 LEU A  34     1036   1079   1020    106     66    277       C  
ATOM    225  N   TRP A  35       6.370   7.753  10.844  1.00  6.20           N  
ANISOU  225  N   TRP A  35      897    953    504     89      1    -38       N  
ATOM    226  CA  TRP A  35       5.989   9.010  10.211  1.00  6.65           C  
ANISOU  226  CA  TRP A  35     1029    940    557    113      6    -77       C  
ATOM    227  C   TRP A  35       4.547   8.962   9.726  1.00  6.51           C  
ANISOU  227  C   TRP A  35      966    874    634     17    -11    -52       C  
ATOM    228  O   TRP A  35       3.706   9.837  10.063  1.00  6.43           O  
ANISOU  228  O   TRP A  35      881   1010    551     85    -84    -97       O  
ATOM    229  CB  TRP A  35       6.937   9.308   9.068  1.00  7.71           C  
ANISOU  229  CB  TRP A  35     1062   1157    708    -28      2    -52       C  
ATOM    230  CG  TRP A  35       6.897  10.706   8.515  1.00  7.70           C  
ANISOU  230  CG  TRP A  35     1265   1103    557     55     89   -175       C  
ATOM    231  CD1 TRP A  35       5.785  11.522   8.320  1.00  9.03           C  
ANISOU  231  CD1 TRP A  35     1216   1060   1154    -37    120   -136       C  
ATOM    232  CD2 TRP A  35       8.010  11.441   8.013  1.00  7.83           C  
ANISOU  232  CD2 TRP A  35     1263   1131    580    -24   -177   -192       C  
ATOM    233  CE2 TRP A  35       7.523  12.677   7.526  1.00  8.21           C  
ANISOU  233  CE2 TRP A  35     1096   1194    830    -14      2   -181       C  
ATOM    234  CE3 TRP A  35       9.374  11.159   7.872  1.00  7.81           C  
ANISOU  234  CE3 TRP A  35     1347   1148    472   -196   -125   -126       C  
ATOM    235  NE1 TRP A  35       6.172  12.715   7.749  1.00  8.09           N  
ANISOU  235  NE1 TRP A  35     1041   1217    816    -33     -4     16       N  
ATOM    236  CZ2 TRP A  35       8.359  13.638   6.984  1.00  8.74           C  
ANISOU  236  CZ2 TRP A  35     1572   1060    687    -13    215   -120       C  
ATOM    237  CZ3 TRP A  35      10.220  12.146   7.321  1.00  8.38           C  
ANISOU  237  CZ3 TRP A  35     1234   1242    706    -15    -74   -129       C  
ATOM    238  CH2 TRP A  35       9.708  13.368   6.910  1.00  9.65           C  
ANISOU  238  CH2 TRP A  35     1599    940   1127    -18    -93   -170       C  
ATOM    239  N   LEU A  36       4.186   7.883   9.031  1.00  5.94           N  
ANISOU  239  N   LEU A  36      955    761    538    100    -42     10       N  
ATOM    240  CA  LEU A  36       2.837   7.734   8.469  1.00  6.16           C  
ANISOU  240  CA  LEU A  36      924    839    577     16    -61     44       C  
ATOM    241  C   LEU A  36       1.744   7.603   9.535  1.00  6.57           C  
ANISOU  241  C   LEU A  36      897    960    640     81   -112    -49       C  
ATOM    242  O   LEU A  36       0.576   7.954   9.324  1.00  7.61           O  
ANISOU  242  O   LEU A  36      957   1253    681    103   -159    -67       O  
ATOM    243  CB  LEU A  36       2.780   6.573   7.472  1.00  6.77           C  
ANISOU  243  CB  LEU A  36      967    853    749     37     35     50       C  
ATOM    244  CG  LEU A  36       3.542   6.810   6.185  1.00  8.34           C  
ANISOU  244  CG  LEU A  36     1169   1185    814     67    -71   -119       C  
ATOM    245  CD1 LEU A  36       3.747   5.491   5.448  1.00  9.44           C  
ANISOU  245  CD1 LEU A  36     1516   1084    986    268     41    -62       C  
ATOM    246  CD2 LEU A  36       2.828   7.823   5.301  1.00  8.80           C  
ANISOU  246  CD2 LEU A  36     1281   1219    842     56     32     18       C  
ATOM    247  N   LYS A  37       2.104   7.072  10.708  1.00  6.78           N  
ANISOU  247  N   LYS A  37      986    972    618     63    -39    -65       N  
ATOM    248  CA  LYS A  37       1.129   6.976  11.787  1.00  7.07           C  
ANISOU  248  CA  LYS A  37      868   1057    759     36    -55    -12       C  
ATOM    249  C   LYS A  37       0.768   8.320  12.387  1.00  7.73           C  
ANISOU  249  C   LYS A  37     1066   1135    735    -22    -87     16       C  
ATOM    250  O   LYS A  37      -0.309   8.460  12.920  1.00  8.14           O  
ANISOU  250  O   LYS A  37     1062   1173    857     72      0   -140       O  
ATOM    251  CB  LYS A  37       1.631   6.043  12.900  1.00  7.50           C  
ANISOU  251  CB  LYS A  37      832   1279    737    -24    -90     -6       C  
ATOM    252  CG  LYS A  37       1.615   4.573  12.553  1.00  8.24           C  
ANISOU  252  CG  LYS A  37     1048   1243    839     10    -39    -25       C  
ATOM    253  CD  LYS A  37       0.170   4.019  12.430  1.00  6.90           C  
ANISOU  253  CD  LYS A  37      929   1026    666     72     76     43       C  
ATOM    254  CE  LYS A  37       0.139   2.483  12.252  1.00  7.72           C  
ANISOU  254  CE  LYS A  37      981   1145    807     34     -5    -54       C  
ATOM    255  NZ  LYS A  37      -1.261   1.954  12.175  1.00  7.29           N1+
ANISOU  255  NZ  LYS A  37      798   1092    879    -44   -149   -151       N1+
ATOM    256  N   GLY A  38       1.646   9.294  12.305  1.00  6.71           N  
ANISOU  256  N   GLY A  38      938    809    800     75    -89   -175       N  
ATOM    257  CA  GLY A  38       1.393  10.595  12.917  1.00  7.43           C  
ANISOU  257  CA  GLY A  38     1111    912    800     17    -55    -56       C  
ATOM    258  C   GLY A  38       1.718  10.710  14.396  1.00  8.43           C  
ANISOU  258  C   GLY A  38     1222   1113    868     57    -37    -44       C  
ATOM    259  O   GLY A  38       1.451  11.746  15.002  1.00  9.72           O  
ANISOU  259  O   GLY A  38     1777   1045    868    166     52     -3       O  
ATOM    260  N   VAL A  39       2.271   9.664  14.966  1.00  7.65           N  
ANISOU  260  N   VAL A  39     1119   1071    716     22    -48     -6       N  
ATOM    261  CA  VAL A  39       2.667   9.639  16.356  1.00  7.54           C  
ANISOU  261  CA  VAL A  39      993   1089    783     20    -63     -7       C  
ATOM    262  C   VAL A  39       3.918  10.538  16.553  1.00  7.75           C  
ANISOU  262  C   VAL A  39     1050   1103    791    -16     -5     73       C  
ATOM    263  O   VAL A  39       4.704  10.735  15.640  1.00  8.25           O  
ANISOU  263  O   VAL A  39     1057   1322    754    -71     99    141       O  
ATOM    264  CB  VAL A  39       2.982   8.169  16.776  1.00  8.63           C  
ANISOU  264  CB  VAL A  39     1153   1245    879     23    -42    155       C  
ATOM    265  CG1 VAL A  39       4.217   7.618  16.085  1.00  8.33           C  
ANISOU  265  CG1 VAL A  39     1060   1111    994     24   -123     99       C  
ATOM    266  CG2 VAL A  39       3.043   8.028  18.287  1.00  8.67           C  
ANISOU  266  CG2 VAL A  39     1124   1275    893     76    -49    -47       C  
ATOM    267  N   THR A  40       4.094  11.068  17.762  1.00  7.59           N  
ANISOU  267  N   THR A  40     1051   1075    755    -57     16     52       N  
ATOM    268  CA  THR A  40       5.323  11.768  18.120  1.00  8.63           C  
ANISOU  268  CA  THR A  40     1128   1179    972    -66      4     57       C  
ATOM    269  C   THR A  40       6.399  10.748  18.414  1.00  8.05           C  
ANISOU  269  C   THR A  40     1048   1131    879    -45     46     86       C  
ATOM    270  O   THR A  40       6.154   9.814  19.212  1.00  8.42           O  
ANISOU  270  O   THR A  40     1000   1224    971   -152    164    415       O  
ATOM    271  CB  THR A  40       5.077  12.638  19.350  1.00  8.62           C  
ANISOU  271  CB  THR A  40     1148   1094   1030   -117    114    105       C  
ATOM    272  CG2 THR A  40       6.312  13.425  19.746  1.00 10.27           C  
ANISOU  272  CG2 THR A  40     1249   1556   1097     -9     93   -283       C  
ATOM    273  OG1 THR A  40       4.043  13.572  19.051  1.00 12.30           O  
ANISOU  273  OG1 THR A  40     1465   1614   1592     93    -66   -146       O  
ATOM    274  N   PHE A  41       7.576  10.845  17.792  1.00  6.43           N  
ANISOU  274  N   PHE A  41      866    897    679    -61      5     60       N  
ATOM    275  CA  PHE A  41       8.633   9.863  18.008  1.00  7.30           C  
ANISOU  275  CA  PHE A  41     1046   1018    706    -77     26     69       C  
ATOM    276  C   PHE A  41      10.004  10.464  17.849  1.00  6.68           C  
ANISOU  276  C   PHE A  41      906    936    694    -27     20     29       C  
ATOM    277  O   PHE A  41      10.190  11.441  17.157  1.00  6.77           O  
ANISOU  277  O   PHE A  41      891   1075    606   -128    -51    214       O  
ATOM    278  CB  PHE A  41       8.470   8.640  17.061  1.00  6.87           C  
ANISOU  278  CB  PHE A  41      843    934    832    -94     -7     57       C  
ATOM    279  CG  PHE A  41       8.682   8.936  15.616  1.00  7.09           C  
ANISOU  279  CG  PHE A  41     1020    884    790   -141    -49     59       C  
ATOM    280  CD1 PHE A  41       9.855   8.601  15.000  1.00  8.00           C  
ANISOU  280  CD1 PHE A  41     1084   1150    806     56   -167     65       C  
ATOM    281  CD2 PHE A  41       7.709   9.591  14.866  1.00  6.78           C  
ANISOU  281  CD2 PHE A  41      889    956    729   -169     51     19       C  
ATOM    282  CE1 PHE A  41      10.064   8.930  13.640  1.00  7.34           C  
ANISOU  282  CE1 PHE A  41      819   1102    865    -43    140    -80       C  
ATOM    283  CE2 PHE A  41       7.910   9.855  13.529  1.00  7.88           C  
ANISOU  283  CE2 PHE A  41     1027   1192    774     94    -64    -77       C  
ATOM    284  CZ  PHE A  41       9.080   9.521  12.929  1.00  8.12           C  
ANISOU  284  CZ  PHE A  41      988   1181    914   -191    115    -35       C  
ATOM    285  N   ASN A  42      10.973   9.817  18.456  1.00  5.98           N  
ANISOU  285  N   ASN A  42      671    757    843   -120    123    169       N  
ATOM    286  CA  ASN A  42      12.382  10.121  18.295  1.00  6.84           C  
ANISOU  286  CA  ASN A  42      811    905    883    -22     98    168       C  
ATOM    287  C   ASN A  42      13.054   9.076  17.413  1.00  6.43           C  
ANISOU  287  C   ASN A  42      869    897    677      4     44    246       C  
ATOM    288  O   ASN A  42      12.759   7.867  17.540  1.00  7.99           O  
ANISOU  288  O   ASN A  42     1236    848    951    -78    216    218       O  
ATOM    289  CB  ASN A  42      13.138  10.075  19.625  1.00  8.64           C  
ANISOU  289  CB  ASN A  42      890   1327   1064    -20     34    283       C  
ATOM    290  CG  ASN A  42      12.767  11.088  20.647  1.00 11.98           C  
ANISOU  290  CG  ASN A  42     1798   1434   1319    -86    -11    310       C  
ATOM    291  ND2 ASN A  42      13.347  10.857  21.856  1.00 17.03           N  
ANISOU  291  ND2 ASN A  42     2638   2263   1570     -1   -155    269       N  
ATOM    292  OD1 ASN A  42      12.143  12.108  20.424  1.00 10.57           O  
ANISOU  292  OD1 ASN A  42     1447   1423   1143    190    -49    149       O  
ATOM    293  N   VAL A  43      14.020   9.500  16.595  1.00  5.19           N  
ANISOU  293  N   VAL A  43      769    681    519    -29     45    295       N  
ATOM    294  CA  VAL A  43      14.961   8.598  15.953  1.00  6.30           C  
ANISOU  294  CA  VAL A  43      900    804    687    -43     51    171       C  
ATOM    295  C   VAL A  43      16.368   8.951  16.432  1.00  6.95           C  
ANISOU  295  C   VAL A  43      872    904    862    -56    140    111       C  
ATOM    296  O   VAL A  43      16.754  10.114  16.387  1.00  8.43           O  
ANISOU  296  O   VAL A  43     1203    828   1171   -267    110    163       O  
ATOM    297  CB  VAL A  43      14.924   8.720  14.426  1.00  7.60           C  
ANISOU  297  CB  VAL A  43      992   1086    809    -55    123     89       C  
ATOM    298  CG1 VAL A  43      15.894   7.737  13.808  1.00  9.09           C  
ANISOU  298  CG1 VAL A  43     1365   1322    764     93    179     69       C  
ATOM    299  CG2 VAL A  43      13.518   8.533  13.901  1.00  8.55           C  
ANISOU  299  CG2 VAL A  43     1139   1222    887      8    164    -36       C  
ATOM    300  N   THR A  44      17.093   7.939  16.858  1.00  6.90           N  
ANISOU  300  N   THR A  44      709    958    953    -70    -11      9       N  
ATOM    301  CA  THR A  44      18.433   8.073  17.390  1.00  8.61           C  
ANISOU  301  CA  THR A  44      911   1103   1255     -9     -1   -115       C  
ATOM    302  C   THR A  44      19.339   7.074  16.707  1.00  7.81           C  
ANISOU  302  C   THR A  44      877   1059   1030     19    -66   -121       C  
ATOM    303  O   THR A  44      18.967   5.909  16.570  1.00  8.16           O  
ANISOU  303  O   THR A  44      953   1064   1081   -263    153   -157       O  
ATOM    304  CB  THR A  44      18.431   7.735  18.942  1.00 10.65           C  
ANISOU  304  CB  THR A  44     1002   1701   1342     29   -138   -371       C  
ATOM    305  CG2 THR A  44      19.838   7.846  19.497  1.00 15.38           C  
ANISOU  305  CG2 THR A  44     1699   2236   1908     77   -233    -31       C  
ATOM    306  OG1 THR A  44      17.628   8.756  19.590  1.00 17.42           O  
ANISOU  306  OG1 THR A  44     1850   2630   2136    354    -99   -402       O  
ATOM    307  N   THR A  45      20.542   7.486  16.364  1.00  7.10           N  
ANISOU  307  N   THR A  45      979    822    895    -19     25   -103       N  
ATOM    308  CA  THR A  45      21.490   6.568  15.755  1.00  7.24           C  
ANISOU  308  CA  THR A  45      874    774   1102    -57     22    -83       C  
ATOM    309  C   THR A  45      22.456   5.957  16.757  1.00  7.89           C  
ANISOU  309  C   THR A  45      936    986   1075    -17     27    -52       C  
ATOM    310  O   THR A  45      22.776   6.523  17.789  1.00  8.54           O  
ANISOU  310  O   THR A  45     1088   1024   1131    -15   -101     42       O  
ATOM    311  CB  THR A  45      22.245   7.264  14.632  1.00  7.54           C  
ANISOU  311  CB  THR A  45     1041    901    921      0     65   -113       C  
ATOM    312  CG2 THR A  45      21.310   7.790  13.579  1.00  8.66           C  
ANISOU  312  CG2 THR A  45     1072   1002   1213   -219    175     70       C  
ATOM    313  OG1 THR A  45      22.971   8.376  15.185  1.00  8.54           O  
ANISOU  313  OG1 THR A  45     1139    952   1154   -101    112   -192       O  
ATOM    314  N   VAL A  46      22.971   4.801  16.393  1.00  7.21           N  
ANISOU  314  N   VAL A  46      840    875   1023   -102   -107    -92       N  
ATOM    315  CA  VAL A  46      23.856   3.996  17.219  1.00  7.23           C  
ANISOU  315  CA  VAL A  46      900    862    984    -62      8     28       C  
ATOM    316  C   VAL A  46      25.088   3.613  16.414  1.00  7.52           C  
ANISOU  316  C   VAL A  46     1030    877    948     12    -58    101       C  
ATOM    317  O   VAL A  46      24.996   2.906  15.415  1.00  7.85           O  
ANISOU  317  O   VAL A  46     1041    888   1053     38     36    -67       O  
ATOM    318  CB  VAL A  46      23.122   2.700  17.678  1.00  7.55           C  
ANISOU  318  CB  VAL A  46      938    860   1069    -49     89      0       C  
ATOM    319  CG1 VAL A  46      24.060   1.791  18.428  1.00  8.67           C  
ANISOU  319  CG1 VAL A  46     1197   1142    952   -157    -42    -10       C  
ATOM    320  CG2 VAL A  46      21.907   3.031  18.536  1.00  9.64           C  
ANISOU  320  CG2 VAL A  46     1033   1351   1276    -85    -30    102       C  
ATOM    321  N   ASP A  47      26.235   4.068  16.868  1.00  7.80           N  
ANISOU  321  N   ASP A  47     1040    808   1112     -6     15    -10       N  
ATOM    322  CA  ASP A  47      27.507   3.646  16.296  1.00  8.17           C  
ANISOU  322  CA  ASP A  47      977   1067   1060    -59     70     53       C  
ATOM    323  C   ASP A  47      27.858   2.309  16.967  1.00  9.46           C  
ANISOU  323  C   ASP A  47      983   1263   1345    -40    188     25       C  
ATOM    324  O   ASP A  47      28.199   2.289  18.126  1.00  9.37           O  
ANISOU  324  O   ASP A  47      884   1336   1337     13    179    177       O  
ATOM    325  CB  ASP A  47      28.584   4.708  16.581  1.00  8.24           C  
ANISOU  325  CB  ASP A  47      972   1040   1118     18     78     84       C  
ATOM    326  CG  ASP A  47      29.929   4.361  15.958  1.00 10.56           C  
ANISOU  326  CG  ASP A  47     1205   1440   1364    -88    188    -28       C  
ATOM    327  OD1 ASP A  47      30.126   3.186  15.576  1.00 11.55           O  
ANISOU  327  OD1 ASP A  47     1218   1461   1706     60    288    123       O  
ATOM    328  OD2 ASP A  47      30.823   5.220  15.827  1.00 11.37           O1-
ANISOU  328  OD2 ASP A  47      994   1474   1851    -80     77     41       O1-
ATOM    329  N   THR A  48      27.820   1.215  16.221  1.00  9.84           N  
ANISOU  329  N   THR A  48     1126   1152   1458    -69    161     70       N  
ATOM    330  CA  THR A  48      28.064  -0.105  16.832  1.00 12.55           C  
ANISOU  330  CA  THR A  48     1552   1530   1686     40     65    151       C  
ATOM    331  C   THR A  48      29.483  -0.277  17.383  1.00 13.39           C  
ANISOU  331  C   THR A  48     1661   1596   1831     72      9    148       C  
ATOM    332  O   THR A  48      29.702  -1.143  18.232  1.00 14.78           O  
ANISOU  332  O   THR A  48     2012   1554   2048    200     33    344       O  
ATOM    333  CB  THR A  48      27.731  -1.238  15.859  1.00 12.99           C  
ANISOU  333  CB  THR A  48     1685   1476   1774     27     98    164       C  
ATOM    334  CG2 THR A  48      26.308  -1.226  15.474  1.00 16.16           C  
ANISOU  334  CG2 THR A  48     1994   1919   2226    -76    147    -11       C  
ATOM    335  OG1 THR A  48      28.487  -1.122  14.640  1.00 15.32           O  
ANISOU  335  OG1 THR A  48     2161   1703   1956    -64    249   -173       O  
ATOM    336  N   LYS A  49      30.403   0.587  16.982  1.00 13.53           N  
ANISOU  336  N   LYS A  49     1552   1685   1903    134      5     57       N  
ATOM    337  CA  LYS A  49      31.781   0.524  17.464  1.00 14.60           C  
ANISOU  337  CA  LYS A  49     1690   1923   1933     48    -38     46       C  
ATOM    338  C   LYS A  49      31.985   1.350  18.710  1.00 13.65           C  
ANISOU  338  C   LYS A  49     1552   1800   1832      4    -11    118       C  
ATOM    339  O   LYS A  49      33.049   1.264  19.339  1.00 14.87           O  
ANISOU  339  O   LYS A  49     1627   2190   1832    -53   -153    165       O  
ATOM    340  CB  LYS A  49      32.750   1.002  16.381  1.00 16.14           C  
ANISOU  340  CB  LYS A  49     1784   2140   2208     -9     40     34       C  
ATOM    341  CG  LYS A  49      32.702   0.184  15.100  1.00 19.99           C  
ANISOU  341  CG  LYS A  49     2465   2565   2565      4    -74    -73       C  
ATOM    342  CD  LYS A  49      33.280  -1.205  15.310  1.00 25.90           C  
ANISOU  342  CD  LYS A  49     3320   3291   3230    -89     93     59       C  
ATOM    343  CE  LYS A  49      33.232  -2.023  14.030  1.00 28.65           C  
ANISOU  343  CE  LYS A  49     3711   3618   3555     -9    -10    -79       C  
ATOM    344  NZ  LYS A  49      33.796  -3.388  14.221  1.00 30.58           N1+
ANISOU  344  NZ  LYS A  49     4076   3744   3795    -99     83     14       N1+
ATOM    345  N   ARG A  50      30.986   2.153  19.078  1.00 12.58           N  
ANISOU  345  N   ARG A  50     1292   1759   1727    -84     -6     84       N  
ATOM    346  CA  ARG A  50      31.052   2.975  20.264  1.00 13.57           C  
ANISOU  346  CA  ARG A  50     1568   1795   1792    -29     57     58       C  
ATOM    347  C   ARG A  50      29.624   3.308  20.708  1.00 12.57           C  
ANISOU  347  C   ARG A  50     1396   1656   1723    -33    -92     77       C  
ATOM    348  O   ARG A  50      29.138   4.433  20.540  1.00 13.77           O  
ANISOU  348  O   ARG A  50     1409   1712   2111   -206     31     21       O  
ATOM    349  CB  ARG A  50      31.905   4.236  20.012  1.00 15.07           C  
ANISOU  349  CB  ARG A  50     1746   1987   1991   -104    -12     39       C  
ATOM    350  CG  ARG A  50      31.965   5.181  21.187  1.00 21.02           C  
ANISOU  350  CG  ARG A  50     2752   2680   2551     34    110    -63       C  
ATOM    351  CD  ARG A  50      33.310   5.673  21.607  1.00 26.92           C  
ANISOU  351  CD  ARG A  50     3289   3497   3440   -113    -45    -16       C  
ATOM    352  NE  ARG A  50      33.076   6.754  22.568  1.00 31.67           N  
ANISOU  352  NE  ARG A  50     4030   3929   4074     55     94   -144       N  
ATOM    353  CZ  ARG A  50      33.856   7.080  23.595  1.00 34.76           C  
ANISOU  353  CZ  ARG A  50     4417   4409   4379    -27    -81    -60       C  
ATOM    354  NH1 ARG A  50      35.007   6.453  23.822  1.00 36.11           N1+
ANISOU  354  NH1 ARG A  50     4572   4470   4676     77    -12    -29       N1+
ATOM    355  NH2 ARG A  50      33.476   8.074  24.395  1.00 36.10           N  
ANISOU  355  NH2 ARG A  50     4623   4514   4578     13     28    -72       N  
ATOM    356  N   ARG A  51      28.957   2.294  21.264  1.00 12.17           N  
ANISOU  356  N   ARG A  51     1335   1707   1580    -17     10     80       N  
ATOM    357  CA  ARG A  51      27.575   2.440  21.736  1.00 11.33           C  
ANISOU  357  CA  ARG A  51     1295   1506   1501      6    -13     45       C  
ATOM    358  C   ARG A  51      27.563   3.210  23.065  1.00 12.97           C  
ANISOU  358  C   ARG A  51     1518   1744   1665    -73    -20     11       C  
ATOM    359  O   ARG A  51      28.469   3.069  23.920  1.00 13.12           O  
ANISOU  359  O   ARG A  51     1446   1916   1622   -147     18    133       O  
ATOM    360  CB  ARG A  51      26.896   1.073  21.916  1.00 10.46           C  
ANISOU  360  CB  ARG A  51     1176   1541   1256    -33    117     -3       C  
ATOM    361  CG  ARG A  51      26.839   0.205  20.677  1.00  8.63           C  
ANISOU  361  CG  ARG A  51     1050   1058   1169    -84    -34     69       C  
ATOM    362  CD  ARG A  51      25.769  -0.851  20.720  1.00  8.61           C  
ANISOU  362  CD  ARG A  51     1136   1138    995     -8     56     24       C  
ATOM    363  NE  ARG A  51      25.996  -1.790  21.809  1.00  8.74           N  
ANISOU  363  NE  ARG A  51     1105   1254    960      7     35     71       N  
ATOM    364  CZ  ARG A  51      25.053  -2.506  22.389  1.00  8.52           C  
ANISOU  364  CZ  ARG A  51     1074   1270    893    -95   -139     68       C  
ATOM    365  NH1 ARG A  51      23.780  -2.359  22.045  1.00 11.14           N1+
ANISOU  365  NH1 ARG A  51     1141   1724   1368   -334    -64    288       N1+
ATOM    366  NH2 ARG A  51      25.376  -3.347  23.362  1.00  7.54           N  
ANISOU  366  NH2 ARG A  51      772   1272    819   -223     55    143       N  
ATOM    367  N   THR A  52      26.573   4.061  23.239  1.00 13.91           N  
ANISOU  367  N   THR A  52     1550   1862   1871    -80     34    -57       N  
ATOM    368  CA  THR A  52      26.435   4.813  24.481  1.00 15.50           C  
ANISOU  368  CA  THR A  52     1870   2059   1961    -88    -18    -81       C  
ATOM    369  C   THR A  52      26.015   3.885  25.625  1.00 16.14           C  
ANISOU  369  C   THR A  52     1943   2137   2051    -50     -8    -38       C  
ATOM    370  O   THR A  52      25.444   2.805  25.426  1.00 14.89           O  
ANISOU  370  O   THR A  52     1542   2263   1850   -199     64    -48       O  
ATOM    371  CB  THR A  52      25.369   5.911  24.363  1.00 16.47           C  
ANISOU  371  CB  THR A  52     2085   2130   2043    -12     -6    -98       C  
ATOM    372  CG2 THR A  52      25.611   6.857  23.168  1.00 17.54           C  
ANISOU  372  CG2 THR A  52     2189   2185   2290   -114     40      0       C  
ATOM    373  OG1 THR A  52      24.074   5.338  24.109  1.00 17.57           O  
ANISOU  373  OG1 THR A  52     2149   2096   2429   -195    263    -63       O  
ATOM    374  N   GLU A  53      26.275   4.329  26.843  1.00 17.81           N  
ANISOU  374  N   GLU A  53     2199   2368   2200    -78     -6    -82       N  
ATOM    375  CA  GLU A  53      25.978   3.547  28.027  1.00 19.53           C  
ANISOU  375  CA  GLU A  53     2431   2540   2448     -8     12    -16       C  
ATOM    376  C   GLU A  53      24.474   3.237  28.082  1.00 18.49           C  
ANISOU  376  C   GLU A  53     2357   2420   2247      8     17    -67       C  
ATOM    377  O   GLU A  53      24.051   2.109  28.387  1.00 18.00           O  
ANISOU  377  O   GLU A  53     2301   2400   2137     91     54   -100       O  
ATOM    378  CB  GLU A  53      26.471   4.360  29.242  1.00 21.53           C  
ANISOU  378  CB  GLU A  53     2722   2773   2684    -11      2    -83       C  
ATOM    379  CG AGLU A  53      27.967   4.518  29.398  0.50 23.33           C  
ANISOU  379  CG AGLU A  53     2862   3007   2994      0     14     13       C  
ATOM    380  CG BGLU A  53      25.614   5.539  29.652  0.50 23.86           C  
ANISOU  380  CG BGLU A  53     2989   2998   3079     74     22     -9       C  
ATOM    381  CD AGLU A  53      28.385   5.307  30.618  0.50 26.90           C  
ANISOU  381  CD AGLU A  53     3482   3409   3329    -35    -58    -80       C  
ATOM    382  CD BGLU A  53      26.254   6.384  30.754  0.50 27.24           C  
ANISOU  382  CD BGLU A  53     3458   3434   3455    -50    -41    -82       C  
ATOM    383  OE1AGLU A  53      27.520   5.639  31.468  0.50 28.74           O  
ANISOU  383  OE1AGLU A  53     3665   3720   3533      0      2    -39       O  
ATOM    384  OE2AGLU A  53      29.597   5.594  30.707  0.50 28.31           O1-
ANISOU  384  OE2AGLU A  53     3569   3642   3546    -46    -43    -48       O1-
ATOM    385  OE1BGLU A  53      27.332   6.012  31.262  0.50 29.29           O  
ANISOU  385  OE1BGLU A  53     3667   3732   3729     41    -96    -10       O  
ATOM    386  OE2BGLU A  53      25.681   7.430  31.114  0.50 28.98           O1-
ANISOU  386  OE2BGLU A  53     3666   3568   3777      0     26   -108       O1-
ATOM    387  N   THR A  54      23.671   4.225  27.708  1.00 17.78           N  
ANISOU  387  N   THR A  54     2290   2288   2175     -4     56    -37       N  
ATOM    388  CA  THR A  54      22.228   4.073  27.741  1.00 18.36           C  
ANISOU  388  CA  THR A  54     2288   2331   2356     16     59      4       C  
ATOM    389  C   THR A  54      21.813   2.972  26.788  1.00 15.42           C  
ANISOU  389  C   THR A  54     1851   2059   1948     36     61     46       C  
ATOM    390  O   THR A  54      21.013   2.115  27.124  1.00 16.03           O  
ANISOU  390  O   THR A  54     1788   2147   2154    125    241     72       O  
ATOM    391  CB  THR A  54      21.544   5.392  27.314  1.00 19.48           C  
ANISOU  391  CB  THR A  54     2449   2440   2511     62     35     75       C  
ATOM    392  CG2 THR A  54      20.040   5.300  27.388  1.00 22.05           C  
ANISOU  392  CG2 THR A  54     2657   2772   2948     52     66     13       C  
ATOM    393  OG1 THR A  54      21.908   6.454  28.205  1.00 23.62           O  
ANISOU  393  OG1 THR A  54     3120   2888   2964     88     70   -137       O  
ATOM    394  N   VAL A  55      22.326   2.999  25.568  1.00 13.17           N  
ANISOU  394  N   VAL A  55     1457   1788   1758     33     43      3       N  
ATOM    395  CA  VAL A  55      22.022   1.965  24.602  1.00 11.23           C  
ANISOU  395  CA  VAL A  55     1132   1634   1500    -32    -16      0       C  
ATOM    396  C   VAL A  55      22.514   0.568  25.021  1.00 11.18           C  
ANISOU  396  C   VAL A  55     1262   1598   1388    -54    -63    -60       C  
ATOM    397  O   VAL A  55      21.825  -0.419  24.864  1.00 10.07           O  
ANISOU  397  O   VAL A  55     1085   1589   1149    -44    -46    -22       O  
ATOM    398  CB  VAL A  55      22.502   2.382  23.185  1.00 11.73           C  
ANISOU  398  CB  VAL A  55     1209   1647   1598     44    -66     58       C  
ATOM    399  CG1 VAL A  55      22.461   1.226  22.252  1.00 12.54           C  
ANISOU  399  CG1 VAL A  55     1232   1828   1704    -68    -24      8       C  
ATOM    400  CG2 VAL A  55      21.641   3.558  22.661  1.00 12.74           C  
ANISOU  400  CG2 VAL A  55     1430   1886   1523     98   -167    142       C  
ATOM    401  N   GLN A  56      23.713   0.469  25.611  1.00  9.45           N  
ANISOU  401  N   GLN A  56     1047   1311   1231    -10   -120     -8       N  
ATOM    402  CA  GLN A  56      24.220  -0.805  26.083  1.00  9.81           C  
ANISOU  402  CA  GLN A  56     1159   1326   1243    -31    -45    -66       C  
ATOM    403  C   GLN A  56      23.296  -1.457  27.126  1.00  9.76           C  
ANISOU  403  C   GLN A  56     1073   1369   1262    -29   -137    -35       C  
ATOM    404  O   GLN A  56      23.163  -2.672  27.180  1.00  8.74           O  
ANISOU  404  O   GLN A  56      903   1359   1057    -91    -64   -122       O  
ATOM    405  CB  GLN A  56      25.641  -0.607  26.611  1.00  9.92           C  
ANISOU  405  CB  GLN A  56     1276   1269   1222    -86    -35    -17       C  
ATOM    406  CG  GLN A  56      26.671  -0.323  25.517  1.00  9.25           C  
ANISOU  406  CG  GLN A  56     1045   1409   1060     48   -172   -119       C  
ATOM    407  CD  GLN A  56      28.037  -0.091  26.092  1.00 11.25           C  
ANISOU  407  CD  GLN A  56     1209   1722   1341    -33    -93   -127       C  
ATOM    408  NE2 GLN A  56      29.060  -0.565  25.408  1.00 11.87           N  
ANISOU  408  NE2 GLN A  56     1235   1976   1297      9     -7   -160       N  
ATOM    409  OE1 GLN A  56      28.148   0.452  27.192  1.00 11.68           O  
ANISOU  409  OE1 GLN A  56     1264   1512   1659   -103   -124   -248       O  
ATOM    410  N   LYS A  57      22.663  -0.638  27.953  1.00 10.86           N  
ANISOU  410  N   LYS A  57     1241   1533   1351    -55    -55    -89       N  
ATOM    411  CA  LYS A  57      21.740  -1.125  28.975  1.00 12.30           C  
ANISOU  411  CA  LYS A  57     1505   1685   1484    -67     22     -2       C  
ATOM    412  C   LYS A  57      20.368  -1.502  28.399  1.00 12.95           C  
ANISOU  412  C   LYS A  57     1599   1734   1585    -72     14      3       C  
ATOM    413  O   LYS A  57      19.758  -2.501  28.807  1.00 13.87           O  
ANISOU  413  O   LYS A  57     1593   1996   1681   -189     87     34       O  
ATOM    414  CB  LYS A  57      21.564  -0.040  30.035  1.00 13.35           C  
ANISOU  414  CB  LYS A  57     1630   1699   1742     26     64    -53       C  
ATOM    415  CG  LYS A  57      22.839   0.339  30.777  1.00 15.67           C  
ANISOU  415  CG  LYS A  57     1857   2122   1974    -70     50    -56       C  
ATOM    416  CD  LYS A  57      22.529   1.243  31.970  1.00 20.88           C  
ANISOU  416  CD  LYS A  57     2716   2645   2572     43     96   -181       C  
ATOM    417  CE  LYS A  57      23.596   2.244  32.208  1.00 23.04           C  
ANISOU  417  CE  LYS A  57     3012   2821   2918    -99     93    -60       C  
ATOM    418  NZ  LYS A  57      23.358   3.060  33.437  1.00 23.76           N1+
ANISOU  418  NZ  LYS A  57     3139   3054   2833     38     80    -76       N1+
ATOM    419  N   LEU A  58      19.907  -0.732  27.424  1.00 13.21           N  
ANISOU  419  N   LEU A  58     1577   1799   1640   -105     13     72       N  
ATOM    420  CA  LEU A  58      18.599  -0.985  26.788  1.00 13.99           C  
ANISOU  420  CA  LEU A  58     1663   1866   1785    -39    -50     44       C  
ATOM    421  C   LEU A  58      18.594  -2.197  25.921  1.00 15.30           C  
ANISOU  421  C   LEU A  58     1833   2027   1950    -54    -35     30       C  
ATOM    422  O   LEU A  58      17.596  -2.928  25.849  1.00 15.93           O  
ANISOU  422  O   LEU A  58     1770   2166   2115   -193   -124    114       O  
ATOM    423  CB  LEU A  58      18.203   0.172  25.901  1.00 15.01           C  
ANISOU  423  CB  LEU A  58     1836   1991   1876    -61     -7     23       C  
ATOM    424  CG  LEU A  58      17.712   1.434  26.595  1.00 16.62           C  
ANISOU  424  CG  LEU A  58     2111   2043   2160     -3      1    -39       C  
ATOM    425  CD1 LEU A  58      17.424   2.466  25.530  1.00 17.38           C  
ANISOU  425  CD1 LEU A  58     2136   2230   2238     35    -19     37       C  
ATOM    426  CD2 LEU A  58      16.500   1.172  27.481  1.00 18.01           C  
ANISOU  426  CD2 LEU A  58     2166   2351   2324     13     -3   -152       C  
ATOM    427  N   CYS A  59      19.677  -2.405  25.202  1.00 14.74           N  
ANISOU  427  N   CYS A  59     1793   1977   1827    -51    -36     75       N  
ATOM    428  CA  CYS A  59      19.727  -3.480  24.235  1.00 14.85           C  
ANISOU  428  CA  CYS A  59     1952   1829   1858     -6    -48     81       C  
ATOM    429  C   CYS A  59      21.060  -4.188  24.365  1.00 15.50           C  
