CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 2408151235214107745

Job options:

ID        	=	 2408151235214107745
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 -1
CUTOFF    	=	 8
CAONLY    	=	 0


Input data for this run:


HETATM    1 ZN    ZN A   1       7.334   0.113 -17.364  1.00 15.27          ZN  
ANISOU    1 ZN    ZN A   1     2621   1464   1716     94    181    -10      ZN  
ATOM      2  N   VAL A  97      -7.159   8.004  -0.981  1.00 32.40           N  
ANISOU    2  N   VAL A  97     4001   4280   4029   -266    165     -5       N  
ATOM      3  CA  VAL A  97      -6.411   8.590  -2.131  1.00 29.58           C  
ANISOU    3  CA  VAL A  97     3470   3825   3942     34     58     47       C  
ATOM      4  C   VAL A  97      -6.234  10.099  -1.941  1.00 26.68           C  
ANISOU    4  C   VAL A  97     2692   3651   3794   -120     -3    170       C  
ATOM      5  O   VAL A  97      -7.147  10.779  -1.474  1.00 33.18           O  
ANISOU    5  O   VAL A  97     3969   4232   4404   -114    996   -161       O  
ATOM      6  CB  VAL A  97      -7.105   8.279  -3.495  1.00 30.59           C  
ANISOU    6  CB  VAL A  97     3796   3659   4166   -220    -33   -155       C  
ATOM      7  CG1 VAL A  97      -8.296   9.175  -3.724  1.00 32.02           C  
ANISOU    7  CG1 VAL A  97     3969   3968   4229     24    247   -469       C  
ATOM      8  CG2 VAL A  97      -6.134   8.439  -4.651  1.00 32.08           C  
ANISOU    8  CG2 VAL A  97     4254   4134   3798    -98    123     54       C  
ATOM      9  N   PRO A  98      -5.042  10.621  -2.274  1.00 27.34           N  
ANISOU    9  N   PRO A  98     3305   3786   3296   -229     -9    244       N  
ATOM     10  CA  PRO A  98      -4.811  12.061  -2.300  1.00 26.91           C  
ANISOU   10  CA  PRO A  98     3048   3491   3685   -471    245    141       C  
ATOM     11  C   PRO A  98      -5.779  12.793  -3.223  1.00 24.12           C  
ANISOU   11  C   PRO A  98     2914   2824   3423   -588    498      6       C  
ATOM     12  O   PRO A  98      -6.149  12.278  -4.285  1.00 25.02           O  
ANISOU   12  O   PRO A  98     2984   2510   4010   -468    252    206       O  
ATOM     13  CB  PRO A  98      -3.377  12.175  -2.832  1.00 30.22           C  
ANISOU   13  CB  PRO A  98     3401   4009   4071   -325    240    299       C  
ATOM     14  CG  PRO A  98      -3.081  10.856  -3.435  1.00 32.02           C  
ANISOU   14  CG  PRO A  98     3372   4729   4062   -269    150    -10       C  
ATOM     15  CD  PRO A  98      -3.820   9.880  -2.613  1.00 34.10           C  
ANISOU   15  CD  PRO A  98     4279   4327   4349     15    130    280       C  
ATOM     16  N   SER A  99      -6.186  13.990  -2.810  1.00 26.75           N  
ANISOU   16  N   SER A  99     3347   3039   3778   -895    668    180       N  
ATOM     17  CA  SER A  99      -7.106  14.802  -3.588  1.00 29.22           C  
ANISOU   17  CA  SER A  99     3662   3456   3981   -384    554    217       C  
ATOM     18  C   SER A  99      -6.422  15.369  -4.821  1.00 25.97           C  
ANISOU   18  C   SER A  99     2894   3050   3921   -329    362    207       C  
ATOM     19  O   SER A  99      -5.223  15.652  -4.805  1.00 27.51           O  
ANISOU   19  O   SER A  99     2895   3311   4244   -880    273    208       O  
ATOM     20  CB  SER A  99      -7.659  15.945  -2.740  1.00 31.88           C  
ANISOU   20  CB  SER A  99     3827   4008   4276    -25    233     48       C  
ATOM     21  OG  SER A  99      -8.576  16.729  -3.482  1.00 34.04           O  
ANISOU   21  OG  SER A  99     4934   3694   4301    324   -129    372       O  
ATOM     22  N   GLN A 100      -7.198  15.523  -5.886  1.00 27.64           N  
ANISOU   22  N   GLN A 100     2570   3472   4457    111    -41    123       N  
ATOM     23  CA  GLN A 100      -6.727  16.128  -7.121  1.00 28.04           C  
ANISOU   23  CA  GLN A 100     3247   2955   4452    261     -9    -53       C  
ATOM     24  C   GLN A 100      -7.287  17.538  -7.266  1.00 22.72           C  
ANISOU   24  C   GLN A 100     2429   2287   3914    618    234   -695       C  
ATOM     25  O   GLN A 100      -6.951  18.243  -8.220  1.00 27.70           O  
ANISOU   25  O   GLN A 100     3809   2969   3747    387     77   -262       O  
ATOM     26  CB  GLN A 100      -7.160  15.278  -8.320  1.00 29.70           C  
ANISOU   26  CB  GLN A 100     3373   3359   4549    -67   -224   -365       C  
ATOM     27  CG  GLN A 100      -8.656  15.362  -8.627  1.00 37.03           C  
ANISOU   27  CG  GLN A 100     3925   4873   5269     35   -286   -133       C  
ATOM     28  CD  GLN A 100      -9.045  14.614  -9.882  1.00 37.64           C  
ANISOU   28  CD  GLN A 100     4512   4799   4991     11   -115   -234       C  
ATOM     29  NE2 GLN A 100      -9.249  13.309  -9.751  1.00 41.93           N  
ANISOU   29  NE2 GLN A 100     5310   4935   5687    -41     44     -1       N  
ATOM     30  OE1 GLN A 100      -9.159  15.200 -10.959  1.00 44.11           O  
ANISOU   30  OE1 GLN A 100     5768   5365   5626   -170    108    162       O  
ATOM     31  N   LYS A 101      -8.140  17.938  -6.321  1.00 21.30           N  
ANISOU   31  N   LYS A 101     2302   2249   3539    152    121    184       N  
ATOM     32  CA  LYS A 101      -8.930  19.164  -6.451  1.00 19.30           C  
ANISOU   32  CA  LYS A 101     2289   2232   2812    331    173     60       C  
ATOM     33  C   LYS A 101      -8.062  20.404  -6.630  1.00 18.83           C  
ANISOU   33  C   LYS A 101     2625   2049   2477    123   -468   -180       C  
ATOM     34  O   LYS A 101      -7.217  20.707  -5.791  1.00 17.75           O  
ANISOU   34  O   LYS A 101     2188   2130   2426    160    268    169       O  
ATOM     35  CB  LYS A 101      -9.869  19.344  -5.249  1.00 22.25           C  
ANISOU   35  CB  LYS A 101     2771   2726   2955    117    379    -49       C  
ATOM     36  CG  LYS A 101     -10.830  20.528  -5.370  1.00 24.54           C  
ANISOU   36  CG  LYS A 101     2802   3039   3482    127    224    160       C  
ATOM     37  CD  LYS A 101     -12.022  20.214  -6.273  1.00 31.40           C  
ANISOU   37  CD  LYS A 101     3864   3997   4069    174   -467   -262       C  
ATOM     38  CE  LYS A 101     -13.105  19.451  -5.525  1.00 39.16           C  
ANISOU   38  CE  LYS A 101     5151   5140   4586    -18     97      8       C  
ATOM     39  N   THR A 102      -8.287  21.137  -7.714  1.00 16.90           N  
ANISOU   39  N   THR A 102     1644   2402   2373    170    180   -443       N  
ATOM     40  CA  THR A 102      -7.596  22.423  -7.897  1.00 15.49           C  
ANISOU   40  CA  THR A 102     1672   2266   1945     30    -68   -301       C  
ATOM     41  C   THR A 102      -7.831  23.337  -6.699  1.00 13.98           C  
ANISOU   41  C   THR A 102     1472   1870   1967     78    -86    149       C  
ATOM     42  O   THR A 102      -8.966  23.509  -6.257  1.00 14.55           O  
ANISOU   42  O   THR A 102     1422   2125   1980    155     27   -125       O  
ATOM     43  CB  THR A 102      -8.058  23.108  -9.177  1.00 19.45           C  
ANISOU   43  CB  THR A 102     2244   2993   2152    156    292    -29       C  
ATOM     44  CG2 THR A 102      -7.397  24.462  -9.348  1.00 19.29           C  
ANISOU   44  CG2 THR A 102     2115   3046   2167    279    -57    356       C  
ATOM     45  OG1 THR A 102      -7.724  22.268 -10.285  1.00 23.50           O  
ANISOU   45  OG1 THR A 102     3078   3907   1941    151    204   -599       O  
ATOM     46  N   TYR A 103      -6.742  23.888  -6.171  1.00 13.35           N  
ANISOU   46  N   TYR A 103     1424   1949   1699    229     42    -70       N  
ATOM     47  CA  TYR A 103      -6.781  24.803  -5.045  1.00 13.47           C  
ANISOU   47  CA  TYR A 103     1670   1869   1577    238     32   -107       C  
ATOM     48  C   TYR A 103      -5.727  25.858  -5.312  1.00 13.75           C  
ANISOU   48  C   TYR A 103     1962   1465   1794    189      4    -69       C  
ATOM     49  O   TYR A 103      -4.546  25.649  -5.053  1.00 13.41           O  
ANISOU   49  O   TYR A 103     1690   1595   1809    184     76    -35       O  
ATOM     50  CB  TYR A 103      -6.486  24.051  -3.749  1.00 14.27           C  
ANISOU   50  CB  TYR A 103     1742   1755   1921    120    167     -6       C  
ATOM     51  CG  TYR A 103      -6.510  24.873  -2.477  1.00 12.90           C  
ANISOU   51  CG  TYR A 103     1584   1729   1584    -72    194    103       C  
ATOM     52  CD1 TYR A 103      -7.650  25.589  -2.100  1.00 14.17           C  
ANISOU   52  CD1 TYR A 103     1763   1776   1843    122    321   -148       C  
ATOM     53  CD2 TYR A 103      -5.407  24.903  -1.622  1.00 15.96           C  
ANISOU   53  CD2 TYR A 103     1844   2565   1652   -192    243     31       C  
ATOM     54  CE1 TYR A 103      -7.687  26.316  -0.919  1.00 15.39           C  
ANISOU   54  CE1 TYR A 103     2162   1853   1830    -56    257     14       C  
ATOM     55  CE2 TYR A 103      -5.438  25.634  -0.427  1.00 15.29           C  
ANISOU   55  CE2 TYR A 103     2031   2234   1543   -214     87   -110       C  
ATOM     56  CZ  TYR A 103      -6.582  26.338  -0.087  1.00 14.39           C  
ANISOU   56  CZ  TYR A 103     1905   1697   1864     30    351     23       C  
ATOM     57  OH  TYR A 103      -6.642  27.057   1.092  1.00 15.97           O  
ANISOU   57  OH  TYR A 103     2100   2047   1918   -553    499   -201       O  
ATOM     58  N   GLN A 104      -6.145  26.994  -5.855  1.00 16.14           N  
ANISOU   58  N   GLN A 104     1984   1813   2333    252     20    481       N  
ATOM     59  CA  GLN A 104      -5.184  28.041  -6.178  1.00 16.71           C  
ANISOU   59  CA  GLN A 104     2152   1795   2401     43    102    497       C  
ATOM     60  C   GLN A 104      -4.565  28.623  -4.912  1.00 17.38           C  
ANISOU   60  C   GLN A 104     2282   1554   2766    119    250    145       C  
ATOM     61  O   GLN A 104      -3.399  29.018  -4.906  1.00 18.10           O  
ANISOU   61  O   GLN A 104     2540   1833   2504   -226    478     87       O  
ATOM     62  CB  GLN A 104      -5.815  29.124  -7.053  1.00 21.14           C  
ANISOU   62  CB  GLN A 104     2988   2158   2884      1   -316    605       C  
ATOM     63  CG  GLN A 104      -6.110  28.653  -8.469  1.00 26.07           C  
ANISOU   63  CG  GLN A 104     3867   3274   2764   -101    -29    734       C  
ATOM     64  N   GLY A 105      -5.349  28.654  -3.836  1.00 17.67           N  
ANISOU   64  N   GLY A 105     2392   1568   2753    326    353    -18       N  
ATOM     65  CA  GLY A 105      -4.851  29.074  -2.534  1.00 17.85           C  
ANISOU   65  CA  GLY A 105     2367   1665   2748    103    305   -137       C  
ATOM     66  C   GLY A 105      -4.541  30.555  -2.461  1.00 18.61           C  
ANISOU   66  C   GLY A 105     2500   1929   2640    204    305    -42       C  
ATOM     67  O   GLY A 105      -4.867  31.321  -3.377  1.00 21.17           O  
ANISOU   67  O   GLY A 105     3207   1992   2843     32     89     26       O  
ATOM     68  N   SER A 106      -3.879  30.945  -1.376  1.00 18.14           N  
ANISOU   68  N   SER A 106     2405   1866   2620     92    432   -105       N  
ATOM     69  CA ASER A 106      -3.610  32.349  -1.074  0.50 18.70           C  
ANISOU   69  CA ASER A 106     2584   1664   2854     65    261   -213       C  
ATOM     70  CA BSER A 106      -3.637  32.359  -1.098  0.50 20.00           C  
ANISOU   70  CA BSER A 106     2708   1921   2970     18    238   -197       C  
ATOM     71  C   SER A 106      -2.579  32.973  -2.011  1.00 20.15           C  
ANISOU   71  C   SER A 106     2604   2170   2882    150    310   -271       C  
ATOM     72  O   SER A 106      -2.522  34.194  -2.159  1.00 22.43           O  
ANISOU   72  O   SER A 106     3395   1866   3259     50    517   -395       O  
ATOM     73  CB ASER A 106      -3.149  32.487   0.377  0.50 20.09           C  
ANISOU   73  CB ASER A 106     2869   1911   2851    146    198    -60       C  
ATOM     74  CB BSER A 106      -3.271  32.568   0.373  0.50 24.28           C  
ANISOU   74  CB BSER A 106     3218   2933   3074    -22    155     -9       C  
ATOM     75  OG ASER A 106      -4.160  32.063   1.277  0.50 24.84           O  
ANISOU   75  OG ASER A 106     3491   2714   3230   -181    501     57       O  
ATOM     76  OG BSER A 106      -2.102  31.851   0.719  0.50 29.84           O  
ANISOU   76  OG BSER A 106     3730   3933   3674    352   -267    -69       O  
ATOM     77  N   TYR A 107      -1.761  32.128  -2.638  1.00 19.29           N  
ANISOU   77  N   TYR A 107     2526   1764   3037    -52    434    -81       N  
ATOM     78  CA  TYR A 107      -0.671  32.603  -3.489  1.00 18.12           C  
ANISOU   78  CA  TYR A 107     2319   1820   2743     -3    284     86       C  
ATOM     79  C   TYR A 107      -0.983  32.567  -4.986  1.00 18.73           C  
ANISOU   79  C   TYR A 107     2535   1829   2752    -74    179     43       C  
ATOM     80  O   TYR A 107      -0.119  32.884  -5.803  1.00 19.81           O  
ANISOU   80  O   TYR A 107     2664   2057   2805     40    586    156       O  
ATOM     81  CB  TYR A 107       0.635  31.868  -3.150  1.00 19.45           C  
ANISOU   81  CB  TYR A 107     2550   2161   2676     -7    205     26       C  
ATOM     82  CG  TYR A 107       0.984  31.998  -1.686  1.00 19.75           C  
ANISOU   82  CG  TYR A 107     2636   2129   2740    157    361   -183       C  
ATOM     83  CD1 TYR A 107       0.679  30.981  -0.781  1.00 22.93           C  
ANISOU   83  CD1 TYR A 107     2912   2974   2825    -88    169    254       C  
ATOM     84  CD2 TYR A 107       1.577  33.161  -1.194  1.00 23.91           C  
ANISOU   84  CD2 TYR A 107     3209   2656   3218   -260    213   -441       C  
ATOM     85  CE1 TYR A 107       0.974  31.115   0.572  1.00 24.06           C  
ANISOU   85  CE1 TYR A 107     3003   3122   3016     86    115    -43       C  
ATOM     86  CE2 TYR A 107       1.878  33.301   0.156  1.00 24.97           C  
ANISOU   86  CE2 TYR A 107     3681   2877   2929    -69    221   -120       C  
ATOM     87  CZ  TYR A 107       1.572  32.275   1.032  1.00 24.16           C  
ANISOU   87  CZ  TYR A 107     3253   3073   2852     20     50    143       C  
ATOM     88  OH  TYR A 107       1.867  32.407   2.370  1.00 27.91           O  
ANISOU   88  OH  TYR A 107     4142   3413   3049    160     89   -186       O  
ATOM     89  N   GLY A 108      -2.216  32.193  -5.336  1.00 18.03           N  
ANISOU   89  N   GLY A 108     2424   1673   2750    210    363   -231       N  
ATOM     90  CA  GLY A 108      -2.659  32.180  -6.732  1.00 18.81           C  
ANISOU   90  CA  GLY A 108     2783   1534   2827     63    405    -36       C  
ATOM     91  C   GLY A 108      -1.839  31.217  -7.571  1.00 17.81           C  
ANISOU   91  C   GLY A 108     2774   1538   2454     10    442    -33       C  
ATOM     92  O   GLY A 108      -1.335  31.570  -8.632  1.00 20.23           O  
ANISOU   92  O   GLY A 108     3141   1772   2771     78    518     77       O  
ATOM     93  N   PHE A 109      -1.707  29.993  -7.075  1.00 16.25           N  
ANISOU   93  N   PHE A 109     2279   1438   2455     -8    600   -256       N  
ATOM     94  CA  PHE A 109      -0.874  28.972  -7.685  1.00 15.80           C  
ANISOU   94  CA  PHE A 109     2090   1551   2361    -96    236   -210       C  
ATOM     95  C   PHE A 109      -1.544  28.343  -8.894  1.00 15.41           C  
ANISOU   95  C   PHE A 109     2062   1473   2320   -100    380    -44       C  
ATOM     96  O   PHE A 109      -2.677  27.855  -8.804  1.00 17.23           O  
ANISOU   96  O   PHE A 109     1852   1743   2950   -264    307     32       O  
ATOM     97  CB  PHE A 109      -0.542  27.903  -6.635  1.00 17.16           C  
ANISOU   97  CB  PHE A 109     2295   1595   2628    -12    418    183       C  
ATOM     98  CG  PHE A 109       0.220  26.717  -7.169  1.00 14.66           C  
ANISOU   98  CG  PHE A 109     2301   1211   2058    -46    260     20       C  
ATOM     99  CD1 PHE A 109       1.434  26.877  -7.822  1.00 21.25           C  
ANISOU   99  CD1 PHE A 109     2759   1867   3448      6    970    128       C  
ATOM    100  CD2 PHE A 109      -0.260  25.423  -6.972  1.00 14.19           C  
ANISOU  100  CD2 PHE A 109     2304   1418   1669   -172    -79     84       C  
ATOM    101  CE1 PHE A 109       2.138  25.774  -8.302  1.00 22.06           C  
ANISOU  101  CE1 PHE A 109     3038   1664   3678      0   1135    286       C  
ATOM    102  CE2 PHE A 109       0.445  24.311  -7.448  1.00 14.52           C  
ANISOU  102  CE2 PHE A 109     2040   1466   2011   -162      0    -91       C  
ATOM    103  CZ  PHE A 109       1.642  24.488  -8.115  1.00 16.64           C  
ANISOU  103  CZ  PHE A 109     2261   1663   2398   -103    468    -85       C  
ATOM    104  N  AARG A 110      -0.846  28.344 -10.019  0.50 17.21           N  
ANISOU  104  N  AARG A 110     2134   1913   2492   -193    112   -310       N  
ATOM    105  N  BARG A 110      -0.838  28.379 -10.027  0.50 14.00           N  
ANISOU  105  N  BARG A 110     1536   1386   2396   -225      7   -298       N  
ATOM    106  CA AARG A 110      -1.292  27.563 -11.162  0.50 19.75           C  
ANISOU  106  CA AARG A 110     2383   2335   2785    -99     94   -343       C  
ATOM    107  CA BARG A 110      -1.291  27.757 -11.281  0.50 13.92           C  
ANISOU  107  CA BARG A 110     1708   1466   2115    -66    233    218       C  
ATOM    108  C  AARG A 110      -0.113  27.009 -11.938  0.50 16.27           C  
ANISOU  108  C  AARG A 110     1994   1877   2309   -213     48     19       C  
ATOM    109  C  BARG A 110      -0.123  27.139 -12.056  0.50 13.74           C  
ANISOU  109  C  BARG A 110     1662   1374   2181   -107     93    143       C  
ATOM    110  O  AARG A 110       1.045  27.340 -11.664  0.50 12.81           O  
ANISOU  110  O  AARG A 110     1816   1241   1808   -311    156    144       O  
ATOM    111  O  BARG A 110       1.028  27.553 -11.886  0.50 14.49           O  
ANISOU  111  O  BARG A 110     1612   1550   2343   -134      9   -201       O  
ATOM    112  CB AARG A 110      -2.270  28.338 -12.061  0.50 24.12           C  
ANISOU  112  CB AARG A 110     2952   2985   3225    138    -68   -278       C  
ATOM    113  CB BARG A 110      -2.090  28.750 -12.147  0.50 18.85           C  
ANISOU  113  CB BARG A 110     2219   2191   2749    754    -84   -354       C  
ATOM    114  CG AARG A 110      -1.676  29.487 -12.844  0.50 20.32           C  
ANISOU  114  CG AARG A 110     2081   2737   2900     44    277   -290       C  
ATOM    115  CG BARG A 110      -1.291  29.840 -12.852  0.50 28.14           C  
ANISOU  115  CG BARG A 110     3493   3559   3640    122     58    -14       C  
ATOM    116  CD AARG A 110      -1.610  30.742 -12.003  0.50 23.82           C  
ANISOU  116  CD AARG A 110     3267   2669   3113    -58     38   -129       C  
ATOM    117  CD BARG A 110      -1.054  29.493 -14.318  0.50 28.25           C  
ANISOU  117  CD BARG A 110     3464   3686   3580    -75     86   -102       C  
ATOM    118  NE AARG A 110      -1.086  31.875 -12.754  0.50 24.99           N  
ANISOU  118  NE AARG A 110     3133   3073   3288   -191    353    169       N  
ATOM    119  NE BARG A 110      -0.463  30.599 -15.071  0.50 30.12           N  
ANISOU  119  NE BARG A 110     3834   3895   3712   -331    -55    -75       N  
ATOM    120  CZ AARG A 110      -0.524  32.941 -12.196  0.50 23.01           C  
ANISOU  120  CZ AARG A 110     2992   2680   3070     83     52    132       C  
ATOM    121  CZ BARG A 110      -0.088  30.529 -16.347  0.50 28.89           C  
ANISOU  121  CZ BARG A 110     3345   3867   3765   -108    -43    -45       C  
ATOM    122  NH1AARG A 110      -0.401  33.014 -10.876  0.50 16.07           N1+
ANISOU  122  NH1AARG A 110     2409   1189   2507    280    307    230       N1+
ATOM    123  NH2AARG A 110      -0.071  33.926 -12.959  0.50 22.58           N  
ANISOU  123  NH2AARG A 110     2677   2565   3336    456    411    549       N  
ATOM    124  NH1BARG A 110       0.438  31.592 -16.942  0.50 28.43           N1+
ANISOU  124  NH1BARG A 110     2914   4181   3706     49   -314    103       N1+
ATOM    125  NH2BARG A 110      -0.236  29.401 -17.033  0.50 34.19           N  
ANISOU  125  NH2BARG A 110     4462   4044   4482    256   -174   -104       N  
ATOM    126  N   LEU A 111      -0.426  26.150 -12.898  1.00 14.21           N  
ANISOU  126  N   LEU A 111     1703   1528   2167   -267     71   -112       N  
ATOM    127  CA  LEU A 111       0.586  25.506 -13.717  1.00 13.16           C  
ANISOU  127  CA  LEU A 111     1721   1453   1827    -31    107      0       C  
ATOM    128  C   LEU A 111       0.584  26.057 -15.122  1.00 14.20           C  
ANISOU  128  C   LEU A 111     1686   1831   1877   -120   -146    419       C  
ATOM    129  O   LEU A 111      -0.453  26.493 -15.623  1.00 17.05           O  
ANISOU  129  O   LEU A 111     1925   2333   2220    148    -63    505       O  
ATOM    130  CB  LEU A 111       0.344  24.000 -13.786  1.00 14.09           C  
ANISOU  130  CB  LEU A 111     2053   1349   1949   -309     90     18       C  
ATOM    131  CG  LEU A 111       0.412  23.238 -12.467  1.00 12.92           C  
ANISOU  131  CG  LEU A 111     1988   1420   1499   -358    -45    146       C  
ATOM    132  CD1 LEU A 111       0.124  21.769 -12.723  1.00 13.67           C  
ANISOU  132  CD1 LEU A 111     1853   1360   1979   -195     81     -3       C  
ATOM    133  CD2 LEU A 111       1.756  23.417 -11.790  1.00 14.31           C  
ANISOU  133  CD2 LEU A 111     2138   1511   1786   -232   -241    222       C  
ATOM    134  N   GLY A 112       1.753  26.039 -15.751  1.00 13.36           N  
ANISOU  134  N   GLY A 112     1907   1401   1765   -441    -53    252       N  
ATOM    135  CA  GLY A 112       1.860  26.310 -17.165  1.00 14.78           C  
ANISOU  135  CA  GLY A 112     2127   1688   1799   -165   -143    460       C  
ATOM    136  C   GLY A 112       2.720  25.264 -17.829  1.00 14.29           C  
ANISOU  136  C   GLY A 112     2065   1713   1648   -606   -125    288       C  
ATOM    137  O   GLY A 112       3.460  24.523 -17.171  1.00 14.29           O  
ANISOU  137  O   GLY A 112     1811   1843   1772   -307   -177     34       O  
ATOM    138  N   PHE A 113       2.620  25.218 -19.152  1.00 15.91           N  
ANISOU  138  N   PHE A 113     2267   2141   1636   -535   -152    366       N  
ATOM    139  CA  PHE A 113       3.310  24.229 -19.953  1.00 17.38           C  
ANISOU  139  CA  PHE A 113     2477   2348   1778   -351    -16    196       C  
ATOM    140  C   PHE A 113       3.779  24.924 -21.224  1.00 21.91           C  
ANISOU  140  C   PHE A 113     2813   3232   2278   -246    116    349       C  
ATOM    141  O   PHE A 113       3.161  25.893 -21.678  1.00 24.92           O  
ANISOU  141  O   PHE A 113     3849   3445   2172   -443    305    777       O  
ATOM    142  CB  PHE A 113       2.369  23.056 -20.275  1.00 17.11           C  
ANISOU  142  CB  PHE A 113     2633   2151   1717   -150   -125     60       C  
ATOM    143  CG  PHE A 113       1.715  22.450 -19.054  1.00 15.20           C  
ANISOU  143  CG  PHE A 113     2404   1812   1559   -320   -352    148       C  
ATOM    144  CD1 PHE A 113       2.299  21.372 -18.396  1.00 17.72           C  
ANISOU  144  CD1 PHE A 113     2665   2141   1927   -315   -335   -118       C  
ATOM    145  CD2 PHE A 113       0.523  22.973 -18.553  1.00 14.49           C  
ANISOU  145  CD2 PHE A 113     2113   1911   1481   -442   -367     66       C  
ATOM    146  CE1 PHE A 113       1.709  20.829 -17.254  1.00 16.42           C  
ANISOU  146  CE1 PHE A 113     2439   1827   1970   -211   -473    -69       C  
ATOM    147  CE2 PHE A 113      -0.073  22.445 -17.407  1.00 15.05           C  
ANISOU  147  CE2 PHE A 113     2270   1674   1770   -496   -249     43       C  
ATOM    148  CZ  PHE A 113       0.514  21.366 -16.765  1.00 15.07           C  
ANISOU  148  CZ  PHE A 113     2222   1600   1901   -286   -514    192       C  
ATOM    149  N   LEU A 114       4.878  24.439 -21.789  1.00 26.06           N  
ANISOU  149  N   LEU A 114     3347   4183   2369     -5    358    428       N  
ATOM    150  CA  LEU A 114       5.455  25.043 -22.994  1.00 27.17           C  
ANISOU  150  CA  LEU A 114     3661   3869   2793   -315    249    501       C  
ATOM    151  C   LEU A 114       4.572  24.853 -24.227  1.00 30.06           C  
ANISOU  151  C   LEU A 114     4009   3919   3491   -226   -115    120       C  
ATOM    152  O   LEU A 114       3.531  24.194 -24.169  1.00 29.55           O  
ANISOU  152  O   LEU A 114     4230   3766   3231    -76    247    354       O  
ATOM    153  CB  LEU A 114       6.861  24.487 -23.254  1.00 30.06           C  
ANISOU  153  CB  LEU A 114     3998   3649   3773   -146    287    242       C  
ATOM    154  CG  LEU A 114       8.078  25.073 -22.518  1.00 38.28           C  
ANISOU  154  CG  LEU A 114     4788   4779   4976    -98   -331    -45       C  
ATOM    155  CD1 LEU A 114       8.393  26.493 -22.988  1.00 41.34           C  
ANISOU  155  CD1 LEU A 114     5445   4843   5420   -136   -120     98       C  
ATOM    156  CD2 LEU A 114       7.927  25.030 -21.000  1.00 46.04           C  
ANISOU  156  CD2 LEU A 114     6063   5775   5655      4    101     44       C  
TER     157      LEU A 114 
ATOM    158  N   VAL A 122       8.475  15.137 -31.280  1.00 32.86           N  
ANISOU  158  N   VAL A 122     4767   4348   3369    -85     40   -473       N  
ATOM    159  CA  VAL A 122       8.211  15.790 -30.004  1.00 30.48           C  
ANISOU  159  CA  VAL A 122     4357   4135   3088    -28     80   -164       C  
ATOM    160  C   VAL A 122       8.489  14.859 -28.826  1.00 29.76           C  
ANISOU  160  C   VAL A 122     4141   3710   3455   -142    131    -55       C  
ATOM    161  O   VAL A 122       8.120  13.682 -28.850  1.00 31.18           O  
ANISOU  161  O   VAL A 122     4255   3720   3872   -448    355    -82       O  
ATOM    162  CB  VAL A 122       6.756  16.294 -29.918  1.00 34.18           C  
ANISOU  162  CB  VAL A 122     4586   4546   3852    194   -214    206       C  
ATOM    163  N   THR A 123       9.142  15.398 -27.799  1.00 25.66           N  
ANISOU  163  N   THR A 123     3438   3561   2748   -335    276    375       N  
ATOM    164  CA  THR A 123       9.460  14.641 -26.589  1.00 24.75           C  
ANISOU  164  CA  THR A 123     3484   3306   2613   -192    379    359       C  
ATOM    165  C   THR A 123       8.432  14.886 -25.484  1.00 22.09           C  
ANISOU  165  C   THR A 123     2872   2782   2739   -324    210    262       C  
ATOM    166  O   THR A 123       8.215  14.014 -24.637  1.00 21.43           O  
ANISOU  166  O   THR A 123     2954   2347   2839   -516    274    436       O  
ATOM    167  CB  THR A 123      10.863  14.988 -26.051  1.00 27.71           C  
ANISOU  167  CB  THR A 123     3810   3861   2857     12    235    298       C  
ATOM    168  CG2 THR A 123      11.950  14.456 -26.979  1.00 32.74           C  
ANISOU  168  CG2 THR A 123     3894   4792   3750    191    316    203       C  
ATOM    169  OG1 THR A 123      10.990  16.410 -25.934  1.00 27.90           O  
ANISOU  169  OG1 THR A 123     3757   4099   2745   -532    479    103       O  
ATOM    170  N   CYS A 124       7.830  16.081 -25.493  1.00 20.78           N  
ANISOU  170  N   CYS A 124     2839   2676   2380   -365    243    327       N  
ATOM    171  CA ACYS A 124       6.810  16.468 -24.510  0.70 18.76           C  
ANISOU  171  CA ACYS A 124     2406   1996   2724   -371    -69    378       C  
ATOM    172  CA BCYS A 124       6.802  16.457 -24.525  0.30 22.61           C  
ANISOU  172  CA BCYS A 124     2931   2634   3025    -96     65    303       C  
ATOM    173  C   CYS A 124       5.890  17.525 -25.117  1.00 20.19           C  
ANISOU  173  C   CYS A 124     2672   2131   2866   -411    182    637       C  
ATOM    174  O   CYS A 124       6.359  18.562 -25.590  1.00 24.42           O  
ANISOU  174  O   CYS A 124     3304   2303   3668   -644    253   1147       O  
ATOM    175  CB ACYS A 124       7.467  17.003 -23.226  0.70 21.89           C  
ANISOU  175  CB ACYS A 124     3030   2946   2338   -322    -43    530       C  
ATOM    176  CB BCYS A 124       7.438  16.963 -23.227  0.30 27.59           C  
ANISOU  176  CB BCYS A 124     3701   3662   3119     72    -53    180       C  
ATOM    177  SG ACYS A 124       6.334  17.394 -21.856  0.70 18.88           S  
ANISOU  177  SG ACYS A 124     2726   2431   2013   -358    -60    357       S  
ATOM    178  SG BCYS A 124       8.605  18.320 -23.456  0.30 39.31           S  
ANISOU  178  SG BCYS A 124     5275   4428   5230   -174   -106     84       S  
ATOM    179  N   THR A 125       4.587  17.257 -25.112  1.00 17.99           N  
ANISOU  179  N   THR A 125     2692   1834   2307   -228     29    497       N  
ATOM    180  CA  THR A 125       3.596  18.207 -25.622  1.00 17.63           C  
ANISOU  180  CA  THR A 125     2757   1800   2139   -516     21    238       C  
ATOM    181  C   THR A 125       2.346  18.213 -24.743  1.00 18.11           C  
ANISOU  181  C   THR A 125     2802   2158   1918     61     22    523       C  
ATOM    182  O   THR A 125       1.901  17.176 -24.269  1.00 26.43           O  
ANISOU  182  O   THR A 125     3946   2493   3602    -42    269    364       O  
ATOM    183  CB  THR A 125       3.236  17.946 -27.112  1.00 20.98           C  
ANISOU  183  CB  THR A 125     3587   2146   2238   -180   -218    414       C  
ATOM    184  CG2 THR A 125       2.581  16.579 -27.311  1.00 20.50           C  
ANISOU  184  CG2 THR A 125     3058   2240   2491   -528   -427    229       C  
ATOM    185  OG1 THR A 125       2.350  18.967 -27.582  1.00 23.45           O  
ANISOU  185  OG1 THR A 125     4319   2364   2228     60   -210    751       O  
ATOM    186  N   TYR A 126       1.797  19.400 -24.527  1.00 17.04           N  
ANISOU  186  N   TYR A 126     3080   1539   1855   -221     87    503       N  
ATOM    187  CA  TYR A 126       0.662  19.578 -23.642  1.00 15.48           C  
ANISOU  187  CA  TYR A 126     2732   1427   1721    -78   -394    333       C  