ANISOU  429  C   CYS A  59     1935   1957   1997   -102    -11    -35       C  
ATOM    430  O   CYS A  59      21.973  -4.004  23.563  1.00 15.60           O  
ANISOU  430  O   CYS A  59     2078   1904   1942   -199    115     76       O  
ATOM    431  CB  CYS A  59      19.482  -2.943  22.823  1.00 15.91           C  
ANISOU  431  CB  CYS A  59     2154   1945   1944     16    -90     40       C  
ATOM    432  SG ACYS A  59      19.465  -4.220  21.524  0.50 13.80           S  
ANISOU  432  SG ACYS A  59     1560   1711   1970    227   -496     -1       S  
ATOM    433  SG BCYS A  59      18.831  -4.279  21.851  0.50 14.85           S  
ANISOU  433  SG BCYS A  59     2678   1803   1159    -55     70    101       S  
ATOM    434  N   PRO A  60      21.199  -4.996  25.395  1.00 16.02           N  
ANISOU  434  N   PRO A  60     2018   1972   2095    -26    -22     -9       N  
ATOM    435  CA  PRO A  60      22.485  -5.610  25.663  1.00 16.81           C  
ANISOU  435  CA  PRO A  60     2072   2159   2156      0    -30     -6       C  
ATOM    436  C   PRO A  60      22.966  -6.504  24.561  1.00 17.74           C  
ANISOU  436  C   PRO A  60     2170   2264   2306     14      7    -58       C  
ATOM    437  O   PRO A  60      24.188  -6.661  24.424  1.00 20.22           O  
ANISOU  437  O   PRO A  60     2250   2716   2717     -9    -14   -168       O  
ATOM    438  CB  PRO A  60      22.220  -6.497  26.882  1.00 17.29           C  
ANISOU  438  CB  PRO A  60     2220   2185   2164     22    -42     22       C  
ATOM    439  CG  PRO A  60      20.874  -6.316  27.288  1.00 16.58           C  
ANISOU  439  CG  PRO A  60     2145   2096   2057    -15    -59     73       C  
ATOM    440  CD  PRO A  60      20.191  -5.392  26.369  1.00 15.35           C  
ANISOU  440  CD  PRO A  60     2005   1895   1933      9    -62     14       C  
ATOM    441  N   GLY A  61      22.023  -7.139  23.871  1.00 16.46           N  
ANISOU  441  N   GLY A  61     2126   2044   2083     17      1     29       N  
ATOM    442  CA  GLY A  61      22.282  -8.059  22.794  1.00 15.35           C  
ANISOU  442  CA  GLY A  61     2003   1853   1976     68     46     83       C  
ATOM    443  C   GLY A  61      22.751  -7.467  21.496  1.00 15.01           C  
ANISOU  443  C   GLY A  61     1948   1843   1909     31     20     43       C  
ATOM    444  O   GLY A  61      23.224  -8.219  20.646  1.00 17.00           O  
ANISOU  444  O   GLY A  61     2343   1992   2124     33     73     43       O  
ATOM    445  N   GLY A  62      22.637  -6.148  21.319  1.00 13.81           N  
ANISOU  445  N   GLY A  62     1711   1678   1855    137     38     67       N  
ATOM    446  CA  GLY A  62      23.137  -5.512  20.097  1.00 14.20           C  
ANISOU  446  CA  GLY A  62     1732   1833   1830     55     44     76       C  
ATOM    447  C   GLY A  62      22.226  -5.524  18.878  1.00 14.15           C  
ANISOU  447  C   GLY A  62     1825   1805   1746    -20     90     98       C  
ATOM    448  O   GLY A  62      22.577  -5.097  17.774  1.00 15.66           O  
ANISOU  448  O   GLY A  62     2001   2080   1865    209    283    146       O  
ATOM    449  N   GLU A  63      21.002  -5.976  19.059  1.00 13.30           N  
ANISOU  449  N   GLU A  63     1643   1665   1743     61     47     58       N  
ATOM    450  CA  GLU A  63      20.051  -5.984  17.962  1.00 13.22           C  
ANISOU  450  CA  GLU A  63     1720   1661   1641     19     17     17       C  
ATOM    451  C   GLU A  63      19.722  -4.559  17.469  1.00 12.15           C  
ANISOU  451  C   GLU A  63     1685   1470   1460    -25    140     53       C  
ATOM    452  O   GLU A  63      19.497  -3.675  18.279  1.00 14.45           O  
ANISOU  452  O   GLU A  63     2322   1647   1518    163    206    117       O  
ATOM    453  CB  GLU A  63      18.747  -6.609  18.433  1.00 13.48           C  
ANISOU  453  CB  GLU A  63     1823   1632   1667     38     79    116       C  
ATOM    454  CG  GLU A  63      18.806  -8.094  18.780  1.00 15.66           C  
ANISOU  454  CG  GLU A  63     2044   1766   2139    -32     26    -16       C  
ATOM    455  CD  GLU A  63      19.095  -8.409  20.240  1.00 19.03           C  
ANISOU  455  CD  GLU A  63     2638   2327   2263   -114     -7     45       C  
ATOM    456  OE1 GLU A  63      19.522  -7.524  21.000  1.00 16.37           O  
ANISOU  456  OE1 GLU A  63     2213   2002   2004   -170    226    237       O  
ATOM    457  OE2 GLU A  63      18.892  -9.611  20.624  1.00 24.06           O1-
ANISOU  457  OE2 GLU A  63     3438   2617   3087   -230    -87     63       O1-
ATOM    458  N   LEU A  64      19.653  -4.343  16.172  1.00 10.79           N  
ANISOU  458  N   LEU A  64     1365   1384   1348     79     47    -70       N  
ATOM    459  CA  LEU A  64      19.305  -3.030  15.582  1.00 10.11           C  
ANISOU  459  CA  LEU A  64     1162   1348   1329    -93     63    -16       C  
ATOM    460  C   LEU A  64      18.548  -3.327  14.307  1.00  9.45           C  
ANISOU  460  C   LEU A  64     1255   1191   1145   -103     94    -96       C  
ATOM    461  O   LEU A  64      18.919  -4.260  13.571  1.00 12.20           O  
ANISOU  461  O   LEU A  64     1414   1672   1549     85    206   -266       O  
ATOM    462  CB  LEU A  64      20.540  -2.206  15.176  1.00 11.47           C  
ANISOU  462  CB  LEU A  64     1380   1517   1458   -145    194      0       C  
ATOM    463  CG  LEU A  64      21.254  -1.454  16.286  1.00 12.62           C  
ANISOU  463  CG  LEU A  64     1420   1793   1579    -77     87     11       C  
ATOM    464  CD1 LEU A  64      22.555  -0.918  15.749  1.00 12.15           C  
ANISOU  464  CD1 LEU A  64     1408   1584   1624   -109     42    -86       C  
ATOM    465  CD2 LEU A  64      20.438  -0.336  16.857  1.00 12.00           C  
ANISOU  465  CD2 LEU A  64     1314   1759   1486    -10     94   -119       C  
ATOM    466  N   PRO A  65      17.504  -2.575  13.997  1.00  8.37           N  
ANISOU  466  N   PRO A  65     1022   1112   1043   -148    118    -37       N  
ATOM    467  CA  PRO A  65      16.949  -1.501  14.819  1.00  9.06           C  
ANISOU  467  CA  PRO A  65     1165   1217   1058    -87     67    -33       C  
ATOM    468  C   PRO A  65      16.218  -2.058  16.034  1.00  8.84           C  
ANISOU  468  C   PRO A  65     1118   1136   1102   -174    139    -49       C  
ATOM    469  O   PRO A  65      15.888  -3.221  16.112  1.00 10.33           O  
ANISOU  469  O   PRO A  65     1374   1145   1405   -208    428   -222       O  
ATOM    470  CB  PRO A  65      15.957  -0.809  13.887  1.00 10.07           C  
ANISOU  470  CB  PRO A  65     1399   1232   1192     13     13    -81       C  
ATOM    471  CG  PRO A  65      15.530  -1.869  12.883  1.00 10.93           C  
ANISOU  471  CG  PRO A  65     1327   1387   1436    -96     27    -42       C  
ATOM    472  CD  PRO A  65      16.751  -2.767  12.759  1.00  9.29           C  
ANISOU  472  CD  PRO A  65     1156   1190   1182   -143      1    -12       C  
ATOM    473  N   PHE A  66      16.006  -1.213  17.021  1.00  7.86           N  
ANISOU  473  N   PHE A  66     1068    967    949    -96    132      7       N  
ATOM    474  CA  PHE A  66      15.140  -1.571  18.115  1.00  8.11           C  
ANISOU  474  CA  PHE A  66     1023   1041   1015    -37    121     92       C  
ATOM    475  C   PHE A  66      14.272  -0.387  18.464  1.00  7.81           C  
ANISOU  475  C   PHE A  66      964   1024    978    -67    131     22       C  
ATOM    476  O   PHE A  66      14.578   0.752  18.118  1.00  7.88           O  
ANISOU  476  O   PHE A  66     1022    999    969    -54     53    133       O  
ATOM    477  CB  PHE A  66      15.897  -2.188  19.349  1.00  8.79           C  
ANISOU  477  CB  PHE A  66     1157   1140   1042     28    154    251       C  
ATOM    478  CG  PHE A  66      16.759  -1.236  20.133  1.00  8.68           C  
ANISOU  478  CG  PHE A  66     1104   1187   1007    208    129    264       C  
ATOM    479  CD1 PHE A  66      16.233  -0.530  21.210  1.00 10.79           C  
ANISOU  479  CD1 PHE A  66     1529   1569    999    118     23    224       C  
ATOM    480  CD2 PHE A  66      18.137  -1.079  19.826  1.00  9.50           C  
ANISOU  480  CD2 PHE A  66     1100   1341   1165     99    -11    211       C  
ATOM    481  CE1 PHE A  66      17.029   0.329  21.929  1.00 10.55           C  
ANISOU  481  CE1 PHE A  66     1524   1380   1104    134    159     18       C  
ATOM    482  CE2 PHE A  66      18.917  -0.215  20.571  1.00  9.31           C  
ANISOU  482  CE2 PHE A  66     1220   1192   1122    175    -36    252       C  
ATOM    483  CZ  PHE A  66      18.335   0.483  21.622  1.00  9.81           C  
ANISOU  483  CZ  PHE A  66     1456   1303    967    111   -265    176       C  
ATOM    484  N   LEU A  67      13.175  -0.658  19.164  1.00  7.39           N  
ANISOU  484  N   LEU A  67      914    789   1101    -70    187    125       N  
ATOM    485  CA  LEU A  67      12.193   0.345  19.503  1.00  7.70           C  
ANISOU  485  CA  LEU A  67     1023    885   1016    -26     86     39       C  
ATOM    486  C   LEU A  67      11.925   0.334  20.993  1.00  6.50           C  
ANISOU  486  C   LEU A  67      840    755    873     13     61     39       C  
ATOM    487  O   LEU A  67      11.716  -0.730  21.584  1.00  8.36           O  
ANISOU  487  O   LEU A  67     1431    795    950   -168    229     66       O  
ATOM    488  CB  LEU A  67      10.870   0.075  18.765  1.00  9.82           C  
ANISOU  488  CB  LEU A  67     1315   1285   1129    -42    126   -105       C  
ATOM    489  CG  LEU A  67       9.794   1.156  19.006  1.00 11.29           C  
ANISOU  489  CG  LEU A  67     1338   1659   1293    111   -323   -151       C  
ATOM    490  CD1 LEU A  67       9.795   2.120  17.857  1.00 14.55           C  
ANISOU  490  CD1 LEU A  67     1617   1745   2166    234    121    118       C  
ATOM    491  CD2 LEU A  67       8.439   0.546  19.171  1.00 14.73           C  
ANISOU  491  CD2 LEU A  67     1934   1753   1909    235    254    168       C  
ATOM    492  N   LEU A  68      11.964   1.508  21.599  1.00  6.13           N  
ANISOU  492  N   LEU A  68      895    678    755    -67     98     25       N  
ATOM    493  CA  LEU A  68      11.537   1.728  22.976  1.00  7.66           C  
ANISOU  493  CA  LEU A  68     1102    909    898    -64     46    157       C  
ATOM    494  C   LEU A  68      10.140   2.327  22.943  1.00  7.24           C  
ANISOU  494  C   LEU A  68     1079    853    818      6     36     63       C  
ATOM    495  O   LEU A  68       9.923   3.365  22.335  1.00  8.36           O  
ANISOU  495  O   LEU A  68     1157    980   1039    203    216    235       O  
ATOM    496  CB  LEU A  68      12.510   2.687  23.675  1.00  9.48           C  
ANISOU  496  CB  LEU A  68     1350   1023   1228   -163    -12     57       C  
ATOM    497  CG  LEU A  68      12.260   2.983  25.132  1.00 12.78           C  
ANISOU  497  CG  LEU A  68     1862   1419   1574   -239     62    -63       C  
ATOM    498  CD1 LEU A  68      12.369   1.758  25.986  1.00 13.28           C  
ANISOU  498  CD1 LEU A  68     1752   1719   1572   -192   -162     33       C  
ATOM    499  CD2 LEU A  68      13.276   4.035  25.650  1.00 13.94           C  
ANISOU  499  CD2 LEU A  68     1977   1640   1678   -212    -92   -121       C  
ATOM    500  N   TYR A  69       9.195   1.645  23.547  1.00  6.44           N  
ANISOU  500  N   TYR A  69      955    723    765     35     74     39       N  
ATOM    501  CA  TYR A  69       7.789   2.064  23.633  1.00  6.95           C  
ANISOU  501  CA  TYR A  69      933    747    959     58     66    107       C  
ATOM    502  C   TYR A  69       7.509   2.195  25.123  1.00  7.04           C  
ANISOU  502  C   TYR A  69     1027    743    902    -47     68     89       C  
ATOM    503  O   TYR A  69       7.460   1.187  25.838  1.00  7.08           O  
ANISOU  503  O   TYR A  69     1103    492   1094    -55    104    239       O  
ATOM    504  CB  TYR A  69       6.828   1.072  22.980  1.00  8.33           C  
ANISOU  504  CB  TYR A  69     1123   1046    995     54     44      6       C  
ATOM    505  CG  TYR A  69       5.427   1.609  22.830  1.00  8.26           C  
ANISOU  505  CG  TYR A  69     1191    758   1187    -12    -99     42       C  
ATOM    506  CD1 TYR A  69       5.062   2.380  21.745  1.00 10.82           C  
ANISOU  506  CD1 TYR A  69     1482   1028   1600   -258   -207    154       C  
ATOM    507  CD2 TYR A  69       4.447   1.406  23.800  1.00  9.78           C  
ANISOU  507  CD2 TYR A  69     1169    831   1715     95     97    205       C  
ATOM    508  CE1 TYR A  69       3.798   2.868  21.607  1.00 11.94           C  
ANISOU  508  CE1 TYR A  69     1591   1197   1746    -52   -181     20       C  
ATOM    509  CE2 TYR A  69       3.166   1.946  23.650  1.00 11.50           C  
ANISOU  509  CE2 TYR A  69     1197   1091   2078      6    134    120       C  
ATOM    510  CZ  TYR A  69       2.869   2.688  22.550  1.00 11.83           C  
ANISOU  510  CZ  TYR A  69     1196   1341   1956     17   -263    -81       C  
ATOM    511  OH  TYR A  69       1.587   3.242  22.359  1.00 16.31           O  
ANISOU  511  OH  TYR A  69     1435   1554   3206    244   -384   -195       O  
ATOM    512  N   GLY A  70       7.407   3.414  25.644  1.00  8.09           N  
ANISOU  512  N   GLY A  70     1272    927    872    123    176    120       N  
ATOM    513  CA  GLY A  70       7.368   3.596  27.103  1.00  9.84           C  
ANISOU  513  CA  GLY A  70     1529   1102   1105     52     95    -18       C  
ATOM    514  C   GLY A  70       8.704   3.172  27.688  1.00 10.92           C  
ANISOU  514  C   GLY A  70     1627   1236   1283    -54     38    -94       C  
ATOM    515  O   GLY A  70       9.732   3.678  27.295  1.00 13.15           O  
ANISOU  515  O   GLY A  70     1989   1118   1889   -176    -19    -96       O  
ATOM    516  N   THR A  71       8.689   2.160  28.554  1.00 11.55           N  
ANISOU  516  N   THR A  71     1737   1129   1521     -1    -22   -100       N  
ATOM    517  CA  THR A  71       9.891   1.613  29.142  1.00 11.65           C  
ANISOU  517  CA  THR A  71     1696   1302   1428      6    -90   -122       C  
ATOM    518  C   THR A  71      10.254   0.236  28.557  1.00  9.71           C  
ANISOU  518  C   THR A  71     1380   1011   1296      5   -132    -13       C  
ATOM    519  O   THR A  71      11.181  -0.430  29.013  1.00 11.93           O  
ANISOU  519  O   THR A  71     1642   1076   1814     23   -378   -158       O  
ATOM    520  CB  THR A  71       9.692   1.429  30.649  1.00 13.69           C  
ANISOU  520  CB  THR A  71     1992   1599   1608     74    -24   -156       C  
ATOM    521  CG2 THR A  71       9.342   2.769  31.291  1.00 15.56           C  
ANISOU  521  CG2 THR A  71     2196   1800   1915     73    -34   -176       C  
ATOM    522  OG1 THR A  71       8.540   0.614  30.890  1.00 15.28           O  
ANISOU  522  OG1 THR A  71     2309   1812   1681     80     61     41       O  
ATOM    523  N   GLU A  72       9.537  -0.187  27.537  1.00  6.67           N  
ANISOU  523  N   GLU A  72      882    780    873     47   -131    -13       N  
ATOM    524  CA  GLU A  72       9.701  -1.537  27.017  1.00  6.37           C  
ANISOU  524  CA  GLU A  72      856    756    807     -3   -110     76       C  
ATOM    525  C   GLU A  72      10.398  -1.590  25.660  1.00  5.61           C  
ANISOU  525  C   GLU A  72      716    656    756    -22    -45    -44       C  
ATOM    526  O   GLU A  72      10.010  -0.857  24.734  1.00  6.12           O  
ANISOU  526  O   GLU A  72      692    810    821    107    -16    120       O  
ATOM    527  CB  GLU A  72       8.325  -2.214  26.921  1.00  6.76           C  
ANISOU  527  CB  GLU A  72      922    861    784    -66   -121     67       C  
ATOM    528  CG  GLU A  72       7.630  -2.315  28.266  1.00  6.96           C  
ANISOU  528  CG  GLU A  72      923    947    775   -180    -47    135       C  
ATOM    529  CD  GLU A  72       6.214  -2.875  28.154  1.00  7.92           C  
ANISOU  529  CD  GLU A  72      905   1075   1030   -118     84    121       C  
ATOM    530  OE1 GLU A  72       5.349  -2.239  27.526  1.00  9.29           O  
ANISOU  530  OE1 GLU A  72      896   1542   1091   -334   -161    167       O  
ATOM    531  OE2 GLU A  72       5.945  -3.930  28.757  1.00  9.93           O1-
ANISOU  531  OE2 GLU A  72      972   1104   1697   -297      8    445       O1-
ATOM    532  N   VAL A  73      11.415  -2.445  25.544  1.00  7.30           N  
ANISOU  532  N   VAL A  73      910   1038    823     51   -118     49       N  
ATOM    533  CA  VAL A  73      12.231  -2.585  24.348  1.00  8.48           C  
ANISOU  533  CA  VAL A  73     1041   1106   1072     32      3     63       C  
ATOM    534  C   VAL A  73      11.675  -3.695  23.460  1.00  7.33           C  
ANISOU  534  C   VAL A  73      974    780   1029     54     20     18       C  
ATOM    535  O   VAL A  73      11.306  -4.798  23.927  1.00  9.18           O  
ANISOU  535  O   VAL A  73     1494    928   1064    -27     54    -71       O  
ATOM    536  CB  VAL A  73      13.683  -2.895  24.699  1.00 10.60           C  
ANISOU  536  CB  VAL A  73     1212   1478   1336     19    -16     -8       C  
ATOM    537  CG1 VAL A  73      14.479  -3.259  23.399  1.00 11.93           C  
ANISOU  537  CG1 VAL A  73     1172   1684   1676     85     67     16       C  
ATOM    538  CG2 VAL A  73      14.296  -1.718  25.401  1.00 14.73           C  
ANISOU  538  CG2 VAL A  73     1712   1952   1929     60     -6   -181       C  
ATOM    539  N   HIS A  74      11.526  -3.374  22.182  1.00  7.40           N  
ANISOU  539  N   HIS A  74      919    862   1030      0     27    -23       N  
ATOM    540  CA  HIS A  74      11.068  -4.311  21.147  1.00  7.39           C  
ANISOU  540  CA  HIS A  74     1002    818    986    -13     51    -12       C  
ATOM    541  C   HIS A  74      12.150  -4.517  20.102  1.00  7.79           C  
ANISOU  541  C   HIS A  74     1078    919    963    -18     89     -8       C  
ATOM    542  O   HIS A  74      12.751  -3.534  19.683  1.00  8.07           O  
ANISOU  542  O   HIS A  74     1184    813   1069     36    301    -41       O  
ATOM    543  CB  HIS A  74       9.849  -3.774  20.462  1.00  6.94           C  
ANISOU  543  CB  HIS A  74      987    742    906   -233      8   -164       C  
ATOM    544  CG  HIS A  74       8.661  -3.608  21.346  1.00  6.89           C  
ANISOU  544  CG  HIS A  74      861    822    931    -30    -19    -47       C  
ATOM    545  CD2 HIS A  74       8.390  -2.713  22.331  1.00  7.29           C  
ANISOU  545  CD2 HIS A  74      832    912   1024    -90     65    -69       C  
ATOM    546  ND1 HIS A  74       7.558  -4.428  21.245  1.00  8.42           N  
ANISOU  546  ND1 HIS A  74      835   1330   1033   -296    149   -147       N  
ATOM    547  CE1 HIS A  74       6.655  -4.038  22.129  1.00  7.98           C  
ANISOU  547  CE1 HIS A  74      866   1042   1122   -196    120   -299       C  
ATOM    548  NE2 HIS A  74       7.123  -2.980  22.785  1.00  6.78           N  
ANISOU  548  NE2 HIS A  74     1011    926    639   -169     -9    -67       N  
ATOM    549  N   THR A  75      12.464  -5.761  19.718  1.00  9.23           N  
ANISOU  549  N   THR A  75     1325   1053   1128    -10     81     69       N  
ATOM    550  CA  THR A  75      13.413  -6.081  18.683  1.00  9.93           C  
ANISOU  550  CA  THR A  75     1387   1146   1239    -24    -37      8       C  
ATOM    551  C   THR A  75      12.690  -6.924  17.600  1.00 10.01           C  
ANISOU  551  C   THR A  75     1282   1245   1274    -38      1     -5       C  
ATOM    552  O   THR A  75      11.555  -7.407  17.786  1.00 12.15           O  
ANISOU  552  O   THR A  75     1526   1476   1613   -142    -35    -71       O  
ATOM    553  CB  THR A  75      14.624  -6.863  19.249  1.00 10.84           C  
ANISOU  553  CB  THR A  75     1393   1332   1391     15      6    -72       C  
ATOM    554  CG2 THR A  75      15.327  -6.102  20.402  1.00 11.80           C  
ANISOU  554  CG2 THR A  75     1649   1428   1404    -46     18      9       C  
ATOM    555  OG1 THR A  75      14.186  -8.092  19.824  1.00 10.77           O  
ANISOU  555  OG1 THR A  75     1601   1300   1190     37    -33    -19       O  
ATOM    556  N   ASP A  76      13.359  -7.027  16.470  1.00  9.85           N  
ANISOU  556  N   ASP A  76     1264   1296   1179    142    -62     79       N  
ATOM    557  CA  ASP A  76      12.934  -7.730  15.278  1.00 10.24           C  
ANISOU  557  CA  ASP A  76     1316   1302   1271     79    -80     -5       C  
ATOM    558  C   ASP A  76      12.021  -6.800  14.473  1.00  9.83           C  
ANISOU  558  C   ASP A  76     1368   1376    988    128    -38     22       C  
ATOM    559  O   ASP A  76      10.904  -6.478  14.894  1.00  9.68           O  
ANISOU  559  O   ASP A  76     1425   1414    837    127    -62      8       O  
ATOM    560  CB  ASP A  76      12.228  -9.034  15.608  1.00 10.98           C  
ANISOU  560  CB  ASP A  76     1483   1380   1306     15    -62     67       C  
ATOM    561  CG  ASP A  76      11.840  -9.827  14.386  1.00 13.13           C  
ANISOU  561  CG  ASP A  76     2009   1461   1518    -87   -128     70       C  
ATOM    562  OD1 ASP A  76      12.144 -11.038  14.354  1.00 22.21           O  
ANISOU  562  OD1 ASP A  76     3032   2504   2903    366   -155   -186       O  
ATOM    563  OD2 ASP A  76      11.127  -9.413  13.471  1.00 15.54           O1-
ANISOU  563  OD2 ASP A  76     2119   2202   1582    309   -116    -95       O1-
ATOM    564  N   THR A  77      12.501  -6.349  13.326  1.00  9.39           N  
ANISOU  564  N   THR A  77     1135   1318   1114     48     40     21       N  
ATOM    565  CA  THR A  77      11.780  -5.399  12.515  1.00  9.66           C  
ANISOU  565  CA  THR A  77     1279   1345   1043     44    -23    -14       C  
ATOM    566  C   THR A  77      10.352  -5.821  12.199  1.00  8.36           C  
ANISOU  566  C   THR A  77     1089   1181    905     72    -19     25       C  
ATOM    567  O   THR A  77       9.429  -5.016  12.315  1.00  9.19           O  
ANISOU  567  O   THR A  77     1405   1258    826    160     10    -68       O  
ATOM    568  CB  THR A  77      12.550  -5.139  11.228  1.00  9.07           C  
ANISOU  568  CB  THR A  77     1090   1336   1020      0    -23     46       C  
ATOM    569  CG2 THR A  77      11.795  -4.163  10.251  1.00 10.52           C  
ANISOU  569  CG2 THR A  77     1280   1546   1169     40     10    151       C  
ATOM    570  OG1 THR A  77      13.813  -4.550  11.531  1.00 12.19           O  
ANISOU  570  OG1 THR A  77     1407   1805   1419   -226      6    219       O  
ATOM    571  N   ASN A  78      10.132  -7.068  11.804  1.00  8.78           N  
ANISOU  571  N   ASN A  78     1203   1236    897     13    -29    -35       N  
ATOM    572  CA  ASN A  78       8.766  -7.503  11.512  1.00 10.11           C  
ANISOU  572  CA  ASN A  78     1322   1299   1217    -16    -79    -55       C  
ATOM    573  C   ASN A  78       7.846  -7.444  12.736  1.00  9.99           C  
ANISOU  573  C   ASN A  78     1281   1291   1221     53    -56    -16       C  
ATOM    574  O   ASN A  78       6.694  -6.989  12.632  1.00  9.70           O  
ANISOU  574  O   ASN A  78     1091   1430   1165     29     46    101       O  
ATOM    575  CB  ASN A  78       8.708  -8.923  10.929  1.00 10.89           C  
ANISOU  575  CB  ASN A  78     1468   1370   1298    -43    -20   -150       C  
ATOM    576  CG  ASN A  78       9.321  -9.048   9.542  1.00 14.87           C  
ANISOU  576  CG  ASN A  78     2131   1872   1645    -18    -67    -64       C  
ATOM    577  ND2 ASN A  78       9.900 -10.224   9.276  1.00 21.95           N  
ANISOU  577  ND2 ASN A  78     2841   2682   2815    415    136   -246       N  
ATOM    578  OD1 ASN A  78       9.248  -8.158   8.726  1.00 18.50           O  
ANISOU  578  OD1 ASN A  78     2854   2223   1952    -92     81     27       O  
ATOM    579  N   LYS A  79       8.377  -7.854  13.896  1.00  9.37           N  
ANISOU  579  N   LYS A  79     1311   1212   1034     11    -36   -137       N  
ATOM    580  CA  LYS A  79       7.612  -7.825  15.135  1.00  9.82           C  
ANISOU  580  CA  LYS A  79     1301   1266   1162    -11     30     12       C  
ATOM    581  C   LYS A  79       7.333  -6.374  15.564  1.00  8.89           C  
ANISOU  581  C   LYS A  79     1256   1196    922     10    -68     17       C  
ATOM    582  O   LYS A  79       6.250  -6.060  15.978  1.00  8.20           O  
ANISOU  582  O   LYS A  79     1212   1283    619   -107     90    139       O  
ATOM    583  CB  LYS A  79       8.318  -8.580  16.267  1.00 11.49           C  
ANISOU  583  CB  LYS A  79     1471   1423   1469     74      1     -7       C  
ATOM    584  CG  LYS A  79       8.426 -10.077  15.987  1.00 14.20           C  
ANISOU  584  CG  LYS A  79     1866   1661   1867    143    -11   -126       C  
ATOM    585  CD  LYS A  79       8.883 -10.829  17.233  1.00 19.56           C  
ANISOU  585  CD  LYS A  79     2687   2408   2336    -35    -77    136       C  
ATOM    586  CE  LYS A  79       9.406 -12.248  16.806  1.00 23.26           C  
ANISOU  586  CE  LYS A  79     3054   2786   2997     97    -33    -33       C  
ATOM    587  NZ  LYS A  79       9.173 -13.397  17.715  1.00 26.71           N1+
ANISOU  587  NZ  LYS A  79     3540   3365   3241      0      0     41       N1+
ATOM    588  N   ILE A  80       8.313  -5.490  15.425  1.00  7.85           N  
ANISOU  588  N   ILE A  80     1038   1157    786     11     40     70       N  
ATOM    589  CA  ILE A  80       8.112  -4.083  15.728  1.00  9.28           C  
ANISOU  589  CA  ILE A  80     1186   1276   1061     57     19    -13       C  
ATOM    590  C   ILE A  80       7.006  -3.513  14.859  1.00  7.91           C  
ANISOU  590  C   ILE A  80     1103   1113    787    105     87     26       C  
ATOM    591  O   ILE A  80       6.109  -2.801  15.362  1.00  7.93           O  
ANISOU  591  O   ILE A  80     1145   1046    819    111      5     60       O  
ATOM    592  CB  ILE A  80       9.425  -3.301  15.578  1.00  9.01           C  
ANISOU  592  CB  ILE A  80     1196   1293    932     78    -54      3       C  
ATOM    593  CG1 ILE A  80      10.495  -3.739  16.611  1.00  9.46           C  
ANISOU  593  CG1 ILE A  80     1277   1187   1131    108    -82     22       C  
ATOM    594  CG2 ILE A  80       9.158  -1.790  15.704  1.00  9.61           C  
ANISOU  594  CG2 ILE A  80     1172   1454   1026   -130    -24     29       C  
ATOM    595  CD1 ILE A  80      11.900  -3.289  16.243  1.00 11.99           C  
ANISOU  595  CD1 ILE A  80     1502   1683   1369      3   -162   -110       C  
ATOM    596  N   GLU A  81       7.063  -3.751  13.544  1.00  7.57           N  
ANISOU  596  N   GLU A  81     1028   1146    700    208    -39    -47       N  
ATOM    597  CA  GLU A  81       6.053  -3.214  12.663  1.00  8.03           C  
ANISOU  597  CA  GLU A  81     1093   1147    810     72     14     11       C  
ATOM    598  C   GLU A  81       4.651  -3.712  13.009  1.00  8.34           C  
ANISOU  598  C   GLU A  81     1165   1302    700     20     34     24       C  
ATOM    599  O   GLU A  81       3.703  -2.937  13.055  1.00  8.38           O  
ANISOU  599  O   GLU A  81     1396   1234    550    -89     62    112       O  
ATOM    600  CB  GLU A  81       6.408  -3.568  11.218  1.00  8.56           C  
ANISOU  600  CB  GLU A  81     1082   1378    793    -30     62    -34       C  
ATOM    601  CG  GLU A  81       5.478  -2.939  10.211  1.00 10.36           C  
ANISOU  601  CG  GLU A  81     1435   1520    979    -41   -137    101       C  
ATOM    602  CD  GLU A  81       5.824  -3.206   8.786  1.00 14.37           C  
ANISOU  602  CD  GLU A  81     1912   1840   1708   -106    276    -68       C  
ATOM    603  OE1 GLU A  81       5.351  -4.185   8.196  1.00 17.57           O  
ANISOU  603  OE1 GLU A  81     2932   2087   1656    -49      1    -54       O  
ATOM    604  OE2 GLU A  81       6.551  -2.395   8.249  1.00 16.02           O1-
ANISOU  604  OE2 GLU A  81     2664   1597   1826     94    194     62       O1-
ATOM    605  N   GLU A  82       4.533  -5.012  13.253  1.00  8.56           N  
ANISOU  605  N   GLU A  82     1194   1342    717    -12     31     -2       N  
ATOM    606  CA  GLU A  82       3.252  -5.565  13.645  1.00  9.44           C  
ANISOU  606  CA  GLU A  82     1246   1282   1057    -72     46   -121       C  
ATOM    607  C   GLU A  82       2.733  -4.929  14.951  1.00  8.69           C  
ANISOU  607  C   GLU A  82     1154   1184    965    -10      9    -33       C  
ATOM    608  O   GLU A  82       1.536  -4.641  15.059  1.00  8.42           O  
ANISOU  608  O   GLU A  82     1160   1160    879     10     84     -4       O  
ATOM    609  CB  GLU A  82       3.386  -7.084  13.780  1.00 11.19           C  
ANISOU  609  CB  GLU A  82     1526   1478   1246    -20    -44   -106       C  
ATOM    610  CG AGLU A  82       3.509  -7.865  12.479  0.50 13.87           C  
ANISOU  610  CG AGLU A  82     1792   2047   1429     87     12    -54       C  
ATOM    611  CG BGLU A  82       2.057  -7.829  13.913  0.50 15.80           C  
ANISOU  611  CG BGLU A  82     1917   2155   1928    -82     22    -17       C  
ATOM    612  CD AGLU A  82       3.270  -9.351  12.549  0.50 21.13           C  
ANISOU  612  CD AGLU A  82     2778   2528   2723     -2    -49    -10       C  
ATOM    613  CD BGLU A  82       2.217  -9.319  14.129  0.50 22.67           C  
ANISOU  613  CD BGLU A  82     2997   2637   2979     58     62     89       C  
ATOM    614  OE1AGLU A  82       2.683  -9.861  13.529  0.50 25.61           O  
ANISOU  614  OE1AGLU A  82     3286   3434   3010     88     90    153       O  
ATOM    615  OE2AGLU A  82       3.660 -10.025  11.569  0.50 24.82           O1-
ANISOU  615  OE2AGLU A  82     3264   3257   2907     39     37   -105       O1-
ATOM    616  OE1BGLU A  82       3.377  -9.780  14.177  0.50 27.87           O  
ANISOU  616  OE1BGLU A  82     3289   3454   3843    104    -36     99       O  
ATOM    617  OE2BGLU A  82       1.185 -10.028  14.233  0.50 25.29           O1-
ANISOU  617  OE2BGLU A  82     3097   3039   3472   -115    -40    -20       O1-
ATOM    618  N   PHE A  83       3.618  -4.739  15.919  1.00  7.71           N  
ANISOU  618  N   PHE A  83     1089    943    895     61     49    -50       N  
ATOM    619  CA  PHE A  83       3.260  -4.107  17.161  1.00  7.24           C  
ANISOU  619  CA  PHE A  83     1075    873    801     -1     87     27       C  
ATOM    620  C   PHE A  83       2.766  -2.667  16.939  1.00  7.71           C  
ANISOU  620  C   PHE A  83     1113    982    832     75     52    -59       C  
ATOM    621  O   PHE A  83       1.706  -2.300  17.439  1.00  6.95           O  
ANISOU  621  O   PHE A  83     1179    890    569    -10    127      2       O  
ATOM    622  CB  PHE A  83       4.442  -4.150  18.125  1.00  8.34           C  
ANISOU  622  CB  PHE A  83     1162   1039    966     26     -4     27       C  
ATOM    623  CG  PHE A  83       4.273  -3.275  19.325  1.00  8.66           C  
ANISOU  623  CG  PHE A  83     1072   1104   1112      5    131      5       C  
ATOM    624  CD1 PHE A  83       3.464  -3.656  20.362  1.00  9.83           C  
ANISOU  624  CD1 PHE A  83     1279   1294   1159    -21     53     80       C  
ATOM    625  CD2 PHE A  83       4.997  -2.079  19.444  1.00  9.60           C  
ANISOU  625  CD2 PHE A  83     1342   1302   1000   -178    -68   -189       C  
ATOM    626  CE1 PHE A  83       3.315  -2.812  21.474  1.00  9.44           C  
ANISOU  626  CE1 PHE A  83     1368   1206   1013    116     39    207       C  
ATOM    627  CE2 PHE A  83       4.843  -1.249  20.542  1.00  9.90           C  
ANISOU  627  CE2 PHE A  83     1293   1101   1365    -21     -2   -163       C  
ATOM    628  CZ  PHE A  83       4.008  -1.612  21.543  1.00  9.49           C  
ANISOU  628  CZ  PHE A  83     1374   1231   1000    164   -133    -66       C  
ATOM    629  N   LEU A  84       3.520  -1.861  16.178  1.00  7.00           N  
ANISOU  629  N   LEU A  84     1091    945    623    122     -9     69       N  
ATOM    630  CA  LEU A  84       3.098  -0.502  15.877  1.00  8.14           C  
ANISOU  630  CA  LEU A  84     1144   1057    891    -68    -29    -42       C  
ATOM    631  C   LEU A  84       1.755  -0.456  15.175  1.00  7.36           C  
ANISOU  631  C   LEU A  84     1135   1046    616     58     61    116       C  
ATOM    632  O   LEU A  84       0.928   0.413  15.471  1.00  7.33           O  
ANISOU  632  O   LEU A  84     1157   1005    621    -10     74    -67       O  
ATOM    633  CB  LEU A  84       4.183   0.212  15.075  1.00  8.64           C  
ANISOU  633  CB  LEU A  84     1211   1110    962    -27    -42     61       C  
ATOM    634  CG  LEU A  84       5.510   0.499  15.788  1.00  8.76           C  
ANISOU  634  CG  LEU A  84     1166   1169    990     24    -55     81       C  
ATOM    635  CD1 LEU A  84       6.517   1.017  14.773  1.00  9.41           C  
ANISOU  635  CD1 LEU A  84     1238   1175   1161    109     11     35       C  
ATOM    636  CD2 LEU A  84       5.349   1.481  16.930  1.00 10.01           C  
ANISOU  636  CD2 LEU A  84     1252   1312   1239    -49    -46    -40       C  
ATOM    637  N   GLU A  85       1.554  -1.324  14.190  1.00  7.58           N  
ANISOU  637  N   GLU A  85     1204    989    686    -17      2    162       N  
ATOM    638  CA  GLU A  85       0.282  -1.358  13.512  1.00  8.25           C  
ANISOU  638  CA  GLU A  85     1111   1124    898     25     36    -42       C  
ATOM    639  C   GLU A  85      -0.865  -1.702  14.451  1.00  8.54           C  
ANISOU  639  C   GLU A  85     1184   1181    877     21     -6   -101       C  
ATOM    640  O   GLU A  85      -1.954  -1.115  14.397  1.00  9.23           O  
ANISOU  640  O   GLU A  85     1271   1257    979    135      1    -96       O  
ATOM    641  CB  GLU A  85       0.342  -2.325  12.325  1.00  8.65           C  
ANISOU  641  CB  GLU A  85     1302   1249    734     45     21    -14       C  
ATOM    642  CG  GLU A  85      -0.968  -2.560  11.575  1.00  8.82           C  
ANISOU  642  CG  GLU A  85     1234   1292    822     17     30    -48       C  
ATOM    643  CD  GLU A  85      -1.476  -1.401  10.709  1.00  8.54           C  
ANISOU  643  CD  GLU A  85     1172   1213    857    -36     44    -59       C  
ATOM    644  OE1 GLU A  85      -0.909  -0.309  10.664  1.00  8.20           O  
ANISOU  644  OE1 GLU A  85     1473   1148    494    -87    249    -52       O  
ATOM    645  OE2 GLU A  85      -2.466  -1.626   9.999  1.00  8.91           O1-
ANISOU  645  OE2 GLU A  85     1336   1249    798     59    -61   -118       O1-
ATOM    646  N   ALA A  86      -0.595  -2.583  15.391  1.00  8.47           N  
ANISOU  646  N   ALA A  86     1135   1054   1028    -52     51    -22       N  
ATOM    647  CA  ALA A  86      -1.642  -2.987  16.346  1.00  9.51           C  
ANISOU  647  CA  ALA A  86     1306   1250   1055    -27     70    -25       C  
ATOM    648  C   ALA A  86      -1.977  -1.926  17.399  1.00  9.85           C  
ANISOU  648  C   ALA A  86     1285   1291   1167    -47    150    -16       C  
ATOM    649  O   ALA A  86      -3.173  -1.760  17.744  1.00 12.77           O  
ANISOU  649  O   ALA A  86     1464   1773   1613     32    385   -155       O  
ATOM    650  CB  ALA A  86      -1.256  -4.294  17.023  1.00 10.26           C  
ANISOU  650  CB  ALA A  86     1474   1178   1246    -72     93    -22       C  
ATOM    651  N   VAL A  87      -0.997  -1.233  17.931  1.00  8.77           N  
ANISOU  651  N   VAL A  87     1265   1138    929     -7    199     34       N  
ATOM    652  CA  VAL A  87      -1.225  -0.288  19.054  1.00  9.06           C  
ANISOU  652  CA  VAL A  87     1302   1193    946     -8    124    -11       C  
ATOM    653  C   VAL A  87      -1.466   1.153  18.632  1.00  9.65           C  
ANISOU  653  C   VAL A  87     1463   1226    976     43    120    -53       C  
ATOM    654  O   VAL A  87      -2.128   1.906  19.350  1.00 11.42           O  
ANISOU  654  O   VAL A  87     1877   1351   1110    283    184     75       O  
ATOM    655  CB  VAL A  87      -0.125  -0.385  20.122  1.00  8.94           C  
ANISOU  655  CB  VAL A  87     1337   1118    941    132     83     67       C  
ATOM    656  CG1 VAL A  87      -0.031  -1.818  20.599  1.00  9.85           C  
ANISOU  656  CG1 VAL A  87     1365   1231   1145     60    -64     76       C  
ATOM    657  CG2 VAL A  87       1.202   0.152  19.700  1.00 10.29           C  
ANISOU  657  CG2 VAL A  87     1471   1161   1277     90   -113   -149       C  
ATOM    658  N   LEU A  88      -0.953   1.546  17.471  1.00  8.26           N  
ANISOU  658  N   LEU A  88     1331   1123    684     -4    -33    -10       N  
ATOM    659  CA  LEU A  88      -1.221   2.881  16.912  1.00  8.76           C  
ANISOU  659  CA  LEU A  88     1321   1096    910     -6      7    -24       C  
ATOM    660  C   LEU A  88      -2.296   2.677  15.869  1.00  8.56           C  
ANISOU  660  C   LEU A  88     1225   1080    945     33     -4     49       C  
ATOM    661  O   LEU A  88      -2.040   2.605  14.677  1.00  9.32           O  
ANISOU  661  O   LEU A  88     1444   1314    780    113    -17    -51       O  
ATOM    662  CB  LEU A  88       0.036   3.505  16.314  1.00  8.64           C  
ANISOU  662  CB  LEU A  88     1278   1147    858     15    -77    -12       C  
ATOM    663  CG  LEU A  88       1.210   3.614  17.296  1.00  9.33           C  
ANISOU  663  CG  LEU A  88     1314   1078   1149    -94    -67    -34       C  
ATOM    664  CD1 LEU A  88       2.439   4.133  16.590  1.00  9.50           C  
ANISOU  664  CD1 LEU A  88     1203   1199   1204      9   -170    233       C  
ATOM    665  CD2 LEU A  88       0.905   4.520  18.523  1.00 10.19           C  
ANISOU  665  CD2 LEU A  88     1448   1123   1298     19   -183     61       C  
ATOM    666  N   CYS A  89      -3.533   2.593  16.314  1.00 10.30           N  
ANISOU  666  N   CYS A  89     1302   1550   1062   -106    115    -96       N  
ATOM    667  CA  CYS A  89      -4.633   2.105  15.478  1.00 11.72           C  
ANISOU  667  CA  CYS A  89     1443   1572   1436   -166     59    -65       C  
ATOM    668  C   CYS A  89      -5.793   3.071  15.508  1.00 13.07           C  
ANISOU  668  C   CYS A  89     1524   1821   1618   -161    170    -60       C  
ATOM    669  O   CYS A  89      -5.804   4.015  16.286  1.00 12.05           O  
ANISOU  669  O   CYS A  89     1392   1731   1454   -249    137      2       O  
ATOM    670  CB  CYS A  89      -5.061   0.718  15.963  1.00 12.01           C  
ANISOU  670  CB  CYS A  89     1460   1565   1535   -144    138   -166       C  
ATOM    671  SG  CYS A  89      -5.631   0.669  17.678  1.00 15.50           S  
ANISOU  671  SG  CYS A  89     1913   2053   1920   -316    504     56       S  
ATOM    672  N   PRO A  90      -6.773   2.897  14.628  1.00 19.00           N  
ANISOU  672  N   PRO A  90     2264   2609   2345   -187     72   -104       N  
ATOM    673  CA  PRO A  90      -7.935   3.780  14.672  1.00 20.72           C  
ANISOU  673  CA  PRO A  90     2495   2787   2589   -112     94     31       C  
ATOM    674  C   PRO A  90      -8.720   3.695  15.998  1.00 21.89           C  
ANISOU  674  C   PRO A  90     2493   3013   2811    -74    186     41       C  
ATOM    675  O   PRO A  90      -8.680   2.626  16.655  1.00 22.82           O  
ANISOU  675  O   PRO A  90     2379   3273   3017   -131    316    175       O  
ATOM    676  CB  PRO A  90      -8.772   3.292  13.507  1.00 22.10           C  
ANISOU  676  CB  PRO A  90     2722   2840   2832   -175     60    -27       C  
ATOM    677  CG  PRO A  90      -7.783   2.717  12.604  1.00 21.71           C  
ANISOU  677  CG  PRO A  90     2651   2829   2767   -148     -7    -84       C  
ATOM    678  CD  PRO A  90      -6.792   1.989  13.453  1.00 19.10           C  
ANISOU  678  CD  PRO A  90     2196   2517   2542   -185    156    -93       C  
ATOM    679  N   PRO A  91      -9.433   4.754  16.364  1.00 22.42           N  
ANISOU  679  N   PRO A  91     2551   3011   2956    -79    241     44       N  
ATOM    680  CA  PRO A  91      -9.610   5.973  15.575  1.00 22.75           C  
ANISOU  680  CA  PRO A  91     2573   3107   2961     75    146    -37       C  
ATOM    681  C   PRO A  91      -8.505   7.010  15.659  1.00 22.18           C  
ANISOU  681  C   PRO A  91     2583   2974   2869     29    143     26       C  
ATOM    682  O   PRO A  91      -8.509   7.913  14.824  1.00 22.89           O  
ANISOU  682  O   PRO A  91     2451   3125   3121     69     81    107       O  
ATOM    683  CB  PRO A  91     -10.861   6.613  16.211  1.00 23.56           C  
ANISOU  683  CB  PRO A  91     2653   3151   3148     44    161    -52       C  
ATOM    684  CG  PRO A  91     -10.847   6.135  17.605  1.00 24.43           C  
ANISOU  684  CG  PRO A  91     2708   3359   3215     79    170     72       C  
ATOM    685  CD  PRO A  91     -10.245   4.780  17.608  1.00 22.90           C  
ANISOU  685  CD  PRO A  91     2643   3088   2968    -83    232     53       C  
ATOM    686  N   ARG A  92      -7.574   6.888  16.610  1.00 21.51           N  
ANISOU  686  N   ARG A  92     2563   2918   2693    110    192     34       N  
ATOM    687  CA  ARG A  92      -6.568   7.926  16.816  1.00 20.95           C  
ANISOU  687  CA  ARG A  92     2484   2801   2673    134    180   -128       C  
ATOM    688  C   ARG A  92      -5.498   7.986  15.704  1.00 18.90           C  
ANISOU  688  C   ARG A  92     2231   2512   2438     55    158    -74       C  
ATOM    689  O   ARG A  92      -5.075   9.069  15.350  1.00 19.63           O  
ANISOU  689  O   ARG A  92     2349   2530   2580     75    284   -316       O  
ATOM    690  CB  ARG A  92      -5.856   7.724  18.155  1.00 22.37           C  
ANISOU  690  CB  ARG A  92     2729   3010   2761    303    199    -59       C  
ATOM    691  CG  ARG A  92      -4.965   8.885  18.566  1.00 28.54           C  
ANISOU  691  CG  ARG A  92     3680   3577   3586     15    113      1       C  
ATOM    692  CD  ARG A  92      -4.106   8.523  19.767  1.00 36.40           C  
ANISOU  692  CD  ARG A  92     4387   4727   4714      1   -161    -40       C  
ATOM    693  NE  ARG A  92      -3.243   9.629  20.174  1.00 42.56           N  
ANISOU  693  NE  ARG A  92     5433   5534   5202     60    109    -27       N  
ATOM    694  CZ  ARG A  92      -2.395   9.576  21.196  1.00 46.97           C  
ANISOU  694  CZ  ARG A  92     6044   5870   5931     13     54     90       C  
ATOM    695  NH1 ARG A  92      -2.293   8.468  21.917  1.00 49.50           N1+
ANISOU  695  NH1 ARG A  92     6354   6189   6264      6     25   -106       N1+
ATOM    696  NH2 ARG A  92      -1.649  10.632  21.493  1.00 48.31           N  
ANISOU  696  NH2 ARG A  92     6210   6196   5948     39    -23     10       N  
ATOM    697  N   TYR A  93      -5.097   6.833  15.167  1.00 16.84           N  
ANISOU  697  N   TYR A  93     2096   2105   2194      9    159     -5       N  
ATOM    698  CA  TYR A  93      -4.075   6.754  14.108  1.00 15.79           C  
ANISOU  698  CA  TYR A  93     1979   1979   2038     27     33      9       C  
ATOM    699  C   TYR A  93      -4.595   5.921  12.949  1.00 15.47           C  
ANISOU  699  C   TYR A  93     1957   1870   2050     46    106    -77       C  
ATOM    700  O   TYR A  93      -5.441   5.057  13.123  1.00 17.58           O  
ANISOU  700  O   TYR A  93     2271   2319   2087   -118    237   -113       O  
ATOM    701  CB  TYR A  93      -2.837   6.082  14.644  1.00 15.39           C  
ANISOU  701  CB  TYR A  93     1886   1934   2025    183    105   -129       C  
ATOM    702  CG  TYR A  93      -2.296   6.651  15.924  1.00 17.16           C  
ANISOU  702  CG  TYR A  93     2093   2208   2216    164     55    -53       C  
ATOM    703  CD1 TYR A  93      -1.444   7.743  15.920  1.00 18.07           C  
ANISOU  703  CD1 TYR A  93     2049   2510   2305    -31    164   -122       C  
ATOM    704  CD2 TYR A  93      -2.627   6.097  17.140  1.00 18.86           C  
ANISOU  704  CD2 TYR A  93     2575   2297   2291    160     71      0       C  
ATOM    705  CE1 TYR A  93      -0.945   8.313  17.108  1.00 21.16           C  
ANISOU  705  CE1 TYR A  93     2343   2949   2747   -147      4   -175       C  
ATOM    706  CE2 TYR A  93      -2.152   6.654  18.326  1.00 19.92           C  
ANISOU  706  CE2 TYR A  93     2746   2563   2259    213    -22     -8       C  
ATOM    707  CZ  TYR A  93      -1.273   7.742  18.309  1.00 19.92           C  
ANISOU  707  CZ  TYR A  93     2420   2826   2322    182    -78   -359       C  
ATOM    708  OH  TYR A  93      -0.758   8.291  19.518  1.00 24.36           O  
ANISOU  708  OH  TYR A  93     2971   3683   2602    230   -257   -507       O  
ATOM    709  N   PRO A  94      -4.127   6.185  11.739  1.00 14.10           N  
ANISOU  709  N   PRO A  94     1726   1754   1876     20     26    -21       N  
ATOM    710  CA  PRO A  94      -4.618   5.431  10.591  1.00 14.66           C  
ANISOU  710  CA  PRO A  94     1763   1929   1875    -56     47    -60       C  
ATOM    711  C   PRO A  94      -4.061   4.028  10.529  1.00 14.98           C  
ANISOU  711  C   PRO A  94     1859   1982   1850    -13    -18    -99       C  
ATOM    712  O   PRO A  94      -2.915   3.793  10.872  1.00 13.18           O  
ANISOU  712  O   PRO A  94     1622   1809   1574   -131     78    -36       O  
ATOM    713  CB  PRO A  94      -4.106   6.225   9.390  1.00 14.60           C  
ANISOU  713  CB  PRO A  94     1905   1788   1851     69    -93     37       C  
ATOM    714  CG  PRO A  94      -2.806   6.805   9.909  1.00 15.39           C  
ANISOU  714  CG  PRO A  94     1950   1902   1995     31     94    -69       C  
ATOM    715  CD  PRO A  94      -3.159   7.216  11.327  1.00 14.51           C  
ANISOU  715  CD  PRO A  94     1881   1642   1987     44     35     -3       C  
ATOM    716  N   LYS A  95      -4.909   3.091  10.100  1.00 14.75           N  
ANISOU  716  N   LYS A  95     1658   1961   1984   -116     53    -34       N  
ATOM    717  CA  LYS A  95      -4.487   1.745   9.753  1.00 15.47           C  
ANISOU  717  CA  LYS A  95     1864   2032   1980    -41    -24    -36       C  
ATOM    718  C   LYS A  95      -3.598   1.819   8.507  1.00 14.31           C  
ANISOU  718  C   LYS A  95     1819   1894   1723    -82    -27     -7       C  
ATOM    719  O   LYS A  95      -3.976   2.430   7.499  1.00 16.98           O  
ANISOU  719  O   LYS A  95     2191   2432   1829    258    182     60       O  
ATOM    720  CB  LYS A  95      -5.701   0.830   9.581  1.00 17.19           C  
ANISOU  720  CB  LYS A  95     2067   2238   2225   -171     27   -148       C  
ATOM    721  CG  LYS A  95      -5.352  -0.603   9.216  1.00 21.43           C  
ANISOU  721  CG  LYS A  95     2550   2654   2939    -71    -18   -197       C  
ATOM    722  CD  LYS A  95      -6.602  -1.454   9.061  1.00 24.32           C  
ANISOU  722  CD  LYS A  95     2749   3074   3415   -160   -109   -196       C  
ATOM    723  CE  LYS A  95      -6.253  -2.887   8.696  1.00 30.73           C  
ANISOU  723  CE  LYS A  95     3880   3969   3825   -121     33    -14       C  
ATOM    724  NZ  LYS A  95      -7.468  -3.733   8.541  1.00 35.54           N1+
ANISOU  724  NZ  LYS A  95     4275   4494   4734     27    140    -35       N1+
ATOM    725  N   LEU A  96      -2.426   1.207   8.543  1.00 12.89           N  
ANISOU  725  N   LEU A  96     1683   1685   1526   -159      7    -59       N  
ATOM    726  CA  LEU A  96      -1.517   1.238   7.393  1.00 13.07           C  
ANISOU  726  CA  LEU A  96     1683   1657   1624   -144     73    -26       C  
ATOM    727  C   LEU A  96      -1.390  -0.074   6.654  1.00 13.68           C  
ANISOU  727  C   LEU A  96     1866   1650   1682   -264     38    -57       C  
ATOM    728  O   LEU A  96      -0.837  -0.104   5.556  1.00 13.78           O  
ANISOU  728  O   LEU A  96     1702   1811   1720   -452     39   -288       O  
ATOM    729  CB  LEU A  96      -0.101   1.697   7.771  1.00 12.14           C  
ANISOU  729  CB  LEU A  96     1595   1466   1553   -153    101     56       C  
ATOM    730  CG  LEU A  96      -0.001   3.070   8.447  1.00 13.10           C  
ANISOU  730  CG  LEU A  96     1722   1735   1521   -122    153    -56       C  
ATOM    731  CD1 LEU A  96       1.439   3.355   8.777  1.00 12.63           C  
ANISOU  731  CD1 LEU A  96     1772   1510   1517   -156     61    111       C  
ATOM    732  CD2 LEU A  96      -0.544   4.136   7.507  1.00 13.67           C  
ANISOU  732  CD2 LEU A  96     1597   1779   1815     20    188   -117       C  
ATOM    733  N   ALA A  97      -2.023  -1.131   7.156  1.00 13.76           N  
ANISOU  733  N   ALA A  97     1994   1556   1676   -266    184   -188       N  
ATOM    734  CA  ALA A  97      -1.948  -2.410   6.454  1.00 14.33           C  
ANISOU  734  CA  ALA A  97     1975   1622   1847   -223    140    -64       C  
ATOM    735  C   ALA A  97      -2.639  -2.330   5.092  1.00 15.02           C  
ANISOU  735  C   ALA A  97     2005   1744   1958   -247    122    -70       C  
ATOM    736  O   ALA A  97      -3.689  -1.735   4.942  1.00 15.89           O  
ANISOU  736  O   ALA A  97     2194   1920   1922   -342    151   -299       O  
ATOM    737  CB  ALA A  97      -2.669  -3.484   7.315  1.00 15.59           C  
ANISOU  737  CB  ALA A  97     2332   1722   1869   -270    117     32       C  
ATOM    738  N   ALA A  98      -2.024  -2.967   4.098  1.00 14.74           N  
ANISOU  738  N   ALA A  98     2016   1672   1909   -193    168    -46       N  
ATOM    739  CA  ALA A  98      -2.652  -3.081   2.806  1.00 14.89           C  
ANISOU  739  CA  ALA A  98     1886   1811   1957   -157    132    -88       C  
ATOM    740  C   ALA A  98      -3.977  -3.837   2.862  1.00 13.96           C  
ANISOU  740  C   ALA A  98     1836   1687   1778   -151     88    -91       C  
ATOM    741  O   ALA A  98      -4.159  -4.736   3.653  1.00 15.15           O  
ANISOU  741  O   ALA A  98     2313   1739   1701   -160    110   -127       O  
ATOM    742  CB  ALA A  98      -1.717  -3.745   1.805  1.00 15.14           C  
ANISOU  742  CB  ALA A  98     2015   1840   1897   -145    177    -60       C  
ATOM    743  N   LEU A  99      -4.882  -3.469   1.971  1.00 11.52           N  
ANISOU  743  N   LEU A  99     1571   1386   1417   -211    122   -106       N  
ATOM    744  CA  LEU A  99      -6.163  -4.141   1.912  1.00 11.81           C  
ANISOU  744  CA  LEU A  99     1625   1499   1364   -242    136    -95       C  
ATOM    745  C   LEU A  99      -6.086  -5.429   1.061  1.00 11.67           C  
ANISOU  745  C   LEU A  99     1582   1514   1335   -234     64   -105       C  
ATOM    746  O   LEU A  99      -6.888  -6.343   1.233  1.00 13.54           O  
ANISOU  746  O   LEU A  99     2006   1632   1505   -445    222   -118       O  
ATOM    747  CB  LEU A  99      -7.160  -3.203   1.316  1.00 12.17           C  
ANISOU  747  CB  LEU A  99     1618   1464   1542   -306     14   -181       C  
ATOM    748  CG  LEU A  99      -7.393  -1.807   1.898  1.00 16.45           C  
ANISOU  748  CG  LEU A  99     2246   1817   2187    -20    167    -74       C  
ATOM    749  CD1 LEU A  99      -8.553  -1.097   1.208  1.00 19.77           C  
ANISOU  749  CD1 LEU A  99     2439   2480   2591    -31    109     46       C  
ATOM    750  CD2 LEU A  99      -7.630  -1.968   3.348  1.00 19.27           C  
ANISOU  750  CD2 LEU A  99     2667   2285   2367    -55     81    -90       C  
ATOM    751  N   ASN A 100      -5.160  -5.491   0.121  1.00  9.92           N  
ANISOU  751  N   ASN A 100     1407   1251   1110   -111    -30    -19       N  
ATOM    752  CA  ASN A 100      -4.994  -6.652  -0.782  1.00  9.79           C  
ANISOU  752  CA  ASN A 100     1459   1240   1019   -226    -70      5       C  
ATOM    753  C   ASN A 100      -3.757  -7.450  -0.387  1.00 11.41           C  
ANISOU  753  C   ASN A 100     1711   1420   1203    -52     32     39       C  
ATOM    754  O   ASN A 100      -2.650  -6.893  -0.384  1.00  9.75           O  
ANISOU  754  O   ASN A 100     1387   1429    886    -84    -33    268       O  
ATOM    755  CB  ASN A 100      -4.834  -6.126  -2.207  1.00  9.70           C  
ANISOU  755  CB  ASN A 100     1530   1019   1134   -165    -13     54       C  
ATOM    756  CG  ASN A 100      -6.035  -5.414  -2.686  1.00 11.79           C  
ANISOU  756  CG  ASN A 100     1719   1389   1373    -41   -267     10       C  
ATOM    757  ND2 ASN A 100      -6.054  -4.074  -2.573  1.00 11.74           N  
ANISOU  757  ND2 ASN A 100     2279   1381    799   -191   -219    166       N  
ATOM    758  OD1 ASN A 100      -6.991  -6.063  -3.134  1.00 12.88           O  
ANISOU  758  OD1 ASN A 100     2109   1442   1340   -242   -419    293       O  
ATOM    759  N   PRO A 101      -3.873  -8.733  -0.033  1.00 10.08           N  
ANISOU  759  N   PRO A 101     1387   1293   1148   -113      2     77       N  
ATOM    760  CA  PRO A 101      -2.682  -9.475   0.372  1.00 11.30           C  
ANISOU  760  CA  PRO A 101     1651   1299   1343    -54    -54    135       C  
ATOM    761  C   PRO A 101      -1.634  -9.485  -0.700  1.00 10.83           C  
ANISOU  761  C   PRO A 101     1496   1210   1408     26    -86     85       C  
ATOM    762  O   PRO A 101      -0.474  -9.570  -0.388  1.00 11.05           O  
ANISOU  762  O   PRO A 101     1704   1149   1345   -101    -54    129       O  
ATOM    763  CB  PRO A 101      -3.242 -10.851   0.738  1.00 12.15           C  
ANISOU  763  CB  PRO A 101     1712   1427   1477    -81    -95    289       C  
ATOM    764  CG  PRO A 101      -4.699 -10.616   0.957  1.00 12.60           C  
ANISOU  764  CG  PRO A 101     1779   1288   1718   -112    -23    179       C  
ATOM    765  CD  PRO A 101      -5.125  -9.630  -0.094  1.00 10.45           C  
ANISOU  765  CD  PRO A 101     1515   1255   1197    -13     -6    151       C  
ATOM    766  N   GLU A 102      -2.051  -9.426  -1.960  1.00 10.12           N  
ANISOU  766  N   GLU A 102     1422   1118   1302   -121   -103      0       N  
ATOM    767  CA  GLU A 102      -1.140  -9.425  -3.081  1.00 10.81           C  
ANISOU  767  CA  GLU A 102     1511   1239   1356    -70    -45    -19       C  
ATOM    768  C   GLU A 102      -0.177  -8.236  -3.002  1.00  9.85           C  
ANISOU  768  C   GLU A 102     1255   1280   1206    -63    -54    -26       C  
ATOM    769  O   GLU A 102       0.924  -8.308  -3.452  1.00 10.79           O  
ANISOU  769  O   GLU A 102     1504   1377   1217    -26     88   -136       O  
ATOM    770  CB  GLU A 102      -1.943  -9.417  -4.427  1.00 12.30           C  
ANISOU  770  CB  GLU A 102     1721   1600   1350     -6      0   -146       C  
ATOM    771  CG  GLU A 102      -2.947 -10.572  -4.643  1.00 13.74           C  
ANISOU  771  CG  GLU A 102     1812   1692   1715     29    -18     39       C  
ATOM    772  CD  GLU A 102      -4.344 -10.471  -4.010  1.00 15.04           C  
ANISOU  772  CD  GLU A 102     2012   1871   1831     60     31   -249       C  
ATOM    773  OE1 GLU A 102      -4.599  -9.583  -3.183  1.00 12.45           O  
ANISOU  773  OE1 GLU A 102     1887   1320   1522     -4     -3   -185       O  
ATOM    774  OE2 GLU A 102      -5.182 -11.382  -4.315  1.00 16.19           O1-
ANISOU  774  OE2 GLU A 102     2433   1699   2019     24   -104    214       O1-
ATOM    775  N   SER A 103      -0.583  -7.147  -2.383  1.00  8.50           N  
ANISOU  775  N   SER A 103     1272   1052    904    -89     48     67       N  
ATOM    776  CA  SER A 103       0.323  -6.009  -2.242  1.00  9.27           C  
ANISOU  776  CA  SER A 103     1289   1209   1022    -50    130     31       C  
ATOM    777  C   SER A 103       1.500  -6.284  -1.346  1.00  9.20           C  
ANISOU  777  C   SER A 103     1359   1138    996   -100     63    -14       C  
ATOM    778  O   SER A 103       2.555  -5.640  -1.471  1.00  9.05           O  
ANISOU  778  O   SER A 103     1340   1148    950   -133    -21     14       O  
ATOM    779  CB  SER A 103      -0.442  -4.794  -1.709  1.00  8.84           C  
ANISOU  779  CB  SER A 103     1136   1125   1097      9     20      8       C  
ATOM    780  OG  SER A 103      -1.415  -4.342  -2.637  1.00  9.46           O  
ANISOU  780  OG  SER A 103     1645   1185    762     35    -29    147       O  
ATOM    781  N   ASN A 104       1.341  -7.265  -0.448  1.00  8.62           N  
ANISOU  781  N   ASN A 104     1142   1154    975    -63    131    109       N  
ATOM    782  CA  ASN A 104       2.343  -7.619   0.502  1.00 10.29           C  
ANISOU  782  CA  ASN A 104     1430   1248   1231    -39     15     27       C  
ATOM    783  C   ASN A 104       3.343  -8.612  -0.049  1.00 11.02           C  
ANISOU  783  C   ASN A 104     1557   1297   1331    -15      4    105       C  
ATOM    784  O   ASN A 104       4.339  -8.819   0.603  1.00 13.89           O  
ANISOU  784  O   ASN A 104     1771   1476   2027    323   -130     93       O  
ATOM    785  CB  ASN A 104       1.710  -8.175   1.808  1.00 11.03           C  
ANISOU  785  CB  ASN A 104     1611   1333   1245    -41    -59    117       C  
ATOM    786  CG  ASN A 104       0.837  -7.189   2.505  1.00 11.62           C  
ANISOU  786  CG  ASN A 104     1815   1494   1106    -38     -8    159       C  
ATOM    787  ND2 ASN A 104      -0.224  -7.671   3.143  1.00 13.37           N  
ANISOU  787  ND2 ASN A 104     1946   1675   1457   -254     27     27       N  
ATOM    788  OD1 ASN A 104       1.096  -5.986   2.468  1.00 13.59           O  
ANISOU  788  OD1 ASN A 104     2250   1506   1406   -371    452   -120       O  
ATOM    789  N   THR A 105       3.103  -9.175  -1.218  1.00 10.85           N  
ANISOU  789  N   THR A 105     1598   1222   1301     93     14    140       N  
ATOM    790  CA  THR A 105       4.028 -10.095  -1.884  1.00 13.01           C  
ANISOU  790  CA  THR A 105     1748   1570   1623    162     29     25       C  
ATOM    791  C   THR A 105       4.660  -9.514  -3.166  1.00 12.43           C  
ANISOU  791  C   THR A 105     1597   1585   1540    173     22    111       C  
ATOM    792  O   THR A 105       5.734  -9.937  -3.633  1.00 14.59           O  
ANISOU  792  O   THR A 105     1896   1860   1788    511    163    187       O  
ATOM    793  CB  THR A 105       3.338 -11.453  -2.192  1.00 13.00           C  
ANISOU  793  CB  THR A 105     1847   1545   1548    173    177    -22       C  
ATOM    794  CG2 THR A 105       2.840 -12.095  -0.941  1.00 17.05           C  
ANISOU  794  CG2 THR A 105     2507   1701   2269     -8    113    169       C  
ATOM    795  OG1 THR A 105       2.194 -11.287  -3.043  1.00 17.20           O  
ANISOU  795  OG1 THR A 105     2282   1854   2399     39    -39   -148       O  
ATOM    796  N   ALA A 106       4.039  -8.490  -3.742  1.00 10.12           N  
ANISOU  796  N   ALA A 106     1331   1147   1367    158     85    -43       N  
ATOM    797  CA  ALA A 106       4.560  -7.913  -4.972  1.00 10.74           C  
ANISOU  797  CA  ALA A 106     1273   1416   1392     29      1     67       C  
ATOM    798  C   ALA A 106       5.963  -7.327  -4.803  1.00 10.77           C  
ANISOU  798  C   ALA A 106     1292   1443   1357     74    -23    -91       C  
ATOM    799  O   ALA A 106       6.176  -6.494  -3.957  1.00 11.90           O  
ANISOU  799  O   ALA A 106     1280   1546   1693     39     -4   -306       O  
ATOM    800  CB  ALA A 106       3.626  -6.842  -5.439  1.00 12.11           C  
ANISOU  800  CB  ALA A 106     1311   1666   1622     -4     83    312       C  
ATOM    801  N   GLY A 107       6.900  -7.790  -5.612  1.00 10.63           N  
ANISOU  801  N   GLY A 107     1318   1535   1186     76    -18     22       N  
ATOM    802  CA  GLY A 107       8.248  -7.285  -5.597  1.00 10.33           C  
ANISOU  802  CA  GLY A 107     1270   1540   1114    125     44    -56       C  
ATOM    803  C   GLY A 107       9.115  -7.790  -4.456  1.00 10.23           C  
ANISOU  803  C   GLY A 107     1375   1425   1085    147     95   -130       C  
ATOM    804  O   GLY A 107      10.245  -7.363  -4.378  1.00  9.97           O  
ANISOU  804  O   GLY A 107     1317   1600    869    136   -178   -259       O  
ATOM    805  N   LEU A 108       8.610  -8.704  -3.635  1.00 11.56           N  
ANISOU  805  N   LEU A 108     1346   1712   1333    115     91      0       N  
ATOM    806  CA  LEU A 108       9.313  -9.184  -2.433  1.00 13.08           C  
ANISOU  806  CA  LEU A 108     1633   1878   1457     -3     40     57       C  
ATOM    807  C   LEU A 108      10.630  -9.851  -2.776  1.00 12.17           C  
ANISOU  807  C   LEU A 108     1531   1770   1323     36    -12    153       C  
ATOM    808  O   LEU A 108      11.581  -9.784  -2.012  1.00 13.31           O  
ANISOU  808  O   LEU A 108     1582   2352   1121     74    -64    155       O  
ATOM    809  CB  LEU A 108       8.433 -10.187  -1.647  1.00 16.47           C  
ANISOU  809  CB  LEU A 108     2067   2149   2039   -105     33     69       C  
ATOM    810  CG  LEU A 108       8.285  -9.952  -0.153  1.00 20.86           C  
ANISOU  810  CG  LEU A 108     2723   2695   2507   -141    105    101       C  
ATOM    811  CD1 LEU A 108       8.072  -8.505   0.169  1.00 20.97           C  
ANISOU  811  CD1 LEU A 108     2717   2591   2657     19      5   -165       C  
ATOM    812  CD2 LEU A 108       7.116 -10.761   0.392  1.00 22.08           C  
ANISOU  812  CD2 LEU A 108     2750   2957   2680   -135     67    224       C  
ATOM    813  N   ASP A 109      10.729 -10.450  -3.942  1.00  9.99           N  
ANISOU  813  N   ASP A 109     1214   1508   1071    162   -181    160       N  
ATOM    814  CA  ASP A 109      11.926 -11.185  -4.359  1.00 10.07           C  
ANISOU  814  CA  ASP A 109     1351   1398   1076     35     17     53       C  
ATOM    815  C   ASP A 109      12.998 -10.341  -5.025  1.00  8.65           C  
ANISOU  815  C   ASP A 109     1230   1251    805    108     23    -40       C  
ATOM    816  O   ASP A 109      14.075 -10.832  -5.295  1.00 10.08           O  
ANISOU  816  O   ASP A 109     1271   1570    988    243    -52     79       O  
ATOM    817  CB  ASP A 109      11.505 -12.314  -5.294  1.00 10.41           C  
ANISOU  817  CB  ASP A 109     1450   1293   1211     34    -24    115       C  
ATOM    818  CG  ASP A 109      10.886 -11.834  -6.591  1.00 12.63           C  
ANISOU  818  CG  ASP A 109     1621   1712   1466    -54   -146   -115       C  
ATOM    819  OD1 ASP A 109      10.383 -10.709  -6.669  1.00 12.99           O  
ANISOU  819  OD1 ASP A 109     2247   1701    985      9   -174    -86       O  
ATOM    820  OD2 ASP A 109      10.827 -12.613  -7.593  1.00 17.10           O1-
ANISOU  820  OD2 ASP A 109     2326   2440   1729    246   -365   -409       O1-
ATOM    821  N   ILE A 110      12.725  -9.075  -5.292  1.00  8.52           N  
ANISOU  821  N   ILE A 110     1164   1253    820    183    -55    -30       N  
ATOM    822  CA  ILE A 110      13.660  -8.251  -6.035  1.00  7.50           C  
ANISOU  822  CA  ILE A 110     1020   1071    757    182    -65    -28       C  
ATOM    823  C   ILE A 110      14.972  -8.038  -5.279  1.00  7.78           C  
ANISOU  823  C   ILE A 110      914   1367    672    116      4    -23       C  
ATOM    824  O   ILE A 110      16.047  -8.164  -5.844  1.00  7.54           O  
ANISOU  824  O   ILE A 110      965   1370    530    226     52    -44       O  
ATOM    825  CB  ILE A 110      13.039  -6.881  -6.435  1.00  7.77           C  
ANISOU  825  CB  ILE A 110     1121   1083    748    201   -105    -41       C  
ATOM    826  CG1 ILE A 110      11.920  -7.098  -7.449  1.00  8.57           C  
ANISOU  826  CG1 ILE A 110     1026   1250    979    125     20    -46       C  
ATOM    827  CG2 ILE A 110      14.106  -5.962  -6.956  1.00  8.71           C  
ANISOU  827  CG2 ILE A 110     1233   1194    881    135     10    -69       C  
ATOM    828  CD1 ILE A 110      11.035  -5.894  -7.624  1.00  8.86           C  
ANISOU  828  CD1 ILE A 110     1111   1174   1080     -6    -36     49       C  
ATOM    829  N   PHE A 111      14.898  -7.741  -3.985  1.00  7.44           N  
ANISOU  829  N   PHE A 111      860   1322    642     17     15     26       N  
ATOM    830  CA  PHE A 111      16.083  -7.347  -3.281  1.00  7.61           C  
ANISOU  830  CA  PHE A 111      949   1230    711     45     -2    -21       C  
ATOM    831  C   PHE A 111      17.139  -8.478  -3.271  1.00  8.57           C  
ANISOU  831  C   PHE A 111     1130   1264    861     30     18     36       C  
ATOM    832  O   PHE A 111      18.330  -8.222  -3.473  1.00  7.58           O  
ANISOU  832  O   PHE A 111     1078   1236    564     77    124    -83       O  
ATOM    833  CB  PHE A 111      15.735  -6.873  -1.864  1.00  8.62           C  
ANISOU  833  CB  PHE A 111     1074   1358    840     15     -6     -1       C  
ATOM    834  CG  PHE A 111      16.833  -6.103  -1.187  1.00  8.68           C  
ANISOU  834  CG  PHE A 111     1088   1256    953     88      0    -75       C  
ATOM    835  CD1 PHE A 111      17.200  -4.865  -1.678  1.00  8.62           C  
ANISOU  835  CD1 PHE A 111     1165   1198    909    134     95   -160       C  
ATOM    836  CD2 PHE A 111      17.524  -6.596  -0.076  1.00 11.46           C  
ANISOU  836  CD2 PHE A 111     1607   1484   1263   -351    -72    150       C  
ATOM    837  CE1 PHE A 111      18.206  -4.119  -1.068  1.00 10.34           C  
ANISOU  837  CE1 PHE A 111     1411   1282   1234     92     35   -120       C  
ATOM    838  CE2 PHE A 111      18.512  -5.823   0.532  1.00 13.52           C  