ATOM    188  C   TYR A 126      -0.569  20.054 -24.403  1.00 17.04           C  
ANISOU  188  C   TYR A 126     3044   1577   1851      0   -364    297       C  
ATOM    189  O   TYR A 126      -0.484  20.959 -25.234  1.00 18.80           O  
ANISOU  189  O   TYR A 126     3670   1610   1862    -44   -418    623       O  
ATOM    190  CB  TYR A 126       1.019  20.560 -22.523  1.00 18.20           C  
ANISOU  190  CB  TYR A 126     3169   1851   1894    -59   -414     84       C  
ATOM    191  CG  TYR A 126      -0.143  20.936 -21.633  1.00 15.51           C  
ANISOU  191  CG  TYR A 126     2614   1508   1768   -207   -671     43       C  
ATOM    192  CD1 TYR A 126      -0.589  20.078 -20.625  1.00 16.18           C  
ANISOU  192  CD1 TYR A 126     2717   1791   1637   -172   -368    148       C  
ATOM    193  CD2 TYR A 126      -0.797  22.159 -21.797  1.00 16.67           C  
ANISOU  193  CD2 TYR A 126     2658   1641   2032   -184   -675     39       C  
ATOM    194  CE1 TYR A 126      -1.670  20.429 -19.808  1.00 16.15           C  
ANISOU  194  CE1 TYR A 126     2548   1654   1933   -341   -752     40       C  
ATOM    195  CE2 TYR A 126      -1.861  22.518 -20.993  1.00 16.95           C  
ANISOU  195  CE2 TYR A 126     2451   2052   1937     94   -840    162       C  
ATOM    196  CZ  TYR A 126      -2.294  21.656 -20.003  1.00 17.46           C  
ANISOU  196  CZ  TYR A 126     2557   2118   1956    -69   -657   -170       C  
ATOM    197  OH  TYR A 126      -3.345  22.035 -19.210  1.00 18.80           O  
ANISOU  197  OH  TYR A 126     2772   2122   2247    -72   -875   -160       O  
ATOM    198  N   SER A 127      -1.707  19.438 -24.098  1.00 16.99           N  
ANISOU  198  N   SER A 127     3245   1628   1580   -181   -613    195       N  
ATOM    199  CA  SER A 127      -2.997  19.814 -24.653  1.00 16.64           C  
ANISOU  199  CA  SER A 127     3041   1541   1738   -372   -556    421       C  
ATOM    200  C   SER A 127      -3.812  20.569 -23.611  1.00 16.76           C  
ANISOU  200  C   SER A 127     3007   1444   1915     -5   -759    260       C  
ATOM    201  O   SER A 127      -4.307  19.961 -22.666  1.00 17.93           O  
ANISOU  201  O   SER A 127     3325   1825   1661     62   -640    308       O  
ATOM    202  CB  SER A 127      -3.764  18.569 -25.074  1.00 17.71           C  
ANISOU  202  CB  SER A 127     3151   1525   2053   -410   -520    372       C  
ATOM    203  OG  SER A 127      -5.092  18.902 -25.433  1.00 19.28           O  
ANISOU  203  OG  SER A 127     3335   2005   1984   -206   -778    151       O  
ATOM    204  N   PRO A 128      -3.941  21.903 -23.759  1.00 18.06           N  
ANISOU  204  N   PRO A 128     3324   1594   1942    -45  -1094    157       N  
ATOM    205  CA  PRO A 128      -4.856  22.617 -22.866  1.00 18.89           C  
ANISOU  205  CA  PRO A 128     3334   1399   2442    223   -761    278       C  
ATOM    206  C   PRO A 128      -6.297  22.095 -22.901  1.00 18.90           C  
ANISOU  206  C   PRO A 128     3518   1361   2299    240   -936    137       C  
ATOM    207  O   PRO A 128      -6.931  21.980 -21.855  1.00 20.81           O  
ANISOU  207  O   PRO A 128     3159   2136   2610    335  -1251   -112       O  
ATOM    208  CB  PRO A 128      -4.770  24.069 -23.360  1.00 20.94           C  
ANISOU  208  CB  PRO A 128     3599   1610   2746    355   -907    325       C  
ATOM    209  CG  PRO A 128      -3.412  24.156 -23.977  1.00 20.02           C  
ANISOU  209  CG  PRO A 128     3412   1589   2606    -58  -1005    254       C  
ATOM    210  CD  PRO A 128      -3.218  22.828 -24.651  1.00 19.74           C  
ANISOU  210  CD  PRO A 128     3179   1668   2652    -55  -1044    314       C  
ATOM    211  N   ALA A 129      -6.799  21.759 -24.089  1.00 20.29           N  
ANISOU  211  N   ALA A 129     3486   1573   2648    167  -1270    110       N  
ATOM    212  CA  ALA A 129      -8.171  21.249 -24.227  1.00 21.63           C  
ANISOU  212  CA  ALA A 129     3486   2070   2660     71  -1009    199       C  
ATOM    213  C   ALA A 129      -8.436  20.006 -23.379  1.00 20.14           C  
ANISOU  213  C   ALA A 129     3055   2162   2436     82   -845     92       C  
ATOM    214  O   ALA A 129      -9.505  19.871 -22.781  1.00 24.47           O  
ANISOU  214  O   ALA A 129     3136   2932   3227    307  -1016    265       O  
ATOM    215  CB  ALA A 129      -8.483  20.961 -25.672  1.00 21.63           C  
ANISOU  215  CB  ALA A 129     3346   2593   2278     87  -1292    642       C  
ATOM    216  N   LEU A 130      -7.451  19.112 -23.331  1.00 18.42           N  
ANISOU  216  N   LEU A 130     2958   1698   2343    313  -1205    176       N  
ATOM    217  CA  LEU A 130      -7.542  17.878 -22.558  1.00 17.21           C  
ANISOU  217  CA  LEU A 130     2931   1570   2038     31   -831    134       C  
ATOM    218  C   LEU A 130      -6.961  17.988 -21.143  1.00 17.34           C  
ANISOU  218  C   LEU A 130     2659   1845   2084    132   -754     83       C  
ATOM    219  O   LEU A 130      -7.118  17.059 -20.348  1.00 18.37           O  
ANISOU  219  O   LEU A 130     2871   1991   2117    106   -624    240       O  
ATOM    220  CB  LEU A 130      -6.812  16.752 -23.292  1.00 17.54           C  
ANISOU  220  CB  LEU A 130     2939   1827   1897   -157   -716    114       C  
ATOM    221  CG  LEU A 130      -7.356  16.303 -24.648  1.00 20.21           C  
ANISOU  221  CG  LEU A 130     3423   2222   2031   -211   -821     58       C  
ATOM    222  CD1 LEU A 130      -6.358  15.389 -25.339  1.00 20.88           C  
ANISOU  222  CD1 LEU A 130     3716   2098   2119   -243   -362    -47       C  
ATOM    223  CD2 LEU A 130      -8.704  15.612 -24.488  1.00 21.53           C  
ANISOU  223  CD2 LEU A 130     2923   2906   2350   -449   -578   -123       C  
ATOM    224  N   ASN A 131      -6.302  19.111 -20.843  1.00 16.42           N  
ANISOU  224  N   ASN A 131     2625   1688   1923    385   -819    110       N  
ATOM    225  CA  ASN A 131      -5.457  19.267 -19.643  1.00 15.88           C  
ANISOU  225  CA  ASN A 131     2615   1687   1732    289   -749    -15       C  
ATOM    226  C   ASN A 131      -4.564  18.042 -19.476  1.00 14.83           C  
ANISOU  226  C   ASN A 131     2454   1431   1747     92   -789     70       C  
ATOM    227  O   ASN A 131      -4.540  17.396 -18.424  1.00 14.83           O  
ANISOU  227  O   ASN A 131     2417   1661   1556    399   -518     97       O  
ATOM    228  CB  ASN A 131      -6.280  19.542 -18.377  1.00 17.67           C  
ANISOU  228  CB  ASN A 131     2493   2013   2205    534   -690    -73       C  
ATOM    229  CG  ASN A 131      -5.406  19.810 -17.144  1.00 17.35           C  
ANISOU  229  CG  ASN A 131     2535   1883   2173    315   -415     85       C  
ATOM    230  ND2 ASN A 131      -4.239  20.399 -17.358  1.00 16.54           N  
ANISOU  230  ND2 ASN A 131     2705   1835   1742    583   -657   -125       N  
ATOM    231  OD1 ASN A 131      -5.783  19.476 -16.019  1.00 21.41           O  
ANISOU  231  OD1 ASN A 131     3290   2654   2191    643   -214    -25       O  
ATOM    232  N   LYS A 132      -3.844  17.732 -20.550  1.00 14.40           N  
ANISOU  232  N   LYS A 132     2409   1315   1745     72   -577     80       N  
ATOM    233  CA  LYS A 132      -3.103  16.489 -20.643  1.00 12.96           C  
ANISOU  233  CA  LYS A 132     1977   1249   1699    -58   -317    234       C  
ATOM    234  C   LYS A 132      -1.745  16.670 -21.296  1.00 13.47           C  
ANISOU  234  C   LYS A 132     2166   1385   1564   -204   -309    101       C  
ATOM    235  O   LYS A 132      -1.632  17.239 -22.389  1.00 14.94           O  
ANISOU  235  O   LYS A 132     2894   1435   1345   -319   -320    332       O  
ATOM    236  CB  LYS A 132      -3.929  15.436 -21.392  1.00 14.39           C  
ANISOU  236  CB  LYS A 132     2287   1361   1819   -258   -492     65       C  
ATOM    237  CG  LYS A 132      -3.297  14.053 -21.434  1.00 13.97           C  
ANISOU  237  CG  LYS A 132     2292   1126   1887   -270   -243     31       C  
ATOM    238  CD  LYS A 132      -4.308  13.019 -21.877  1.00 15.61           C  
ANISOU  238  CD  LYS A 132     2513   1201   2216   -257    -62    181       C  
ATOM    239  CE  LYS A 132      -3.717  11.627 -21.855  1.00 18.58           C  
ANISOU  239  CE  LYS A 132     2883   1175   3000   -384    225    -79       C  
ATOM    240  NZ  LYS A 132      -4.796  10.624 -21.998  1.00 21.60           N1+
ANISOU  240  NZ  LYS A 132     3002   1514   3690   -539    258   -231       N1+
ATOM    241  N   MET A 133      -0.731  16.177 -20.590  1.00 13.39           N  
ANISOU  241  N   MET A 133     2323   1204   1560   -183   -221    176       N  
ATOM    242  CA AMET A 133       0.629  16.101 -21.100  0.70 13.21           C  
ANISOU  242  CA AMET A 133     2355   1362   1300   -461   -148    242       C  
ATOM    243  CA BMET A 133       0.631  16.106 -21.097  0.30 14.09           C  
ANISOU  243  CA BMET A 133     2273   1547   1531   -252   -123    134       C  
ATOM    244  C   MET A 133       0.866  14.763 -21.787  1.00 13.64           C  
ANISOU  244  C   MET A 133     2156   1493   1531   -143   -227    213       C  
ATOM    245  O   MET A 133       0.476  13.710 -21.268  1.00 14.57           O  
ANISOU  245  O   MET A 133     2470   1344   1721   -135    160    228       O  
ATOM    246  CB AMET A 133       1.618  16.241 -19.948  0.70 13.43           C  
ANISOU  246  CB AMET A 133     2069   1580   1453   -316   -297    198       C  
ATOM    247  CB BMET A 133       1.623  16.289 -19.941  0.30 14.87           C  
ANISOU  247  CB BMET A 133     2149   1832   1665    -87   -186    164       C  
ATOM    248  CG AMET A 133       3.064  15.950 -20.334  0.70 15.45           C  
ANISOU  248  CG AMET A 133     2212   2101   1555   -367    -97    206       C  
ATOM    249  CG BMET A 133       3.097  16.179 -20.325  0.30 15.99           C  
ANISOU  249  CG BMET A 133     2230   1900   1944    -73    -50     57       C  
ATOM    250  SD AMET A 133       4.201  16.039 -18.949  0.70 16.80           S  
ANISOU  250  SD AMET A 133     2406   2133   1842     16   -150    -94       S  
ATOM    251  SD BMET A 133       3.667  17.501 -21.411  0.30 17.32           S  
ANISOU  251  SD BMET A 133     2073   2172   2333   -419    160    115       S  
ATOM    252  CE AMET A 133       4.124  17.789 -18.594  0.70 18.57           C  
ANISOU  252  CE AMET A 133     2854   2000   2201     82    211    244       C  
ATOM    253  CE BMET A 133       3.942  18.821 -20.236  0.30 20.43           C  
ANISOU  253  CE BMET A 133     2882   2345   2533     45     56     48       C  
ATOM    254  N   PHE A 134       1.512  14.813 -22.949  1.00 14.69           N  
ANISOU  254  N   PHE A 134     2758   1471   1352   -272   -139    227       N  
ATOM    255  CA  PHE A 134       1.939  13.621 -23.672  1.00 14.44           C  
ANISOU  255  CA  PHE A 134     2465   1552   1468    -75   -257     25       C  
ATOM    256  C   PHE A 134       3.451  13.702 -23.730  1.00 14.10           C  
ANISOU  256  C   PHE A 134     2645   1312   1399    -49   -258    -12       C  
ATOM    257  O   PHE A 134       3.987  14.710 -24.187  1.00 15.20           O  
ANISOU  257  O   PHE A 134     2758   1350   1664   -323    -43    268       O  
ATOM    258  CB  PHE A 134       1.347  13.610 -25.087  1.00 15.78           C  
ANISOU  258  CB  PHE A 134     2624   1959   1412   -308    -32     57       C  
ATOM    259  CG  PHE A 134      -0.153  13.535 -25.118  1.00 14.58           C  
ANISOU  259  CG  PHE A 134     2545   1737   1256   -274   -166     71       C  
ATOM    260  CD1 PHE A 134      -0.924  14.670 -24.881  1.00 15.17           C  
ANISOU  260  CD1 PHE A 134     2711   1481   1570   -260   -311    271       C  
ATOM    261  CD2 PHE A 134      -0.797  12.332 -25.386  1.00 15.39           C  
ANISOU  261  CD2 PHE A 134     2696   1595   1554   -399    -56     17       C  
ATOM    262  CE1 PHE A 134      -2.318  14.614 -24.909  1.00 15.60           C  
ANISOU  262  CE1 PHE A 134     2560   1785   1581   -245   -226    263       C  
ATOM    263  CE2 PHE A 134      -2.185  12.260 -25.419  1.00 16.26           C  
ANISOU  263  CE2 PHE A 134     2634   1933   1612   -166    -90    -23       C  
ATOM    264  CZ  PHE A 134      -2.950  13.406 -25.176  1.00 16.34           C  
ANISOU  264  CZ  PHE A 134     2578   1936   1694   -516     18    -28       C  
ATOM    265  N   CYS A 135       4.144  12.671 -23.251  1.00 14.47           N  
ANISOU  265  N   CYS A 135     2321   1672   1504    -92     63    150       N  
ATOM    266  CA ACYS A 135       5.599  12.715 -23.185  0.80 15.14           C  
ANISOU  266  CA ACYS A 135     2440   1601   1709    -19    198     42       C  
ATOM    267  CA BCYS A 135       5.599  12.717 -23.124  0.20 16.39           C  
ANISOU  267  CA BCYS A 135     2406   1800   2019     22    106     92       C  
ATOM    268  C   CYS A 135       6.228  11.349 -23.371  1.00 15.03           C  
ANISOU  268  C   CYS A 135     2501   1525   1681    -27    275    132       C  
ATOM    269  O   CYS A 135       5.579  10.324 -23.179  1.00 18.26           O  
ANISOU  269  O   CYS A 135     2918   1713   2306    -45    527    138       O  
ATOM    270  CB ACYS A 135       6.038  13.299 -21.846  0.80 15.58           C  
ANISOU  270  CB ACYS A 135     2328   1967   1624   -211     81    206       C  
ATOM    271  CB BCYS A 135       5.976  13.234 -21.727  0.20 18.46           C  
ANISOU  271  CB BCYS A 135     2621   2165   2228     66      1     -6       C  
ATOM    272  SG ACYS A 135       5.452  12.314 -20.438  0.80 16.25           S  
ANISOU  272  SG ACYS A 135     2645   2002   1525   -184     13    167       S  
ATOM    273  SG BCYS A 135       7.705  13.718 -21.493  0.20 20.34           S  
ANISOU  273  SG BCYS A 135     2781   2370   2575    165     75    374       S  
ATOM    274  N   GLN A 136       7.496  11.347 -23.774  1.00 15.93           N  
ANISOU  274  N   GLN A 136     2324   1932   1794    -21    321     83       N  
ATOM    275  CA  GLN A 136       8.261  10.110 -23.914  1.00 16.16           C  
ANISOU  275  CA  GLN A 136     2221   2024   1891     67    313     88       C  
ATOM    276  C   GLN A 136       8.939   9.721 -22.609  1.00 16.88           C  
ANISOU  276  C   GLN A 136     2783   1842   1785     85    440     21       C  
ATOM    277  O   GLN A 136       9.317  10.584 -21.816  1.00 17.14           O  
ANISOU  277  O   GLN A 136     2816   1992   1702     98    300     32       O  
ATOM    278  CB  GLN A 136       9.319  10.255 -25.001  1.00 20.15           C  
ANISOU  278  CB  GLN A 136     2755   3039   1860     71    534   -108       C  
ATOM    279  CG  GLN A 136       8.753  10.311 -26.404  1.00 21.41           C  
ANISOU  279  CG  GLN A 136     2985   3239   1910    -40    195     86       C  
ATOM    280  CD  GLN A 136       9.820  10.479 -27.462  1.00 26.09           C  
ANISOU  280  CD  GLN A 136     3595   3923   2393   -131    398    -68       C  
ATOM    281  NE2 GLN A 136       9.566   9.930 -28.642  1.00 26.94           N  
ANISOU  281  NE2 GLN A 136     3702   3995   2536   -124    479   -359       N  
ATOM    282  OE1 GLN A 136      10.857  11.101 -27.227  1.00 29.66           O  
ANISOU  282  OE1 GLN A 136     3726   5181   2361   -378    441    -63       O  
ATOM    283  N   LEU A 137       9.096   8.414 -22.403  1.00 16.76           N  
ANISOU  283  N   LEU A 137     2565   1831   1969      9    515    150       N  
ATOM    284  CA  LEU A 137       9.757   7.879 -21.223  1.00 16.91           C  
ANISOU  284  CA  LEU A 137     2587   1969   1869    177    172    -43       C  
ATOM    285  C   LEU A 137      11.152   8.475 -21.052  1.00 17.85           C  
ANISOU  285  C   LEU A 137     2514   2019   2248     74    398    118       C  
ATOM    286  O   LEU A 137      11.940   8.514 -22.003  1.00 19.23           O  
ANISOU  286  O   LEU A 137     2661   2615   2029    371    760     12       O  
ATOM    287  CB  LEU A 137       9.836   6.346 -21.310  1.00 20.05           C  
ANISOU  287  CB  LEU A 137     3101   2044   2472     35    297    106       C  
ATOM    288  CG  LEU A 137      10.133   5.512 -20.054  1.00 21.74           C  
ANISOU  288  CG  LEU A 137     3344   2106   2810    487    104   -156       C  
ATOM    289  CD1 LEU A 137       9.674   4.083 -20.262  1.00 23.07           C  
ANISOU  289  CD1 LEU A 137     3204   2384   3175    364    371    173       C  
ATOM    290  CD2 LEU A 137      11.610   5.529 -19.670  1.00 25.05           C  
ANISOU  290  CD2 LEU A 137     3704   2518   3295   -128    -41   -153       C  
ATOM    291  N   ALA A 138      11.421   8.954 -19.836  1.00 17.84           N  
ANISOU  291  N   ALA A 138     2665   2041   2073    506    329    156       N  
ATOM    292  CA  ALA A 138      12.725   9.488 -19.401  1.00 18.69           C  
ANISOU  292  CA  ALA A 138     2467   2257   2374    395    353    222       C  
ATOM    293  C   ALA A 138      13.118  10.850 -19.981  1.00 19.07           C  
ANISOU  293  C   ALA A 138     2260   2472   2513    318    305    218       C  
ATOM    294  O   ALA A 138      14.170  11.396 -19.637  1.00 24.60           O  
ANISOU  294  O   ALA A 138     2757   3225   3362    -45     25    468       O  
ATOM    295  CB  ALA A 138      13.849   8.463 -19.609  1.00 21.84           C  
ANISOU  295  CB  ALA A 138     2733   2692   2870    691    129    152       C  
ATOM    296  N   LYS A 139      12.275  11.405 -20.843  1.00 17.35           N  
ANISOU  296  N   LYS A 139     2301   2166   2122    409    560     24       N  
ATOM    297  CA  LYS A 139      12.565  12.699 -21.452  1.00 16.51           C  
ANISOU  297  CA  LYS A 139     2399   1934   1940     71    249    131       C  
ATOM    298  C   LYS A 139      12.130  13.861 -20.565  1.00 15.95           C  
ANISOU  298  C   LYS A 139     2227   1817   2014    238    382     32       C  
ATOM    299  O   LYS A 139      11.265  13.724 -19.698  1.00 16.71           O  
ANISOU  299  O   LYS A 139     2226   2137   1986   -142    474    216       O  
ATOM    300  CB  LYS A 139      11.915  12.805 -22.837  1.00 19.27           C  
ANISOU  300  CB  LYS A 139     3038   2276   2006    -44    184    -70       C  
ATOM    301  CG  LYS A 139      12.396  11.764 -23.847  1.00 20.30           C  
ANISOU  301  CG  LYS A 139     2559   2852   2300   -575    464   -335       C  
ATOM    302  CD  LYS A 139      13.886  11.888 -24.149  1.00 25.85           C  
ANISOU  302  CD  LYS A 139     3019   3438   3365   -151    596   -705       C  
ATOM    303  CE  LYS A 139      14.306  10.927 -25.255  1.00 29.22           C  
ANISOU  303  CE  LYS A 139     4082   4079   2939    127    283   -689       C  
ATOM    304  N   THR A 140      12.737  15.015 -20.805  1.00 16.92           N  
ANISOU  304  N   THR A 140     2454   2069   1903    -62    562    186       N  
ATOM    305  CA  THR A 140      12.445  16.223 -20.053  1.00 17.15           C  
ANISOU  305  CA  THR A 140     2581   2076   1856     82    302    309       C  
ATOM    306  C   THR A 140      11.004  16.682 -20.246  1.00 15.54           C  
ANISOU  306  C   THR A 140     2260   1778   1864    126    156    172       C  
ATOM    307  O   THR A 140      10.563  16.904 -21.374  1.00 18.12           O  
ANISOU  307  O   THR A 140     2902   2324   1658    112    177    273       O  
ATOM    308  CB  THR A 140      13.394  17.353 -20.484  1.00 18.25           C  
ANISOU  308  CB  THR A 140     2560   2292   2081    -95    257    452       C  
ATOM    309  CG2 THR A 140      13.176  18.596 -19.632  1.00 21.77           C  
ANISOU  309  CG2 THR A 140     3429   2295   2545   -537    426     43       C  
ATOM    310  OG1 THR A 140      14.746  16.905 -20.345  1.00 20.18           O  
ANISOU  310  OG1 THR A 140     2513   2840   2313   -154    367    209       O  
ATOM    311  N   CYS A 141      10.291  16.833 -19.130  1.00 14.72           N  
ANISOU  311  N   CYS A 141     2136   1750   1703     63    302    156       N  
ATOM    312  CA ACYS A 141       8.929  17.359 -19.134  0.70 14.70           C  
ANISOU  312  CA ACYS A 141     2019   1987   1578   -145    199    398       C  
ATOM    313  CA BCYS A 141       8.921  17.326 -19.130  0.30 15.74           C  
ANISOU  313  CA BCYS A 141     2081   1897   2003    -35     85    158       C  
ATOM    314  C   CYS A 141       8.879  18.621 -18.309  1.00 14.84           C  
ANISOU  314  C   CYS A 141     1929   1738   1972    -60    218     41       C  
ATOM    315  O   CYS A 141       8.795  18.562 -17.076  1.00 14.50           O  
ANISOU  315  O   CYS A 141     1964   1993   1551     27    120    216       O  
ATOM    316  CB ACYS A 141       7.946  16.363 -18.541  0.70 15.10           C  
ANISOU  316  CB ACYS A 141     2097   2066   1574   -325    198    218       C  
ATOM    317  CB BCYS A 141       7.987  16.255 -18.542  0.30 16.82           C  
ANISOU  317  CB BCYS A 141     2183   2058   2150   -108     65    183       C  
ATOM    318  SG ACYS A 141       7.885  14.863 -19.432  0.70 16.12           S  
ANISOU  318  SG ACYS A 141     2482   1798   1844   -276     77    143       S  
ATOM    319  SG BCYS A 141       6.203  16.573 -18.618  0.30 19.81           S  
ANISOU  319  SG BCYS A 141     2425   1938   3160    -94   -710    394       S  
ATOM    320  N   PRO A 142       8.954  19.789 -18.982  1.00 16.16           N  
ANISOU  320  N   PRO A 142     2551   1822   1766   -178    280     55       N  
ATOM    321  CA  PRO A 142       8.930  21.041 -18.235  1.00 15.20           C  
ANISOU  321  CA  PRO A 142     2118   1585   2071     94    180     88       C  
ATOM    322  C   PRO A 142       7.534  21.357 -17.720  1.00 15.33           C  
ANISOU  322  C   PRO A 142     1893   1892   2040    176     30    327       C  
ATOM    323  O   PRO A 142       6.556  21.348 -18.473  1.00 19.67           O  
ANISOU  323  O   PRO A 142     2465   3134   1871    180   -149    -70       O  
ATOM    324  CB  PRO A 142       9.391  22.096 -19.254  1.00 17.92           C  
ANISOU  324  CB  PRO A 142     2431   2071   2305   -209    527    290       C  
ATOM    325  CG  PRO A 142       9.669  21.381 -20.523  1.00 21.56           C  
ANISOU  325  CG  PRO A 142     4069   1971   2150   -166    438    -32       C  
ATOM    326  CD  PRO A 142       9.075  20.015 -20.434  1.00 17.22           C  
ANISOU  326  CD  PRO A 142     2902   1925   1713     89    327    294       C  
ATOM    327  N   VAL A 143       7.449  21.608 -16.424  1.00 12.88           N  
ANISOU  327  N   VAL A 143     1861   1331   1700   -308     98    131       N  
ATOM    328  CA  VAL A 143       6.212  22.062 -15.811  1.00 12.68           C  
ANISOU  328  CA  VAL A 143     1611   1510   1694   -165    -41    113       C  
ATOM    329  C   VAL A 143       6.501  23.405 -15.142  1.00 12.11           C  
ANISOU  329  C   VAL A 143     1492   1346   1763   -215     77     80       C  
ATOM    330  O   VAL A 143       7.462  23.534 -14.384  1.00 13.71           O  
ANISOU  330  O   VAL A 143     1707   1382   2120   -400   -289    199       O  
ATOM    331  CB  VAL A 143       5.685  21.033 -14.800  1.00 12.73           C  
ANISOU  331  CB  VAL A 143     1780   1221   1834   -193    -46    125       C  
ATOM    332  CG1 VAL A 143       4.487  21.582 -14.059  1.00 14.73           C  
ANISOU  332  CG1 VAL A 143     1860   1595   2141   -226    139    196       C  
ATOM    333  CG2 VAL A 143       5.322  19.732 -15.506  1.00 14.75           C  
ANISOU  333  CG2 VAL A 143     1869   1615   2119   -184   -273    155       C  
ATOM    334  N   GLN A 144       5.689  24.409 -15.462  1.00 12.03           N  
ANISOU  334  N   GLN A 144     1574   1359   1637   -160     32    152       N  
ATOM    335  CA  GLN A 144       5.887  25.754 -14.939  1.00 13.16           C  
ANISOU  335  CA  GLN A 144     2025   1316   1656   -236     91     89       C  
ATOM    336  C   GLN A 144       4.992  25.997 -13.747  1.00 11.69           C  
ANISOU  336  C   GLN A 144     1471   1065   1902   -272    -98     78       C  
ATOM    337  O   GLN A 144       3.806  25.664 -13.770  1.00 12.88           O  
ANISOU  337  O   GLN A 144     1522   1568   1803   -322     -4     90       O  
ATOM    338  CB  GLN A 144       5.556  26.797 -15.996  1.00 13.94           C  
ANISOU  338  CB  GLN A 144     2094   1354   1848   -289     25    237       C  
ATOM    339  CG  GLN A 144       6.349  26.677 -17.271  1.00 15.08           C  
ANISOU  339  CG  GLN A 144     2392   1543   1794   -223    137    159       C  
ATOM    340  CD  GLN A 144       5.852  27.626 -18.334  1.00 17.03           C  
ANISOU  340  CD  GLN A 144     2529   1760   2178   -348     58    147       C  
ATOM    341  NE2 GLN A 144       6.691  27.890 -19.318  1.00 21.78           N  
ANISOU  341  NE2 GLN A 144     3095   3107   2072   -482    660    503       N  
ATOM    342  OE1 GLN A 144       4.727  28.127 -18.268  1.00 16.76           O  
ANISOU  342  OE1 GLN A 144     2740   1829   1796   -246    -28    305       O  
ATOM    343  N   LEU A 145       5.573  26.608 -12.723  1.00 12.20           N  
ANISOU  343  N   LEU A 145     1590   1435   1608   -438    -25    -15       N  
ATOM    344  CA  LEU A 145       4.836  27.068 -11.565  1.00 12.67           C  
ANISOU  344  CA  LEU A 145     1720   1402   1692   -297     -2     56       C  
ATOM    345  C   LEU A 145       4.678  28.573 -11.679  1.00 14.34           C  
ANISOU  345  C   LEU A 145     2044   1486   1916   -346   -103    108       C  
ATOM    346  O   LEU A 145       5.662  29.303 -11.844  1.00 14.59           O  
ANISOU  346  O   LEU A 145     1789   1420   2334   -564     60    151       O  
ATOM    347  CB  LEU A 145       5.575  26.723 -10.269  1.00 14.54           C  
ANISOU  347  CB  LEU A 145     1998   1646   1879   -466    -35     11       C  
ATOM    348  CG  LEU A 145       6.211  25.340 -10.147  1.00 13.85           C  
ANISOU  348  CG  LEU A 145     1880   1333   2048   -304   -169     66       C  
ATOM    349  CD1 LEU A 145       6.946  25.235  -8.830  1.00 15.80           C  
ANISOU  349  CD1 LEU A 145     2060   1774   2167   -354   -329    262       C  
ATOM    350  CD2 LEU A 145       5.171  24.226 -10.270  1.00 14.62           C  
ANISOU  350  CD2 LEU A 145     2056   1403   2095   -489    104     20       C  
ATOM    351  N   TRP A 146       3.430  29.021 -11.583  1.00 13.46           N  
ANISOU  351  N   TRP A 146     2046   1182   1886   -164    116     93       N  
ATOM    352  CA  TRP A 146       3.091  30.431 -11.590  1.00 14.97           C  
ANISOU  352  CA  TRP A 146     2158   1274   2255   -173    -28    176       C  
ATOM    353  C   TRP A 146       2.406  30.770 -10.272  1.00 15.01           C  
ANISOU  353  C   TRP A 146     2055   1322   2325   -158    221   -103       C  
ATOM    354  O   TRP A 146       1.495  30.059  -9.829  1.00 16.59           O  
ANISOU  354  O   TRP A 146     2107   1734   2460   -339    366   -202       O  
ATOM    355  CB  TRP A 146       2.154  30.742 -12.755  1.00 15.91           C  
ANISOU  355  CB  TRP A 146     2141   1349   2554    -24    -11     -2       C  
ATOM    356  CG  TRP A 146       2.757  30.559 -14.116  1.00 14.85           C  
ANISOU  356  CG  TRP A 146     1916   1609   2118    -39     39    199       C  
ATOM    357  CD1 TRP A 146       2.978  29.379 -14.775  1.00 16.27           C  
ANISOU  357  CD1 TRP A 146     2129   1829   2221   -378    112    167       C  
ATOM    358  CD2 TRP A 146       3.204  31.596 -14.995  1.00 15.24           C  
ANISOU  358  CD2 TRP A 146     1952   1293   2544   -186   -144    519       C  
ATOM    359  CE2 TRP A 146       3.685  30.975 -16.169  1.00 16.32           C  
ANISOU  359  CE2 TRP A 146     2130   1870   2197   -266   -208    479       C  
ATOM    360  CE3 TRP A 146       3.240  32.992 -14.906  1.00 17.60           C  
ANISOU  360  CE3 TRP A 146     2418   1428   2839   -203   -121    431       C  
ATOM    361  NE1 TRP A 146       3.541  29.622 -16.009  1.00 15.86           N  
ANISOU  361  NE1 TRP A 146     2199   1274   2553   -139    -18    314       N  
ATOM    362  CZ2 TRP A 146       4.208  31.705 -17.242  1.00 18.16           C  
ANISOU  362  CZ2 TRP A 146     2447   1849   2601   -309    -98    427       C  
ATOM    363  CZ3 TRP A 146       3.753  33.714 -15.974  1.00 19.34           C  
ANISOU  363  CZ3 TRP A 146     2379   1747   3223   -152    292    499       C  
ATOM    364  CH2 TRP A 146       4.231  33.068 -17.126  1.00 20.05           C  
ANISOU  364  CH2 TRP A 146     2787   1862   2967    -72    335    592       C  
ATOM    365  N   VAL A 147       2.868  31.839  -9.630  1.00 15.73           N  
ANISOU  365  N   VAL A 147     2188   1489   2298   -204    269     46       N  
ATOM    366  CA  VAL A 147       2.219  32.364  -8.426  1.00 16.21           C  
ANISOU  366  CA  VAL A 147     2369   1317   2472   -134    219    -61       C  
ATOM    367  C   VAL A 147       1.988  33.872  -8.547  1.00 16.74           C  
ANISOU  367  C   VAL A 147     2916   1221   2224   -216    -88    -61       C  
ATOM    368  O   VAL A 147       2.709  34.567  -9.275  1.00 20.67           O  
ANISOU  368  O   VAL A 147     3298   1545   3010   -542    535    -91       O  
ATOM    369  CB  VAL A 147       3.019  32.044  -7.126  1.00 17.65           C  
ANISOU  369  CB  VAL A 147     2454   1829   2420   -252    208    151       C  
ATOM    370  CG1 VAL A 147       3.039  30.546  -6.848  1.00 19.08           C  
ANISOU  370  CG1 VAL A 147     2756   1532   2960   -238   -111    -53       C  
ATOM    371  CG2 VAL A 147       4.442  32.612  -7.188  1.00 19.60           C  
ANISOU  371  CG2 VAL A 147     2289   2218   2940   -419    234    -44       C  
ATOM    372  N   ASP A 148       0.970  34.366  -7.847  1.00 20.31           N  
ANISOU  372  N   ASP A 148     2874   1906   2935    140    263   -199       N  
ATOM    373  CA  ASP A 148       0.670  35.800  -7.817  1.00 20.85           C  
ANISOU  373  CA  ASP A 148     3150   1738   3032     33      1   -122       C  
ATOM    374  C   ASP A 148       1.434  36.525  -6.709  1.00 21.87           C  
ANISOU  374  C   ASP A 148     3666   1749   2892    -82     91     56       C  
ATOM    375  O   ASP A 148       1.650  37.740  -6.800  1.00 25.45           O  