ANISOU  838  CE2 PHE A 111     1826   1888   1422    -69   -466     15       C  
ATOM    839  CZ  PHE A 111      18.859  -4.626  -0.002  1.00 11.93           C  
ANISOU  839  CZ  PHE A 111     1399   1757   1374   -167   -171   -214       C  
ATOM    840  N   ALA A 112      16.716  -9.724  -3.040  1.00  9.28           N  
ANISOU  840  N   ALA A 112     1197   1368    959     -2     50    139       N  
ATOM    841  CA  ALA A 112      17.672 -10.835  -3.020  1.00  9.76           C  
ANISOU  841  CA  ALA A 112     1303   1274   1131    -53     70     97       C  
ATOM    842  C   ALA A 112      18.277 -11.103  -4.387  1.00  8.90           C  
ANISOU  842  C   ALA A 112     1227   1135   1020     67     14     -2       C  
ATOM    843  O   ALA A 112      19.439 -11.497  -4.501  1.00  9.33           O  
ANISOU  843  O   ALA A 112     1261   1311    971     82    141     82       O  
ATOM    844  CB  ALA A 112      17.005 -12.106  -2.473  1.00 10.80           C  
ANISOU  844  CB  ALA A 112     1468   1381   1251     30     84    255       C  
ATOM    845  N   LYS A 113      17.507 -10.883  -5.443  1.00  7.97           N  
ANISOU  845  N   LYS A 113     1124    978    925    103    100    -16       N  
ATOM    846  CA  LYS A 113      18.037 -11.008  -6.821  1.00  8.75           C  
ANISOU  846  CA  LYS A 113     1213   1114    995    119     91    -62       C  
ATOM    847  C   LYS A 113      19.038  -9.914  -7.135  1.00  7.49           C  
ANISOU  847  C   LYS A 113     1081    983    779     84     41    -42       C  
ATOM    848  O   LYS A 113      20.066 -10.174  -7.757  1.00  7.67           O  
ANISOU  848  O   LYS A 113     1182   1082    650    135    136    -37       O  
ATOM    849  CB  LYS A 113      16.873 -11.071  -7.823  1.00 10.31           C  
ANISOU  849  CB  LYS A 113     1428   1427   1062    119    102   -206       C  
ATOM    850  CG  LYS A 113      16.110 -12.395  -7.586  1.00 11.64           C  
ANISOU  850  CG  LYS A 113     1498   1470   1455    105    -15   -106       C  
ATOM    851  CD  LYS A 113      14.836 -12.575  -8.364  1.00 13.39           C  
ANISOU  851  CD  LYS A 113     1821   1689   1575    236    -35   -164       C  
ATOM    852  CE  LYS A 113      14.254 -13.967  -8.166  1.00 16.06           C  
ANISOU  852  CE  LYS A 113     1657   2363   2081   -296    239   -127       C  
ATOM    853  NZ  LYS A 113      12.984 -14.103  -8.934  1.00 19.33           N1+
ANISOU  853  NZ  LYS A 113     2400   2671   2272     -9   -202     46       N1+
ATOM    854  N   PHE A 114      18.779  -8.700  -6.643  1.00  6.87           N  
ANISOU  854  N   PHE A 114     1030    984    593    101     90    -84       N  
ATOM    855  CA  PHE A 114      19.748  -7.631  -6.727  1.00  7.09           C  
ANISOU  855  CA  PHE A 114     1059    863    771    150     75    -30       C  
ATOM    856  C   PHE A 114      20.999  -7.984  -5.972  1.00  7.03           C  
ANISOU  856  C   PHE A 114     1038    962    668     -5    100     -3       C  
ATOM    857  O   PHE A 114      22.125  -7.747  -6.451  1.00  6.22           O  
ANISOU  857  O   PHE A 114      850    961    552    207     -2     23       O  
ATOM    858  CB  PHE A 114      19.104  -6.297  -6.188  1.00  7.43           C  
ANISOU  858  CB  PHE A 114      984   1067    772    170    248   -114       C  
ATOM    859  CG  PHE A 114      20.087  -5.353  -5.579  1.00  6.76           C  
ANISOU  859  CG  PHE A 114     1099    887    580    135    172    -42       C  
ATOM    860  CD1 PHE A 114      20.952  -4.586  -6.370  1.00  7.33           C  
ANISOU  860  CD1 PHE A 114     1004   1071    710    162     85   -162       C  
ATOM    861  CD2 PHE A 114      20.125  -5.200  -4.217  1.00  7.23           C  
ANISOU  861  CD2 PHE A 114      968   1151    625     85    206    -88       C  
ATOM    862  CE1 PHE A 114      21.873  -3.750  -5.787  1.00  7.12           C  
ANISOU  862  CE1 PHE A 114      857   1070    776     39     11     70       C  
ATOM    863  CE2 PHE A 114      21.027  -4.363  -3.614  1.00  7.64           C  
ANISOU  863  CE2 PHE A 114     1020   1254    629    168     25    -39       C  
ATOM    864  CZ  PHE A 114      21.911  -3.642  -4.371  1.00  8.39           C  
ANISOU  864  CZ  PHE A 114     1069   1146    971     80   -103    -72       C  
ATOM    865  N   SER A 115      20.862  -8.579  -4.774  1.00  7.31           N  
ANISOU  865  N   SER A 115      893   1029    852      9     42     88       N  
ATOM    866  CA  SER A 115      22.042  -8.881  -3.978  1.00  7.45           C  
ANISOU  866  CA  SER A 115      936   1076    819     17     67    116       C  
ATOM    867  C   SER A 115      22.921  -9.891  -4.708  1.00  7.54           C  
ANISOU  867  C   SER A 115     1110    966    788     36      1    293       C  
ATOM    868  O   SER A 115      24.137  -9.731  -4.752  1.00  7.80           O  
ANISOU  868  O   SER A 115      970   1083    911     74    -59    287       O  
ATOM    869  CB  SER A 115      21.629  -9.378  -2.588  1.00  7.93           C  
ANISOU  869  CB  SER A 115      979   1091    940     85      1     58       C  
ATOM    870  OG  SER A 115      20.950  -8.377  -1.876  1.00  9.40           O  
ANISOU  870  OG  SER A 115     1273   1457    842    168    126     18       O  
ATOM    871  N   ALA A 116      22.328 -10.934  -5.260  1.00  7.19           N  
ANISOU  871  N   ALA A 116     1073   1050    609    171     63    101       N  
ATOM    872  CA  ALA A 116      23.098 -11.939  -5.995  1.00  7.51           C  
ANISOU  872  CA  ALA A 116     1015   1008    829    135     69     67       C  
ATOM    873  C   ALA A 116      23.809 -11.297  -7.189  1.00  7.51           C  
ANISOU  873  C   ALA A 116     1078   1021    753    144     27     16       C  
ATOM    874  O   ALA A 116      24.980 -11.575  -7.450  1.00  7.68           O  
ANISOU  874  O   ALA A 116     1163   1076    678    187     43      4       O  
ATOM    875  CB  ALA A 116      22.212 -13.084  -6.416  1.00  8.93           C  
ANISOU  875  CB  ALA A 116     1290   1150    950    202    -10     -5       C  
ATOM    876  N   TYR A 117      23.089 -10.438  -7.935  1.00  6.59           N  
ANISOU  876  N   TYR A 117      831   1078    594    180    -32     51       N  
ATOM    877  CA  TYR A 117      23.656  -9.725  -9.051  1.00  6.93           C  
ANISOU  877  CA  TYR A 117      834    987    809    169     42     23       C  
ATOM    878  C   TYR A 117      24.841  -8.862  -8.653  1.00  7.19           C  
ANISOU  878  C   TYR A 117     1035    924    771    192    -38   -106       C  
ATOM    879  O   TYR A 117      25.917  -8.963  -9.270  1.00  7.16           O  
ANISOU  879  O   TYR A 117      918   1165    634    155    -98    -88       O  
ATOM    880  CB  TYR A 117      22.538  -8.889  -9.661  1.00  7.15           C  
ANISOU  880  CB  TYR A 117      891   1183    642    220      6   -226       C  
ATOM    881  CG  TYR A 117      22.902  -7.864 -10.718  1.00  6.54           C  
ANISOU  881  CG  TYR A 117      830   1062    593    281    -58    -70       C  
ATOM    882  CD1 TYR A 117      23.396  -8.239 -11.959  1.00  7.10           C  
ANISOU  882  CD1 TYR A 117     1159   1093    443    106    -71     19       C  
ATOM    883  CD2 TYR A 117      22.724  -6.488 -10.469  1.00  7.63           C  
ANISOU  883  CD2 TYR A 117      877   1175    847    136    182   -135       C  
ATOM    884  CE1 TYR A 117      23.672  -7.289 -12.934  1.00  5.90           C  
ANISOU  884  CE1 TYR A 117      976    963    299    166     72   -144       C  
ATOM    885  CE2 TYR A 117      22.997  -5.544 -11.451  1.00  7.29           C  
ANISOU  885  CE2 TYR A 117     1150   1014    604    158    124   -165       C  
ATOM    886  CZ  TYR A 117      23.462  -5.944 -12.663  1.00  7.10           C  
ANISOU  886  CZ  TYR A 117      979   1013    704    -43     59    -10       C  
ATOM    887  OH  TYR A 117      23.740  -4.989 -13.615  1.00  7.27           O  
ANISOU  887  OH  TYR A 117     1025   1009    727     87     64    122       O  
ATOM    888  N   ILE A 118      24.699  -8.049  -7.613  1.00  5.98           N  
ANISOU  888  N   ILE A 118      737    930    602    195    -34     -6       N  
ATOM    889  CA  ILE A 118      25.727  -7.102  -7.318  1.00  7.50           C  
ANISOU  889  CA  ILE A 118     1037   1069    742     90     23   -108       C  
ATOM    890  C   ILE A 118      26.981  -7.727  -6.707  1.00  7.06           C  
ANISOU  890  C   ILE A 118      987   1017    677     73     38    -77       C  
ATOM    891  O   ILE A 118      28.077  -7.140  -6.822  1.00  7.45           O  
ANISOU  891  O   ILE A 118     1000   1252    576    264     84    -89       O  
ATOM    892  CB  ILE A 118      25.172  -5.917  -6.492  1.00  7.77           C  
ANISOU  892  CB  ILE A 118     1110   1025    815     97     65   -115       C  
ATOM    893  CG1 ILE A 118      25.899  -4.612  -6.828  1.00  8.80           C  
ANISOU  893  CG1 ILE A 118     1222   1203    916    107     -1   -175       C  
ATOM    894  CG2 ILE A 118      25.122  -6.231  -4.990  1.00  8.62           C  
ANISOU  894  CG2 ILE A 118     1335   1103    835    153     -9    -80       C  
ATOM    895  CD1 ILE A 118      25.469  -4.025  -8.189  1.00  9.80           C  
ANISOU  895  CD1 ILE A 118     1667   1111    943    -20     -1    -61       C  
ATOM    896  N   LYS A 119      26.825  -8.887  -6.057  1.00  6.55           N  
ANISOU  896  N   LYS A 119      978    942    566    205      2   -214       N  
ATOM    897  CA  LYS A 119      27.931  -9.567  -5.366  1.00  7.88           C  
ANISOU  897  CA  LYS A 119     1076   1143    772    199     -3    -86       C  
ATOM    898  C   LYS A 119      28.749 -10.465  -6.303  1.00  8.23           C  
ANISOU  898  C   LYS A 119     1096   1196    833    206    -43     11       C  
ATOM    899  O   LYS A 119      29.727 -11.022  -5.880  1.00  9.39           O  
ANISOU  899  O   LYS A 119     1238   1557    771    542   -108   -137       O  
ATOM    900  CB  LYS A 119      27.339 -10.432  -4.220  1.00  7.87           C  
ANISOU  900  CB  LYS A 119     1078   1097    813    288    -74    -46       C  
ATOM    901  CG  LYS A 119      26.789  -9.585  -3.081  1.00 11.13           C  
ANISOU  901  CG  LYS A 119     1574   1601   1052    135    -65   -225       C  
ATOM    902  CD  LYS A 119      25.991 -10.407  -2.018  1.00 13.96           C  
ANISOU  902  CD  LYS A 119     1694   2062   1547    -66     14    -49       C  
ATOM    903  CE  LYS A 119      26.826 -11.476  -1.352  1.00 18.09           C  
ANISOU  903  CE  LYS A 119     2320   2211   2340    -74     62    207       C  
ATOM    904  NZ  LYS A 119      28.006 -10.907  -0.545  1.00 21.38           N1+
ANISOU  904  NZ  LYS A 119     2688   2941   2493    -75     27     59       N1+
ATOM    905  N   ASN A 120      28.274 -10.685  -7.530  1.00  6.29           N  
ANISOU  905  N   ASN A 120      889    958    541    152      1    -47       N  
ATOM    906  CA  ASN A 120      28.996 -11.492  -8.502  1.00  7.28           C  
ANISOU  906  CA  ASN A 120     1021   1020    723    136     -4    -33       C  
ATOM    907  C   ASN A 120      30.107 -10.730  -9.156  1.00  6.61           C  
ANISOU  907  C   ASN A 120     1050    906    556     81   -100    -81       C  
ATOM    908  O   ASN A 120      29.947  -9.538  -9.458  1.00  6.27           O  
ANISOU  908  O   ASN A 120     1003    929    447     58     21    -56       O  
ATOM    909  CB  ASN A 120      28.018 -11.983  -9.578  1.00  6.52           C  
ANISOU  909  CB  ASN A 120      979    885    610     21     52     20       C  
ATOM    910  CG  ASN A 120      28.742 -12.478 -10.811  1.00  6.58           C  
ANISOU  910  CG  ASN A 120     1114    870    514    -72     59   -216       C  
ATOM    911  ND2 ASN A 120      28.674 -11.685 -11.872  1.00  5.63           N  
ANISOU  911  ND2 ASN A 120      758    986    393     84   -119     39       N  
ATOM    912  OD1 ASN A 120      29.402 -13.533 -10.812  1.00  6.01           O  
ANISOU  912  OD1 ASN A 120     1046    766    472     53     70    -41       O  
ATOM    913  N   SER A 121      31.202 -11.421  -9.476  1.00  6.67           N  
ANISOU  913  N   SER A 121     1053    758    723    120    -35   -115       N  
ATOM    914  CA  SER A 121      32.333 -10.832 -10.143  1.00  6.84           C  
ANISOU  914  CA  SER A 121     1043    896    657     37   -119    -80       C  
ATOM    915  C   SER A 121      32.581 -11.383 -11.575  1.00  6.75           C  
ANISOU  915  C   SER A 121     1052    771    740    182    -88    -58       C  
ATOM    916  O   SER A 121      33.395 -10.824 -12.309  1.00  7.90           O  
ANISOU  916  O   SER A 121     1291   1034    678     39    129   -286       O  
ATOM    917  CB  SER A 121      33.609 -11.015  -9.329  1.00 10.07           C  
ANISOU  917  CB  SER A 121     1287   1340   1199      5   -165   -206       C  
ATOM    918  OG  SER A 121      33.933 -12.352  -9.198  1.00 11.93           O  
ANISOU  918  OG  SER A 121     1585   1888   1058    192   -183     97       O  
ATOM    919  N   ASN A 122      31.927 -12.467 -11.972  1.00  5.84           N  
ANISOU  919  N   ASN A 122      907    763    550    -51   -127     81       N  
ATOM    920  CA  ASN A 122      32.230 -13.049 -13.262  1.00  6.38           C  
ANISOU  920  CA  ASN A 122      958    770    696    -14    -30      9       C  
ATOM    921  C   ASN A 122      31.432 -12.310 -14.362  1.00  6.50           C  
ANISOU  921  C   ASN A 122     1038    808    622     46    -22     43       C  
ATOM    922  O   ASN A 122      30.196 -12.142 -14.269  1.00  5.89           O  
ANISOU  922  O   ASN A 122     1078    768    389     77    117    -41       O  
ATOM    923  CB  ASN A 122      31.847 -14.521 -13.280  1.00  5.68           C  
ANISOU  923  CB  ASN A 122      945    826    387     28     42    137       C  
ATOM    924  CG  ASN A 122      32.184 -15.163 -14.614  1.00  6.45           C  
ANISOU  924  CG  ASN A 122     1106    774    569     62    -50    -44       C  
ATOM    925  ND2 ASN A 122      33.474 -15.452 -14.827  1.00  7.00           N  
ANISOU  925  ND2 ASN A 122     1023    734    901    140    142    122       N  
ATOM    926  OD1 ASN A 122      31.319 -15.405 -15.438  1.00  5.73           O  
ANISOU  926  OD1 ASN A 122     1126    529    522     78     10     28       O  
ATOM    927  N   PRO A 123      32.100 -11.858 -15.414  1.00  6.02           N  
ANISOU  927  N   PRO A 123      741    717    827    291     19    180       N  
ATOM    928  CA  PRO A 123      31.403 -11.064 -16.433  1.00  7.48           C  
ANISOU  928  CA  PRO A 123     1121    950    770    198     75    160       C  
ATOM    929  C   PRO A 123      30.250 -11.748 -17.127  1.00  7.37           C  
ANISOU  929  C   PRO A 123     1188   1044    567    208     87    134       C  
ATOM    930  O   PRO A 123      29.153 -11.170 -17.229  1.00  8.28           O  
ANISOU  930  O   PRO A 123     1183   1272    691    258    110    100       O  
ATOM    931  CB  PRO A 123      32.538 -10.650 -17.403  1.00  8.79           C  
ANISOU  931  CB  PRO A 123     1356   1061    921    210     84    145       C  
ATOM    932  CG  PRO A 123      33.789 -10.676 -16.546  1.00  8.24           C  
ANISOU  932  CG  PRO A 123     1408    944    776    112    180    171       C  
ATOM    933  CD  PRO A 123      33.566 -11.834 -15.623  1.00  7.07           C  
ANISOU  933  CD  PRO A 123     1075    840    770    190    231    227       C  
ATOM    934  N   ALA A 124      30.418 -13.001 -17.566  1.00  7.25           N  
ANISOU  934  N   ALA A 124     1111    978    663    162     68    118       N  
ATOM    935  CA  ALA A 124      29.346 -13.705 -18.200  1.00  7.92           C  
ANISOU  935  CA  ALA A 124     1218   1046    742    185    -55    -97       C  
ATOM    936  C   ALA A 124      28.184 -14.016 -17.254  1.00  7.33           C  
ANISOU  936  C   ALA A 124     1121    970    691     18   -136   -152       C  
ATOM    937  O   ALA A 124      27.006 -13.793 -17.598  1.00  8.93           O  
ANISOU  937  O   ALA A 124     1266   1493    632    212   -215   -213       O  
ATOM    938  CB  ALA A 124      29.818 -14.981 -18.851  1.00  8.37           C  
ANISOU  938  CB  ALA A 124     1313   1150    714    197    -66    -41       C  
ATOM    939  N   LEU A 125      28.496 -14.419 -16.021  1.00  6.70           N  
ANISOU  939  N   LEU A 125      924    999    622     80     -6    -33       N  
ATOM    940  CA  LEU A 125      27.427 -14.747 -15.085  1.00  6.70           C  
ANISOU  940  CA  LEU A 125      993    796    754     40     69   -130       C  
ATOM    941  C   LEU A 125      26.603 -13.510 -14.740  1.00  6.51           C  
ANISOU  941  C   LEU A 125      874    922    677     74     36     -2       C  
ATOM    942  O   LEU A 125      25.381 -13.603 -14.461  1.00  6.39           O  
ANISOU  942  O   LEU A 125      784    883    758     71     25      3       O  
ATOM    943  CB  LEU A 125      28.009 -15.359 -13.815  1.00  6.98           C  
ANISOU  943  CB  LEU A 125      991    878    780    126      0   -176       C  
ATOM    944  CG  LEU A 125      27.014 -15.857 -12.762  1.00  7.91           C  
ANISOU  944  CG  LEU A 125     1157    934    912     97     -8    -63       C  
ATOM    945  CD1 LEU A 125      26.177 -16.989 -13.379  1.00 10.13           C  
ANISOU  945  CD1 LEU A 125     1220   1478   1150   -186   -126    221       C  
ATOM    946  CD2 LEU A 125      27.805 -16.360 -11.543  1.00  9.24           C  
ANISOU  946  CD2 LEU A 125     1435   1156    918   -170     41     71       C  
ATOM    947  N   ASN A 126      27.246 -12.348 -14.751  1.00  6.66           N  
ANISOU  947  N   ASN A 126      815    959    755     77    107   -122       N  
ATOM    948  CA  ASN A 126      26.549 -11.069 -14.543  1.00  6.59           C  
ANISOU  948  CA  ASN A 126      903    977    622     65     98    -66       C  
ATOM    949  C   ASN A 126      25.313 -10.994 -15.398  1.00  6.02           C  
ANISOU  949  C   ASN A 126      924    806    555     21     61    -45       C  
ATOM    950  O   ASN A 126      24.274 -10.462 -14.963  1.00  6.16           O  
ANISOU  950  O   ASN A 126      842    944    553    179     55     34       O  
ATOM    951  CB  ASN A 126      27.479  -9.910 -14.914  1.00  6.61           C  
ANISOU  951  CB  ASN A 126     1037    933    541     65     14     32       C  
ATOM    952  CG  ASN A 126      26.771  -8.576 -14.990  1.00  6.14           C  
ANISOU  952  CG  ASN A 126      972    825    535    -38    108   -111       C  
ATOM    953  ND2 ASN A 126      26.655  -7.927 -13.904  1.00  4.08           N  
ANISOU  953  ND2 ASN A 126      701    512    336     24    -40     94       N  
ATOM    954  OD1 ASN A 126      26.352  -8.126 -16.114  1.00  9.62           O  
ANISOU  954  OD1 ASN A 126     1489   1339    824     -9    -31    154       O  
ATOM    955  N   ASP A 127      25.427 -11.421 -16.651  1.00  5.84           N  
ANISOU  955  N   ASP A 127      748    860    609     81     64    -49       N  
ATOM    956  CA  ASP A 127      24.340 -11.315 -17.594  1.00  6.85           C  
ANISOU  956  CA  ASP A 127      931    977    693     78     -1    -59       C  
ATOM    957  C   ASP A 127      23.162 -12.244 -17.257  1.00  7.14           C  
ANISOU  957  C   ASP A 127      926   1052    734     15     -2    -25       C  
ATOM    958  O   ASP A 127      22.011 -11.817 -17.412  1.00  8.37           O  
ANISOU  958  O   ASP A 127     1045   1213    921    166   -181     -9       O  
ATOM    959  CB  ASP A 127      24.829 -11.551 -19.020  1.00  6.58           C  
ANISOU  959  CB  ASP A 127      964   1054    479     94   -143      4       C  
ATOM    960  CG  ASP A 127      25.875 -10.563 -19.478  1.00  8.24           C  
ANISOU  960  CG  ASP A 127     1461   1202    466    -14    -51     93       C  
ATOM    961  OD1 ASP A 127      26.158  -9.549 -18.808  1.00  8.16           O  
ANISOU  961  OD1 ASP A 127     1185   1370    544    109    -76    -38       O  
ATOM    962  OD2 ASP A 127      26.490 -10.778 -20.549  1.00 11.26           O1-
ANISOU  962  OD2 ASP A 127     1929   1487    860   -205    159    -40       O1-
ATOM    963  N   ASN A 128      23.408 -13.441 -16.746  1.00  7.11           N  
ANISOU  963  N   ASN A 128      887   1051    762     41    -79    -85       N  
ATOM    964  CA  ASN A 128      22.329 -14.276 -16.264  1.00  8.22           C  
ANISOU  964  CA  ASN A 128      992   1149    981     24    -97    -51       C  
ATOM    965  C   ASN A 128      21.631 -13.608 -15.049  1.00  7.19           C  
ANISOU  965  C   ASN A 128      905   1072    755    122    -72     53       C  
ATOM    966  O   ASN A 128      20.407 -13.645 -14.891  1.00  7.70           O  
ANISOU  966  O   ASN A 128      964   1119    841    150     45    -89       O  
ATOM    967  CB  ASN A 128      22.853 -15.674 -15.800  1.00  9.59           C  
ANISOU  967  CB  ASN A 128     1178   1331   1132    131    -30     -3       C  
ATOM    968  CG  ASN A 128      23.260 -16.579 -16.937  1.00 10.19           C  
ANISOU  968  CG  ASN A 128     1153   1687   1033     67   -173    -15       C  
ATOM    969  ND2 ASN A 128      24.461 -17.091 -16.869  1.00  9.49           N  
ANISOU  969  ND2 ASN A 128     1398   1098   1110    182     22   -118       N  
ATOM    970  OD1 ASN A 128      22.437 -16.922 -17.823  1.00 16.79           O  
ANISOU  970  OD1 ASN A 128     2196   2523   1658     85   -840   -180       O  
ATOM    971  N   LEU A 129      22.422 -13.085 -14.132  1.00  6.17           N  
ANISOU  971  N   LEU A 129      774    918    651     53     99    -92       N  
ATOM    972  CA  LEU A 129      21.910 -12.466 -12.924  1.00  6.90           C  
ANISOU  972  CA  LEU A 129      935   1000    687    192     10     -4       C  
ATOM    973  C   LEU A 129      21.126 -11.189 -13.290  1.00  7.07           C  
ANISOU  973  C   LEU A 129      937   1074    673    175     -6     33       C  
ATOM    974  O   LEU A 129      20.095 -10.879 -12.639  1.00  7.51           O  
ANISOU  974  O   LEU A 129      875   1191    786    176     33     10       O  
ATOM    975  CB  LEU A 129      23.019 -12.193 -11.932  1.00  7.21           C  
ANISOU  975  CB  LEU A 129     1137    909    693    132     11    -15       C  
ATOM    976  CG  LEU A 129      23.652 -13.481 -11.368  1.00  8.01           C  
ANISOU  976  CG  LEU A 129     1073    995    977     48     43     26       C  
ATOM    977  CD1 LEU A 129      24.947 -13.209 -10.750  1.00  8.27           C  
ANISOU  977  CD1 LEU A 129     1132   1009   1000    160    -44    -30       C  
ATOM    978  CD2 LEU A 129      22.698 -14.177 -10.369  1.00  9.94           C  
ANISOU  978  CD2 LEU A 129     1262   1168   1344     -3    -72     99       C  
ATOM    979  N   GLU A 130      21.594 -10.438 -14.298  1.00  6.67           N  
ANISOU  979  N   GLU A 130      942    902    689    128     80     -3       N  
ATOM    980  CA  GLU A 130      20.863  -9.256 -14.760  1.00  7.28           C  
ANISOU  980  CA  GLU A 130      963   1084    716     62    -68    -43       C  
ATOM    981  C   GLU A 130      19.471  -9.631 -15.241  1.00  7.57           C  
ANISOU  981  C   GLU A 130      921   1242    714     86     23    -28       C  
ATOM    982  O   GLU A 130      18.463  -8.986 -14.921  1.00  7.65           O  
ANISOU  982  O   GLU A 130      930   1274    700    239     -1     49       O  
ATOM    983  CB  GLU A 130      21.634  -8.517 -15.855  1.00  7.40           C  
ANISOU  983  CB  GLU A 130      932   1181    696     38    -32     12       C  
ATOM    984  CG  GLU A 130      20.975  -7.195 -16.314  1.00  9.03           C  
ANISOU  984  CG  GLU A 130     1277   1167    985     38   -234     96       C  
ATOM    985  CD  GLU A 130      21.619  -6.488 -17.469  1.00 12.40           C  
ANISOU  985  CD  GLU A 130     1523   2184   1001    431    -41    170       C  
ATOM    986  OE1 GLU A 130      22.794  -6.559 -17.673  1.00 14.57           O  
ANISOU  986  OE1 GLU A 130     1813   2814    909   -133    -51    -93       O  
ATOM    987  OE2 GLU A 130      20.881  -5.752 -18.177  1.00 18.22           O1-
ANISOU  987  OE2 GLU A 130     2324   2516   2081    500   -268    359       O1-
ATOM    988  N   LYS A 131      19.399 -10.716 -15.981  1.00  7.66           N  
ANISOU  988  N   LYS A 131      903   1328    676    226    -30    -92       N  
ATOM    989  CA  LYS A 131      18.104 -11.199 -16.462  1.00  8.68           C  
ANISOU  989  CA  LYS A 131     1071   1219   1007     51   -115    -89       C  
ATOM    990  C   LYS A 131      17.180 -11.616 -15.313  1.00  8.66           C  
ANISOU  990  C   LYS A 131      999   1200   1089    121    -29   -140       C  
ATOM    991  O   LYS A 131      15.976 -11.309 -15.331  1.00  9.31           O  
ANISOU  991  O   LYS A 131      989   1293   1254    214      0   -315       O  
ATOM    992  CB  LYS A 131      18.282 -12.391 -17.383  1.00  9.36           C  
ANISOU  992  CB  LYS A 131      851   1485   1219     66   -209   -100       C  
ATOM    993  CG  LYS A 131      18.914 -12.020 -18.673  1.00 14.01           C  
ANISOU  993  CG  LYS A 131     1674   2027   1621    -23    -95    -35       C  
ATOM    994  CD  LYS A 131      18.999 -13.235 -19.610  1.00 19.61           C  
ANISOU  994  CD  LYS A 131     2617   2494   2339     44    -18   -199       C  
ATOM    995  CE  LYS A 131      19.668 -12.920 -20.914  1.00 24.06           C  
ANISOU  995  CE  LYS A 131     2972   3211   2958    -93     38    125       C  
ATOM    996  NZ  LYS A 131      19.561 -14.145 -21.734  1.00 29.75           N1+
ANISOU  996  NZ  LYS A 131     3984   3678   3642     75    104   -129       N1+
ATOM    997  N   GLY A 132      17.707 -12.257 -14.277  1.00  8.97           N  
ANISOU  997  N   GLY A 132     1148   1206   1051     41     87   -136       N  
ATOM    998  CA  GLY A 132      16.901 -12.622 -13.149  1.00  9.27           C  
ANISOU  998  CA  GLY A 132     1115   1126   1279    106     92    -46       C  
ATOM    999  C   GLY A 132      16.332 -11.375 -12.462  1.00  8.44           C  
ANISOU  999  C   GLY A 132      992   1041   1171    114    107    -44       C  
ATOM   1000  O   GLY A 132      15.165 -11.359 -12.052  1.00  9.77           O  
ANISOU 1000  O   GLY A 132      953   1268   1488     91    215    -76       O  
ATOM   1001  N   LEU A 133      17.124 -10.341 -12.327  1.00  7.92           N  
ANISOU 1001  N   LEU A 133      881   1034   1092    195     65    -71       N  
ATOM   1002  CA  LEU A 133      16.701  -9.092 -11.699  1.00  7.77           C  
ANISOU 1002  CA  LEU A 133     1051   1025    874    127    -59    -17       C  
ATOM   1003  C   LEU A 133      15.652  -8.381 -12.546  1.00  7.15           C  
ANISOU 1003  C   LEU A 133      896    974    844    108      6    -31       C  
ATOM   1004  O   LEU A 133      14.615  -7.928 -12.038  1.00  6.99           O  
ANISOU 1004  O   LEU A 133      798   1053    803    100     28   -207       O  
ATOM   1005  CB  LEU A 133      17.890  -8.203 -11.448  1.00  7.49           C  
ANISOU 1005  CB  LEU A 133      907   1077    862    251   -168    -39       C  
ATOM   1006  CG  LEU A 133      17.655  -6.778 -10.926  1.00  7.57           C  
ANISOU 1006  CG  LEU A 133     1001   1109    764    108   -118    -22       C  
ATOM   1007  CD1 LEU A 133      16.891  -6.820  -9.585  1.00  9.01           C  
ANISOU 1007  CD1 LEU A 133     1522   1029    870     10    -54   -112       C  
ATOM   1008  CD2 LEU A 133      18.956  -6.049 -10.776  1.00  8.75           C  
ANISOU 1008  CD2 LEU A 133     1055   1344    924     35   -196     17       C  
ATOM   1009  N   LEU A 134      15.891  -8.312 -13.844  1.00  7.09           N  
ANISOU 1009  N   LEU A 134      901    962    828     82    -64    -45       N  
ATOM   1010  CA  LEU A 134      14.936  -7.716 -14.778  1.00  7.28           C  
ANISOU 1010  CA  LEU A 134     1020    948    798    146      1    -64       C  
ATOM   1011  C   LEU A 134      13.586  -8.439 -14.744  1.00  7.27           C  
ANISOU 1011  C   LEU A 134      983    968    811    103     65    -19       C  
ATOM   1012  O   LEU A 134      12.524  -7.793 -14.712  1.00  7.84           O  
ANISOU 1012  O   LEU A 134      943   1040    993    235   -129   -224       O  
ATOM   1013  CB  LEU A 134      15.481  -7.716 -16.201  1.00  8.21           C  
ANISOU 1013  CB  LEU A 134     1109   1236    773    124    -70     30       C  
ATOM   1014  CG  LEU A 134      16.524  -6.664 -16.520  1.00  8.69           C  
ANISOU 1014  CG  LEU A 134      931   1230   1138    145    -67    -42       C  
ATOM   1015  CD1 LEU A 134      17.268  -6.955 -17.829  1.00 10.18           C  
ANISOU 1015  CD1 LEU A 134     1212   1473   1181    255     78    159       C  
ATOM   1016  CD2 LEU A 134      15.930  -5.271 -16.574  1.00 10.21           C  
ANISOU 1016  CD2 LEU A 134     1236   1313   1331     27   -193    205       C  
ATOM   1017  N   LYS A 135      13.581  -9.779 -14.678  1.00  7.49           N  
ANISOU 1017  N   LYS A 135      874   1011    959    187     55   -137       N  
ATOM   1018  CA  LYS A 135      12.325 -10.526 -14.641  1.00  8.13           C  
ANISOU 1018  CA  LYS A 135      926   1174    988     66    -41    -53       C  
ATOM   1019  C   LYS A 135      11.544 -10.181 -13.378  1.00  8.16           C  
ANISOU 1019  C   LYS A 135      918   1191    990    131    -70    -71       C  
ATOM   1020  O   LYS A 135      10.315 -10.013 -13.418  1.00  7.73           O  
ANISOU 1020  O   LYS A 135      805    946   1186     40    -63    -41       O  
ATOM   1021  CB  LYS A 135      12.587 -12.015 -14.735  1.00 10.30           C  
ANISOU 1021  CB  LYS A 135     1231   1340   1341     90    -40     67       C  
ATOM   1022  CG ALYS A 135      13.192 -12.576 -16.016  0.50 15.22           C  
ANISOU 1022  CG ALYS A 135     2000   2024   1756    -28     62    -97       C  
ATOM   1023  CG BLYS A 135      11.310 -12.877 -14.804  0.50 13.44           C  
ANISOU 1023  CG BLYS A 135     1772   1596   1736    -58     22     16       C  
ATOM   1024  CD ALYS A 135      13.275 -14.033 -16.137  0.50 19.33           C  
ANISOU 1024  CD ALYS A 135     2562   2249   2534     91     -3     -9       C  
ATOM   1025  CD BLYS A 135      11.619 -14.378 -14.881  0.50 19.44           C  
ANISOU 1025  CD BLYS A 135     2694   2158   2535    145     19    -51       C  
ATOM   1026  CE ALYS A 135      14.064 -14.394 -17.346  0.50 23.86           C  
ANISOU 1026  CE ALYS A 135     3077   3149   2837     62     62    -20       C  
ATOM   1027  CE BLYS A 135      10.357 -15.164 -14.798  0.50 24.05           C  
ANISOU 1027  CE BLYS A 135     3024   3027   3085    -30     -2    -10       C  
ATOM   1028  NZ ALYS A 135      14.020 -15.872 -17.575  0.50 28.10           N1+
ANISOU 1028  NZ ALYS A 135     3794   3343   3540    -18     26     -6       N1+
ATOM   1029  NZ BLYS A 135      10.634 -16.616 -14.847  0.50 26.91           N1+
ANISOU 1029  NZ BLYS A 135     3716   3100   3405     24     38    -39       N1+
ATOM   1030  N   ALA A 136      12.238 -10.085 -12.245  1.00  7.83           N  
ANISOU 1030  N   ALA A 136      997   1029    949     82    -68   -219       N  
ATOM   1031  CA  ALA A 136      11.576  -9.776 -10.985  1.00  7.62           C  
ANISOU 1031  CA  ALA A 136      963    965    965     96     14      3       C  
ATOM   1032  C   ALA A 136      10.993  -8.333 -11.026  1.00  7.83           C  
ANISOU 1032  C   ALA A 136      942   1071    961     61    -41    -60       C  
ATOM   1033  O   ALA A 136       9.885  -8.080 -10.530  1.00  8.10           O  
ANISOU 1033  O   ALA A 136      868   1214    994    103    -47   -123       O  
ATOM   1034  CB  ALA A 136      12.512 -10.006  -9.858  1.00  9.83           C  
ANISOU 1034  CB  ALA A 136     1200   1248   1285     15    -60    -88       C  
ATOM   1035  N   LEU A 137      11.731  -7.382 -11.594  1.00  6.75           N  
ANISOU 1035  N   LEU A 137      820    884    859    187     46   -104       N  
ATOM   1036  CA  LEU A 137      11.241  -6.032 -11.742  1.00  7.20           C  
ANISOU 1036  CA  LEU A 137      864    943    929    113    -15    -28       C  
ATOM   1037  C   LEU A 137      10.003  -5.997 -12.670  1.00  7.28           C  
ANISOU 1037  C   LEU A 137      991    956    816     42    -12   -105       C  
ATOM   1038  O   LEU A 137       9.077  -5.260 -12.410  1.00  7.11           O  
ANISOU 1038  O   LEU A 137      763   1089    847     94    -56    -53       O  
ATOM   1039  CB  LEU A 137      12.353  -5.153 -12.317  1.00  7.51           C  
ANISOU 1039  CB  LEU A 137     1032    935    885    135    -68    -12       C  
ATOM   1040  CG  LEU A 137      13.429  -4.736 -11.287  1.00  8.86           C  
ANISOU 1040  CG  LEU A 137     1056   1158   1152     67    -87    -64       C  
ATOM   1041  CD1 LEU A 137      14.709  -4.273 -12.016  1.00  9.15           C  
ANISOU 1041  CD1 LEU A 137      903   1245   1326    201    -94   -137       C  
ATOM   1042  CD2 LEU A 137      12.915  -3.631 -10.312  1.00  9.52           C  
ANISOU 1042  CD2 LEU A 137     1290   1149   1176   -184    -48   -187       C  
ATOM   1043  N   LYS A 138      10.012  -6.805 -13.723  1.00  7.00           N  
ANISOU 1043  N   LYS A 138      865    989    805    134    -72   -189       N  
ATOM   1044  CA  LYS A 138       8.869  -6.866 -14.643  1.00  7.32           C  
ANISOU 1044  CA  LYS A 138      937   1014    827     72    -14   -174       C  
ATOM   1045  C   LYS A 138       7.623  -7.440 -13.963  1.00  6.80           C  
ANISOU 1045  C   LYS A 138      976    936    669     78     -2   -198       C  
ATOM   1046  O   LYS A 138       6.514  -6.987 -14.211  1.00  7.57           O  
ANISOU 1046  O   LYS A 138     1046    947    880     69   -213   -216       O  
ATOM   1047  CB  LYS A 138       9.262  -7.680 -15.886  1.00  7.63           C  
ANISOU 1047  CB  LYS A 138      878   1170    849    -52     40   -167       C  
ATOM   1048  CG  LYS A 138       8.125  -7.824 -16.913  1.00  9.22           C  
ANISOU 1048  CG  LYS A 138      967   1638    897   -101     19   -259       C  
ATOM   1049  CD  LYS A 138       7.745  -6.444 -17.513  1.00 14.60           C  
ANISOU 1049  CD  LYS A 138     1684   2035   1826    182     17    -93       C  
ATOM   1050  CE  LYS A 138       6.686  -6.423 -18.547  1.00 18.66           C  
ANISOU 1050  CE  LYS A 138     2288   2465   2334     11    -73    -15       C  
ATOM   1051  NZ  LYS A 138       6.250  -4.920 -18.667  1.00 18.80           N1+
ANISOU 1051  NZ  LYS A 138     2297   2550   2294    270     24    -57       N1+
ATOM   1052  N   VAL A 139       7.767  -8.453 -13.116  1.00  7.02           N  
ANISOU 1052  N   VAL A 139      803   1008    856     39    -55    -95       N  
ATOM   1053  CA  VAL A 139       6.632  -9.009 -12.385  1.00  7.65           C  
ANISOU 1053  CA  VAL A 139     1056   1052    798     -9    -86    -48       C  
ATOM   1054  C   VAL A 139       6.027  -7.909 -11.478  1.00  7.76           C  
ANISOU 1054  C   VAL A 139     1062   1034    850    139    -79    -62       C  
ATOM   1055  O   VAL A 139       4.794  -7.731 -11.399  1.00  7.29           O  
ANISOU 1055  O   VAL A 139      889   1102    779    242   -180   -136       O  
ATOM   1056  CB  VAL A 139       7.009 -10.276 -11.605  1.00  8.10           C  
ANISOU 1056  CB  VAL A 139     1101    936   1041    -41     -6    -75       C  
ATOM   1057  CG1 VAL A 139       5.902 -10.739 -10.692  1.00  8.78           C  
ANISOU 1057  CG1 VAL A 139     1192   1042   1101    136    -30    -83       C  
ATOM   1058  CG2 VAL A 139       7.321 -11.360 -12.592  1.00  8.71           C  
ANISOU 1058  CG2 VAL A 139     1160    833   1316    -61    -41    -76       C  
ATOM   1059  N   LEU A 140       6.868  -7.116 -10.828  1.00  6.82           N  
ANISOU 1059  N   LEU A 140      848    990    752    118    -44    -79       N  
ATOM   1060  CA  LEU A 140       6.363  -5.985 -10.039  1.00  6.48           C  
ANISOU 1060  CA  LEU A 140      862    965    633     40    -55      9       C  
ATOM   1061  C   LEU A 140       5.665  -4.972 -10.979  1.00  6.79           C  
ANISOU 1061  C   LEU A 140      882    982    714     61   -119    -37       C  
ATOM   1062  O   LEU A 140       4.612  -4.453 -10.649  1.00  6.22           O  
ANISOU 1062  O   LEU A 140      874    912    575     90    -65   -193       O  
ATOM   1063  CB  LEU A 140       7.517  -5.331  -9.278  1.00  7.15           C  
ANISOU 1063  CB  LEU A 140      930    999    785     91    -97    -21       C  
ATOM   1064  CG  LEU A 140       7.154  -4.005  -8.587  1.00  7.19           C  
ANISOU 1064  CG  LEU A 140     1075   1007    651    120    -65   -105       C  
ATOM   1065  CD1 LEU A 140       6.064  -4.227  -7.516  1.00  7.66           C  
ANISOU 1065  CD1 LEU A 140      866   1143    900    228    -37   -292       C  
ATOM   1066  CD2 LEU A 140       8.365  -3.338  -7.994  1.00  8.00           C  
ANISOU 1066  CD2 LEU A 140     1121   1042    876    118   -130    -76       C  
ATOM   1067  N   ASP A 141       6.279  -4.659 -12.120  1.00  5.83           N  
ANISOU 1067  N   ASP A 141      763    819    631    137   -149   -115       N  
ATOM   1068  CA  ASP A 141       5.682  -3.749 -13.076  1.00  5.98           C  
ANISOU 1068  CA  ASP A 141      818    748    704     43    -96    -62       C  
ATOM   1069  C   ASP A 141       4.254  -4.233 -13.466  1.00  6.24           C  
ANISOU 1069  C   ASP A 141      838    757    773     75    -91    -35       C  
ATOM   1070  O   ASP A 141       3.320  -3.404 -13.527  1.00  6.90           O  
ANISOU 1070  O   ASP A 141      953    870    796    122   -128     25       O  
ATOM   1071  CB  ASP A 141       6.552  -3.656 -14.336  1.00  6.73           C  
ANISOU 1071  CB  ASP A 141      944    912    701     78   -121   -191       C  
ATOM   1072  CG  ASP A 141       6.131  -2.584 -15.245  1.00  7.09           C  
ANISOU 1072  CG  ASP A 141      962    983    747    -34     58    -85       C  
ATOM   1073  OD1 ASP A 141       6.265  -1.410 -14.870  1.00  7.34           O  
ANISOU 1073  OD1 ASP A 141      968   1082    736     14   -102     94       O  
ATOM   1074  OD2 ASP A 141       5.599  -2.818 -16.370  1.00  8.81           O1-
ANISOU 1074  OD2 ASP A 141     1220   1444    683     27   -106      2       O1-
ATOM   1075  N   ASN A 142       4.096  -5.533 -13.691  1.00  6.17           N  
ANISOU 1075  N   ASN A 142      855    830    658     -3   -117    -56       N  
ATOM   1076  CA  ASN A 142       2.787  -6.086 -14.029  1.00  6.62           C  
ANISOU 1076  CA  ASN A 142      952    875    686      0    -74      0       C  
ATOM   1077  C   ASN A 142       1.786  -5.847 -12.910  1.00  6.43           C  
ANISOU 1077  C   ASN A 142      913    806    725     91    -25    113       C  
ATOM   1078  O   ASN A 142       0.626  -5.477 -13.143  1.00  7.44           O  
ANISOU 1078  O   ASN A 142      891   1202    734    142    -80     24       O  
ATOM   1079  CB  ASN A 142       2.883  -7.574 -14.317  1.00  7.45           C  
ANISOU 1079  CB  ASN A 142      887   1049    892     41    -23    102       C  
ATOM   1080  CG  ASN A 142       3.653  -7.878 -15.575  1.00  9.47           C  
ANISOU 1080  CG  ASN A 142     1287   1198   1112    -31    -41    -96       C  
ATOM   1081  ND2 ASN A 142       4.110  -9.114 -15.668  1.00 10.80           N  
ANISOU 1081  ND2 ASN A 142     1361   1269   1472    114    -97   -382       N  
ATOM   1082  OD1 ASN A 142       3.799  -7.039 -16.448  1.00 11.02           O  
ANISOU 1082  OD1 ASN A 142     1567   1636    984    -99    103   -483       O  
ATOM   1083  N   TYR A 143       2.205  -6.034 -11.655  1.00  6.45           N  
ANISOU 1083  N   TYR A 143      708   1051    691    140    -81     15       N  
ATOM   1084  CA  TYR A 143       1.297  -5.747 -10.540  1.00  6.17           C  
ANISOU 1084  CA  TYR A 143      868    881    592    113    -66     51       C  
ATOM   1085  C   TYR A 143       0.875  -4.297 -10.502  1.00  6.68           C  
ANISOU 1085  C   TYR A 143      901    964    671     97    -55    109       C  
ATOM   1086  O   TYR A 143      -0.294  -3.987 -10.247  1.00  7.25           O  
ANISOU 1086  O   TYR A 143      937   1074    742     43    -23     12       O  
ATOM   1087  CB  TYR A 143       1.911  -6.168  -9.185  1.00  7.46           C  
ANISOU 1087  CB  TYR A 143     1170   1011    653    165   -203     24       C  
ATOM   1088  CG  TYR A 143       0.941  -6.031  -8.014  1.00  7.99           C  
ANISOU 1088  CG  TYR A 143     1067   1152    814   -103    -66    -15       C  
ATOM   1089  CD1 TYR A 143      -0.123  -6.898  -7.884  1.00 11.70           C  
ANISOU 1089  CD1 TYR A 143     1865   1256   1324   -477     56   -235       C  
ATOM   1090  CD2 TYR A 143       1.027  -5.015  -7.091  1.00  7.59           C  
ANISOU 1090  CD2 TYR A 143     1106    990    785    -61   -138    -43       C  
ATOM   1091  CE1 TYR A 143      -1.013  -6.789  -6.884  1.00 11.40           C  
ANISOU 1091  CE1 TYR A 143     1863   1290   1176   -477      6   -243       C  
ATOM   1092  CE2 TYR A 143       0.110  -4.913  -6.052  1.00  9.48           C  
ANISOU 1092  CE2 TYR A 143     1152   1290   1158    -57   -146    -10       C  
ATOM   1093  CZ  TYR A 143      -0.923  -5.791  -5.966  1.00  9.90           C  
ANISOU 1093  CZ  TYR A 143     1620   1462    679   -157      3   -133       C  
ATOM   1094  OH  TYR A 143      -1.873  -5.706  -4.949  1.00 11.14           O  
ANISOU 1094  OH  TYR A 143     1335   2093    802   -341    -30    141       O  
ATOM   1095  N   LEU A 144       1.829  -3.398 -10.738  1.00  6.38           N  
ANISOU 1095  N   LEU A 144      885    795    743     70    -20    -21       N  
ATOM   1096  CA  LEU A 144       1.568  -1.959 -10.680  1.00  7.02           C  
ANISOU 1096  CA  LEU A 144      953    871    842     44    -22      9       C  
ATOM   1097  C   LEU A 144       0.718  -1.465 -11.847  1.00  6.99           C  
ANISOU 1097  C   LEU A 144      899    880    874    150    -68    -74       C  
ATOM   1098  O   LEU A 144       0.126  -0.403 -11.728  1.00 10.43           O  
ANISOU 1098  O   LEU A 144     1657   1006   1296    448   -493   -194       O  
ATOM   1099  CB  LEU A 144       2.918  -1.181 -10.619  1.00  6.10           C  
ANISOU 1099  CB  LEU A 144      824    744    748     19    -69    -20       C  
ATOM   1100  CG  LEU A 144       3.646  -1.354  -9.282  1.00  7.54           C  
ANISOU 1100  CG  LEU A 144     1081   1044    737     33     82    -77       C  
ATOM   1101  CD1 LEU A 144       5.134  -0.923  -9.429  1.00  7.73           C  
ANISOU 1101  CD1 LEU A 144     1148    934    851     70    -66   -124       C  
ATOM   1102  CD2 LEU A 144       2.946  -0.633  -8.159  1.00 10.39           C  
ANISOU 1102  CD2 LEU A 144     1443   1632    872     68    -21   -261       C  
ATOM   1103  N   THR A 145       0.682  -2.182 -12.954  1.00  5.61           N  
ANISOU 1103  N   THR A 145      759    724    648    130    -67    101       N  
ATOM   1104  CA  THR A 145      -0.132  -1.792 -14.095  1.00  6.98           C  
ANISOU 1104  CA  THR A 145     1020    859    773    135    -21    146       C  
ATOM   1105  C   THR A 145      -1.439  -2.587 -14.184  1.00  8.30           C  
ANISOU 1105  C   THR A 145      947   1225    978     90   -156    116       C  
ATOM   1106  O   THR A 145      -2.256  -2.378 -15.087  1.00 12.74           O  
ANISOU 1106  O   THR A 145     1343   2025   1472   -182   -399    478       O  
ATOM   1107  CB  THR A 145       0.632  -1.864 -15.420  1.00  8.15           C  
ANISOU 1107  CB  THR A 145     1038   1142    914    176    -61     62       C  
ATOM   1108  CG2 THR A 145       1.900  -1.044 -15.406  1.00  8.65           C  
ANISOU 1108  CG2 THR A 145     1365   1177    745     36     71    136       C  
ATOM   1109  OG1 THR A 145       1.008  -3.233 -15.698  1.00  8.58           O  
ANISOU 1109  OG1 THR A 145     1462    876    921    -48    -91     24       O  
ATOM   1110  N   SER A 146      -1.683  -3.511 -13.279  1.00  7.02           N  
ANISOU 1110  N   SER A 146      890   1025    751     40   -123     -7       N  
ATOM   1111  CA  SER A 146      -2.919  -4.295 -13.228  1.00  7.93           C  
ANISOU 1111  CA  SER A 146      994   1203    815      0   -144    -36       C  
ATOM   1112  C   SER A 146      -3.853  -3.574 -12.271  1.00  7.06           C  
ANISOU 1112  C   SER A 146      955   1008    719    -27    -69    -48       C  
ATOM   1113  O   SER A 146      -3.404  -2.941 -11.317  1.00 10.29           O  
ANISOU 1113  O   SER A 146     1142   1662   1106    -76     36   -542       O  
ATOM   1114  CB  SER A 146      -2.583  -5.704 -12.725  1.00  8.64           C  
ANISOU 1114  CB  SER A 146     1199   1140    943    -90    -62   -183       C  
ATOM   1115  OG ASER A 146      -2.541  -5.753 -11.286  0.50 12.94           O  
ANISOU 1115  OG ASER A 146     1522   1787   1606     -7    -55    285       O  
ATOM   1116  OG BSER A 146      -3.770  -6.520 -12.502  0.50 10.45           O  
ANISOU 1116  OG BSER A 146     1236   1159   1576     19   -146    191       O  
ATOM   1117  N   PRO A 147      -5.136  -3.596 -12.486  1.00  6.38           N  
ANISOU 1117  N   PRO A 147      972    852    598    -48   -111    -93       N  
ATOM   1118  CA  PRO A 147      -6.023  -2.799 -11.662  1.00  6.69           C  
ANISOU 1118  CA  PRO A 147      980    715    847    -87    -60    -50       C  
ATOM   1119  C   PRO A 147      -6.390  -3.314 -10.282  1.00  7.76           C  
ANISOU 1119  C   PRO A 147     1142    893    913   -108    -79     12       C  
ATOM   1120  O   PRO A 147      -6.459  -4.522 -10.073  1.00  7.66           O  
ANISOU 1120  O   PRO A 147     1472    903    535    -58   -132    -25       O  
ATOM   1121  CB  PRO A 147      -7.309  -2.758 -12.488  1.00  8.80           C  
ANISOU 1121  CB  PRO A 147     1165   1125   1052    -55   -108    104       C  
ATOM   1122  CG  PRO A 147      -7.267  -4.009 -13.245  1.00  7.62           C  
ANISOU 1122  CG  PRO A 147      928    962   1005   -155   -125    148       C  
ATOM   1123  CD  PRO A 147      -5.847  -4.242 -13.613  1.00  6.51           C  
ANISOU 1123  CD  PRO A 147     1036   1024    409   -195    -17     34       C  
ATOM   1124  N   LEU A 148      -6.650  -2.369  -9.371  1.00  8.19           N  
ANISOU 1124  N   LEU A 148     1287    882    942   -158     34    -53       N  
ATOM   1125  CA  LEU A 148      -7.211  -2.672  -8.042  1.00  8.36           C  
ANISOU 1125  CA  LEU A 148     1113   1032   1031    -90    -16    -77       C  
ATOM   1126  C   LEU A 148      -8.472  -1.853  -7.907  1.00  9.25           C  
ANISOU 1126  C   LEU A 148     1394   1017   1102      5     48   -126       C  
ATOM   1127  O   LEU A 148      -8.660  -0.940  -8.710  1.00  9.33           O  
ANISOU 1127  O   LEU A 148     1301   1176   1066    135   -111   -163       O  
ATOM   1128  CB  LEU A 148      -6.208  -2.377  -6.899  1.00  9.13           C  
ANISOU 1128  CB  LEU A 148     1248   1130   1089   -185     11    -93       C  
ATOM   1129  CG  LEU A 148      -5.023  -3.320  -6.798  1.00  9.92           C  
ANISOU 1129  CG  LEU A 148     1265   1254   1247   -146   -233    -94       C  
ATOM   1130  CD1 LEU A 148      -4.044  -2.787  -5.723  1.00 11.25           C  
ANISOU 1130  CD1 LEU A 148     1457   1702   1113   -239   -312    -60       C  
ATOM   1131  CD2 LEU A 148      -5.369  -4.765  -6.518  1.00 11.99           C  
ANISOU 1131  CD2 LEU A 148     1486   1583   1485   -147    -19    -10       C  
ATOM   1132  N   PRO A 149      -9.338  -2.125  -6.921  1.00  9.00           N  
ANISOU 1132  N   PRO A 149     1176   1005   1237    -88    -14     49       N  
ATOM   1133  CA  PRO A 149     -10.514  -1.267  -6.716  1.00 10.08           C  
ANISOU 1133  CA  PRO A 149     1462   1097   1270    -44      3    -62       C  
ATOM   1134  C   PRO A 149     -10.033   0.171  -6.586  1.00 10.77           C  
ANISOU 1134  C   PRO A 149     1387   1293   1409    -76    -22   -162       C  
ATOM   1135  O   PRO A 149      -9.097   0.471  -5.832  1.00 11.43           O  
ANISOU 1135  O   PRO A 149     1501   1472   1368    -20     31   -174       O  
ATOM   1136  CB  PRO A 149     -11.158  -1.858  -5.435  1.00  9.85           C  
ANISOU 1136  CB  PRO A 149     1423   1023   1296     21    -66    -32       C  
ATOM   1137  CG  PRO A 149     -10.684  -3.297  -5.408  1.00  9.71           C  
ANISOU 1137  CG  PRO A 149     1403   1081   1203    -39    111    -56       C  
ATOM   1138  CD  PRO A 149      -9.293  -3.209  -5.910  1.00  9.76           C  
ANISOU 1138  CD  PRO A 149     1376   1065   1267    -50     62     79       C  
ATOM   1139  N   GLU A 150     -10.727   1.053  -7.297  1.00 10.67           N  
ANISOU 1139  N   GLU A 150     1491   1154   1407   -248    -12    -91       N  
ATOM   1140  CA  GLU A 150     -10.393   2.482  -7.324  1.00 11.24           C  
ANISOU 1140  CA  GLU A 150     1541   1234   1496   -148     59    -28       C  
ATOM   1141  C   GLU A 150     -10.793   3.186  -6.045  1.00 11.68           C  
ANISOU 1141  C   GLU A 150     1471   1467   1498   -201     23   -117       C  
ATOM   1142  O   GLU A 150     -11.906   3.076  -5.603  1.00 10.69           O  
ANISOU 1142  O   GLU A 150     1425   1245   1390   -239     14   -247       O  
ATOM   1143  CB  GLU A 150     -11.104   3.152  -8.500  1.00 10.93           C  
ANISOU 1143  CB  GLU A 150     1762   1065   1324   -199    151    -54       C  
ATOM   1144  CG  GLU A 150     -10.741   4.604  -8.765  1.00  9.85           C  
ANISOU 1144  CG  GLU A 150     1544   1005   1193   -206    233    -28       C  
ATOM   1145  CD  GLU A 150     -11.568   5.113  -9.905  1.00 10.71           C  
ANISOU 1145  CD  GLU A 150     1553   1202   1313    -76    169   -211       C  
ATOM   1146  OE1 GLU A 150     -12.817   5.030  -9.826  1.00  9.95           O  
ANISOU 1146  OE1 GLU A 150     1508    847   1426   -403    107   -240       O  
ATOM   1147  OE2 GLU A 150     -10.982   5.607 -10.920  1.00 11.64           O1-
ANISOU 1147  OE2 GLU A 150     2228    976   1216   -723     68   -431       O1-
ATOM   1148  N   GLY A 151      -9.870   3.982  -5.504  1.00 11.71           N  
ANISOU 1148  N   GLY A 151     1424   1484   1541   -213     27   -238       N  
ATOM   1149  CA  GLY A 151     -10.049   4.814  -4.337  1.00 11.44           C  
ANISOU 1149  CA  GLY A 151     1345   1551   1451    -96     -1   -117       C  
ATOM   1150  C   GLY A 151     -11.124   5.839  -4.610  1.00 11.47           C  
ANISOU 1150  C   GLY A 151     1544   1226   1586   -225    -51    -73       C  
ATOM   1151  O   GLY A 151     -11.466   6.230  -5.739  1.00 10.33           O  
ANISOU 1151  O   GLY A 151     1583    815   1526   -536    -82   -238       O  
ATOM   1152  N   VAL A 152     -11.696   6.301  -3.529  1.00 12.52           N  
ANISOU 1152  N   VAL A 152     1684   1532   1539   -162    -50   -129       N  
ATOM   1153  CA  VAL A 152     -12.766   7.263  -3.627  1.00 14.28           C  
ANISOU 1153  CA  VAL A 152     1839   1768   1819    -47    -49    -66       C  
ATOM   1154  C   VAL A 152     -12.332   8.631  -4.121  1.00 14.61           C  
ANISOU 1154  C   VAL A 152     1936   1781   1835     -5     54   -108       C  
ATOM   1155  O   VAL A 152     -13.138   9.380  -4.636  1.00 16.15           O  
ANISOU 1155  O   VAL A 152     2196   1881   2059    -35    -48    -30       O  
ATOM   1156  CB  VAL A 152     -13.452   7.397  -2.261  1.00 15.28           C  
ANISOU 1156  CB  VAL A 152     1963   1947   1892   -136     24    -34       C  
ATOM   1157  CG1AVAL A 152     -14.106   6.087  -1.812  0.50 17.02           C  
ANISOU 1157  CG1AVAL A 152     2251   2119   2096   -100    -26      8       C  
ATOM   1158  CG2AVAL A 152     -12.712   8.230  -1.211  0.50 14.96           C  
ANISOU 1158  CG2AVAL A 152     2007   1863   1810     37    -25    -52       C  
ATOM   1159  CG1BVAL A 152     -14.372   8.583  -2.250  0.50 17.54           C  
ANISOU 1159  CG1BVAL A 152     2263   2199   2200     -7    -48     30       C  
ATOM   1160  CG2BVAL A 152     -14.150   6.116  -1.869  0.50 17.00           C  
ANISOU 1160  CG2BVAL A 152     2244   2127   2088   -110    -30      7       C  
ATOM   1161  N   ASP A 153     -11.049   8.919  -4.057  1.00 14.33           N  
ANISOU 1161  N   ASP A 153     2065   1689   1689   -121    -18   -109       N  
ATOM   1162  CA  ASP A 153     -10.489  10.193  -4.530  1.00 15.84           C  
ANISOU 1162  CA  ASP A 153     2171   1854   1993   -120     30    -77       C  
ATOM   1163  C   ASP A 153     -10.029  10.210  -5.996  1.00 16.82           C  
ANISOU 1163  C   ASP A 153     2343   2019   2029   -235     86    -99       C  
ATOM   1164  O   ASP A 153      -9.285  11.119  -6.423  1.00 17.78           O  
ANISOU 1164  O   ASP A 153     2720   2044   1989   -375    146    -81       O  
ATOM   1165  CB  ASP A 153      -9.327  10.562  -3.615  1.00 16.55           C  
ANISOU 1165  CB  ASP A 153     2264   1999   2024   -181    -46   -196       C  
ATOM   1166  CG  ASP A 153      -8.201   9.520  -3.601  1.00 19.73           C  
ANISOU 1166  CG  ASP A 153     2441   2332   2722   -115    -79    -37       C  
ATOM   1167  OD1 ASP A 153      -8.402   8.271  -3.784  1.00 18.09           O  
ANISOU 1167  OD1 ASP A 153     2124   2246   2502   -127     90   -318       O  
ATOM   1168  OD2 ASP A 153      -7.015   9.880  -3.376  1.00 24.56           O1-
ANISOU 1168  OD2 ASP A 153     2678   3046   3607   -226   -286    -15       O1-
ATOM   1169  N   GLU A 154     -10.447   9.209  -6.777  1.00 15.98           N  
ANISOU 1169  N   GLU A 154     2219   1917   1932   -228     71    -76       N  
ATOM   1170  CA  GLU A 154     -10.137   9.131  -8.209  1.00 15.57           C  
ANISOU 1170  CA  GLU A 154     2110   1896   1909   -137      7    -21       C  
ATOM   1171  C   GLU A 154     -11.404   8.579  -8.853  1.00 15.24           C  
ANISOU 1171  C   GLU A 154     2119   1911   1758   -182     22    -29       C  
ATOM   1172  O   GLU A 154     -11.997   7.627  -8.310  1.00 15.94           O  
ANISOU 1172  O   GLU A 154     2401   1904   1750   -334    -91    -63       O  
ATOM   1173  CB  GLU A 154      -8.929   8.199  -8.417  1.00 15.95           C  
ANISOU 1173  CB  GLU A 154     2176   2023   1859   -148    127    -62       C  
ATOM   1174  CG  GLU A 154      -8.518   7.975  -9.877  1.00 16.20           C  
ANISOU 1174  CG  GLU A 154     2209   1982   1962   -110     37   -170       C  
ATOM   1175  CD  GLU A 154      -8.160   9.268 -10.585  1.00 19.03           C  
ANISOU 1175  CD  GLU A 154     2312   2324   2595   -140     63     39       C  
ATOM   1176  OE1 GLU A 154      -9.039   9.945 -11.179  1.00 18.74           O  
ANISOU 1176  OE1 GLU A 154     2472   2040   2606   -365     26   -245       O  
ATOM   1177  OE2 GLU A 154      -6.954   9.605 -10.523  1.00 20.84           O1-
ANISOU 1177  OE2 GLU A 154     2344   2650   2921   -458     19    119       O1-
ATOM   1178  N   THR A 155     -11.864   9.192  -9.948  1.00 14.80           N  
ANISOU 1178  N   THR A 155     1986   1788   1846   -160    -57     20       N  
ATOM   1179  CA  THR A 155     -13.016   8.682 -10.724  1.00 14.89           C  
ANISOU 1179  CA  THR A 155     1981   1851   1825   -135      6      0       C  
ATOM   1180  C   THR A 155     -12.689   8.402 -12.189  1.00 13.96           C  
ANISOU 1180  C   THR A 155     1886   1615   1803   -171    -44    -18       C  
ATOM   1181  O   THR A 155     -13.595   8.088 -12.958  1.00 14.49           O  
ANISOU 1181  O   THR A 155     2162   1631   1713   -114   -206     75       O  
ATOM   1182  CB  THR A 155     -14.242   9.597 -10.643  1.00 15.79           C  
ANISOU 1182  CB  THR A 155     2164   1918   1916   -101     12     68       C  
ATOM   1183  CG2 THR A 155     -14.625   9.854  -9.199  1.00 16.88           C  
ANISOU 1183  CG2 THR A 155     2262   2184   1966    -55     14    -59       C  
ATOM   1184  OG1 THR A 155     -13.976  10.900 -11.214  1.00 18.49           O  
ANISOU 1184  OG1 THR A 155     2805   1726   2494    -88     27    -54       O  
ATOM   1185  N   SER A 156     -11.430   8.483 -12.580  1.00 12.19           N  
ANISOU 1185  N   SER A 156     1883   1249   1498   -166    -24    -12       N  
ATOM   1186  CA  SER A 156     -11.079   8.349 -14.006  1.00 11.52           C  
ANISOU 1186  CA  SER A 156     1715   1223   1439   -121     61    -51       C  
ATOM   1187  C   SER A 156     -11.388   6.981 -14.628  1.00 11.34           C  
ANISOU 1187  C   SER A 156     1876   1229   1204   -169    -21    -10       C  
ATOM   1188  O   SER A 156     -11.633   6.871 -15.837  1.00 10.23           O  
ANISOU 1188  O   SER A 156     1783    920   1180   -392     52    -69       O  
ATOM   1189  CB  SER A 156      -9.612   8.714 -14.186  1.00 12.00           C  
ANISOU 1189  CB  SER A 156     1710   1377   1470   -201    -21    -77       C  
ATOM   1190  OG  SER A 156      -8.717   7.847 -13.465  1.00 13.33           O  
ANISOU 1190  OG  SER A 156     2006   1255   1802   -372    -60    -30       O  
ATOM   1191  N   ALA A 157     -11.388   5.925 -13.828  1.00 11.54           N  
ANISOU 1191  N   ALA A 157     1931   1154   1299   -178    -26    -37       N  
ATOM   1192  CA  ALA A 157     -11.606   4.591 -14.404  1.00 11.09           C  
ANISOU 1192  CA  ALA A 157     1719   1244   1249   -183    -11    -39       C  
ATOM   1193  C   ALA A 157     -12.953   4.496 -15.055  1.00 12.09           C  
ANISOU 1193  C   ALA A 157     1825   1398   1370   -125    -62    -45       C  
ATOM   1194  O   ALA A 157     -13.065   4.075 -16.243  1.00 11.96           O  
ANISOU 1194  O   ALA A 157     1978   1322   1242   -514    -73      5       O  
ATOM   1195  CB  ALA A 157     -11.458   3.514 -13.320  1.00 10.53           C  
ANISOU 1195  CB  ALA A 157     1777   1065   1156   -222     44   -102       C  
ATOM   1196  N   GLU A 158     -13.987   4.854 -14.288  1.00 13.45           N  
ANISOU 1196  N   GLU A 158     1792   1717   1600   -218    -41      8       N  
ATOM   1197  CA  GLU A 158     -15.383   4.802 -14.735  1.00 14.40           C  
ANISOU 1197  CA  GLU A 158     1832   1833   1805    -51    -28     11       C  
ATOM   1198  C   GLU A 158     -15.727   6.026 -15.602  1.00 15.11           C  
ANISOU 1198  C   GLU A 158     1920   1926   1895    -73   -110     79       C  
ATOM   1199  O   GLU A 158     -16.532   5.949 -16.525  1.00 16.41           O  
ANISOU 1199  O   GLU A 158     2073   2120   2040   -157   -151    144       O  
ATOM   1200  CB  GLU A 158     -16.348   4.679 -13.523  1.00 14.43           C  
ANISOU 1200  CB  GLU A 158     1765   1902   1816    -20    -74    114       C  
ATOM   1201  CG  GLU A 158     -16.363   5.879 -12.557  1.00 16.25           C  
ANISOU 1201  CG  GLU A 158     1934   2076   2161     47     -8     70       C  
ATOM   1202  CD  GLU A 158     -15.340   5.817 -11.442  1.00 16.30           C  
ANISOU 1202  CD  GLU A 158     2253   1996   1943     29     -8     72       C  
ATOM   1203  OE1 GLU A 158     -14.280   5.240 -11.659  1.00 14.11           O  
ANISOU 1203  OE1 GLU A 158     2084   1677   1598    -49    274    268       O  
ATOM   1204  OE2 GLU A 158     -15.596   6.396 -10.349  1.00 17.10           O1-
ANISOU 1204  OE2 GLU A 158     2544   1946   2006     11     26     64       O1-
ATOM   1205  N   ASP A 159     -15.096   7.156 -15.345  1.00 15.12           N  
ANISOU 1205  N   ASP A 159     2015   1857   1872    -35   -101    110       N  
ATOM   1206  CA  ASP A 159     -15.478   8.388 -16.064  1.00 16.09           C  
ANISOU 1206  CA  ASP A 159     2166   1941   2007    -27    -26     86       C  
ATOM   1207  C   ASP A 159     -14.895   8.431 -17.495  1.00 15.40           C  
ANISOU 1207  C   ASP A 159     2049   1899   1900    -57    -47     56       C  
ATOM   1208  O   ASP A 159     -15.579   8.822 -18.444  1.00 16.18           O  
ANISOU 1208  O   ASP A 159     2248   1923   1976   -100   -107    142       O  
ATOM   1209  CB  ASP A 159     -14.985   9.616 -15.299  1.00 15.83           C  
ANISOU 1209  CB  ASP A 159     2118   1882   2015     41      2     40       C  
ATOM   1210  CG  ASP A 159     -15.871   9.995 -14.105  1.00 18.55           C  
ANISOU 1210  CG  ASP A 159     2513   2321   2214     33     -8    135       C  
ATOM   1211  OD1 ASP A 159     -16.938   9.375 -13.869  1.00 20.21           O  
ANISOU 1211  OD1 ASP A 159     2674   2493   2509    -57    212    235       O  
ATOM   1212  OD2 ASP A 159     -15.554  10.946 -13.364  1.00 23.18           O1-
ANISOU 1212  OD2 ASP A 159     3422   2678   2705     78   -115    -98       O1-
ATOM   1213  N   GLU A 160     -13.646   8.008 -17.633  1.00 14.38           N  
ANISOU 1213  N   GLU A 160     2038   1719   1704    -72     -9     -7       N  
ATOM   1214  CA  GLU A 160     -12.845   8.155 -18.849  1.00 14.82           C  
ANISOU 1214  CA  GLU A 160     2016   1782   1830    -74     29    -19       C  
ATOM   1215  C   GLU A 160     -12.298   6.845 -19.400  1.00 12.29           C  
ANISOU 1215  C   GLU A 160     1748   1392   1528   -134      3     45       C  
ATOM   1216  O   GLU A 160     -11.831   6.825 -20.519  1.00 11.28           O  
ANISOU 1216  O   GLU A 160     1942    884   1459   -414    150     -8       O  
ATOM   1217  CB  GLU A 160     -11.583   8.997 -18.538  1.00 16.82           C  
ANISOU 1217  CB  GLU A 160     2281   2045   2064   -122     68     -8       C  
ATOM   1218  CG  GLU A 160     -11.730  10.494 -18.513  1.00 22.05           C  
ANISOU 1218  CG  GLU A 160     2980   2557   2837     36     66    -30       C  
ATOM   1219  CD  GLU A 160     -10.440  11.174 -18.074  1.00 26.61           C  
ANISOU 1219  CD  GLU A 160     3242   3400   3469   -138    -26    -51       C  
ATOM   1220  OE1 GLU A 160      -9.486  10.492 -17.605  1.00 28.90           O  
ANISOU 1220  OE1 GLU A 160     3777   3389   3813    -87     84      5       O  
ATOM   1221  OE2 GLU A 160     -10.391  12.411 -18.186  1.00 32.26           O1-
ANISOU 1221  OE2 GLU A 160     4258   3716   4283    -98    -55     80       O1-
ATOM   1222  N   GLY A 161     -12.239   5.776 -18.597  1.00 10.10           N  
ANISOU 1222  N   GLY A 161     1558   1075   1203   -140     15     20       N  
ATOM   1223  CA  GLY A 161     -11.583   4.551 -19.035  1.00  9.17           C  
ANISOU 1223  CA  GLY A 161     1337   1022   1123   -112     14      6       C  
ATOM   1224  C   GLY A 161     -10.092   4.440 -18.661  1.00  7.97           C  
ANISOU 1224  C   GLY A 161     1361    747    919    -61    -56     36       C  
ATOM   1225  O   GLY A 161      -9.337   3.704 -19.254  1.00  8.67           O  
ANISOU 1225  O   GLY A 161     1513    545   1234   -341    -10   -176       O  
ATOM   1226  N   VAL A 162      -9.652   5.193 -17.652  1.00  8.31           N  
ANISOU 1226  N   VAL A 162     1432    780    942   -195    -49     27       N  
ATOM   1227  CA  VAL A 162      -8.256   5.224 -17.264  1.00  9.90           C  
ANISOU 1227  CA  VAL A 162     1554   1061   1145   -187     19     77       C  
ATOM   1228  C   VAL A 162      -8.115   4.811 -15.815  1.00  9.56           C  
ANISOU 1228  C   VAL A 162     1442   1089   1101   -153    -65     31       C  
ATOM   1229  O   VAL A 162      -8.431   5.577 -14.909  1.00  9.91           O  
ANISOU 1229  O   VAL A 162     1686    992   1088   -442    -14    169       O  
ATOM   1230  CB  VAL A 162      -7.674   6.667 -17.486  1.00  9.94           C  
ANISOU 1230  CB  VAL A 162     1572    990   1216   -180    -75      4       C  
ATOM   1231  CG1 VAL A 162      -6.271   6.772 -17.029  1.00 12.77           C  
ANISOU 1231  CG1 VAL A 162     1723   1592   1536   -324    -75    -20       C  
ATOM   1232  CG2 VAL A 162      -7.779   7.074 -18.961  1.00 13.11           C  
ANISOU 1232  CG2 VAL A 162     2007   1385   1587   -190     29    132       C  
ATOM   1233  N   SER A 163      -7.728   3.575 -15.593  1.00 10.67           N  
ANISOU 1233  N   SER A 163     1611   1228   1214   -125     -1      9       N  
ATOM   1234  CA  SER A 163      -7.521   3.062 -14.253  1.00 12.08           C  
ANISOU 1234  CA  SER A 163     1761   1458   1371   -135   -101     36       C  
ATOM   1235  C   SER A 163      -6.081   3.343 -13.873  1.00 12.68           C  
ANISOU 1235  C   SER A 163     1726   1555   1536    -60    -43     33       C  
ATOM   1236  O   SER A 163      -5.150   2.987 -14.632  1.00 15.21           O  
ANISOU 1236  O   SER A 163     1990   1947   1839    -19   -136    -57       O  
ATOM   1237  CB  SER A 163      -7.799   1.544 -14.253  1.00 13.57           C  
ANISOU 1237  CB  SER A 163     2016   1464   1676    -94    -65    121       C  
ATOM   1238  OG  SER A 163      -7.105   0.832 -13.202  1.00 16.80           O  
ANISOU 1238  OG  SER A 163     2841   1838   1704   -135   -364    163       O  
ATOM   1239  N   GLN A 164      -5.903   4.010 -12.727  1.00 11.62           N  
ANISOU 1239  N   GLN A 164     1601   1548   1264   -126   -115     82       N  
ATOM   1240  CA  GLN A 164      -4.587   4.410 -12.220  1.00 11.59           C  
ANISOU 1240  CA  GLN A 164     1455   1515   1434   -105    -31     51       C  
ATOM   1241  C   GLN A 164      -4.638   4.512 -10.686  1.00 11.71           C  
ANISOU 1241  C   GLN A 164     1484   1552   1411    -14    -49      8       C  
ATOM   1242  O   GLN A 164      -5.717   4.773 -10.102  1.00 13.01           O  
ANISOU 1242  O   GLN A 164     1599   1823   1520   -160   -124    -46       O  
ATOM   1243  CB  GLN A 164      -4.204   5.788 -12.773  1.00 12.96           C  
ANISOU 1243  CB  GLN A 164     1563   1765   1595   -207   -125     46       C  
ATOM   1244  CG  GLN A 164      -5.214   6.892 -12.458  1.00 16.52           C  
ANISOU 1244  CG  GLN A 164     2309   2002   1965   -110     71      6       C  
ATOM   1245  CD  GLN A 164      -4.901   8.198 -13.209  1.00 18.61           C  
ANISOU 1245  CD  GLN A 164     2338   2196   2534    -98     10    211       C  
ATOM   1246  NE2 GLN A 164      -5.934   8.884 -13.717  1.00 18.81           N  
ANISOU 1246  NE2 GLN A 164     2450   2158   2537   -245    -87    151       N  
ATOM   1247  OE1 GLN A 164      -3.722   8.577 -13.303  1.00 23.02           O  
ANISOU 1247  OE1 GLN A 164     2494   2980   3273   -265     24    127       O  