ANISOU  375  O   ASP A 148     4486   1282   3899   -493     18    -39       O  
ATOM    376  CB  ASP A 148      -0.839  36.031  -7.672  1.00 22.47           C  
ANISOU  376  CB  ASP A 148     3173   1947   3415    168     37   -253       C  
ATOM    377  CG  ASP A 148      -1.621  35.633  -8.915  1.00 22.72           C  
ANISOU  377  CG  ASP A 148     3125   1606   3899    603   -175    235       C  
ATOM    378  OD1 ASP A 148      -1.040  35.621 -10.026  1.00 28.88           O  
ANISOU  378  OD1 ASP A 148     4140   2963   3869    391    349   -192       O  
ATOM    379  OD2 ASP A 148      -2.828  35.333  -8.783  1.00 29.02           O1-
ANISOU  379  OD2 ASP A 148     3442   2625   4959     64    340     -9       O1-
ATOM    380  N   SER A 149       1.817  35.784  -5.667  1.00 22.68           N  
ANISOU  380  N   SER A 149     3546   2028   3043   -258     89   -219       N  
ATOM    381  CA ASER A 149       2.638  36.328  -4.588  0.50 25.24           C  
ANISOU  381  CA ASER A 149     3490   2684   3414    -98     13    -79       C  
ATOM    382  CA BSER A 149       2.592  36.312  -4.541  0.50 25.32           C  
ANISOU  382  CA BSER A 149     3501   2727   3393    -71     16    -78       C  
ATOM    383  C   SER A 149       3.634  35.288  -4.089  1.00 25.15           C  
ANISOU  383  C   SER A 149     3440   2551   3562   -219   -184   -141       C  
ATOM    384  O   SER A 149       3.436  34.085  -4.265  1.00 23.23           O  
ANISOU  384  O   SER A 149     3763   1844   3216   -392    131   -425       O  
ATOM    385  CB ASER A 149       1.773  36.873  -3.444  0.50 27.37           C  
ANISOU  385  CB ASER A 149     3704   3137   3558   -145     59    -60       C  
ATOM    386  CB BSER A 149       1.667  36.658  -3.372  0.50 28.09           C  
ANISOU  386  CB BSER A 149     3843   3308   3521    -15      8    -89       C  
ATOM    387  OG ASER A 149       0.879  35.895  -2.950  0.50 22.78           O  
ANISOU  387  OG ASER A 149     3313   2158   3184     14    243   -492       O  
ATOM    388  OG BSER A 149       0.609  37.501  -3.788  0.50 28.35           O  
ANISOU  388  OG BSER A 149     3778   3217   3774    264    303   -153       O  
ATOM    389  N   THR A 150       4.724  35.767  -3.491  1.00 26.26           N  
ANISOU  389  N   THR A 150     3428   2545   4005   -419   -247    146       N  
ATOM    390  CA  THR A 150       5.817  34.914  -3.029  1.00 28.19           C  
ANISOU  390  CA  THR A 150     3672   3213   3827   -245   -173    247       C  
ATOM    391  C   THR A 150       5.388  33.996  -1.882  1.00 26.92           C  
ANISOU  391  C   THR A 150     3482   2923   3820   -117   -145     68       C  
ATOM    392  O   THR A 150       4.927  34.477  -0.844  1.00 28.43           O  
ANISOU  392  O   THR A 150     4219   2815   3767   -407   -325   -121       O  
ATOM    393  CB  THR A 150       7.040  35.759  -2.583  1.00 30.68           C  
ANISOU  393  CB  THR A 150     3952   3406   4297   -504   -126    274       C  
ATOM    394  CG2 THR A 150       8.279  34.882  -2.429  1.00 37.14           C  
ANISOU  394  CG2 THR A 150     4260   4643   5207    -15     12    196       C  
ATOM    395  OG1 THR A 150       7.303  36.783  -3.551  1.00 31.77           O  
ANISOU  395  OG1 THR A 150     4036   3335   4699   -771     97    270       O  
ATOM    396  N   PRO A 151       5.528  32.668  -2.074  1.00 25.17           N  
ANISOU  396  N   PRO A 151     3393   2751   3417   -294   -188   -169       N  
ATOM    397  CA  PRO A 151       5.261  31.693  -1.015  1.00 24.52           C  
ANISOU  397  CA  PRO A 151     3156   2812   3346    -28   -281   -120       C  
ATOM    398  C   PRO A 151       6.256  31.843   0.144  1.00 24.61           C  
ANISOU  398  C   PRO A 151     3215   2824   3312   -126   -266   -160       C  
ATOM    399  O   PRO A 151       7.357  32.368  -0.063  1.00 26.15           O  
ANISOU  399  O   PRO A 151     3384   3016   3533   -314   -313   -381       O  
ATOM    400  CB  PRO A 151       5.458  30.343  -1.718  1.00 23.44           C  
ANISOU  400  CB  PRO A 151     3717   2106   3083   -335   -760   -289       C  
ATOM    401  CG  PRO A 151       5.383  30.636  -3.174  1.00 27.41           C  
ANISOU  401  CG  PRO A 151     3671   3447   3296   -404    182   -114       C  
ATOM    402  CD  PRO A 151       5.934  32.008  -3.328  1.00 25.52           C  
ANISOU  402  CD  PRO A 151     3622   2755   3317    -70   -136    -20       C  
ATOM    403  N   PRO A 152       5.881  31.382   1.354  1.00 23.31           N  
ANISOU  403  N   PRO A 152     3229   2657   2968     31   -183   -524       N  
ATOM    404  CA  PRO A 152       6.733  31.579   2.532  1.00 24.39           C  
ANISOU  404  CA  PRO A 152     3477   2866   2921   -168   -454   -503       C  
ATOM    405  C   PRO A 152       8.070  30.834   2.451  1.00 23.93           C  
ANISOU  405  C   PRO A 152     3359   2653   3078   -341   -490   -654       C  
ATOM    406  O   PRO A 152       8.210  29.909   1.647  1.00 21.84           O  
ANISOU  406  O   PRO A 152     3019   2318   2961   -505   -450   -913       O  
ATOM    407  CB  PRO A 152       5.879  31.026   3.678  1.00 26.41           C  
ANISOU  407  CB  PRO A 152     3967   2732   3334   -266    -81   -409       C  
ATOM    408  CG  PRO A 152       4.951  30.064   3.032  1.00 28.27           C  
ANISOU  408  CG  PRO A 152     3639   3662   3441   -255   -487    -75       C  
ATOM    409  CD  PRO A 152       4.640  30.662   1.695  1.00 24.40           C  
ANISOU  409  CD  PRO A 152     3444   2777   3050    120     15   -334       C  
ATOM    410  N   PRO A 153       9.055  31.240   3.273  1.00 25.07           N  
ANISOU  410  N   PRO A 153     3467   2979   3077   -151   -492   -679       N  
ATOM    411  CA  PRO A 153      10.340  30.555   3.293  1.00 24.02           C  
ANISOU  411  CA  PRO A 153     3324   2722   3079   -474   -187   -415       C  
ATOM    412  C   PRO A 153      10.184  29.062   3.542  1.00 21.55           C  
ANISOU  412  C   PRO A 153     2621   2725   2841   -878   -311   -694       C  
ATOM    413  O   PRO A 153       9.423  28.646   4.422  1.00 21.78           O  
ANISOU  413  O   PRO A 153     2498   3130   2645   -514   -413   -577       O  
ATOM    414  CB  PRO A 153      11.066  31.211   4.470  0.50 21.80           C  
ANISOU  414  CB  PRO A 153     2481   2842   2959   -594   -348   -382       C  
ATOM    415  CG  PRO A 153      10.477  32.551   4.570  0.50 19.89           C  
ANISOU  415  CG  PRO A 153     2655   2692   2211   -304   -462   -505       C  
ATOM    416  CD  PRO A 153       9.032  32.375   4.216  0.50 19.79           C  
ANISOU  416  CD  PRO A 153     2967   2350   2201   -189   -640   -530       C  
ATOM    417  N   GLY A 154      10.894  28.268   2.751  1.00 23.49           N  
ANISOU  417  N   GLY A 154     2821   3478   2625   -407   -195   -304       N  
ATOM    418  CA  GLY A 154      10.923  26.835   2.947  1.00 20.30           C  
ANISOU  418  CA  GLY A 154     2251   2945   2516   -917   -515   -341       C  
ATOM    419  C   GLY A 154       9.767  26.130   2.275  1.00 17.63           C  
ANISOU  419  C   GLY A 154     2338   2672   1687   -598   -582   -520       C  
ATOM    420  O   GLY A 154       9.540  24.956   2.532  1.00 21.52           O  
ANISOU  420  O   GLY A 154     2575   3229   2369   -713   -530     34       O  
ATOM    421  N   THR A 155       9.044  26.842   1.410  1.00 16.67           N  
ANISOU  421  N   THR A 155     2026   2411   1897   -788     49   -289       N  
ATOM    422  CA  THR A 155       7.986  26.228   0.606  1.00 15.13           C  
ANISOU  422  CA  THR A 155     1961   1808   1980   -539     12   -403       C  
ATOM    423  C   THR A 155       8.568  25.139  -0.287  1.00 14.62           C  
ANISOU  423  C   THR A 155     1520   2364   1669   -545   -195   -235       C  
ATOM    424  O   THR A 155       9.688  25.263  -0.794  1.00 14.51           O  
ANISOU  424  O   THR A 155     1571   2176   1766   -570   -168   -312       O  
ATOM    425  CB  THR A 155       7.232  27.281  -0.216  1.00 15.47           C  
ANISOU  425  CB  THR A 155     1953   1967   1956   -452    -92   -277       C  
ATOM    426  CG2 THR A 155       6.255  26.654  -1.196  1.00 15.73           C  
ANISOU  426  CG2 THR A 155     1862   1898   2216   -337     32   -332       C  
ATOM    427  OG1 THR A 155       6.493  28.117   0.673  1.00 17.95           O  
ANISOU  427  OG1 THR A 155     2093   2253   2471   -164    253   -534       O  
ATOM    428  N   ARG A 156       7.790  24.076  -0.462  1.00 13.46           N  
ANISOU  428  N   ARG A 156     1520   1748   1846   -330   -192   -281       N  
ATOM    429  CA  ARG A 156       8.206  22.896  -1.193  1.00 14.33           C  
ANISOU  429  CA  ARG A 156     1405   2098   1938   -317    -95   -329       C  
ATOM    430  C   ARG A 156       7.191  22.578  -2.273  1.00 11.90           C  
ANISOU  430  C   ARG A 156     1216   1631   1674   -436    -93    -92       C  
ATOM    431  O   ARG A 156       6.027  22.983  -2.179  1.00 13.17           O  
ANISOU  431  O   ARG A 156     1430   1922   1652   -125   -128   -424       O  
ATOM    432  CB  ARG A 156       8.370  21.728  -0.220  1.00 17.01           C  
ANISOU  432  CB  ARG A 156     2269   2113   2082    -63   -764   -177       C  
ATOM    433  CG  ARG A 156       9.567  21.898   0.721  1.00 19.49           C  
ANISOU  433  CG  ARG A 156     2559   2191   2653     83   -985   -224       C  
ATOM    434  CD  ARG A 156       9.353  21.242   2.077  1.00 23.68           C  
ANISOU  434  CD  ARG A 156     3463   3015   2520    862   -670   -473       C  
ATOM    435  NE  ARG A 156       9.189  19.786   2.023  1.00 21.45           N  
ANISOU  435  NE  ARG A 156     3086   3079   1983    887   -651   -128       N  
ATOM    436  CZ  ARG A 156      10.183  18.909   1.896  1.00 19.96           C  
ANISOU  436  CZ  ARG A 156     2887   2768   1928    630   -492    -89       C  
ATOM    437  NH1 ARG A 156      11.438  19.325   1.770  1.00 21.56           N1+
ANISOU  437  NH1 ARG A 156     2977   3110   2103    368   -729   -123       N1+
ATOM    438  NH2 ARG A 156       9.915  17.609   1.877  1.00 20.76           N  
ANISOU  438  NH2 ARG A 156     2763   3210   1916    680   -499     -7       N  
ATOM    439  N   VAL A 157       7.640  21.854  -3.294  1.00 11.22           N  
ANISOU  439  N   VAL A 157     1258   1385   1621   -344   -103    -55       N  
ATOM    440  CA  VAL A 157       6.795  21.475  -4.416  1.00 11.15           C  
ANISOU  440  CA  VAL A 157     1475   1495   1264   -291   -216     26       C  
ATOM    441  C   VAL A 157       6.818  19.957  -4.543  1.00 10.87           C  
ANISOU  441  C   VAL A 157     1465   1430   1234   -241   -140     54       C  
ATOM    442  O   VAL A 157       7.875  19.371  -4.773  1.00 11.27           O  
ANISOU  442  O   VAL A 157     1236   1424   1620   -149    -90     55       O  
ATOM    443  CB  VAL A 157       7.291  22.095  -5.739  1.00 11.88           C  
ANISOU  443  CB  VAL A 157     1724   1269   1518   -522    -37     47       C  
ATOM    444  CG1 VAL A 157       6.293  21.816  -6.858  1.00 13.03           C  
ANISOU  444  CG1 VAL A 157     1842   1600   1507   -253    -79    138       C  
ATOM    445  CG2 VAL A 157       7.526  23.592  -5.583  1.00 14.18           C  
ANISOU  445  CG2 VAL A 157     1873   1568   1943   -368    173    130       C  
ATOM    446  N   ARG A 158       5.651  19.326  -4.396  1.00 10.86           N  
ANISOU  446  N   ARG A 158     1257   1352   1517   -315    -46    -39       N  
ATOM    447  CA  ARG A 158       5.523  17.876  -4.461  1.00 10.93           C  
ANISOU  447  CA  ARG A 158     1414   1406   1333   -360   -115    107       C  
ATOM    448  C   ARG A 158       4.806  17.469  -5.737  1.00 10.11           C  
ANISOU  448  C   ARG A 158     1142   1137   1560   -125    -37     70       C  
ATOM    449  O   ARG A 158       3.828  18.103  -6.132  1.00 11.13           O  
ANISOU  449  O   ARG A 158     1267   1339   1620   -102    -87     13       O  
ATOM    450  CB  ARG A 158       4.729  17.369  -3.255  1.00 11.46           C  
ANISOU  450  CB  ARG A 158     1418   1354   1581   -200    -49    115       C  
ATOM    451  CG  ARG A 158       4.604  15.848  -3.152  1.00 12.36           C  
ANISOU  451  CG  ARG A 158     1635   1471   1589   -260    -44    203       C  
ATOM    452  CD  ARG A 158       3.631  15.423  -2.063  1.00 13.61           C  
ANISOU  452  CD  ARG A 158     1789   1806   1575   -315     -6    145       C  
ATOM    453  NE  ARG A 158       3.995  15.950  -0.747  1.00 14.77           N  
ANISOU  453  NE  ARG A 158     2092   1769   1749     26     82    312       N  
ATOM    454  CZ  ARG A 158       4.718  15.299   0.162  1.00 16.34           C  
ANISOU  454  CZ  ARG A 158     2733   1721   1753    266    266     25       C  
ATOM    455  NH1 ARG A 158       5.184  14.083  -0.082  1.00 18.65           N1+
ANISOU  455  NH1 ARG A 158     3445   2066   1573    266    -74    382       N1+
ATOM    456  NH2 ARG A 158       4.971  15.870   1.329  1.00 22.76           N  
ANISOU  456  NH2 ARG A 158     3711   3141   1797    668   -134   -115       N  
ATOM    457  N   ALA A 159       5.287  16.387  -6.350  1.00 10.59           N  
ANISOU  457  N   ALA A 159     1501   1192   1331   -246    -45     89       N  
ATOM    458  CA  ALA A 159       4.598  15.744  -7.470  1.00 10.85           C  
ANISOU  458  CA  ALA A 159     1581   1131   1409   -284    -21    193       C  
ATOM    459  C   ALA A 159       4.280  14.307  -7.102  1.00 10.62           C  
ANISOU  459  C   ALA A 159     1467   1178   1388   -287      6     89       C  
ATOM    460  O   ALA A 159       5.119  13.602  -6.541  1.00 11.51           O  
ANISOU  460  O   ALA A 159     1447   1297   1629   -146   -105    223       O  
ATOM    461  CB  ALA A 159       5.442  15.788  -8.742  1.00 11.35           C  
ANISOU  461  CB  ALA A 159     1410   1321   1582   -251     71    203       C  
ATOM    462  N   MET A 160       3.063  13.884  -7.436  1.00 10.27           N  
ANISOU  462  N   MET A 160     1457    980   1463   -306    -79    102       N  
ATOM    463  CA AMET A 160       2.576  12.543  -7.151  0.50 12.73           C  
ANISOU  463  CA AMET A 160     1788   1413   1635   -391   -276     98       C  
ATOM    464  CA BMET A 160       2.602  12.523  -7.178  0.50 10.50           C  
ANISOU  464  CA BMET A 160     1556   1013   1418   -312   -228    217       C  
ATOM    465  C   MET A 160       1.652  12.130  -8.288  1.00 10.98           C  
ANISOU  465  C   MET A 160     1646   1062   1463   -412   -101    208       C  
ATOM    466  O   MET A 160       0.917  12.963  -8.813  1.00 13.20           O  
ANISOU  466  O   MET A 160     1915   1139   1960   -129   -640    227       O  
ATOM    467  CB AMET A 160       1.799  12.569  -5.835  0.50 15.30           C  
ANISOU  467  CB AMET A 160     2252   1744   1813   -492      8    233       C  
ATOM    468  CB BMET A 160       1.876  12.432  -5.831  0.50 12.03           C  
ANISOU  468  CB BMET A 160     1852   1337   1378   -594    -39    393       C  
ATOM    469  CG AMET A 160       1.154  11.267  -5.406  0.50 16.49           C  
ANISOU  469  CG AMET A 160     2278   1547   2438     67    -64    368       C  
ATOM    470  CG BMET A 160       1.374  11.038  -5.461  0.50 14.17           C  
ANISOU  470  CG BMET A 160     1687   1850   1844   -468     -7    -33       C  
ATOM    471  SD AMET A 160       0.108  11.560  -3.970  0.50 22.80           S  
ANISOU  471  SD AMET A 160     2664   3892   2105  -1004    305   -507       S  
ATOM    472  SD BMET A 160       0.431  11.041  -3.926  0.50 13.19           S  
ANISOU  472  SD BMET A 160     1758   1334   1918   -204    142    441       S  
ATOM    473  CE AMET A 160       1.338  11.819  -2.689  0.50 22.94           C  
ANISOU  473  CE AMET A 160     2015   3822   2877   -181     55   -250       C  
ATOM    474  CE BMET A 160       1.746  11.141  -2.718  0.50 14.66           C  
ANISOU  474  CE BMET A 160     2076   1690   1803     49    -21    379       C  
ATOM    475  N   ALA A 161       1.686  10.856  -8.653  1.00 10.92           N  
ANISOU  475  N   ALA A 161     1550   1117   1481   -280   -198    128       N  
ATOM    476  CA  ALA A 161       0.762  10.318  -9.648  1.00 11.30           C  
ANISOU  476  CA  ALA A 161     1644   1110   1539   -358   -278     94       C  
ATOM    477  C   ALA A 161      -0.353   9.527  -8.971  1.00 11.27           C  
ANISOU  477  C   ALA A 161     1695   1065   1521   -429   -369     73       C  
ATOM    478  O   ALA A 161      -0.107   8.822  -7.993  1.00 13.21           O  
ANISOU  478  O   ALA A 161     1985   1423   1611   -518   -390    479       O  
ATOM    479  CB  ALA A 161       1.503   9.429 -10.623  1.00 13.25           C  
ANISOU  479  CB  ALA A 161     2017   1453   1563   -292   -181    -73       C  
ATOM    480  N   ILE A 162      -1.572   9.650  -9.499  1.00 11.60           N  
ANISOU  480  N   ILE A 162     1646   1106   1653   -412   -307    114       N  
ATOM    481  CA  ILE A 162      -2.699   8.798  -9.116  1.00 12.78           C  
ANISOU  481  CA  ILE A 162     1788   1485   1583   -481   -133     42       C  
ATOM    482  C   ILE A 162      -3.417   8.354 -10.379  1.00 12.07           C  
ANISOU  482  C   ILE A 162     1557   1541   1485   -329    -81    121       C  
ATOM    483  O   ILE A 162      -3.296   8.993 -11.423  1.00 13.00           O  
ANISOU  483  O   ILE A 162     1845   1598   1496   -548   -219    293       O  
ATOM    484  CB  ILE A 162      -3.713   9.506  -8.161  1.00 13.75           C  
ANISOU  484  CB  ILE A 162     2037   1417   1769   -176   -132    190       C  
ATOM    485  CG1 ILE A 162      -4.411  10.693  -8.840  1.00 14.31           C  
ANISOU  485  CG1 ILE A 162     1952   1630   1856   -215     38    -97       C  
ATOM    486  CG2 ILE A 162      -3.035   9.918  -6.863  1.00 16.33           C  
ANISOU  486  CG2 ILE A 162     2426   2063   1713   -211   -283   -172       C  
ATOM    487  CD1 ILE A 162      -5.662  11.177  -8.117  1.00 16.89           C  
ANISOU  487  CD1 ILE A 162     1825   2173   2416   -255    -10   -112       C  
ATOM    488  N   TYR A 163      -4.166   7.260 -10.297  1.00 12.11           N  
ANISOU  488  N   TYR A 163     1514   1500   1585   -475    -87     59       N  
ATOM    489  CA  TYR A 163      -5.026   6.898 -11.418  1.00 12.86           C  
ANISOU  489  CA  TYR A 163     1527   1636   1724   -413   -109     62       C  
ATOM    490  C   TYR A 163      -6.188   7.868 -11.531  1.00 14.29           C  
ANISOU  490  C   TYR A 163     1643   1911   1875   -706   -155   -107       C  
ATOM    491  O   TYR A 163      -6.747   8.291 -10.524  1.00 16.23           O  
ANISOU  491  O   TYR A 163     1975   2015   2176   -198   -186   -264       O  
ATOM    492  CB  TYR A 163      -5.517   5.451 -11.301  1.00 14.01           C  
ANISOU  492  CB  TYR A 163     1879   1570   1875   -615   -115   -102       C  
ATOM    493  CG  TYR A 163      -4.399   4.483 -11.582  1.00 12.96           C  
ANISOU  493  CG  TYR A 163     1769   1384   1770   -480     48    162       C  
ATOM    494  CD1 TYR A 163      -3.877   4.354 -12.870  1.00 14.11           C  
ANISOU  494  CD1 TYR A 163     2132   1368   1859   -474     41    -42       C  
ATOM    495  CD2 TYR A 163      -3.816   3.744 -10.561  1.00 13.77           C  
ANISOU  495  CD2 TYR A 163     1983   1347   1900   -592    -26     70       C  
ATOM    496  CE1 TYR A 163      -2.825   3.498 -13.137  1.00 15.07           C  
ANISOU  496  CE1 TYR A 163     2137   1280   2308   -281     63    -34       C  
ATOM    497  CE2 TYR A 163      -2.768   2.868 -10.823  1.00 13.91           C  
ANISOU  497  CE2 TYR A 163     1804   1499   1981   -542    160    119       C  
ATOM    498  CZ  TYR A 163      -2.270   2.763 -12.111  1.00 14.92           C  
ANISOU  498  CZ  TYR A 163     1944   1568   2155   -268    168    121       C  
ATOM    499  OH  TYR A 163      -1.220   1.917 -12.378  1.00 17.24           O  
ANISOU  499  OH  TYR A 163     2205   2086   2256   -155    117    -95       O  
ATOM    500  N   LYS A 164      -6.544   8.207 -12.768  1.00 14.78           N  
ANISOU  500  N   LYS A 164     1820   1774   2020   -516   -346     78       N  
ATOM    501  CA  LYS A 164      -7.638   9.136 -13.044  1.00 17.26           C  
ANISOU  501  CA  LYS A 164     1749   2290   2518   -311   -145    134       C  
ATOM    502  C   LYS A 164      -9.008   8.523 -12.754  1.00 17.31           C  
ANISOU  502  C   LYS A 164     2035   1973   2570   -197   -377    188       C  
ATOM    503  O   LYS A 164      -9.898   9.198 -12.241  1.00 19.69           O  
ANISOU  503  O   LYS A 164     1791   2207   3481   -138    -60    133       O  
ATOM    504  CB  LYS A 164      -7.563   9.612 -14.495  1.00 18.30           C  
ANISOU  504  CB  LYS A 164     2054   2407   2490   -275   -512    311       C  
ATOM    505  CG  LYS A 164      -8.654  10.598 -14.888  1.00 21.60           C  
ANISOU  505  CG  LYS A 164     2365   2737   3104    -79   -266    450       C  
ATOM    506  CD  LYS A 164      -8.546  10.998 -16.345  1.00 25.96           C  
ANISOU  506  CD  LYS A 164     3331   3533   3000    481   -279    626       C  
ATOM    507  CE  LYS A 164      -9.723  11.866 -16.756  1.00 28.00           C  
ANISOU  507  CE  LYS A 164     3953   3270   3415    418   -538    753       C  
ATOM    508  NZ  LYS A 164      -9.654  12.246 -18.196  1.00 31.24           N1+
ANISOU  508  NZ  LYS A 164     3697   4742   3428    230   -143    543       N1+
ATOM    509  N   GLN A 165      -9.174   7.246 -13.083  1.00 17.31           N  
ANISOU  509  N   GLN A 165     1935   1779   2863   -398   -294    210       N  
ATOM    510  CA  GLN A 165     -10.464   6.581 -12.924  1.00 18.60           C  
ANISOU  510  CA  GLN A 165     1971   2231   2862   -414   -240     -3       C  
ATOM    511  C   GLN A 165     -10.720   6.240 -11.469  1.00 16.98           C  
ANISOU  511  C   GLN A 165     1568   1875   3005   -581     33   -249       C  
ATOM    512  O   GLN A 165      -9.881   5.615 -10.822  1.00 18.41           O  
ANISOU  512  O   GLN A 165     1903   2066   3027   -380    -70     42       O  
ATOM    513  CB  GLN A 165     -10.517   5.303 -13.749  1.00 20.89           C  
ANISOU  513  CB  GLN A 165     2628   2319   2988   -686   -241   -297       C  
ATOM    514  CG  GLN A 165     -10.423   5.506 -15.238  1.00 21.21           C  
ANISOU  514  CG  GLN A 165     2286   2614   3160   -313   -433    144       C  
ATOM    515  CD  GLN A 165     -10.121   4.211 -15.940  1.00 29.30           C  
ANISOU  515  CD  GLN A 165     3820   3196   4117    -91    127   -337       C  
ATOM    516  NE2 GLN A 165      -8.843   3.957 -16.175  1.00 26.23           N  
ANISOU  516  NE2 GLN A 165     3372   3034   3559   -748   -457   -534       N  
ATOM    517  OE1 GLN A 165     -11.023   3.435 -16.256  1.00 37.54           O  
ANISOU  517  OE1 GLN A 165     4290   4691   5281   -768   -402   -673       O  
ATOM    518  N   SER A 166     -11.894   6.634 -10.977  1.00 21.28           N  
ANISOU  518  N   SER A 166     2076   2559   3447   -392    135   -306       N  
ATOM    519  CA ASER A 166     -12.284   6.387  -9.590  0.50 20.94           C  
ANISOU  519  CA ASER A 166     2211   2476   3266    -61    154   -127       C  
ATOM    520  CA BSER A 166     -12.282   6.387  -9.590  0.50 21.82           C  
ANISOU  520  CA BSER A 166     2357   2612   3320    -94    162   -109       C  
ATOM    521  C   SER A 166     -12.083   4.927  -9.188  1.00 20.37           C  
ANISOU  521  C   SER A 166     2170   2489   3079   -426    185   -223       C  
ATOM    522  O   SER A 166     -11.604   4.639  -8.086  1.00 21.46           O  
ANISOU  522  O   SER A 166     2581   2553   3019   -232    326   -293       O  
ATOM    523  CB ASER A 166     -13.741   6.801  -9.363  0.50 21.72           C  
ANISOU  523  CB ASER A 166     2514   2387   3349    123    154   -348       C  
ATOM    524  CB BSER A 166     -13.737   6.806  -9.356  0.50 24.40           C  
ANISOU  524  CB BSER A 166     2752   3024   3492    125    250   -189       C  
ATOM    525  OG ASER A 166     -14.132   6.590  -8.016  0.50 26.72           O  
ANISOU  525  OG ASER A 166     3206   3351   3594    215     35    125       O  
ATOM    526  OG BSER A 166     -14.625   6.065 -10.175  0.50 30.57           O  
ANISOU  526  OG BSER A 166     3392   4093   4129   -234     98   -278       O  
ATOM    527  N   GLN A 167     -12.431   4.015 -10.096  0.50 12.88           N  
ANISOU  527  N   GLN A 167     1020   1328   2546   -280    392   -386       N  
ATOM    528  CA AGLN A 167     -12.383   2.582  -9.811  0.50 19.20           C  
ANISOU  528  CA AGLN A 167     2287   2018   2988   -324     43   -173       C  
ATOM    529  CA BGLN A 167     -12.382   2.581  -9.821  0.50 18.86           C  
ANISOU  529  CA BGLN A 167     2228   1938   2997   -374     68   -203       C  
ATOM    530  C   GLN A 167     -10.970   2.049  -9.577  0.50 12.58           C  
ANISOU  530  C   GLN A 167     1381   1526   1873   -501    156   -448       C  
ATOM    531  O   GLN A 167     -10.808   0.959  -9.034  0.50 13.60           O  
ANISOU  531  O   GLN A 167     1554   1422   2188   -592    269    -73       O  
ATOM    532  CB AGLN A 167     -13.072   1.787 -10.920  0.50 20.39           C  
ANISOU  532  CB AGLN A 167     2583   2117   3047   -379   -131   -244       C  
ATOM    533  CB BGLN A 167     -13.061   1.785 -10.940  0.50 20.62           C  
ANISOU  533  CB BGLN A 167     2570   2143   3122   -405   -162   -254       C  
ATOM    534  CG AGLN A 167     -12.350   1.832 -12.253  0.50 18.96           C  
ANISOU  534  CG AGLN A 167     2551   1804   2846   -190   -149    -63       C  
ATOM    535  CG BGLN A 167     -12.497   2.034 -12.332  0.50 23.59           C  
ANISOU  535  CG BGLN A 167     2834   2932   3198   -266     18   -177       C  
ATOM    536  CD AGLN A 167     -13.144   1.209 -13.386  0.50 22.76           C  
ANISOU  536  CD AGLN A 167     2861   2855   2928    -56   -143    -57       C  
ATOM    537  CD BGLN A 167     -13.290   3.060 -13.131  0.50 25.74           C  
ANISOU  537  CD BGLN A 167     2831   3570   3377    -96     64    -16       C  
ATOM    538  NE2AGLN A 167     -14.450   1.457 -13.413  0.50 28.64           N  
ANISOU  538  NE2AGLN A 167     3181   3988   3713     39   -254    -77       N  
ATOM    539  OE1AGLN A 167     -12.584   0.518 -14.233  0.50 22.55           O  
ANISOU  539  OE1AGLN A 167     3385   2144   3039   -190   -454   -439       O  
ATOM    540  NE2BGLN A 167     -13.532   2.749 -14.400  0.50 28.41           N  
ANISOU  540  NE2BGLN A 167     3630   3537   3626     84   -205   -158       N  
ATOM    541  OE1BGLN A 167     -13.673   4.118 -12.622  0.50 22.94           O  
ANISOU  541  OE1BGLN A 167     2251   3258   3207   -564   -149     11       O  
ATOM    542  N   HIS A 168      -9.951   2.813  -9.985  1.00 16.36           N  
ANISOU  542  N   HIS A 168     1817   1735   2662   -477    106   -228       N  
ATOM    543  CA  HIS A 168      -8.558   2.404  -9.774  1.00 16.15           C  
ANISOU  543  CA  HIS A 168     2061   1887   2187   -107    295   -304       C  
ATOM    544  C   HIS A 168      -7.791   3.330  -8.841  1.00 15.81           C  
ANISOU  544  C   HIS A 168     1817   2075   2115   -286    517   -286       C  
ATOM    545  O   HIS A 168      -6.604   3.131  -8.597  1.00 16.40           O  
ANISOU  545  O   HIS A 168     1907   2054   2269   -299    431   -194       O  
ATOM    546  CB  HIS A 168      -7.817   2.301 -11.106  1.00 16.57           C  
ANISOU  546  CB  HIS A 168     1904   2339   2052   -335    162   -225       C  
ATOM    547  CG  HIS A 168      -8.472   1.386 -12.084  1.00 17.55           C  
ANISOU  547  CG  HIS A 168     2244   1827   2597   -453    -72   -536       C  
ATOM    548  CD2 HIS A 168      -8.828   1.575 -13.375  1.00 19.39           C  
ANISOU  548  CD2 HIS A 168     2827   2116   2425   -226   -148   -382       C  
ATOM    549  ND1 HIS A 168      -8.846   0.100 -11.764  1.00 18.19           N  
ANISOU  549  ND1 HIS A 168     2291   1865   2752   -241    417   -420       N  
ATOM    550  CE1 HIS A 168      -9.399  -0.467 -12.821  1.00 19.21           C  
ANISOU  550  CE1 HIS A 168     2585   2433   2279   -341    181   -406       C  
ATOM    551  NE2 HIS A 168      -9.400   0.407 -13.811  1.00 20.01           N  
ANISOU  551  NE2 HIS A 168     2904   2124   2571   -171   -238   -677       N  
ATOM    552  N   MET A 169      -8.474   4.326  -8.298  1.00 16.74           N  
ANISOU  552  N   MET A 169     1977   2050   2332   -537    292   -278       N  
ATOM    553  CA  MET A 169      -7.790   5.367  -7.540  1.00 17.35           C  
ANISOU  553  CA  MET A 169     2250   1982   2358   -513    285    -52       C  
ATOM    554  C   MET A 169      -7.070   4.918  -6.279  1.00 17.38           C  
ANISOU  554  C   MET A 169     2453   2138   2011   -522    594     48       C  
ATOM    555  O   MET A 169      -6.105   5.553  -5.867  1.00 18.09           O  
ANISOU  555  O   MET A 169     2548   2242   2081   -758    259   -251       O  
ATOM    556  CB  MET A 169      -8.742   6.491  -7.206  1.00 19.47           C  
ANISOU  556  CB  MET A 169     2843   1888   2666   -413    142   -264       C  
ATOM    557  CG  MET A 169      -8.818   7.505  -8.280  1.00 25.27           C  
ANISOU  557  CG  MET A 169     3198   2985   3418      2     94     98       C  
ATOM    558  SD  MET A 169      -9.619   8.930  -7.602  1.00 27.95           S  
ANISOU  558  SD  MET A 169     3758   2511   4347     18    432    358       S  
ATOM    559  CE  MET A 169      -9.649   9.983  -9.043  1.00 27.70           C  
ANISOU  559  CE  MET A 169     3758   3007   3757    -94   -328     68       C  
ATOM    560  N   THR A 170      -7.536   3.834  -5.666  1.00 18.56           N  
ANISOU  560  N   THR A 170     2553   2450   2046   -430    613     53       N  
ATOM    561  CA  THR A 170      -6.872   3.321  -4.469  1.00 19.89           C  
ANISOU  561  CA  THR A 170     2738   2633   2185   -161    423    240       C  
ATOM    562  C   THR A 170      -5.587   2.563  -4.794  1.00 18.87           C  
ANISOU  562  C   THR A 170     2614   2424   2129   -324    338    157       C  
ATOM    563  O   THR A 170      -4.813   2.243  -3.889  1.00 23.61           O  
ANISOU  563  O   THR A 170     2903   3854   2214     84    126    227       O  
ATOM    564  CB  THR A 170      -7.790   2.418  -3.627  1.00 21.25           C  
ANISOU  564  CB  THR A 170     2646   2893   2535   -286    645    291       C  
ATOM    565  CG2 THR A 170      -9.079   3.142  -3.254  1.00 24.60           C  
ANISOU  565  CG2 THR A 170     2775   3419   3153   -171    652    172       C  
ATOM    566  OG1 THR A 170      -8.105   1.236  -4.367  1.00 23.69           O  
ANISOU  566  OG1 THR A 170     2895   3077   3029   -436    753    -77       O  
ATOM    567  N   GLU A 171      -5.359   2.277  -6.077  1.00 17.29           N  
ANISOU  567  N   GLU A 171     2344   2127   2098   -495    281    242       N  
ATOM    568  CA  GLU A 171      -4.136   1.598  -6.494  1.00 16.86           C  
ANISOU  568  CA  GLU A 171     1996   2003   2407   -267    146    330       C  
ATOM    569  C   GLU A 171      -2.985   2.591  -6.570  1.00 15.92           C  
ANISOU  569  C   GLU A 171     2148   1821   2078   -179     71    196       C  
ATOM    570  O   GLU A 171      -3.127   3.675  -7.134  1.00 18.58           O  
ANISOU  570  O   GLU A 171     2606   1744   2709   -188     40    821       O  
ATOM    571  CB  GLU A 171      -4.311   0.906  -7.849  1.00 18.62           C  
ANISOU  571  CB  GLU A 171     2338   2237   2497   -314     -1   -151       C  
ATOM    572  CG  GLU A 171      -5.407  -0.162  -7.887  1.00 22.36           C  
ANISOU  572  CG  GLU A 171     2689   2148   3656   -328     92    227       C  
ATOM    573  CD  GLU A 171      -5.125  -1.374  -7.000  1.00 26.88           C  
ANISOU  573  CD  GLU A 171     3419   2485   4308   -525     39    272       C  
ATOM    574  OE1 GLU A 171      -3.943  -1.677  -6.732  1.00 28.96           O  
ANISOU  574  OE1 GLU A 171     4004   2719   4278    180   -686   -101       O  
ATOM    575  OE2 GLU A 171      -6.100  -2.040  -6.585  1.00 30.86           O1-
ANISOU  575  OE2 GLU A 171     3936   3316   4472   -443    105     93       O1-
ATOM    576  N   VAL A 172      -1.846   2.218  -6.000  1.00 15.17           N  
ANISOU  576  N   VAL A 172     2157   1528   2077   -391    120    168       N  
ATOM    577  CA  VAL A 172      -0.661   3.066  -6.030  1.00 13.92           C  
ANISOU  577  CA  VAL A 172     1959   1480   1850   -135    161    174       C  
ATOM    578  C   VAL A 172      -0.018   2.993  -7.410  1.00 13.18           C  
ANISOU  578  C   VAL A 172     2082   1102   1822    -43    -63     79       C  
ATOM    579  O   VAL A 172       0.199   1.902  -7.941  1.00 15.65           O  
ANISOU  579  O   VAL A 172     2755   1225   1965    -56    189    143       O  
ATOM    580  CB  VAL A 172       0.349   2.645  -4.942  1.00 15.57           C  
ANISOU  580  CB  VAL A 172     2230   1870   1814     78    138    422       C  
ATOM    581  CG1 VAL A 172       1.659   3.421  -5.074  1.00 16.73           C  
ANISOU  581  CG1 VAL A 172     2585   1670   2101   -156   -353    306       C  
ATOM    582  CG2 VAL A 172      -0.261   2.829  -3.555  1.00 17.17           C  
ANISOU  582  CG2 VAL A 172     2892   1823   1808    202    157    273       C  
ATOM    583  N   VAL A 173       0.265   4.153  -7.988  1.00 12.13           N  
ANISOU  583  N   VAL A 173     1888   1172   1546   -133     73     73       N  
ATOM    584  CA  VAL A 173       0.966   4.224  -9.262  1.00 13.02           C  
ANISOU  584  CA  VAL A 173     2106   1071   1769    -53     65     26       C  
ATOM    585  C   VAL A 173       2.453   3.990  -9.019  1.00 13.49           C  
ANISOU  585  C   VAL A 173     2075   1501   1547      1    351    -64       C  
ATOM    586  O   VAL A 173       3.099   4.713  -8.260  1.00 14.19           O  
ANISOU  586  O   VAL A 173     2017   1619   1753   -153     40    -45       O  
ATOM    587  CB  VAL A 173       0.754   5.590  -9.947  1.00 12.52           C  
ANISOU  587  CB  VAL A 173     1924   1134   1699     23    118     50       C  
ATOM    588  CG1 VAL A 173       1.522   5.647 -11.258  1.00 14.33           C  
ANISOU  588  CG1 VAL A 173     2220   1612   1613    -98    367     49       C  
ATOM    589  CG2 VAL A 173      -0.730   5.838 -10.185  1.00 12.97           C  
ANISOU  589  CG2 VAL A 173     1684   1390   1853   -231   -141    238       C  
ATOM    590  N   ARG A 174       2.987   2.959  -9.662  1.00 14.75           N  
ANISOU  590  N   ARG A 174     2266   1616   1720    191     95     64       N  
ATOM    591  CA  ARG A 174       4.397   2.618  -9.542  1.00 15.82           C  
ANISOU  591  CA  ARG A 174     2464   1803   1742    342    -25   -140       C  
ATOM    592  C   ARG A 174       4.879   2.033 -10.856  1.00 15.61           C  
ANISOU  592  C   ARG A 174     2372   1751   1807    507     37     -4       C  
ATOM    593  O   ARG A 174       4.077   1.691 -11.732  1.00 17.02           O  
ANISOU  593  O   ARG A 174     2726   1918   1822    131     81   -149       O  
ATOM    594  CB  ARG A 174       4.632   1.622  -8.395  1.00 18.09           C  
ANISOU  594  CB  ARG A 174     2702   2237   1932    507   -131    -68       C  
ATOM    595  CG  ARG A 174       3.899   0.292  -8.541  1.00 20.36           C  
ANISOU  595  CG  ARG A 174     3105   2064   2566      9     92    255       C  
ATOM    596  CD  ARG A 174       4.079  -0.590  -7.309  1.00 23.66           C  
ANISOU  596  CD  ARG A 174     3242   2746   3002    284     59    596       C  
ATOM    597  NE  ARG A 174       5.448  -1.092  -7.176  1.00 26.39           N  
ANISOU  597  NE  ARG A 174     3987   3038   3002    255    -23    294       N  
ATOM    598  CZ  ARG A 174       5.912  -1.761  -6.122  1.00 26.44           C  
ANISOU  598  CZ  ARG A 174     3446   3201   3398    567    -61    175       C  
ATOM    599  NH1 ARG A 174       5.129  -2.015  -5.082  1.00 31.47           N1+
ANISOU  599  NH1 ARG A 174     4541   3621   3795    282    139    662       N1+
ATOM    600  NH2 ARG A 174       7.172  -2.170  -6.106  1.00 29.56           N  
ANISOU  600  NH2 ARG A 174     3705   4113   3413    302   -269    213       N  
ATOM    601  N   ARG A 175       6.189   1.909 -10.986  1.00 16.28           N  
ANISOU  601  N   ARG A 175     2807   1589   1789    687    254    -14       N  
ATOM    602  CA AARG A 175       6.776   1.338 -12.189  0.60 16.04           C  
ANISOU  602  CA AARG A 175     2812   1513   1770    378    188    -30       C  
ATOM    603  CA BARG A 175       6.767   1.339 -12.194  0.40 16.21           C  
ANISOU  603  CA BARG A 175     2658   1630   1870    326    189    -35       C  
ATOM    604  C   ARG A 175       6.451  -0.143 -12.318  1.00 16.19           C  
ANISOU  604  C   ARG A 175     2566   1573   2011    450    202     79       C  
ATOM    605  O   ARG A 175       6.279  -0.841 -11.314  1.00 18.40           O  
ANISOU  605  O   ARG A 175     3633   1513   1842    674    370    143       O  
ATOM    606  CB AARG A 175       8.284   1.552 -12.198  0.60 16.52           C  
ANISOU  606  CB AARG A 175     2571   1438   2266    307    289   -125       C  
ATOM    607  CB BARG A 175       8.272   1.569 -12.232  0.40 16.54           C  
ANISOU  607  CB BARG A 175     2454   1702   2127    236    135    -35       C  
ATOM    608  CG AARG A 175       8.693   3.010 -12.292  0.60 15.80           C  
ANISOU  608  CG AARG A 175     3034   1413   1557    439   -262    -25       C  
ATOM    609  CG BARG A 175       8.654   3.024 -12.398  0.40 18.54           C  
ANISOU  609  CG BARG A 175     2818   1806   2420    229    243    -48       C  
ATOM    610  CD AARG A 175      10.194   3.139 -12.418  0.60 15.71           C  
ANISOU  610  CD AARG A 175     2595   1349   2023     38    466     65       C  
ATOM    611  CD BARG A 175       9.907   3.147 -13.229  0.40 14.85           C  
ANISOU  611  CD BARG A 175     1488   1804   2349   -276    -41    688       C  
ATOM    612  NE AARG A 175      10.672   2.915 -13.782  0.60 16.85           N  
ANISOU  612  NE AARG A 175     2754   1311   2334    231    247     54       N  
ATOM    613  NE BARG A 175      11.122   2.868 -12.468  0.40 18.05           N  
ANISOU  613  NE BARG A 175     1870   2620   2366    340   -286   -183       N  
ATOM    614  CZ AARG A 175      11.956   2.888 -14.128  0.60 17.34           C  
ANISOU  614  CZ AARG A 175     2185   1776   2625    549    291   -134       C  
ATOM    615  CZ BARG A 175      12.340   2.786 -12.998  0.40 14.59           C  
ANISOU  615  CZ BARG A 175     1903   1427   2212   -297    121   -380       C  
ATOM    616  NH1AARG A 175      12.906   3.036 -13.211  0.60 23.83           N1+
ANISOU  616  NH1AARG A 175     2810   3294   2950    102   -122   -137       N1+
ATOM    617  NH2AARG A 175      12.296   2.701 -15.394  0.60 20.60           N  
ANISOU  617  NH2AARG A 175     3455   2264   2107    328    107     28       N  
ATOM    618  NH1BARG A 175      12.528   2.962 -14.301  0.40 22.55           N1+
ANISOU  618  NH1BARG A 175     4094   1729   2743     24      9   -332       N1+
ATOM    619  NH2BARG A 175      13.378   2.532 -12.217  0.40 16.47           N  
ANISOU  619  NH2BARG A 175     2432   1514   2310     58    -65   -241       N  
ATOM    620  N   CYS A 176       6.368  -0.611 -13.558  1.00 16.03           N  
ANISOU  620  N   CYS A 176     2788   1479   1821    369    263    -28       N  
ATOM    621  CA  CYS A 176       6.101  -2.014 -13.843  1.00 16.55           C  
ANISOU  621  CA  CYS A 176     2801   1377   2109    309    279     50       C  
ATOM    622  C   CYS A 176       7.283  -2.877 -13.393  1.00 17.24           C  
ANISOU  622  C   CYS A 176     3053   1695   1799    281    216    -55       C  
ATOM    623  O   CYS A 176       8.376  -2.352 -13.162  1.00 17.62           O  
ANISOU  623  O   CYS A 176     3053   1784   1855    481    208   -124       O  
ATOM    624  CB  CYS A 176       5.830  -2.192 -15.340  1.00 17.07           C  
ANISOU  624  CB  CYS A 176     3056   1623   1806     81    477    182       C  
ATOM    625  SG  CYS A 176       7.284  -2.012 -16.411  1.00 15.86           S  
ANISOU  625  SG  CYS A 176     2815   1365   1844    253    217    -15       S  
ATOM    626  N   PRO A 177       7.072  -4.201 -13.253  1.00 18.80           N  
ANISOU  626  N   PRO A 177     3261   1466   2415    492    160    -35       N  
ATOM    627  CA  PRO A 177       8.169  -5.060 -12.809  1.00 21.19           C  
ANISOU  627  CA  PRO A 177     3352   1922   2778    528    333    171       C  
ATOM    628  C   PRO A 177       9.431  -4.939 -13.666  1.00 19.63           C  
ANISOU  628  C   PRO A 177     3165   1936   2354    601     65    157       C  
ATOM    629  O   PRO A 177      10.534  -4.882 -13.119  1.00 21.91           O  
ANISOU  629  O   PRO A 177     3590   2376   2360    883   -251   -173       O  
ATOM    630  CB  PRO A 177       7.573  -6.467 -12.912  1.00 22.46           C  
ANISOU  630  CB  PRO A 177     3534   1638   3361    514    331    212       C  
ATOM    631  CG  PRO A 177       6.111  -6.253 -12.714  1.00 22.37           C  
ANISOU  631  CG  PRO A 177     3417   1961   3119    325    394    365       C  
ATOM    632  CD  PRO A 177       5.826  -4.968 -13.440  1.00 22.91           C  
ANISOU  632  CD  PRO A 177     3484   2112   3109    134     94    173       C  
ATOM    633  N   HIS A 178       9.274  -4.872 -14.987  1.00 19.52           N  
ANISOU  633  N   HIS A 178     3296   1856   2264    747    177     54       N  
ATOM    634  CA  HIS A 178      10.433  -4.796 -15.874  1.00 20.14           C  
ANISOU  634  CA  HIS A 178     2720   2571   2362    828    129   -142       C  
ATOM    635  C   HIS A 178      11.272  -3.550 -15.604  1.00 21.63           C  
ANISOU  635  C   HIS A 178     2858   3004   2354    412     98    -75       C  
ATOM    636  O   HIS A 178      12.492  -3.636 -15.451  1.00 23.89           O  
ANISOU  636  O   HIS A 178     3032   3416   2629    231   -363   -320       O  
ATOM    637  CB  HIS A 178      10.022  -4.843 -17.348  1.00 22.62           C  
ANISOU  637  CB  HIS A 178     3095   3374   2126    421     46   -249       C  
ATOM    638  CG  HIS A 178      11.148  -4.548 -18.289  1.00 24.10           C  
ANISOU  638  CG  HIS A 178     3074   3923   2157    398    118   -401       C  
ATOM    639  CD2 HIS A 178      11.584  -3.380 -18.818  1.00 27.21           C  
ANISOU  639  CD2 HIS A 178     3923   4007   2407     88     55   -401       C  
ATOM    640  ND1 HIS A 178      11.995  -5.525 -18.767  1.00 26.80           N  
ANISOU  640  ND1 HIS A 178     3377   4143   2659    789   -273   -109       N  
ATOM    641  CE1 HIS A 178      12.898  -4.974 -19.558  1.00 30.01           C  
ANISOU  641  CE1 HIS A 178     3528   4097   3775    -34   -223    124       C  
ATOM    642  NE2 HIS A 178      12.670  -3.674 -19.607  1.00 26.84           N  
ANISOU  642  NE2 HIS A 178     3139   4071   2985    103    -36   -479       N  
ATOM    643  N   HIS A 179      10.609  -2.397 -15.545  1.00 20.22           N  
ANISOU  643  N   HIS A 179     2923   2722   2038    225   -256   -175       N  
ATOM    644  CA  HIS A 179      11.304  -1.128 -15.354  1.00 20.36           C  
ANISOU  644  CA  HIS A 179     2835   2658   2241    -26   -259    175       C  
ATOM    645  C   HIS A 179      11.840  -0.940 -13.933  1.00 22.01           C  
ANISOU  645  C   HIS A 179     3177   2738   2446    142   -192    331       C  
ATOM    646  O   HIS A 179      12.875  -0.302 -13.739  1.00 24.43           O  
ANISOU  646  O   HIS A 179     3171   3449   2660    -63   -809    383       O  
ATOM    647  CB  HIS A 179      10.418   0.046 -15.773  1.00 21.32           C  
ANISOU  647  CB  HIS A 179     3348   2680   2071     36   -526    388       C  
ATOM    648  CG  HIS A 179      10.375   0.268 -17.252  1.00 20.27           C  
ANISOU  648  CG  HIS A 179     2644   2859   2198   -162   -119    358       C  
ATOM    649  CD2 HIS A 179      11.368   0.500 -18.143  1.00 24.66           C  
ANISOU  649  CD2 HIS A 179     2652   3827   2889    -49     25     -1       C  
ATOM    650  ND1 HIS A 179       9.202   0.250 -17.978  1.00 18.74           N  
ANISOU  650  ND1 HIS A 179     3036   1895   2189   -124   -426    115       N  
ATOM    651  CE1 HIS A 179       9.478   0.465 -19.253  1.00 20.64           C  
ANISOU  651  CE1 HIS A 179     2347   2989   2507   -131    110    474       C  
ATOM    652  NE2 HIS A 179      10.783   0.624 -19.378  1.00 22.89           N  
ANISOU  652  NE2 HIS A 179     2701   3821   2173    198   -146    703       N  
ATOM    653  N   GLU A 180      11.147  -1.500 -12.945  1.00 20.00           N  
ANISOU  653  N   GLU A 180     3142   2197   2257    464   -235      3       N  
ATOM    654  CA  GLU A 180      11.638  -1.467 -11.566  1.00 21.32           C  
ANISOU  654  CA  GLU A 180     2919   2595   2584    425   -588    163       C  
ATOM    655  C   GLU A 180      12.971  -2.212 -11.443  1.00 24.32           C  
ANISOU  655  C   GLU A 180     3326   3010   2904    441   -598    123       C  
ATOM    656  O   GLU A 180      13.830  -1.828 -10.650  1.00 27.52           O  
ANISOU  656  O   GLU A 180     3714   3622   3118    455  -1224    119       O  
ATOM    657  CB  GLU A 180      10.602  -2.047 -10.603  1.00 21.07           C  
ANISOU  657  CB  GLU A 180     3288   2283   2432    487   -447   -122       C  
ATOM    658  CG  GLU A 180      11.031  -2.036  -9.136  1.00 26.24           C  
ANISOU  658  CG  GLU A 180     3715   3323   2931    356   -489    281       C  
ATOM    659  CD  GLU A 180      10.053  -2.749  -8.225  1.00 25.55           C  
ANISOU  659  CD  GLU A 180     3485   2836   3386    177   -272    491       C  
ATOM    660  OE1 GLU A 180       8.833  -2.717  -8.492  1.00 29.26           O  
ANISOU  660  OE1 GLU A 180     3944   3251   3920    203   -165    259       O  
ATOM    661  OE2 GLU A 180      10.508  -3.342  -7.225  1.00 35.34           O1-
ANISOU  661  OE2 GLU A 180     4835   4463   4129    333   -649    832       O1-
ATOM    662  N   ARG A 181      13.136  -3.264 -12.244  1.00 22.48           N  
ANISOU  662  N   ARG A 181     3130   2605   2805    557   -429     42       N  
ATOM    663  CA  ARG A 181      14.340  -4.092 -12.220  1.00 27.19           C  
ANISOU  663  CA  ARG A 181     3398   3403   3529    556   -323    315       C  
ATOM    664  C   ARG A 181      15.310  -3.693 -13.328  1.00 32.25           C  
ANISOU  664  C   ARG A 181     3401   4452   4399    308     38     35       C  
ATOM    665  O   ARG A 181      16.490  -4.052 -13.294  1.00 37.57           O  
ANISOU  665  O   ARG A 181     3882   5297   5095    376    136    149       O  
ATOM    666  CB  ARG A 181      13.969  -5.572 -12.353  1.00 28.51           C  
ANISOU  666  CB  ARG A 181     3248   3425   4159    734   -386    -13       C  
TER     667      ARG A 181 
ATOM    668  N   LEU A 188      19.705   8.250  -6.924  1.00 27.43           N  
ANISOU  668  N   LEU A 188     2715   3797   3909    -15   -194   -209       N  
ATOM    669  CA  LEU A 188      18.913   9.170  -6.117  1.00 24.27           C  
ANISOU  669  CA  LEU A 188     2568   3432   3219   -179   -175     90       C  
ATOM    670  C   LEU A 188      17.482   8.677  -5.987  1.00 22.49           C  
ANISOU  670  C   LEU A 188     2444   3244   2856    -25   -114     19       C  
ATOM    671  O   LEU A 188      16.910   8.685  -4.893  1.00 25.83           O  
ANISOU  671  O   LEU A 188     2988   3881   2946    612   -336    470       O  
ATOM    672  CB  LEU A 188      18.916  10.572  -6.737  1.00 23.32           C  
ANISOU  672  CB  LEU A 188     2724   3285   2851   -196   -286   -185       C  
ATOM    673  CG  LEU A 188      20.264  11.255  -6.981  1.00 24.36           C  
ANISOU  673  CG  LEU A 188     2614   3754   2884   -502   -326   -464       C  
ATOM    674  CD1 LEU A 188      20.062  12.557  -7.739  1.00 31.75           C  
ANISOU  674  CD1 LEU A 188     3907   4334   3821   -389    -73    138       C  
ATOM    675  CD2 LEU A 188      21.003  11.497  -5.673  1.00 24.97           C  
ANISOU  675  CD2 LEU A 188     2570   4007   2908   -333   -295   -564       C  
ATOM    676  N   ALA A 189      16.909   8.264  -7.116  1.00 21.71           N  
ANISOU  676  N   ALA A 189     2365   2530   3353    138   -395   -282       N  
ATOM    677  CA  ALA A 189      15.522   7.823  -7.177  1.00 21.87           C  
ANISOU  677  CA  ALA A 189     2531   2260   3518     73   -371     -5       C  
ATOM    678  C   ALA A 189      15.407   6.343  -6.865  1.00 20.99           C  
ANISOU  678  C   ALA A 189     2333   2381   3260    346   -377     43       C  
ATOM    679  O   ALA A 189      16.118   5.531  -7.464  1.00 23.60           O  
ANISOU  679  O   ALA A 189     2259   2628   4079    561   -344   -240       O  
ATOM    680  CB  ALA A 189      14.945   8.105  -8.550  1.00 22.17           C  
ANISOU  680  CB  ALA A 189     2694   2508   3219    410   -335   -154       C  
ATOM    681  N   PRO A 190      14.501   5.981  -5.937  1.00 20.34           N  
ANISOU  681  N   PRO A 190     2346   1965   3416    356   -265    -60       N  
ATOM    682  CA  PRO A 190      14.194   4.570  -5.748  1.00 21.25           C  
ANISOU  682  CA  PRO A 190     2965   1775   3333    361   -540    -73       C  
ATOM    683  C   PRO A 190      13.645   4.001  -7.056  1.00 19.92           C  
ANISOU  683  C   PRO A 190     2282   2121   3164    334   -480   -122       C  
ATOM    684  O   PRO A 190      12.937   4.707  -7.783  1.00 20.08           O  
ANISOU  684  O   PRO A 190     2714   2036   2879    409   -465    202       O  
ATOM    685  CB  PRO A 190      13.109   4.581  -4.666  1.00 22.34           C  
ANISOU  685  CB  PRO A 190     3429   2148   2911    284   -440    241       C  
ATOM    686  CG  PRO A 190      13.267   5.889  -3.971  1.00 22.12           C  
ANISOU  686  CG  PRO A 190     3393   1941   3070    -10   -124    238       C  
ATOM    687  CD  PRO A 190      13.716   6.837  -5.033  1.00 21.29           C  
ANISOU  687  CD  PRO A 190     2496   2243   3348    435    -42    150       C  
ATOM    688  N   PRO A 191      13.983   2.739  -7.366  1.00 20.69           N  
ANISOU  688  N   PRO A 191     2488   1830   3541    732   -545     82       N  
ATOM    689  CA  PRO A 191      13.655   2.152  -8.665  1.00 20.28           C  
ANISOU  689  CA  PRO A 191     2500   1846   3357    778   -415   -268       C  
ATOM    690  C   PRO A 191      12.157   2.011  -8.927  1.00 19.20           C  
ANISOU  690  C   PRO A 191     2694   1515   3083    424   -274    247       C  
ATOM    691  O   PRO A 191      11.754   1.846 -10.075  1.00 19.38           O  
ANISOU  691  O   PRO A 191     2405   1995   2960    292   -360      0       O  
ATOM    692  CB  PRO A 191      14.316   0.770  -8.599  1.00 23.55           C  
ANISOU  692  CB  PRO A 191     3127   1966   3854    928   -291   -297       C  
ATOM    693  CG  PRO A 191      14.409   0.466  -7.146  1.00 27.40           C  
ANISOU  693  CG  PRO A 191     3851   2351   4207    481   -382   -240       C  
ATOM    694  CD  PRO A 191      14.701   1.781  -6.502  1.00 23.29           C  
ANISOU  694  CD  PRO A 191     2816   2048   3984    691   -730    155       C  
ATOM    695  N   GLN A 192      11.347   2.073  -7.875  1.00 18.29           N  
ANISOU  695  N   GLN A 192     2622   1681   2645    311   -464    191       N  
ATOM    696  CA  GLN A 192       9.899   1.898  -8.002  1.00 17.45           C  
ANISOU  696  CA  GLN A 192     2557   1472   2600    198   -192    316       C  
ATOM    697  C   GLN A 192       9.171   3.176  -8.417  1.00 14.98           C  
ANISOU  697  C   GLN A 192     2099   1474   2118    125    -45    208       C  
ATOM    698  O   GLN A 192       8.034   3.122  -8.881  1.00 15.27           O  
ANISOU  698  O   GLN A 192     2514   1384   1901    -42    -79    169       O  
ATOM    699  CB  GLN A 192       9.303   1.390  -6.687  1.00 21.20           C  
ANISOU  699  CB  GLN A 192     3551   1736   2767    -15    -45    756       C  
ATOM    700  CG  GLN A 192       9.964   0.132  -6.121  1.00 27.80           C  
ANISOU  700  CG  GLN A 192     4435   2479   3646     34   -172    541       C  
ATOM    701  CD  GLN A 192      11.211   0.421  -5.286  1.00 34.41           C  
ANISOU  701  CD  GLN A 192     4480   3788   4804   -202   -258    190       C  
ATOM    702  OE1 GLN A 192      11.607   1.572  -5.083  1.00 28.04           O  
ANISOU  702  OE1 GLN A 192     4125   3678   2852    -11   -905    450       O  
ATOM    703  N   HIS A 193       9.824   4.321  -8.242  1.00 15.28           N  
ANISOU  703  N   HIS A 193     2351   1539   1915    186   -352    187       N  
ATOM    704  CA  HIS A 193       9.181   5.610  -8.477  1.00 13.90           C  
ANISOU  704  CA  HIS A 193     2302   1273   1706    195   -258    163       C  
ATOM    705  C   HIS A 193       8.995   5.923  -9.956  1.00 12.74           C  
ANISOU  705  C   HIS A 193     1836   1196   1806    100    -66    -32       C  
ATOM    706  O   HIS A 193       9.953   5.929 -10.728  1.00 14.04           O  
ANISOU  706  O   HIS A 193     1908   1674   1752    288     70     38       O  
ATOM    707  CB  HIS A 193       9.990   6.737  -7.833  1.00 14.43           C  
ANISOU  707  CB  HIS A 193     2359   1296   1828     80   -239     64       C  
ATOM    708  CG  HIS A 193       9.802   6.856  -6.354  1.00 14.50           C  
ANISOU  708  CG  HIS A 193     2254   1827   1426    117   -236    237       C  
ATOM    709  CD2 HIS A 193       9.805   5.923  -5.371  1.00 18.42           C  
ANISOU  709  CD2 HIS A 193     2979   2008   2010    314   -165     93       C  
ATOM    710  ND1 HIS A 193       9.568   8.065  -5.736  1.00 13.85           N  
ANISOU  710  ND1 HIS A 193     1897   1559   1804     19   -281    -21       N  
ATOM    711  CE1 HIS A 193       9.452   7.875  -4.434  1.00 14.04           C  
ANISOU  711  CE1 HIS A 193     2287   1410   1636    -49   -308    168       C  
ATOM    712  NE2 HIS A 193       9.585   6.584  -4.186  1.00 17.46           N  
ANISOU  712  NE2 HIS A 193     2976   1924   1732    110   -370    143       N  
ATOM    713  N   LEU A 194       7.760   6.237 -10.330  1.00 12.34           N  
ANISOU  713  N   LEU A 194     1756   1406   1524     39    -59     66       N  
ATOM    714  CA  LEU A 194       7.456   6.666 -11.692  1.00 12.50           C  
ANISOU  714  CA  LEU A 194     1931   1255   1563      9     17    209       C  
ATOM    715  C   LEU A 194       8.061   8.031 -12.033  1.00 11.82           C  
ANISOU  715  C   LEU A 194     1570   1462   1456     93    -21    -48       C  
ATOM    716  O   LEU A 194       8.633   8.214 -13.110  1.00 13.05           O  
ANISOU  716  O   LEU A 194     1846   1544   1566     18     98    121       O  
ATOM    717  CB  LEU A 194       5.938   6.707 -11.899  1.00 12.42           C  
ANISOU  717  CB  LEU A 194     1452   1780   1485   -100    -25    114       C  
ATOM    718  CG  LEU A 194       5.483   7.284 -13.242  1.00 12.68           C  
ANISOU  718  CG  LEU A 194     1728   1649   1438   -100    -34    -54       C  
ATOM    719  CD1 LEU A 194       5.832   6.337 -14.379  1.00 15.85           C  
ANISOU  719  CD1 LEU A 194     2096   1992   1934    -31    -12   -145       C  
ATOM    720  CD2 LEU A 194       4.001   7.544 -13.236  1.00 13.25           C  
ANISOU  720  CD2 LEU A 194     1618   1684   1729    -55   -192    308       C  
ATOM    721  N   ILE A 195       7.902   8.998 -11.130  1.00 11.77           N  
ANISOU  721  N   ILE A 195     1612   1272   1585   -114   -135    173       N  
ATOM    722  CA  ILE A 195       8.267  10.387 -11.420  1.00 11.72           C  
ANISOU  722  CA  ILE A 195     1449   1373   1628   -113     -1     39       C  
ATOM    723  C   ILE A 195       9.602  10.751 -10.779  1.00 11.60           C  
ANISOU  723  C   ILE A 195     1613   1379   1416   -115    -14    164       C  
ATOM    724  O   ILE A 195       9.793  10.595  -9.562  1.00 12.74           O  
ANISOU  724  O   ILE A 195     1689   1552   1600     14   -163    263       O  
ATOM    725  CB  ILE A 195       7.182  11.384 -10.930  1.00 12.17           C  
ANISOU  725  CB  ILE A 195     1698   1419   1505   -176     50    172       C  
ATOM    726  CG1 ILE A 195       5.778  10.998 -11.434  1.00 12.18           C  
ANISOU  726  CG1 ILE A 195     1496   1409   1721   -127   -290    184       C  
ATOM    727  CG2 ILE A 195       7.546  12.815 -11.357  1.00 12.69           C  
ANISOU  727  CG2 ILE A 195     1540   1499   1780   -238   -195    218       C  
ATOM    728  CD1 ILE A 195       4.677  11.926 -10.937  1.00 13.34           C  
ANISOU  728  CD1 ILE A 195     1434   1561   2074    130     98    -64       C  
ATOM    729  N   ARG A 196      10.516  11.241 -11.612  1.00 12.20           N  
ANISOU  729  N   ARG A 196     1411   1494   1731     25     13    164       N  
ATOM    730  CA  ARG A 196      11.793  11.769 -11.161  1.00 12.51           C  
ANISOU  730  CA  ARG A 196     1493   1453   1808     40     25     94       C  
ATOM    731  C   ARG A 196      11.892  13.247 -11.503  1.00 12.27           C  
ANISOU  731  C   ARG A 196     1539   1615   1508    127    -63    119       C  
ATOM    732  O   ARG A 196      11.136  13.756 -12.336  1.00 12.44           O  
ANISOU  732  O   ARG A 196     1444   1723   1557   -110    -71    194       O  
ATOM    733  CB  ARG A 196      12.945  11.017 -11.820  1.00 14.91           C  
ANISOU  733  CB  ARG A 196     1794   1826   2042    100     21    154       C  
ATOM    734  CG  ARG A 196      13.004   9.566 -11.449  1.00 15.39           C  
ANISOU  734  CG  ARG A 196     1527   1911   2409    272    -92    236       C  
ATOM    735  CD  ARG A 196      14.226   8.922 -12.060  1.00 18.33           C  
ANISOU  735  CD  ARG A 196     1744   1827   3392    391    -17    232       C  
ATOM    736  NE  ARG A 196      14.187   7.473 -11.887  1.00 18.25           N  
ANISOU  736  NE  ARG A 196     2139   1756   3039    323     20     22       N  
ATOM    737  CZ  ARG A 196      15.044   6.624 -12.442  1.00 18.10           C  
ANISOU  737  CZ  ARG A 196     1991   2067   2818    314     -4    222       C  
ATOM    738  NH1 ARG A 196      16.024   7.070 -13.215  1.00 20.59           N1+
ANISOU  738  NH1 ARG A 196     2203   2264   3356    209    220    -61       N1+
ATOM    739  NH2 ARG A 196      14.918   5.324 -12.220  1.00 19.85           N  
ANISOU  739  NH2 ARG A 196     2652   1760   3129    449    137    125       N  
ATOM    740  N   VAL A 197      12.820  13.937 -10.846  1.00 13.42           N  
ANISOU  740  N   VAL A 197     1624   1783   1689   -102    -92    109       N  
ATOM    741  CA  VAL A 197      13.167  15.304 -11.209  1.00 12.93           C  
ANISOU  741  CA  VAL A 197     1423   1656   1833   -255     12    163       C  
ATOM    742  C   VAL A 197      14.619  15.346 -11.650  1.00 14.58           C  
ANISOU  742  C   VAL A 197     1511   1874   2153    -41      2    267       C  
ATOM    743  O   VAL A 197      15.491  14.791 -10.987  1.00 16.88           O  
ANISOU  743  O   VAL A 197     1596   2438   2377    -80      1    571       O  
ATOM    744  CB  VAL A 197      12.957  16.295 -10.032  1.00 13.37           C  
ANISOU  744  CB  VAL A 197     1468   1703   1907    -93    -33    147       C  
ATOM    745  CG1 VAL A 197      13.541  17.675 -10.359  1.00 14.98           C  
ANISOU  745  CG1 VAL A 197     1946   1480   2265   -288    226     59       C  
ATOM    746  CG2 VAL A 197      11.481  16.420  -9.695  1.00 14.62           C  
ANISOU  746  CG2 VAL A 197     1659   1810   2083    -99     18    -28       C  
ATOM    747  N   GLU A 198      14.873  16.006 -12.773  1.00 13.83           N  
ANISOU  747  N   GLU A 198     1567   1831   1855   -105    227    112       N  
ATOM    748  CA  GLU A 198      16.242  16.212 -13.223  1.00 17.10           C  
ANISOU  748  CA  GLU A 198     2000   2212   2284    -77    428     18       C  
ATOM    749  C   GLU A 198      16.627  17.682 -13.069  1.00 15.87           C  
ANISOU  749  C   GLU A 198     2010   2013   2006   -339    247    224       C  
ATOM    750  O   GLU A 198      15.758  18.553 -13.009  1.00 17.46           O  
ANISOU  750  O   GLU A 198     1841   2115   2675   -115    261    312       O  
ATOM    751  CB  GLU A 198      16.415  15.744 -14.665  1.00 21.33           C  
ANISOU  751  CB  GLU A 198     2775   2816   2511   -102    627    -61       C  