ATOM   1248  N   ARG A 165      -3.489   4.259 -10.046  1.00 10.97           N  
ANISOU 1248  N   ARG A 165     1289   1632   1245   -182   -118   -303       N  
ATOM   1249  CA  ARG A 165      -3.325   4.436  -8.592  1.00 10.53           C  
ANISOU 1249  CA  ARG A 165     1321   1446   1231   -179   -100    -15       C  
ATOM   1250  C   ARG A 165      -1.870   4.837  -8.324  1.00 10.52           C  
ANISOU 1250  C   ARG A 165     1351   1380   1265   -178    -34   -131       C  
ATOM   1251  O   ARG A 165      -0.991   4.617  -9.129  1.00 12.78           O  
ANISOU 1251  O   ARG A 165     1436   2032   1388   -415   -180   -421       O  
ATOM   1252  CB  ARG A 165      -3.713   3.192  -7.808  1.00  8.96           C  
ANISOU 1252  CB  ARG A 165     1174   1073   1157   -205   -262    -60       C  
ATOM   1253  CG  ARG A 165      -2.670   2.107  -7.978  1.00 11.20           C  
ANISOU 1253  CG  ARG A 165     1243   1471   1541   -111   -291    -75       C  
ATOM   1254  CD  ARG A 165      -3.051   0.844  -7.413  1.00 10.94           C  
ANISOU 1254  CD  ARG A 165     1358   1436   1363     39   -325      4       C  
ATOM   1255  NE  ARG A 165      -1.996  -0.175  -7.330  1.00  9.23           N  
ANISOU 1255  NE  ARG A 165     1630   1047    828    119   -390   -204       N  
ATOM   1256  CZ  ARG A 165      -1.857  -1.201  -8.155  1.00  9.71           C  
ANISOU 1256  CZ  ARG A 165     1580   1045   1061     35   -239    -54       C  
ATOM   1257  NH1 ARG A 165      -2.565  -1.238  -9.256  1.00 12.42           N1+
ANISOU 1257  NH1 ARG A 165     2321   1305   1090   -153   -299    -99       N1+
ATOM   1258  NH2 ARG A 165      -0.961  -2.131  -7.906  1.00  9.30           N  
ANISOU 1258  NH2 ARG A 165     1351   1253    927    -31    259   -235       N  
ATOM   1259  N   LYS A 166      -1.627   5.428  -7.168  1.00  9.26           N  
ANISOU 1259  N   LYS A 166     1231   1275   1011   -301    -86    -46       N  
ATOM   1260  CA  LYS A 166      -0.272   5.907  -6.908  1.00  8.91           C  
ANISOU 1260  CA  LYS A 166     1071   1239   1073   -134   -113      6       C  
ATOM   1261  C   LYS A 166       0.750   4.889  -6.417  1.00  8.15           C  
ANISOU 1261  C   LYS A 166     1060   1214    823   -117   -120    -78       C  
ATOM   1262  O   LYS A 166       1.919   4.937  -6.834  1.00  8.76           O  
ANISOU 1262  O   LYS A 166     1159   1462    706   -231   -104    -38       O  
ATOM   1263  CB  LYS A 166      -0.274   7.070  -5.894  1.00 10.60           C  
ANISOU 1263  CB  LYS A 166     1338   1301   1386     18     14    -59       C  
ATOM   1264  CG  LYS A 166      -1.049   8.278  -6.379  1.00 13.37           C  
ANISOU 1264  CG  LYS A 166     1744   1652   1684     84   -227    110       C  
ATOM   1265  CD  LYS A 166      -1.084   9.441  -5.427  1.00 18.88           C  
ANISOU 1265  CD  LYS A 166     2518   2351   2302   -130   -200   -207       C  
ATOM   1266  CE  LYS A 166      -2.035  10.534  -5.968  1.00 26.16           C  
ANISOU 1266  CE  LYS A 166     3295   3167   3477     93   -162    -60       C  
ATOM   1267  NZ  LYS A 166      -2.951  11.049  -4.870  1.00 31.16           N1+
ANISOU 1267  NZ  LYS A 166     3967   4025   3845      2     97    -90       N1+
ATOM   1268  N   PHE A 167       0.331   3.969  -5.550  1.00  7.60           N  
ANISOU 1268  N   PHE A 167      983   1145    759    -59   -117    -74       N  
ATOM   1269  CA  PHE A 167       1.254   3.109  -4.809  1.00  8.52           C  
ANISOU 1269  CA  PHE A 167     1069   1252    915      1     -5    -40       C  
ATOM   1270  C   PHE A 167       0.883   1.623  -4.944  1.00  7.98           C  
ANISOU 1270  C   PHE A 167     1101   1108    820     88    -48    -12       C  
ATOM   1271  O   PHE A 167       0.064   1.274  -5.803  1.00  9.03           O  
ANISOU 1271  O   PHE A 167     1080   1373    976     16   -261    -75       O  
ATOM   1272  CB  PHE A 167       1.321   3.580  -3.327  1.00  7.99           C  
ANISOU 1272  CB  PHE A 167      924   1305    807     39    -54    -34       C  
ATOM   1273  CG  PHE A 167       1.661   5.030  -3.156  1.00  8.05           C  
ANISOU 1273  CG  PHE A 167     1095   1382    579     91    -67     -2       C  
ATOM   1274  CD1 PHE A 167       2.883   5.525  -3.623  1.00  8.67           C  
ANISOU 1274  CD1 PHE A 167     1209   1349    733    -29   -122    -38       C  
ATOM   1275  CD2 PHE A 167       0.774   5.916  -2.571  1.00  8.34           C  
ANISOU 1275  CD2 PHE A 167     1211   1373    581    -34   -187    -60       C  
ATOM   1276  CE1 PHE A 167       3.217   6.863  -3.480  1.00  9.17           C  
ANISOU 1276  CE1 PHE A 167     1166   1487    831   -269    -13    -24       C  
ATOM   1277  CE2 PHE A 167       1.117   7.245  -2.428  1.00  9.59           C  
ANISOU 1277  CE2 PHE A 167     1279   1399    963     14   -120   -100       C  
ATOM   1278  CZ  PHE A 167       2.315   7.733  -2.936  1.00  9.94           C  
ANISOU 1278  CZ  PHE A 167     1468   1361    945   -128   -277    -11       C  
ATOM   1279  N   LEU A 168       1.461   0.739  -4.140  1.00  7.39           N  
ANISOU 1279  N   LEU A 168      894   1215    696    -57   -142     23       N  
ATOM   1280  CA  LEU A 168       1.197  -0.664  -4.291  1.00  7.80           C  
ANISOU 1280  CA  LEU A 168     1090   1188    683    130    -55   -160       C  
ATOM   1281  C   LEU A 168      -0.258  -1.055  -4.210  1.00  8.01           C  
ANISOU 1281  C   LEU A 168     1190   1131    721      9    -62    -30       C  
ATOM   1282  O   LEU A 168      -0.754  -1.860  -5.011  1.00  8.45           O  
ANISOU 1282  O   LEU A 168     1357   1112    739     72   -121    -42       O  
ATOM   1283  CB  LEU A 168       1.977  -1.469  -3.261  1.00  8.77           C  
ANISOU 1283  CB  LEU A 168     1290   1255    786     50    -11     21       C  
ATOM   1284  CG  LEU A 168       3.424  -1.810  -3.572  1.00  8.58           C  
ANISOU 1284  CG  LEU A 168     1169   1381    709     -2     -6    -98       C  
ATOM   1285  CD1 LEU A 168       4.091  -2.392  -2.311  1.00  8.73           C  
ANISOU 1285  CD1 LEU A 168     1106   1351    859    211    -16    -60       C  
ATOM   1286  CD2 LEU A 168       3.515  -2.822  -4.780  1.00  9.69           C  
ANISOU 1286  CD2 LEU A 168     1103   1578    998     37    -40   -152       C  
ATOM   1287  N   ASP A 169      -0.952  -0.502  -3.226  1.00  7.19           N  
ANISOU 1287  N   ASP A 169     1178    890    663     71    -35    -90       N  
ATOM   1288  CA  ASP A 169      -2.266  -0.959  -2.846  1.00  8.41           C  
ANISOU 1288  CA  ASP A 169     1267   1064    863     -8    -29    -43       C  
ATOM   1289  C   ASP A 169      -3.400  -0.018  -3.152  1.00  9.14           C  
ANISOU 1289  C   ASP A 169     1207   1176   1087     16    -15     16       C  
ATOM   1290  O   ASP A 169      -4.560  -0.357  -2.933  1.00 11.39           O  
ANISOU 1290  O   ASP A 169     1362   1384   1581     -5    164     46       O  
ATOM   1291  CB  ASP A 169      -2.268  -1.181  -1.314  1.00  9.04           C  
ANISOU 1291  CB  ASP A 169     1543   1040    850     10     27    -80       C  
ATOM   1292  CG  ASP A 169      -3.409  -2.038  -0.832  1.00 10.07           C  
ANISOU 1292  CG  ASP A 169     1583   1408    834    -47    -38    -57       C  
ATOM   1293  OD1 ASP A 169      -3.530  -3.207  -1.278  1.00  9.02           O  
ANISOU 1293  OD1 ASP A 169     1433   1294    698   -156     -7    131       O  
ATOM   1294  OD2 ASP A 169      -4.218  -1.630   0.042  1.00 10.88           O1-
ANISOU 1294  OD2 ASP A 169     1584   1336   1212   -267    285     11       O1-
ATOM   1295  N   GLY A 170      -3.076   1.161  -3.664  1.00  8.16           N  
ANISOU 1295  N   GLY A 170      990   1064   1046     30     77    -29       N  
ATOM   1296  CA  GLY A 170      -4.020   2.237  -3.793  1.00  7.94           C  
ANISOU 1296  CA  GLY A 170      958   1071    984    -19    -84     90       C  
ATOM   1297  C   GLY A 170      -3.321   3.577  -3.762  1.00  7.54           C  
ANISOU 1297  C   GLY A 170     1040    988    836     13    -24     39       C  
ATOM   1298  O   GLY A 170      -2.124   3.666  -4.064  1.00  7.98           O  
ANISOU 1298  O   GLY A 170     1066   1193    774      6    -73     76       O  
ATOM   1299  N   ASN A 171      -4.045   4.595  -3.352  1.00  7.67           N  
ANISOU 1299  N   ASN A 171      976   1067    871      6   -169    -10       N  
ATOM   1300  CA  ASN A 171      -3.516   5.941  -3.402  1.00  8.59           C  
ANISOU 1300  CA  ASN A 171     1117   1076   1070     -3    -86    -51       C  
ATOM   1301  C   ASN A 171      -2.853   6.428  -2.119  1.00  9.26           C  
ANISOU 1301  C   ASN A 171     1048   1275   1195    -19    -72   -106       C  
ATOM   1302  O   ASN A 171      -2.420   7.555  -2.087  1.00 11.67           O  
ANISOU 1302  O   ASN A 171     1320   1657   1456    -93   -105    -69       O  
ATOM   1303  CB  ASN A 171      -4.601   6.910  -3.844  1.00  9.61           C  
ANISOU 1303  CB  ASN A 171     1194   1218   1240    -15   -125   -112       C  
ATOM   1304  CG  ASN A 171      -5.016   6.688  -5.307  1.00 11.41           C  
ANISOU 1304  CG  ASN A 171     1479   1488   1367    -80     19    -11       C  
ATOM   1305  ND2 ASN A 171      -6.306   6.938  -5.608  1.00 11.37           N  
ANISOU 1305  ND2 ASN A 171     1540   1305   1474   -191   -180    104       N  
ATOM   1306  OD1 ASN A 171      -4.175   6.386  -6.145  1.00 11.34           O  
ANISOU 1306  OD1 ASN A 171     1691   1516   1098    342    -89     11       O  
ATOM   1307  N   GLU A 172      -2.838   5.606  -1.097  1.00  9.54           N  
ANISOU 1307  N   GLU A 172     1021   1392   1212     36   -110   -137       N  
ATOM   1308  CA  GLU A 172      -2.163   5.925   0.167  1.00 10.58           C  
ANISOU 1308  CA  GLU A 172     1288   1500   1233    -12   -104   -142       C  
ATOM   1309  C   GLU A 172      -0.997   4.970   0.409  1.00  9.59           C  
ANISOU 1309  C   GLU A 172     1280   1322   1041    -85    -84    -24       C  
ATOM   1310  O   GLU A 172      -1.068   3.793   0.042  1.00  9.29           O  
ANISOU 1310  O   GLU A 172     1220   1504    804    -59    -72    -77       O  
ATOM   1311  CB  GLU A 172      -3.163   5.853   1.318  1.00 14.21           C  
ANISOU 1311  CB  GLU A 172     1662   2183   1554    -22   -155   -126       C  
ATOM   1312  CG  GLU A 172      -4.348   6.828   1.256  1.00 17.74           C  
ANISOU 1312  CG  GLU A 172     2134   2464   2140     62    -48    -88       C  
ATOM   1313  CD  GLU A 172      -3.982   8.301   1.167  1.00 21.02           C  
ANISOU 1313  CD  GLU A 172     2702   2327   2957    393     25     55       C  
ATOM   1314  OE1 GLU A 172      -2.906   8.722   1.673  1.00 26.98           O  
ANISOU 1314  OE1 GLU A 172     3324   3354   3572    215   -268   -151       O  
ATOM   1315  OE2 GLU A 172      -4.816   9.119   0.642  1.00 26.60           O1-
ANISOU 1315  OE2 GLU A 172     3018   3641   3447    373   -387    320       O1-
ATOM   1316  N   LEU A 173       0.066   5.460   1.032  1.00  8.45           N  
ANISOU 1316  N   LEU A 173     1044   1235    930    -54     30     16       N  
ATOM   1317  CA  LEU A 173       1.157   4.597   1.417  1.00  7.65           C  
ANISOU 1317  CA  LEU A 173     1088   1035    780    -68    -46    -28       C  
ATOM   1318  C   LEU A 173       0.714   3.592   2.499  1.00  8.15           C  
ANISOU 1318  C   LEU A 173     1132   1295    666    -39    -30    -66       C  
ATOM   1319  O   LEU A 173      -0.013   3.960   3.440  1.00  9.85           O  
ANISOU 1319  O   LEU A 173     1332   1547    863     20    133   -106       O  
ATOM   1320  CB  LEU A 173       2.352   5.431   1.909  1.00  7.82           C  
ANISOU 1320  CB  LEU A 173     1084   1127    759    -67     13     12       C  
ATOM   1321  CG  LEU A 173       3.081   6.248   0.835  1.00  7.59           C  
ANISOU 1321  CG  LEU A 173      991   1148    745     79    -68      8       C  
ATOM   1322  CD1 LEU A 173       3.966   7.276   1.476  1.00  9.09           C  
ANISOU 1322  CD1 LEU A 173     1217   1389    845    -54     51    -19       C  
ATOM   1323  CD2 LEU A 173       3.866   5.299  -0.098  1.00  8.84           C  
ANISOU 1323  CD2 LEU A 173     1350   1153    852     -4     75    -21       C  
ATOM   1324  N   THR A 174       1.127   2.357   2.334  1.00  7.44           N  
ANISOU 1324  N   THR A 174     1088   1053    683   -196     16    -58       N  
ATOM   1325  CA  THR A 174       0.814   1.280   3.286  1.00  7.77           C  
ANISOU 1325  CA  THR A 174     1210   1131    610   -115     87    -84       C  
ATOM   1326  C   THR A 174       2.089   0.647   3.824  1.00  7.51           C  
ANISOU 1326  C   THR A 174     1149    971    731   -147     15    -98       C  
ATOM   1327  O   THR A 174       3.205   0.929   3.369  1.00  7.48           O  
ANISOU 1327  O   THR A 174     1233   1053    555   -263    110    -39       O  
ATOM   1328  CB  THR A 174      -0.024   0.147   2.611  1.00  9.24           C  
ANISOU 1328  CB  THR A 174     1281   1254    975   -107     53    -42       C  
ATOM   1329  CG2 THR A 174      -1.368   0.643   2.143  1.00  9.55           C  
ANISOU 1329  CG2 THR A 174     1351   1548    729   -233      4   -189       C  
ATOM   1330  OG1 THR A 174       0.693  -0.382   1.484  1.00  9.01           O  
ANISOU 1330  OG1 THR A 174     1404   1260    759   -333    152   -207       O  
ATOM   1331  N   LEU A 175       1.938  -0.270   4.768  1.00  8.23           N  
ANISOU 1331  N   LEU A 175     1200   1233    694   -293     30     -4       N  
ATOM   1332  CA  LEU A 175       3.079  -1.006   5.284  1.00  8.03           C  
ANISOU 1332  CA  LEU A 175     1191   1059    798   -171     51     57       C  
ATOM   1333  C   LEU A 175       3.872  -1.676   4.142  1.00  8.31           C  
ANISOU 1333  C   LEU A 175     1196    991    970   -166     36     57       C  
ATOM   1334  O   LEU A 175       5.091  -1.777   4.157  1.00  7.58           O  
ANISOU 1334  O   LEU A 175     1096   1188    595   -115     69    115       O  
ATOM   1335  CB  LEU A 175       2.665  -2.098   6.314  1.00  7.33           C  
ANISOU 1335  CB  LEU A 175     1055   1021    710   -219     81     46       C  
ATOM   1336  CG  LEU A 175       1.960  -1.569   7.548  1.00  8.53           C  
ANISOU 1336  CG  LEU A 175     1286   1136    817   -272     98    -67       C  
ATOM   1337  CD1 LEU A 175       1.585  -2.732   8.460  1.00  9.56           C  
ANISOU 1337  CD1 LEU A 175     1370   1235   1027    -50    293    -78       C  
ATOM   1338  CD2 LEU A 175       2.799  -0.574   8.325  1.00  8.13           C  
ANISOU 1338  CD2 LEU A 175     1383    975    731   -245     -6     26       C  
ATOM   1339  N   ALA A 176       3.168  -2.144   3.124  1.00  7.79           N  
ANISOU 1339  N   ALA A 176     1144   1078    735   -192     25    -41       N  
ATOM   1340  CA  ALA A 176       3.846  -2.802   1.992  1.00  8.04           C  
ANISOU 1340  CA  ALA A 176     1086   1184    781   -196     45    -28       C  
ATOM   1341  C   ALA A 176       4.828  -1.873   1.326  1.00  7.77           C  
ANISOU 1341  C   ALA A 176     1101   1104    745   -105     34      3       C  
ATOM   1342  O   ALA A 176       5.912  -2.303   0.950  1.00  7.30           O  
ANISOU 1342  O   ALA A 176     1125    975    674    -93    -49    -67       O  
ATOM   1343  CB  ALA A 176       2.844  -3.385   0.998  1.00  9.93           C  
ANISOU 1343  CB  ALA A 176     1325   1407   1038   -359     -9    -97       C  
ATOM   1344  N   ASP A 177       4.445  -0.618   1.156  1.00  6.33           N  
ANISOU 1344  N   ASP A 177      888    962    553    -81     68     70       N  
ATOM   1345  CA  ASP A 177       5.337   0.358   0.518  1.00  6.80           C  
ANISOU 1345  CA  ASP A 177     1055    867    659   -160    -16      6       C  
ATOM   1346  C   ASP A 177       6.528   0.690   1.415  1.00  6.40           C  
ANISOU 1346  C   ASP A 177     1027    793    611   -137     55    -38       C  
ATOM   1347  O   ASP A 177       7.619   0.917   0.964  1.00  5.86           O  
ANISOU 1347  O   ASP A 177     1043    776    406    -46     57     33       O  
ATOM   1348  CB  ASP A 177       4.616   1.672   0.216  1.00  7.34           C  
ANISOU 1348  CB  ASP A 177     1100   1174    511     50    -85    -26       C  
ATOM   1349  CG  ASP A 177       3.420   1.496  -0.674  1.00  7.54           C  
ANISOU 1349  CG  ASP A 177     1037   1240    588    -31    -83    -53       C  
ATOM   1350  OD1 ASP A 177       3.577   1.185  -1.893  1.00  8.05           O  
ANISOU 1350  OD1 ASP A 177     1110   1375    572    -86     55    -32       O  
ATOM   1351  OD2 ASP A 177       2.284   1.723  -0.204  1.00  8.68           O1-
ANISOU 1351  OD2 ASP A 177      974   1745    578    -41   -120   -217       O1-
ATOM   1352  N   CYS A 178       6.289   0.704   2.732  1.00  6.54           N  
ANISOU 1352  N   CYS A 178      932    933    619   -281    -20    -15       N  
ATOM   1353  CA  CYS A 178       7.354   0.943   3.680  1.00  6.81           C  
ANISOU 1353  CA  CYS A 178     1074    903    608    -89    -50      1       C  
ATOM   1354  C   CYS A 178       8.438  -0.127   3.626  1.00  6.74           C  
ANISOU 1354  C   CYS A 178     1062   1001    495    -79     -8     28       C  
ATOM   1355  O   CYS A 178       9.633   0.159   3.830  1.00  6.65           O  
ANISOU 1355  O   CYS A 178     1153    937    435    -18     32      0       O  
ATOM   1356  CB  CYS A 178       6.816   1.076   5.126  1.00  6.90           C  
ANISOU 1356  CB  CYS A 178     1052   1058    511   -151   -109     20       C  
ATOM   1357  SG  CYS A 178       5.683   2.467   5.381  1.00  7.11           S  
ANISOU 1357  SG  CYS A 178     1104   1037    560    -82     90   -121       S  
ATOM   1358  N   ASN A 179       8.060  -1.373   3.335  1.00  7.75           N  
ANISOU 1358  N   ASN A 179     1247    961    736   -116    -39    -35       N  
ATOM   1359  CA  ASN A 179       9.053  -2.427   3.151  1.00  9.08           C  
ANISOU 1359  CA  ASN A 179     1293   1166    990   -101   -126    -35       C  
ATOM   1360  C   ASN A 179       9.734  -2.325   1.799  1.00  8.48           C  
ANISOU 1360  C   ASN A 179     1233    940   1045      5    -87   -248       C  
ATOM   1361  O   ASN A 179      10.980  -2.345   1.690  1.00  8.95           O  
ANISOU 1361  O   ASN A 179     1331    998   1071    -40   -172   -330       O  
ATOM   1362  CB  ASN A 179       8.362  -3.759   3.335  1.00 10.23           C  
ANISOU 1362  CB  ASN A 179     1674   1301    910   -162   -135     49       C  
ATOM   1363  CG  ASN A 179       9.279  -4.928   3.413  1.00 14.89           C  
ANISOU 1363  CG  ASN A 179     1998   1659   1997    -39    122   -126       C  
ATOM   1364  ND2 ASN A 179       8.810  -5.900   4.186  1.00 21.55           N  
ANISOU 1364  ND2 ASN A 179     2823   2519   2844   -287    129    233       N  
ATOM   1365  OD1 ASN A 179      10.372  -5.025   2.830  1.00 17.03           O  
ANISOU 1365  OD1 ASN A 179     2720   1399   2350   -255    427    156       O  
ATOM   1366  N   LEU A 180       8.933  -2.164   0.734  1.00  6.93           N  
ANISOU 1366  N   LEU A 180     1029    812    790    -23   -101    -54       N  
ATOM   1367  CA  LEU A 180       9.486  -2.247  -0.593  1.00  7.38           C  
ANISOU 1367  CA  LEU A 180      996    864    942     89    -42    -37       C  
ATOM   1368  C   LEU A 180      10.294  -1.024  -1.051  1.00  6.75           C  
ANISOU 1368  C   LEU A 180      963    899    699    -17    -41   -108       C  
ATOM   1369  O   LEU A 180      11.388  -1.179  -1.661  1.00  7.27           O  
ANISOU 1369  O   LEU A 180      937    954    870     69     91   -247       O  
ATOM   1370  CB  LEU A 180       8.388  -2.531  -1.608  1.00  7.87           C  
ANISOU 1370  CB  LEU A 180     1072   1087    832     39    -45   -102       C  
ATOM   1371  CG  LEU A 180       8.836  -2.774  -3.056  1.00  8.36           C  
ANISOU 1371  CG  LEU A 180      954   1268    953     21      0    -99       C  
ATOM   1372  CD1 LEU A 180       9.713  -3.955  -3.177  1.00 10.16           C  
ANISOU 1372  CD1 LEU A 180     1142   1679   1037     98     -1   -438       C  
ATOM   1373  CD2 LEU A 180       7.583  -2.942  -3.944  1.00  9.38           C  
ANISOU 1373  CD2 LEU A 180     1267   1554    743     98    -89   -241       C  
ATOM   1374  N   LEU A 181       9.807   0.190  -0.783  1.00  5.69           N  
ANISOU 1374  N   LEU A 181      863    818    478     21     -4   -158       N  
ATOM   1375  CA  LEU A 181      10.469   1.380  -1.338  1.00  6.44           C  
ANISOU 1375  CA  LEU A 181      959    924    562    -20     59   -114       C  
ATOM   1376  C   LEU A 181      11.912   1.555  -0.872  1.00  6.62           C  
ANISOU 1376  C   LEU A 181     1036    843    635     39     80   -158       C  
ATOM   1377  O   LEU A 181      12.778   1.873  -1.706  1.00  7.52           O  
ANISOU 1377  O   LEU A 181     1095    963    799    -13    233   -229       O  
ATOM   1378  CB  LEU A 181       9.629   2.619  -1.019  1.00  6.17           C  
ANISOU 1378  CB  LEU A 181      768   1008    567    -91     87    -74       C  
ATOM   1379  CG  LEU A 181       8.384   2.793  -1.900  1.00  6.52           C  
ANISOU 1379  CG  LEU A 181      960    845    670     25    -82     99       C  
ATOM   1380  CD1 LEU A 181       7.465   3.892  -1.285  1.00  6.64           C  
ANISOU 1380  CD1 LEU A 181      804   1049    668    -42    157     57       C  
ATOM   1381  CD2 LEU A 181       8.719   3.143  -3.317  1.00  7.39           C  
ANISOU 1381  CD2 LEU A 181      987   1076    743    104      0     54       C  
ATOM   1382  N   PRO A 182      12.246   1.361   0.409  1.00  5.69           N  
ANISOU 1382  N   PRO A 182      707    773    681      8     79   -147       N  
ATOM   1383  CA  PRO A 182      13.669   1.483   0.798  1.00  6.65           C  
ANISOU 1383  CA  PRO A 182      856    963    705     30    -20   -186       C  
ATOM   1384  C   PRO A 182      14.573   0.510   0.020  1.00  7.62           C  
ANISOU 1384  C   PRO A 182     1016    993    886     47    -11    -84       C  
ATOM   1385  O   PRO A 182      15.694   0.840  -0.353  1.00  7.64           O  
ANISOU 1385  O   PRO A 182      920   1092    888    -26    -11   -377       O  
ATOM   1386  CB  PRO A 182      13.671   1.180   2.304  1.00  6.53           C  
ANISOU 1386  CB  PRO A 182      829    875    776    114     10    -71       C  
ATOM   1387  CG  PRO A 182      12.294   1.633   2.733  1.00  6.44           C  
ANISOU 1387  CG  PRO A 182      844    958    642    -65     55    -84       C  
ATOM   1388  CD  PRO A 182      11.360   1.172   1.577  1.00  7.24           C  
ANISOU 1388  CD  PRO A 182      973   1045    730      0    -36   -183       C  
ATOM   1389  N   LYS A 183      14.050  -0.683  -0.241  1.00  7.46           N  
ANISOU 1389  N   LYS A 183      969    970    895     -4     47   -206       N  
ATOM   1390  CA  LYS A 183      14.810  -1.694  -0.991  1.00  7.66           C  
ANISOU 1390  CA  LYS A 183      945   1019    946     95    -30   -167       C  
ATOM   1391  C   LYS A 183      14.981  -1.296  -2.441  1.00  7.53           C  
ANISOU 1391  C   LYS A 183      990    968    902      6     35   -208       C  
ATOM   1392  O   LYS A 183      16.096  -1.368  -2.983  1.00  7.32           O  
ANISOU 1392  O   LYS A 183      879   1003    897    -86    141   -288       O  
ATOM   1393  CB  LYS A 183      14.139  -3.044  -0.829  1.00  8.46           C  
ANISOU 1393  CB  LYS A 183     1095   1184    934    107     63   -158       C  
ATOM   1394  CG  LYS A 183      14.338  -3.635   0.560  1.00  8.90           C  
ANISOU 1394  CG  LYS A 183     1362    995   1022     82    -47   -123       C  
ATOM   1395  CD  LYS A 183      13.507  -4.833   0.750  1.00 10.80           C  
ANISOU 1395  CD  LYS A 183     1756   1374    971    -24    223    -72       C  
ATOM   1396  CE  LYS A 183      13.737  -5.492   2.077  1.00 12.69           C  
ANISOU 1396  CE  LYS A 183     2185   1381   1255     83   -170   -189       C  
ATOM   1397  NZ  LYS A 183      12.806  -6.617   2.376  1.00 15.50           N1+
ANISOU 1397  NZ  LYS A 183     2555   1708   1623   -193     97     81       N1+
ATOM   1398  N   LEU A 184      13.913  -0.875  -3.103  1.00  6.86           N  
ANISOU 1398  N   LEU A 184      908    881    815      7     16   -174       N  
ATOM   1399  CA  LEU A 184      14.025  -0.420  -4.487  1.00  8.40           C  
ANISOU 1399  CA  LEU A 184     1100   1221    870     92     35   -172       C  
ATOM   1400  C   LEU A 184      14.965   0.754  -4.615  1.00  8.17           C  
ANISOU 1400  C   LEU A 184     1113   1171    820     92    129    -61       C  
ATOM   1401  O   LEU A 184      15.685   0.881  -5.591  1.00  7.98           O  
ANISOU 1401  O   LEU A 184      928   1312    792    207     35    -69       O  
ATOM   1402  CB  LEU A 184      12.674  -0.030  -5.049  1.00 10.06           C  
ANISOU 1402  CB  LEU A 184     1091   1479   1252    153    171   -116       C  
ATOM   1403  CG  LEU A 184      11.727  -1.171  -5.300  1.00 10.73           C  
ANISOU 1403  CG  LEU A 184     1341   1513   1223    181     27    -44       C  
ATOM   1404  CD1 LEU A 184      10.362  -0.646  -5.835  1.00 11.22           C  
ANISOU 1404  CD1 LEU A 184     1343   1584   1334    -16   -143   -266       C  
ATOM   1405  CD2 LEU A 184      12.292  -2.173  -6.269  1.00 12.23           C  
ANISOU 1405  CD2 LEU A 184     1473   1666   1507   -106     15   -386       C  
ATOM   1406  N   HIS A 185      14.943   1.656  -3.636  1.00  7.07           N  
ANISOU 1406  N   HIS A 185      885   1036    763     -7    226   -112       N  
ATOM   1407  CA  HIS A 185      15.848   2.781  -3.683  1.00  7.43           C  
ANISOU 1407  CA  HIS A 185      953    974    895    132    160    -76       C  
ATOM   1408  C   HIS A 185      17.328   2.344  -3.674  1.00  7.43           C  
ANISOU 1408  C   HIS A 185     1006   1083    732     44     97   -105       C  
ATOM   1409  O   HIS A 185      18.140   2.862  -4.464  1.00  7.15           O  
ANISOU 1409  O   HIS A 185     1056    939    720    133    160    -88       O  
ATOM   1410  CB  HIS A 185      15.553   3.769  -2.539  1.00  8.69           C  
ANISOU 1410  CB  HIS A 185     1190   1211    898     92    138   -144       C  
ATOM   1411  CG  HIS A 185      16.323   5.020  -2.656  1.00  9.31           C  
ANISOU 1411  CG  HIS A 185     1265   1230   1041    237    280   -205       C  
ATOM   1412  CD2 HIS A 185      16.312   5.947  -3.632  1.00  9.56           C  
ANISOU 1412  CD2 HIS A 185     1264   1384    982    203    -13    -31       C  
ATOM   1413  ND1 HIS A 185      17.312   5.391  -1.768  1.00 11.84           N  
ANISOU 1413  ND1 HIS A 185     1513   1237   1746     93    284   -289       N  
ATOM   1414  CE1 HIS A 185      17.848   6.539  -2.180  1.00  9.22           C  
ANISOU 1414  CE1 HIS A 185     1378    933   1190     34    340   -333       C  
ATOM   1415  NE2 HIS A 185      17.256   6.892  -3.303  1.00 13.73           N  
ANISOU 1415  NE2 HIS A 185     1658   1558   1997    -42    342   -109       N  
ATOM   1416  N   ILE A 186      17.664   1.416  -2.792  1.00  6.36           N  
ANISOU 1416  N   ILE A 186      784   1022    609    141    102   -185       N  
ATOM   1417  CA  ILE A 186      19.000   0.846  -2.756  1.00  6.47           C  
ANISOU 1417  CA  ILE A 186      862    932    661     95    131   -175       C  
ATOM   1418  C   ILE A 186      19.352   0.196  -4.090  1.00  6.59           C  
ANISOU 1418  C   ILE A 186      835   1034    634     66     25   -136       C  
ATOM   1419  O   ILE A 186      20.425   0.415  -4.624  1.00  6.22           O  
ANISOU 1419  O   ILE A 186      753   1051    559    145     35    -87       O  
ATOM   1420  CB  ILE A 186      19.148  -0.130  -1.575  1.00  6.55           C  
ANISOU 1420  CB  ILE A 186      849   1079    560     86     -4   -161       C  
ATOM   1421  CG1 ILE A 186      19.065   0.613  -0.259  1.00  7.05           C  
ANISOU 1421  CG1 ILE A 186      930   1055    692     59    -38   -199       C  
ATOM   1422  CG2 ILE A 186      20.488  -0.904  -1.691  1.00  7.50           C  
ANISOU 1422  CG2 ILE A 186     1134    877    838    180     63   -140       C  
ATOM   1423  CD1 ILE A 186      18.786  -0.330   0.893  1.00  9.53           C  
ANISOU 1423  CD1 ILE A 186     1339   1210   1070   -122    -47   -180       C  
ATOM   1424  N   VAL A 187      18.452  -0.599  -4.620  1.00  6.10           N  
ANISOU 1424  N   VAL A 187      847   1035    435    137      4   -182       N  
ATOM   1425  CA  VAL A 187      18.680  -1.238  -5.929  1.00  6.97           C  
ANISOU 1425  CA  VAL A 187      924   1186    537    183     15   -200       C  
ATOM   1426  C   VAL A 187      19.058  -0.179  -6.951  1.00  7.07           C  
ANISOU 1426  C   VAL A 187      928   1220    539     74     24   -167       C  
ATOM   1427  O   VAL A 187      20.044  -0.288  -7.699  1.00  7.86           O  
ANISOU 1427  O   VAL A 187      915   1442    629    203     14   -183       O  
ATOM   1428  CB  VAL A 187      17.455  -2.033  -6.386  1.00  7.56           C  
ANISOU 1428  CB  VAL A 187      952   1223    695    124    146   -185       C  
ATOM   1429  CG1 VAL A 187      17.624  -2.512  -7.825  1.00  8.55           C  
ANISOU 1429  CG1 VAL A 187      882   1509    857     15     37   -241       C  
ATOM   1430  CG2 VAL A 187      17.144  -3.169  -5.460  1.00  8.15           C  
ANISOU 1430  CG2 VAL A 187      936   1235    923    246     36   -262       C  
ATOM   1431  N   GLN A 188      18.268   0.893  -7.028  1.00  7.13           N  
ANISOU 1431  N   GLN A 188      835   1202    670    118    133   -108       N  
ATOM   1432  CA  GLN A 188      18.529   1.919  -7.997  1.00  7.82           C  
ANISOU 1432  CA  GLN A 188     1076   1186    709    163     39    -98       C  
ATOM   1433  C   GLN A 188      19.888   2.572  -7.848  1.00  7.76           C  
ANISOU 1433  C   GLN A 188     1058   1150    738    147    106   -140       C  
ATOM   1434  O   GLN A 188      20.670   2.714  -8.819  1.00  7.71           O  
ANISOU 1434  O   GLN A 188      923   1295    711    232     53    -69       O  
ATOM   1435  CB  GLN A 188      17.476   3.035  -7.987  1.00  8.82           C  
ANISOU 1435  CB  GLN A 188     1074   1308    967    128    206   -189       C  
ATOM   1436  CG  GLN A 188      16.176   2.679  -8.549  1.00 11.03           C  
ANISOU 1436  CG  GLN A 188     1371   1518   1300    -86     90     26       C  
ATOM   1437  CD  GLN A 188      15.363   3.911  -8.913  1.00 14.68           C  
ANISOU 1437  CD  GLN A 188     1608   2124   1845    326   -100   -230       C  
ATOM   1438  NE2 GLN A 188      15.164   4.163 -10.227  1.00 14.62           N  
ANISOU 1438  NE2 GLN A 188     1568   2043   1944    586   -271     -5       N  
ATOM   1439  OE1 GLN A 188      14.975   4.623  -8.047  1.00 17.12           O  
ANISOU 1439  OE1 GLN A 188     1807   2399   2298    418   -160   -761       O  
ATOM   1440  N   VAL A 189      20.195   3.022  -6.639  1.00  6.56           N  
ANISOU 1440  N   VAL A 189      847   1000    644    208     67    -67       N  
ATOM   1441  CA  VAL A 189      21.422   3.754  -6.403  1.00  7.63           C  
ANISOU 1441  CA  VAL A 189     1138    975    783    139     62    -87       C  
ATOM   1442  C   VAL A 189      22.635   2.862  -6.645  1.00  6.85           C  
ANISOU 1442  C   VAL A 189      916   1065    622     88     59    -30       C  
ATOM   1443  O   VAL A 189      23.590   3.279  -7.298  1.00  6.96           O  
ANISOU 1443  O   VAL A 189     1045   1104    495    206     63   -105       O  
ATOM   1444  CB  VAL A 189      21.442   4.363  -4.959  1.00  8.05           C  
ANISOU 1444  CB  VAL A 189     1095   1135    827    135    130   -155       C  
ATOM   1445  CG1 VAL A 189      22.803   4.921  -4.600  1.00  8.98           C  
ANISOU 1445  CG1 VAL A 189     1217   1246    946     49    106   -172       C  
ATOM   1446  CG2 VAL A 189      20.355   5.442  -4.845  1.00  8.49           C  
ANISOU 1446  CG2 VAL A 189     1246    864   1113    129     65   -174       C  
ATOM   1447  N   VAL A 190      22.615   1.651  -6.090  1.00  6.05           N  
ANISOU 1447  N   VAL A 190      723   1009    565    163    108   -124       N  
ATOM   1448  CA  VAL A 190      23.760   0.779  -6.176  1.00  6.28           C  
ANISOU 1448  CA  VAL A 190      724   1008    653     89    -36   -160       C  
ATOM   1449  C   VAL A 190      23.978   0.259  -7.600  1.00  6.79           C  
ANISOU 1449  C   VAL A 190      950    940    689     37      9    -63       C  
ATOM   1450  O   VAL A 190      25.127   0.189  -8.094  1.00  6.32           O  
ANISOU 1450  O   VAL A 190      965    966    467    108     83    -39       O  
ATOM   1451  CB  VAL A 190      23.660  -0.345  -5.133  1.00  6.21           C  
ANISOU 1451  CB  VAL A 190      841   1014    503     83    124   -252       C  
ATOM   1452  CG1 VAL A 190      24.795  -1.381  -5.264  1.00  7.62           C  
ANISOU 1452  CG1 VAL A 190      931   1077    885     60     87    -25       C  