ATOM    752  CG  GLU A 198      15.650  16.564 -15.676  1.00 22.76           C  
ANISOU  752  CG  GLU A 198     2372   3379   2895    -62    -49   -261       C  
ATOM    753  CD  GLU A 198      16.045  16.266 -17.111  1.00 23.63           C  
ANISOU  753  CD  GLU A 198     2932   3100   2944   -403    555     29       C  
ATOM    754  OE1 GLU A 198      15.132  16.070 -17.928  1.00 22.48           O  
ANISOU  754  OE1 GLU A 198     2549   3189   2801   -353    265    343       O  
ATOM    755  OE2 GLU A 198      17.256  16.232 -17.427  1.00 33.77           O1-
ANISOU  755  OE2 GLU A 198     3219   5072   4538     19    233   -405       O1-
ATOM    756  N   GLY A 199      17.926  17.952 -12.985  1.00 17.66           N  
ANISOU  756  N   GLY A 199     1580   2772   2355   -350     97    134       N  
ATOM    757  CA  GLY A 199      18.423  19.328 -12.935  1.00 18.44           C  
ANISOU  757  CA  GLY A 199     2255   2337   2411   -630    114    183       C  
ATOM    758  C   GLY A 199      18.161  20.048 -11.623  1.00 18.35           C  
ANISOU  758  C   GLY A 199     2108   2542   2322   -533    -44    203       C  
ATOM    759  O   GLY A 199      18.050  21.276 -11.592  1.00 20.72           O  
ANISOU  759  O   GLY A 199     2913   2418   2541   -701   -243    306       O  
ATOM    760  N   ASN A 200      18.066  19.284 -10.538  1.00 16.74           N  
ANISOU  760  N   ASN A 200     1644   2363   2352   -325     13    203       N  
ATOM    761  CA  ASN A 200      17.828  19.842  -9.214  1.00 16.13           C  
ANISOU  761  CA  ASN A 200     1481   2302   2342   -180    -98    278       C  
ATOM    762  C   ASN A 200      18.669  19.109  -8.178  1.00 15.81           C  
ANISOU  762  C   ASN A 200     1586   2242   2176   -414   -112    267       C  
ATOM    763  O   ASN A 200      18.675  17.877  -8.128  1.00 18.02           O  
ANISOU  763  O   ASN A 200     1777   2316   2751   -278   -364    332       O  
ATOM    764  CB  ASN A 200      16.337  19.774  -8.859  1.00 15.29           C  
ANISOU  764  CB  ASN A 200     1400   2106   2303   -172   -202    355       C  
ATOM    765  CG  ASN A 200      15.986  20.622  -7.650  1.00 16.65           C  
ANISOU  765  CG  ASN A 200     1392   2683   2249   -189      0    113       C  
ATOM    766  ND2 ASN A 200      15.204  21.672  -7.870  1.00 17.19           N  
ANISOU  766  ND2 ASN A 200     1459   2420   2650   -173    217    577       N  
ATOM    767  OD1 ASN A 200      16.408  20.334  -6.531  1.00 18.37           O  
ANISOU  767  OD1 ASN A 200     1836   2942   2199    102   -284    401       O  
ATOM    768  N   LEU A 201      19.380  19.876  -7.354  1.00 16.06           N  
ANISOU  768  N   LEU A 201     1361   2455   2285   -246    -21    388       N  
ATOM    769  CA  LEU A 201      20.296  19.317  -6.362  1.00 15.56           C  
ANISOU  769  CA  LEU A 201     1491   2271   2150   -290   -200    367       C  
ATOM    770  C   LEU A 201      19.660  18.994  -5.016  1.00 15.27           C  
ANISOU  770  C   LEU A 201     1440   2188   2170   -253    -66    127       C  
ATOM    771  O   LEU A 201      20.348  18.538  -4.107  1.00 15.68           O  
ANISOU  771  O   LEU A 201     1509   2158   2288    -10   -205    150       O  
ATOM    772  CB  LEU A 201      21.461  20.280  -6.140  1.00 18.84           C  
ANISOU  772  CB  LEU A 201     1682   2923   2552   -471   -370    517       C  
ATOM    773  CG  LEU A 201      22.325  20.595  -7.356  1.00 20.35           C  
ANISOU  773  CG  LEU A 201     1957   2700   3073   -654     47    846       C  
ATOM    774  CD1 LEU A 201      23.385  21.612  -6.974  1.00 23.81           C  
ANISOU  774  CD1 LEU A 201     1904   3597   3543  -1279      0    627       C  
ATOM    775  CD2 LEU A 201      22.959  19.329  -7.920  1.00 23.33           C  
ANISOU  775  CD2 LEU A 201     2293   3666   2904   -333    502    476       C  
ATOM    776  N   ARG A 202      18.358  19.226  -4.883  1.00 14.98           N  
ANISOU  776  N   ARG A 202     1395   2057   2237      5   -123    -15       N  
ATOM    777  CA  ARG A 202      17.689  19.072  -3.597  1.00 15.43           C  
ANISOU  777  CA  ARG A 202     1491   2071   2300   -170   -211     -3       C  
ATOM    778  C   ARG A 202      16.414  18.242  -3.712  1.00 13.35           C  
ANISOU  778  C   ARG A 202     1492   1710   1870   -148   -196    167       C  
ATOM    779  O   ARG A 202      15.396  18.532  -3.077  1.00 14.26           O  
ANISOU  779  O   ARG A 202     1502   1937   1977     -8    -20    281       O  
ATOM    780  CB  ARG A 202      17.421  20.442  -2.975  1.00 16.54           C  
ANISOU  780  CB  ARG A 202     1515   2024   2743   -322    -70   -136       C  
ATOM    781  CG  ARG A 202      18.690  21.141  -2.445  1.00 19.34           C  
ANISOU  781  CG  ARG A 202     1812   2335   3199   -345   -167   -120       C  
ATOM    782  CD  ARG A 202      19.285  20.363  -1.263  1.00 21.89           C  
ANISOU  782  CD  ARG A 202     2020   3652   2644   -212   -419   -295       C  
ATOM    783  NE  ARG A 202      20.506  20.945  -0.711  1.00 21.40           N  
ANISOU  783  NE  ARG A 202     2304   2842   2986   -109   -229   -171       N  
ATOM    784  CZ  ARG A 202      21.739  20.534  -0.996  1.00 18.24           C  
ANISOU  784  CZ  ARG A 202     2112   2007   2811   -202   -258     43       C  
ATOM    785  NH1 ARG A 202      21.951  19.544  -1.856  1.00 19.81           N1+
ANISOU  785  NH1 ARG A 202     2286   2351   2890   -242   -480    123       N1+
ATOM    786  NH2 ARG A 202      22.768  21.134  -0.424  1.00 22.74           N  
ANISOU  786  NH2 ARG A 202     2656   2905   3078   -640   -645     67       N  
ATOM    787  N   VAL A 203      16.496  17.181  -4.505  1.00 14.10           N  
ANISOU  787  N   VAL A 203     1424   1943   1989   -140   -269    -42       N  
ATOM    788  CA  VAL A 203      15.359  16.301  -4.733  1.00 14.28           C  
ANISOU  788  CA  VAL A 203     1201   2158   2066   -140   -108    104       C  
ATOM    789  C   VAL A 203      15.185  15.300  -3.591  1.00 13.53           C  
ANISOU  789  C   VAL A 203     1488   1733   1919     23   -250     84       C  
ATOM    790  O   VAL A 203      16.126  14.617  -3.196  1.00 15.49           O  
ANISOU  790  O   VAL A 203     1484   2252   2150    351   -308    -56       O  
ATOM    791  CB  VAL A 203      15.492  15.538  -6.077  1.00 14.87           C  
ANISOU  791  CB  VAL A 203     1712   2028   1909    -59   -256   -203       C  
ATOM    792  CG1 VAL A 203      14.252  14.731  -6.343  1.00 15.82           C  
ANISOU  792  CG1 VAL A 203     1545   2488   1976   -410   -215    -46       C  
ATOM    793  CG2 VAL A 203      15.733  16.488  -7.229  1.00 15.64           C  
ANISOU  793  CG2 VAL A 203     1897   2134   1912    -99   -241     52       C  
ATOM    794  N   GLU A 204      13.963  15.208  -3.078  1.00 13.21           N  
ANISOU  794  N   GLU A 204     1313   1716   1989   -204   -266    210       N  
ATOM    795  CA  GLU A 204      13.612  14.185  -2.105  1.00 14.45           C  
ANISOU  795  CA  GLU A 204     1582   1823   2083   -122   -334    147       C  
ATOM    796  C   GLU A 204      12.648  13.203  -2.717  1.00 12.96           C  
ANISOU  796  C   GLU A 204     1500   1739   1682   -126   -163    219       C  
ATOM    797  O   GLU A 204      11.648  13.598  -3.307  1.00 15.21           O  
ANISOU  797  O   GLU A 204     1617   1751   2409    -24   -720    375       O  
ATOM    798  CB  GLU A 204      12.958  14.799  -0.875  1.00 14.50           C  
ANISOU  798  CB  GLU A 204     1537   2095   1874     18   -240    113       C  
ATOM    799  CG  GLU A 204      13.880  15.669  -0.073  1.00 15.40           C  
ANISOU  799  CG  GLU A 204     1693   2225   1933    -45   -309   -113       C  
ATOM    800  CD  GLU A 204      13.167  16.423   1.019  1.00 14.57           C  
ANISOU  800  CD  GLU A 204     1801   1925   1810   -224   -442     14       C  
ATOM    801  OE1 GLU A 204      13.555  17.586   1.253  1.00 15.60           O  
ANISOU  801  OE1 GLU A 204     2016   2079   1831   -246   -285     63       O  
ATOM    802  OE2 GLU A 204      12.243  15.858   1.648  1.00 16.30           O1-
ANISOU  802  OE2 GLU A 204     1822   2042   2329      3   -137    123       O1-
ATOM    803  N   TYR A 205      12.963  11.921  -2.571  1.00 13.56           N  
ANISOU  803  N   TYR A 205     1820   1604   1727     20   -366    222       N  
ATOM    804  CA  TYR A 205      12.066  10.847  -2.968  1.00 14.41           C  
ANISOU  804  CA  TYR A 205     1828   1935   1709   -187   -259    369       C  
ATOM    805  C   TYR A 205      11.419  10.283  -1.727  1.00 15.47           C  
ANISOU  805  C   TYR A 205     2137   2027   1712   -153   -418    129       C  
ATOM    806  O   TYR A 205      12.097   9.816  -0.824  1.00 18.08           O  
ANISOU  806  O   TYR A 205     2491   2432   1946    -66   -805    547       O  
ATOM    807  CB  TYR A 205      12.816   9.785  -3.770  1.00 15.72           C  
ANISOU  807  CB  TYR A 205     2185   2068   1718    -66   -253    -30       C  
ATOM    808  CG  TYR A 205      13.205  10.306  -5.126  1.00 15.05           C  
ANISOU  808  CG  TYR A 205     2297   1656   1764     63   -306     49       C  
ATOM    809  CD1 TYR A 205      12.294  10.276  -6.183  1.00 14.63           C  
ANISOU  809  CD1 TYR A 205     1896   1846   1816    101   -481    161       C  
ATOM    810  CD2 TYR A 205      14.459  10.870  -5.346  1.00 15.64           C  
ANISOU  810  CD2 TYR A 205     2033   1840   2066   -104   -471     99       C  
ATOM    811  CE1 TYR A 205      12.624  10.784  -7.427  1.00 14.48           C  
ANISOU  811  CE1 TYR A 205     2118   1817   1565     11   -254    123       C  
ATOM    812  CE2 TYR A 205      14.806  11.380  -6.596  1.00 16.13           C  
ANISOU  812  CE2 TYR A 205     2184   1932   2013    137   -232    295       C  
ATOM    813  CZ  TYR A 205      13.874  11.335  -7.628  1.00 14.95           C  
ANISOU  813  CZ  TYR A 205     1913   1821   1945    196   -340     90       C  
ATOM    814  OH  TYR A 205      14.177  11.836  -8.868  1.00 15.84           O  
ANISOU  814  OH  TYR A 205     2117   1979   1922     13   -166    160       O  
ATOM    815  N   LEU A 206      10.093  10.335  -1.693  1.00 14.09           N  
ANISOU  815  N   LEU A 206     1881   1989   1482   -250   -268    188       N  
ATOM    816  CA  LEU A 206       9.347  10.036  -0.491  1.00 15.47           C  
ANISOU  816  CA  LEU A 206     2131   1992   1753   -389   -426    172       C  
ATOM    817  C   LEU A 206       8.367   8.903  -0.724  1.00 16.09           C  
ANISOU  817  C   LEU A 206     2519   2033   1558   -301   -319    181       C  
ATOM    818  O   LEU A 206       7.742   8.806  -1.778  1.00 14.40           O  
ANISOU  818  O   LEU A 206     2326   1607   1535   -294   -349    335       O  
ATOM    819  CB  LEU A 206       8.627  11.293   0.009  1.00 17.26           C  
ANISOU  819  CB  LEU A 206     2064   2554   1937   -503    -81    222       C  
ATOM    820  CG  LEU A 206       9.533  12.486   0.341  1.00 16.64           C  
ANISOU  820  CG  LEU A 206     2136   2200   1986   -362   -139   -107       C  
ATOM    821  CD1 LEU A 206       8.710  13.695   0.708  1.00 20.06           C  
ANISOU  821  CD1 LEU A 206     3004   2113   2503    -19   -521     66       C  
ATOM    822  CD2 LEU A 206      10.503  12.141   1.466  1.00 18.45           C  
ANISOU  822  CD2 LEU A 206     2360   2344   2304   -384   -349   -202       C  
ATOM    823  N   ASP A 207       8.284   8.023   0.265  1.00 18.56           N  
ANISOU  823  N   ASP A 207     3109   2319   1623   -560   -524    502       N  
ATOM    824  CA  ASP A 207       7.329   6.930   0.285  1.00 19.61           C  
ANISOU  824  CA  ASP A 207     3055   2302   2092   -545   -359    342       C  
ATOM    825  C   ASP A 207       6.444   7.134   1.507  1.00 20.89           C  
ANISOU  825  C   ASP A 207     3301   2701   1933   -569   -115    105       C  
ATOM    826  O   ASP A 207       6.936   7.136   2.635  1.00 24.62           O  
ANISOU  826  O   ASP A 207     3855   3696   1801  -1072   -524    202       O  
ATOM    827  CB  ASP A 207       8.050   5.579   0.377  1.00 23.46           C  
ANISOU  827  CB  ASP A 207     3468   2423   3021   -445   -303    278       C  
ATOM    828  CG  ASP A 207       8.657   5.137  -0.947  1.00 32.23           C  
ANISOU  828  CG  ASP A 207     4343   3424   4476     45    275    -83       C  
ATOM    829  OD1 ASP A 207       9.596   5.796  -1.440  1.00 33.30           O  
ANISOU  829  OD1 ASP A 207     4965   3963   3722     22    202    747       O  
ATOM    830  OD2 ASP A 207       8.208   4.105  -1.485  1.00 42.43           O1-
ANISOU  830  OD2 ASP A 207     5620   5019   5482   -233   -316   -303       O1-
ATOM    831  N   ASP A 208       5.147   7.328   1.284  1.00 20.71           N  
ANISOU  831  N   ASP A 208     3662   2646   1559   -473    198    508       N  
ATOM    832  CA  ASP A 208       4.196   7.543   2.375  1.00 23.20           C  
ANISOU  832  CA  ASP A 208     3735   2656   2421   -383    136    291       C  
ATOM    833  C   ASP A 208       4.082   6.292   3.245  1.00 22.75           C  
ANISOU  833  C   ASP A 208     4142   3004   1499   -315    112    421       C  
ATOM    834  O   ASP A 208       3.851   5.200   2.733  1.00 21.99           O  
ANISOU  834  O   ASP A 208     3999   2363   1992   -183    161    507       O  
ATOM    835  CB  ASP A 208       2.831   7.936   1.811  1.00 26.87           C  
ANISOU  835  CB  ASP A 208     4220   3280   2706     15     88    265       C  
ATOM    836  CG  ASP A 208       1.899   8.493   2.866  1.00 30.80           C  
ANISOU  836  CG  ASP A 208     4451   3441   3810    127    291     48       C  
ATOM    837  OD1 ASP A 208       1.331   7.699   3.646  1.00 31.46           O  
ANISOU  837  OD1 ASP A 208     4761   4319   2871    519    750    -35       O  
ATOM    838  OD2 ASP A 208       1.723   9.729   2.902  1.00 31.97           O1-
ANISOU  838  OD2 ASP A 208     5039   3464   3644    748    194   -151       O1-
ATOM    839  N   ARG A 209       4.253   6.461   4.554  1.00 24.68           N  
ANISOU  839  N   ARG A 209     4293   3245   1838   -534    108    454       N  
ATOM    840  CA  ARG A 209       4.269   5.328   5.488  1.00 27.51           C  
ANISOU  840  CA  ARG A 209     4396   3673   2381   -215   -203    754       C  
ATOM    841  C   ARG A 209       2.925   4.599   5.642  1.00 30.92           C  
ANISOU  841  C   ARG A 209     4566   3970   3210   -178    130    517       C  
ATOM    842  O   ARG A 209       2.896   3.421   6.006  1.00 35.32           O  
ANISOU  842  O   ARG A 209     5263   4260   3896    -42    208   1122       O  
ATOM    843  CB  ARG A 209       4.825   5.747   6.859  1.00 29.42           C  
ANISOU  843  CB  ARG A 209     4531   4036   2611    -23   -164    593       C  
ATOM    844  CG  ARG A 209       4.003   6.801   7.593  1.00 37.46           C  
ANISOU  844  CG  ARG A 209     4830   5015   4386    -58    157   -104       C  
ATOM    845  N   ASN A 210       1.826   5.296   5.364  1.00 28.59           N  
ANISOU  845  N   ASN A 210     4500   4180   2183   -116    481    372       N  
ATOM    846  CA  ASN A 210       0.489   4.708   5.465  1.00 32.92           C  
ANISOU  846  CA  ASN A 210     4448   4477   3581    -31    207    166       C  
ATOM    847  C   ASN A 210      -0.101   4.255   4.129  1.00 31.54           C  
ANISOU  847  C   ASN A 210     4391   4181   3409   -211    207    445       C  
ATOM    848  O   ASN A 210      -0.697   3.178   4.044  1.00 33.55           O  
ANISOU  848  O   ASN A 210     4648   4824   3276   -243    474    865       O  
ATOM    849  CB  ASN A 210      -0.474   5.675   6.160  1.00 36.67           C  
ANISOU  849  CB  ASN A 210     4682   5028   4222    168    183    -96       C  
ATOM    850  CG  ASN A 210      -0.260   5.737   7.662  1.00 41.06           C  
ANISOU  850  CG  ASN A 210     5583   5437   4580      1    140     76       C  
ATOM    851  ND2 ASN A 210      -0.591   4.651   8.356  1.00 40.59           N  
ANISOU  851  ND2 ASN A 210     5591   5020   4809    201     93    -26       N  
ATOM    852  OD1 ASN A 210       0.201   6.748   8.192  1.00 44.44           O  
ANISOU  852  OD1 ASN A 210     6000   5666   5219    -74    -56   -222       O  
ATOM    853  N   THR A 211       0.070   5.076   3.092  1.00 26.49           N  
ANISOU  853  N   THR A 211     3793   4222   2048    148    759    440       N  
ATOM    854  CA  THR A 211      -0.550   4.822   1.789  1.00 24.88           C  
ANISOU  854  CA  THR A 211     3324   3365   2765     37    415    420       C  
ATOM    855  C   THR A 211       0.404   4.141   0.814  1.00 19.83           C  
ANISOU  855  C   THR A 211     2810   2378   2343   -106    556    576       C  
ATOM    856  O   THR A 211      -0.033   3.609  -0.207  1.00 20.51           O  
ANISOU  856  O   THR A 211     2870   2728   2192   -690    244    755       O  
ATOM    857  CB  THR A 211      -1.049   6.124   1.118  1.00 25.71           C  
ANISOU  857  CB  THR A 211     3174   3491   3101    248    181    197       C  
ATOM    858  CG2 THR A 211      -1.871   6.969   2.088  1.00 28.38           C  
ANISOU  858  CG2 THR A 211     3184   3912   3686    525    611     -1       C  
ATOM    859  OG1 THR A 211       0.074   6.879   0.655  1.00 25.23           O  
ANISOU  859  OG1 THR A 211     3695   3049   2842    558    572    368       O  
ATOM    860  N   PHE A 212       1.701   4.180   1.126  1.00 18.58           N  
ANISOU  860  N   PHE A 212     2965   2029   2063   -373    281    531       N  
ATOM    861  CA  PHE A 212       2.762   3.639   0.256  1.00 17.13           C  
ANISOU  861  CA  PHE A 212     2787   1680   2040   -171    339    529       C  
ATOM    862  C   PHE A 212       2.941   4.407  -1.046  1.00 15.98           C  
ANISOU  862  C   PHE A 212     2401   1704   1965   -271    191    441       C  
ATOM    863  O   PHE A 212       3.720   4.007  -1.910  1.00 18.77           O  
ANISOU  863  O   PHE A 212     2662   2188   2281    186    538    810       O  
ATOM    864  CB  PHE A 212       2.555   2.150  -0.023  1.00 18.42           C  
ANISOU  864  CB  PHE A 212     3196   1619   2182   -233    177    665       C  
ATOM    865  CG  PHE A 212       2.636   1.311   1.204  1.00 19.21           C  
ANISOU  865  CG  PHE A 212     3355   1733   2210   -249    -24    429       C  
ATOM    866  CD1 PHE A 212       3.862   0.823   1.641  1.00 23.51           C  
ANISOU  866  CD1 PHE A 212     3516   2460   2956   -163   -356    768       C  
ATOM    867  CD2 PHE A 212       1.493   1.031   1.944  1.00 21.95           C  
ANISOU  867  CD2 PHE A 212     3372   2418   2550   -658    294    604       C  
ATOM    868  CE1 PHE A 212       3.946   0.049   2.791  1.00 23.59           C  
ANISOU  868  CE1 PHE A 212     3816   2182   2964     41   -101    759       C  
ATOM    869  CE2 PHE A 212       1.567   0.267   3.103  1.00 22.88           C  
ANISOU  869  CE2 PHE A 212     3715   2290   2687   -245    139   1169       C  
ATOM    870  CZ  PHE A 212       2.796  -0.225   3.524  1.00 24.35           C  
ANISOU  870  CZ  PHE A 212     3439   2924   2887   -435   -156   1061       C  
ATOM    871  N   ARG A 213       2.238   5.521  -1.184  1.00 15.53           N  
ANISOU  871  N   ARG A 213     2347   1782   1769   -311     68    421       N  
ATOM    872  CA  ARG A 213       2.338   6.306  -2.404  1.00 14.67           C  
ANISOU  872  CA  ARG A 213     2515   1504   1551   -267    112    372       C  
ATOM    873  C   ARG A 213       3.671   7.022  -2.493  1.00 14.15           C  
ANISOU  873  C   ARG A 213     2538   1170   1665   -385   -321    445       C  
ATOM    874  O   ARG A 213       4.226   7.476  -1.488  1.00 15.81           O  
ANISOU  874  O   ARG A 213     2701   1837   1469   -490     78    278       O  
ATOM    875  CB  ARG A 213       1.186   7.290  -2.503  1.00 18.23           C  
ANISOU  875  CB  ARG A 213     2598   2057   2268    -73   -216    537       C  
ATOM    876  CG  ARG A 213      -0.116   6.595  -2.779  1.00 20.42           C  
ANISOU  876  CG  ARG A 213     2675   2491   2593   -494    458    587       C  
ATOM    877  CD  ARG A 213      -1.233   7.562  -2.921  1.00 20.84           C  
ANISOU  877  CD  ARG A 213     2721   2902   2295   -260   -242   -279       C  
ATOM    878  NE  ARG A 213      -2.506   6.858  -2.906  1.00 19.45           N  
ANISOU  878  NE  ARG A 213     2495   2584   2311   -829   -258    490       N  
ATOM    879  CZ  ARG A 213      -3.090   6.334  -3.977  1.00 18.36           C  
ANISOU  879  CZ  ARG A 213     2560   2640   1775   -146   -184    159       C  
ATOM    880  NH1 ARG A 213      -2.527   6.428  -5.178  1.00 18.45           N1+
ANISOU  880  NH1 ARG A 213     2494   2369   2147    -93     40   -130       N1+
ATOM    881  NH2 ARG A 213      -4.250   5.719  -3.842  1.00 21.99           N  
ANISOU  881  NH2 ARG A 213     2252   3473   2627   -471    290     45       N  
ATOM    882  N   HIS A 214       4.179   7.112  -3.715  1.00 13.66           N  
ANISOU  882  N   HIS A 214     2433   1425   1330   -292      8    305       N  
ATOM    883  CA  HIS A 214       5.443   7.767  -3.978  1.00 12.92           C  
ANISOU  883  CA  HIS A 214     2065   1328   1514   -294   -302    248       C  
ATOM    884  C   HIS A 214       5.228   9.218  -4.314  1.00 12.47           C  
ANISOU  884  C   HIS A 214     2080   1262   1393   -283    -67    315       C  
ATOM    885  O   HIS A 214       4.230   9.589  -4.925  1.00 13.23           O  
ANISOU  885  O   HIS A 214     1859   1567   1599   -193   -350    342       O  
ATOM    886  CB  HIS A 214       6.118   7.115  -5.178  1.00 13.80           C  
ANISOU  886  CB  HIS A 214     2101   1559   1582     -1    -44    241       C  
ATOM    887  CG  HIS A 214       6.302   5.637  -5.048  1.00 15.02           C  
ANISOU  887  CG  HIS A 214     2284   1794   1629    180   -119    301       C  
ATOM    888  CD2 HIS A 214       6.456   4.845  -3.961  1.00 18.31           C  
ANISOU  888  CD2 HIS A 214     2922   1845   2190    215    -17    259       C  
ATOM    889  ND1 HIS A 214       6.344   4.804  -6.143  1.00 17.60           N  
ANISOU  889  ND1 HIS A 214     2953   1851   1883    -64     14    320       N  
ATOM    890  CE1 HIS A 214       6.522   3.560  -5.737  1.00 17.71           C  
ANISOU  890  CE1 HIS A 214     2995   1729   2001    -13    -50    230       C  
ATOM    891  NE2 HIS A 214       6.594   3.558  -4.418  1.00 17.76           N  
ANISOU  891  NE2 HIS A 214     3035   1670   2042    333     90    290       N  
ATOM    892  N   SER A 215       6.188  10.046  -3.936  1.00 13.00           N  
ANISOU  892  N   SER A 215     1910   1384   1645   -189   -263    382       N  
ATOM    893  CA  SER A 215       6.199  11.404  -4.431  1.00 12.87           C  
ANISOU  893  CA  SER A 215     1760   1202   1926   -353   -242    274       C  
ATOM    894  C   SER A 215       7.615  11.913  -4.503  1.00 12.36           C  
ANISOU  894  C   SER A 215     1660   1429   1606    -25   -344    196       C  
ATOM    895  O   SER A 215       8.530  11.328  -3.920  1.00 12.81           O  
ANISOU  895  O   SER A 215     1780   1402   1684    -57   -273    177       O  
ATOM    896  CB  SER A 215       5.314  12.312  -3.581  1.00 15.18           C  
ANISOU  896  CB  SER A 215     2164   1582   2022    -90    -78    185       C  
ATOM    897  OG  SER A 215       5.768  12.368  -2.249  1.00 15.15           O  
ANISOU  897  OG  SER A 215     2260   1659   1836   -323   -340     53       O  
ATOM    898  N   VAL A 216       7.787  12.995  -5.248  1.00 12.16           N  
ANISOU  898  N   VAL A 216     1670   1217   1732   -338   -266    291       N  
ATOM    899  CA  VAL A 216       9.084  13.604  -5.424  1.00 12.07           C  
ANISOU  899  CA  VAL A 216     1618   1306   1659   -203   -237    213       C  
ATOM    900  C   VAL A 216       8.934  15.083  -5.122  1.00 11.78           C  
ANISOU  900  C   VAL A 216     1454   1384   1637   -168   -221    172       C  
ATOM    901  O   VAL A 216       8.010  15.740  -5.613  1.00 11.32           O  
ANISOU  901  O   VAL A 216     1190   1405   1704    -89   -133    235       O  
ATOM    902  CB  VAL A 216       9.699  13.294  -6.830  1.00 13.34           C  
ANISOU  902  CB  VAL A 216     1493   1661   1911   -185   -380    155       C  
ATOM    903  CG1 VAL A 216       8.812  13.763  -7.978  1.00 13.36           C  
ANISOU  903  CG1 VAL A 216     1701   1685   1687     -1   -310    231       C  
ATOM    904  CG2 VAL A 216      11.079  13.884  -6.952  1.00 13.79           C  
ANISOU  904  CG2 VAL A 216     1561   1677   2001   -135   -205    104       C  
ATOM    905  N   VAL A 217       9.824  15.587  -4.272  1.00 12.06           N  
ANISOU  905  N   VAL A 217     1405   1477   1698   -212   -236     21       N  
ATOM    906  CA  VAL A 217       9.719  16.944  -3.753  1.00 11.42           C  
ANISOU  906  CA  VAL A 217     1193   1462   1684   -208   -190    135       C  
ATOM    907  C   VAL A 217      10.993  17.719  -4.046  1.00 11.90           C  
ANISOU  907  C   VAL A 217     1278   1425   1816    -96   -234    131       C  
ATOM    908  O   VAL A 217      12.090  17.178  -3.916  1.00 13.33           O  
ANISOU  908  O   VAL A 217     1172   1565   2325   -162   -340    273       O  
ATOM    909  CB  VAL A 217       9.464  16.937  -2.221  1.00 13.02           C  
ANISOU  909  CB  VAL A 217     1721   1668   1556   -174   -247     87       C  
ATOM    910  CG1 VAL A 217       9.485  18.350  -1.652  1.00 16.89           C  
ANISOU  910  CG1 VAL A 217     2552   1908   1956   -129     96     78       C  
ATOM    911  CG2 VAL A 217       8.139  16.260  -1.907  1.00 14.78           C  
ANISOU  911  CG2 VAL A 217     1327   2406   1882   -495   -208    362       C  
ATOM    912  N   VAL A 218      10.836  18.986  -4.424  1.00 11.76           N  
ANISOU  912  N   VAL A 218     1336   1432   1697   -234   -115     78       N  
ATOM    913  CA  VAL A 218      11.952  19.924  -4.508  1.00 12.49           C  
ANISOU  913  CA  VAL A 218     1233   1798   1711   -454    -89     85       C  
ATOM    914  C   VAL A 218      11.562  21.217  -3.793  1.00 12.44           C  
ANISOU  914  C   VAL A 218     1397   1557   1770   -441     59    124       C  
ATOM    915  O   VAL A 218      10.373  21.520  -3.621  1.00 12.77           O  
ANISOU  915  O   VAL A 218     1235   1641   1974   -276     20    109       O  
ATOM    916  CB  VAL A 218      12.366  20.240  -5.973  1.00 13.33           C  
ANISOU  916  CB  VAL A 218     1445   1816   1801   -294   -169    258       C  
ATOM    917  CG1 VAL A 218      12.956  19.014  -6.663  1.00 13.89           C  
ANISOU  917  CG1 VAL A 218     1728   1723   1824   -107    103    -28       C  
ATOM    918  CG2 VAL A 218      11.211  20.859  -6.766  1.00 13.72           C  
ANISOU  918  CG2 VAL A 218     1595   1723   1895   -113    105    241       C  
ATOM    919  N   PRO A 219      12.561  21.996  -3.363  1.00 12.28           N  
ANISOU  919  N   PRO A 219     1257   1514   1892   -333    -86    112       N  
ATOM    920  CA  PRO A 219      12.225  23.305  -2.813  1.00 13.12           C  
ANISOU  920  CA  PRO A 219     1416   1533   2034   -344     32     59       C  
ATOM    921  C   PRO A 219      11.600  24.198  -3.874  1.00 13.58           C  
ANISOU  921  C   PRO A 219     1479   1610   2069   -393     95    153       C  
ATOM    922  O   PRO A 219      11.982  24.129  -5.052  1.00 14.13           O  
ANISOU  922  O   PRO A 219     1650   1627   2089   -295     49    134       O  
ATOM    923  CB  PRO A 219      13.593  23.878  -2.411  1.00 14.53           C  
ANISOU  923  CB  PRO A 219     1475   1623   2419   -357   -363    -96       C  
ATOM    924  CG  PRO A 219      14.485  22.685  -2.271  1.00 15.29           C  
ANISOU  924  CG  PRO A 219     1460   1901   2448   -373   -398     -3       C  
ATOM    925  CD  PRO A 219      14.009  21.731  -3.321  1.00 13.53           C  
ANISOU  925  CD  PRO A 219     1128   1749   2263   -170   -153     31       C  
ATOM    926  N   TYR A 220      10.640  25.023  -3.470  1.00 13.44           N  
ANISOU  926  N   TYR A 220     1503   1635   1966   -332   -128    108       N  
ATOM    927  CA  TYR A 220      10.161  26.063  -4.351  1.00 13.76           C  
ANISOU  927  CA  TYR A 220     1572   1626   2027   -478     47    -18       C  
ATOM    928  C   TYR A 220      11.256  27.117  -4.495  1.00 14.38           C  
ANISOU  928  C   TYR A 220     1778   1645   2038   -373    -38     43       C  
ATOM    929  O   TYR A 220      11.811  27.583  -3.502  1.00 17.01           O  
ANISOU  929  O   TYR A 220     2416   2084   1961   -938   -218     80       O  
ATOM    930  CB  TYR A 220       8.887  26.723  -3.808  1.00 14.46           C  
ANISOU  930  CB  TYR A 220     1822   1574   2097   -219     51     64       C  
ATOM    931  CG  TYR A 220       8.491  27.913  -4.645  1.00 14.37           C  
ANISOU  931  CG  TYR A 220     1990   1258   2209   -204    -12    -36       C  
ATOM    932  CD1 TYR A 220       7.777  27.749  -5.835  1.00 14.49           C  
ANISOU  932  CD1 TYR A 220     1690   1746   2068   -254    -66    -30       C  
ATOM    933  CD2 TYR A 220       8.894  29.196  -4.286  1.00 16.40           C  
ANISOU  933  CD2 TYR A 220     2477   1380   2374   -275     -4    -69       C  
ATOM    934  CE1 TYR A 220       7.445  28.840  -6.633  1.00 15.81           C  
ANISOU  934  CE1 TYR A 220     1856   1459   2689   -262    -73    210       C  
ATOM    935  CE2 TYR A 220       8.577  30.285  -5.070  1.00 16.83           C  
ANISOU  935  CE2 TYR A 220     2328   1586   2479   -162   -104    146       C  
ATOM    936  CZ  TYR A 220       7.851  30.109  -6.238  1.00 16.85           C  
ANISOU  936  CZ  TYR A 220     2401   1573   2428   -271   -143     60       C  
ATOM    937  OH  TYR A 220       7.550  31.215  -6.997  1.00 18.58           O  
ANISOU  937  OH  TYR A 220     2850   1531   2678    -74   -204    242       O  
ATOM    938  N   GLU A 221      11.558  27.487  -5.733  1.00 14.50           N  
ANISOU  938  N   GLU A 221     1623   1576   2309   -484     36    266       N  
ATOM    939  CA  GLU A 221      12.453  28.601  -6.017  1.00 15.83           C  
ANISOU  939  CA  GLU A 221     1678   1988   2346   -413   -156    383       C  
ATOM    940  C   GLU A 221      11.681  29.619  -6.847  1.00 14.84           C  
ANISOU  940  C   GLU A 221     1718   1556   2363   -461    139    229       C  
ATOM    941  O   GLU A 221      10.903  29.235  -7.714  1.00 17.04           O  
ANISOU  941  O   GLU A 221     2308   1910   2257   -718   -267    277       O  
ATOM    942  CB  GLU A 221      13.673  28.116  -6.800  1.00 18.19           C  
ANISOU  942  CB  GLU A 221     1917   1986   3007   -358    265    295       C  
ATOM    943  CG  GLU A 221      14.641  27.272  -5.993  1.00 22.04           C  
ANISOU  943  CG  GLU A 221     2286   2632   3456   -266    121    258       C  
ATOM    944  CD  GLU A 221      15.810  26.782  -6.823  0.50 19.78           C  
ANISOU  944  CD  GLU A 221     2063   2619   2831   -112    107     72       C  
ATOM    945  OE1 GLU A 221      15.632  25.807  -7.584  0.50 16.62           O  
ANISOU  945  OE1 GLU A 221     1784   2153   2377   -308     66    463       O  
ATOM    946  OE2 GLU A 221      16.908  27.370  -6.709  0.50 25.31           O1-
ANISOU  946  OE2 GLU A 221     2663   3358   3595   -301    419    -74       O1-
ATOM    947  N  APRO A 222      11.939  30.918  -6.622  0.50 15.37           N  
ANISOU  947  N  APRO A 222     2168   1471   2198   -598   -135    264       N  
ATOM    948  N  BPRO A 222      11.857  30.921  -6.565  0.50 18.57           N  
ANISOU  948  N  BPRO A 222     2463   1982   2609   -494   -100    105       N  
ATOM    949  CA APRO A 222      11.278  31.916  -7.448  0.50 15.12           C  
ANISOU  949  CA APRO A 222     2210   1183   2351   -355   -100     14       C  
ATOM    950  CA BPRO A 222      11.246  31.939  -7.423  0.50 20.89           C  
ANISOU  950  CA BPRO A 222     2773   2249   2914   -236   -115     53       C  
ATOM    951  C  APRO A 222      11.841  31.871  -8.869  0.50 13.80           C  
ANISOU  951  C  APRO A 222     1745   1227   2270   -557     27    178       C  
ATOM    952  C  BPRO A 222      11.843  31.907  -8.836  0.50 20.70           C  
ANISOU  952  C  BPRO A 222     2709   2313   2843   -237   -114     78       C  
ATOM    953  O  APRO A 222      12.886  31.251  -9.098  0.50 14.45           O  
ANISOU  953  O  APRO A 222     1816   1352   2322   -485   -221    512       O  
ATOM    954  O  BPRO A 222      12.925  31.342  -9.026  0.50 25.53           O  
ANISOU  954  O  BPRO A 222     2964   3204   3529   -159   -157    219       O  
ATOM    955  CB APRO A 222      11.662  33.235  -6.771  0.50 17.05           C  
ANISOU  955  CB APRO A 222     2665   1268   2544   -351   -269   -100       C  
ATOM    956  CB BPRO A 222      11.613  33.254  -6.722  0.50 23.23           C  
ANISOU  956  CB BPRO A 222     3283   2521   3021   -230   -182   -111       C  
ATOM    957  CG APRO A 222      12.975  32.958  -6.127  0.50 16.84           C  
ANISOU  957  CG APRO A 222     2443   1388   2567   -436   -200    396       C  
ATOM    958  CG BPRO A 222      11.960  32.866  -5.322  0.50 23.97           C  
ANISOU  958  CG BPRO A 222     3230   2990   2886    174   -184   -109       C  
ATOM    959  CD APRO A 222      12.867  31.532  -5.651  0.50 16.90           C  
ANISOU  959  CD APRO A 222     2482   1496   2441   -354   -269    117       C  
ATOM    960  CD BPRO A 222      12.596  31.523  -5.443  0.50 23.45           C  
ANISOU  960  CD BPRO A 222     3142   2570   3198   -261   -427    -86       C  
ATOM    961  N   PRO A 223      11.144  32.497  -9.829  1.00 17.55           N  
ANISOU  961  N   PRO A 223     2486   1523   2658   -628    -96    206       N  
ATOM    962  CA  PRO A 223      11.663  32.525 -11.197  1.00 17.62           C  
ANISOU  962  CA  PRO A 223     2326   1805   2561   -676    -12    332       C  
ATOM    963  C   PRO A 223      13.063  33.118 -11.259  1.00 16.32           C  
ANISOU  963  C   PRO A 223     2243   1463   2495   -562     85    121       C  
ATOM    964  O   PRO A 223      13.379  34.050 -10.511  1.00 19.29           O  
ANISOU  964  O   PRO A 223     2883   1892   2554   -972     54     84       O  
ATOM    965  CB  PRO A 223      10.667  33.424 -11.928  1.00 17.83           C  
ANISOU  965  CB  PRO A 223     2357   1574   2842   -462      5    135       C  
ATOM    966  CG  PRO A 223       9.405  33.274 -11.152  1.00 17.82           C  
ANISOU  966  CG  PRO A 223     2667   1885   2219   -256     -5     49       C  
ATOM    967  CD  PRO A 223       9.833  33.167  -9.732  1.00 17.02           C  
ANISOU  967  CD  PRO A 223     2294   1611   2561   -373   -196     16       C  
ATOM    968  N   GLU A 224      13.901  32.558 -12.123  1.00 17.59           N  
ANISOU  968  N   GLU A 224     1955   1570   3155   -521    -17    134       N  
ATOM    969  CA  GLU A 224      15.209  33.137 -12.394  1.00 18.58           C  
ANISOU  969  CA  GLU A 224     2251   1733   3073   -655    266     18       C  
ATOM    970  C   GLU A 224      15.033  34.547 -12.948  1.00 17.13           C  
ANISOU  970  C   GLU A 224     2388   1562   2557   -542    338    -52       C  
ATOM    971  O   GLU A 224      14.006  34.872 -13.539  1.00 16.82           O  
ANISOU  971  O   GLU A 224     2392   1360   2635   -536    474     90       O  
ATOM    972  CB  GLU A 224      15.984  32.271 -13.391  1.00 22.59           C  
ANISOU  972  CB  GLU A 224     2572   2238   3772   -265    640    -69       C  
ATOM    973  CG  GLU A 224      16.465  30.942 -12.825  1.00 26.66           C  
ANISOU  973  CG  GLU A 224     3394   2322   4412   -539    332    128       C  
ATOM    974  N   VAL A 225      16.033  35.392 -12.737  1.00 16.83           N  
ANISOU  974  N   VAL A 225     1993   1702   2699   -502    321    132       N  
ATOM    975  CA  VAL A 225      16.076  36.689 -13.404  1.00 17.51           C  
ANISOU  975  CA  VAL A 225     2427   1715   2510   -551    237    100       C  
ATOM    976  C   VAL A 225      15.840  36.458 -14.906  1.00 17.61           C  
ANISOU  976  C   VAL A 225     2172   1797   2722   -639    309     19       C  
ATOM    977  O   VAL A 225      16.435  35.554 -15.495  1.00 19.81           O  
ANISOU  977  O   VAL A 225     2675   2161   2689   -758    559   -252       O  
ATOM    978  CB  VAL A 225      17.421  37.395 -13.141  1.00 17.30           C  
ANISOU  978  CB  VAL A 225     2185   1825   2561   -900    345     13       C  
ATOM    979  CG1 VAL A 225      17.545  38.661 -13.973  1.00 20.11           C  
ANISOU  979  CG1 VAL A 225     2765   1925   2948   -616    649    113       C  
ATOM    980  CG2 VAL A 225      17.561  37.719 -11.660  1.00 19.62           C  
ANISOU  980  CG2 VAL A 225     2464   2243   2748   -643     28     80       C  
ATOM    981  N   GLY A 226      14.942  37.242 -15.499  1.00 18.29           N  
ANISOU  981  N   GLY A 226     2434   2119   2395   -997    217    162       N  
ATOM    982  CA  GLY A 226      14.596  37.108 -16.917  1.00 21.52           C  
ANISOU  982  CA  GLY A 226     2874   2504   2796   -739    234    360       C  
ATOM    983  C   GLY A 226      13.452  36.146 -17.200  1.00 20.62           C  
ANISOU  983  C   GLY A 226     2716   2713   2404   -954    169     94       C  
ATOM    984  O   GLY A 226      13.143  35.874 -18.366  1.00 24.11           O  
ANISOU  984  O   GLY A 226     3317   3279   2562  -1059     55    100       O  
ATOM    985  N   SER A 227      12.820  35.635 -16.142  1.00 18.12           N  
ANISOU  985  N   SER A 227     2623   1757   2502   -802    312    105       N  
ATOM    986  CA  SER A 227      11.703  34.695 -16.276  1.00 17.60           C  
ANISOU  986  CA  SER A 227     2436   1520   2731   -516    109     91       C  
ATOM    987  C   SER A 227      10.516  35.099 -15.400  1.00 16.97           C  
ANISOU  987  C   SER A 227     2662   1397   2387   -413    161    114       C  
ATOM    988  O   SER A 227      10.689  35.791 -14.389  1.00 18.32           O  
ANISOU  988  O   SER A 227     2811   1695   2453   -570     88    -73       O  
ATOM    989  CB ASER A 227      12.163  33.278 -15.925  0.60 20.87           C  
ANISOU  989  CB ASER A 227     2878   1789   3263   -357    332   -289       C  
ATOM    990  CB BSER A 227      12.151  33.271 -15.941  0.40 21.20           C  
ANISOU  990  CB BSER A 227     2801   2142   3109   -202    249   -142       C  
ATOM    991  OG ASER A 227      11.094  32.359 -16.026  0.60 21.49           O  
ANISOU  991  OG ASER A 227     3409   2037   2719   -600    146    -10       O  
ATOM    992  OG BSER A 227      13.080  32.792 -16.898  0.40 23.09           O  
ANISOU  992  OG BSER A 227     2841   2577   3353     30    262   -408       O  
ATOM    993  N   ASP A 228       9.318  34.658 -15.792  1.00 17.57           N  
ANISOU  993  N   ASP A 228     2533   1548   2593   -569    163    220       N  
ATOM    994  CA  ASP A 228       8.075  34.967 -15.077  1.00 17.80           C  
ANISOU  994  CA  ASP A 228     2353   1636   2772   -106     79    270       C  
ATOM    995  C   ASP A 228       7.567  33.785 -14.259  1.00 16.09           C  
ANISOU  995  C   ASP A 228     1843   1373   2895    -55    -59    130       C  
ATOM    996  O   ASP A 228       6.623  33.917 -13.481  1.00 18.29           O  
ANISOU  996  O   ASP A 228     2137   1773   3039    -59    221    152       O  
ATOM    997  CB  ASP A 228       6.973  35.382 -16.065  1.00 20.68           C  
ANISOU  997  CB  ASP A 228     2834   2074   2948     42   -123    540       C  
ATOM    998  CG  ASP A 228       7.304  36.649 -16.835  1.00 27.27           C  
ANISOU  998  CG  ASP A 228     3875   2878   3608    -59   -201    428       C  
ATOM    999  OD1 ASP A 228       8.029  37.507 -16.302  1.00 28.18           O  
ANISOU  999  OD1 ASP A 228     4285   2351   4071   -430   -132    415       O  
ATOM   1000  OD2 ASP A 228       6.820  36.790 -17.980  1.00 34.34           O1-
ANISOU 1000  OD2 ASP A 228     5016   3783   4247   -129   -569    527       O1-
ATOM   1001  N   CYS A 229       8.184  32.624 -14.444  1.00 15.79           N  
ANISOU 1001  N   CYS A 229     2227   1475   2296   -317     16    103       N  
ATOM   1002  CA  CYS A 229       7.704  31.406 -13.803  1.00 15.46           C  
ANISOU 1002  CA  CYS A 229     1874   1525   2473   -251    -73     96       C  
ATOM   1003  C   CYS A 229       8.868  30.516 -13.438  1.00 15.58           C  
ANISOU 1003  C   CYS A 229     1838   1604   2474   -331   -131    271       C  
ATOM   1004  O   CYS A 229       9.991  30.723 -13.893  1.00 16.61           O  
ANISOU 1004  O   CYS A 229     1929   1772   2610   -415     60    419       O  
ATOM   1005  CB  CYS A 229       6.719  30.670 -14.714  1.00 16.21           C  
ANISOU 1005  CB  CYS A 229     2219   1490   2450   -472     98    315       C  
ATOM   1006  SG  CYS A 229       7.440  30.043 -16.236  1.00 17.34           S  
ANISOU 1006  SG  CYS A 229     2358   1760   2469   -549     21    175       S  
ATOM   1007  N   THR A 230       8.584  29.525 -12.604  1.00 14.19           N  
ANISOU 1007  N   THR A 230     1766   1569   2057   -414    -59    203       N  
ATOM   1008  CA  THR A 230       9.575  28.577 -12.159  1.00 14.21           C  
ANISOU 1008  CA  THR A 230     1780   1519   2100   -163    -89     84       C  
ATOM   1009  C   THR A 230       9.345  27.269 -12.884  1.00 13.98           C  
ANISOU 1009  C   THR A 230     1701   1548   2059   -410     16    104       C  
ATOM   1010  O   THR A 230       8.241  26.737 -12.876  1.00 17.59           O  
ANISOU 1010  O   THR A 230     1722   2304   2656   -764     77   -404       O  
ATOM   1011  CB  THR A 230       9.449  28.353 -10.652  1.00 15.68           C  
ANISOU 1011  CB  THR A 230     2006   1870   2081   -462   -293    345       C  
ATOM   1012  CG2 THR A 230      10.483  27.336 -10.151  1.00 18.46           C  
ANISOU 1012  CG2 THR A 230     2831   1858   2325   -349   -429    399       C  
ATOM   1013  OG1 THR A 230       9.626  29.604  -9.981  1.00 18.55           O  
ANISOU 1013  OG1 THR A 230     2793   1570   2682   -460   -550    -55       O  
ATOM   1014  N   THR A 231      10.385  26.740 -13.508  1.00 14.24           N  
ANISOU 1014  N   THR A 231     1753   1330   2326   -315    -95    239       N  
ATOM   1015  CA  THR A 231      10.240  25.489 -14.242  1.00 14.46           C  
ANISOU 1015  CA  THR A 231     1883   1556   2053   -198    -35    294       C  
ATOM   1016  C   THR A 231      10.884  24.332 -13.494  1.00 14.03           C  
ANISOU 1016  C   THR A 231     1537   1401   2390   -321   -135    284       C  
ATOM   1017  O   THR A 231      12.002  24.453 -12.984  1.00 16.69           O  
ANISOU 1017  O   THR A 231     1688   1874   2778   -463   -240    418       O  
ATOM   1018  CB  THR A 231      10.803  25.613 -15.671  1.00 16.89           C  
ANISOU 1018  CB  THR A 231     2394   1724   2300   -383     93    364       C  
ATOM   1019  CG2 THR A 231      10.663  24.304 -16.441  1.00 19.03           C  
ANISOU 1019  CG2 THR A 231     2866   2203   2161   -485    182   -273       C  
ATOM   1020  OG1 THR A 231      10.070  26.622 -16.368  1.00 18.63           O  
ANISOU 1020  OG1 THR A 231     2453   2091   2532   -384     77    688       O  
ATOM   1021  N   ILE A 232      10.157  23.222 -13.416  1.00 13.43           N  
ANISOU 1021  N   ILE A 232     1631   1508   1961   -310    -75    189       N  
ATOM   1022  CA  ILE A 232      10.709  21.976 -12.910  1.00 13.33           C  
ANISOU 1022  CA  ILE A 232     1675   1538   1851   -317    -55    300       C  
ATOM   1023  C   ILE A 232      10.704  20.983 -14.062  1.00 13.23           C  
ANISOU 1023  C   ILE A 232     1744   1470   1811   -423     27    125       C  
ATOM   1024  O   ILE A 232       9.720  20.884 -14.803  1.00 14.42           O  
ANISOU 1024  O   ILE A 232     1659   1745   2075   -321   -216    -23       O  
ATOM   1025  CB  ILE A 232       9.899  21.427 -11.711  1.00 14.30           C  
ANISOU 1025  CB  ILE A 232     2038   1437   1959    -88    -55    224       C  
ATOM   1026  CG1 ILE A 232       9.941  22.433 -10.550  1.00 16.33           C  
ANISOU 1026  CG1 ILE A 232     2237   1822   2144   -199    339     24       C  
ATOM   1027  CG2 ILE A 232      10.447  20.072 -11.260  1.00 14.16           C  
ANISOU 1027  CG2 ILE A 232     2012   1490   1878   -182   -126    138       C  
ATOM   1028  CD1 ILE A 232       8.951  22.141  -9.433  1.00 16.63           C  
ANISOU 1028  CD1 ILE A 232     1828   1983   2505   -131    -32    360       C  
ATOM   1029  N   HIS A 233      11.803  20.250 -14.205  1.00 13.86           N  
ANISOU 1029  N   HIS A 233     1651   1481   2133   -231    143    161       N  
ATOM   1030  CA  HIS A 233      11.933  19.235 -15.239  1.00 13.85           C  
ANISOU 1030  CA  HIS A 233     1892   1568   1801   -191    268    144       C  
ATOM   1031  C   HIS A 233      11.643  17.862 -14.655  1.00 13.01           C  
ANISOU 1031  C   HIS A 233     1653   1554   1736   -269    102     -9       C  
ATOM   1032  O   HIS A 233      12.464  17.292 -13.927  1.00 15.27           O  
ANISOU 1032  O   HIS A 233     1685   1972   2144   -209   -162    442       O  
ATOM   1033  CB  HIS A 233      13.345  19.247 -15.834  1.00 15.96           C  
ANISOU 1033  CB  HIS A 233     2041   1732   2288   -169    405    269       C  
ATOM   1034  CG  HIS A 233      13.636  20.427 -16.706  1.00 19.64           C  
ANISOU 1034  CG  HIS A 233     2135   2687   2640   -290    738    251       C  
ATOM   1035  CD2 HIS A 233      12.816  21.326 -17.297  1.00 20.11           C  
ANISOU 1035  CD2 HIS A 233     3179   1732   2728   -230    538    472       C  
ATOM   1036  ND1 HIS A 233      14.918  20.778 -17.074  1.00 24.65           N  
ANISOU 1036  ND1 HIS A 233     2873   3024   3468    -86    735    624       N  
ATOM   1037  CE1 HIS A 233      14.874  21.847 -17.849  1.00 26.43           C  
ANISOU 1037  CE1 HIS A 233     3572   3018   3450   -424    273    788       C  
ATOM   1038  NE2 HIS A 233      13.610  22.202 -17.997  1.00 24.77           N  
ANISOU 1038  NE2 HIS A 233     3117   2829   3466   -441    707   1227       N  
ATOM   1039  N   TYR A 234      10.463  17.343 -14.961  1.00 12.35           N  
ANISOU 1039  N   TYR A 234     1514   1564   1613   -148     22    123       N  
ATOM   1040  CA  TYR A 234      10.079  16.007 -14.533  1.00 12.34           C  
ANISOU 1040  CA  TYR A 234     1563   1393   1731   -116    194    281       C  
ATOM   1041  C   TYR A 234      10.453  14.978 -15.591  1.00 12.68           C  
ANISOU 1041  C   TYR A 234     1661   1698   1456   -123     52    136       C  
ATOM   1042  O   TYR A 234      10.533  15.290 -16.781  1.00 14.17           O  
ANISOU 1042  O   TYR A 234     1999   1860   1524     41    183    230       O  
ATOM   1043  CB  TYR A 234       8.580  15.959 -14.240  1.00 13.30           C  
ANISOU 1043  CB  TYR A 234     1846   1635   1570   -313     78    271       C  
ATOM   1044  CG  TYR A 234       8.192  16.755 -13.017  1.00 11.97           C  
ANISOU 1044  CG  TYR A 234     1592   1437   1516   -309     21     23       C  
ATOM   1045  CD1 TYR A 234       8.512  16.293 -11.740  1.00 11.88           C  
ANISOU 1045  CD1 TYR A 234     1353   1623   1537   -331     36    217       C  
ATOM   1046  CD2 TYR A 234       7.495  17.956 -13.127  1.00 13.25           C  
ANISOU 1046  CD2 TYR A 234     1553   1705   1775   -172     40    129       C  
ATOM   1047  CE1 TYR A 234       8.166  17.008 -10.602  1.00 11.25           C  
ANISOU 1047  CE1 TYR A 234     1385   1383   1505   -294     27    145       C  
ATOM   1048  CE2 TYR A 234       7.145  18.686 -11.997  1.00 12.70           C  
ANISOU 1048  CE2 TYR A 234     1477   1764   1584   -252     90    295       C  
ATOM   1049  CZ  TYR A 234       7.483  18.207 -10.740  1.00 11.50           C  
ANISOU 1049  CZ  TYR A 234     1327   1344   1696   -199     83    175       C  
ATOM   1050  OH  TYR A 234       7.119  18.935  -9.630  1.00 12.18           O  
ANISOU 1050  OH  TYR A 234     1672   1376   1577   -206     72     36       O  
ATOM   1051  N   ASN A 235      10.688  13.751 -15.138  1.00 12.71           N  
ANISOU 1051  N   ASN A 235     1709   1339   1781     54    -26    174       N  
ATOM   1052  CA  ASN A 235      10.889  12.612 -16.020  1.00 13.00           C  
ANISOU 1052  CA  ASN A 235     1770   1407   1762    141    161     71       C  
ATOM   1053  C   ASN A 235       9.941  11.504 -15.568  1.00 12.95           C  
ANISOU 1053  C   ASN A 235     1873   1475   1569     93    139     86       C  
ATOM   1054  O   ASN A 235       9.852  11.221 -14.372  1.00 14.96           O  
ANISOU 1054  O   ASN A 235     2494   1736   1455   -321    -22    174       O  
ATOM   1055  CB  ASN A 235      12.328  12.074 -15.930  1.00 15.58           C  
ANISOU 1055  CB  ASN A 235     2161   1807   1950    124     34     94       C  
ATOM   1056  CG  ASN A 235      13.386  13.083 -16.349  1.00 17.42           C  
ANISOU 1056  CG  ASN A 235     2209   1906   2503    199     -5    109       C  
ATOM   1057  ND2 ASN A 235      14.598  12.870 -15.856  1.00 20.99           N  
ANISOU 1057  ND2 ASN A 235     2225   2569   3179    -20   -210    608       N  
ATOM   1058  OD1 ASN A 235      13.139  14.020 -17.115  1.00 19.50           O  
ANISOU 1058  OD1 ASN A 235     2511   2623   2273    -76    336    276       O  
ATOM   1059  N   TYR A 236       9.253  10.879 -16.516  1.00 12.32           N  
ANISOU 1059  N   TYR A 236     1786   1440   1454    204    121     60       N  
ATOM   1060  CA  TYR A 236       8.377   9.740 -16.230  1.00 13.00           C  
ANISOU 1060  CA  TYR A 236     1834   1373   1729     82    -10    123       C  
ATOM   1061  C   TYR A 236       9.059   8.476 -16.715  1.00 13.94           C  
ANISOU 1061  C   TYR A 236     2197   1483   1616    141    106     82       C  
ATOM   1062  O   TYR A 236       9.479   8.395 -17.870  1.00 14.53           O  
ANISOU 1062  O   TYR A 236     2394   1594   1533    314    295    188       O  
ATOM   1063  CB  TYR A 236       7.024   9.936 -16.915  1.00 13.77           C  
ANISOU 1063  CB  TYR A 236     1995   1611   1626     61    -54    -29       C  
ATOM   1064  CG  TYR A 236       6.232  11.103 -16.354  1.00 12.66           C  
ANISOU 1064  CG  TYR A 236     1862   1484   1461    136    -70    185       C  
ATOM   1065  CD1 TYR A 236       6.466  12.409 -16.794  1.00 13.11           C  
ANISOU 1065  CD1 TYR A 236     1742   1556   1681    153    -93    208       C  
ATOM   1066  CD2 TYR A 236       5.260  10.897 -15.370  1.00 12.85           C  
ANISOU 1066  CD2 TYR A 236     1743   1709   1429    -15    -49     98       C  
ATOM   1067  CE1 TYR A 236       5.746  13.480 -16.274  1.00 12.54           C  
ANISOU 1067  CE1 TYR A 236     1446   1528   1789     46    104    116       C  
ATOM   1068  CE2 TYR A 236       4.535  11.961 -14.848  1.00 12.55           C  
ANISOU 1068  CE2 TYR A 236     2007   1266   1492     75    -71    -14       C  
ATOM   1069  CZ  TYR A 236       4.788  13.250 -15.302  1.00 12.36           C  
ANISOU 1069  CZ  TYR A 236     1597   1519   1577      9   -126    173       C  
ATOM   1070  OH  TYR A 236       4.093  14.321 -14.795  1.00 13.19           O  
ANISOU 1070  OH  TYR A 236     1869   1335   1807    155     20      0       O  
ATOM   1071  N   MET A 237       9.147   7.485 -15.835  1.00 13.91           N  
ANISOU 1071  N   MET A 237     2030   1554   1701    183     89    100       N  
ATOM   1072  CA  MET A 237      10.092   6.385 -16.017  1.00 15.20           C  
ANISOU 1072  CA  MET A 237     2210   1433   2129    358     40   -133       C  
ATOM   1073  C   MET A 237       9.456   5.053 -16.420  1.00 15.72           C  
ANISOU 1073  C   MET A 237     2583   1455   1933    202    343     13       C  
ATOM   1074  O   MET A 237      10.118   4.016 -16.442  1.00 20.08           O  
ANISOU 1074  O   MET A 237     2655   1517   3455    523    404    140       O  
ATOM   1075  CB  MET A 237      10.955   6.243 -14.761  1.00 17.24           C  
ANISOU 1075  CB  MET A 237     2388   2218   1942    556     17    168       C  
ATOM   1076  CG  MET A 237      11.721   7.514 -14.377  1.00 17.46           C  
ANISOU 1076  CG  MET A 237     2375   2228   2031    331    -71     15       C  
ATOM   1077  SD  MET A 237      12.768   8.190 -15.692  1.00 18.90           S  
ANISOU 1077  SD  MET A 237     2284   2433   2464    295   -106    138       S  
ATOM   1078  CE  MET A 237      13.849   6.795 -16.048  1.00 22.63           C  
ANISOU 1078  CE  MET A 237     2384   3480   2733    564    609     28       C  
ATOM   1079  N   CYS A 238       8.170   5.118 -16.750  1.00 14.76           N  
ANISOU 1079  N   CYS A 238     2374   1570   1662     30    122     11       N  
ATOM   1080  CA ACYS A 238       7.384   3.986 -17.215  0.50 17.98           C  
ANISOU 1080  CA ACYS A 238     2471   1982   2378    -39    199     14       C  
ATOM   1081  CA BCYS A 238       7.433   3.987 -17.301  0.50 14.12           C  
ANISOU 1081  CA BCYS A 238     2203   1365   1796    -32    491     68       C  
ATOM   1082  C   CYS A 238       6.416   4.519 -18.277  1.00 16.05           C  
ANISOU 1082  C   CYS A 238     2122   1734   2242    -49    167   -360       C  
ATOM   1083  O   CYS A 238       5.941   5.643 -18.139  1.00 16.84           O  
ANISOU 1083  O   CYS A 238     2510   1338   2548    163    244   -202       O  
ATOM   1084  CB ACYS A 238       6.591   3.442 -16.028  0.50 22.87           C  
ANISOU 1084  CB ACYS A 238     3322   2154   3212   -297    322    443       C  
ATOM   1085  CB BCYS A 238       6.703   3.205 -16.217  0.50 15.31           C  
ANISOU 1085  CB BCYS A 238     2848    431   2537    380    850    341       C  
ATOM   1086  SG ACYS A 238       6.323   1.680 -15.964  0.50 15.57           S  
ANISOU 1086  SG ACYS A 238     3037   1281   1597     98    523    154       S  
ATOM   1087  SG BCYS A 238       7.521   1.729 -15.682  0.50 16.33           S  
ANISOU 1087  SG BCYS A 238     2999   1367   1839     16   -258    -90       S  
ATOM   1088  N   ASN A 239       6.114   3.715 -19.296  1.00 17.12           N  
ANISOU 1088  N   ASN A 239     2132   1760   2610    -85    178   -445       N  
ATOM   1089  CA AASN A 239       5.096   4.070 -20.280  0.50 17.17           C  
ANISOU 1089  CA AASN A 239     2404   1870   2250   -152    231   -305       C  
ATOM   1090  CA BASN A 239       5.096   4.060 -20.286  0.50 17.56           C  
ANISOU 1090  CA BASN A 239     2480   1888   2302   -151    193   -293       C  
ATOM   1091  C   ASN A 239       3.688   3.799 -19.761  1.00 15.53           C  
ANISOU 1091  C   ASN A 239     2264   1452   2184    -41     81   -245       C  
ATOM   1092  O   ASN A 239       3.482   2.900 -18.955  1.00 15.48           O  
ANISOU 1092  O   ASN A 239     2454   1552   1875     38    137    121       O  
ATOM   1093  CB AASN A 239       5.329   3.315 -21.592  0.50 18.18           C  
ANISOU 1093  CB AASN A 239     2229   2055   2624   -119    403   -406       C  
ATOM   1094  CB BASN A 239       5.323   3.265 -21.577  0.50 19.72           C  
ANISOU 1094  CB BASN A 239     2663   2167   2662    -36    248   -441       C  
ATOM   1095  CG AASN A 239       5.982   4.175 -22.652  0.50 22.51           C  
ANISOU 1095  CG AASN A 239     2850   3000   2700    319    852   -406       C  
ATOM   1096  CG BASN A 239       6.345   3.909 -22.488  0.50 25.26           C  
ANISOU 1096  CG BASN A 239     3548   2810   3240    111    421   -123       C  
ATOM   1097  ND2AASN A 239       5.640   3.920 -23.909  0.50 30.14           N  
ANISOU 1097  ND2AASN A 239     3716   4090   3644     -4    -95   -219       N  
ATOM   1098  OD1AASN A 239       6.783   5.060 -22.347  0.50 23.22           O  
ANISOU 1098  OD1AASN A 239     2984   2672   3165   -278    439    401       O  
ATOM   1099  ND2BASN A 239       7.442   3.204 -22.736  0.50 26.60           N  
ANISOU 1099  ND2BASN A 239     3353   3471   3281     75    237   -587       N  
ATOM   1100  OD1BASN A 239       6.144   5.023 -22.977  0.50 21.39           O  
ANISOU 1100  OD1BASN A 239     2584   2441   3100   -206      1    103       O  
ATOM   1101  N   SER A 240       2.712   4.573 -20.227  1.00 16.75           N  
ANISOU 1101  N   SER A 240     2404   1545   2416   -268    -71     55       N  
ATOM   1102  CA  SER A 240       1.324   4.335 -19.824  1.00 16.37           C  
ANISOU 1102  CA  SER A 240     2376   1483   2359   -158   -181    209       C  
ATOM   1103  C   SER A 240       0.896   2.910 -20.161  1.00 16.67           C  
ANISOU 1103  C   SER A 240     2246   1779   2306    -26   -139    274       C  
ATOM   1104  O   SER A 240       0.082   2.311 -19.456  1.00 18.88           O  
ANISOU 1104  O   SER A 240     2575   2051   2544   -426     59    350       O  
ATOM   1105  CB  SER A 240       0.382   5.339 -20.489  1.00 17.85           C  
ANISOU 1105  CB  SER A 240     2449   1767   2566     36    -94    350       C  
ATOM   1106  OG  SER A 240       0.603   6.635 -19.972  1.00 19.61           O  
ANISOU 1106  OG  SER A 240     2931   1490   3028   -103    -81    190       O  
ATOM   1107  N   SER A 241       1.464   2.370 -21.237  1.00 16.40           N  
ANISOU 1107  N   SER A 241     2354   1740   2138   -233   -395    208       N  
ATOM   1108  CA  SER A 241       1.088   1.061 -21.750  1.00 19.83           C  
ANISOU 1108  CA  SER A 241     3108   2005   2418     76   -124   -333       C  
ATOM   1109  C   SER A 241       1.783  -0.095 -21.049  1.00 20.84           C  
ANISOU 1109  C   SER A 241     2733   2439   2744   -138   -463    101       C  
ATOM   1110  O   SER A 241       1.531  -1.252 -21.393  1.00 24.42           O  
ANISOU 1110  O   SER A 241     3306   2323   3649   -587   -428    -55       O  
ATOM   1111  CB  SER A 241       1.415   0.990 -23.241  1.00 23.85           C  
ANISOU 1111  CB  SER A 241     3749   2920   2390   -338    -90   -494       C  
ATOM   1112  OG  SER A 241       2.821   0.944 -23.433  1.00 28.30           O  
ANISOU 1112  OG  SER A 241     4059   3917   2774   -269    302   -546       O  
ATOM   1113  N   CYS A 242       2.664   0.200 -20.092  1.00 17.16           N  
ANISOU 1113  N   CYS A 242     2575   1712   2234    135    323    263       N  
ATOM   1114  CA  CYS A 242       3.389  -0.863 -19.399  1.00 19.30           C  
ANISOU 1114  CA  CYS A 242     2245   2192   2894    -20     19    305       C  
ATOM   1115  C   CYS A 242       2.410  -1.766 -18.662  1.00 19.38           C  
ANISOU 1115  C   CYS A 242     2868   1569   2926     60     84   -135       C  
ATOM   1116  O   CYS A 242       1.708  -1.320 -17.753  1.00 21.50           O  
ANISOU 1116  O   CYS A 242     2572   2400   3195    239    498   -117       O  
ATOM   1117  CB  CYS A 242       4.429  -0.287 -18.435  1.00 18.77           C  
ANISOU 1117  CB  CYS A 242     2561   2335   2234    119    314    535       C  
ATOM   1118  SG  CYS A 242       5.967   0.300 -19.220  1.00 15.78           S  
ANISOU 1118  SG  CYS A 242     2289   1731   1972    187    250    117       S  
ATOM   1119  N   MET A 243       2.343  -3.028 -19.080  1.00 21.80           N  
ANISOU 1119  N   MET A 243     2832   2351   3099     24    281   -257       N  
ATOM   1120  CA  MET A 243       1.487  -3.998 -18.403  1.00 21.53           C  
ANISOU 1120  CA  MET A 243     2898   2487   2794   -272    -80   -200       C  
ATOM   1121  C   MET A 243       2.136  -4.439 -17.094  1.00 22.07           C  
ANISOU 1121  C   MET A 243     3038   2189   3159    -34     55    -92       C  
ATOM   1122  O   MET A 243       3.363  -4.500 -16.990  1.00 23.24           O  
ANISOU 1122  O   MET A 243     2817   2748   3263     14    238    161       O  
ATOM   1123  CB  MET A 243       1.161  -5.191 -19.307  1.00 26.33           C  
ANISOU 1123  CB  MET A 243     3859   2549   3596   -479    -92   -399       C  
ATOM   1124  CG  MET A 243       0.321  -4.834 -20.549  1.00 26.59           C  
ANISOU 1124  CG  MET A 243     3164   3556   3381     12     29   -310       C  
ATOM   1125  SD  MET A 243      -1.150  -3.830 -20.215  1.00 30.54           S  
ANISOU 1125  SD  MET A 243     3388   3840   4374    -15   -111   -977       S  
ATOM   1126  CE  MET A 243      -2.035  -3.981 -21.764  1.00 35.45           C  
ANISOU 1126  CE  MET A 243     4448   4725   4297   -292   -392   -397       C  
ATOM   1127  N   GLY A 244       1.304  -4.720 -16.093  1.00 23.77           N  