ATOM   1453  CG2 VAL A 190      23.587   0.201  -3.713  1.00  7.39           C  
ANISOU 1453  CG2 VAL A 190      993   1249    565     -5     -5   -215       C  
ATOM   1454  N   CYS A 191      22.906  -0.147  -8.262  1.00  5.95           N  
ANISOU 1454  N   CYS A 191      835    932    494     79     56   -190       N  
ATOM   1455  CA  CYS A 191      23.074  -0.605  -9.638  1.00  6.48           C  
ANISOU 1455  CA  CYS A 191      859    990    612    103     18   -201       C  
ATOM   1456  C   CYS A 191      23.582   0.479 -10.581  1.00  6.62           C  
ANISOU 1456  C   CYS A 191      808   1029    675    101    -31   -116       C  
ATOM   1457  O   CYS A 191      24.360   0.177 -11.502  1.00  7.08           O  
ANISOU 1457  O   CYS A 191      847   1243    599    187   -139    -79       O  
ATOM   1458  CB  CYS A 191      21.772  -1.225 -10.197  1.00  7.06           C  
ANISOU 1458  CB  CYS A 191      786   1201    693     69     37   -170       C  
ATOM   1459  SG  CYS A 191      21.286  -2.795  -9.450  1.00  7.73           S  
ANISOU 1459  SG  CYS A 191     1036   1109    792     66    176   -189       S  
ATOM   1460  N   LYS A 192      23.137   1.722 -10.408  1.00  6.96           N  
ANISOU 1460  N   LYS A 192      955   1000    688    151    -76    -41       N  
ATOM   1461  CA  LYS A 192      23.640   2.790 -11.239  1.00  7.95           C  
ANISOU 1461  CA  LYS A 192     1105   1058    854     77     20    -90       C  
ATOM   1462  C   LYS A 192      25.150   2.973 -11.010  1.00  7.97           C  
ANISOU 1462  C   LYS A 192     1143   1047    837      4     64     -2       C  
ATOM   1463  O   LYS A 192      25.952   3.033 -11.963  1.00  9.31           O  
ANISOU 1463  O   LYS A 192     1178   1338   1018     71     63    -10       O  
ATOM   1464  CB  LYS A 192      22.876   4.100 -10.987  1.00 10.29           C  
ANISOU 1464  CB  LYS A 192     1311   1262   1334     97     11    -64       C  
ATOM   1465  CG  LYS A 192      23.297   5.218 -11.924  1.00 15.19           C  
ANISOU 1465  CG  LYS A 192     1955   1939   1877     63     75    137       C  
ATOM   1466  CD  LYS A 192      22.299   6.387 -11.907  1.00 21.96           C  
ANISOU 1466  CD  LYS A 192     2826   2493   3024    318     27     15       C  
ATOM   1467  CE  LYS A 192      22.785   7.549 -12.800  1.00 27.76           C  
ANISOU 1467  CE  LYS A 192     3681   3521   3346    -57    -12    204       C  
ATOM   1468  NZ  LYS A 192      22.035   8.830 -12.613  1.00 32.63           N1+
ANISOU 1468  NZ  LYS A 192     4169   4154   4074    142     17    -95       N1+
ATOM   1469  N   LYS A 193      25.541   3.018  -9.735  1.00  7.81           N  
ANISOU 1469  N   LYS A 193      962   1156    849     69    -31    -74       N  
ATOM   1470  CA  LYS A 193      26.943   3.292  -9.391  1.00  8.02           C  
ANISOU 1470  CA  LYS A 193     1014    992   1039     74     48    -35       C  
ATOM   1471  C   LYS A 193      27.880   2.191  -9.876  1.00  7.53           C  
ANISOU 1471  C   LYS A 193     1025    997    839     85    153    -38       C  
ATOM   1472  O   LYS A 193      28.925   2.488 -10.463  1.00  8.92           O  
ANISOU 1472  O   LYS A 193     1046    999   1344     57     38    156       O  
ATOM   1473  CB  LYS A 193      27.066   3.463  -7.861  1.00  9.13           C  
ANISOU 1473  CB  LYS A 193     1075   1180   1213    239    -21    -76       C  
ATOM   1474  CG  LYS A 193      28.475   3.482  -7.259  1.00 12.61           C  
ANISOU 1474  CG  LYS A 193     1426   1791   1572     87     34   -151       C  
ATOM   1475  CD  LYS A 193      29.208   4.694  -7.528  1.00 13.58           C  
ANISOU 1475  CD  LYS A 193     1608   1744   1806    181    212    -52       C  
ATOM   1476  CE  LYS A 193      30.550   4.800  -6.771  1.00 14.62           C  
ANISOU 1476  CE  LYS A 193     2012   1907   1636    -54      3    -65       C  
ATOM   1477  NZ  LYS A 193      31.276   6.019  -7.204  1.00 16.38           N1+
ANISOU 1477  NZ  LYS A 193     2278   2206   1739   -230    -26   -274       N1+
ATOM   1478  N   TYR A 194      27.521   0.949  -9.573  1.00  5.93           N  
ANISOU 1478  N   TYR A 194      670    905    676      2      0    -82       N  
ATOM   1479  CA  TYR A 194      28.492  -0.122  -9.763  1.00  6.25           C  
ANISOU 1479  CA  TYR A 194      823    979    570     69     26    -49       C  
ATOM   1480  C   TYR A 194      28.302  -0.945 -11.018  1.00  6.30           C  
ANISOU 1480  C   TYR A 194      880    974    537    -17    101    -23       C  
ATOM   1481  O   TYR A 194      29.159  -1.762 -11.358  1.00  6.56           O  
ANISOU 1481  O   TYR A 194      858   1026    607     82   -121   -162       O  
ATOM   1482  CB  TYR A 194      28.472  -1.068  -8.545  1.00  6.73           C  
ANISOU 1482  CB  TYR A 194      938   1082    537     49     -8    -52       C  
ATOM   1483  CG  TYR A 194      28.978  -0.454  -7.248  1.00  7.70           C  
ANISOU 1483  CG  TYR A 194      991   1264    667     -6    -85   -142       C  
ATOM   1484  CD1 TYR A 194      30.342  -0.266  -7.024  1.00 10.04           C  
ANISOU 1484  CD1 TYR A 194     1171   1801    842    136    -60   -320       C  
ATOM   1485  CD2 TYR A 194      28.107  -0.015  -6.251  1.00  8.81           C  
ANISOU 1485  CD2 TYR A 194     1084   1547    714    101    -77    -40       C  
ATOM   1486  CE1 TYR A 194      30.817   0.297  -5.832  1.00 10.29           C  
ANISOU 1486  CE1 TYR A 194     1115   2028    764     61    -26   -305       C  
ATOM   1487  CE2 TYR A 194      28.566   0.528  -5.062  1.00  9.46           C  
ANISOU 1487  CE2 TYR A 194     1080   1455   1059     29     27   -219       C  
ATOM   1488  CZ  TYR A 194      29.920   0.650  -4.849  1.00  9.40           C  
ANISOU 1488  CZ  TYR A 194     1102   1727    741    116   -145   -621       C  
ATOM   1489  OH  TYR A 194      30.393   1.147  -3.682  1.00 12.72           O  
ANISOU 1489  OH  TYR A 194     1397   2492    944    136   -235   -688       O  
ATOM   1490  N   ARG A 195      27.199  -0.772 -11.710  1.00  5.91           N  
ANISOU 1490  N   ARG A 195      926    916    402     83     14   -162       N  
ATOM   1491  CA  ARG A 195      26.942  -1.474 -12.972  1.00  5.91           C  
ANISOU 1491  CA  ARG A 195      890    907    445     83     65   -151       C  
ATOM   1492  C   ARG A 195      26.493  -0.590 -14.126  1.00  5.81           C  
ANISOU 1492  C   ARG A 195      706   1034    467    -13     37    -75       C  
ATOM   1493  O   ARG A 195      26.349  -1.068 -15.257  1.00  6.57           O  
ANISOU 1493  O   ARG A 195      844   1220    432     75     -8      8       O  
ATOM   1494  CB  ARG A 195      25.899  -2.600 -12.778  1.00  6.28           C  
ANISOU 1494  CB  ARG A 195      895    988    500     85    -35    -70       C  
ATOM   1495  CG  ARG A 195      26.397  -3.743 -11.930  1.00  6.24           C  
ANISOU 1495  CG  ARG A 195      996    944    431    -51    -66   -171       C  
ATOM   1496  CD  ARG A 195      27.350  -4.668 -12.725  1.00  6.56           C  
ANISOU 1496  CD  ARG A 195     1006    939    546    119   -100   -110       C  
ATOM   1497  NE  ARG A 195      27.738  -5.873 -11.966  1.00  6.42           N  
ANISOU 1497  NE  ARG A 195      940    808    691     90   -202     61       N  
ATOM   1498  CZ  ARG A 195      28.682  -5.893 -11.031  1.00  6.38           C  
ANISOU 1498  CZ  ARG A 195      966    987    472     82   -177    -12       C  
ATOM   1499  NH1 ARG A 195      29.367  -4.789 -10.752  1.00  6.76           N1+
ANISOU 1499  NH1 ARG A 195      901   1026    641    156   -172    -47       N1+
ATOM   1500  NH2 ARG A 195      28.924  -6.985 -10.366  1.00  6.73           N  
ANISOU 1500  NH2 ARG A 195      918    946    690    -31   -222   -125       N  
ATOM   1501  N   GLY A 196      26.208   0.670 -13.874  1.00  6.04           N  
ANISOU 1501  N   GLY A 196      825   1070    399     96   -118     23       N  
ATOM   1502  CA  GLY A 196      25.616   1.481 -14.934  1.00  6.90           C  
ANISOU 1502  CA  GLY A 196     1092    962    564    120    -31     63       C  
ATOM   1503  C   GLY A 196      24.262   0.955 -15.381  1.00  8.36           C  
ANISOU 1503  C   GLY A 196     1149   1300    726    112    -99     61       C  
ATOM   1504  O   GLY A 196      23.871   1.133 -16.558  1.00 10.90           O  
ANISOU 1504  O   GLY A 196     1461   1935    742     29   -275    369       O  
ATOM   1505  N   PHE A 197      23.569   0.257 -14.504  1.00  7.62           N  
ANISOU 1505  N   PHE A 197      943   1273    676     75   -182     41       N  
ATOM   1506  CA  PHE A 197      22.284  -0.388 -14.795  1.00  7.61           C  
ANISOU 1506  CA  PHE A 197      965   1269    654     91   -119     -3       C  
ATOM   1507  C   PHE A 197      21.164   0.426 -14.243  1.00  8.40           C  
ANISOU 1507  C   PHE A 197      982   1451    757    107    -51    -78       C  
ATOM   1508  O   PHE A 197      21.208   0.852 -13.099  1.00  9.46           O  
ANISOU 1508  O   PHE A 197      949   1914    728    134    -23   -152       O  
ATOM   1509  CB  PHE A 197      22.248  -1.785 -14.140  1.00  9.55           C  
ANISOU 1509  CB  PHE A 197     1280   1364    982     56   -131    103       C  
ATOM   1510  CG  PHE A 197      20.886  -2.503 -14.199  1.00 11.14           C  
ANISOU 1510  CG  PHE A 197     1350   1641   1239     12   -280   -106       C  
ATOM   1511  CD1 PHE A 197      20.545  -3.325 -15.267  1.00 12.75           C  
ANISOU 1511  CD1 PHE A 197     1369   1578   1897    160   -121   -102       C  
ATOM   1512  CD2 PHE A 197      19.932  -2.261 -13.229  1.00 12.92           C  
ANISOU 1512  CD2 PHE A 197     1488   2182   1238   -345   -335      4       C  
ATOM   1513  CE1 PHE A 197      19.311  -3.940 -15.321  1.00 12.53           C  
ANISOU 1513  CE1 PHE A 197     1355   1666   1737    157   -311   -215       C  
ATOM   1514  CE2 PHE A 197      18.685  -2.888 -13.290  1.00 13.27           C  
ANISOU 1514  CE2 PHE A 197     1297   2275   1468    -61     48    173       C  
ATOM   1515  CZ  PHE A 197      18.399  -3.724 -14.331  1.00 13.30           C  
ANISOU 1515  CZ  PHE A 197     1471   1689   1894    -78    -53     38       C  
ATOM   1516  N   THR A 198      20.152   0.624 -15.050  1.00  8.90           N  
ANISOU 1516  N   THR A 198      965   1633    782    202    -44   -135       N  
ATOM   1517  CA  THR A 198      18.953   1.318 -14.622  1.00  9.81           C  
ANISOU 1517  CA  THR A 198     1157   1507   1060    146     42    -89       C  
ATOM   1518  C   THR A 198      17.711   0.468 -14.898  1.00  8.57           C  
ANISOU 1518  C   THR A 198      914   1474    868    229   -241   -198       C  
ATOM   1519  O   THR A 198      17.678  -0.393 -15.751  1.00 10.52           O  
ANISOU 1519  O   THR A 198      995   2061    938    212   -139   -425       O  
ATOM   1520  CB  THR A 198      18.779   2.631 -15.337  1.00 10.98           C  
ANISOU 1520  CB  THR A 198     1095   1755   1320    230    -55    -70       C  
ATOM   1521  CG2 THR A 198      19.886   3.562 -15.010  1.00 15.25           C  
ANISOU 1521  CG2 THR A 198     1937   1949   1907    -16     16    -20       C  
ATOM   1522  OG1 THR A 198      18.769   2.445 -16.769  1.00 15.77           O  
ANISOU 1522  OG1 THR A 198     2050   2321   1617    311    154    160       O  
ATOM   1523  N   ILE A 199      16.661   0.745 -14.151  1.00  7.48           N  
ANISOU 1523  N   ILE A 199      694   1436    708     95   -207   -189       N  
ATOM   1524  CA  ILE A 199      15.375   0.082 -14.343  1.00  8.02           C  
ANISOU 1524  CA  ILE A 199      973   1314    760      0   -138     -7       C  
ATOM   1525  C   ILE A 199      14.849   0.588 -15.691  1.00  7.82           C  
ANISOU 1525  C   ILE A 199      992   1227    751     75   -118    -24       C  
ATOM   1526  O   ILE A 199      14.725   1.774 -15.875  1.00  7.39           O  
ANISOU 1526  O   ILE A 199      690   1273    842    164   -192     64       O  
ATOM   1527  CB  ILE A 199      14.381   0.419 -13.226  1.00  8.25           C  
ANISOU 1527  CB  ILE A 199     1009   1420    705    100   -255   -114       C  
ATOM   1528  CG1 ILE A 199      14.874  -0.087 -11.869  1.00  8.56           C  
ANISOU 1528  CG1 ILE A 199     1109   1374    770     46   -174    -15       C  
ATOM   1529  CG2 ILE A 199      13.014  -0.173 -13.518  1.00  9.46           C  
ANISOU 1529  CG2 ILE A 199     1197   1610    785   -144   -129    -63       C  
ATOM   1530  CD1 ILE A 199      14.065   0.392 -10.674  1.00  9.83           C  
ANISOU 1530  CD1 ILE A 199     1459   1529    747    -69   -151    -71       C  
ATOM   1531  N   PRO A 200      14.537  -0.308 -16.620  1.00  6.74           N  
ANISOU 1531  N   PRO A 200      861   1027    671    101    -89     38       N  
ATOM   1532  CA  PRO A 200      14.134   0.150 -17.944  1.00  8.29           C  
ANISOU 1532  CA  PRO A 200     1072   1290    786     73    -49     -2       C  
ATOM   1533  C   PRO A 200      12.975   1.144 -17.908  1.00  8.05           C  
ANISOU 1533  C   PRO A 200     1083   1205    770     20   -107     20       C  
ATOM   1534  O   PRO A 200      11.995   0.983 -17.197  1.00  7.28           O  
ANISOU 1534  O   PRO A 200     1058   1028    678     19   -220     55       O  
ATOM   1535  CB  PRO A 200      13.704  -1.173 -18.622  1.00  9.44           C  
ANISOU 1535  CB  PRO A 200     1236   1503    849    115   -183    -99       C  
ATOM   1536  CG  PRO A 200      14.520  -2.232 -17.991  1.00  9.03           C  
ANISOU 1536  CG  PRO A 200     1148   1510    771    253    -65   -176       C  
ATOM   1537  CD  PRO A 200      14.693  -1.778 -16.566  1.00  7.69           C  
ANISOU 1537  CD  PRO A 200      969   1241    710    105   -192   -137       C  
ATOM   1538  N   GLU A 201      13.077   2.176 -18.754  1.00  8.09           N  
ANISOU 1538  N   GLU A 201      783   1333    956     50    -23    164       N  
ATOM   1539  CA  GLU A 201      11.978   3.141 -18.954  1.00  8.13           C  
ANISOU 1539  CA  GLU A 201      971   1117    997     68   -144     44       C  
ATOM   1540  C   GLU A 201      10.682   2.459 -19.416  1.00  8.37           C  
ANISOU 1540  C   GLU A 201     1001   1221    956     52    -36    153       C  
ATOM   1541  O   GLU A 201       9.616   2.964 -19.172  1.00  8.90           O  
ANISOU 1541  O   GLU A 201      844   1490   1046    118    -40     14       O  
ATOM   1542  CB  GLU A 201      12.419   4.264 -19.913  1.00  9.85           C  
ANISOU 1542  CB  GLU A 201      995   1469   1276     57   -122    108       C  
ATOM   1543  CG  GLU A 201      13.519   5.151 -19.272  1.00 11.03           C  
ANISOU 1543  CG  GLU A 201     1184   1487   1520    -86   -108    274       C  
ATOM   1544  CD  GLU A 201      12.997   5.942 -18.098  1.00 14.86           C  
ANISOU 1544  CD  GLU A 201     1782   1906   1956    -47   -202    -48       C  
ATOM   1545  OE1 GLU A 201      11.820   6.258 -18.063  1.00 17.97           O  
ANISOU 1545  OE1 GLU A 201     2021   2709   2097    388   -291   -263       O  
ATOM   1546  OE2 GLU A 201      13.748   6.249 -17.146  1.00 23.35           O1-
ANISOU 1546  OE2 GLU A 201     2806   3354   2712   -210   -500   -521       O1-
ATOM   1547  N   ALA A 202      10.811   1.320 -20.081  1.00  7.31           N  
ANISOU 1547  N   ALA A 202      682   1466    627     60   -150    -19       N  
ATOM   1548  CA  ALA A 202       9.657   0.527 -20.512  1.00  8.04           C  
ANISOU 1548  CA  ALA A 202      932   1288    834    -63   -125     14       C  
ATOM   1549  C   ALA A 202       8.845  -0.004 -19.356  1.00  7.78           C  
ANISOU 1549  C   ALA A 202      892   1413    651    -12    -45    -12       C  
ATOM   1550  O   ALA A 202       7.701  -0.431 -19.560  1.00  9.50           O  
ANISOU 1550  O   ALA A 202     1149   1978    480   -228    -40     -3       O  
ATOM   1551  CB  ALA A 202      10.082  -0.612 -21.371  1.00  9.53           C  
ANISOU 1551  CB  ALA A 202     1106   1679    836     22    -93    -45       C  
ATOM   1552  N   PHE A 203       9.383  -0.001 -18.144  1.00  6.77           N  
ANISOU 1552  N   PHE A 203      915   1153    503    -93    -30    -85       N  
ATOM   1553  CA  PHE A 203       8.615  -0.494 -16.972  1.00  6.85           C  
ANISOU 1553  CA  PHE A 203      880   1024    699    -69    -55    -87       C  
ATOM   1554  C   PHE A 203       7.885   0.711 -16.406  1.00  7.00           C  
ANISOU 1554  C   PHE A 203      951   1044    665    -13    -98    -78       C  
ATOM   1555  O   PHE A 203       8.315   1.338 -15.441  1.00  6.60           O  
ANISOU 1555  O   PHE A 203      975    994    536    -33   -114    -71       O  
ATOM   1556  CB  PHE A 203       9.526  -1.114 -15.919  1.00  7.10           C  
ANISOU 1556  CB  PHE A 203      954   1058    682    -42     55    -44       C  
ATOM   1557  CG  PHE A 203      10.215  -2.426 -16.342  1.00  7.75           C  
ANISOU 1557  CG  PHE A 203      923   1227    792     67   -129    -97       C  
ATOM   1558  CD1 PHE A 203      10.044  -3.019 -17.580  1.00 10.42           C  
ANISOU 1558  CD1 PHE A 203     1802   1356    799    360     -3     74       C  
ATOM   1559  CD2 PHE A 203      11.049  -3.033 -15.466  1.00 10.45           C  
ANISOU 1559  CD2 PHE A 203     1321   1329   1316    149   -201    -90       C  
ATOM   1560  CE1 PHE A 203      10.725  -4.192 -17.907  1.00 11.14           C  
ANISOU 1560  CE1 PHE A 203     1868   1450    914    182    -67    -81       C  
ATOM   1561  CE2 PHE A 203      11.711  -4.185 -15.798  1.00 10.28           C  
ANISOU 1561  CE2 PHE A 203     1117   1513   1274    254   -200      3       C  
ATOM   1562  CZ  PHE A 203      11.575  -4.747 -16.987  1.00 10.55           C  
ANISOU 1562  CZ  PHE A 203     1225   1472   1309    160    164     13       C  
ATOM   1563  N   ARG A 204       6.751   1.055 -17.030  1.00  7.11           N  
ANISOU 1563  N   ARG A 204      887   1138    674     57   -134   -176       N  
ATOM   1564  CA  ARG A 204       6.023   2.247 -16.652  1.00  7.88           C  
ANISOU 1564  CA  ARG A 204     1018   1147    827    131   -136     42       C  
ATOM   1565  C   ARG A 204       5.447   2.179 -15.277  1.00  7.34           C  
ANISOU 1565  C   ARG A 204      858   1083    846     31    -76     -1       C  
ATOM   1566  O   ARG A 204       5.391   3.200 -14.584  1.00  7.96           O  
ANISOU 1566  O   ARG A 204     1073   1307    644     70   -156    -88       O  
ATOM   1567  CB  ARG A 204       4.876   2.548 -17.637  1.00  8.43           C  
ANISOU 1567  CB  ARG A 204     1061   1232    909    107   -141     90       C  
ATOM   1568  CG  ARG A 204       5.287   2.665 -19.057  1.00  9.98           C  
ANISOU 1568  CG  ARG A 204     1274   1480   1036    217    -56     25       C  
ATOM   1569  CD  ARG A 204       6.321   3.660 -19.320  1.00  9.62           C  
ANISOU 1569  CD  ARG A 204     1403   1338    912    175     20     33       C  
ATOM   1570  NE  ARG A 204       6.076   4.929 -18.679  1.00  8.80           N  
ANISOU 1570  NE  ARG A 204     1320   1393    629     88   -227     99       N  
ATOM   1571  CZ  ARG A 204       6.906   5.630 -17.990  1.00 13.26           C  
ANISOU 1571  CZ  ARG A 204     1963   1698   1376   -129     15     79       C  
ATOM   1572  NH1 ARG A 204       8.205   5.294 -17.888  1.00 14.22           N1+
ANISOU 1572  NH1 ARG A 204     2065   1810   1525   -138     -5    -44       N1+
ATOM   1573  NH2 ARG A 204       6.403   6.697 -17.380  1.00 12.84           N  
ANISOU 1573  NH2 ARG A 204     1700   1314   1862   -104     16    101       N  
ATOM   1574  N   GLY A 205       4.959   1.021 -14.868  1.00  6.57           N  
ANISOU 1574  N   GLY A 205      818   1073    603     44   -176    -39       N  
ATOM   1575  CA  GLY A 205       4.411   0.884 -13.528  1.00  7.54           C  
ANISOU 1575  CA  GLY A 205     1009   1114    740     59    -87    -37       C  
ATOM   1576  C   GLY A 205       5.453   1.188 -12.461  1.00  6.84           C  
ANISOU 1576  C   GLY A 205      952    968    678    -40    -92    -14       C  
ATOM   1577  O   GLY A 205       5.180   1.940 -11.545  1.00  6.81           O  
ANISOU 1577  O   GLY A 205     1143    911    534    -71    -83   -100       O  
ATOM   1578  N   VAL A 206       6.636   0.627 -12.622  1.00  6.87           N  
ANISOU 1578  N   VAL A 206      916   1130    560     64    -62    -91       N  
ATOM   1579  CA  VAL A 206       7.706   0.839 -11.649  1.00  6.63           C  
ANISOU 1579  CA  VAL A 206      964   1020    534    -64     -4    -83       C  
ATOM   1580  C   VAL A 206       8.135   2.303 -11.638  1.00  6.86           C  
ANISOU 1580  C   VAL A 206      969   1067    570   -108    -10    -31       C  
ATOM   1581  O   VAL A 206       8.262   2.903 -10.562  1.00  7.22           O  
ANISOU 1581  O   VAL A 206     1250   1109    382    132   -192   -104       O  
ATOM   1582  CB  VAL A 206       8.897  -0.086 -11.904  1.00  6.61           C  
ANISOU 1582  CB  VAL A 206     1053   1121    336     45    -76   -103       C  
ATOM   1583  CG1 VAL A 206      10.022   0.187 -10.903  1.00  8.65           C  
ANISOU 1583  CG1 VAL A 206     1099   1394    792     45    -78    -69       C  
ATOM   1584  CG2 VAL A 206       8.500  -1.526 -11.794  1.00  7.55           C  
ANISOU 1584  CG2 VAL A 206      941   1169    756    174    -72    -70       C  
ATOM   1585  N   HIS A 207       8.291   2.912 -12.804  1.00  6.64           N  
ANISOU 1585  N   HIS A 207     1055    922    545    -18    -60   -147       N  
ATOM   1586  CA  HIS A 207       8.681   4.302 -12.837  1.00  6.85           C  
ANISOU 1586  CA  HIS A 207     1047    934    619     14    -24     -7       C  
ATOM   1587  C   HIS A 207       7.647   5.268 -12.300  1.00  7.14           C  
ANISOU 1587  C   HIS A 207     1025   1122    564    -80     76    -78       C  
ATOM   1588  O   HIS A 207       8.027   6.218 -11.576  1.00  7.83           O  
ANISOU 1588  O   HIS A 207     1343   1091    539     27    -16   -117       O  
ATOM   1589  CB  HIS A 207       9.137   4.699 -14.261  1.00  7.52           C  
ANISOU 1589  CB  HIS A 207     1139   1090    625    -46    -51     51       C  
ATOM   1590  CG  HIS A 207      10.544   4.242 -14.541  1.00  7.12           C  
ANISOU 1590  CG  HIS A 207     1095   1022    588   -117     65      0       C  
ATOM   1591  CD2 HIS A 207      11.028   3.198 -15.253  1.00  7.17           C  
ANISOU 1591  CD2 HIS A 207      997   1104    623    -28    -33   -119       C  
ATOM   1592  ND1 HIS A 207      11.638   4.881 -13.982  1.00 10.84           N  
ANISOU 1592  ND1 HIS A 207     1206   1305   1606   -193    -42   -359       N  
ATOM   1593  CE1 HIS A 207      12.741   4.269 -14.377  1.00 10.66           C  
ANISOU 1593  CE1 HIS A 207     1032   1364   1652    -72    -86   -195       C  
ATOM   1594  NE2 HIS A 207      12.401   3.239 -15.152  1.00  9.01           N  
ANISOU 1594  NE2 HIS A 207     1138   1081   1203   -102    -34    -87       N  
ATOM   1595  N   ARG A 208       6.385   5.042 -12.598  1.00  6.41           N  
ANISOU 1595  N   ARG A 208      956    942    536     82    -57   -121       N  
ATOM   1596  CA  ARG A 208       5.306   5.875 -12.047  1.00  6.36           C  
ANISOU 1596  CA  ARG A 208     1063    706    644     37     11    -36       C  
ATOM   1597  C   ARG A 208       5.289   5.748 -10.499  1.00  7.42           C  
ANISOU 1597  C   ARG A 208     1179   1014    624     52     63    -49       C  
ATOM   1598  O   ARG A 208       5.190   6.782  -9.777  1.00  8.03           O  
ANISOU 1598  O   ARG A 208     1417   1084    548    126     27   -128       O  
ATOM   1599  CB  ARG A 208       3.932   5.494 -12.580  1.00  6.87           C  
ANISOU 1599  CB  ARG A 208     1043    902    664    110     52    -41       C  
ATOM   1600  CG  ARG A 208       3.710   5.701 -14.065  1.00  6.85           C  
ANISOU 1600  CG  ARG A 208      954    966    682    -61   -100    114       C  
ATOM   1601  CD  ARG A 208       2.505   4.818 -14.557  1.00  7.86           C  
ANISOU 1601  CD  ARG A 208      977   1392    615    -96    -73    143       C  
ATOM   1602  NE  ARG A 208       2.359   4.905 -15.989  1.00  6.48           N  
ANISOU 1602  NE  ARG A 208     1129    921    410   -179   -134     39       N  
ATOM   1603  CZ  ARG A 208       1.743   3.996 -16.729  1.00  7.87           C  
ANISOU 1603  CZ  ARG A 208     1159   1254    578   -255     49      3       C  
ATOM   1604  NH1 ARG A 208       1.137   2.970 -16.131  1.00  7.66           N1+
ANISOU 1604  NH1 ARG A 208     1097    885    929   -188     84   -128       N1+
ATOM   1605  NH2 ARG A 208       1.708   4.145 -18.053  1.00  7.51           N  
ANISOU 1605  NH2 ARG A 208     1085   1076    689   -451   -147     75       N  
ATOM   1606  N   TYR A 209       5.429   4.512  -9.998  1.00  6.51           N  
ANISOU 1606  N   TYR A 209     1196    904    372     12    -12   -114       N  
ATOM   1607  CA  TYR A 209       5.450   4.282  -8.572  1.00  7.40           C  
ANISOU 1607  CA  TYR A 209     1111   1068    630     -4      1     19       C  
ATOM   1608  C   TYR A 209       6.587   5.044  -7.892  1.00  6.89           C  
ANISOU 1608  C   TYR A 209     1090    980    545      8     17    104       C  
ATOM   1609  O   TYR A 209       6.358   5.724  -6.876  1.00  7.31           O  
ANISOU 1609  O   TYR A 209     1329   1068    378    -75    -22   -204       O  
ATOM   1610  CB  TYR A 209       5.593   2.789  -8.372  1.00  7.21           C  
ANISOU 1610  CB  TYR A 209     1106   1017    615     75     11     -8       C  
ATOM   1611  CG  TYR A 209       5.676   2.260  -6.937  1.00  6.36           C  
ANISOU 1611  CG  TYR A 209      973    998    443    -65    -87    -86       C  
ATOM   1612  CD1 TYR A 209       4.826   2.717  -5.950  1.00  7.17           C  
ANISOU 1612  CD1 TYR A 209     1185    898    640      0     51     40       C  
ATOM   1613  CD2 TYR A 209       6.638   1.360  -6.578  1.00  6.60           C  
ANISOU 1613  CD2 TYR A 209      900   1197    409    -59     84      0       C  
ATOM   1614  CE1 TYR A 209       4.914   2.195  -4.656  1.00  7.23           C  
ANISOU 1614  CE1 TYR A 209     1101   1024    621     65    -22    -77       C  
ATOM   1615  CE2 TYR A 209       6.705   0.807  -5.344  1.00  7.17           C  
ANISOU 1615  CE2 TYR A 209     1053   1169    501     46   -147    -10       C  
ATOM   1616  CZ  TYR A 209       5.856   1.243  -4.363  1.00  5.92           C  
ANISOU 1616  CZ  TYR A 209      893   1009    345    -21   -108     13       C  
ATOM   1617  OH  TYR A 209       5.924   0.662  -3.114  1.00  7.17           O  
ANISOU 1617  OH  TYR A 209     1014   1268    440   -121   -178     46       O  
ATOM   1618  N   LEU A 210       7.805   4.909  -8.413  1.00  7.44           N  
ANISOU 1618  N   LEU A 210     1172    983    670    -28     -6     -9       N  
ATOM   1619  CA  LEU A 210       8.929   5.579  -7.818  1.00  7.12           C  
ANISOU 1619  CA  LEU A 210     1019   1142    542    -10    -64     76       C  
ATOM   1620  C   LEU A 210       8.810   7.095  -7.900  1.00  8.11           C  
ANISOU 1620  C   LEU A 210     1213   1154    713    -30     35   -124       C  
ATOM   1621  O   LEU A 210       9.163   7.778  -6.951  1.00  8.01           O  
ANISOU 1621  O   LEU A 210     1548   1069    425    -99     -4   -155       O  
ATOM   1622  CB  LEU A 210      10.217   5.084  -8.464  1.00  8.29           C  
ANISOU 1622  CB  LEU A 210     1259   1263    628    -41   -137   -200       C  
ATOM   1623  CG  LEU A 210      10.592   3.629  -8.182  1.00  9.51           C  
ANISOU 1623  CG  LEU A 210     1243   1446    925    -56   -102    -16       C  
ATOM   1624  CD1 LEU A 210      11.769   3.219  -9.034  1.00 11.21           C  
ANISOU 1624  CD1 LEU A 210     1519   1443   1297    165    -51   -304       C  
ATOM   1625  CD2 LEU A 210      10.897   3.465  -6.682  1.00 11.62           C  
ANISOU 1625  CD2 LEU A 210     1547   1645   1223    239   -196    287       C  
ATOM   1626  N   SER A 211       8.295   7.635  -9.013  1.00  7.64           N  
ANISOU 1626  N   SER A 211     1221    994    684    -28     70    -53       N  
ATOM   1627  CA  SER A 211       8.052   9.073  -9.130  1.00  9.10           C  
ANISOU 1627  CA  SER A 211     1326   1189    940    -40     10    -32       C  
ATOM   1628  C   SER A 211       7.044   9.546  -8.056  1.00  7.65           C  
ANISOU 1628  C   SER A 211     1128   1024    753     17    -42   -129       C  
ATOM   1629  O   SER A 211       7.233  10.568  -7.363  1.00  8.42           O  
ANISOU 1629  O   SER A 211     1478   1021    699   -124   -145   -135       O  
ATOM   1630  CB  SER A 211       7.561   9.366 -10.526  1.00 10.83           C  
ANISOU 1630  CB  SER A 211     1530   1453   1131   -122     15     73       C  
ATOM   1631  OG ASER A 211       8.617   9.317 -11.464  0.50 11.93           O  
ANISOU 1631  OG ASER A 211     1847   1514   1169    -91     93     26       O  
ATOM   1632  OG BSER A 211       7.400  10.762 -10.754  0.50 13.89           O  
ANISOU 1632  OG BSER A 211     2127   1762   1387    -39    -13    -91       O  
ATOM   1633  N   ASN A 212       5.956   8.808  -7.894  1.00  7.20           N  
ANISOU 1633  N   ASN A 212     1114    952    667    -60      5    -18       N  
ATOM   1634  CA  ASN A 212       4.968   9.148  -6.904  1.00  8.24           C  
ANISOU 1634  CA  ASN A 212     1187   1080    864     39    -55    -89       C  
ATOM   1635  C   ASN A 212       5.533   9.086  -5.488  1.00  7.32           C  
ANISOU 1635  C   ASN A 212     1151   1003    625    -10    -36   -115       C  
ATOM   1636  O   ASN A 212       5.235   9.908  -4.611  1.00  8.56           O  
ANISOU 1636  O   ASN A 212     1508   1059    682    -35     94   -180       O  
ATOM   1637  CB  ASN A 212       3.753   8.250  -6.982  1.00  9.81           C  
ANISOU 1637  CB  ASN A 212     1409   1289   1029    -59    -54     57       C  
ATOM   1638  CG  ASN A 212       3.021   8.346  -8.313  1.00 11.75           C  
ANISOU 1638  CG  ASN A 212     1539   1609   1315    -68    -72    118       C  
ATOM   1639  ND2 ASN A 212       2.311   7.287  -8.659  1.00 12.26           N  
ANISOU 1639  ND2 ASN A 212     1305   2297   1053   -161   -162   -266       N  
ATOM   1640  OD1 ASN A 212       3.111   9.328  -9.009  1.00 15.25           O  
ANISOU 1640  OD1 ASN A 212     1674   2175   1943   -124   -404    460       O  
ATOM   1641  N   ALA A 213       6.382   8.090  -5.238  1.00  7.44           N  
ANISOU 1641  N   ALA A 213     1299    885    643     67    -45   -163       N  
ATOM   1642  CA  ALA A 213       7.005   7.947  -3.932  1.00  8.00           C  
ANISOU 1642  CA  ALA A 213     1195   1076    767    -26     10     -2       C  
ATOM   1643  C   ALA A 213       8.024   9.007  -3.621  1.00  7.93           C  
ANISOU 1643  C   ALA A 213      973   1311    728    -42    -23   -103       C  
ATOM   1644  O   ALA A 213       8.026   9.551  -2.486  1.00  7.86           O  
ANISOU 1644  O   ALA A 213     1429    969    586    -19    -53   -188       O  
ATOM   1645  CB  ALA A 213       7.629   6.619  -3.823  1.00  8.91           C  
ANISOU 1645  CB  ALA A 213     1493   1115    774    -82    -57      4       C  
ATOM   1646  N   TYR A 214       8.855   9.375  -4.601  1.00  8.88           N  
ANISOU 1646  N   TYR A 214     1324   1315    733   -169     -6    -30       N  
ATOM   1647  CA  TYR A 214       9.846  10.420  -4.371  1.00 10.58           C  
ANISOU 1647  CA  TYR A 214     1391   1607   1020   -155   -107    -98       C  
ATOM   1648  C   TYR A 214       9.167  11.760  -4.060  1.00 10.36           C  
ANISOU 1648  C   TYR A 214     1632   1399    904   -265     -9     21       C  
ATOM   1649  O   TYR A 214       9.784  12.612  -3.415  1.00 12.68           O  
ANISOU 1649  O   TYR A 214     2171   1499   1145   -397   -192    -78       O  
ATOM   1650  CB  TYR A 214      10.928  10.501  -5.511  1.00 11.89           C  
ANISOU 1650  CB  TYR A 214     1715   1730   1071   -307     24   -183       C  
ATOM   1651  CG  TYR A 214      11.919   9.282  -5.481  1.00 16.28           C  
ANISOU 1651  CG  TYR A 214     2060   2205   1919   -186   -103   -143       C  
ATOM   1652  CD1 TYR A 214      12.801   9.059  -4.422  1.00 21.34           C  
ANISOU 1652  CD1 TYR A 214     2660   2833   2613    105   -218    137       C  
ATOM   1653  CD2 TYR A 214      11.903   8.311  -6.462  1.00 18.52           C  
ANISOU 1653  CD2 TYR A 214     2231   2660   2144    -24     38   -270       C  
ATOM   1654  CE1 TYR A 214      13.660   7.911  -4.391  1.00 22.15           C  
ANISOU 1654  CE1 TYR A 214     2922   2868   2623    182   -117   -190       C  
ATOM   1655  CE2 TYR A 214      12.699   7.211  -6.443  1.00 17.56           C  
ANISOU 1655  CE2 TYR A 214     2427   2244   1999   -139   -353   -240       C  
ATOM   1656  CZ  TYR A 214      13.603   6.959  -5.416  1.00 18.32           C  
ANISOU 1656  CZ  TYR A 214     2303   2240   2415    265   -119    -83       C  
ATOM   1657  OH  TYR A 214      14.374   5.743  -5.471  1.00 18.54           O  