ANISOU 1127  N   GLY A 244     3293   2596   3143   -174    246    -49       N  
ATOM   1128  CA  GLY A 244       1.790  -4.971 -14.739  1.00 26.23           C  
ANISOU 1128  CA  GLY A 244     3934   2561   3470    -14     81     40       C  
ATOM   1129  C   GLY A 244       2.052  -3.668 -14.008  1.00 23.68           C  
ANISOU 1129  C   GLY A 244     3646   2106   3245    356     30    113       C  
ATOM   1130  O   GLY A 244       2.560  -3.662 -12.885  1.00 27.12           O  
ANISOU 1130  O   GLY A 244     3969   3093   3240    457     57    302       O  
ATOM   1131  N   GLY A 245       1.709  -2.560 -14.662  1.00 26.43           N  
ANISOU 1131  N   GLY A 245     4136   2321   3582    523    -75   -241       N  
ATOM   1132  CA  GLY A 245       1.819  -1.232 -14.081  1.00 25.39           C  
ANISOU 1132  CA  GLY A 245     3553   2532   3562    477   -133   -283       C  
ATOM   1133  C   GLY A 245       0.565  -0.453 -14.406  1.00 22.58           C  
ANISOU 1133  C   GLY A 245     3190   2146   3242    116    -32    -32       C  
ATOM   1134  O   GLY A 245      -0.536  -0.837 -14.001  1.00 24.36           O  
ANISOU 1134  O   GLY A 245     3498   2429   3327     96    179     20       O  
ATOM   1135  N   MET A 246       0.727   0.632 -15.158  1.00 21.46           N  
ANISOU 1135  N   MET A 246     2838   1829   3485   -102   -229   -245       N  
ATOM   1136  CA  MET A 246      -0.400   1.503 -15.489  1.00 20.40           C  
ANISOU 1136  CA  MET A 246     2734   2238   2776    -87     50     65       C  
ATOM   1137  C   MET A 246      -1.416   0.875 -16.439  1.00 19.16           C  
ANISOU 1137  C   MET A 246     2667   1669   2943     13     17    -41       C  
ATOM   1138  O   MET A 246      -2.565   1.308 -16.486  1.00 19.13           O  
ANISOU 1138  O   MET A 246     2472   2037   2759     85    108   -266       O  
ATOM   1139  CB  MET A 246       0.096   2.851 -15.994  1.00 19.59           C  
ANISOU 1139  CB  MET A 246     2855   2067   2518   -644    264   -285       C  
ATOM   1140  CG  MET A 246       0.704   3.694 -14.882  1.00 18.28           C  
ANISOU 1140  CG  MET A 246     2435   1897   2612   -304    209   -355       C  
ATOM   1141  SD  MET A 246       1.322   5.281 -15.433  1.00 20.47           S  
ANISOU 1141  SD  MET A 246     2648   2604   2523   -439    -19   -153       S  
ATOM   1142  CE  MET A 246       2.863   4.820 -16.224  1.00 21.26           C  
ANISOU 1142  CE  MET A 246     2676   3222   2178   -156    526     95       C  
ATOM   1143  N   ASN A 247      -1.003  -0.152 -17.181  1.00 19.09           N  
ANISOU 1143  N   ASN A 247     2661   1975   2617   -353    209   -431       N  
ATOM   1144  CA  ASN A 247      -1.951  -0.983 -17.943  1.00 21.15           C  
ANISOU 1144  CA  ASN A 247     2801   2407   2826   -236     95   -184       C  
ATOM   1145  C   ASN A 247      -2.831  -0.179 -18.904  1.00 21.58           C  
ANISOU 1145  C   ASN A 247     2697   2535   2966   -187   -233   -175       C  
ATOM   1146  O   ASN A 247      -4.015  -0.493 -19.079  1.00 23.47           O  
ANISOU 1146  O   ASN A 247     2922   2810   3186   -394     -9   -264       O  
ATOM   1147  CB  ASN A 247      -2.852  -1.791 -16.994  1.00 22.26           C  
ANISOU 1147  CB  ASN A 247     2729   2387   3342   -564    -96    191       C  
ATOM   1148  CG  ASN A 247      -2.112  -2.892 -16.252  1.00 21.85           C  
ANISOU 1148  CG  ASN A 247     2738   2372   3189   -207    227     72       C  
ATOM   1149  ND2 ASN A 247      -2.841  -3.620 -15.413  1.00 23.41           N  
ANISOU 1149  ND2 ASN A 247     2904   2536   3452   -250    308    176       N  
ATOM   1150  OD1 ASN A 247      -0.911  -3.090 -16.427  1.00 24.41           O  
ANISOU 1150  OD1 ASN A 247     2810   2720   3744    119    234   -168       O  
ATOM   1151  N   ARG A 248      -2.248   0.861 -19.507  1.00 20.80           N  
ANISOU 1151  N   ARG A 248     3158   2549   2195   -281    -71   -154       N  
ATOM   1152  CA  ARG A 248      -2.937   1.756 -20.455  1.00 22.84           C  
ANISOU 1152  CA  ARG A 248     3012   3138   2527    103   -440   -103       C  
ATOM   1153  C   ARG A 248      -3.919   2.730 -19.791  1.00 23.08           C  
ANISOU 1153  C   ARG A 248     3056   3117   2597     62   -253    -77       C  
ATOM   1154  O   ARG A 248      -4.489   3.597 -20.461  1.00 27.50           O  
ANISOU 1154  O   ARG A 248     3730   3485   3232    270   -424     20       O  
ATOM   1155  CB  ARG A 248      -3.620   0.972 -21.589  1.00 24.45           C  
ANISOU 1155  CB  ARG A 248     3058   3631   2598     10   -305   -287       C  
ATOM   1156  CG  ARG A 248      -2.663   0.157 -22.453  1.00 24.75           C  
ANISOU 1156  CG  ARG A 248     3234   3425   2743    -93   -177   -799       C  
ATOM   1157  CD  ARG A 248      -3.386  -0.504 -23.623  1.00 29.56           C  
ANISOU 1157  CD  ARG A 248     3650   4193   3386   -196   -304   -607       C  
ATOM   1158  NE  ARG A 248      -4.184  -1.653 -23.204  1.00 38.54           N  
ANISOU 1158  NE  ARG A 248     5143   4391   5108    -75     -4    176       N  
ATOM   1159  N   ARG A 249      -4.091   2.605 -18.470  1.00  0.00           N  
ATOM   1160  CA  ARG A 249      -5.046   3.429 -17.733  1.00  0.00           C  
ATOM   1161  C   ARG A 249      -4.481   4.804 -17.468  1.00  0.00           C  
ATOM   1162  O   ARG A 249      -3.315   4.930 -17.075  1.00  0.00           O  
ATOM   1163  CB  ARG A 249      -5.417   2.703 -16.409  1.00  0.00           C  
ATOM   1164  CG  ARG A 249      -6.131   1.332 -16.574  1.00  0.00           C  
ATOM   1165  CD  ARG A 249      -7.579   1.491 -17.067  1.00  0.00           C  
ATOM   1166  NE  ARG A 249      -8.276   0.173 -17.008  1.00  0.00           N  
ATOM   1167  CZ  ARG A 249      -8.286  -0.736 -17.979  1.00  0.00           C  
ATOM   1168  NH1 ARG A 249      -7.670  -0.583 -19.117  1.00  0.00           N1+
ATOM   1169  NH2 ARG A 249      -8.944  -1.836 -17.785  1.00  0.00           N  
ATOM   1170  N   PRO A 250      -5.295   5.866 -17.681  1.00 20.16           N  
ANISOU 1170  N   PRO A 250     2818   2600   2241    182   -761   -410       N  
ATOM   1171  CA APRO A 250      -4.822   7.238 -17.509  0.50 17.99           C  
ANISOU 1171  CA APRO A 250     2737   2207   1891   -216   -538   -152       C  
ATOM   1172  CA BPRO A 250      -4.794   7.226 -17.510  0.50 17.79           C  
ANISOU 1172  CA BPRO A 250     2756   2215   1786   -159   -629   -103       C  
ATOM   1173  C   PRO A 250      -4.414   7.568 -16.078  1.00 15.46           C  
ANISOU 1173  C   PRO A 250     2503   1958   1412   -179   -195     61       C  
ATOM   1174  O   PRO A 250      -5.067   7.125 -15.124  1.00 15.84           O  
ANISOU 1174  O   PRO A 250     2054   2100   1863   -587   -551    -46       O  
ATOM   1175  CB APRO A 250      -6.036   8.081 -17.912  0.50 21.50           C  
ANISOU 1175  CB APRO A 250     2793   2768   2605    -11   -513     41       C  
ATOM   1176  CB BPRO A 250      -5.972   8.099 -17.953  0.50 19.94           C  
ANISOU 1176  CB BPRO A 250     2707   2758   2110     87   -788     60       C  
ATOM   1177  CG APRO A 250      -7.212   7.176 -17.736  0.50 18.36           C  
ANISOU 1177  CG APRO A 250     2210   2734   2032    134     39   -280       C  
ATOM   1178  CG BPRO A 250      -6.824   7.209 -18.784  0.50 23.47           C  
ANISOU 1178  CG BPRO A 250     3144   3280   2491   -201   -732   -469       C  
ATOM   1179  CD APRO A 250      -6.702   5.827 -18.119  0.50 21.33           C  
ANISOU 1179  CD APRO A 250     2512   2665   2926    -16   -402   -170       C  
ATOM   1180  CD BPRO A 250      -6.694   5.865 -18.140  0.50 22.49           C  
ANISOU 1180  CD BPRO A 250     2617   2968   2960   -129   -518   -225       C  
ATOM   1181  N   ILE A 251      -3.355   8.351 -15.950  1.00 15.15           N  
ANISOU 1181  N   ILE A 251     2400   1666   1688   -391   -403    210       N  
ATOM   1182  CA  ILE A 251      -2.939   8.864 -14.664  1.00 13.11           C  
ANISOU 1182  CA  ILE A 251     1871   1517   1593   -338   -413     97       C  
ATOM   1183  C   ILE A 251      -3.001  10.380 -14.649  1.00 13.00           C  
ANISOU 1183  C   ILE A 251     1715   1629   1595   -403   -166    304       C  
ATOM   1184  O   ILE A 251      -2.975  11.040 -15.703  1.00 14.15           O  
ANISOU 1184  O   ILE A 251     2143   1731   1502   -569   -233    410       O  
ATOM   1185  CB  ILE A 251      -1.524   8.396 -14.250  1.00 16.92           C  
ANISOU 1185  CB  ILE A 251     2300   2073   2053    -63    188    716       C  
ATOM   1186  CG1 ILE A 251      -0.454   8.856 -15.243  1.00 19.40           C  
ANISOU 1186  CG1 ILE A 251     1988   3155   2226      2    -48    690       C  
ATOM   1187  CG2 ILE A 251      -1.507   6.885 -14.049  1.00 17.37           C  
ANISOU 1187  CG2 ILE A 251     2066   2100   2433   -200    -74    744       C  
ATOM   1188  CD1 ILE A 251       0.955   8.836 -14.650  1.00 20.31           C  
ANISOU 1188  CD1 ILE A 251     1842   3285   2588   -147   -156    992       C  
ATOM   1189  N   LEU A 252      -3.108  10.908 -13.435  1.00 13.07           N  
ANISOU 1189  N   LEU A 252     1940   1597   1426   -394   -290    116       N  
ATOM   1190  CA  LEU A 252      -2.970  12.321 -13.167  1.00 13.25           C  
ANISOU 1190  CA  LEU A 252     2106   1313   1614   -418   -417    204       C  
ATOM   1191  C   LEU A 252      -1.685  12.546 -12.401  1.00 12.63           C  
ANISOU 1191  C   LEU A 252     1825   1368   1605   -389   -416    145       C  
ATOM   1192  O   LEU A 252      -1.320  11.750 -11.543  1.00 14.24           O  
ANISOU 1192  O   LEU A 252     2140   1509   1760   -507   -646    532       O  
ATOM   1193  CB  LEU A 252      -4.142  12.818 -12.319  1.00 15.69           C  
ANISOU 1193  CB  LEU A 252     2075   2175   1710   -296   -206     41       C  
ATOM   1194  CG  LEU A 252      -5.560  12.557 -12.828  1.00 16.01           C  
ANISOU 1194  CG  LEU A 252     1978   2215   1889   -283   -141    111       C  
ATOM   1195  CD1 LEU A 252      -6.572  13.113 -11.853  1.00 22.77           C  
ANISOU 1195  CD1 LEU A 252     2534   3761   2355    -22     41    -35       C  
ATOM   1196  CD2 LEU A 252      -5.766  13.137 -14.227  1.00 21.71           C  
ANISOU 1196  CD2 LEU A 252     2392   3347   2507    -92   -383    527       C  
ATOM   1197  N   THR A 253      -0.992  13.628 -12.729  1.00 11.07           N  
ANISOU 1197  N   THR A 253     1595   1176   1432   -315   -191     43       N  
ATOM   1198  CA  THR A 253       0.048  14.149 -11.856  1.00 10.67           C  
ANISOU 1198  CA  THR A 253     1587   1042   1422   -216    -84     50       C  
ATOM   1199  C   THR A 253      -0.552  15.279 -11.036  1.00  9.98           C  
ANISOU 1199  C   THR A 253     1216   1198   1376   -177   -136    241       C  
ATOM   1200  O   THR A 253      -1.168  16.192 -11.583  1.00 11.63           O  
ANISOU 1200  O   THR A 253     1697   1330   1392     83   -101    236       O  
ATOM   1201  CB  THR A 253       1.257  14.660 -12.653  1.00 11.59           C  
ANISOU 1201  CB  THR A 253     1430   1460   1511   -308   -125    108       C  
ATOM   1202  CG2 THR A 253       2.334  15.218 -11.736  1.00 12.33           C  
ANISOU 1202  CG2 THR A 253     1503   1409   1770   -381     16    -33       C  
ATOM   1203  OG1 THR A 253       1.816  13.580 -13.401  1.00 12.65           O  
ANISOU 1203  OG1 THR A 253     1782   1365   1657     68    125    -80       O  
ATOM   1204  N   ILE A 254      -0.370  15.191  -9.719  1.00  9.98           N  
ANISOU 1204  N   ILE A 254     1405   1064   1322   -212    -35    132       N  
ATOM   1205  CA AILE A 254      -0.825  16.211  -8.788  0.50 10.82           C  
ANISOU 1205  CA AILE A 254     1396   1265   1448   -235     -4     65       C  
ATOM   1206  CA BILE A 254      -0.827  16.213  -8.790  0.50 11.21           C  
ANISOU 1206  CA BILE A 254     1448   1331   1481   -262    -53     38       C  
ATOM   1207  C   ILE A 254       0.393  16.981  -8.303  1.00 10.57           C  
ANISOU 1207  C   ILE A 254     1626   1151   1237    -30    -76     34       C  
ATOM   1208  O   ILE A 254       1.325  16.387  -7.754  1.00 10.82           O  
ANISOU 1208  O   ILE A 254     1388   1274   1449    -37   -126    191       O  
ATOM   1209  CB AILE A 254      -1.545  15.584  -7.577  0.50 10.59           C  
ANISOU 1209  CB AILE A 254     1465   1074   1484   -278    182    -83       C  
ATOM   1210  CB BILE A 254      -1.571  15.597  -7.573  0.50 11.46           C  
ANISOU 1210  CB BILE A 254     1374   1440   1541   -327     63      5       C  
ATOM   1211  CG1AILE A 254      -2.818  14.854  -8.017  0.50 11.13           C  
ANISOU 1211  CG1AILE A 254     1263   1311   1654   -131    329    186       C  
ATOM   1212  CG2AILE A 254      -1.854  16.658  -6.533  0.50  9.05           C  
ANISOU 1212  CG2AILE A 254      826   1268   1345   -116     18    108       C  
ATOM   1213  CG1BILE A 254      -2.482  14.427  -7.994  0.50 13.54           C  
ANISOU 1213  CG1BILE A 254     1488   1408   2247   -337   -240    216       C  
ATOM   1214  CG2BILE A 254      -2.315  16.690  -6.786  0.50 13.40           C  
ANISOU 1214  CG2BILE A 254     1656   1676   1759   -392   -215   -308       C  
ATOM   1215  CD1AILE A 254      -3.342  13.881  -6.980  0.50 12.21           C  
ANISOU 1215  CD1AILE A 254     1483   1646   1507   -311    345    241       C  
ATOM   1216  CD1BILE A 254      -3.637  14.796  -8.898  0.50 18.72           C  
ANISOU 1216  CD1BILE A 254     2272   2147   2693     69   -186    517       C  
ATOM   1217  N   ILE A 255       0.378  18.294  -8.515  1.00 10.11           N  
ANISOU 1217  N   ILE A 255     1268   1187   1386    -89    -81    108       N  
ATOM   1218  CA  ILE A 255       1.447  19.175  -8.056  1.00 10.71           C  
ANISOU 1218  CA  ILE A 255     1379   1356   1333   -192    -69    -70       C  
ATOM   1219  C   ILE A 255       0.920  19.975  -6.882  1.00 11.14           C  
ANISOU 1219  C   ILE A 255     1227   1500   1504   -216   -103     36       C  
ATOM   1220  O   ILE A 255      -0.091  20.682  -7.006  1.00 11.55           O  
ANISOU 1220  O   ILE A 255     1390   1424   1573    -31   -111    -54       O  
ATOM   1221  CB  ILE A 255       1.941  20.148  -9.156  1.00 11.46           C  
ANISOU 1221  CB  ILE A 255     1487   1455   1410   -347   -168    191       C  
ATOM   1222  CG1 ILE A 255       2.317  19.400 -10.442  1.00 11.79           C  
ANISOU 1222  CG1 ILE A 255     1570   1570   1339    -60     -4    149       C  
ATOM   1223  CG2 ILE A 255       3.090  20.996  -8.617  1.00 12.27           C  
ANISOU 1223  CG2 ILE A 255     1479   1468   1712   -273    -69    -63       C  
ATOM   1224  CD1 ILE A 255       3.482  18.441 -10.320  1.00 12.89           C  
ANISOU 1224  CD1 ILE A 255     1507   1532   1856   -294   -146   -197       C  
ATOM   1225  N   THR A 256       1.583  19.838  -5.739  1.00 11.10           N  
ANISOU 1225  N   THR A 256     1343   1581   1294   -132     -3   -138       N  
ATOM   1226  CA ATHR A 256       1.199  20.518  -4.512  0.50 11.72           C  
ANISOU 1226  CA ATHR A 256     1255   1526   1672   -199     73    -86       C  
ATOM   1227  CA BTHR A 256       1.184  20.605  -4.571  0.50 12.80           C  
ANISOU 1227  CA BTHR A 256     1501   1690   1670   -345     25   -109       C  
ATOM   1228  C   THR A 256       2.279  21.509  -4.076  1.00 11.36           C  
ANISOU 1228  C   THR A 256     1180   1668   1468   -239     11   -164       C  
ATOM   1229  O   THR A 256       3.453  21.145  -4.023  1.00 13.36           O  
ANISOU 1229  O   THR A 256     1353   1560   2161   -116    -47   -413       O  
ATOM   1230  CB ATHR A 256       0.970  19.488  -3.379  0.50 11.47           C  
ANISOU 1230  CB ATHR A 256     1190   1677   1489   -346     97   -185       C  
ATOM   1231  CB BTHR A 256       0.714  19.729  -3.409  0.50 14.21           C  
ANISOU 1231  CB BTHR A 256     1900   1740   1758   -229    -44   -183       C  
ATOM   1232  CG2ATHR A 256       0.332  20.145  -2.172  0.50 12.40           C  
ANISOU 1232  CG2ATHR A 256     1575   1454   1680   -134    174   -116       C  
ATOM   1233  OG1ATHR A 256       0.111  18.439  -3.847  0.50 12.94           O  
ANISOU 1233  OG1ATHR A 256     1508   1515   1891    -66   -124    173       O  
ATOM   1234  CG2BTHR A 256      -0.642  19.144  -3.718  0.50 12.99           C  
ANISOU 1234  CG2BTHR A 256     1224   1760   1950   -106   -190   -207       C  
ATOM   1235  OG1BTHR A 256       1.665  18.686  -3.186  0.50 11.76           O  
ANISOU 1235  OG1BTHR A 256     1177   1585   1705   -128     22    -33       O  
ATOM   1236  N   LEU A 257       1.871  22.727  -3.756  1.00 11.20           N  
ANISOU 1236  N   LEU A 257     1399   1244   1611   -153   -117   -124       N  
ATOM   1237  CA  LEU A 257       2.726  23.680  -3.093  1.00 12.08           C  
ANISOU 1237  CA  LEU A 257     1411   1547   1630   -280     79    -59       C  
ATOM   1238  C   LEU A 257       2.459  23.505  -1.606  1.00 12.05           C  
ANISOU 1238  C   LEU A 257     1478   1344   1756    -60    -51   -216       C  
ATOM   1239  O   LEU A 257       1.300  23.524  -1.177  1.00 13.13           O  
ANISOU 1239  O   LEU A 257     1393   1889   1705    -82     18   -272       O  
ATOM   1240  CB  LEU A 257       2.344  25.086  -3.537  1.00 15.58           C  
ANISOU 1240  CB  LEU A 257     1890   1313   2714    -24     83   -221       C  
ATOM   1241  CG  LEU A 257       3.324  26.240  -3.360  1.00 17.96           C  
ANISOU 1241  CG  LEU A 257     2512   2268   2040   -157   -224   -110       C  
ATOM   1242  CD1 LEU A 257       4.573  26.048  -4.211  1.00 19.34           C  
ANISOU 1242  CD1 LEU A 257     1890   2803   2653   -369    448    229       C  
ATOM   1243  CD2 LEU A 257       2.619  27.514  -3.759  1.00 22.76           C  
ANISOU 1243  CD2 LEU A 257     2572   1484   4592      6     60    553       C  
ATOM   1244  N   GLU A 258       3.523  23.307  -0.835  1.00 12.89           N  
ANISOU 1244  N   GLU A 258     1656   1638   1603   -164   -134   -216       N  
ATOM   1245  CA  GLU A 258       3.409  23.021   0.591  1.00 13.77           C  
ANISOU 1245  CA  GLU A 258     1639   1701   1891   -366   -257   -179       C  
ATOM   1246  C   GLU A 258       4.338  23.913   1.386  1.00 13.81           C  
ANISOU 1246  C   GLU A 258     1637   1901   1707   -169    -18   -152       C  
ATOM   1247  O   GLU A 258       5.427  24.243   0.921  1.00 15.54           O  
ANISOU 1247  O   GLU A 258     1553   2513   1839   -429    161   -439       O  
ATOM   1248  CB  GLU A 258       3.774  21.565   0.862  1.00 18.08           C  
ANISOU 1248  CB  GLU A 258     2882   1988   1998   -309   -305    142       C  
ATOM   1249  CG  GLU A 258       2.870  20.593   0.148  1.00 20.07           C  
ANISOU 1249  CG  GLU A 258     2525   2049   3050   -336   -160     -3       C  
ATOM   1250  CD  GLU A 258       3.319  19.159   0.244  1.00 23.49           C  
ANISOU 1250  CD  GLU A 258     2929   2837   3157    279    823   -436       C  
ATOM   1251  OE1 GLU A 258       4.236  18.869   1.038  1.00 27.70           O  
ANISOU 1251  OE1 GLU A 258     4634   2524   3366    927    767    131       O  
ATOM   1252  OE2 GLU A 258       2.734  18.329  -0.485  1.00 23.94           O1-
ANISOU 1252  OE2 GLU A 258     3394   2613   3087     86    638    -21       O1-
ATOM   1253  N   ASP A 259       3.936  24.282   2.598  1.00 14.98           N  
ANISOU 1253  N   ASP A 259     1481   2333   1877   -342     95   -457       N  
ATOM   1254  CA  ASP A 259       4.843  25.055   3.444  1.00 16.74           C  
ANISOU 1254  CA  ASP A 259     1651   2746   1964   -342   -156   -548       C  
ATOM   1255  C   ASP A 259       5.892  24.141   4.077  1.00 17.64           C  
ANISOU 1255  C   ASP A 259     1447   2991   2262   -332    -88   -201       C  
ATOM   1256  O   ASP A 259       5.881  22.929   3.850  1.00 18.53           O  
ANISOU 1256  O   ASP A 259     1672   3317   2048   -126   -166   -305       O  
ATOM   1257  CB  ASP A 259       4.093  25.952   4.453  1.00 18.30           C  
ANISOU 1257  CB  ASP A 259     2358   2428   2164   -408      0   -426       C  
ATOM   1258  CG  ASP A 259       3.437  25.185   5.606  1.00 17.87           C  
ANISOU 1258  CG  ASP A 259     1806   2327   2654   -479   -169   -764       C  
ATOM   1259  OD1 ASP A 259       3.718  23.988   5.830  1.00 19.47           O  
ANISOU 1259  OD1 ASP A 259     1781   3315   2300   -349   -261   -167       O  
ATOM   1260  OD2 ASP A 259       2.627  25.823   6.316  1.00 23.09           O1-
ANISOU 1260  OD2 ASP A 259     2319   3670   2784   -129      6   -995       O1-
ATOM   1261  N   SER A 260       6.818  24.715   4.843  1.00 20.06           N  
ANISOU 1261  N   SER A 260     1826   3389   2404   -380   -364   -429       N  
ATOM   1262  CA  SER A 260       7.916  23.943   5.421  1.00 21.39           C  
ANISOU 1262  CA  SER A 260     1462   3905   2760   -181   -416   -178       C  
ATOM   1263  C   SER A 260       7.456  22.821   6.357  1.00 22.94           C  
ANISOU 1263  C   SER A 260     2345   3806   2561    282   -238     58       C  
ATOM   1264  O   SER A 260       8.169  21.829   6.537  1.00 27.56           O  
ANISOU 1264  O   SER A 260     2337   4316   3818    339   -494     68       O  
ATOM   1265  CB  SER A 260       8.901  24.869   6.139  1.00 23.00           C  
ANISOU 1265  CB  SER A 260     1677   4083   2979   -443   -196   -299       C  
ATOM   1266  OG  SER A 260       8.276  25.537   7.223  1.00 27.66           O  
ANISOU 1266  OG  SER A 260     2919   4762   2825   -152   -302   -705       O  
ATOM   1267  N   SER A 261       6.263  22.987   6.929  1.00 22.09           N  
ANISOU 1267  N   SER A 261     2067   3900   2425   -234   -428     47       N  
ATOM   1268  CA ASER A 261       5.672  22.012   7.847  0.70 22.47           C  
ANISOU 1268  CA ASER A 261     2317   3785   2434   -186   -376     86       C  
ATOM   1269  CA BSER A 261       5.698  21.994   7.843  0.30 23.52           C  
ANISOU 1269  CA BSER A 261     2572   3588   2773   -139   -238     86       C  
ATOM   1270  C   SER A 261       4.852  20.950   7.111  1.00 22.02           C  
ANISOU 1270  C   SER A 261     1998   3751   2617   -131   -494    256       C  
ATOM   1271  O   SER A 261       4.353  20.001   7.724  1.00 26.33           O  
ANISOU 1271  O   SER A 261     2593   4302   3109   -174   -414    566       O  
ATOM   1272  CB ASER A 261       4.793  22.725   8.881  0.70 22.86           C  
ANISOU 1272  CB ASER A 261     2157   4039   2490    -17   -437     27       C  
ATOM   1273  CB BSER A 261       4.885  22.675   8.951  0.30 26.28           C  
ANISOU 1273  CB BSER A 261     3104   3781   3100    -68    -58    -21       C  
ATOM   1274  OG ASER A 261       5.578  23.525   9.751  0.70 26.90           O  
ANISOU 1274  OG ASER A 261     3027   4420   2774   -333   -320   -450       O  
ATOM   1275  OG BSER A 261       3.973  23.619   8.419  0.30 27.06           O  
ANISOU 1275  OG BSER A 261     3398   3520   3360    -60    128    101       O  
ATOM   1276  N   GLY A 262       4.708  21.116   5.796  1.00 20.17           N  
ANISOU 1276  N   GLY A 262     1808   3475   2381    123   -257     81       N  
ATOM   1277  CA  GLY A 262       3.956  20.165   4.978  1.00 20.37           C  
ANISOU 1277  CA  GLY A 262     1513   3150   3075    209   -198     13       C  
ATOM   1278  C   GLY A 262       2.505  20.525   4.720  1.00 17.92           C  
ANISOU 1278  C   GLY A 262     1823   2870   2115    136    -77    261       C  
ATOM   1279  O   GLY A 262       1.787  19.771   4.065  1.00 18.70           O  
ANISOU 1279  O   GLY A 262     1826   2822   2454     44     81    148       O  
ATOM   1280  N   ASN A 263       2.073  21.674   5.233  1.00 16.72           N  
ANISOU 1280  N   ASN A 263     1503   2833   2014    110   -149    184       N  
ATOM   1281  CA  ASN A 263       0.710  22.144   5.019  1.00 16.26           C  
ANISOU 1281  CA  ASN A 263     1655   2652   1871   -136   -356     93       C  
ATOM   1282  C   ASN A 263       0.454  22.569   3.589  1.00 15.83           C  
ANISOU 1282  C   ASN A 263     1532   2530   1952   -238   -123    130       C  
ATOM   1283  O   ASN A 263       1.303  23.172   2.936  1.00 16.62           O  
ANISOU 1283  O   ASN A 263     1640   2733   1938   -354   -209     63       O  
ATOM   1284  CB  ASN A 263       0.386  23.313   5.943  1.00 17.16           C  
ANISOU 1284  CB  ASN A 263     1870   2781   1868    -64   -143    -36       C  
ATOM   1285  CG  ASN A 263       0.361  22.911   7.394  1.00 21.86           C  
ANISOU 1285  CG  ASN A 263     2057   3840   2406   -215    109    -24       C  
ATOM   1286  ND2 ASN A 263       1.270  23.478   8.174  1.00 25.27           N  
ANISOU 1286  ND2 ASN A 263     2500   4338   2763   -449   -344   -261       N  
ATOM   1287  OD1 ASN A 263      -0.459  22.097   7.812  1.00 23.05           O  
ANISOU 1287  OD1 ASN A 263     2610   3799   2346   -368    231     54       O  
ATOM   1288  N   LEU A 264      -0.752  22.275   3.125  1.00 15.73           N  
ANISOU 1288  N   LEU A 264     1681   2597   1698   -216    -99    165       N  
ATOM   1289  CA  LEU A 264      -1.167  22.607   1.781  1.00 14.00           C  
ANISOU 1289  CA  LEU A 264     1616   1994   1710   -311     38     81       C  
ATOM   1290  C   LEU A 264      -1.262  24.113   1.556  1.00 14.33           C  
ANISOU 1290  C   LEU A 264     1479   2333   1632   -256    -84   -132       C  
ATOM   1291  O   LEU A 264      -1.969  24.811   2.287  1.00 15.39           O  
ANISOU 1291  O   LEU A 264     1762   2314   1770   -214    221   -179       O  
ATOM   1292  CB  LEU A 264      -2.524  21.953   1.521  1.00 15.02           C  
ANISOU 1292  CB  LEU A 264     1575   2310   1820   -341   -147    143       C  
ATOM   1293  CG  LEU A 264      -3.187  22.257   0.181  1.00 15.02           C  
ANISOU 1293  CG  LEU A 264     1409   2694   1604   -430    -25     63       C  
ATOM   1294  CD1 LEU A 264      -2.422  21.614  -0.961  1.00 17.29           C  
ANISOU 1294  CD1 LEU A 264     2000   2842   1725   -585    114   -199       C  
ATOM   1295  CD2 LEU A 264      -4.605  21.739   0.215  1.00 16.73           C  
ANISOU 1295  CD2 LEU A 264     1600   2930   1825   -701   -154    204       C  
ATOM   1296  N   LEU A 265      -0.567  24.600   0.529  1.00 13.12           N  
ANISOU 1296  N   LEU A 265     1592   1876   1515    -86     76   -217       N  
ATOM   1297  CA  LEU A 265      -0.710  25.990   0.100  1.00 13.69           C  
ANISOU 1297  CA  LEU A 265     1950   1553   1696   -186   -108   -189       C  
ATOM   1298  C   LEU A 265      -1.455  26.124  -1.216  1.00 13.00           C  
ANISOU 1298  C   LEU A 265     1794   1473   1671   -253    161   -265       C  
ATOM   1299  O   LEU A 265      -2.126  27.128  -1.452  1.00 14.11           O  
ANISOU 1299  O   LEU A 265     1924   1491   1944    -32    104   -169       O  
ATOM   1300  CB  LEU A 265       0.655  26.657  -0.023  1.00 14.71           C  
ANISOU 1300  CB  LEU A 265     1655   1877   2057   -160   -202   -277       C  
ATOM   1301  CG  LEU A 265       1.504  26.684   1.248  1.00 15.36           C  
ANISOU 1301  CG  LEU A 265     1501   2235   2098    -96   -255   -395       C  
ATOM   1302  CD1 LEU A 265       2.836  27.328   0.933  1.00 18.51           C  
ANISOU 1302  CD1 LEU A 265     1562   2695   2775   -473   -284   -266       C  
ATOM   1303  CD2 LEU A 265       0.790  27.424   2.376  1.00 19.04           C  
ANISOU 1303  CD2 LEU A 265     2010   3080   2144    -98   -121   -707       C  
ATOM   1304  N   GLY A 266      -1.309  25.126  -2.081  1.00 13.07           N  
ANISOU 1304  N   GLY A 266     1706   1586   1674     -5   -100    -30       N  
ATOM   1305  CA  GLY A 266      -1.944  25.155  -3.393  1.00 12.81           C  
ANISOU 1305  CA  GLY A 266     1705   1608   1554    -88    -71    -82       C  
ATOM   1306  C   GLY A 266      -1.836  23.810  -4.066  1.00 11.48           C  
ANISOU 1306  C   GLY A 266     1392   1598   1371    -76     -2    -34       C  
ATOM   1307  O   GLY A 266      -0.948  23.026  -3.742  1.00 12.20           O  
ANISOU 1307  O   GLY A 266     1364   1601   1670     41   -243    -54       O  
ATOM   1308  N  AARG A 267      -2.735  23.557  -5.014  0.50 12.03           N  
ANISOU 1308  N  AARG A 267     1652   1438   1478    183    -18   -125       N  
ATOM   1309  N  BARG A 267      -2.739  23.536  -5.004  0.50 12.75           N  
ANISOU 1309  N  BARG A 267     1659   1595   1588    149     22   -160       N  
ATOM   1310  CA AARG A 267      -2.773  22.289  -5.731  0.50 11.43           C  
ANISOU 1310  CA AARG A 267     1479   1475   1387    -38    -55    -50       C  
ATOM   1311  CA BARG A 267      -2.723  22.268  -5.731  0.50 12.75           C  
ANISOU 1311  CA BARG A 267     1565   1564   1714    -52     49    -87       C  
ATOM   1312  C  AARG A 267      -3.232  22.502  -7.162  0.50 10.56           C  
ANISOU 1312  C  AARG A 267     1379   1262   1369    -39    -24    -72       C  
ATOM   1313  C  BARG A 267      -3.274  22.419  -7.137  0.50 12.89           C  
ANISOU 1313  C  BARG A 267     1488   1822   1585     84    102   -124       C  
ATOM   1314  O  AARG A 267      -4.153  23.276  -7.414  0.50 11.30           O  
ANISOU 1314  O  AARG A 267     1436   1579   1277    -16     -9    156       O  
ATOM   1315  O  BARG A 267      -4.297  23.063  -7.348  0.50 13.50           O  
ANISOU 1315  O  BARG A 267     1555   1532   2040    299     56   -342       O  
ATOM   1316  CB AARG A 267      -3.725  21.308  -5.037  0.50 10.87           C  
ANISOU 1316  CB AARG A 267     1512   1446   1169   -121    -82    -39       C  
ATOM   1317  CB BARG A 267      -3.511  21.188  -4.979  0.50 14.09           C  
ANISOU 1317  CB BARG A 267     1492   1634   2228    -10    219    -99       C  
ATOM   1318  CG AARG A 267      -3.598  19.866  -5.523  0.50 14.59           C  
ANISOU 1318  CG AARG A 267     2034   1586   1924    -93    -25     90       C  
ATOM   1319  CG BARG A 267      -3.590  19.842  -5.715  0.50 13.46           C  
ANISOU 1319  CG BARG A 267     1867   1392   1855    -98    184   -106       C  
ATOM   1320  CD AARG A 267      -4.731  18.984  -5.017  0.50 12.51           C  