ANISOU 1657  OH  TYR A 214     2185   2716   2143    608     10    120       O  
ATOM   1658  N   ALA A 215       7.917  11.966  -4.477  1.00  9.58           N  
ANISOU 1658  N   ALA A 215     1735   1112    792    -70     25     13       N  
ATOM   1659  CA  ALA A 215       7.156  13.174  -4.194  1.00 10.57           C  
ANISOU 1659  CA  ALA A 215     1620   1269   1125     -9     60     24       C  
ATOM   1660  C   ALA A 215       6.550  13.196  -2.793  1.00 10.31           C  
ANISOU 1660  C   ALA A 215     1901   1135    881     45    -11    -69       C  
ATOM   1661  O   ALA A 215       5.907  14.199  -2.418  1.00 13.67           O  
ANISOU 1661  O   ALA A 215     2783   1445    966    436    143    -86       O  
ATOM   1662  CB  ALA A 215       6.030  13.374  -5.245  1.00 11.53           C  
ANISOU 1662  CB  ALA A 215     1901   1318   1161     41    -14    181       C  
ATOM   1663  N   ARG A 216       6.745  12.156  -2.002  1.00  8.99           N  
ANISOU 1663  N   ARG A 216     1488   1010    915     21    -94   -109       N  
ATOM   1664  CA  ARG A 216       6.268  12.103  -0.641  1.00  9.02           C  
ANISOU 1664  CA  ARG A 216     1277   1265    885      1    -91     -4       C  
ATOM   1665  C   ARG A 216       7.466  12.203   0.304  1.00  7.91           C  
ANISOU 1665  C   ARG A 216     1062   1124    819    -13      0      4       C  
ATOM   1666  O   ARG A 216       8.404  11.396   0.218  1.00  8.00           O  
ANISOU 1666  O   ARG A 216     1179   1329    531    -10     -2     33       O  
ATOM   1667  CB  ARG A 216       5.531  10.783  -0.372  1.00  9.08           C  
ANISOU 1667  CB  ARG A 216     1346   1290    813     -3   -128    -30       C  
ATOM   1668  CG  ARG A 216       4.079  10.773  -0.986  1.00 10.66           C  
ANISOU 1668  CG  ARG A 216     1612   1695    743    -64   -229     64       C  
ATOM   1669  CD  ARG A 216       3.147  11.750  -0.323  1.00 11.44           C  
ANISOU 1669  CD  ARG A 216     1311   1886   1146     27    -85    324       C  
ATOM   1670  NE  ARG A 216       2.844  11.308   1.028  1.00 10.50           N  
ANISOU 1670  NE  ARG A 216     1425   1636    928    106     51    -21       N  
ATOM   1671  CZ  ARG A 216       1.853  10.503   1.332  1.00 11.15           C  
ANISOU 1671  CZ  ARG A 216     1216   1873   1148    -36    -76    -26       C  
ATOM   1672  NH1 ARG A 216       1.038  10.042   0.393  1.00 12.66           N1+
ANISOU 1672  NH1 ARG A 216     1474   1857   1479   -108    -51   -125       N1+
ATOM   1673  NH2 ARG A 216       1.667  10.177   2.585  1.00 12.28           N  
ANISOU 1673  NH2 ARG A 216     1495   1740   1429    104    -39    325       N  
ATOM   1674  N   GLU A 217       7.403  13.155   1.232  1.00  7.31           N  
ANISOU 1674  N   GLU A 217     1125    951    702   -164     27    107       N  
ATOM   1675  CA  GLU A 217       8.521  13.303   2.154  1.00  8.52           C  
ANISOU 1675  CA  GLU A 217     1190   1086    959   -152    -17    104       C  
ATOM   1676  C   GLU A 217       8.792  12.120   3.066  1.00  8.28           C  
ANISOU 1676  C   GLU A 217     1153   1166    823     51    -73     -1       C  
ATOM   1677  O   GLU A 217       9.923  11.875   3.454  1.00  8.26           O  
ANISOU 1677  O   GLU A 217     1243   1116    778   -117   -123     -2       O  
ATOM   1678  CB  GLU A 217       8.365  14.552   3.008  1.00 10.02           C  
ANISOU 1678  CB  GLU A 217     1465   1191   1149   -191    -82    105       C  
ATOM   1679  CG  GLU A 217       8.585  15.816   2.186  1.00 15.37           C  
ANISOU 1679  CG  GLU A 217     2158   1787   1893    -36   -112    108       C  
ATOM   1680  CD  GLU A 217      10.015  15.981   1.641  1.00 20.59           C  
ANISOU 1680  CD  GLU A 217     2675   2524   2625     52    110    109       C  
ATOM   1681  OE1 GLU A 217      10.414  15.356   0.621  1.00 25.10           O  
ANISOU 1681  OE1 GLU A 217     3611   2964   2963   -102    280    -47       O  
ATOM   1682  OE2 GLU A 217      10.786  16.708   2.230  1.00 21.56           O1-
ANISOU 1682  OE2 GLU A 217     2584   3085   2523   -138    -95    -65       O1-
ATOM   1683  N   GLU A 218       7.759  11.369   3.357  1.00  6.39           N  
ANISOU 1683  N   GLU A 218      887    939    600     62    -89     13       N  
ATOM   1684  CA  GLU A 218       7.902  10.202   4.206  1.00  6.87           C  
ANISOU 1684  CA  GLU A 218      970    994    645     16    -33     13       C  
ATOM   1685  C   GLU A 218       8.936   9.239   3.637  1.00  7.48           C  
ANISOU 1685  C   GLU A 218     1068   1063    709     34     74     38       C  
ATOM   1686  O   GLU A 218       9.641   8.546   4.375  1.00  7.62           O  
ANISOU 1686  O   GLU A 218     1067   1177    649   -110     31    -33       O  
ATOM   1687  CB  GLU A 218       6.560   9.526   4.440  1.00  7.22           C  
ANISOU 1687  CB  GLU A 218     1055    944    743    -45      0      7       C  
ATOM   1688  CG  GLU A 218       5.524  10.408   5.117  1.00  8.52           C  
ANISOU 1688  CG  GLU A 218     1039   1199    999     15     15    -30       C  
ATOM   1689  CD  GLU A 218       4.595  11.115   4.136  1.00  9.14           C  
ANISOU 1689  CD  GLU A 218     1445   1068    958     -5      2    103       C  
ATOM   1690  OE1 GLU A 218       5.018  11.420   2.996  1.00  8.88           O  
ANISOU 1690  OE1 GLU A 218     1131   1327    916    204   -208     79       O  
ATOM   1691  OE2 GLU A 218       3.420  11.372   4.539  1.00 11.12           O1-
ANISOU 1691  OE2 GLU A 218     1400   1553   1272    225    -25    135       O1-
ATOM   1692  N   PHE A 219       8.965   9.130   2.304  1.00  6.87           N  
ANISOU 1692  N   PHE A 219      950   1019    641    119    -37     -8       N  
ATOM   1693  CA  PHE A 219       9.971   8.310   1.592  1.00  6.93           C  
ANISOU 1693  CA  PHE A 219      892   1010    729     36    -52     26       C  
ATOM   1694  C   PHE A 219      11.245   9.113   1.335  1.00  8.34           C  
ANISOU 1694  C   PHE A 219     1158   1114    897     32     31    -32       C  
ATOM   1695  O   PHE A 219      12.343   8.712   1.717  1.00  7.35           O  
ANISOU 1695  O   PHE A 219      925   1177    690    -52    115     64       O  
ATOM   1696  CB  PHE A 219       9.417   7.744   0.296  1.00  7.95           C  
ANISOU 1696  CB  PHE A 219     1026   1049    944     83    -58    110       C  
ATOM   1697  CG  PHE A 219      10.430   7.047  -0.529  1.00  8.31           C  
ANISOU 1697  CG  PHE A 219      783   1403    970   -158    -34     32       C  
ATOM   1698  CD1 PHE A 219      11.164   5.975  -0.062  1.00  8.57           C  
ANISOU 1698  CD1 PHE A 219     1083   1154   1019    -45    145    -40       C  
ATOM   1699  CD2 PHE A 219      10.650   7.469  -1.784  1.00 12.35           C  
ANISOU 1699  CD2 PHE A 219     1620   1841   1228    588    -29    125       C  
ATOM   1700  CE1 PHE A 219      12.100   5.354  -0.868  1.00  9.32           C  
ANISOU 1700  CE1 PHE A 219     1212   1200   1127    -63     69    -76       C  
ATOM   1701  CE2 PHE A 219      11.569   6.826  -2.605  1.00 14.44           C  
ANISOU 1701  CE2 PHE A 219     1842   2656    989    637     97    191       C  
ATOM   1702  CZ  PHE A 219      12.276   5.776  -2.143  1.00 11.85           C  
ANISOU 1702  CZ  PHE A 219     1414   1866   1220    358    -98    -75       C  
ATOM   1703  N   ALA A 220      11.103  10.246   0.649  1.00  8.10           N  
ANISOU 1703  N   ALA A 220     1077   1089    910   -111     35     -4       N  
ATOM   1704  CA  ALA A 220      12.307  10.947   0.173  1.00  9.20           C  
ANISOU 1704  CA  ALA A 220     1200   1292   1003   -165     24    109       C  
ATOM   1705  C   ALA A 220      13.199  11.369   1.324  1.00  8.05           C  
ANISOU 1705  C   ALA A 220     1036   1169    853   -113     -9    186       C  
ATOM   1706  O   ALA A 220      14.428  11.241   1.232  1.00  9.78           O  
ANISOU 1706  O   ALA A 220     1179   1669    868   -102    108     88       O  
ATOM   1707  CB  ALA A 220      11.923  12.168  -0.710  1.00 10.45           C  
ANISOU 1707  CB  ALA A 220     1364   1332   1273   -228     50    117       C  
ATOM   1708  N   SER A 221      12.587  11.872   2.410  1.00  7.46           N  
ANISOU 1708  N   SER A 221      842   1015    978   -111   -127    224       N  
ATOM   1709  CA  SER A 221      13.313  12.444   3.540  1.00  7.51           C  
ANISOU 1709  CA  SER A 221      953   1001    899   -112    -96    145       C  
ATOM   1710  C   SER A 221      13.907  11.386   4.422  1.00  8.23           C  
ANISOU 1710  C   SER A 221     1212    919    993    -71   -176     49       C  
ATOM   1711  O   SER A 221      14.797  11.716   5.227  1.00 10.48           O  
ANISOU 1711  O   SER A 221     1569   1199   1214    -85   -437    144       O  
ATOM   1712  CB  SER A 221      12.414  13.335   4.368  1.00  9.25           C  
ANISOU 1712  CB  SER A 221     1289   1225    999   -132   -160    104       C  
ATOM   1713  OG  SER A 221      13.115  14.215   5.170  1.00 15.46           O  
ANISOU 1713  OG  SER A 221     2135   2078   1660      4   -164   -313       O  
ATOM   1714  N   THR A 222      13.475  10.137   4.307  1.00  6.79           N  
ANISOU 1714  N   THR A 222      991    766    822   -103    -13     16       N  
ATOM   1715  CA  THR A 222      14.031   9.039   5.104  1.00  6.64           C  
ANISOU 1715  CA  THR A 222      789    936    798    -33     70      7       C  
ATOM   1716  C   THR A 222      15.073   8.200   4.357  1.00  7.69           C  
ANISOU 1716  C   THR A 222     1048    943    929     -5    132     62       C  
ATOM   1717  O   THR A 222      15.573   7.197   4.898  1.00  8.13           O  
ANISOU 1717  O   THR A 222     1039    789   1260   -118    231    145       O  
ATOM   1718  CB  THR A 222      12.940   8.140   5.682  1.00  7.03           C  
ANISOU 1718  CB  THR A 222      983    970    716    -67    129     25       C  
ATOM   1719  CG2 THR A 222      11.962   8.939   6.540  1.00  6.71           C  
ANISOU 1719  CG2 THR A 222      916   1042    591   -221    -44     34       C  
ATOM   1720  OG1 THR A 222      12.218   7.496   4.612  1.00  7.40           O  
ANISOU 1720  OG1 THR A 222     1186    945    680   -144    141     25       O  
ATOM   1721  N   CYS A 223      15.388   8.582   3.120  1.00  8.02           N  
ANISOU 1721  N   CYS A 223     1116    892   1037    -30     59    -37       N  
ATOM   1722  CA  CYS A 223      16.449   7.918   2.374  1.00  8.53           C  
ANISOU 1722  CA  CYS A 223     1035   1085   1118     35     52      2       C  
ATOM   1723  C   CYS A 223      17.811   8.406   2.827  1.00  8.74           C  
ANISOU 1723  C   CYS A 223     1125   1120   1075    -19    150    -66       C  
ATOM   1724  O   CYS A 223      17.993   9.605   2.872  1.00 10.26           O  
ANISOU 1724  O   CYS A 223     1303    967   1626    -66    128   -171       O  
ATOM   1725  CB  CYS A 223      16.349   8.227   0.860  1.00  9.92           C  
ANISOU 1725  CB  CYS A 223     1341   1297   1130    -52    121    106       C  
ATOM   1726  SG  CYS A 223      14.991   7.489  -0.062  1.00  9.86           S  
ANISOU 1726  SG  CYS A 223     1359   1429    957   -131    311    -79       S  
ATOM   1727  N   PRO A 224      18.755   7.553   3.136  1.00  8.12           N  
ANISOU 1727  N   PRO A 224     1094    964   1026   -101    226    -66       N  
ATOM   1728  CA  PRO A 224      20.139   8.027   3.266  1.00  8.32           C  
ANISOU 1728  CA  PRO A 224     1214   1069    878    -37    -31   -194       C  
ATOM   1729  C   PRO A 224      20.637   8.606   1.956  1.00  8.67           C  
ANISOU 1729  C   PRO A 224     1127   1121   1044     13     37    -43       C  
ATOM   1730  O   PRO A 224      20.116   8.230   0.920  1.00  9.03           O  
ANISOU 1730  O   PRO A 224     1196   1208   1027    -15    126     38       O  
ATOM   1731  CB  PRO A 224      20.928   6.762   3.625  1.00  9.47           C  
ANISOU 1731  CB  PRO A 224     1104   1495    997     98     -7    -41       C  
ATOM   1732  CG  PRO A 224      19.921   5.802   4.011  1.00 11.52           C  
ANISOU 1732  CG  PRO A 224     1565   1417   1392     67     16      8       C  
ATOM   1733  CD  PRO A 224      18.639   6.101   3.308  1.00  9.46           C  
ANISOU 1733  CD  PRO A 224     1371   1167   1054   -201    149     42       C  
ATOM   1734  N   ASP A 225      21.605   9.516   2.007  1.00  8.50           N  
ANISOU 1734  N   ASP A 225     1165   1143    921     -6    -51    -73       N  
ATOM   1735  CA  ASP A 225      22.139  10.131   0.781  1.00  9.07           C  
ANISOU 1735  CA  ASP A 225     1213   1093   1139     26     12    -57       C  
ATOM   1736  C   ASP A 225      22.833   9.061  -0.078  1.00  9.47           C  
ANISOU 1736  C   ASP A 225     1336   1258   1001     52     78    -45       C  
ATOM   1737  O   ASP A 225      23.233   7.997   0.416  1.00  7.89           O  
ANISOU 1737  O   ASP A 225      992   1174    831    -78     -3   -263       O  
ATOM   1738  CB  ASP A 225      23.003  11.351   1.098  1.00  9.79           C  
ANISOU 1738  CB  ASP A 225     1394   1157   1168     15     50   -112       C  
ATOM   1739  CG  ASP A 225      24.241  11.004   1.848  1.00 12.03           C  
ANISOU 1739  CG  ASP A 225     1576   1347   1648     62   -184   -264       C  
ATOM   1740  OD1 ASP A 225      25.112  10.355   1.332  1.00 13.20           O  
ANISOU 1740  OD1 ASP A 225     1703   1615   1698     20    -19   -251       O  
ATOM   1741  OD2 ASP A 225      24.532  11.477   2.973  1.00 17.92           O1-
ANISOU 1741  OD2 ASP A 225     2380   2859   1568    278   -254   -203       O1-
ATOM   1742  N   ASP A 226      22.939   9.363  -1.361  1.00  8.76           N  
ANISOU 1742  N   ASP A 226     1323   1063    940    -24    -30   -188       N  
ATOM   1743  CA  ASP A 226      23.461   8.387  -2.312  1.00  9.22           C  
ANISOU 1743  CA  ASP A 226     1462    979   1062     82     76    -35       C  
ATOM   1744  C   ASP A 226      24.876   7.928  -1.910  1.00  9.43           C  
ANISOU 1744  C   ASP A 226     1279   1156   1147    -74     61   -105       C  
ATOM   1745  O   ASP A 226      25.185   6.714  -2.008  1.00  9.76           O  
ANISOU 1745  O   ASP A 226     1355   1126   1224      5    283   -175       O  
ATOM   1746  CB  ASP A 226      23.530   8.968  -3.717  1.00 10.21           C  
ANISOU 1746  CB  ASP A 226     1602   1192   1085     65    231   -125       C  
ATOM   1747  CG  ASP A 226      22.221   9.071  -4.423  1.00 12.05           C  
ANISOU 1747  CG  ASP A 226     1925   1281   1371     20     63    -74       C  
ATOM   1748  OD1 ASP A 226      21.118   8.797  -3.860  1.00 11.89           O  
ANISOU 1748  OD1 ASP A 226     1815   1328   1373     74     -5    -10       O  
ATOM   1749  OD2 ASP A 226      22.254   9.434  -5.641  1.00 13.59           O1-
ANISOU 1749  OD2 ASP A 226     1834   2095   1235     50    -51     79       O1-
ATOM   1750  N   GLU A 227      25.741   8.856  -1.473  1.00  9.96           N  
ANISOU 1750  N   GLU A 227     1330   1279   1175    -69     24    -85       N  
ATOM   1751  CA  GLU A 227      27.096   8.472  -1.169  1.00 11.22           C  
ANISOU 1751  CA  GLU A 227     1502   1397   1364     57     22    -85       C  
ATOM   1752  C   GLU A 227      27.166   7.472  -0.007  1.00  9.61           C  
ANISOU 1752  C   GLU A 227     1258   1315   1076      0    -33   -214       C  
ATOM   1753  O   GLU A 227      27.980   6.538   0.011  1.00 10.63           O  
ANISOU 1753  O   GLU A 227     1445   1436   1155     57    236   -296       O  
ATOM   1754  CB  GLU A 227      27.935   9.732  -0.957  1.00 14.14           C  
ANISOU 1754  CB  GLU A 227     1843   1720   1809    -27    -46    109       C  
ATOM   1755  CG  GLU A 227      28.233  10.471  -2.273  1.00 19.81           C  
ANISOU 1755  CG  GLU A 227     2719   2632   2175    -10    147     66       C  
ATOM   1756  CD  GLU A 227      29.563  11.210  -2.279  1.00 27.79           C  
ANISOU 1756  CD  GLU A 227     3415   3515   3626   -237     48     22       C  
ATOM   1757  OE1 GLU A 227      30.147  11.501  -1.194  1.00 32.06           O  
ANISOU 1757  OE1 GLU A 227     4219   4075   3883   -175    -70    -40       O  
ATOM   1758  OE2 GLU A 227      30.038  11.486  -3.403  1.00 33.13           O1-
ANISOU 1758  OE2 GLU A 227     4325   4390   3869    -92    217     84       O1-
ATOM   1759  N   GLU A 228      26.301   7.632   0.980  1.00  9.43           N  
ANISOU 1759  N   GLU A 228     1198   1237   1146    -79     78   -171       N  
ATOM   1760  CA  GLU A 228      26.280   6.738   2.107  1.00  9.29           C  
ANISOU 1760  CA  GLU A 228     1225   1225   1081     77     36   -169       C  
ATOM   1761  C   GLU A 228      25.846   5.310   1.670  1.00 10.36           C  
ANISOU 1761  C   GLU A 228     1396   1372   1167     38     92   -119       C  
ATOM   1762  O   GLU A 228      26.382   4.305   2.101  1.00  8.98           O  
ANISOU 1762  O   GLU A 228     1435   1272    703      7      7   -340       O  
ATOM   1763  CB  GLU A 228      25.360   7.330   3.180  1.00 10.37           C  
ANISOU 1763  CB  GLU A 228     1369   1337   1232      3     38   -120       C  
ATOM   1764  CG  GLU A 228      25.431   6.515   4.406  1.00 11.37           C  
ANISOU 1764  CG  GLU A 228     1450   1539   1331    241    149     39       C  
ATOM   1765  CD  GLU A 228      26.752   6.672   5.143  1.00 14.04           C  
ANISOU 1765  CD  GLU A 228     1978   1807   1547     50    -29     10       C  
ATOM   1766  OE1 GLU A 228      27.533   7.656   4.926  1.00 13.24           O  
ANISOU 1766  OE1 GLU A 228     1998   1933   1098     39   -197    437       O  
ATOM   1767  OE2 GLU A 228      27.020   5.781   5.940  1.00 14.43           O1-
ANISOU 1767  OE2 GLU A 228     2146   1991   1344     38    -26    292       O1-
ATOM   1768  N   ILE A 229      24.840   5.231   0.817  1.00  8.06           N  
ANISOU 1768  N   ILE A 229     1284   1015    763     24     69   -101       N  
ATOM   1769  CA  ILE A 229      24.386   3.923   0.308  1.00  8.68           C  
ANISOU 1769  CA  ILE A 229     1190   1163    943    -66     39   -215       C  
ATOM   1770  C   ILE A 229      25.504   3.274  -0.474  1.00  8.83           C  
ANISOU 1770  C   ILE A 229     1339   1183    830    -59     78   -208       C  
ATOM   1771  O   ILE A 229      25.811   2.105  -0.307  1.00  8.84           O  
ANISOU 1771  O   ILE A 229     1458   1312    587     86    212   -257       O  
ATOM   1772  CB  ILE A 229      23.131   4.098  -0.574  1.00  8.39           C  
ANISOU 1772  CB  ILE A 229     1247   1025    913    -19     35   -245       C  
ATOM   1773  CG1 ILE A 229      21.996   4.641   0.288  1.00  9.52           C  
ANISOU 1773  CG1 ILE A 229     1297   1266   1053     20    172   -243       C  
ATOM   1774  CG2 ILE A 229      22.776   2.775  -1.270  1.00  9.88           C  
ANISOU 1774  CG2 ILE A 229     1495   1210   1049    -72     90   -312       C  
ATOM   1775  CD1 ILE A 229      20.744   4.997  -0.499  1.00 12.14           C  
ANISOU 1775  CD1 ILE A 229     1513   1703   1394    -31    177   -286       C  
ATOM   1776  N   GLU A 230      26.129   4.042  -1.364  1.00  8.47           N  
ANISOU 1776  N   GLU A 230     1173   1157    884     21    100   -239       N  
ATOM   1777  CA  GLU A 230      27.241   3.505  -2.158  1.00  8.77           C  
ANISOU 1777  CA  GLU A 230     1248   1167    916     47    110   -238       C  
ATOM   1778  C   GLU A 230      28.397   3.012  -1.291  1.00 10.34           C  
ANISOU 1778  C   GLU A 230     1366   1439   1122    100    156   -121       C  
ATOM   1779  O   GLU A 230      28.956   1.928  -1.528  1.00 10.07           O  
ANISOU 1779  O   GLU A 230     1544   1426    853    218     24   -151       O  
ATOM   1780  CB  GLU A 230      27.702   4.594  -3.120  1.00  9.70           C  
ANISOU 1780  CB  GLU A 230     1427   1140   1119     99    114   -149       C  
ATOM   1781  CG  GLU A 230      26.697   4.928  -4.205  1.00 10.01           C  
ANISOU 1781  CG  GLU A 230     1242   1415   1146    209    145      5       C  
ATOM   1782  CD  GLU A 230      26.985   6.216  -4.968  1.00  8.55           C  
ANISOU 1782  CD  GLU A 230     1318   1179    751    -42    173   -279       C  
ATOM   1783  OE1 GLU A 230      27.998   6.850  -4.683  1.00 13.89           O  
ANISOU 1783  OE1 GLU A 230     1661   2132   1483   -212    -10    -36       O  
ATOM   1784  OE2 GLU A 230      26.164   6.624  -5.822  1.00 11.99           O1-
ANISOU 1784  OE2 GLU A 230     1769   1837    949    -34     72     64       O1-
ATOM   1785  N   LEU A 231      28.748   3.774  -0.270  1.00  9.29           N  
ANISOU 1785  N   LEU A 231     1256   1319    954    225    128   -198       N  
ATOM   1786  CA  LEU A 231      29.833   3.449   0.629  1.00  9.80           C  
ANISOU 1786  CA  LEU A 231     1340   1341   1041    151     94   -176       C  
ATOM   1787  C   LEU A 231      29.519   2.133   1.349  1.00  9.28           C  
ANISOU 1787  C   LEU A 231     1358   1342    825     79    -69   -208       C  
ATOM   1788  O   LEU A 231      30.390   1.282   1.506  1.00 10.39           O  
ANISOU 1788  O   LEU A 231     1411   1458   1078    145    -46   -196       O  
ATOM   1789  CB  LEU A 231      30.069   4.626   1.613  1.00 11.22           C  
ANISOU 1789  CB  LEU A 231     1539   1497   1224    268     38   -234       C  
ATOM   1790  CG  LEU A 231      31.215   4.494   2.579  1.00 12.22           C  
ANISOU 1790  CG  LEU A 231     1558   1730   1352    158    141    -88       C  
ATOM   1791  CD1 LEU A 231      32.555   4.301   1.895  1.00 11.73           C  
ANISOU 1791  CD1 LEU A 231     1258   1755   1441    -88     81    -17       C  
ATOM   1792  CD2 LEU A 231      31.264   5.762   3.411  1.00 13.69           C  
ANISOU 1792  CD2 LEU A 231     1809   1823   1566   -119     84   -203       C  
ATOM   1793  N   ALA A 232      28.280   1.924   1.751  1.00  9.93           N  
ANISOU 1793  N   ALA A 232     1460   1370    941    113     53   -137       N  
ATOM   1794  CA  ALA A 232      27.885   0.692   2.430  1.00 11.10           C  
ANISOU 1794  CA  ALA A 232     1572   1448   1197     66    -20    -69       C  
ATOM   1795  C   ALA A 232      28.022  -0.540   1.531  1.00 11.77           C  
ANISOU 1795  C   ALA A 232     1762   1510   1199     30     19    -39       C  
ATOM   1796  O   ALA A 232      28.020  -1.680   2.045  1.00 13.45           O  
ANISOU 1796  O   ALA A 232     2294   1565   1249     31     39   -158       O  
ATOM   1797  CB  ALA A 232      26.448   0.806   2.910  1.00 11.78           C  
ANISOU 1797  CB  ALA A 232     1797   1503   1173     80     69    -43       C  
ATOM   1798  N   TYR A 233      28.099  -0.332   0.209  1.00 10.11           N  
ANISOU 1798  N   TYR A 233     1461   1396    985     39      0   -128       N  
ATOM   1799  CA  TYR A 233      28.277  -1.407  -0.755  1.00  9.35           C  
ANISOU 1799  CA  TYR A 233     1189   1297   1064    -21    -67   -173       C  
ATOM   1800  C   TYR A 233      29.710  -1.615  -1.254  1.00  9.59           C  
ANISOU 1800  C   TYR A 233     1291   1275   1075   -105     59   -259       C  
ATOM   1801  O   TYR A 233      29.972  -2.501  -2.044  1.00  9.09           O  
ANISOU 1801  O   TYR A 233     1350   1316    787    -96      8   -378       O  
ATOM   1802  CB  TYR A 233      27.285  -1.248  -1.905  1.00  9.80           C  
ANISOU 1802  CB  TYR A 233     1307   1495    921    -22   -114   -267       C  
ATOM   1803  CG  TYR A 233      25.939  -1.903  -1.545  1.00  8.24           C  
ANISOU 1803  CG  TYR A 233     1112   1310    708     46   -164    -53       C  
ATOM   1804  CD1 TYR A 233      25.628  -3.198  -1.986  1.00 10.23           C  
ANISOU 1804  CD1 TYR A 233     1311   1611    962      2   -141   -284       C  
ATOM   1805  CD2 TYR A 233      25.013  -1.268  -0.715  1.00  8.41           C  
ANISOU 1805  CD2 TYR A 233     1529    983    684     41    -58   -132       C  
ATOM   1806  CE1 TYR A 233      24.446  -3.817  -1.627  1.00  9.09           C  
ANISOU 1806  CE1 TYR A 233     1288   1388    777     17   -210   -354       C  
ATOM   1807  CE2 TYR A 233      23.859  -1.881  -0.312  1.00  9.26           C  
ANISOU 1807  CE2 TYR A 233     1403   1347    768    111   -114   -382       C  
ATOM   1808  CZ  TYR A 233      23.575  -3.163  -0.771  1.00  8.11           C  
ANISOU 1808  CZ  TYR A 233      956   1177    947     74   -164   -120       C  
ATOM   1809  OH  TYR A 233      22.459  -3.825  -0.389  1.00 10.11           O  
ANISOU 1809  OH  TYR A 233     1333   1337   1169    -38    -76   -105       O  
ATOM   1810  N   GLU A 234      30.671  -0.856  -0.727  1.00 10.03           N  
ANISOU 1810  N   GLU A 234     1219   1405   1187    -69    -24   -337       N  
ATOM   1811  CA  GLU A 234      32.052  -1.015  -1.186  1.00 10.90           C  
ANISOU 1811  CA  GLU A 234     1392   1499   1249   -121    -28   -116       C  
ATOM   1812  C   GLU A 234      32.646  -2.377  -0.851  1.00 10.47           C  
ANISOU 1812  C   GLU A 234     1396   1401   1179   -153    -43   -162       C  
ATOM   1813  O   GLU A 234      33.569  -2.787  -1.536  1.00 11.46           O  
ANISOU 1813  O   GLU A 234     1405   1595   1351   -187    144     -5       O  
ATOM   1814  CB  GLU A 234      32.959   0.096  -0.619  1.00 10.16           C  
ANISOU 1814  CB  GLU A 234     1520   1267   1069   -108    -91   -115       C  
ATOM   1815  CG  GLU A 234      32.707   1.487  -1.158  1.00 12.45           C  
ANISOU 1815  CG  GLU A 234     1578   1689   1462    -97   -139     64       C  
ATOM   1816  CD  GLU A 234      33.128   1.764  -2.599  1.00 14.09           C  
ANISOU 1816  CD  GLU A 234     2048   1759   1546    120     21   -154       C  
ATOM   1817  OE1 GLU A 234      33.756   0.893  -3.245  1.00 16.44           O  
ANISOU 1817  OE1 GLU A 234     2433   1958   1853     81    135   -237       O  
ATOM   1818  OE2 GLU A 234      32.740   2.893  -3.104  1.00 14.90           O1-
ANISOU 1818  OE2 GLU A 234     2045   1805   1811     51    -30     37       O1-
ATOM   1819  N   GLN A 235      32.168  -3.087   0.181  1.00 10.97           N  
ANISOU 1819  N   GLN A 235     1374   1535   1259   -220     60   -235       N  
ATOM   1820  CA  GLN A 235      32.600  -4.434   0.507  1.00 12.31           C  
ANISOU 1820  CA  GLN A 235     1486   1676   1514    -84      4    -18       C  
ATOM   1821  C   GLN A 235      31.526  -5.465   0.242  1.00 12.38           C  
ANISOU 1821  C   GLN A 235     1584   1606   1511    -30    -75     60       C  
ATOM   1822  O   GLN A 235      31.556  -6.583   0.768  1.00 13.36           O  
ANISOU 1822  O   GLN A 235     1742   1730   1602   -119   -207     61       O  
ATOM   1823  CB  GLN A 235      33.034  -4.578   1.947  1.00 14.94           C  
ANISOU 1823  CB  GLN A 235     1945   1881   1850   -127    -12     16       C  
ATOM   1824  CG  GLN A 235      34.252  -3.799   2.296  1.00 16.85           C  
ANISOU 1824  CG  GLN A 235     2010   2234   2155   -173    -29     77       C  
ATOM   1825  CD  GLN A 235      34.655  -4.022   3.743  1.00 16.89           C  
ANISOU 1825  CD  GLN A 235     1858   2376   2180   -285   -282    -43       C  
ATOM   1826  NE2 GLN A 235      34.157  -3.174   4.660  1.00 19.03           N  
ANISOU 1826  NE2 GLN A 235     2125   2639   2466    -10   -116     21       N  
ATOM   1827  OE1 GLN A 235      35.361  -4.975   4.029  1.00 23.46           O  
ANISOU 1827  OE1 GLN A 235     2887   2712   3313    -56   -202    128       O  
ATOM   1828  N   VAL A 236      30.587  -5.092  -0.622  1.00  9.73           N  
ANISOU 1828  N   VAL A 236     1249   1368   1079     73    -85    -36       N  
ATOM   1829  CA  VAL A 236      29.509  -5.990  -1.011  1.00  9.48           C  
ANISOU 1829  CA  VAL A 236     1363   1215   1024     27     52    -56       C  
ATOM   1830  C   VAL A 236      29.518  -6.140  -2.557  1.00  9.34           C  
ANISOU 1830  C   VAL A 236     1443   1163    940     33     12     19       C  
ATOM   1831  O   VAL A 236      29.572  -7.240  -3.091  1.00  9.40           O  
ANISOU 1831  O   VAL A 236     1378   1206    985     95    110     87       O  
ATOM   1832  CB  VAL A 236      28.129  -5.515  -0.508  1.00  8.50           C  
ANISOU 1832  CB  VAL A 236     1194   1196    837    -76      4     -7       C  
ATOM   1833  CG1 VAL A 236      27.058  -6.487  -0.936  1.00  8.52           C  
ANISOU 1833  CG1 VAL A 236     1348    924    966    -79     49    -11       C  
ATOM   1834  CG2 VAL A 236      28.111  -5.405   0.990  1.00 10.27           C  
ANISOU 1834  CG2 VAL A 236     1648   1208   1043    -16    151   -208       C  
ATOM   1835  N   ALA A 237      29.381  -5.023  -3.270  1.00  9.18           N  
ANISOU 1835  N   ALA A 237     1563   1156    766     98      2    -22       N  
ATOM   1836  CA  ALA A 237      29.460  -4.991  -4.734  1.00  7.85           C  
ANISOU 1836  CA  ALA A 237     1234   1034    712     -7    -53   -162       C  
ATOM   1837  C   ALA A 237      30.828  -5.416  -5.169  1.00  8.69           C  
ANISOU 1837  C   ALA A 237     1267   1147    885    -16    -36    -24       C  
ATOM   1838  O   ALA A 237      31.846  -5.038  -4.568  1.00 10.59           O  
ANISOU 1838  O   ALA A 237     1497   1674    851   -288    126   -399       O  
ATOM   1839  CB  ALA A 237      29.167  -3.581  -5.259  1.00  9.02           C  
ANISOU 1839  CB  ALA A 237     1412   1236    776     87    -90    -67       C  
ATOM   1840  N   LYS A 238      30.866  -6.160  -6.259  1.00  7.49           N  
ANISOU 1840  N   LYS A 238     1026   1150    668     81    -39     52       N  
ATOM   1841  CA  LYS A 238      32.128  -6.609  -6.833  1.00  8.12           C  
ANISOU 1841  CA  LYS A 238      994   1276    812     51    -29    -17       C  
ATOM   1842  C   LYS A 238      32.276  -6.070  -8.222  1.00  6.70           C  
ANISOU 1842  C   LYS A 238      951   1037    554     51    -57   -106       C  
ATOM   1843  O   LYS A 238      31.303  -5.979  -8.989  1.00  6.96           O  
ANISOU 1843  O   LYS A 238      946   1090    608     38    -70   -122       O  
ATOM   1844  CB  LYS A 238      32.186  -8.139  -6.883  1.00  8.96           C  
ANISOU 1844  CB  LYS A 238     1203   1438    761    158    -85    214       C  
ATOM   1845  CG  LYS A 238      31.977  -8.798  -5.525  1.00 12.20           C  
ANISOU 1845  CG  LYS A 238     1833   1565   1237    303    173    156       C  
ATOM   1846  CD  LYS A 238      33.180  -8.630  -4.716  1.00 13.59           C  
ANISOU 1846  CD  LYS A 238     2027   1615   1520    -80     94    120       C  
ATOM   1847  CE  LYS A 238      34.325  -9.546  -5.199  1.00 12.99           C  
ANISOU 1847  CE  LYS A 238     1844   1923   1165   -140    -68    262       C  
ATOM   1848  NZ  LYS A 238      35.426  -9.496  -4.181  1.00 12.02           N1+
ANISOU 1848  NZ  LYS A 238     1728   1375   1462     56   -263      5       N1+
ATOM   1849  N   ALA A 239      33.499  -5.726  -8.599  1.00  7.18           N  
ANISOU 1849  N   ALA A 239     1034   1188    503    -27    -57    -49       N  
ATOM   1850  CA  ALA A 239      33.799  -5.312  -9.952  1.00  6.90           C  
ANISOU 1850  CA  ALA A 239      981   1043    594      4    -73     57       C  
ATOM   1851  C   ALA A 239      33.848  -6.555 -10.863  1.00  7.66           C  
ANISOU 1851  C   ALA A 239     1052   1045    812     33    -65     29       C  
ATOM   1852  O   ALA A 239      34.286  -7.643 -10.467  1.00  9.01           O  
ANISOU 1852  O   ALA A 239     1531   1197    694    275   -208    -76       O  
ATOM   1853  CB  ALA A 239      35.119  -4.550 -10.006  1.00  8.86           C  
ANISOU 1853  CB  ALA A 239     1203   1344    817    -83     44     94       C  
ATOM   1854  N   LEU A 240      33.425  -6.390 -12.106  1.00  6.64           N  
ANISOU 1854  N   LEU A 240      964    963    594     65    -42   -101       N  
ATOM   1855  CA  LEU A 240      33.473  -7.476 -13.097  1.00  8.04           C  
ANISOU 1855  CA  LEU A 240     1132   1083    837     82    -64   -161       C  
ATOM   1856  C   LEU A 240      34.873  -7.661 -13.671  1.00  9.57           C  
ANISOU 1856  C   LEU A 240     1331   1392    910     51   -107   -132       C  
ATOM   1857  O   LEU A 240      35.374  -6.703 -14.273  1.00 12.61           O  
ANISOU 1857  O   LEU A 240     1261   2042   1485    -35      1   -151       O  
ATOM   1858  CB  LEU A 240      32.473  -7.203 -14.214  1.00  7.34           C  
ANISOU 1858  CB  LEU A 240     1151   1037    598    -16     22    -59       C  
ATOM   1859  CG  LEU A 240      31.023  -7.152 -13.783  1.00  7.12           C  
ANISOU 1859  CG  LEU A 240     1154    974    575    -36     42   -119       C  
ATOM   1860  CD1 LEU A 240      30.106  -6.901 -14.990  1.00  8.21           C  
ANISOU 1860  CD1 LEU A 240     1134   1276    708    -70   -105   -185       C  
ATOM   1861  CD2 LEU A 240      30.531  -8.373 -13.035  1.00  7.24           C  
ANISOU 1861  CD2 LEU A 240     1191    829    730     19    115   -114       C  
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.