ANISOU 1320  CD AARG A 267     1801   1389   1562    103    316    -13       C  
ATOM   1321  CD BARG A 267      -4.382  18.798  -4.941  0.50 13.96           C  
ANISOU 1321  CD BARG A 267     1289   1460   2553    319    193    267       C  
ATOM   1322  NE AARG A 267      -4.629  18.664  -3.592  0.50 12.44           N  
ANISOU 1322  NE AARG A 267     2086   1456   1182    -69    140     55       N  
ATOM   1323  NE BARG A 267      -5.747  19.234  -4.661  0.50 16.88           N  
ANISOU 1323  NE BARG A 267     2067   2199   2146     97    380   -181       N  
ATOM   1324  CZ AARG A 267      -5.472  19.089  -2.653  0.50 10.66           C  
ANISOU 1324  CZ AARG A 267     1583   1251   1213   -339     90   -138       C  
ATOM   1325  CZ BARG A 267      -6.212  19.527  -3.447  0.50 15.84           C  
ANISOU 1325  CZ BARG A 267     1306   2178   2534   -416   1344   -397       C  
ATOM   1326  NH1AARG A 267      -6.483  19.882  -2.966  0.50 11.16           N1+
ANISOU 1326  NH1AARG A 267     1299   1040   1900    -66    161     26       N1+
ATOM   1327  NH2AARG A 267      -5.293  18.729  -1.388  0.50 13.10           N  
ANISOU 1327  NH2AARG A 267     1729   1879   1367   -186   -197     77       N  
ATOM   1328  NH1BARG A 267      -5.432  19.425  -2.379  0.50 27.17           N1+
ANISOU 1328  NH1BARG A 267     3705   3243   3375     91    268    -54       N1+
ATOM   1329  NH2BARG A 267      -7.465  19.922  -3.303  0.50 28.73           N  
ANISOU 1329  NH2BARG A 267     2796   3569   4549     10    489   -387       N  
ATOM   1330  N   ASN A 268      -2.584  21.805  -8.092  1.00 11.06           N  
ANISOU 1330  N   ASN A 268     1444   1303   1452   -182      8   -114       N  
ATOM   1331  CA  ASN A 268      -3.069  21.701  -9.459  1.00 11.33           C  
ANISOU 1331  CA  ASN A 268     1541   1379   1384    -97      6     11       C  
ATOM   1332  C   ASN A 268      -2.735  20.315  -9.974  1.00 11.07           C  
ANISOU 1332  C   ASN A 268     1450   1198   1556    -29    164    -21       C  
ATOM   1333  O   ASN A 268      -1.976  19.591  -9.348  1.00 13.78           O  
ANISOU 1333  O   ASN A 268     1690   1499   2044    294   -477   -362       O  
ATOM   1334  CB  ASN A 268      -2.446  22.774 -10.346  1.00 13.37           C  
ANISOU 1334  CB  ASN A 268     1992   1452   1634   -173    103    179       C  
ATOM   1335  CG  ASN A 268      -3.053  24.138 -10.124  1.00 17.35           C  
ANISOU 1335  CG  ASN A 268     2397   2243   1953   -188      0   -161       C  
ATOM   1336  ND2 ASN A 268      -2.303  25.018  -9.477  1.00 17.38           N  
ANISOU 1336  ND2 ASN A 268     2173   2146   2282    -32    -46     61       N  
ATOM   1337  OD1 ASN A 268      -4.185  24.403 -10.535  1.00 19.35           O  
ANISOU 1337  OD1 ASN A 268     2200   1705   3447    -63   -182    -60       O  
ATOM   1338  N   SER A 269      -3.330  19.926 -11.089  1.00 12.78           N  
ANISOU 1338  N   SER A 269     2061   1181   1614    173   -220    -89       N  
ATOM   1339  CA  SER A 269      -3.114  18.597 -11.634  1.00 13.31           C  
ANISOU 1339  CA  SER A 269     2004   1505   1544      8   -131     10       C  
ATOM   1340  C   SER A 269      -3.258  18.614 -13.134  1.00 12.54           C  
ANISOU 1340  C   SER A 269     1981   1327   1457    -54   -354    148       C  
ATOM   1341  O   SER A 269      -3.859  19.525 -13.709  1.00 14.05           O  
ANISOU 1341  O   SER A 269     2323   1480   1535    267   -519     47       O  
ATOM   1342  CB  SER A 269      -4.100  17.602 -11.032  1.00 12.98           C  
ANISOU 1342  CB  SER A 269     1756   1481   1692     12    -99    -44       C  
ATOM   1343  OG  SER A 269      -5.426  17.936 -11.369  1.00 17.63           O  
ANISOU 1343  OG  SER A 269     1738   2417   2541     68     47    -95       O  
ATOM   1344  N   PHE A 270      -2.706  17.586 -13.761  1.00 11.46           N  
ANISOU 1344  N   PHE A 270     1703   1306   1344    -19   -198     -1       N  
ATOM   1345  CA  PHE A 270      -2.837  17.401 -15.191  1.00 12.07           C  
ANISOU 1345  CA  PHE A 270     2076   1274   1233      1   -228     13       C  
ATOM   1346  C   PHE A 270      -2.781  15.916 -15.465  1.00 11.63           C  
ANISOU 1346  C   PHE A 270     1848   1391   1180    -20   -157    101       C  
ATOM   1347  O   PHE A 270      -2.124  15.166 -14.747  1.00 11.88           O  
ANISOU 1347  O   PHE A 270     1961   1198   1353    -38   -295    168       O  
ATOM   1348  CB  PHE A 270      -1.751  18.161 -15.982  1.00 13.25           C  
ANISOU 1348  CB  PHE A 270     2093   1433   1507      6    -29    170       C  
ATOM   1349  CG  PHE A 270      -0.327  17.836 -15.579  1.00 12.30           C  
ANISOU 1349  CG  PHE A 270     2079   1097   1497    -44   -224    180       C  
ATOM   1350  CD1 PHE A 270       0.287  18.501 -14.522  1.00 12.72           C  
ANISOU 1350  CD1 PHE A 270     1977   1181   1672   -176   -154    136       C  
ATOM   1351  CD2 PHE A 270       0.419  16.900 -16.289  1.00 12.74           C  
ANISOU 1351  CD2 PHE A 270     1869   1389   1581    -45   -125     76       C  
ATOM   1352  CE1 PHE A 270       1.603  18.218 -14.164  1.00 12.47           C  
ANISOU 1352  CE1 PHE A 270     2008   1210   1516   -300   -136    184       C  
ATOM   1353  CE2 PHE A 270       1.745  16.620 -15.946  1.00 13.13           C  
ANISOU 1353  CE2 PHE A 270     1843   1413   1731   -228    -56     94       C  
ATOM   1354  CZ  PHE A 270       2.342  17.282 -14.882  1.00 12.79           C  
ANISOU 1354  CZ  PHE A 270     2162   1098   1597   -273    -68    170       C  
ATOM   1355  N   GLU A 271      -3.480  15.486 -16.507  1.00 12.18           N  
ANISOU 1355  N   GLU A 271     1912   1341   1373     85   -210     62       N  
ATOM   1356  CA  GLU A 271      -3.410  14.107 -16.937  1.00 12.29           C  
ANISOU 1356  CA  GLU A 271     1961   1274   1435   -201   -206    129       C  
ATOM   1357  C   GLU A 271      -2.095  13.917 -17.683  1.00 11.57           C  
ANISOU 1357  C   GLU A 271     2086   1127   1181     23   -209    108       C  
ATOM   1358  O   GLU A 271      -1.558  14.870 -18.254  1.00 11.74           O  
ANISOU 1358  O   GLU A 271     1978   1209   1270    -17   -177    190       O  
ATOM   1359  CB  GLU A 271      -4.620  13.800 -17.823  1.00 13.34           C  
ANISOU 1359  CB  GLU A 271     2033   1559   1475   -210   -410    216       C  
ATOM   1360  CG  GLU A 271      -4.773  12.354 -18.242  1.00 16.30           C  
ANISOU 1360  CG  GLU A 271     2398   1811   1982   -604   -519    416       C  
ATOM   1361  CD  GLU A 271      -6.087  12.082 -18.948  1.00 18.28           C  
ANISOU 1361  CD  GLU A 271     2408   2261   2276      9   -495    169       C  
ATOM   1362  OE1 GLU A 271      -7.016  12.914 -18.838  1.00 21.31           O  
ANISOU 1362  OE1 GLU A 271     2332   2765   3000   -469   -636    303       O  
ATOM   1363  OE2 GLU A 271      -6.170  11.036 -19.620  1.00 21.94           O1-
ANISOU 1363  OE2 GLU A 271     3581   2753   2001   -952   -513    394       O1-
ATOM   1364  N   VAL A 272      -1.559  12.699 -17.664  1.00 12.21           N  
ANISOU 1364  N   VAL A 272     2081   1261   1296   -152   -175      6       N  
ATOM   1365  CA AVAL A 272      -0.306  12.382 -18.353  0.50 11.69           C  
ANISOU 1365  CA AVAL A 272     2405    957   1080     15   -187    171       C  
ATOM   1366  CA BVAL A 272      -0.351  12.429 -18.419  0.50 13.48           C  
ANISOU 1366  CA BVAL A 272     2359   1281   1481    135   -138   -191       C  
ATOM   1367  C   VAL A 272      -0.435  11.081 -19.124  1.00 14.06           C  
ANISOU 1367  C   VAL A 272     2853   1153   1334      2    146    163       C  
ATOM   1368  O   VAL A 272      -0.973  10.104 -18.593  1.00 17.95           O  
ANISOU 1368  O   VAL A 272     4011   1144   1665   -147    485    155       O  
ATOM   1369  CB AVAL A 272       0.869  12.212 -17.363  0.50 12.58           C  
ANISOU 1369  CB AVAL A 272     2102   1634   1041    198     78    438       C  
ATOM   1370  CB BVAL A 272       0.964  12.635 -17.575  0.50 14.08           C  
ANISOU 1370  CB BVAL A 272     2013   1771   1563    306     61    486       C  
ATOM   1371  CG1AVAL A 272       2.189  11.982 -18.099  0.50 14.38           C  
ANISOU 1371  CG1AVAL A 272     2054   2126   1284    101   -257     48       C  
ATOM   1372  CG2AVAL A 272       0.985  13.411 -16.482  0.50 13.48           C  
ANISOU 1372  CG2AVAL A 272     1792   1964   1365   -169   -229    -38       C  
ATOM   1373  CG1BVAL A 272       1.031  11.704 -16.380  0.50 13.68           C  
ANISOU 1373  CG1BVAL A 272     1451   1713   2033    121    700    272       C  
ATOM   1374  CG2BVAL A 272       2.214  12.500 -18.442  0.50 16.59           C  
ANISOU 1374  CG2BVAL A 272     2152   2030   2121     49    190    112       C  
ATOM   1375  N   ARG A 273       0.059  11.071 -20.359  1.00 12.63           N  
ANISOU 1375  N   ARG A 273     2467   1070   1258     16     38     32       N  
ATOM   1376  CA  ARG A 273       0.240   9.837 -21.108  1.00 13.76           C  
ANISOU 1376  CA  ARG A 273     2354   1351   1523    189    -89    -30       C  
ATOM   1377  C   ARG A 273       1.703   9.780 -21.477  1.00 13.89           C  
ANISOU 1377  C   ARG A 273     2674   1320   1280    137     34      5       C  
ATOM   1378  O   ARG A 273       2.219  10.679 -22.135  1.00 15.85           O  
ANISOU 1378  O   ARG A 273     2634   1609   1777    182    333    403       O  
ATOM   1379  CB  ARG A 273      -0.627   9.798 -22.366  1.00 14.40           C  
ANISOU 1379  CB  ARG A 273     2654   1404   1412   -234   -151     12       C  
ATOM   1380  CG  ARG A 273      -0.382   8.558 -23.225  1.00 17.05           C  
ANISOU 1380  CG  ARG A 273     3045   1720   1711   -307     59     -8       C  
ATOM   1381  CD  ARG A 273      -1.354   8.504 -24.382  1.00 18.42           C  
ANISOU 1381  CD  ARG A 273     3076   2153   1767   -212   -293   -298       C  
ATOM   1382  NE  ARG A 273      -1.010   7.465 -25.352  1.00 22.64           N  
ANISOU 1382  NE  ARG A 273     3303   2838   2458    -75   -279   -598       N  
ATOM   1383  CZ  ARG A 273      -1.519   6.238 -25.361  1.00 33.74           C  
ANISOU 1383  CZ  ARG A 273     4517   3761   4543   -181    346   -501       C  
ATOM   1384  NH1 ARG A 273      -2.407   5.870 -24.447  1.00 38.87           N1+
ANISOU 1384  NH1 ARG A 273     5375   4843   4547   -398    384    108       N1+
ATOM   1385  NH2 ARG A 273      -1.140   5.373 -26.294  1.00 34.63           N  
ANISOU 1385  NH2 ARG A 273     5263   3776   4116   -185     -4   -667       N  
ATOM   1386  N   VAL A 274       2.371   8.730 -21.024  1.00 14.08           N  
ANISOU 1386  N   VAL A 274     2342   1458   1549     24    -92    103       N  
ATOM   1387  CA  VAL A 274       3.757   8.498 -21.370  1.00 16.12           C  
ANISOU 1387  CA  VAL A 274     2793   1598   1732     88     85    -51       C  
ATOM   1388  C   VAL A 274       3.734   7.513 -22.528  1.00 16.80           C  
ANISOU 1388  C   VAL A 274     2876   1696   1810    -88    197    186       C  
ATOM   1389  O   VAL A 274       3.217   6.405 -22.401  1.00 17.24           O  
ANISOU 1389  O   VAL A 274     3120   1351   2078   -186    489      4       O  
ATOM   1390  CB  VAL A 274       4.558   7.948 -20.177  1.00 15.62           C  
ANISOU 1390  CB  VAL A 274     2406   1655   1874    100    -16     -6       C  
ATOM   1391  CG1 VAL A 274       6.041   7.924 -20.509  1.00 17.34           C  
ANISOU 1391  CG1 VAL A 274     2522   1872   2194   -108    356    100       C  
ATOM   1392  CG2 VAL A 274       4.277   8.779 -18.917  1.00 15.15           C  
ANISOU 1392  CG2 VAL A 274     2263   1832   1660   -155   -186    105       C  
ATOM   1393  N   CYS A 275       4.252   7.944 -23.670  1.00 17.21           N  
ANISOU 1393  N   CYS A 275     3001   1825   1712   -138    205    176       N  
ATOM   1394  CA  CYS A 275       4.079   7.203 -24.908  1.00 18.83           C  
ANISOU 1394  CA  CYS A 275     3255   2041   1857    -90    344   -309       C  
ATOM   1395  C   CYS A 275       5.214   7.481 -25.883  1.00 20.03           C  
ANISOU 1395  C   CYS A 275     3372   2590   1648   -188    165    -61       C  
ATOM   1396  O   CYS A 275       5.956   8.456 -25.732  1.00 21.05           O  
ANISOU 1396  O   CYS A 275     2951   3373   1674   -573    240    -65       O  
ATOM   1397  CB  CYS A 275       2.725   7.552 -25.532  1.00 20.19           C  
ANISOU 1397  CB  CYS A 275     3357   2196   2116   -481     30   -445       C  
ATOM   1398  SG  CYS A 275       2.465   9.322 -25.847  1.00 20.44           S  
ANISOU 1398  SG  CYS A 275     3274   2581   1908   -516    -27    123       S  
ATOM   1399  N   ALA A 276       5.340   6.617 -26.885  1.00 22.82           N  
ANISOU 1399  N   ALA A 276     3724   2804   2142    298    386    -82       N  
ATOM   1400  CA  ALA A 276       6.433   6.693 -27.852  1.00 22.16           C  
ANISOU 1400  CA  ALA A 276     3199   2831   2390    260    519    -99       C  
ATOM   1401  C   ALA A 276       6.321   7.892 -28.783  1.00 21.36           C  
ANISOU 1401  C   ALA A 276     3221   2833   2060     -2    343   -440       C  
ATOM   1402  O   ALA A 276       7.338   8.470 -29.176  1.00 23.55           O  
ANISOU 1402  O   ALA A 276     3459   3655   1833   -155    435   -127       O  
ATOM   1403  CB  ALA A 276       6.501   5.407 -28.666  1.00 28.42           C  
ANISOU 1403  CB  ALA A 276     4150   3097   3549    440    497   -260       C  
ATOM   1404  N   CYS A 277       5.084   8.248 -29.131  1.00 19.73           N  
ANISOU 1404  N   CYS A 277     3271   2657   1566     44    205   -377       N  
ATOM   1405  CA ACYS A 277       4.822   9.300 -30.109  0.50 19.76           C  
ANISOU 1405  CA ACYS A 277     2859   2955   1692    -73      6   -197       C  
ATOM   1406  CA BCYS A 277       4.831   9.321 -30.094  0.50 21.92           C  
ANISOU 1406  CA BCYS A 277     3188   3100   2041     -4     36   -144       C  
ATOM   1407  C   CYS A 277       3.835  10.344 -29.553  1.00 19.19           C  
ANISOU 1407  C   CYS A 277     2963   2503   1823   -113     32     17       C  
ATOM   1408  O   CYS A 277       2.660  10.348 -29.928  1.00 20.32           O  
ANISOU 1408  O   CYS A 277     2921   3265   1533   -334      1   -239       O  
ATOM   1409  CB ACYS A 277       4.293   8.679 -31.413  0.50 20.02           C  
ANISOU 1409  CB ACYS A 277     2559   3066   1982    -84    -22   -258       C  
ATOM   1410  CB BCYS A 277       4.355   8.746 -31.429  0.50 24.37           C  
ANISOU 1410  CB BCYS A 277     3447   3347   2465    -21      3   -201       C  
ATOM   1411  SG ACYS A 277       5.171   7.167 -31.976  0.50 23.03           S  
ANISOU 1411  SG ACYS A 277     2651   3763   2334   -175    469   -432       S  
ATOM   1412  SG BCYS A 277       5.611   7.755 -32.259  0.50 31.19           S  
ANISOU 1412  SG BCYS A 277     4797   5233   1820    -33    671   -892       S  
ATOM   1413  N   PRO A 278       4.308  11.239 -28.654  1.00 19.32           N  
ANISOU 1413  N   PRO A 278     3011   2600   1729   -442    198    -58       N  
ATOM   1414  CA  PRO A 278       3.423  12.208 -27.993  1.00 19.04           C  
ANISOU 1414  CA  PRO A 278     2701   2921   1613   -182     -5   -139       C  
ATOM   1415  C   PRO A 278       2.594  13.074 -28.933  1.00 17.06           C  
ANISOU 1415  C   PRO A 278     2715   2106   1661   -778    -27     38       C  
ATOM   1416  O   PRO A 278       1.405  13.268 -28.685  1.00 18.04           O  
ANISOU 1416  O   PRO A 278     2754   2372   1726   -598   -284     71       O  
ATOM   1417  CB  PRO A 278       4.393  13.077 -27.181  1.00 20.49           C  
ANISOU 1417  CB  PRO A 278     2909   3027   1850   -458   -473   -414       C  
ATOM   1418  CG  PRO A 278       5.562  12.216 -26.947  1.00 22.54           C  
ANISOU 1418  CG  PRO A 278     3197   2900   2465   -109   -140   -394       C  
ATOM   1419  CD  PRO A 278       5.698  11.377 -28.181  1.00 20.46           C  
ANISOU 1419  CD  PRO A 278     2736   2985   2051   -307     47    -79       C  
ATOM   1420  N   GLY A 279       3.211  13.574 -30.001  1.00 20.41           N  
ANISOU 1420  N   GLY A 279     2992   2937   1826   -831   -131    375       N  
ATOM   1421  CA  GLY A 279       2.523  14.444 -30.950  1.00 21.74           C  
ANISOU 1421  CA  GLY A 279     3129   2940   2188   -653   -360    231       C  
ATOM   1422  C   GLY A 279       1.385  13.717 -31.637  1.00 20.53           C  
ANISOU 1422  C   GLY A 279     3439   2477   1881   -550    -73    230       C  
ATOM   1423  O   GLY A 279       0.288  14.251 -31.777  1.00 21.92           O  
ANISOU 1423  O   GLY A 279     3343   2983   2002   -640   -324    380       O  
ATOM   1424  N   ARG A 280       1.642  12.479 -32.038  1.00 20.29           N  
ANISOU 1424  N   ARG A 280     2935   3067   1707   -893    -76   -120       N  
ATOM   1425  CA  ARG A 280       0.625  11.682 -32.704  1.00 22.12           C  
ANISOU 1425  CA  ARG A 280     3118   3356   1929   -620   -141   -165       C  
ATOM   1426  C   ARG A 280      -0.526  11.350 -31.760  1.00 19.68           C  
ANISOU 1426  C   ARG A 280     3034   2692   1749   -373    -66   -486       C  
ATOM   1427  O   ARG A 280      -1.697  11.477 -32.130  1.00 21.02           O  
ANISOU 1427  O   ARG A 280     3006   2959   2019   -493   -265   -250       O  
ATOM   1428  CB  ARG A 280       1.240  10.408 -33.267  1.00 23.92           C  
ANISOU 1428  CB  ARG A 280     2916   3734   2439   -621    104   -474       C  
ATOM   1429  CG  ARG A 280       0.325   9.667 -34.233  1.00 27.17           C  
ANISOU 1429  CG  ARG A 280     3874   3927   2520   -695   -118   -696       C  
ATOM   1430  CD  ARG A 280      -0.647   8.739 -33.514  1.00 28.92           C  
ANISOU 1430  CD  ARG A 280     4163   3473   3350     37    261   -252       C  
ATOM   1431  NE  ARG A 280       0.055   7.891 -32.557  1.00 27.48           N  
ANISOU 1431  NE  ARG A 280     3525   3933   2983     10     -9   -586       N  
ATOM   1432  CZ  ARG A 280       0.876   6.905 -32.900  1.00 22.86           C  
ANISOU 1432  CZ  ARG A 280     2193   2996   3495    522   -184   -671       C  
ATOM   1433  NH1 ARG A 280       1.088   6.622 -34.182  1.00 27.59           N1+
ANISOU 1433  NH1 ARG A 280     3389   4491   2602    138   -393     73       N1+
ATOM   1434  NH2 ARG A 280       1.472   6.185 -31.963  1.00 29.66           N  
ANISOU 1434  NH2 ARG A 280     3800   4839   2628    229   -489   -206       N  
ATOM   1435  N   ASP A 281      -0.196  10.931 -30.541  1.00 17.49           N  
ANISOU 1435  N   ASP A 281     2702   2312   1631   -421     -4   -305       N  
ATOM   1436  CA  ASP A 281      -1.227  10.547 -29.590  1.00 18.76           C  
ANISOU 1436  CA  ASP A 281     2659   2396   2070   -278    188    -49       C  
ATOM   1437  C   ASP A 281      -2.072  11.738 -29.158  1.00 17.45           C  
ANISOU 1437  C   ASP A 281     2837   2020   1770   -263   -417    -22       C  
ATOM   1438  O   ASP A 281      -3.285  11.598 -28.972  1.00 20.08           O  
ANISOU 1438  O   ASP A 281     2987   2356   2286   -310   -198   -503       O  
ATOM   1439  CB  ASP A 281      -0.629   9.814 -28.391  1.00 18.20           C  
ANISOU 1439  CB  ASP A 281     2987   2184   1742   -202   -148   -101       C  
ATOM   1440  CG  ASP A 281      -0.207   8.393 -28.729  1.00 20.99           C  
ANISOU 1440  CG  ASP A 281     3419   2212   2342   -185     17   -284       C  
ATOM   1441  OD1 ASP A 281      -0.473   7.928 -29.859  1.00 21.81           O  
ANISOU 1441  OD1 ASP A 281     3847   2411   2030    -50     -3   -396       O  
ATOM   1442  OD2 ASP A 281       0.389   7.733 -27.861  1.00 22.12           O1-
ANISOU 1442  OD2 ASP A 281     3686   2455   2262    -78     49   -122       O1-
ATOM   1443  N   ARG A 282      -1.442  12.907 -29.007  1.00 18.33           N  
ANISOU 1443  N   ARG A 282     3065   2297   1602   -450    -99      9       N  
ATOM   1444  CA AARG A 282      -2.182  14.122 -28.685  0.50 16.62           C  
ANISOU 1444  CA AARG A 282     2818   1966   1529   -418   -298    -28       C  
ATOM   1445  CA BARG A 282      -2.180  14.126 -28.684  0.50 19.89           C  
ANISOU 1445  CA BARG A 282     3038   2432   2087   -280   -230    -56       C  
ATOM   1446  C   ARG A 282      -3.202  14.416 -29.778  1.00 18.63           C  
ANISOU 1446  C   ARG A 282     2930   2073   2076   -432   -104    -37       C  
ATOM   1447  O   ARG A 282      -4.369  14.683 -29.493  1.00 21.26           O  
ANISOU 1447  O   ARG A 282     3111   2575   2389   -423   -384   -385       O  
ATOM   1448  CB AARG A 282      -1.245  15.320 -28.509  0.50 16.14           C  
ANISOU 1448  CB AARG A 282     2673   1925   1531   -403   -211    160       C  
ATOM   1449  CB BARG A 282      -1.234  15.319 -28.501  0.50 20.83           C  
ANISOU 1449  CB BARG A 282     3045   2601   2267   -416    -43     19       C  
ATOM   1450  CG AARG A 282      -1.984  16.627 -28.277  0.50 16.93           C  
ANISOU 1450  CG AARG A 282     3409   1352   1671   -121   -684    -19       C  
ATOM   1451  CG BARG A 282      -1.943  16.618 -28.123  0.50 25.35           C  
ANISOU 1451  CG BARG A 282     3731   2488   3412   -103   -238    162       C  
ATOM   1452  CD AARG A 282      -1.041  17.805 -28.188  0.50 18.69           C  
ANISOU 1452  CD AARG A 282     3252   2495   1351   -513   -360   -363       C  
ATOM   1453  CD BARG A 282      -0.966  17.742 -27.800  0.50 25.10           C  
ANISOU 1453  CD BARG A 282     3675   2943   2918   -384     62   -227       C  
ATOM   1454  NE AARG A 282      -1.772  19.069 -28.163  0.50 18.79           N  
ANISOU 1454  NE AARG A 282     2508   2631   1998     -3   -246    135       N  
ATOM   1455  NE BARG A 282      -0.204  18.184 -28.969  0.50 27.37           N  
ANISOU 1455  NE BARG A 282     3692   3297   3408   -193    208     25       N  
ATOM   1456  CZ AARG A 282      -1.204  20.273 -28.180  0.50 16.05           C  
ANISOU 1456  CZ AARG A 282     2314   2002   1779   -254   -335    204       C  
ATOM   1457  CZ BARG A 282      -0.597  19.128 -29.822  0.50 33.52           C  
ANISOU 1457  CZ BARG A 282     4565   4092   4077     47    -16    204       C  
ATOM   1458  NH1AARG A 282       0.120  20.387 -28.216  0.50 15.97           N1+
ANISOU 1458  NH1AARG A 282     2433   1965   1669     11   -487    475       N1+
ATOM   1459  NH2AARG A 282      -1.962  21.368 -28.155  0.50 19.58           N  
ANISOU 1459  NH2AARG A 282     1773   2784   2880    346    -74   1375       N  
ATOM   1460  NH1BARG A 282      -1.760  19.747 -29.660  0.50 37.91           N1+
ANISOU 1460  NH1BARG A 282     4576   5007   4821     78    108    -11       N1+
ATOM   1461  NH2BARG A 282       0.178  19.451 -30.849  0.50 35.03           N  
ANISOU 1461  NH2BARG A 282     4390   4570   4350    -85    147    -84       N  
ATOM   1462  N   ARG A 283      -2.746  14.360 -31.027  1.00 21.55           N  
ANISOU 1462  N   ARG A 283     3343   2841   2003   -248   -499     50       N  
ATOM   1463  CA  ARG A 283      -3.607  14.600 -32.174  1.00 23.93           C  
ANISOU 1463  CA  ARG A 283     3323   3321   2446   -230   -576   -190       C  
ATOM   1464  C   ARG A 283      -4.774  13.619 -32.217  1.00 24.17           C  
ANISOU 1464  C   ARG A 283     3353   3253   2577   -240   -418   -481       C  
ATOM   1465  O   ARG A 283      -5.909  14.026 -32.447  1.00 27.58           O  
ANISOU 1465  O   ARG A 283     3643   3428   3407     13   -935   -811       O  
ATOM   1466  CB  ARG A 283      -2.800  14.548 -33.468  1.00 26.31           C  
ANISOU 1466  CB  ARG A 283     3498   4059   2438   -204   -564   -125       C  
ATOM   1467  CG  ARG A 283      -1.970  15.795 -33.720  1.00 29.43           C  
ANISOU 1467  CG  ARG A 283     4099   4132   2950    -85   -189    165       C  
ATOM   1468  N   THR A 284      -4.495  12.339 -31.970  1.00 24.46           N  
ANISOU 1468  N   THR A 284     3102   3250   2940   -525   -575   -776       N  
ATOM   1469  CA  THR A 284      -5.544  11.315 -31.925  1.00 25.20           C  
ANISOU 1469  CA  THR A 284     2884   3280   3412   -161   -284   -581       C  
ATOM   1470  C   THR A 284      -6.563  11.598 -30.817  1.00 24.86           C  
ANISOU 1470  C   THR A 284     3008   3297   3141     48   -323   -550       C  
ATOM   1471  O   THR A 284      -7.771  11.598 -31.073  1.00 27.92           O  
ANISOU 1471  O   THR A 284     3253   3156   4196    -87   -580  -1199       O  
ATOM   1472  CB  THR A 284      -4.952   9.896 -31.742  1.00 27.86           C  
ANISOU 1472  CB  THR A 284     3558   3197   3829   -385   -222   -392       C  
ATOM   1473  CG2 THR A 284      -6.047   8.830 -31.779  1.00 26.92           C  
ANISOU 1473  CG2 THR A 284     3269   2751   4209    -65   -323   -788       C  
ATOM   1474  OG1 THR A 284      -4.008   9.632 -32.786  1.00 29.84           O  
ANISOU 1474  OG1 THR A 284     3589   3793   3955   -334   -145  -1117       O  
ATOM   1475  N   GLU A 285      -6.075  11.846 -29.600  1.00 23.46           N  
ANISOU 1475  N   GLU A 285     3238   2175   3499   -410   -171   -763       N  
ATOM   1476  CA  GLU A 285      -6.957  12.062 -28.451  1.00 23.16           C  
ANISOU 1476  CA  GLU A 285     3063   2540   3195     47   -222    -94       C  
ATOM   1477  C   GLU A 285      -7.761  13.354 -28.585  1.00 24.88           C  
ANISOU 1477  C   GLU A 285     3485   2612   3353    140     10   -330       C  
ATOM   1478  O   GLU A 285      -8.891  13.437 -28.098  1.00 27.49           O  
ANISOU 1478  O   GLU A 285     3561   2962   3920    179    -78   -279       O  
ATOM   1479  CB  GLU A 285      -6.181  12.010 -27.128  1.00 21.79           C  
ANISOU 1479  CB  GLU A 285     2960   2427   2889     98   -142   -111       C  
ATOM   1480  CG  GLU A 285      -5.636  10.617 -26.808  1.00 23.28           C  
ANISOU 1480  CG  GLU A 285     3094   2482   3267     22   -128     33       C  
ATOM   1481  CD  GLU A 285      -5.224  10.422 -25.359  1.00 23.01           C  
ANISOU 1481  CD  GLU A 285     2404   2619   3719    -54   -287    -14       C  
ATOM   1482  OE1 GLU A 285      -5.712  11.165 -24.480  1.00 25.83           O  
ANISOU 1482  OE1 GLU A 285     3291   2423   4098   -635    -70   -492       O  
ATOM   1483  OE2 GLU A 285      -4.411   9.505 -25.109  1.00 26.80           O1-
ANISOU 1483  OE2 GLU A 285     3029   2598   4555   -209   -392     18       O1-
ATOM   1484  N   GLU A 286      -7.180  14.343 -29.263  1.00 26.05           N  
ANISOU 1484  N   GLU A 286     3712   2787   3399     72     53   -402       N  
ATOM   1485  CA  GLU A 286      -7.874  15.597 -29.565  1.00 25.35           C  
ANISOU 1485  CA  GLU A 286     3512   2865   3253     60   -308    -31       C  
ATOM   1486  C   GLU A 286      -8.933  15.436 -30.653  1.00 29.71           C  
ANISOU 1486  C   GLU A 286     3622   3863   3803    130   -320   -191       C  
ATOM   1487  O   GLU A 286      -9.997  16.055 -30.583  1.00 32.18           O  
ANISOU 1487  O   GLU A 286     3888   3947   4392    301   -153   -436       O  
ATOM   1488  CB  GLU A 286      -6.880  16.706 -29.928  1.00 25.60           C  
ANISOU 1488  CB  GLU A 286     3833   2946   2948   -134   -218   -197       C  
ATOM   1489  CG  GLU A 286      -6.150  17.248 -28.707  1.00 22.50           C  
ANISOU 1489  CG  GLU A 286     3876   2317   2353   -200   -467    -47       C  
ATOM   1490  CD  GLU A 286      -5.142  18.338 -29.012  1.00 22.81           C  
ANISOU 1490  CD  GLU A 286     3904   2350   2411    -28   -345    197       C  
ATOM   1491  OE1 GLU A 286      -4.720  18.496 -30.175  1.00 22.20           O  
ANISOU 1491  OE1 GLU A 286     3834   2405   2196    -71   -633     89       O  
ATOM   1492  OE2 GLU A 286      -4.758  19.039 -28.056  1.00 22.13           O1-
ANISOU 1492  OE2 GLU A 286     4443   2089   1876    160   -887    115       O1-
ATOM   1493  N   GLU A 287      -8.642  14.600 -31.648  1.00 29.60           N  
ANISOU 1493  N   GLU A 287     3073   4251   3921    193   -308   -447       N  
ATOM   1494  CA  GLU A 287      -9.616  14.270 -32.692  1.00 34.99           C  
ANISOU 1494  CA  GLU A 287     4245   4798   4252    212   -378   -231       C  
ATOM   1495  C   GLU A 287     -10.795  13.466 -32.139  1.00 37.57           C  
ANISOU 1495  C   GLU A 287     4517   4889   4869     27   -298    -91       C  
ATOM   1496  O   GLU A 287     -11.930  13.631 -32.593  1.00 42.66           O  
ANISOU 1496  O   GLU A 287     4720   5859   5629    159   -353   -132       O  
ATOM   1497  CB  GLU A 287      -8.950  13.523 -33.850  1.00 34.24           C  
ANISOU 1497  CB  GLU A 287     4252   4684   4074    -63   -374   -303       C  
ATOM   1498  CG  GLU A 287      -8.216  14.426 -34.830  1.00 34.70           C  
ANISOU 1498  CG  GLU A 287     4251   4807   4124    -48   -312   -113       C  
ATOM   1499  N   ASN A 288     -10.519  12.607 -31.159  1.00 37.30           N  
ANISOU 1499  N   ASN A 288     4335   4890   4944     56   -223    -50       N  
ATOM   1500  CA  ASN A 288     -11.555  11.828 -30.479  1.00 39.17           C  
ANISOU 1500  CA  ASN A 288     4759   5055   5067     74     -8     39       C  
ATOM   1501  C   ASN A 288     -12.459  12.713 -29.622  1.00 41.48           C  
ANISOU 1501  C   ASN A 288     4949   5350   5459     34    118    -30       C  
ATOM   1502  O   ASN A 288     -13.598  12.352 -29.323  1.00 42.47           O  
ANISOU 1502  O   ASN A 288     4722   5676   5737    137   -108   -158       O  
ATOM   1503  CB  ASN A 288     -10.927  10.730 -29.613  1.00 39.61           C  
ANISOU 1503  CB  ASN A 288     4850   5054   5145    -52      8     60       C  
ATOM   1504  CG  ASN A 288     -10.253   9.635 -30.434  1.00 42.19           C  
ANISOU 1504  CG  ASN A 288     5331   5255   5442     25     31     24       C  
ATOM   1505  ND2 ASN A 288      -9.602   8.706 -29.743  1.00 42.89           N  
ANISOU 1505  ND2 ASN A 288     5261   5469   5563   -106   -127    128       N  
ATOM   1506  OD1 ASN A 288     -10.318   9.622 -31.666  1.00 40.41           O  
ANISOU 1506  OD1 ASN A 288     5297   4695   5361   -138   -218   -409       O  
CONECT    1  625  650 1086 1087 1118
CONECT  625    1
CONECT  650    1
CONECT 1086    1
CONECT 1087    1
CONECT 1118    1
END



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.